data_9E0A
# 
_entry.id   9E0A 
# 
_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   9E0A         pdb_00009e0a 10.2210/pdb9e0a/pdb 
WWPDB D_1000289207 ?            ?                   
# 
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                        9E0A 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-17 
_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           N 
# 
_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 'FORMIC ACID'                     46.025     2    ?                ? ? ? 
4  non-polymer syn 'DI(HYDROXYETHYL)ETHER'           106.120    3    ?                ? ? ? 
5  non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE 663.425    2    ?                ? ? ? 
6  non-polymer syn 'SULFATE ION'                     96.063     6    ?                ? ? ? 
7  non-polymer syn 'MAGNESIUM ION'                   24.305     2    ?                ? ? ? 
8  non-polymer syn 'TRIETHYLENE GLYCOL'              150.173    1    ?                ? ? ? 
9  non-polymer syn '(1,4-phenylene)dimethanol'       138.164    1    ?                ? ? ? 
10 water       nat water                             18.015     2520 ?                ? ? ? 
# 
_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  'FORMIC ACID'                     FMT   
4  'DI(HYDROXYETHYL)ETHER'           PEG   
5  NICOTINAMIDE-ADENINE-DINUCLEOTIDE NAD   
6  'SULFATE ION'                     SO4   
7  'MAGNESIUM ION'                   MG    
8  'TRIETHYLENE GLYCOL'              PGE   
9  '(1,4-phenylene)dimethanol'       A1BDW 
10 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 
A1BDW non-polymer         . '(1,4-phenylene)dimethanol'       ? 'C8 H10 O2'         138.164 
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 
MG    non-polymer         . 'MAGNESIUM ION'                   ? 'Mg 2'              24.305  
NAD   non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE ? 'C21 H27 N7 O14 P2' 663.425 
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   79   HIS HIS A . n 
A 1 82   SER 82   80   ?    ?   ?   A . n 
A 1 83   GLY 83   81   ?    ?   ?   A . n 
A 1 84   SER 84   82   82   SER SER A . n 
A 1 85   GLY 85   83   83   GLY GLY A . n 
A 1 86   VAL 86   84   84   VAL VAL A . n 
A 1 87   GLU 87   85   85   GLU GLU A . n 
A 1 88   GLY 88   86   86   GLY GLY A . n 
A 1 89   LEU 89   87   87   LEU LEU A . n 
A 1 90   VAL 90   88   88   VAL VAL A . n 
A 1 91   GLN 91   89   89   GLN GLN A . n 
A 1 92   GLU 92   90   90   GLU GLU A . n 
A 1 93   TYR 93   91   91   TYR TYR A . n 
A 1 94   SER 94   92   92   SER SER A . n 
A 1 95   LEU 95   93   93   LEU LEU A . n 
A 1 96   SER 96   94   94   SER SER A . n 
A 1 97   SER 97   95   95   SER SER A . n 
A 1 98   GLN 98   96   96   GLN GLN A . n 
A 1 99   GLU 99   97   97   GLU GLU A . n 
A 1 100  GLY 100  98   98   GLY GLY A . n 
A 1 101  VAL 101  99   99   VAL VAL A . n 
A 1 102  ALA 102  100  100  ALA ALA A . n 
A 1 103  LEU 103  101  101  LEU LEU A . n 
A 1 104  MET 104  102  102  MET MET A . n 
A 1 105  CYS 105  103  103  CYS CYS A . n 
A 1 106  LEU 106  104  104  LEU LEU A . n 
A 1 107  ALA 107  105  105  ALA ALA A . n 
A 1 108  GLU 108  106  106  GLU GLU A . n 
A 1 109  ALA 109  107  107  ALA ALA A . n 
A 1 110  LEU 110  108  108  LEU LEU A . n 
A 1 111  LEU 111  109  109  LEU LEU A . n 
A 1 112  ARG 112  110  110  ARG ARG A . n 
A 1 113  ILE 113  111  111  ILE ILE A . n 
A 1 114  PRO 114  112  112  PRO PRO A . n 
A 1 115  ASP 115  113  113  ASP ASP A . n 
A 1 116  THR 116  114  114  THR THR A . n 
A 1 117  ALA 117  115  115  ALA ALA A . n 
A 1 118  THR 118  116  116  THR THR A . n 
A 1 119  ARG 119  117  117  ARG ARG A . n 
A 1 120  ASP 120  118  118  ASP ASP A . n 
A 1 121  ALA 121  119  119  ALA ALA A . n 
A 1 122  LEU 122  120  120  LEU LEU A . n 
A 1 123  ILE 123  121  121  ILE ILE A . n 
A 1 124  ARG 124  122  122  ARG ARG A . n 
A 1 125  ASP 125  123  123  ASP ASP A . n 
A 1 126  LYS 126  124  124  LYS LYS A . n 
A 1 127  ILE 127  125  125  ILE ILE A . n 
A 1 128  ALA 128  126  126  ALA ALA A . n 
A 1 129  ASP 129  127  127  ASP ASP A . n 
A 1 130  GLY 130  128  128  GLY GLY A . n 
A 1 131  ASN 131  129  129  ASN ASN A . n 
A 1 132  TRP 132  130  130  TRP TRP A . n 
A 1 133  LYS 133  131  131  LYS LYS A . n 
A 1 134  SER 134  132  132  SER SER A . n 
A 1 135  HIS 135  133  133  HIS HIS A . n 
A 1 136  LEU 136  134  134  LEU LEU A . n 
A 1 137  GLY 137  135  ?    ?   ?   A . n 
A 1 138  GLY 138  136  ?    ?   ?   A . n 
A 1 139  SER 139  137  137  SER SER A . n 
A 1 140  ARG 140  138  138  ARG ARG A . n 
A 1 141  SER 141  139  139  SER SER A . n 
A 1 142  LEU 142  140  140  LEU LEU A . n 
A 1 143  PHE 143  141  141  PHE PHE A . n 
A 1 144  VAL 144  142  142  VAL VAL A . n 
A 1 145  ASN 145  143  143  ASN ASN A . n 
A 1 146  ALA 146  144  144  ALA ALA A . n 
A 1 147  ALA 147  145  145  ALA ALA A . n 
A 1 148  THR 148  146  146  THR THR A . n 
A 1 149  TRP 149  147  147  TRP TRP A . n 
A 1 150  GLY 150  148  148  GLY GLY A . n 
A 1 151  LEU 151  149  149  LEU LEU A . n 
A 1 152  VAL 152  150  150  VAL VAL A . n 
A 1 153  VAL 153  151  151  VAL VAL A . n 
A 1 154  THR 154  152  152  THR THR A . n 
A 1 155  GLY 155  153  153  GLY GLY A . n 
A 1 156  LYS 156  154  154  LYS LYS A . n 
A 1 157  LEU 157  155  155  LEU LEU A . n 
A 1 158  THR 158  156  156  THR THR A . n 
A 1 159  SER 159  157  157  SER SER A . n 
A 1 160  THR 160  158  158  THR THR A . n 
A 1 161  VAL 161  159  159  VAL VAL A . n 
A 1 162  ASN 162  160  160  ASN ASN A . n 
A 1 163  ASP 163  161  161  ASP ASP A . n 
A 1 164  ARG 164  162  162  ARG ARG A . n 
A 1 165  SER 165  163  163  SER SER A . n 
A 1 166  LEU 166  164  164  LEU LEU A . n 
A 1 167  ALA 167  165  165  ALA ALA A . n 
A 1 168  ALA 168  166  166  ALA ALA A . n 
A 1 169  ALA 169  167  167  ALA ALA A . n 
A 1 170  LEU 170  168  168  LEU LEU A . n 
A 1 171  THR 171  169  169  THR THR A . n 
A 1 172  ARG 172  170  170  ARG ARG A . n 
A 1 173  LEU 173  171  171  LEU LEU A . n 
A 1 174  ILE 174  172  172  ILE ILE A . n 
A 1 175  SER 175  173  173  SER SER A . n 
A 1 176  ARG 176  174  174  ARG ARG A . n 
A 1 177  CYS 177  175  175  CYS CYS A . n 
A 1 178  GLY 178  176  176  GLY GLY A . n 
A 1 179  GLU 179  177  177  GLU GLU A . n 
A 1 180  PRO 180  178  178  PRO PRO A . n 
A 1 181  VAL 181  179  179  VAL VAL A . n 
A 1 182  ILE 182  180  180  ILE ILE A . n 
A 1 183  ARG 183  181  181  ARG ARG A . n 
A 1 184  ARG 184  182  182  ARG ARG A . n 
A 1 185  GLY 185  183  183  GLY GLY A . n 
A 1 186  VAL 186  184  184  VAL VAL A . n 
A 1 187  ASP 187  185  185  ASP ASP A . n 
A 1 188  MET 188  186  186  MET MET A . n 
A 1 189  ALA 189  187  187  ALA ALA A . n 
A 1 190  MET 190  188  188  MET MET A . n 
A 1 191  ARG 191  189  189  ARG ARG A . n 
A 1 192  MET 192  190  190  MET MET A . n 
A 1 193  MET 193  191  191  MET MET A . n 
A 1 194  GLY 194  192  192  GLY GLY A . n 
A 1 195  GLU 195  193  193  GLU GLU A . n 
A 1 196  GLN 196  194  194  GLN GLN A . n 
A 1 197  PHE 197  195  195  PHE PHE A . n 
A 1 198  VAL 198  196  196  VAL VAL A . n 
A 1 199  THR 199  197  197  THR THR A . n 
A 1 200  GLY 200  198  198  GLY GLY A . n 
A 1 201  GLU 201  199  199  GLU GLU A . n 
A 1 202  THR 202  200  200  THR THR A . n 
A 1 203  ILE 203  201  201  ILE ILE A . n 
A 1 204  ARG 204  202  202  ARG ARG A . n 
A 1 205  GLU 205  203  203  GLU GLU A . n 
A 1 206  ALA 206  204  204  ALA ALA A . n 
A 1 207  LEU 207  205  205  LEU LEU A . n 
A 1 208  LYS 208  206  206  LYS LYS A . n 
A 1 209  ARG 209  207  207  ARG ARG A . n 
A 1 210  SER 210  208  208  SER SER A . n 
A 1 211  LYS 211  209  209  LYS LYS A . n 
A 1 212  GLU 212  210  210  GLU GLU A . n 
A 1 213  LEU 213  211  211  LEU LEU A . n 
A 1 214  GLU 214  212  212  GLU GLU A . n 
A 1 215  GLU 215  213  213  GLU GLU A . n 
A 1 216  LYS 216  214  214  LYS LYS A . n 
A 1 217  GLY 217  215  215  GLY GLY A . n 
A 1 218  PHE 218  216  216  PHE PHE A . n 
A 1 219  SER 219  217  217  SER SER A . n 
A 1 220  TYR 220  218  218  TYR TYR A . n 
A 1 221  SER 221  219  219  SER SER A . n 
A 1 222  TYR 222  220  220  TYR TYR A . n 
A 1 223  ASP 223  221  221  ASP ASP A . n 
A 1 224  MET 224  222  222  MET MET A . n 
A 1 225  LEU 225  223  223  LEU LEU A . n 
A 1 226  GLY 226  224  224  GLY GLY A . n 
A 1 227  GLU 227  225  225  GLU GLU A . n 
A 1 228  ALA 228  226  226  ALA ALA A . n 
A 1 229  ALA 229  227  227  ALA ALA A . n 
A 1 230  THR 230  228  228  THR THR A . n 
A 1 231  THR 231  229  229  THR THR A . n 
A 1 232  ALA 232  230  230  ALA ALA A . n 
A 1 233  ALA 233  231  231  ALA ALA A . n 
A 1 234  ASP 234  232  232  ASP ASP A . n 
A 1 235  ALA 235  233  233  ALA ALA A . n 
A 1 236  GLU 236  234  234  GLU GLU A . n 
A 1 237  ARG 237  235  235  ARG ARG A . n 
A 1 238  TYR 238  236  236  TYR TYR A . n 
A 1 239  TYR 239  237  237  TYR TYR A . n 
A 1 240  ARG 240  238  238  ARG ARG A . n 
A 1 241  ASP 241  239  239  ASP ASP A . n 
A 1 242  TYR 242  240  240  TYR TYR A . n 
A 1 243  GLU 243  241  241  GLU GLU A . n 
A 1 244  SER 244  242  242  SER SER A . n 
A 1 245  ALA 245  243  243  ALA ALA A . n 
A 1 246  ILE 246  244  244  ILE ILE A . n 
A 1 247  HIS 247  245  245  HIS HIS A . n 
A 1 248  ALA 248  246  246  ALA ALA A . n 
A 1 249  ILE 249  247  247  ILE ILE A . n 
A 1 250  GLY 250  248  248  GLY GLY A . n 
A 1 251  LYS 251  249  249  LYS LYS A . n 
A 1 252  ALA 252  250  250  ALA ALA A . n 
A 1 253  SER 253  251  251  SER SER A . n 
A 1 254  ALA 254  252  252  ALA ALA A . n 
A 1 255  GLY 255  253  253  GLY GLY A . n 
A 1 256  ARG 256  254  254  ARG ARG A . n 
A 1 257  GLY 257  255  255  GLY GLY A . n 
A 1 258  ILE 258  256  256  ILE ILE A . n 
A 1 259  TYR 259  257  257  TYR TYR A . n 
A 1 260  GLU 260  258  258  GLU GLU A . n 
A 1 261  GLY 261  259  259  GLY GLY A . n 
A 1 262  PRO 262  260  260  PRO PRO A . n 
A 1 263  GLY 263  261  261  GLY GLY A . n 
A 1 264  ILE 264  262  262  ILE ILE A . n 
A 1 265  SER 265  263  263  SER SER A . n 
A 1 266  ILE 266  264  264  ILE ILE A . n 
A 1 267  LYS 267  265  265  LYS LYS A . n 
A 1 268  LEU 268  266  266  LEU LEU A . n 
A 1 269  SER 269  267  267  SER SER A . n 
A 1 270  ALA 270  268  268  ALA ALA A . n 
A 1 271  LEU 271  269  269  LEU LEU A . n 
A 1 272  HIS 272  270  270  HIS HIS A . n 
A 1 273  PRO 273  271  271  PRO PRO A . n 
A 1 274  ARG 274  272  272  ARG ARG A . n 
A 1 275  TYR 275  273  273  TYR TYR A . n 
A 1 276  SER 276  274  274  SER SER A . n 
A 1 277  ARG 277  275  275  ARG ARG A . n 
A 1 278  ALA 278  276  276  ALA ALA A . n 
A 1 279  GLN 279  277  277  GLN GLN A . n 
A 1 280  ALA 280  278  278  ALA ALA A . n 
A 1 281  ALA 281  279  279  ALA ALA A . n 
A 1 282  ARG 282  280  280  ARG ARG A . n 
A 1 283  VAL 283  281  281  VAL VAL A . n 
A 1 284  MET 284  282  282  MET MET A . n 
A 1 285  GLY 285  283  283  GLY GLY A . n 
A 1 286  GLU 286  284  284  GLU GLU A . n 
A 1 287  LEU 287  285  285  LEU LEU A . n 
A 1 288  LEU 288  286  286  LEU LEU A . n 
A 1 289  PRO 289  287  287  PRO PRO A . n 
A 1 290  ARG 290  288  288  ARG ARG A . n 
A 1 291  VAL 291  289  289  VAL VAL A . n 
A 1 292  LYS 292  290  290  LYS LYS A . n 
A 1 293  ALA 293  291  291  ALA ALA A . n 
A 1 294  LEU 294  292  292  LEU LEU A . n 
A 1 295  ALA 295  293  293  ALA ALA A . n 
A 1 296  LEU 296  294  294  LEU LEU A . n 
A 1 297  LEU 297  295  295  LEU LEU A . n 
A 1 298  ALA 298  296  296  ALA ALA A . n 
A 1 299  LYS 299  297  297  LYS LYS A . n 
A 1 300  ASN 300  298  298  ASN ASN A . n 
A 1 301  TYR 301  299  299  TYR TYR A . n 
A 1 302  ASP 302  300  300  ASP ASP A . n 
A 1 303  ILE 303  301  301  ILE ILE A . n 
A 1 304  GLY 304  302  302  GLY GLY A . n 
A 1 305  LEU 305  303  303  LEU LEU A . n 
A 1 306  ASN 306  304  304  ASN ASN A . n 
A 1 307  ILE 307  305  305  ILE ILE A . n 
A 1 308  ASP 308  306  306  ASP ASP A . n 
A 1 309  ALA 309  307  307  ALA ALA A . n 
A 1 310  GLU 310  308  308  GLU GLU A . n 
A 1 311  GLU 311  309  309  GLU GLU A . n 
A 1 312  ALA 312  310  310  ALA ALA A . n 
A 1 313  ASP 313  311  311  ASP ASP A . n 
A 1 314  ARG 314  312  312  ARG ARG A . n 
A 1 315  LEU 315  313  313  LEU LEU A . n 
A 1 316  GLU 316  314  314  GLU GLU A . n 
A 1 317  LEU 317  315  315  LEU LEU A . n 
A 1 318  SER 318  316  316  SER SER A . n 
A 1 319  LEU 319  317  317  LEU LEU A . n 
A 1 320  ASP 320  318  318  ASP ASP A . n 
A 1 321  LEU 321  319  319  LEU LEU A . n 
A 1 322  LEU 322  320  320  LEU LEU A . n 
A 1 323  GLU 323  321  321  GLU GLU A . n 
A 1 324  VAL 324  322  322  VAL VAL A . n 
A 1 325  LEU 325  323  323  LEU LEU A . n 
A 1 326  CYS 326  324  324  CYS CYS A . n 
A 1 327  LEU 327  325  325  LEU LEU A . n 
A 1 328  ASP 328  326  326  ASP ASP A . n 
A 1 329  GLY 329  327  327  GLY GLY A . n 
A 1 330  ASP 330  328  328  ASP ASP A . n 
A 1 331  LEU 331  329  329  LEU LEU A . n 
A 1 332  SER 332  330  330  SER SER A . n 
A 1 333  GLY 333  331  331  GLY GLY A . n 
A 1 334  TRP 334  332  332  TRP TRP A . n 
A 1 335  ASN 335  333  333  ASN ASN A . n 
A 1 336  GLY 336  334  334  GLY GLY A . n 
A 1 337  MET 337  335  335  MET MET A . n 
A 1 338  GLY 338  336  336  GLY GLY A . n 
A 1 339  PHE 339  337  337  PHE PHE A . n 
A 1 340  VAL 340  338  338  VAL VAL A . n 
A 1 341  VAL 341  339  339  VAL VAL A . n 
A 1 342  GLN 342  340  340  GLN GLN A . n 
A 1 343  ALA 343  341  341  ALA ALA A . n 
A 1 344  TYR 344  342  342  TYR TYR A . n 
A 1 345  GLY 345  343  343  GLY GLY A . n 
A 1 346  LYS 346  344  344  LYS LYS A . n 
A 1 347  ARG 347  345  345  ARG ARG A . n 
A 1 348  CYS 348  346  346  CYS CYS A . n 
A 1 349  PRO 349  347  347  PRO PRO A . n 
A 1 350  PHE 350  348  348  PHE PHE A . n 
A 1 351  VAL 351  349  349  VAL VAL A . n 
A 1 352  LEU 352  350  350  LEU LEU A . n 
A 1 353  ASP 353  351  351  ASP ASP A . n 
A 1 354  PHE 354  352  352  PHE PHE A . n 
A 1 355  ILE 355  353  353  ILE ILE A . n 
A 1 356  ILE 356  354  354  ILE ILE A . n 
A 1 357  ASP 357  355  355  ASP ASP A . n 
A 1 358  LEU 358  356  356  LEU LEU A . n 
A 1 359  ALA 359  357  357  ALA ALA A . n 
A 1 360  ARG 360  358  358  ARG ARG A . n 
A 1 361  ARG 361  359  359  ARG ARG A . n 
A 1 362  SER 362  360  360  SER SER A . n 
A 1 363  GLY 363  361  361  GLY GLY A . n 
A 1 364  ARG 364  362  362  ARG ARG A . n 
A 1 365  ARG 365  363  363  ARG ARG A . n 
A 1 366  ILE 366  364  364  ILE ILE A . n 
A 1 367  MET 367  365  365  MET MET A . n 
A 1 368  VAL 368  366  366  VAL VAL A . n 
A 1 369  ARG 369  367  367  ARG ARG A . n 
A 1 370  LEU 370  368  368  LEU LEU A . n 
A 1 371  VAL 371  369  369  VAL VAL A . n 
A 1 372  LYS 372  370  370  LYS LYS A . n 
A 1 373  GLY 373  371  371  GLY GLY A . n 
A 1 374  ALA 374  372  372  ALA ALA A . n 
A 1 375  TYR 375  373  373  TYR TYR A . n 
A 1 376  TRP 376  374  374  TRP TRP A . n 
A 1 377  ASP 377  375  375  ASP ASP A . n 
A 1 378  ALA 378  376  376  ALA ALA A . n 
A 1 379  GLU 379  377  377  GLU GLU A . n 
A 1 380  ILE 380  378  378  ILE ILE A . n 
A 1 381  LYS 381  379  379  LYS LYS A . n 
A 1 382  ARG 382  380  380  ARG ARG A . n 
A 1 383  ALA 383  381  381  ALA ALA A . n 
A 1 384  GLN 384  382  382  GLN GLN A . n 
A 1 385  LEU 385  383  383  LEU LEU A . n 
A 1 386  ASP 386  384  384  ASP ASP A . n 
A 1 387  GLY 387  385  385  GLY GLY A . n 
A 1 388  LEU 388  386  386  LEU LEU A . n 
A 1 389  ALA 389  387  387  ALA ALA A . n 
A 1 390  ASP 390  388  388  ASP ASP A . n 
A 1 391  PHE 391  389  389  PHE PHE A . n 
A 1 392  PRO 392  390  390  PRO PRO A . n 
A 1 393  VAL 393  391  391  VAL VAL A . n 
A 1 394  PHE 394  392  392  PHE PHE A . n 
A 1 395  THR 395  393  393  THR THR A . n 
A 1 396  ARG 396  394  394  ARG ARG A . n 
A 1 397  LYS 397  395  395  LYS LYS A . n 
A 1 398  ILE 398  396  396  ILE ILE A . n 
A 1 399  HIS 399  397  397  HIS HIS A . n 
A 1 400  THR 400  398  398  THR THR A . n 
A 1 401  ASP 401  399  399  ASP ASP A . n 
A 1 402  VAL 402  400  400  VAL VAL A . n 
A 1 403  SER 403  401  401  SER SER A . n 
A 1 404  TYR 404  402  402  TYR TYR A . n 
A 1 405  ILE 405  403  403  ILE ILE A . n 
A 1 406  ALA 406  404  404  ALA ALA A . n 
A 1 407  CYS 407  405  405  CYS CYS A . n 
A 1 408  ALA 408  406  406  ALA ALA A . n 
A 1 409  ALA 409  407  407  ALA ALA A . n 
A 1 410  LYS 410  408  408  LYS LYS A . n 
A 1 411  LEU 411  409  409  LEU LEU A . n 
A 1 412  LEU 412  410  410  LEU LEU A . n 
A 1 413  ALA 413  411  411  ALA ALA A . n 
A 1 414  ALA 414  412  412  ALA ALA A . n 
A 1 415  THR 415  413  413  THR THR A . n 
A 1 416  ASP 416  414  414  ASP ASP A . n 
A 1 417  VAL 417  415  415  VAL VAL A . n 
A 1 418  VAL 418  416  416  VAL VAL A . n 
A 1 419  PHE 419  417  417  PHE PHE A . n 
A 1 420  PRO 420  418  418  PRO PRO A . n 
A 1 421  GLN 421  419  419  GLN GLN A . n 
A 1 422  PHE 422  420  420  PHE PHE A . n 
A 1 423  ALA 423  421  421  ALA ALA A . n 
A 1 424  THR 424  422  422  THR THR A . n 
A 1 425  HIS 425  423  423  HIS HIS A . n 
A 1 426  ASN 426  424  424  ASN ASN A . n 
A 1 427  ALA 427  425  425  ALA ALA A . n 
A 1 428  GLN 428  426  426  GLN GLN A . n 
A 1 429  THR 429  427  427  THR THR A . n 
A 1 430  LEU 430  428  428  LEU LEU A . n 
A 1 431  ALA 431  429  429  ALA ALA A . n 
A 1 432  ALA 432  430  430  ALA ALA A . n 
A 1 433  ILE 433  431  431  ILE ILE A . n 
A 1 434  TYR 434  432  432  TYR TYR A . n 
A 1 435  HIS 435  433  433  HIS HIS A . n 
A 1 436  MET 436  434  434  MET MET A . n 
A 1 437  ALA 437  435  435  ALA ALA A . n 
A 1 438  GLY 438  436  436  GLY GLY A . n 
A 1 439  LYS 439  437  437  LYS LYS A . n 
A 1 440  ASP 440  438  438  ASP ASP A . n 
A 1 441  PHE 441  439  439  PHE PHE A . n 
A 1 442  HIS 442  440  440  HIS HIS A . n 
A 1 443  VAL 443  441  441  VAL VAL A . n 
A 1 444  GLY 444  442  442  GLY GLY A . n 
A 1 445  LYS 445  443  443  LYS LYS A . n 
A 1 446  TYR 446  444  444  TYR TYR A . n 
A 1 447  GLU 447  445  445  GLU GLU A . n 
A 1 448  PHE 448  446  446  PHE PHE A . n 
A 1 449  GLN 449  447  447  GLN GLN A . n 
A 1 450  CYS 450  448  448  CYS CYS A . n 
A 1 451  LEU 451  449  449  LEU LEU A . n 
A 1 452  HIS 452  450  450  HIS HIS A . n 
A 1 453  GLY 453  451  451  GLY GLY A . n 
A 1 454  MET 454  452  452  MET MET A . n 
A 1 455  GLY 455  453  453  GLY GLY A . n 
A 1 456  GLU 456  454  454  GLU GLU A . n 
A 1 457  PRO 457  455  455  PRO PRO A . n 
A 1 458  LEU 458  456  456  LEU LEU A . n 
A 1 459  TYR 459  457  457  TYR TYR A . n 
A 1 460  GLU 460  458  458  GLU GLU A . n 
A 1 461  GLU 461  459  459  GLU GLU A . n 
A 1 462  VAL 462  460  460  VAL VAL A . n 
A 1 463  VAL 463  461  461  VAL VAL A . n 
A 1 464  GLY 464  462  462  GLY GLY A . n 
A 1 465  ARG 465  463  463  ARG ARG A . n 
A 1 466  GLY 466  464  464  GLY GLY A . n 
A 1 467  LYS 467  465  465  LYS LYS A . n 
A 1 468  LEU 468  466  466  LEU LEU A . n 
A 1 469  ASP 469  467  467  ASP ASP A . n 
A 1 470  ARG 470  468  468  ARG ARG A . n 
A 1 471  PRO 471  469  469  PRO PRO A . n 
A 1 472  CYS 472  470  470  CYS CYS A . n 
A 1 473  ARG 473  471  471  ARG ARG A . n 
A 1 474  ILE 474  472  472  ILE ILE A . n 
A 1 475  TYR 475  473  473  TYR TYR A . n 
A 1 476  ALA 476  474  474  ALA ALA A . n 
A 1 477  PRO 477  475  475  PRO PRO A . n 
A 1 478  VAL 478  476  476  VAL VAL A . n 
A 1 479  GLY 479  477  477  GLY GLY A . n 
A 1 480  THR 480  478  478  THR THR A . n 
A 1 481  HIS 481  479  479  HIS HIS A . n 
A 1 482  GLU 482  480  480  GLU GLU A . n 
A 1 483  THR 483  481  481  THR THR A . n 
A 1 484  LEU 484  482  482  LEU LEU A . n 
A 1 485  LEU 485  483  483  LEU LEU A . n 
A 1 486  ALA 486  484  484  ALA ALA A . n 
A 1 487  TYR 487  485  485  TYR TYR A . n 
A 1 488  LEU 488  486  486  LEU LEU A . n 
A 1 489  VAL 489  487  487  VAL VAL A . n 
A 1 490  ARG 490  488  488  ARG ARG A . n 
A 1 491  ARG 491  489  489  ARG ARG A . n 
A 1 492  LEU 492  490  490  LEU LEU A . n 
A 1 493  LEU 493  491  491  LEU LEU A . n 
A 1 494  GLU 494  492  492  GLU GLU A . n 
A 1 495  ASN 495  493  493  ASN ASN A . n 
A 1 496  GLY 496  494  494  GLY GLY A . n 
A 1 497  ALA 497  495  495  ALA ALA A . n 
A 1 498  ASN 498  496  496  ASN ASN A . n 
A 1 499  SER 499  497  497  SER SER A . n 
A 1 500  SER 500  498  498  SER SER A . n 
A 1 501  PHE 501  499  499  PHE PHE A . n 
A 1 502  VAL 502  500  500  VAL VAL A . n 
A 1 503  HIS 503  501  501  HIS HIS A . n 
A 1 504  ARG 504  502  502  ARG ARG A . n 
A 1 505  ILE 505  503  503  ILE ILE A . n 
A 1 506  ASN 506  504  504  ASN ASN A . n 
A 1 507  ASP 507  505  505  ASP ASP A . n 
A 1 508  PRO 508  506  506  PRO PRO A . n 
A 1 509  LYS 509  507  507  LYS LYS A . n 
A 1 510  VAL 510  508  508  VAL VAL A . n 
A 1 511  SER 511  509  509  SER SER A . n 
A 1 512  ILE 512  510  510  ILE ILE A . n 
A 1 513  ASP 513  511  511  ASP ASP A . n 
A 1 514  GLU 514  512  512  GLU GLU A . n 
A 1 515  LEU 515  513  513  LEU LEU A . n 
A 1 516  ILE 516  514  514  ILE ILE A . n 
A 1 517  ALA 517  515  515  ALA ALA A . n 
A 1 518  ASP 518  516  516  ASP ASP A . n 
A 1 519  PRO 519  517  517  PRO PRO A . n 
A 1 520  VAL 520  518  518  VAL VAL A . n 
A 1 521  GLU 521  519  519  GLU GLU A . n 
A 1 522  VAL 522  520  520  VAL VAL A . n 
A 1 523  VAL 523  521  521  VAL VAL A . n 
A 1 524  ARG 524  522  522  ARG ARG A . n 
A 1 525  ALA 525  523  523  ALA ALA A . n 
A 1 526  MET 526  524  524  MET MET A . n 
A 1 527  PRO 527  525  525  PRO PRO A . n 
A 1 528  VAL 528  526  526  VAL VAL A . n 
A 1 529  VAL 529  527  527  VAL VAL A . n 
A 1 530  GLY 530  528  528  GLY GLY A . n 
A 1 531  ALA 531  529  529  ALA ALA A . n 
A 1 532  LYS 532  530  530  LYS LYS A . n 
A 1 533  HIS 533  531  531  HIS HIS A . n 
A 1 534  ASP 534  532  532  ASP ASP A . n 
A 1 535  ARG 535  533  533  ARG ARG A . n 
A 1 536  ILE 536  534  534  ILE ILE A . n 
A 1 537  ALA 537  535  535  ALA ALA A . n 
A 1 538  LEU 538  536  536  LEU LEU A . n 
A 1 539  PRO 539  537  537  PRO PRO A . n 
A 1 540  ALA 540  538  538  ALA ALA A . n 
A 1 541  GLU 541  539  539  GLU GLU A . n 
A 1 542  LEU 542  540  540  LEU LEU A . n 
A 1 543  PHE 543  541  541  PHE PHE A . n 
A 1 544  GLY 544  542  542  GLY GLY A . n 
A 1 545  ASP 545  543  543  ASP ASP A . n 
A 1 546  ALA 546  544  544  ALA ALA A . n 
A 1 547  ARG 547  545  545  ARG ARG A . n 
A 1 548  THR 548  546  546  THR THR A . n 
A 1 549  ASN 549  547  547  ASN ASN A . n 
A 1 550  SER 550  548  548  SER SER A . n 
A 1 551  ALA 551  549  549  ALA ALA A . n 
A 1 552  GLY 552  550  550  GLY GLY A . n 
A 1 553  LEU 553  551  551  LEU LEU A . n 
A 1 554  ASP 554  552  552  ASP ASP A . n 
A 1 555  LEU 555  553  553  LEU LEU A . n 
A 1 556  SER 556  554  554  SER SER A . n 
A 1 557  ASN 557  555  555  ASN ASN A . n 
A 1 558  GLU 558  556  556  GLU GLU A . n 
A 1 559  GLU 559  557  557  GLU GLU A . n 
A 1 560  THR 560  558  558  THR THR A . n 
A 1 561  LEU 561  559  559  LEU LEU A . n 
A 1 562  ALA 562  560  560  ALA ALA A . n 
A 1 563  SER 563  561  561  SER SER A . n 
A 1 564  LEU 564  562  562  LEU LEU A . n 
A 1 565  THR 565  563  563  THR THR A . n 
A 1 566  GLU 566  564  564  GLU GLU A . n 
A 1 567  ALA 567  565  565  ALA ALA A . n 
A 1 568  LEU 568  566  566  LEU LEU A . n 
A 1 569  ARG 569  567  567  ARG ARG A . n 
A 1 570  GLU 570  568  568  GLU GLU A . n 
A 1 571  SER 571  569  569  SER SER A . n 
A 1 572  ALA 572  570  570  ALA ALA A . n 
A 1 573  ALA 573  571  571  ALA ALA A . n 
A 1 574  MET 574  572  572  MET MET A . n 
A 1 575  LYS 575  573  573  LYS LYS A . n 
A 1 576  TRP 576  574  574  TRP TRP A . n 
A 1 577  THR 577  575  575  THR THR A . n 
A 1 578  ALA 578  576  576  ALA ALA A . n 
A 1 579  LEU 579  577  577  LEU LEU A . n 
A 1 580  PRO 580  578  578  PRO PRO A . n 
A 1 581  GLN 581  579  579  GLN GLN A . n 
A 1 582  LEU 582  580  580  LEU LEU A . n 
A 1 583  ALA 583  581  581  ALA ALA A . n 
A 1 584  THR 584  582  582  THR THR A . n 
A 1 585  GLY 585  583  583  GLY GLY A . n 
A 1 586  PRO 586  584  584  PRO PRO A . n 
A 1 587  ALA 587  585  585  ALA ALA A . n 
A 1 588  ALA 588  586  586  ALA ALA A . n 
A 1 589  GLY 589  587  587  GLY GLY A . n 
A 1 590  GLU 590  588  588  GLU GLU A . n 
A 1 591  THR 591  589  589  THR THR A . n 
A 1 592  ARG 592  590  590  ARG ARG A . n 
A 1 593  THR 593  591  591  THR THR A . n 
A 1 594  VAL 594  592  592  VAL VAL A . n 
A 1 595  LEU 595  593  593  LEU LEU A . n 
A 1 596  ASN 596  594  594  ASN ASN A . n 
A 1 597  PRO 597  595  595  PRO PRO A . n 
A 1 598  GLY 598  596  596  GLY GLY A . n 
A 1 599  ASP 599  597  597  ASP ASP A . n 
A 1 600  HIS 600  598  598  HIS HIS A . n 
A 1 601  ARG 601  599  599  ARG ARG A . n 
A 1 602  ASP 602  600  600  ASP ASP A . n 
A 1 603  VAL 603  601  601  VAL VAL A . n 
A 1 604  VAL 604  602  602  VAL VAL A . n 
A 1 605  GLY 605  603  603  GLY GLY A . n 
A 1 606  SER 606  604  604  SER SER A . n 
A 1 607  VAL 607  605  605  VAL VAL A . n 
A 1 608  THR 608  606  606  THR THR A . n 
A 1 609  GLU 609  607  607  GLU GLU A . n 
A 1 610  THR 610  608  608  THR THR A . n 
A 1 611  SER 611  609  609  SER SER A . n 
A 1 612  GLU 612  610  610  GLU GLU A . n 
A 1 613  GLU 613  611  611  GLU GLU A . n 
A 1 614  ASP 614  612  612  ASP ASP A . n 
A 1 615  ALA 615  613  613  ALA ALA A . n 
A 1 616  ARG 616  614  614  ARG ARG A . n 
A 1 617  ARG 617  615  615  ARG ARG A . n 
A 1 618  ALA 618  616  616  ALA ALA A . n 
A 1 619  VAL 619  617  617  VAL VAL A . n 
A 1 620  ARG 620  618  618  ARG ARG A . n 
A 1 621  LEU 621  619  619  LEU LEU A . n 
A 1 622  ALA 622  620  620  ALA ALA A . n 
A 1 623  ALA 623  621  621  ALA ALA A . n 
A 1 624  ASP 624  622  622  ASP ASP A . n 
A 1 625  ALA 625  623  623  ALA ALA A . n 
A 1 626  ALA 626  624  624  ALA ALA A . n 
A 1 627  PRO 627  625  625  PRO PRO A . n 
A 1 628  ASP 628  626  626  ASP ASP A . n 
A 1 629  TRP 629  627  627  TRP TRP A . n 
A 1 630  ALA 630  628  628  ALA ALA A . n 
A 1 631  ALA 631  629  629  ALA ALA A . n 
A 1 632  VAL 632  630  630  VAL VAL A . n 
A 1 633  PRO 633  631  631  PRO PRO A . n 
A 1 634  PRO 634  632  632  PRO PRO A . n 
A 1 635  SER 635  633  633  SER SER A . n 
A 1 636  GLU 636  634  634  GLU GLU A . n 
A 1 637  ARG 637  635  635  ARG ARG A . n 
A 1 638  ALA 638  636  636  ALA ALA A . n 
A 1 639  ALA 639  637  637  ALA ALA A . n 
A 1 640  CYS 640  638  638  CYS CYS A . n 
A 1 641  LEU 641  639  639  LEU LEU A . n 
A 1 642  ASP 642  640  640  ASP ASP A . n 
A 1 643  ARG 643  641  641  ARG ARG A . n 
A 1 644  ALA 644  642  642  ALA ALA A . n 
A 1 645  ALA 645  643  643  ALA ALA A . n 
A 1 646  GLU 646  644  644  GLU GLU A . n 
A 1 647  LEU 647  645  645  LEU LEU A . n 
A 1 648  MET 648  646  646  MET MET A . n 
A 1 649  GLN 649  647  647  GLN GLN A . n 
A 1 650  ALA 650  648  648  ALA ALA A . n 
A 1 651  ARG 651  649  649  ARG ARG A . n 
A 1 652  MET 652  650  650  MET MET A . n 
A 1 653  PRO 653  651  651  PRO PRO A . n 
A 1 654  THR 654  652  652  THR THR A . n 
A 1 655  LEU 655  653  653  LEU LEU A . n 
A 1 656  LEU 656  654  654  LEU LEU A . n 
A 1 657  GLY 657  655  655  GLY GLY A . n 
A 1 658  LEU 658  656  656  LEU LEU A . n 
A 1 659  ILE 659  657  657  ILE ILE A . n 
A 1 660  ILE 660  658  658  ILE ILE A . n 
A 1 661  ARG 661  659  659  ARG ARG A . n 
A 1 662  GLU 662  660  660  GLU GLU A . n 
A 1 663  ALA 663  661  661  ALA ALA A . n 
A 1 664  GLY 664  662  662  GLY GLY A . n 
A 1 665  LYS 665  663  663  LYS LYS A . n 
A 1 666  SER 666  664  664  SER SER A . n 
A 1 667  ALA 667  665  665  ALA ALA A . n 
A 1 668  LEU 668  666  666  LEU LEU A . n 
A 1 669  ASN 669  667  667  ASN ASN A . n 
A 1 670  ALA 670  668  668  ALA ALA A . n 
A 1 671  ILE 671  669  669  ILE ILE A . n 
A 1 672  ALA 672  670  670  ALA ALA A . n 
A 1 673  GLU 673  671  671  GLU GLU A . n 
A 1 674  VAL 674  672  672  VAL VAL A . n 
A 1 675  ARG 675  673  673  ARG ARG A . n 
A 1 676  GLU 676  674  674  GLU GLU A . n 
A 1 677  ALA 677  675  675  ALA ALA A . n 
A 1 678  ILE 678  676  676  ILE ILE A . n 
A 1 679  ASP 679  677  677  ASP ASP A . n 
A 1 680  PHE 680  678  678  PHE PHE A . n 
A 1 681  LEU 681  679  679  LEU LEU A . n 
A 1 682  ARG 682  680  680  ARG ARG A . n 
A 1 683  TYR 683  681  681  TYR TYR A . n 
A 1 684  TYR 684  682  682  TYR TYR A . n 
A 1 685  ALA 685  683  683  ALA ALA A . n 
A 1 686  GLU 686  684  684  GLU GLU A . n 
A 1 687  GLN 687  685  685  GLN GLN A . n 
A 1 688  THR 688  686  686  THR THR A . n 
A 1 689  ARG 689  687  687  ARG ARG A . n 
A 1 690  ARG 690  688  688  ARG ARG A . n 
A 1 691  THR 691  689  689  THR THR A . n 
A 1 692  LEU 692  690  690  LEU LEU A . n 
A 1 693  GLY 693  691  691  GLY GLY A . n 
A 1 694  PRO 694  692  692  PRO PRO A . n 
A 1 695  GLY 695  693  693  GLY GLY A . n 
A 1 696  HIS 696  694  694  HIS HIS A . n 
A 1 697  GLY 697  695  695  GLY GLY A . n 
A 1 698  PRO 698  696  696  PRO PRO A . n 
A 1 699  LEU 699  697  697  LEU LEU A . n 
A 1 700  GLY 700  698  698  GLY GLY A . n 
A 1 701  PRO 701  699  699  PRO PRO A . n 
A 1 702  ILE 702  700  700  ILE ILE A . n 
A 1 703  VAL 703  701  701  VAL VAL A . n 
A 1 704  CYS 704  702  702  CYS CYS A . n 
A 1 705  ILE 705  703  703  ILE ILE A . n 
A 1 706  SER 706  704  704  SER SER A . n 
A 1 707  PRO 707  705  705  PRO PRO A . n 
A 1 708  TRP 708  706  706  TRP TRP A . n 
A 1 709  ASN 709  707  707  ASN ASN A . n 
A 1 710  PHE 710  708  708  PHE PHE A . n 
A 1 711  PRO 711  709  709  PRO PRO A . n 
A 1 712  LEU 712  710  710  LEU LEU A . n 
A 1 713  ALA 713  711  711  ALA ALA A . n 
A 1 714  ILE 714  712  712  ILE ILE A . n 
A 1 715  PHE 715  713  713  PHE PHE A . n 
A 1 716  THR 716  714  714  THR THR A . n 
A 1 717  GLY 717  715  715  GLY GLY A . n 
A 1 718  GLN 718  716  716  GLN GLN A . n 
A 1 719  ILE 719  717  717  ILE ILE A . n 
A 1 720  ALA 720  718  718  ALA ALA A . n 
A 1 721  ALA 721  719  719  ALA ALA A . n 
A 1 722  ALA 722  720  720  ALA ALA A . n 
A 1 723  LEU 723  721  721  LEU LEU A . n 
A 1 724  VAL 724  722  722  VAL VAL A . n 
A 1 725  ALA 725  723  723  ALA ALA A . n 
A 1 726  GLY 726  724  724  GLY GLY A . n 
A 1 727  ASN 727  725  725  ASN ASN A . n 
A 1 728  PRO 728  726  726  PRO PRO A . n 
A 1 729  VAL 729  727  727  VAL VAL A . n 
A 1 730  LEU 730  728  728  LEU LEU A . n 
A 1 731  ALA 731  729  729  ALA ALA A . n 
A 1 732  LYS 732  730  730  LYS LYS A . n 
A 1 733  PRO 733  731  731  PRO PRO A . n 
A 1 734  ALA 734  732  732  ALA ALA A . n 
A 1 735  GLU 735  733  733  GLU GLU A . n 
A 1 736  GLU 736  734  734  GLU GLU A . n 
A 1 737  THR 737  735  735  THR THR A . n 
A 1 738  PRO 738  736  736  PRO PRO A . n 
A 1 739  LEU 739  737  737  LEU LEU A . n 
A 1 740  ILE 740  738  738  ILE ILE A . n 
A 1 741  ALA 741  739  739  ALA ALA A . n 
A 1 742  ALA 742  740  740  ALA ALA A . n 
A 1 743  GLU 743  741  741  GLU GLU A . n 
A 1 744  GLY 744  742  742  GLY GLY A . n 
A 1 745  VAL 745  743  743  VAL VAL A . n 
A 1 746  ARG 746  744  744  ARG ARG A . n 
A 1 747  ILE 747  745  745  ILE ILE A . n 
A 1 748  LEU 748  746  746  LEU LEU A . n 
A 1 749  ARG 749  747  747  ARG ARG A . n 
A 1 750  GLU 750  748  748  GLU GLU A . n 
A 1 751  ALA 751  749  749  ALA ALA A . n 
A 1 752  GLY 752  750  750  GLY GLY A . n 
A 1 753  ILE 753  751  751  ILE ILE A . n 
A 1 754  PRO 754  752  752  PRO PRO A . n 
A 1 755  ALA 755  753  753  ALA ALA A . n 
A 1 756  SER 756  754  754  SER SER A . n 
A 1 757  ALA 757  755  755  ALA ALA A . n 
A 1 758  LEU 758  756  756  LEU LEU A . n 
A 1 759  GLN 759  757  757  GLN GLN A . n 
A 1 760  LEU 760  758  758  LEU LEU A . n 
A 1 761  LEU 761  759  759  LEU LEU A . n 
A 1 762  PRO 762  760  760  PRO PRO A . n 
A 1 763  GLY 763  761  761  GLY GLY A . n 
A 1 764  ASP 764  762  762  ASP ASP A . n 
A 1 765  GLY 765  763  763  GLY GLY A . n 
A 1 766  ARG 766  764  764  ARG ARG A . n 
A 1 767  VAL 767  765  765  VAL VAL A . n 
A 1 768  GLY 768  766  766  GLY GLY A . n 
A 1 769  ALA 769  767  767  ALA ALA A . n 
A 1 770  ALA 770  768  768  ALA ALA A . n 
A 1 771  LEU 771  769  769  LEU LEU A . n 
A 1 772  VAL 772  770  770  VAL VAL A . n 
A 1 773  ALA 773  771  771  ALA ALA A . n 
A 1 774  ALA 774  772  772  ALA ALA A . n 
A 1 775  ALA 775  773  773  ALA ALA A . n 
A 1 776  GLU 776  774  774  GLU GLU A . n 
A 1 777  THR 777  775  775  THR THR A . n 
A 1 778  ALA 778  776  776  ALA ALA A . n 
A 1 779  GLY 779  777  777  GLY GLY A . n 
A 1 780  VAL 780  778  778  VAL VAL A . n 
A 1 781  MET 781  779  779  MET MET A . n 
A 1 782  PHE 782  780  780  PHE PHE A . n 
A 1 783  THR 783  781  781  THR THR A . n 
A 1 784  GLY 784  782  782  GLY GLY A . n 
A 1 785  SER 785  783  783  SER SER A . n 
A 1 786  THR 786  784  784  THR THR A . n 
A 1 787  GLU 787  785  785  GLU GLU A . n 
A 1 788  VAL 788  786  786  VAL VAL A . n 
A 1 789  ALA 789  787  787  ALA ALA A . n 
A 1 790  ARG 790  788  788  ARG ARG A . n 
A 1 791  LEU 791  789  789  LEU LEU A . n 
A 1 792  ILE 792  790  790  ILE ILE A . n 
A 1 793  GLN 793  791  791  GLN GLN A . n 
A 1 794  ALA 794  792  792  ALA ALA A . n 
A 1 795  GLN 795  793  793  GLN GLN A . n 
A 1 796  LEU 796  794  794  LEU LEU A . n 
A 1 797  ALA 797  795  795  ALA ALA A . n 
A 1 798  ASP 798  796  796  ASP ASP A . n 
A 1 799  ARG 799  797  797  ARG ARG A . n 
A 1 800  LEU 800  798  798  LEU LEU A . n 
A 1 801  SER 801  799  799  SER SER A . n 
A 1 802  PRO 802  800  800  PRO PRO A . n 
A 1 803  ALA 803  801  801  ALA ALA A . n 
A 1 804  GLY 804  802  802  GLY GLY A . n 
A 1 805  ARG 805  803  803  ARG ARG A . n 
A 1 806  PRO 806  804  804  PRO PRO A . n 
A 1 807  ILE 807  805  805  ILE ILE A . n 
A 1 808  PRO 808  806  806  PRO PRO A . n 
A 1 809  LEU 809  807  807  LEU LEU A . n 
A 1 810  ILE 810  808  808  ILE ILE A . n 
A 1 811  ALA 811  809  809  ALA ALA A . n 
A 1 812  GLU 812  810  810  GLU GLU A . n 
A 1 813  THR 813  811  811  THR THR A . n 
A 1 814  GLY 814  812  812  GLY GLY A . n 
A 1 815  GLY 815  813  813  GLY GLY A . n 
A 1 816  GLN 816  814  814  GLN GLN A . n 
A 1 817  ASN 817  815  815  ASN ASN A . n 
A 1 818  ALA 818  816  816  ALA ALA A . n 
A 1 819  MET 819  817  817  MET MET A . n 
A 1 820  ILE 820  818  818  ILE ILE A . n 
A 1 821  VAL 821  819  819  VAL VAL A . n 
A 1 822  ASP 822  820  820  ASP ASP A . n 
A 1 823  SER 823  821  821  SER SER A . n 
A 1 824  SER 824  822  822  SER SER A . n 
A 1 825  ALA 825  823  823  ALA ALA A . n 
A 1 826  LEU 826  824  824  LEU LEU A . n 
A 1 827  ALA 827  825  825  ALA ALA A . n 
A 1 828  GLU 828  826  826  GLU GLU A . n 
A 1 829  GLN 829  827  827  GLN GLN A . n 
A 1 830  VAL 830  828  828  VAL VAL A . n 
A 1 831  VAL 831  829  829  VAL VAL A . n 
A 1 832  GLY 832  830  830  GLY GLY A . n 
A 1 833  ASP 833  831  831  ASP ASP A . n 
A 1 834  VAL 834  832  832  VAL VAL A . n 
A 1 835  ILE 835  833  833  ILE ILE A . n 
A 1 836  THR 836  834  834  THR THR A . n 
A 1 837  SER 837  835  835  SER SER A . n 
A 1 838  ALA 838  836  836  ALA ALA A . n 
A 1 839  PHE 839  837  837  PHE PHE A . n 
A 1 840  ASP 840  838  838  ASP ASP A . n 
A 1 841  SER 841  839  839  SER SER A . n 
A 1 842  ALA 842  840  840  ALA ALA A . n 
A 1 843  GLY 843  841  841  GLY GLY A . n 
A 1 844  GLN 844  842  842  GLN GLN A . n 
A 1 845  ARG 845  843  843  ARG ARG A . n 
A 1 846  CYS 846  844  844  CYS CYS A . n 
A 1 847  SER 847  845  845  SER SER A . n 
A 1 848  ALA 848  846  846  ALA ALA A . n 
A 1 849  LEU 849  847  847  LEU LEU A . n 
A 1 850  ARG 850  848  848  ARG ARG A . n 
A 1 851  VAL 851  849  849  VAL VAL A . n 
A 1 852  LEU 852  850  850  LEU LEU A . n 
A 1 853  CYS 853  851  851  CYS CYS A . n 
A 1 854  LEU 854  852  852  LEU LEU A . n 
A 1 855  GLN 855  853  853  GLN GLN A . n 
A 1 856  GLU 856  854  854  GLU GLU A . n 
A 1 857  ASP 857  855  855  ASP ASP A . n 
A 1 858  VAL 858  856  856  VAL VAL A . n 
A 1 859  ALA 859  857  857  ALA ALA A . n 
A 1 860  ASP 860  858  858  ASP ASP A . n 
A 1 861  ARG 861  859  859  ARG ARG A . n 
A 1 862  ILE 862  860  860  ILE ILE A . n 
A 1 863  LEU 863  861  861  LEU LEU A . n 
A 1 864  THR 864  862  862  THR THR A . n 
A 1 865  MET 865  863  863  MET MET A . n 
A 1 866  LEU 866  864  864  LEU LEU A . n 
A 1 867  LYS 867  865  865  LYS LYS A . n 
A 1 868  GLY 868  866  866  GLY GLY A . n 
A 1 869  ALA 869  867  867  ALA ALA A . n 
A 1 870  LEU 870  868  868  LEU LEU A . n 
A 1 871  HIS 871  869  869  HIS HIS A . n 
A 1 872  GLU 872  870  870  GLU GLU A . n 
A 1 873  LEU 873  871  871  LEU LEU A . n 
A 1 874  HIS 874  872  872  HIS HIS A . n 
A 1 875  ILE 875  873  873  ILE ILE A . n 
A 1 876  GLY 876  874  874  GLY GLY A . n 
A 1 877  ARG 877  875  875  ARG ARG A . n 
A 1 878  THR 878  876  876  THR THR A . n 
A 1 879  ASP 879  877  877  ASP ASP A . n 
A 1 880  ARG 880  878  878  ARG ARG A . n 
A 1 881  LEU 881  879  879  LEU LEU A . n 
A 1 882  SER 882  880  880  SER SER A . n 
A 1 883  VAL 883  881  881  VAL VAL A . n 
A 1 884  ASP 884  882  882  ASP ASP A . n 
A 1 885  VAL 885  883  883  VAL VAL A . n 
A 1 886  GLY 886  884  884  GLY GLY A . n 
A 1 887  PRO 887  885  885  PRO PRO A . n 
A 1 888  VAL 888  886  886  VAL VAL A . n 
A 1 889  ILE 889  887  887  ILE ILE A . n 
A 1 890  THR 890  888  888  THR THR A . n 
A 1 891  SER 891  889  889  SER SER A . n 
A 1 892  GLU 892  890  890  GLU GLU A . n 
A 1 893  ALA 893  891  891  ALA ALA A . n 
A 1 894  LYS 894  892  892  LYS LYS A . n 
A 1 895  ASP 895  893  893  ASP ASP A . n 
A 1 896  ASN 896  894  894  ASN ASN A . n 
A 1 897  ILE 897  895  895  ILE ILE A . n 
A 1 898  GLU 898  896  896  GLU GLU A . n 
A 1 899  LYS 899  897  897  LYS LYS A . n 
A 1 900  HIS 900  898  898  HIS HIS A . n 
A 1 901  ILE 901  899  899  ILE ILE A . n 
A 1 902  GLU 902  900  900  GLU GLU A . n 
A 1 903  ARG 903  901  901  ARG ARG A . n 
A 1 904  MET 904  902  902  MET MET A . n 
A 1 905  ARG 905  903  903  ARG ARG A . n 
A 1 906  GLY 906  904  904  GLY GLY A . n 
A 1 907  LEU 907  905  905  LEU LEU A . n 
A 1 908  GLY 908  906  906  GLY GLY A . n 
A 1 909  ARG 909  907  907  ARG ARG A . n 
A 1 910  LYS 910  908  908  LYS LYS A . n 
A 1 911  VAL 911  909  909  VAL VAL A . n 
A 1 912  GLU 912  910  910  GLU GLU A . n 
A 1 913  GLN 913  911  911  GLN GLN A . n 
A 1 914  ILE 914  912  912  ILE ILE A . n 
A 1 915  GLY 915  913  913  GLY GLY A . n 
A 1 916  LEU 916  914  914  LEU LEU A . n 
A 1 917  ALA 917  915  915  ALA ALA A . n 
A 1 918  SER 918  916  916  SER SER A . n 
A 1 919  GLU 919  917  917  GLU GLU A . n 
A 1 920  THR 920  918  918  THR THR A . n 
A 1 921  GLY 921  919  919  GLY GLY A . n 
A 1 922  VAL 922  920  920  VAL VAL A . n 
A 1 923  GLY 923  921  921  GLY GLY A . n 
A 1 924  THR 924  922  922  THR THR A . n 
A 1 925  PHE 925  923  923  PHE PHE A . n 
A 1 926  VAL 926  924  924  VAL VAL A . n 
A 1 927  PRO 927  925  925  PRO PRO A . n 
A 1 928  PRO 928  926  926  PRO PRO A . n 
A 1 929  THR 929  927  927  THR THR A . n 
A 1 930  ILE 930  928  928  ILE ILE A . n 
A 1 931  ILE 931  929  929  ILE ILE A . n 
A 1 932  GLU 932  930  930  GLU GLU A . n 
A 1 933  LEU 933  931  931  LEU LEU A . n 
A 1 934  GLU 934  932  932  GLU GLU A . n 
A 1 935  LYS 935  933  933  LYS LYS A . n 
A 1 936  LEU 936  934  934  LEU LEU A . n 
A 1 937  SER 937  935  935  SER SER A . n 
A 1 938  ASP 938  936  936  ASP ASP A . n 
A 1 939  LEU 939  937  937  LEU LEU A . n 
A 1 940  GLN 940  938  938  GLN GLN A . n 
A 1 941  ARG 941  939  939  ARG ARG A . n 
A 1 942  GLU 942  940  940  GLU GLU A . n 
A 1 943  VAL 943  941  941  VAL VAL A . n 
A 1 944  PHE 944  942  942  PHE PHE A . n 
A 1 945  GLY 945  943  943  GLY GLY A . n 
A 1 946  PRO 946  944  944  PRO PRO A . n 
A 1 947  VAL 947  945  945  VAL VAL A . n 
A 1 948  LEU 948  946  946  LEU LEU A . n 
A 1 949  HIS 949  947  947  HIS HIS A . n 
A 1 950  VAL 950  948  948  VAL VAL A . n 
A 1 951  ILE 951  949  949  ILE ILE A . n 
A 1 952  ARG 952  950  950  ARG ARG A . n 
A 1 953  TYR 953  951  951  TYR TYR A . n 
A 1 954  ARG 954  952  952  ARG ARG A . n 
A 1 955  ARG 955  953  953  ARG ARG A . n 
A 1 956  ASP 956  954  954  ASP ASP A . n 
A 1 957  ASP 957  955  955  ASP ASP A . n 
A 1 958  LEU 958  956  956  LEU LEU A . n 
A 1 959  ASP 959  957  957  ASP ASP A . n 
A 1 960  ARG 960  958  958  ARG ARG A . n 
A 1 961  LEU 961  959  959  LEU LEU A . n 
A 1 962  VAL 962  960  960  VAL VAL A . n 
A 1 963  ASP 963  961  961  ASP ASP A . n 
A 1 964  ASP 964  962  962  ASP ASP A . n 
A 1 965  VAL 965  963  963  VAL VAL A . n 
A 1 966  ASN 966  964  964  ASN ASN A . n 
A 1 967  ALA 967  965  965  ALA ALA A . n 
A 1 968  THR 968  966  966  THR THR A . n 
A 1 969  GLY 969  967  967  GLY GLY A . n 
A 1 970  TYR 970  968  968  TYR TYR A . n 
A 1 971  GLY 971  969  969  GLY GLY A . n 
A 1 972  LEU 972  970  970  LEU LEU A . n 
A 1 973  THR 973  971  971  THR THR A . n 
A 1 974  PHE 974  972  972  PHE PHE A . n 
A 1 975  GLY 975  973  973  GLY GLY A . n 
A 1 976  LEU 976  974  974  LEU LEU A . n 
A 1 977  HIS 977  975  975  HIS HIS A . n 
A 1 978  THR 978  976  976  THR THR A . n 
A 1 979  ARG 979  977  977  ARG ARG A . n 
A 1 980  LEU 980  978  978  LEU LEU A . n 
A 1 981  ASP 981  979  979  ASP ASP A . n 
A 1 982  GLU 982  980  980  GLU GLU A . n 
A 1 983  THR 983  981  981  THR THR A . n 
A 1 984  ILE 984  982  982  ILE ILE A . n 
A 1 985  ALA 985  983  983  ALA ALA A . n 
A 1 986  HIS 986  984  984  HIS HIS A . n 
A 1 987  VAL 987  985  985  VAL VAL A . n 
A 1 988  THR 988  986  986  THR THR A . n 
A 1 989  SER 989  987  987  SER SER A . n 
A 1 990  ARG 990  988  988  ARG ARG A . n 
A 1 991  ILE 991  989  989  ILE ILE A . n 
A 1 992  LYS 992  990  990  LYS LYS A . n 
A 1 993  ALA 993  991  991  ALA ALA A . n 
A 1 994  GLY 994  992  992  GLY GLY A . n 
A 1 995  ASN 995  993  993  ASN ASN A . n 
A 1 996  LEU 996  994  994  LEU LEU A . n 
A 1 997  TYR 997  995  995  TYR TYR A . n 
A 1 998  ILE 998  996  996  ILE ILE A . n 
A 1 999  ASN 999  997  997  ASN ASN A . n 
A 1 1000 ARG 1000 998  998  ARG ARG A . n 
A 1 1001 ASN 1001 999  999  ASN ASN A . n 
A 1 1002 ILE 1002 1000 1000 ILE ILE A . n 
A 1 1003 ILE 1003 1001 1001 ILE ILE A . n 
A 1 1004 GLY 1004 1002 1002 GLY GLY A . n 
A 1 1005 ALA 1005 1003 1003 ALA ALA A . n 
A 1 1006 VAL 1006 1004 1004 VAL VAL A . n 
A 1 1007 VAL 1007 1005 1005 VAL VAL A . n 
A 1 1008 GLY 1008 1006 1006 GLY GLY A . n 
A 1 1009 VAL 1009 1007 1007 VAL VAL A . n 
A 1 1010 GLN 1010 1008 1008 GLN GLN A . n 
A 1 1011 PRO 1011 1009 1009 PRO PRO A . n 
A 1 1012 PHE 1012 1010 1010 PHE PHE A . n 
A 1 1013 GLY 1013 1011 1011 GLY GLY A . n 
A 1 1014 GLY 1014 1012 1012 GLY GLY A . n 
A 1 1015 ARG 1015 1013 1013 ARG ARG A . n 
A 1 1016 GLY 1016 1014 1014 GLY GLY A . n 
A 1 1017 LEU 1017 1015 1015 LEU LEU A . n 
A 1 1018 SER 1018 1016 1016 SER SER A . n 
A 1 1019 GLY 1019 1017 1017 GLY GLY A . n 
A 1 1020 THR 1020 1018 1018 THR THR A . n 
A 1 1021 GLY 1021 1019 1019 GLY GLY A . n 
A 1 1022 PRO 1022 1020 1020 PRO PRO A . n 
A 1 1023 LYS 1023 1021 1021 LYS LYS A . n 
A 1 1024 ALA 1024 1022 1022 ALA ALA A . n 
A 1 1025 GLY 1025 1023 1023 GLY GLY A . n 
A 1 1026 GLY 1026 1024 1024 GLY GLY A . n 
A 1 1027 PRO 1027 1025 1025 PRO PRO A . n 
A 1 1028 LEU 1028 1026 1026 LEU LEU A . n 
A 1 1029 TYR 1029 1027 1027 TYR TYR A . n 
A 1 1030 LEU 1030 1028 1028 LEU LEU A . n 
A 1 1031 GLY 1031 1029 1029 GLY GLY A . n 
A 1 1032 ARG 1032 1030 1030 ARG ARG A . n 
A 1 1033 LEU 1033 1031 1031 LEU LEU A . n 
A 1 1034 VAL 1034 1032 1032 VAL VAL A . n 
A 1 1035 THR 1035 1033 1033 THR THR A . n 
A 1 1036 THR 1036 1034 1034 THR THR A . n 
A 1 1037 ALA 1037 1035 1035 ALA ALA A . n 
A 1 1038 PRO 1038 1036 1036 PRO PRO A . n 
A 1 1039 VAL 1039 1037 1037 VAL VAL A . n 
A 1 1040 PRO 1040 1038 1038 PRO PRO A . n 
A 1 1041 PRO 1041 1039 1039 PRO PRO A . n 
A 1 1042 GLN 1042 1040 1040 GLN GLN A . n 
A 1 1043 HIS 1043 1041 1041 HIS HIS A . n 
A 1 1044 SER 1044 1042 1042 SER SER A . n 
A 1 1045 SER 1045 1043 1043 SER SER A . n 
A 1 1046 VAL 1046 1044 1044 VAL VAL A . n 
A 1 1047 HIS 1047 1045 1045 HIS HIS A . n 
A 1 1048 THR 1048 1046 1046 THR THR A . n 
A 1 1049 ASP 1049 1047 1047 ASP ASP A . n 
A 1 1050 PRO 1050 1048 1048 PRO PRO A . n 
A 1 1051 VAL 1051 1049 1049 VAL VAL A . n 
A 1 1052 LEU 1052 1050 1050 LEU LEU A . n 
A 1 1053 LEU 1053 1051 1051 LEU LEU A . n 
A 1 1054 ASP 1054 1052 1052 ASP ASP A . n 
A 1 1055 PHE 1055 1053 1053 PHE PHE A . n 
A 1 1056 ALA 1056 1054 1054 ALA ALA A . n 
A 1 1057 LYS 1057 1055 1055 LYS LYS A . n 
A 1 1058 TRP 1058 1056 1056 TRP TRP A . n 
A 1 1059 LEU 1059 1057 1057 LEU LEU A . n 
A 1 1060 ASP 1060 1058 1058 ASP ASP A . n 
A 1 1061 GLY 1061 1059 1059 GLY GLY A . n 
A 1 1062 LYS 1062 1060 1060 LYS LYS A . n 
A 1 1063 GLY 1063 1061 1061 GLY GLY A . n 
A 1 1064 ALA 1064 1062 1062 ALA ALA A . n 
A 1 1065 ARG 1065 1063 1063 ARG ARG A . n 
A 1 1066 ALA 1066 1064 1064 ALA ALA A . n 
A 1 1067 GLU 1067 1065 1065 GLU GLU A . n 
A 1 1068 ALA 1068 1066 1066 ALA ALA A . n 
A 1 1069 GLU 1069 1067 1067 GLU GLU A . n 
A 1 1070 ALA 1070 1068 1068 ALA ALA A . n 
A 1 1071 ALA 1071 1069 1069 ALA ALA A . n 
A 1 1072 ARG 1072 1070 1070 ARG ARG A . n 
A 1 1073 ASN 1073 1071 1071 ASN ASN A . n 
A 1 1074 ALA 1074 1072 1072 ALA ALA A . n 
A 1 1075 GLY 1075 1073 1073 GLY GLY A . n 
A 1 1076 SER 1076 1074 1074 SER SER A . n 
A 1 1077 SER 1077 1075 1075 SER SER A . n 
A 1 1078 SER 1078 1076 1076 SER SER A . n 
A 1 1079 ALA 1079 1077 1077 ALA ALA A . n 
A 1 1080 LEU 1080 1078 1078 LEU LEU A . n 
A 1 1081 GLY 1081 1079 1079 GLY GLY A . n 
A 1 1082 LEU 1082 1080 1080 LEU LEU A . n 
A 1 1083 ASP 1083 1081 1081 ASP ASP A . n 
A 1 1084 LEU 1084 1082 1082 LEU LEU A . n 
A 1 1085 GLU 1085 1083 1083 GLU GLU A . n 
A 1 1086 LEU 1086 1084 1084 LEU LEU A . n 
A 1 1087 PRO 1087 1085 1085 PRO PRO A . n 
A 1 1088 GLY 1088 1086 1086 GLY GLY A . n 
A 1 1089 PRO 1089 1087 1087 PRO PRO A . n 
A 1 1090 VAL 1090 1088 1088 VAL VAL A . n 
A 1 1091 GLY 1091 1089 1089 GLY GLY A . n 
A 1 1092 GLU 1092 1090 1090 GLU GLU A . n 
A 1 1093 ARG 1093 1091 1091 ARG ARG A . n 
A 1 1094 ASN 1094 1092 1092 ASN ASN A . n 
A 1 1095 LEU 1095 1093 1093 LEU LEU A . n 
A 1 1096 TYR 1096 1094 1094 TYR TYR A . n 
A 1 1097 THR 1097 1095 1095 THR THR A . n 
A 1 1098 LEU 1098 1096 1096 LEU LEU A . n 
A 1 1099 HIS 1099 1097 1097 HIS HIS A . n 
A 1 1100 ALA 1100 1098 1098 ALA ALA A . n 
A 1 1101 ARG 1101 1099 1099 ARG ARG A . n 
A 1 1102 GLY 1102 1100 1100 GLY GLY A . n 
A 1 1103 ARG 1103 1101 1101 ARG ARG A . n 
A 1 1104 ILE 1104 1102 1102 ILE ILE A . n 
A 1 1105 LEU 1105 1103 1103 LEU LEU A . n 
A 1 1106 LEU 1106 1104 1104 LEU LEU A . n 
A 1 1107 VAL 1107 1105 1105 VAL VAL A . n 
A 1 1108 PRO 1108 1106 1106 PRO PRO A . n 
A 1 1109 ALA 1109 1107 1107 ALA ALA A . n 
A 1 1110 THR 1110 1108 1108 THR THR A . n 
A 1 1111 GLU 1111 1109 1109 GLU GLU A . n 
A 1 1112 SER 1112 1110 1110 SER SER A . n 
A 1 1113 GLY 1113 1111 1111 GLY GLY A . n 
A 1 1114 LEU 1114 1112 1112 LEU LEU A . n 
A 1 1115 TYR 1115 1113 1113 TYR TYR A . n 
A 1 1116 HIS 1116 1114 1114 HIS HIS A . n 
A 1 1117 GLN 1117 1115 1115 GLN GLN A . n 
A 1 1118 LEU 1118 1116 1116 LEU LEU A . n 
A 1 1119 ALA 1119 1117 1117 ALA ALA A . n 
A 1 1120 ALA 1120 1118 1118 ALA ALA A . n 
A 1 1121 ALA 1121 1119 1119 ALA ALA A . n 
A 1 1122 LEU 1122 1120 1120 LEU LEU A . n 
A 1 1123 ALA 1123 1121 1121 ALA ALA A . n 
A 1 1124 THR 1124 1122 1122 THR THR A . n 
A 1 1125 GLY 1125 1123 1123 GLY GLY A . n 
A 1 1126 ASN 1126 1124 1124 ASN ASN A . n 
A 1 1127 SER 1127 1125 1125 SER SER A . n 
A 1 1128 VAL 1128 1126 1126 VAL VAL A . n 
A 1 1129 ALA 1129 1127 1127 ALA ALA A . n 
A 1 1130 ILE 1130 1128 1128 ILE ILE A . n 
A 1 1131 ASP 1131 1129 1129 ASP ASP A . n 
A 1 1132 ALA 1132 1130 1130 ALA ALA A . n 
A 1 1133 ALA 1133 1131 1131 ALA ALA A . n 
A 1 1134 SER 1134 1132 1132 SER SER A . n 
A 1 1135 GLY 1135 1133 1133 GLY GLY A . n 
A 1 1136 LEU 1136 1134 1134 LEU LEU A . n 
A 1 1137 GLN 1137 1135 1135 GLN GLN A . n 
A 1 1138 ALA 1138 1136 1136 ALA ALA A . n 
A 1 1139 SER 1139 1137 1137 SER SER A . n 
A 1 1140 LEU 1140 1138 1138 LEU LEU A . n 
A 1 1141 LYS 1141 1139 1139 LYS LYS A . n 
A 1 1142 ASN 1142 1140 1140 ASN ASN A . n 
A 1 1143 LEU 1143 1141 1141 LEU LEU A . n 
A 1 1144 PRO 1144 1142 1142 PRO PRO A . n 
A 1 1145 GLN 1145 1143 1143 GLN GLN A . n 
A 1 1146 THR 1146 1144 1144 THR THR A . n 
A 1 1147 VAL 1147 1145 1145 VAL VAL A . n 
A 1 1148 GLY 1148 1146 1146 GLY GLY A . n 
A 1 1149 LEU 1149 1147 1147 LEU LEU A . n 
A 1 1150 ARG 1150 1148 1148 ARG ARG A . n 
A 1 1151 VAL 1151 1149 1149 VAL VAL A . n 
A 1 1152 SER 1152 1150 1150 SER SER A . n 
A 1 1153 TRP 1153 1151 1151 TRP TRP A . n 
A 1 1154 SER 1154 1152 1152 SER SER A . n 
A 1 1155 LYS 1155 1153 1153 LYS LYS A . n 
A 1 1156 ASP 1156 1154 1154 ASP ASP A . n 
A 1 1157 TRP 1157 1155 1155 TRP TRP A . n 
A 1 1158 ALA 1158 1156 1156 ALA ALA A . n 
A 1 1159 ALA 1159 1157 1157 ALA ALA A . n 
A 1 1160 ASP 1160 1158 1158 ASP ASP A . n 
A 1 1161 GLY 1161 1159 1159 GLY GLY A . n 
A 1 1162 PRO 1162 1160 1160 PRO PRO A . n 
A 1 1163 PHE 1163 1161 1161 PHE PHE A . n 
A 1 1164 ALA 1164 1162 1162 ALA ALA A . n 
A 1 1165 GLY 1165 1163 1163 GLY GLY A . n 
A 1 1166 ALA 1166 1164 1164 ALA ALA A . n 
A 1 1167 LEU 1167 1165 1165 LEU LEU A . n 
A 1 1168 VAL 1168 1166 1166 VAL VAL A . n 
A 1 1169 GLU 1169 1167 1167 GLU GLU A . n 
A 1 1170 GLY 1170 1168 1168 GLY GLY A . n 
A 1 1171 ASP 1171 1169 1169 ASP ASP A . n 
A 1 1172 ALA 1172 1170 1170 ALA ALA A . n 
A 1 1173 GLU 1173 1171 1171 GLU GLU A . n 
A 1 1174 ARG 1174 1172 1172 ARG ARG A . n 
A 1 1175 ILE 1175 1173 1173 ILE ILE A . n 
A 1 1176 ARG 1176 1174 1174 ARG ARG A . n 
A 1 1177 ALA 1177 1175 1175 ALA ALA A . n 
A 1 1178 VAL 1178 1176 1176 VAL VAL A . n 
A 1 1179 ASN 1179 1177 1177 ASN ASN A . n 
A 1 1180 LYS 1180 1178 1178 LYS LYS A . n 
A 1 1181 ALA 1181 1179 1179 ALA ALA A . n 
A 1 1182 ILE 1182 1180 1180 ILE ILE A . n 
A 1 1183 ALA 1183 1181 1181 ALA ALA A . n 
A 1 1184 ALA 1184 1182 1182 ALA ALA A . n 
A 1 1185 LEU 1185 1183 1183 LEU LEU A . n 
A 1 1186 PRO 1186 1184 1184 PRO PRO A . n 
A 1 1187 GLY 1187 1185 1185 GLY GLY A . n 
A 1 1188 PRO 1188 1186 1186 PRO PRO A . n 
A 1 1189 LEU 1189 1187 1187 LEU LEU A . n 
A 1 1190 LEU 1190 1188 1188 LEU LEU A . n 
A 1 1191 LEU 1191 1189 1189 LEU LEU A . n 
A 1 1192 VAL 1192 1190 1190 VAL VAL A . n 
A 1 1193 GLN 1193 1191 1191 GLN GLN A . n 
A 1 1194 ALA 1194 1192 1192 ALA ALA A . n 
A 1 1195 ALA 1195 1193 1193 ALA ALA A . n 
A 1 1196 SER 1196 1194 1194 SER SER A . n 
A 1 1197 SER 1197 1195 1195 SER SER A . n 
A 1 1198 GLY 1198 1196 1196 GLY GLY A . n 
A 1 1199 GLU 1199 1197 1197 GLU GLU A . n 
A 1 1200 ILE 1200 1198 1198 ILE ILE A . n 
A 1 1201 ALA 1201 1199 1199 ALA ALA A . n 
A 1 1202 ARG 1202 1200 1200 ARG ARG A . n 
A 1 1203 ASN 1203 1201 1201 ASN ASN A . n 
A 1 1204 PRO 1204 1202 1202 PRO PRO A . n 
A 1 1205 ASP 1205 1203 1203 ASP ASP A . n 
A 1 1206 ALA 1206 1204 1204 ALA ALA A . n 
A 1 1207 TYR 1207 1205 1205 TYR TYR A . n 
A 1 1208 CYS 1208 1206 1206 CYS CYS A . n 
A 1 1209 LEU 1209 1207 1207 LEU LEU A . n 
A 1 1210 ASN 1210 1208 1208 ASN ASN A . n 
A 1 1211 TRP 1211 1209 1209 TRP TRP A . n 
A 1 1212 LEU 1212 1210 1210 LEU LEU A . n 
A 1 1213 VAL 1213 1211 1211 VAL VAL A . n 
A 1 1214 GLU 1214 1212 1212 GLU GLU A . n 
A 1 1215 GLU 1215 1213 1213 GLU GLU A . n 
A 1 1216 VAL 1216 1214 1214 VAL VAL A . n 
A 1 1217 SER 1217 1215 1215 SER SER A . n 
A 1 1218 ALA 1218 1216 1216 ALA ALA A . n 
A 1 1219 SER 1219 1217 1217 SER SER A . n 
A 1 1220 ILE 1220 1218 1218 ILE ILE A . n 
A 1 1221 ASN 1221 1219 1219 ASN ASN A . n 
A 1 1222 THR 1222 1220 1220 THR THR A . n 
A 1 1223 ALA 1223 1221 1221 ALA ALA A . n 
A 1 1224 ALA 1224 1222 1222 ALA ALA A . n 
A 1 1225 ALA 1225 1223 1223 ALA ALA A . n 
A 1 1226 GLY 1226 1224 1224 GLY GLY A . n 
A 1 1227 GLY 1227 1225 1225 GLY GLY A . n 
A 1 1228 ASN 1228 1226 1226 ASN ASN A . n 
A 1 1229 ALA 1229 1227 1227 ALA ALA A . n 
A 1 1230 SER 1230 1228 1228 SER SER A . n 
A 1 1231 LEU 1231 1229 1229 LEU LEU A . n 
A 1 1232 MET 1232 1230 1230 MET MET A . n 
A 1 1233 ALA 1233 1231 1231 ALA ALA A . n 
A 1 1234 ILE 1234 1232 1232 ILE ILE A . n 
A 1 1235 GLY 1235 1233 1233 GLY GLY A . n 
B 1 1    SER 1    -1   ?    ?   ?   B . n 
B 1 2    MET 2    0    ?    ?   ?   B . n 
B 1 3    MET 3    1    ?    ?   ?   B . n 
B 1 4    SER 4    2    ?    ?   ?   B . n 
B 1 5    PRO 5    3    ?    ?   ?   B . n 
B 1 6    ASN 6    4    ?    ?   ?   B . n 
B 1 7    PRO 7    5    ?    ?   ?   B . n 
B 1 8    LEU 8    6    ?    ?   ?   B . n 
B 1 9    GLN 9    7    ?    ?   ?   B . n 
B 1 10   LYS 10   8    ?    ?   ?   B . n 
B 1 11   PRO 11   9    ?    ?   ?   B . n 
B 1 12   ALA 12   10   ?    ?   ?   B . n 
B 1 13   ILE 13   11   ?    ?   ?   B . n 
B 1 14   ASP 14   12   ?    ?   ?   B . n 
B 1 15   ALA 15   13   ?    ?   ?   B . n 
B 1 16   ALA 16   14   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   ?    ?   ?   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  ?    ?   ?   B . n 
B 1 496  GLY 496  494  494  GLY GLY B . n 
B 1 497  ALA 497  495  495  ALA ALA B . n 
B 1 498  ASN 498  496  496  ASN ASN B . n 
B 1 499  SER 499  497  497  SER SER B . n 
B 1 500  SER 500  498  498  SER SER B . n 
B 1 501  PHE 501  499  499  PHE PHE B . n 
B 1 502  VAL 502  500  500  VAL VAL B . n 
B 1 503  HIS 503  501  501  HIS HIS B . n 
B 1 504  ARG 504  502  502  ARG ARG B . n 
B 1 505  ILE 505  503  503  ILE ILE B . n 
B 1 506  ASN 506  504  504  ASN ASN B . n 
B 1 507  ASP 507  505  505  ASP ASP B . n 
B 1 508  PRO 508  506  506  PRO PRO B . n 
B 1 509  LYS 509  507  507  LYS LYS B . n 
B 1 510  VAL 510  508  508  VAL VAL B . n 
B 1 511  SER 511  509  509  SER SER B . n 
B 1 512  ILE 512  510  510  ILE ILE B . n 
B 1 513  ASP 513  511  511  ASP ASP B . n 
B 1 514  GLU 514  512  512  GLU GLU B . n 
B 1 515  LEU 515  513  513  LEU LEU B . n 
B 1 516  ILE 516  514  514  ILE ILE B . n 
B 1 517  ALA 517  515  515  ALA ALA B . n 
B 1 518  ASP 518  516  516  ASP ASP B . n 
B 1 519  PRO 519  517  517  PRO PRO B . n 
B 1 520  VAL 520  518  518  VAL VAL B . n 
B 1 521  GLU 521  519  519  GLU GLU B . n 
B 1 522  VAL 522  520  520  VAL VAL B . n 
B 1 523  VAL 523  521  521  VAL VAL B . n 
B 1 524  ARG 524  522  522  ARG ARG B . n 
B 1 525  ALA 525  523  523  ALA ALA B . n 
B 1 526  MET 526  524  524  MET MET B . n 
B 1 527  PRO 527  525  525  PRO PRO B . n 
B 1 528  VAL 528  526  526  VAL VAL B . n 
B 1 529  VAL 529  527  527  VAL VAL B . n 
B 1 530  GLY 530  528  528  GLY GLY B . n 
B 1 531  ALA 531  529  529  ALA ALA B . n 
B 1 532  LYS 532  530  530  LYS LYS B . n 
B 1 533  HIS 533  531  531  HIS HIS B . n 
B 1 534  ASP 534  532  532  ASP ASP B . n 
B 1 535  ARG 535  533  533  ARG ARG B . n 
B 1 536  ILE 536  534  534  ILE ILE B . n 
B 1 537  ALA 537  535  535  ALA ALA B . n 
B 1 538  LEU 538  536  536  LEU LEU B . n 
B 1 539  PRO 539  537  537  PRO PRO B . n 
B 1 540  ALA 540  538  538  ALA ALA B . n 
B 1 541  GLU 541  539  539  GLU GLU B . n 
B 1 542  LEU 542  540  540  LEU LEU B . n 
B 1 543  PHE 543  541  541  PHE PHE B . n 
B 1 544  GLY 544  542  542  GLY GLY B . n 
B 1 545  ASP 545  543  543  ASP ASP B . n 
B 1 546  ALA 546  544  544  ALA ALA B . n 
B 1 547  ARG 547  545  545  ARG ARG B . n 
B 1 548  THR 548  546  546  THR THR B . n 
B 1 549  ASN 549  547  547  ASN ASN B . n 
B 1 550  SER 550  548  548  SER SER B . n 
B 1 551  ALA 551  549  549  ALA ALA B . n 
B 1 552  GLY 552  550  550  GLY GLY B . n 
B 1 553  LEU 553  551  551  LEU LEU B . n 
B 1 554  ASP 554  552  552  ASP ASP B . n 
B 1 555  LEU 555  553  553  LEU LEU B . n 
B 1 556  SER 556  554  554  SER SER B . n 
B 1 557  ASN 557  555  555  ASN ASN B . n 
B 1 558  GLU 558  556  556  GLU GLU B . n 
B 1 559  GLU 559  557  557  GLU GLU B . n 
B 1 560  THR 560  558  558  THR THR B . n 
B 1 561  LEU 561  559  559  LEU LEU B . n 
B 1 562  ALA 562  560  560  ALA ALA B . n 
B 1 563  SER 563  561  561  SER SER B . n 
B 1 564  LEU 564  562  562  LEU LEU B . n 
B 1 565  THR 565  563  563  THR THR B . n 
B 1 566  GLU 566  564  564  GLU GLU B . n 
B 1 567  ALA 567  565  565  ALA ALA B . n 
B 1 568  LEU 568  566  566  LEU LEU B . n 
B 1 569  ARG 569  567  567  ARG ARG B . n 
B 1 570  GLU 570  568  568  GLU GLU B . n 
B 1 571  SER 571  569  569  SER SER B . n 
B 1 572  ALA 572  570  570  ALA ALA B . n 
B 1 573  ALA 573  571  571  ALA ALA B . n 
B 1 574  MET 574  572  572  MET MET B . n 
B 1 575  LYS 575  573  573  LYS LYS B . n 
B 1 576  TRP 576  574  574  TRP TRP B . n 
B 1 577  THR 577  575  575  THR THR B . n 
B 1 578  ALA 578  576  576  ALA ALA B . n 
B 1 579  LEU 579  577  577  LEU LEU B . n 
B 1 580  PRO 580  578  578  PRO PRO B . n 
B 1 581  GLN 581  579  579  GLN GLN B . n 
B 1 582  LEU 582  580  580  LEU LEU B . n 
B 1 583  ALA 583  581  581  ALA ALA B . n 
B 1 584  THR 584  582  582  THR THR B . n 
B 1 585  GLY 585  583  583  GLY GLY B . n 
B 1 586  PRO 586  584  584  PRO PRO B . n 
B 1 587  ALA 587  585  585  ALA ALA B . n 
B 1 588  ALA 588  586  586  ALA ALA B . n 
B 1 589  GLY 589  587  587  GLY GLY B . n 
B 1 590  GLU 590  588  588  GLU GLU B . n 
B 1 591  THR 591  589  589  THR THR B . n 
B 1 592  ARG 592  590  590  ARG ARG B . n 
B 1 593  THR 593  591  591  THR THR B . n 
B 1 594  VAL 594  592  592  VAL VAL B . n 
B 1 595  LEU 595  593  593  LEU LEU B . n 
B 1 596  ASN 596  594  594  ASN ASN B . n 
B 1 597  PRO 597  595  595  PRO PRO B . n 
B 1 598  GLY 598  596  596  GLY GLY B . n 
B 1 599  ASP 599  597  597  ASP ASP B . n 
B 1 600  HIS 600  598  598  HIS HIS B . n 
B 1 601  ARG 601  599  599  ARG ARG B . n 
B 1 602  ASP 602  600  600  ASP ASP B . n 
B 1 603  VAL 603  601  601  VAL VAL B . n 
B 1 604  VAL 604  602  602  VAL VAL B . n 
B 1 605  GLY 605  603  603  GLY GLY B . n 
B 1 606  SER 606  604  604  SER SER B . n 
B 1 607  VAL 607  605  605  VAL VAL B . n 
B 1 608  THR 608  606  606  THR THR B . n 
B 1 609  GLU 609  607  607  GLU GLU B . n 
B 1 610  THR 610  608  608  THR THR B . n 
B 1 611  SER 611  609  609  SER SER B . n 
B 1 612  GLU 612  610  610  GLU GLU B . n 
B 1 613  GLU 613  611  611  GLU GLU B . n 
B 1 614  ASP 614  612  612  ASP ASP B . n 
B 1 615  ALA 615  613  613  ALA ALA B . n 
B 1 616  ARG 616  614  614  ARG ARG B . n 
B 1 617  ARG 617  615  615  ARG ARG B . n 
B 1 618  ALA 618  616  616  ALA ALA B . n 
B 1 619  VAL 619  617  617  VAL VAL B . n 
B 1 620  ARG 620  618  618  ARG ARG B . n 
B 1 621  LEU 621  619  619  LEU LEU B . n 
B 1 622  ALA 622  620  620  ALA ALA B . n 
B 1 623  ALA 623  621  621  ALA ALA B . n 
B 1 624  ASP 624  622  622  ASP ASP B . n 
B 1 625  ALA 625  623  623  ALA ALA B . n 
B 1 626  ALA 626  624  624  ALA ALA B . n 
B 1 627  PRO 627  625  625  PRO PRO B . n 
B 1 628  ASP 628  626  626  ASP ASP B . n 
B 1 629  TRP 629  627  627  TRP TRP B . n 
B 1 630  ALA 630  628  628  ALA ALA B . n 
B 1 631  ALA 631  629  629  ALA ALA B . n 
B 1 632  VAL 632  630  630  VAL VAL B . n 
B 1 633  PRO 633  631  631  PRO PRO B . n 
B 1 634  PRO 634  632  632  PRO PRO B . n 
B 1 635  SER 635  633  633  SER SER B . n 
B 1 636  GLU 636  634  634  GLU GLU B . n 
B 1 637  ARG 637  635  635  ARG ARG B . n 
B 1 638  ALA 638  636  636  ALA ALA B . n 
B 1 639  ALA 639  637  637  ALA ALA B . n 
B 1 640  CYS 640  638  638  CYS CYS B . n 
B 1 641  LEU 641  639  639  LEU LEU B . n 
B 1 642  ASP 642  640  640  ASP ASP B . n 
B 1 643  ARG 643  641  641  ARG ARG B . n 
B 1 644  ALA 644  642  642  ALA ALA B . n 
B 1 645  ALA 645  643  643  ALA ALA B . n 
B 1 646  GLU 646  644  644  GLU GLU B . n 
B 1 647  LEU 647  645  645  LEU LEU B . n 
B 1 648  MET 648  646  646  MET MET B . n 
B 1 649  GLN 649  647  647  GLN GLN B . n 
B 1 650  ALA 650  648  648  ALA ALA B . n 
B 1 651  ARG 651  649  649  ARG ARG B . n 
B 1 652  MET 652  650  650  MET MET B . n 
B 1 653  PRO 653  651  651  PRO PRO B . n 
B 1 654  THR 654  652  652  THR THR B . n 
B 1 655  LEU 655  653  653  LEU LEU B . n 
B 1 656  LEU 656  654  654  LEU LEU B . n 
B 1 657  GLY 657  655  655  GLY GLY B . n 
B 1 658  LEU 658  656  656  LEU LEU B . n 
B 1 659  ILE 659  657  657  ILE ILE B . n 
B 1 660  ILE 660  658  658  ILE ILE B . n 
B 1 661  ARG 661  659  659  ARG ARG B . n 
B 1 662  GLU 662  660  660  GLU GLU B . n 
B 1 663  ALA 663  661  661  ALA ALA B . n 
B 1 664  GLY 664  662  662  GLY GLY B . n 
B 1 665  LYS 665  663  663  LYS LYS B . n 
B 1 666  SER 666  664  664  SER SER B . n 
B 1 667  ALA 667  665  665  ALA ALA B . n 
B 1 668  LEU 668  666  666  LEU LEU B . n 
B 1 669  ASN 669  667  667  ASN ASN B . n 
B 1 670  ALA 670  668  668  ALA ALA B . n 
B 1 671  ILE 671  669  669  ILE ILE B . n 
B 1 672  ALA 672  670  670  ALA ALA B . n 
B 1 673  GLU 673  671  671  GLU GLU B . n 
B 1 674  VAL 674  672  672  VAL VAL B . n 
B 1 675  ARG 675  673  673  ARG ARG B . n 
B 1 676  GLU 676  674  674  GLU GLU B . n 
B 1 677  ALA 677  675  675  ALA ALA B . n 
B 1 678  ILE 678  676  676  ILE ILE B . n 
B 1 679  ASP 679  677  677  ASP ASP B . n 
B 1 680  PHE 680  678  678  PHE PHE B . n 
B 1 681  LEU 681  679  679  LEU LEU B . n 
B 1 682  ARG 682  680  680  ARG ARG B . n 
B 1 683  TYR 683  681  681  TYR TYR B . n 
B 1 684  TYR 684  682  682  TYR TYR B . n 
B 1 685  ALA 685  683  683  ALA ALA B . n 
B 1 686  GLU 686  684  684  GLU GLU B . n 
B 1 687  GLN 687  685  685  GLN GLN B . n 
B 1 688  THR 688  686  686  THR THR B . n 
B 1 689  ARG 689  687  687  ARG ARG B . n 
B 1 690  ARG 690  688  688  ARG ARG B . n 
B 1 691  THR 691  689  689  THR THR B . n 
B 1 692  LEU 692  690  690  LEU LEU B . n 
B 1 693  GLY 693  691  691  GLY GLY B . n 
B 1 694  PRO 694  692  692  PRO PRO B . n 
B 1 695  GLY 695  693  693  GLY GLY B . n 
B 1 696  HIS 696  694  694  HIS HIS B . n 
B 1 697  GLY 697  695  695  GLY GLY B . n 
B 1 698  PRO 698  696  696  PRO PRO B . n 
B 1 699  LEU 699  697  697  LEU LEU B . n 
B 1 700  GLY 700  698  698  GLY GLY B . n 
B 1 701  PRO 701  699  699  PRO PRO B . n 
B 1 702  ILE 702  700  700  ILE ILE B . n 
B 1 703  VAL 703  701  701  VAL VAL B . n 
B 1 704  CYS 704  702  702  CYS CYS B . n 
B 1 705  ILE 705  703  703  ILE ILE B . n 
B 1 706  SER 706  704  704  SER SER B . n 
B 1 707  PRO 707  705  705  PRO PRO B . n 
B 1 708  TRP 708  706  706  TRP TRP B . n 
B 1 709  ASN 709  707  707  ASN ASN B . n 
B 1 710  PHE 710  708  708  PHE PHE B . n 
B 1 711  PRO 711  709  709  PRO PRO B . n 
B 1 712  LEU 712  710  710  LEU LEU B . n 
B 1 713  ALA 713  711  711  ALA ALA B . n 
B 1 714  ILE 714  712  712  ILE ILE B . n 
B 1 715  PHE 715  713  713  PHE PHE B . n 
B 1 716  THR 716  714  714  THR THR B . n 
B 1 717  GLY 717  715  715  GLY GLY B . n 
B 1 718  GLN 718  716  716  GLN GLN B . n 
B 1 719  ILE 719  717  717  ILE ILE B . n 
B 1 720  ALA 720  718  718  ALA ALA B . n 
B 1 721  ALA 721  719  719  ALA ALA B . n 
B 1 722  ALA 722  720  720  ALA ALA B . n 
B 1 723  LEU 723  721  721  LEU LEU B . n 
B 1 724  VAL 724  722  722  VAL VAL B . n 
B 1 725  ALA 725  723  723  ALA ALA B . n 
B 1 726  GLY 726  724  724  GLY GLY B . n 
B 1 727  ASN 727  725  725  ASN ASN B . n 
B 1 728  PRO 728  726  726  PRO PRO B . n 
B 1 729  VAL 729  727  727  VAL VAL B . n 
B 1 730  LEU 730  728  728  LEU LEU B . n 
B 1 731  ALA 731  729  729  ALA ALA B . n 
B 1 732  LYS 732  730  730  LYS LYS B . n 
B 1 733  PRO 733  731  731  PRO PRO B . n 
B 1 734  ALA 734  732  732  ALA ALA B . n 
B 1 735  GLU 735  733  733  GLU GLU B . n 
B 1 736  GLU 736  734  734  GLU GLU B . n 
B 1 737  THR 737  735  735  THR THR B . n 
B 1 738  PRO 738  736  736  PRO PRO B . n 
B 1 739  LEU 739  737  737  LEU LEU B . n 
B 1 740  ILE 740  738  738  ILE ILE B . n 
B 1 741  ALA 741  739  739  ALA ALA B . n 
B 1 742  ALA 742  740  740  ALA ALA B . n 
B 1 743  GLU 743  741  741  GLU GLU B . n 
B 1 744  GLY 744  742  742  GLY GLY B . n 
B 1 745  VAL 745  743  743  VAL VAL B . n 
B 1 746  ARG 746  744  744  ARG ARG B . n 
B 1 747  ILE 747  745  745  ILE ILE B . n 
B 1 748  LEU 748  746  746  LEU LEU B . n 
B 1 749  ARG 749  747  747  ARG ARG B . n 
B 1 750  GLU 750  748  748  GLU GLU B . n 
B 1 751  ALA 751  749  749  ALA ALA B . n 
B 1 752  GLY 752  750  750  GLY GLY B . n 
B 1 753  ILE 753  751  751  ILE ILE B . n 
B 1 754  PRO 754  752  752  PRO PRO B . n 
B 1 755  ALA 755  753  753  ALA ALA B . n 
B 1 756  SER 756  754  754  SER SER B . n 
B 1 757  ALA 757  755  755  ALA ALA B . n 
B 1 758  LEU 758  756  756  LEU LEU B . n 
B 1 759  GLN 759  757  757  GLN GLN B . n 
B 1 760  LEU 760  758  758  LEU LEU B . n 
B 1 761  LEU 761  759  759  LEU LEU B . n 
B 1 762  PRO 762  760  760  PRO PRO B . n 
B 1 763  GLY 763  761  761  GLY GLY B . n 
B 1 764  ASP 764  762  762  ASP ASP B . n 
B 1 765  GLY 765  763  763  GLY GLY B . n 
B 1 766  ARG 766  764  764  ARG ARG B . n 
B 1 767  VAL 767  765  765  VAL VAL B . n 
B 1 768  GLY 768  766  766  GLY GLY B . n 
B 1 769  ALA 769  767  767  ALA ALA B . n 
B 1 770  ALA 770  768  768  ALA ALA B . n 
B 1 771  LEU 771  769  769  LEU LEU B . n 
B 1 772  VAL 772  770  770  VAL VAL B . n 
B 1 773  ALA 773  771  771  ALA ALA B . n 
B 1 774  ALA 774  772  772  ALA ALA B . n 
B 1 775  ALA 775  773  773  ALA ALA B . n 
B 1 776  GLU 776  774  774  GLU GLU B . n 
B 1 777  THR 777  775  775  THR THR B . n 
B 1 778  ALA 778  776  776  ALA ALA B . n 
B 1 779  GLY 779  777  777  GLY GLY B . n 
B 1 780  VAL 780  778  778  VAL VAL B . n 
B 1 781  MET 781  779  779  MET MET B . n 
B 1 782  PHE 782  780  780  PHE PHE B . n 
B 1 783  THR 783  781  781  THR THR B . n 
B 1 784  GLY 784  782  782  GLY GLY B . n 
B 1 785  SER 785  783  783  SER SER B . n 
B 1 786  THR 786  784  784  THR THR B . n 
B 1 787  GLU 787  785  785  GLU GLU B . n 
B 1 788  VAL 788  786  786  VAL VAL B . n 
B 1 789  ALA 789  787  787  ALA ALA B . n 
B 1 790  ARG 790  788  788  ARG ARG B . n 
B 1 791  LEU 791  789  789  LEU LEU B . n 
B 1 792  ILE 792  790  790  ILE ILE B . n 
B 1 793  GLN 793  791  791  GLN GLN B . n 
B 1 794  ALA 794  792  792  ALA ALA B . n 
B 1 795  GLN 795  793  793  GLN GLN B . n 
B 1 796  LEU 796  794  794  LEU LEU B . n 
B 1 797  ALA 797  795  795  ALA ALA B . n 
B 1 798  ASP 798  796  796  ASP ASP B . n 
B 1 799  ARG 799  797  797  ARG ARG B . n 
B 1 800  LEU 800  798  798  LEU LEU B . n 
B 1 801  SER 801  799  799  SER SER B . n 
B 1 802  PRO 802  800  800  PRO PRO B . n 
B 1 803  ALA 803  801  801  ALA ALA B . n 
B 1 804  GLY 804  802  802  GLY GLY B . n 
B 1 805  ARG 805  803  803  ARG ARG B . n 
B 1 806  PRO 806  804  804  PRO PRO B . n 
B 1 807  ILE 807  805  805  ILE ILE B . n 
B 1 808  PRO 808  806  806  PRO PRO B . n 
B 1 809  LEU 809  807  807  LEU LEU B . n 
B 1 810  ILE 810  808  808  ILE ILE B . n 
B 1 811  ALA 811  809  809  ALA ALA B . n 
B 1 812  GLU 812  810  810  GLU GLU B . n 
B 1 813  THR 813  811  811  THR THR B . n 
B 1 814  GLY 814  812  812  GLY GLY B . n 
B 1 815  GLY 815  813  813  GLY GLY B . n 
B 1 816  GLN 816  814  814  GLN GLN B . n 
B 1 817  ASN 817  815  815  ASN ASN B . n 
B 1 818  ALA 818  816  816  ALA ALA B . n 
B 1 819  MET 819  817  817  MET MET B . n 
B 1 820  ILE 820  818  818  ILE ILE B . n 
B 1 821  VAL 821  819  819  VAL VAL B . n 
B 1 822  ASP 822  820  820  ASP ASP B . n 
B 1 823  SER 823  821  821  SER SER B . n 
B 1 824  SER 824  822  822  SER SER B . n 
B 1 825  ALA 825  823  823  ALA ALA B . n 
B 1 826  LEU 826  824  824  LEU LEU B . n 
B 1 827  ALA 827  825  825  ALA ALA B . n 
B 1 828  GLU 828  826  826  GLU GLU B . n 
B 1 829  GLN 829  827  827  GLN GLN B . n 
B 1 830  VAL 830  828  828  VAL VAL B . n 
B 1 831  VAL 831  829  829  VAL VAL B . n 
B 1 832  GLY 832  830  830  GLY GLY B . n 
B 1 833  ASP 833  831  831  ASP ASP B . n 
B 1 834  VAL 834  832  832  VAL VAL B . n 
B 1 835  ILE 835  833  833  ILE ILE B . n 
B 1 836  THR 836  834  834  THR THR B . n 
B 1 837  SER 837  835  835  SER SER B . n 
B 1 838  ALA 838  836  836  ALA ALA B . n 
B 1 839  PHE 839  837  837  PHE PHE B . n 
B 1 840  ASP 840  838  838  ASP ASP B . n 
B 1 841  SER 841  839  839  SER SER B . n 
B 1 842  ALA 842  840  840  ALA ALA B . n 
B 1 843  GLY 843  841  841  GLY GLY B . n 
B 1 844  GLN 844  842  842  GLN GLN B . n 
B 1 845  ARG 845  843  843  ARG ARG B . n 
B 1 846  CYS 846  844  844  CYS CYS B . n 
B 1 847  SER 847  845  845  SER SER B . n 
B 1 848  ALA 848  846  846  ALA ALA B . n 
B 1 849  LEU 849  847  847  LEU LEU B . n 
B 1 850  ARG 850  848  848  ARG ARG B . n 
B 1 851  VAL 851  849  849  VAL VAL B . n 
B 1 852  LEU 852  850  850  LEU LEU B . n 
B 1 853  CYS 853  851  851  CYS CYS B . n 
B 1 854  LEU 854  852  852  LEU LEU B . n 
B 1 855  GLN 855  853  853  GLN GLN B . n 
B 1 856  GLU 856  854  854  GLU GLU B . n 
B 1 857  ASP 857  855  855  ASP ASP B . n 
B 1 858  VAL 858  856  856  VAL VAL B . n 
B 1 859  ALA 859  857  857  ALA ALA B . n 
B 1 860  ASP 860  858  858  ASP ASP B . n 
B 1 861  ARG 861  859  859  ARG ARG B . n 
B 1 862  ILE 862  860  860  ILE ILE B . n 
B 1 863  LEU 863  861  861  LEU LEU B . n 
B 1 864  THR 864  862  862  THR THR B . n 
B 1 865  MET 865  863  863  MET MET B . n 
B 1 866  LEU 866  864  864  LEU LEU B . n 
B 1 867  LYS 867  865  865  LYS LYS B . n 
B 1 868  GLY 868  866  866  GLY GLY B . n 
B 1 869  ALA 869  867  867  ALA ALA B . n 
B 1 870  LEU 870  868  868  LEU LEU B . n 
B 1 871  HIS 871  869  869  HIS HIS B . n 
B 1 872  GLU 872  870  870  GLU GLU B . n 
B 1 873  LEU 873  871  871  LEU LEU B . n 
B 1 874  HIS 874  872  872  HIS HIS B . n 
B 1 875  ILE 875  873  873  ILE ILE B . n 
B 1 876  GLY 876  874  874  GLY GLY B . n 
B 1 877  ARG 877  875  875  ARG ARG B . n 
B 1 878  THR 878  876  876  THR THR B . n 
B 1 879  ASP 879  877  877  ASP ASP B . n 
B 1 880  ARG 880  878  878  ARG ARG B . n 
B 1 881  LEU 881  879  879  LEU LEU B . n 
B 1 882  SER 882  880  880  SER SER B . n 
B 1 883  VAL 883  881  881  VAL VAL B . n 
B 1 884  ASP 884  882  882  ASP ASP B . n 
B 1 885  VAL 885  883  883  VAL VAL B . n 
B 1 886  GLY 886  884  884  GLY GLY B . n 
B 1 887  PRO 887  885  885  PRO PRO B . n 
B 1 888  VAL 888  886  886  VAL VAL B . n 
B 1 889  ILE 889  887  887  ILE ILE B . n 
B 1 890  THR 890  888  888  THR THR B . n 
B 1 891  SER 891  889  889  SER SER B . n 
B 1 892  GLU 892  890  890  GLU GLU B . n 
B 1 893  ALA 893  891  891  ALA ALA B . n 
B 1 894  LYS 894  892  892  LYS LYS B . n 
B 1 895  ASP 895  893  893  ASP ASP B . n 
B 1 896  ASN 896  894  894  ASN ASN B . n 
B 1 897  ILE 897  895  895  ILE ILE B . n 
B 1 898  GLU 898  896  896  GLU GLU B . n 
B 1 899  LYS 899  897  897  LYS LYS B . n 
B 1 900  HIS 900  898  898  HIS HIS B . n 
B 1 901  ILE 901  899  899  ILE ILE B . n 
B 1 902  GLU 902  900  900  GLU GLU B . n 
B 1 903  ARG 903  901  901  ARG ARG B . n 
B 1 904  MET 904  902  902  MET MET B . n 
B 1 905  ARG 905  903  903  ARG ARG B . n 
B 1 906  GLY 906  904  904  GLY GLY B . n 
B 1 907  LEU 907  905  905  LEU LEU B . n 
B 1 908  GLY 908  906  906  GLY GLY B . n 
B 1 909  ARG 909  907  907  ARG ARG B . n 
B 1 910  LYS 910  908  908  LYS LYS B . n 
B 1 911  VAL 911  909  909  VAL VAL B . n 
B 1 912  GLU 912  910  910  GLU GLU B . n 
B 1 913  GLN 913  911  911  GLN GLN B . n 
B 1 914  ILE 914  912  912  ILE ILE B . n 
B 1 915  GLY 915  913  913  GLY GLY B . n 
B 1 916  LEU 916  914  914  LEU LEU B . n 
B 1 917  ALA 917  915  915  ALA ALA B . n 
B 1 918  SER 918  916  916  SER SER B . n 
B 1 919  GLU 919  917  917  GLU GLU B . n 
B 1 920  THR 920  918  918  THR THR B . n 
B 1 921  GLY 921  919  919  GLY GLY B . n 
B 1 922  VAL 922  920  920  VAL VAL B . n 
B 1 923  GLY 923  921  921  GLY GLY B . n 
B 1 924  THR 924  922  922  THR THR B . n 
B 1 925  PHE 925  923  923  PHE PHE B . n 
B 1 926  VAL 926  924  924  VAL VAL B . n 
B 1 927  PRO 927  925  925  PRO PRO B . n 
B 1 928  PRO 928  926  926  PRO PRO B . n 
B 1 929  THR 929  927  927  THR THR B . n 
B 1 930  ILE 930  928  928  ILE ILE B . n 
B 1 931  ILE 931  929  929  ILE ILE B . n 
B 1 932  GLU 932  930  930  GLU GLU B . n 
B 1 933  LEU 933  931  931  LEU LEU B . n 
B 1 934  GLU 934  932  932  GLU GLU B . n 
B 1 935  LYS 935  933  933  LYS LYS B . n 
B 1 936  LEU 936  934  934  LEU LEU B . n 
B 1 937  SER 937  935  935  SER SER B . n 
B 1 938  ASP 938  936  936  ASP ASP B . n 
B 1 939  LEU 939  937  937  LEU LEU B . n 
B 1 940  GLN 940  938  938  GLN GLN B . n 
B 1 941  ARG 941  939  939  ARG ARG B . n 
B 1 942  GLU 942  940  940  GLU GLU B . n 
B 1 943  VAL 943  941  941  VAL VAL B . n 
B 1 944  PHE 944  942  942  PHE PHE B . n 
B 1 945  GLY 945  943  943  GLY GLY B . n 
B 1 946  PRO 946  944  944  PRO PRO B . n 
B 1 947  VAL 947  945  945  VAL VAL B . n 
B 1 948  LEU 948  946  946  LEU LEU B . n 
B 1 949  HIS 949  947  947  HIS HIS B . n 
B 1 950  VAL 950  948  948  VAL VAL B . n 
B 1 951  ILE 951  949  949  ILE ILE B . n 
B 1 952  ARG 952  950  950  ARG ARG B . n 
B 1 953  TYR 953  951  951  TYR TYR B . n 
B 1 954  ARG 954  952  952  ARG ARG B . n 
B 1 955  ARG 955  953  953  ARG ARG B . n 
B 1 956  ASP 956  954  954  ASP ASP B . n 
B 1 957  ASP 957  955  955  ASP ASP B . n 
B 1 958  LEU 958  956  956  LEU LEU B . n 
B 1 959  ASP 959  957  957  ASP ASP B . n 
B 1 960  ARG 960  958  958  ARG ARG B . n 
B 1 961  LEU 961  959  959  LEU LEU B . n 
B 1 962  VAL 962  960  960  VAL VAL B . n 
B 1 963  ASP 963  961  961  ASP ASP B . n 
B 1 964  ASP 964  962  962  ASP ASP B . n 
B 1 965  VAL 965  963  963  VAL VAL B . n 
B 1 966  ASN 966  964  964  ASN ASN B . n 
B 1 967  ALA 967  965  965  ALA ALA B . n 
B 1 968  THR 968  966  966  THR THR B . n 
B 1 969  GLY 969  967  967  GLY GLY B . n 
B 1 970  TYR 970  968  968  TYR TYR B . n 
B 1 971  GLY 971  969  969  GLY GLY B . n 
B 1 972  LEU 972  970  970  LEU LEU B . n 
B 1 973  THR 973  971  971  THR THR B . n 
B 1 974  PHE 974  972  972  PHE PHE B . n 
B 1 975  GLY 975  973  973  GLY GLY B . n 
B 1 976  LEU 976  974  974  LEU LEU B . n 
B 1 977  HIS 977  975  975  HIS HIS B . n 
B 1 978  THR 978  976  976  THR THR B . n 
B 1 979  ARG 979  977  977  ARG ARG B . n 
B 1 980  LEU 980  978  978  LEU LEU B . n 
B 1 981  ASP 981  979  979  ASP ASP B . n 
B 1 982  GLU 982  980  980  GLU GLU B . n 
B 1 983  THR 983  981  981  THR THR B . n 
B 1 984  ILE 984  982  982  ILE ILE B . n 
B 1 985  ALA 985  983  983  ALA ALA B . n 
B 1 986  HIS 986  984  984  HIS HIS B . n 
B 1 987  VAL 987  985  985  VAL VAL B . n 
B 1 988  THR 988  986  986  THR THR B . n 
B 1 989  SER 989  987  987  SER SER B . n 
B 1 990  ARG 990  988  988  ARG ARG B . n 
B 1 991  ILE 991  989  989  ILE ILE B . n 
B 1 992  LYS 992  990  990  LYS LYS B . n 
B 1 993  ALA 993  991  991  ALA ALA B . n 
B 1 994  GLY 994  992  992  GLY GLY B . n 
B 1 995  ASN 995  993  993  ASN ASN B . n 
B 1 996  LEU 996  994  994  LEU LEU B . n 
B 1 997  TYR 997  995  995  TYR TYR B . n 
B 1 998  ILE 998  996  996  ILE ILE B . n 
B 1 999  ASN 999  997  997  ASN ASN B . n 
B 1 1000 ARG 1000 998  998  ARG ARG B . n 
B 1 1001 ASN 1001 999  999  ASN ASN B . n 
B 1 1002 ILE 1002 1000 1000 ILE ILE B . n 
B 1 1003 ILE 1003 1001 1001 ILE ILE B . n 
B 1 1004 GLY 1004 1002 1002 GLY GLY B . n 
B 1 1005 ALA 1005 1003 1003 ALA ALA B . n 
B 1 1006 VAL 1006 1004 1004 VAL VAL B . n 
B 1 1007 VAL 1007 1005 1005 VAL VAL B . n 
B 1 1008 GLY 1008 1006 1006 GLY GLY B . n 
B 1 1009 VAL 1009 1007 1007 VAL VAL B . n 
B 1 1010 GLN 1010 1008 1008 GLN GLN B . n 
B 1 1011 PRO 1011 1009 1009 PRO PRO B . n 
B 1 1012 PHE 1012 1010 1010 PHE PHE B . n 
B 1 1013 GLY 1013 1011 1011 GLY GLY B . n 
B 1 1014 GLY 1014 1012 1012 GLY GLY B . n 
B 1 1015 ARG 1015 1013 1013 ARG ARG B . n 
B 1 1016 GLY 1016 1014 1014 GLY GLY B . n 
B 1 1017 LEU 1017 1015 1015 LEU LEU B . n 
B 1 1018 SER 1018 1016 1016 SER SER B . n 
B 1 1019 GLY 1019 1017 1017 GLY GLY B . n 
B 1 1020 THR 1020 1018 1018 THR THR B . n 
B 1 1021 GLY 1021 1019 1019 GLY GLY B . n 
B 1 1022 PRO 1022 1020 1020 PRO PRO B . n 
B 1 1023 LYS 1023 1021 1021 LYS LYS B . n 
B 1 1024 ALA 1024 1022 1022 ALA ALA B . n 
B 1 1025 GLY 1025 1023 1023 GLY GLY B . n 
B 1 1026 GLY 1026 1024 1024 GLY GLY B . n 
B 1 1027 PRO 1027 1025 1025 PRO PRO B . n 
B 1 1028 LEU 1028 1026 1026 LEU LEU B . n 
B 1 1029 TYR 1029 1027 1027 TYR TYR B . n 
B 1 1030 LEU 1030 1028 1028 LEU LEU B . n 
B 1 1031 GLY 1031 1029 1029 GLY GLY B . n 
B 1 1032 ARG 1032 1030 1030 ARG ARG B . n 
B 1 1033 LEU 1033 1031 1031 LEU LEU B . n 
B 1 1034 VAL 1034 1032 1032 VAL VAL B . n 
B 1 1035 THR 1035 1033 1033 THR THR B . n 
B 1 1036 THR 1036 1034 1034 THR THR B . n 
B 1 1037 ALA 1037 1035 1035 ALA ALA B . n 
B 1 1038 PRO 1038 1036 1036 PRO PRO B . n 
B 1 1039 VAL 1039 1037 1037 VAL VAL B . n 
B 1 1040 PRO 1040 1038 1038 PRO PRO B . n 
B 1 1041 PRO 1041 1039 1039 PRO PRO B . n 
B 1 1042 GLN 1042 1040 1040 GLN GLN B . n 
B 1 1043 HIS 1043 1041 1041 HIS HIS B . n 
B 1 1044 SER 1044 1042 1042 SER SER B . n 
B 1 1045 SER 1045 1043 1043 SER SER B . n 
B 1 1046 VAL 1046 1044 1044 VAL VAL B . n 
B 1 1047 HIS 1047 1045 1045 HIS HIS B . n 
B 1 1048 THR 1048 1046 1046 THR THR B . n 
B 1 1049 ASP 1049 1047 1047 ASP ASP B . n 
B 1 1050 PRO 1050 1048 1048 PRO PRO B . n 
B 1 1051 VAL 1051 1049 1049 VAL VAL B . n 
B 1 1052 LEU 1052 1050 1050 LEU LEU B . n 
B 1 1053 LEU 1053 1051 1051 LEU LEU B . n 
B 1 1054 ASP 1054 1052 1052 ASP ASP B . n 
B 1 1055 PHE 1055 1053 1053 PHE PHE B . n 
B 1 1056 ALA 1056 1054 1054 ALA ALA B . n 
B 1 1057 LYS 1057 1055 1055 LYS LYS B . n 
B 1 1058 TRP 1058 1056 1056 TRP TRP B . n 
B 1 1059 LEU 1059 1057 1057 LEU LEU B . n 
B 1 1060 ASP 1060 1058 1058 ASP ASP B . n 
B 1 1061 GLY 1061 1059 1059 GLY GLY B . n 
B 1 1062 LYS 1062 1060 1060 LYS LYS B . n 
B 1 1063 GLY 1063 1061 1061 GLY GLY B . n 
B 1 1064 ALA 1064 1062 1062 ALA ALA B . n 
B 1 1065 ARG 1065 1063 1063 ARG ARG B . n 
B 1 1066 ALA 1066 1064 1064 ALA ALA B . n 
B 1 1067 GLU 1067 1065 1065 GLU GLU B . n 
B 1 1068 ALA 1068 1066 1066 ALA ALA B . n 
B 1 1069 GLU 1069 1067 1067 GLU GLU B . n 
B 1 1070 ALA 1070 1068 1068 ALA ALA B . n 
B 1 1071 ALA 1071 1069 1069 ALA ALA B . n 
B 1 1072 ARG 1072 1070 1070 ARG ARG B . n 
B 1 1073 ASN 1073 1071 1071 ASN ASN B . n 
B 1 1074 ALA 1074 1072 1072 ALA ALA B . n 
B 1 1075 GLY 1075 1073 1073 GLY GLY B . n 
B 1 1076 SER 1076 1074 1074 SER SER B . n 
B 1 1077 SER 1077 1075 1075 SER SER B . n 
B 1 1078 SER 1078 1076 1076 SER SER B . n 
B 1 1079 ALA 1079 1077 1077 ALA ALA B . n 
B 1 1080 LEU 1080 1078 1078 LEU LEU B . n 
B 1 1081 GLY 1081 1079 1079 GLY GLY B . n 
B 1 1082 LEU 1082 1080 1080 LEU LEU B . n 
B 1 1083 ASP 1083 1081 1081 ASP ASP B . n 
B 1 1084 LEU 1084 1082 1082 LEU LEU B . n 
B 1 1085 GLU 1085 1083 1083 GLU GLU B . n 
B 1 1086 LEU 1086 1084 1084 LEU LEU B . n 
B 1 1087 PRO 1087 1085 1085 PRO PRO B . n 
B 1 1088 GLY 1088 1086 1086 GLY GLY B . n 
B 1 1089 PRO 1089 1087 1087 PRO PRO B . n 
B 1 1090 VAL 1090 1088 1088 VAL VAL B . n 
B 1 1091 GLY 1091 1089 1089 GLY GLY B . n 
B 1 1092 GLU 1092 1090 1090 GLU GLU B . n 
B 1 1093 ARG 1093 1091 1091 ARG ARG B . n 
B 1 1094 ASN 1094 1092 1092 ASN ASN B . n 
B 1 1095 LEU 1095 1093 1093 LEU LEU B . n 
B 1 1096 TYR 1096 1094 1094 TYR TYR B . n 
B 1 1097 THR 1097 1095 1095 THR THR B . n 
B 1 1098 LEU 1098 1096 1096 LEU LEU B . n 
B 1 1099 HIS 1099 1097 1097 HIS HIS B . n 
B 1 1100 ALA 1100 1098 1098 ALA ALA B . n 
B 1 1101 ARG 1101 1099 1099 ARG ARG B . n 
B 1 1102 GLY 1102 1100 1100 GLY GLY B . n 
B 1 1103 ARG 1103 1101 1101 ARG ARG B . n 
B 1 1104 ILE 1104 1102 1102 ILE ILE B . n 
B 1 1105 LEU 1105 1103 1103 LEU LEU B . n 
B 1 1106 LEU 1106 1104 1104 LEU LEU B . n 
B 1 1107 VAL 1107 1105 1105 VAL VAL B . n 
B 1 1108 PRO 1108 1106 1106 PRO PRO B . n 
B 1 1109 ALA 1109 1107 1107 ALA ALA B . n 
B 1 1110 THR 1110 1108 1108 THR THR B . n 
B 1 1111 GLU 1111 1109 1109 GLU GLU B . n 
B 1 1112 SER 1112 1110 1110 SER SER B . n 
B 1 1113 GLY 1113 1111 1111 GLY GLY B . n 
B 1 1114 LEU 1114 1112 1112 LEU LEU B . n 
B 1 1115 TYR 1115 1113 1113 TYR TYR B . n 
B 1 1116 HIS 1116 1114 1114 HIS HIS B . n 
B 1 1117 GLN 1117 1115 1115 GLN GLN B . n 
B 1 1118 LEU 1118 1116 1116 LEU LEU B . n 
B 1 1119 ALA 1119 1117 1117 ALA ALA B . n 
B 1 1120 ALA 1120 1118 1118 ALA ALA B . n 
B 1 1121 ALA 1121 1119 1119 ALA ALA B . n 
B 1 1122 LEU 1122 1120 1120 LEU LEU B . n 
B 1 1123 ALA 1123 1121 1121 ALA ALA B . n 
B 1 1124 THR 1124 1122 1122 THR THR B . n 
B 1 1125 GLY 1125 1123 1123 GLY GLY B . n 
B 1 1126 ASN 1126 1124 1124 ASN ASN B . n 
B 1 1127 SER 1127 1125 1125 SER SER B . n 
B 1 1128 VAL 1128 1126 1126 VAL VAL B . n 
B 1 1129 ALA 1129 1127 1127 ALA ALA B . n 
B 1 1130 ILE 1130 1128 1128 ILE ILE B . n 
B 1 1131 ASP 1131 1129 1129 ASP ASP B . n 
B 1 1132 ALA 1132 1130 1130 ALA ALA B . n 
B 1 1133 ALA 1133 1131 1131 ALA ALA B . n 
B 1 1134 SER 1134 1132 1132 SER SER B . n 
B 1 1135 GLY 1135 1133 1133 GLY GLY B . n 
B 1 1136 LEU 1136 1134 1134 LEU LEU B . n 
B 1 1137 GLN 1137 1135 1135 GLN GLN B . n 
B 1 1138 ALA 1138 1136 1136 ALA ALA B . n 
B 1 1139 SER 1139 1137 1137 SER SER B . n 
B 1 1140 LEU 1140 1138 1138 LEU LEU B . n 
B 1 1141 LYS 1141 1139 1139 LYS LYS B . n 
B 1 1142 ASN 1142 1140 1140 ASN ASN B . n 
B 1 1143 LEU 1143 1141 1141 LEU LEU B . n 
B 1 1144 PRO 1144 1142 1142 PRO PRO B . n 
B 1 1145 GLN 1145 1143 1143 GLN GLN B . n 
B 1 1146 THR 1146 1144 1144 THR THR B . n 
B 1 1147 VAL 1147 1145 1145 VAL VAL B . n 
B 1 1148 GLY 1148 1146 1146 GLY GLY B . n 
B 1 1149 LEU 1149 1147 1147 LEU LEU B . n 
B 1 1150 ARG 1150 1148 1148 ARG ARG B . n 
B 1 1151 VAL 1151 1149 1149 VAL VAL B . n 
B 1 1152 SER 1152 1150 1150 SER SER B . n 
B 1 1153 TRP 1153 1151 1151 TRP TRP B . n 
B 1 1154 SER 1154 1152 1152 SER SER B . n 
B 1 1155 LYS 1155 1153 1153 LYS LYS B . n 
B 1 1156 ASP 1156 1154 1154 ASP ASP B . n 
B 1 1157 TRP 1157 1155 1155 TRP TRP B . n 
B 1 1158 ALA 1158 1156 1156 ALA ALA B . n 
B 1 1159 ALA 1159 1157 1157 ALA ALA B . n 
B 1 1160 ASP 1160 1158 1158 ASP ASP B . n 
B 1 1161 GLY 1161 1159 1159 GLY GLY B . n 
B 1 1162 PRO 1162 1160 1160 PRO PRO B . n 
B 1 1163 PHE 1163 1161 1161 PHE PHE B . n 
B 1 1164 ALA 1164 1162 1162 ALA ALA B . n 
B 1 1165 GLY 1165 1163 1163 GLY GLY B . n 
B 1 1166 ALA 1166 1164 1164 ALA ALA B . n 
B 1 1167 LEU 1167 1165 1165 LEU LEU B . n 
B 1 1168 VAL 1168 1166 1166 VAL VAL B . n 
B 1 1169 GLU 1169 1167 1167 GLU GLU B . n 
B 1 1170 GLY 1170 1168 1168 GLY GLY B . n 
B 1 1171 ASP 1171 1169 1169 ASP ASP B . n 
B 1 1172 ALA 1172 1170 1170 ALA ALA B . n 
B 1 1173 GLU 1173 1171 1171 GLU GLU B . n 
B 1 1174 ARG 1174 1172 1172 ARG ARG B . n 
B 1 1175 ILE 1175 1173 1173 ILE ILE B . n 
B 1 1176 ARG 1176 1174 1174 ARG ARG B . n 
B 1 1177 ALA 1177 1175 1175 ALA ALA B . n 
B 1 1178 VAL 1178 1176 1176 VAL VAL B . n 
B 1 1179 ASN 1179 1177 1177 ASN ASN B . n 
B 1 1180 LYS 1180 1178 1178 LYS LYS B . n 
B 1 1181 ALA 1181 1179 1179 ALA ALA B . n 
B 1 1182 ILE 1182 1180 1180 ILE ILE B . n 
B 1 1183 ALA 1183 1181 1181 ALA ALA B . n 
B 1 1184 ALA 1184 1182 1182 ALA ALA B . n 
B 1 1185 LEU 1185 1183 1183 LEU LEU B . n 
B 1 1186 PRO 1186 1184 1184 PRO PRO B . n 
B 1 1187 GLY 1187 1185 1185 GLY GLY B . n 
B 1 1188 PRO 1188 1186 1186 PRO PRO B . n 
B 1 1189 LEU 1189 1187 1187 LEU LEU B . n 
B 1 1190 LEU 1190 1188 1188 LEU LEU B . n 
B 1 1191 LEU 1191 1189 1189 LEU LEU B . n 
B 1 1192 VAL 1192 1190 1190 VAL VAL B . n 
B 1 1193 GLN 1193 1191 1191 GLN GLN B . n 
B 1 1194 ALA 1194 1192 1192 ALA ALA B . n 
B 1 1195 ALA 1195 1193 1193 ALA ALA B . n 
B 1 1196 SER 1196 1194 1194 SER SER B . n 
B 1 1197 SER 1197 1195 1195 SER SER B . n 
B 1 1198 GLY 1198 1196 1196 GLY GLY B . n 
B 1 1199 GLU 1199 1197 1197 GLU GLU B . n 
B 1 1200 ILE 1200 1198 1198 ILE ILE B . n 
B 1 1201 ALA 1201 1199 1199 ALA ALA B . n 
B 1 1202 ARG 1202 1200 1200 ARG ARG B . n 
B 1 1203 ASN 1203 1201 1201 ASN ASN B . n 
B 1 1204 PRO 1204 1202 1202 PRO PRO B . n 
B 1 1205 ASP 1205 1203 1203 ASP ASP B . n 
B 1 1206 ALA 1206 1204 1204 ALA ALA B . n 
B 1 1207 TYR 1207 1205 1205 TYR TYR B . n 
B 1 1208 CYS 1208 1206 1206 CYS CYS B . n 
B 1 1209 LEU 1209 1207 1207 LEU LEU B . n 
B 1 1210 ASN 1210 1208 1208 ASN ASN B . n 
B 1 1211 TRP 1211 1209 1209 TRP TRP B . n 
B 1 1212 LEU 1212 1210 1210 LEU LEU B . n 
B 1 1213 VAL 1213 1211 1211 VAL VAL B . n 
B 1 1214 GLU 1214 1212 1212 GLU GLU B . n 
B 1 1215 GLU 1215 1213 1213 GLU GLU B . n 
B 1 1216 VAL 1216 1214 1214 VAL VAL B . n 
B 1 1217 SER 1217 1215 1215 SER SER B . n 
B 1 1218 ALA 1218 1216 1216 ALA ALA B . n 
B 1 1219 SER 1219 1217 1217 SER SER B . n 
B 1 1220 ILE 1220 1218 1218 ILE ILE B . n 
B 1 1221 ASN 1221 1219 1219 ASN ASN B . n 
B 1 1222 THR 1222 1220 1220 THR THR B . n 
B 1 1223 ALA 1223 1221 1221 ALA ALA B . n 
B 1 1224 ALA 1224 1222 1222 ALA ALA B . n 
B 1 1225 ALA 1225 1223 1223 ALA ALA B . n 
B 1 1226 GLY 1226 1224 1224 GLY GLY B . n 
B 1 1227 GLY 1227 1225 1225 GLY GLY B . n 
B 1 1228 ASN 1228 1226 1226 ASN ASN B . n 
B 1 1229 ALA 1229 1227 1227 ALA ALA B . n 
B 1 1230 SER 1230 1228 1228 SER SER B . n 
B 1 1231 LEU 1231 1229 1229 LEU LEU B . n 
B 1 1232 MET 1232 1230 1230 MET MET B . n 
B 1 1233 ALA 1233 1231 1231 ALA ALA B . n 
B 1 1234 ILE 1234 1232 1232 ILE ILE B . n 
B 1 1235 GLY 1235 1233 1233 GLY GLY B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1BDW ? ? A1BDW ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FAD   ? ? FAD   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NAD   ? ? NAD   ? ? '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    1301 1301 FAD   FAD A . 
D 3  FMT   1    1302 1302 FMT   FMT A . 
E 4  PEG   1    1303 1303 PEG   PEG A . 
F 4  PEG   1    1304 1304 PEG   PEG A . 
G 5  NAD   1    1305 2002 NAD   NAD A . 
H 6  SO4   1    1306 1    SO4   SO4 A . 
I 6  SO4   1    1307 3    SO4   SO4 A . 
J 6  SO4   1    1308 4    SO4   SO4 A . 
K 6  SO4   1    1309 5    SO4   SO4 A . 
L 6  SO4   1    1310 6    SO4   SO4 A . 
M 7  MG    1    1311 1    MG    MG  A . 
N 2  FAD   1    1301 1301 FAD   FAD B . 
O 8  PGE   1    1302 1302 PGE   PGE B . 
P 3  FMT   1    1303 1303 FMT   FMT B . 
Q 9  A1BDW 1    1304 1307 A1BDW 224 B . 
R 4  PEG   1    1305 1308 PEG   PEG B . 
S 5  NAD   1    1306 2002 NAD   NAD B . 
T 6  SO4   1    1307 2    SO4   SO4 B . 
U 7  MG    1    1308 2    MG    MG  B . 
V 10 HOH   1    1401 2158 HOH   HOH A . 
V 10 HOH   2    1402 68   HOH   HOH A . 
V 10 HOH   3    1403 885  HOH   HOH A . 
V 10 HOH   4    1404 2140 HOH   HOH A . 
V 10 HOH   5    1405 693  HOH   HOH A . 
V 10 HOH   6    1406 246  HOH   HOH A . 
V 10 HOH   7    1407 2511 HOH   HOH A . 
V 10 HOH   8    1408 1022 HOH   HOH A . 
V 10 HOH   9    1409 1932 HOH   HOH A . 
V 10 HOH   10   1410 1285 HOH   HOH A . 
V 10 HOH   11   1411 2466 HOH   HOH A . 
V 10 HOH   12   1412 2567 HOH   HOH A . 
V 10 HOH   13   1413 1142 HOH   HOH A . 
V 10 HOH   14   1414 1368 HOH   HOH A . 
V 10 HOH   15   1415 1721 HOH   HOH A . 
V 10 HOH   16   1416 1562 HOH   HOH A . 
V 10 HOH   17   1417 1992 HOH   HOH A . 
V 10 HOH   18   1418 1644 HOH   HOH A . 
V 10 HOH   19   1419 1461 HOH   HOH A . 
V 10 HOH   20   1420 853  HOH   HOH A . 
V 10 HOH   21   1421 982  HOH   HOH A . 
V 10 HOH   22   1422 2459 HOH   HOH A . 
V 10 HOH   23   1423 532  HOH   HOH A . 
V 10 HOH   24   1424 1020 HOH   HOH A . 
V 10 HOH   25   1425 657  HOH   HOH A . 
V 10 HOH   26   1426 2172 HOH   HOH A . 
V 10 HOH   27   1427 2017 HOH   HOH A . 
V 10 HOH   28   1428 1710 HOH   HOH A . 
V 10 HOH   29   1429 1572 HOH   HOH A . 
V 10 HOH   30   1430 1549 HOH   HOH A . 
V 10 HOH   31   1431 2003 HOH   HOH A . 
V 10 HOH   32   1432 949  HOH   HOH A . 
V 10 HOH   33   1433 1460 HOH   HOH A . 
V 10 HOH   34   1434 1678 HOH   HOH A . 
V 10 HOH   35   1435 2149 HOH   HOH A . 
V 10 HOH   36   1436 1883 HOH   HOH A . 
V 10 HOH   37   1437 1978 HOH   HOH A . 
V 10 HOH   38   1438 1083 HOH   HOH A . 
V 10 HOH   39   1439 1594 HOH   HOH A . 
V 10 HOH   40   1440 914  HOH   HOH A . 
V 10 HOH   41   1441 2256 HOH   HOH A . 
V 10 HOH   42   1442 1715 HOH   HOH A . 
V 10 HOH   43   1443 611  HOH   HOH A . 
V 10 HOH   44   1444 2405 HOH   HOH A . 
V 10 HOH   45   1445 1283 HOH   HOH A . 
V 10 HOH   46   1446 2062 HOH   HOH A . 
V 10 HOH   47   1447 239  HOH   HOH A . 
V 10 HOH   48   1448 1091 HOH   HOH A . 
V 10 HOH   49   1449 1447 HOH   HOH A . 
V 10 HOH   50   1450 1441 HOH   HOH A . 
V 10 HOH   51   1451 662  HOH   HOH A . 
V 10 HOH   52   1452 1532 HOH   HOH A . 
V 10 HOH   53   1453 1486 HOH   HOH A . 
V 10 HOH   54   1454 1595 HOH   HOH A . 
V 10 HOH   55   1455 2362 HOH   HOH A . 
V 10 HOH   56   1456 2227 HOH   HOH A . 
V 10 HOH   57   1457 2328 HOH   HOH A . 
V 10 HOH   58   1458 1657 HOH   HOH A . 
V 10 HOH   59   1459 1475 HOH   HOH A . 
V 10 HOH   60   1460 189  HOH   HOH A . 
V 10 HOH   61   1461 2133 HOH   HOH A . 
V 10 HOH   62   1462 442  HOH   HOH A . 
V 10 HOH   63   1463 879  HOH   HOH A . 
V 10 HOH   64   1464 237  HOH   HOH A . 
V 10 HOH   65   1465 755  HOH   HOH A . 
V 10 HOH   66   1466 797  HOH   HOH A . 
V 10 HOH   67   1467 1761 HOH   HOH A . 
V 10 HOH   68   1468 2088 HOH   HOH A . 
V 10 HOH   69   1469 1766 HOH   HOH A . 
V 10 HOH   70   1470 1125 HOH   HOH A . 
V 10 HOH   71   1471 1605 HOH   HOH A . 
V 10 HOH   72   1472 2319 HOH   HOH A . 
V 10 HOH   73   1473 2219 HOH   HOH A . 
V 10 HOH   74   1474 719  HOH   HOH A . 
V 10 HOH   75   1475 1589 HOH   HOH A . 
V 10 HOH   76   1476 153  HOH   HOH A . 
V 10 HOH   77   1477 1559 HOH   HOH A . 
V 10 HOH   78   1478 265  HOH   HOH A . 
V 10 HOH   79   1479 1674 HOH   HOH A . 
V 10 HOH   80   1480 704  HOH   HOH A . 
V 10 HOH   81   1481 261  HOH   HOH A . 
V 10 HOH   82   1482 618  HOH   HOH A . 
V 10 HOH   83   1483 1286 HOH   HOH A . 
V 10 HOH   84   1484 2262 HOH   HOH A . 
V 10 HOH   85   1485 956  HOH   HOH A . 
V 10 HOH   86   1486 1139 HOH   HOH A . 
V 10 HOH   87   1487 2155 HOH   HOH A . 
V 10 HOH   88   1488 2252 HOH   HOH A . 
V 10 HOH   89   1489 1120 HOH   HOH A . 
V 10 HOH   90   1490 1110 HOH   HOH A . 
V 10 HOH   91   1491 613  HOH   HOH A . 
V 10 HOH   92   1492 224  HOH   HOH A . 
V 10 HOH   93   1493 866  HOH   HOH A . 
V 10 HOH   94   1494 1416 HOH   HOH A . 
V 10 HOH   95   1495 1959 HOH   HOH A . 
V 10 HOH   96   1496 314  HOH   HOH A . 
V 10 HOH   97   1497 2153 HOH   HOH A . 
V 10 HOH   98   1498 561  HOH   HOH A . 
V 10 HOH   99   1499 750  HOH   HOH A . 
V 10 HOH   100  1500 1493 HOH   HOH A . 
V 10 HOH   101  1501 48   HOH   HOH A . 
V 10 HOH   102  1502 2025 HOH   HOH A . 
V 10 HOH   103  1503 2087 HOH   HOH A . 
V 10 HOH   104  1504 1018 HOH   HOH A . 
V 10 HOH   105  1505 1427 HOH   HOH A . 
V 10 HOH   106  1506 554  HOH   HOH A . 
V 10 HOH   107  1507 1704 HOH   HOH A . 
V 10 HOH   108  1508 1145 HOH   HOH A . 
V 10 HOH   109  1509 426  HOH   HOH A . 
V 10 HOH   110  1510 459  HOH   HOH A . 
V 10 HOH   111  1511 131  HOH   HOH A . 
V 10 HOH   112  1512 101  HOH   HOH A . 
V 10 HOH   113  1513 718  HOH   HOH A . 
V 10 HOH   114  1514 760  HOH   HOH A . 
V 10 HOH   115  1515 1541 HOH   HOH A . 
V 10 HOH   116  1516 1072 HOH   HOH A . 
V 10 HOH   117  1517 444  HOH   HOH A . 
V 10 HOH   118  1518 575  HOH   HOH A . 
V 10 HOH   119  1519 2351 HOH   HOH A . 
V 10 HOH   120  1520 466  HOH   HOH A . 
V 10 HOH   121  1521 32   HOH   HOH A . 
V 10 HOH   122  1522 827  HOH   HOH A . 
V 10 HOH   123  1523 87   HOH   HOH A . 
V 10 HOH   124  1524 909  HOH   HOH A . 
V 10 HOH   125  1525 1821 HOH   HOH A . 
V 10 HOH   126  1526 1616 HOH   HOH A . 
V 10 HOH   127  1527 2247 HOH   HOH A . 
V 10 HOH   128  1528 1563 HOH   HOH A . 
V 10 HOH   129  1529 754  HOH   HOH A . 
V 10 HOH   130  1530 2089 HOH   HOH A . 
V 10 HOH   131  1531 2350 HOH   HOH A . 
V 10 HOH   132  1532 2526 HOH   HOH A . 
V 10 HOH   133  1533 2150 HOH   HOH A . 
V 10 HOH   134  1534 1360 HOH   HOH A . 
V 10 HOH   135  1535 1196 HOH   HOH A . 
V 10 HOH   136  1536 1256 HOH   HOH A . 
V 10 HOH   137  1537 1085 HOH   HOH A . 
V 10 HOH   138  1538 2357 HOH   HOH A . 
V 10 HOH   139  1539 1909 HOH   HOH A . 
V 10 HOH   140  1540 1000 HOH   HOH A . 
V 10 HOH   141  1541 1624 HOH   HOH A . 
V 10 HOH   142  1542 2156 HOH   HOH A . 
V 10 HOH   143  1543 1274 HOH   HOH A . 
V 10 HOH   144  1544 972  HOH   HOH A . 
V 10 HOH   145  1545 2321 HOH   HOH A . 
V 10 HOH   146  1546 1760 HOH   HOH A . 
V 10 HOH   147  1547 829  HOH   HOH A . 
V 10 HOH   148  1548 384  HOH   HOH A . 
V 10 HOH   149  1549 1440 HOH   HOH A . 
V 10 HOH   150  1550 437  HOH   HOH A . 
V 10 HOH   151  1551 1228 HOH   HOH A . 
V 10 HOH   152  1552 1711 HOH   HOH A . 
V 10 HOH   153  1553 985  HOH   HOH A . 
V 10 HOH   154  1554 628  HOH   HOH A . 
V 10 HOH   155  1555 723  HOH   HOH A . 
V 10 HOH   156  1556 1134 HOH   HOH A . 
V 10 HOH   157  1557 316  HOH   HOH A . 
V 10 HOH   158  1558 499  HOH   HOH A . 
V 10 HOH   159  1559 323  HOH   HOH A . 
V 10 HOH   160  1560 1387 HOH   HOH A . 
V 10 HOH   161  1561 1369 HOH   HOH A . 
V 10 HOH   162  1562 451  HOH   HOH A . 
V 10 HOH   163  1563 713  HOH   HOH A . 
V 10 HOH   164  1564 1517 HOH   HOH A . 
V 10 HOH   165  1565 1307 HOH   HOH A . 
V 10 HOH   166  1566 345  HOH   HOH A . 
V 10 HOH   167  1567 1870 HOH   HOH A . 
V 10 HOH   168  1568 2482 HOH   HOH A . 
V 10 HOH   169  1569 219  HOH   HOH A . 
V 10 HOH   170  1570 1610 HOH   HOH A . 
V 10 HOH   171  1571 1284 HOH   HOH A . 
V 10 HOH   172  1572 600  HOH   HOH A . 
V 10 HOH   173  1573 1389 HOH   HOH A . 
V 10 HOH   174  1574 114  HOH   HOH A . 
V 10 HOH   175  1575 1749 HOH   HOH A . 
V 10 HOH   176  1576 172  HOH   HOH A . 
V 10 HOH   177  1577 312  HOH   HOH A . 
V 10 HOH   178  1578 1787 HOH   HOH A . 
V 10 HOH   179  1579 344  HOH   HOH A . 
V 10 HOH   180  1580 1314 HOH   HOH A . 
V 10 HOH   181  1581 2002 HOH   HOH A . 
V 10 HOH   182  1582 1015 HOH   HOH A . 
V 10 HOH   183  1583 1675 HOH   HOH A . 
V 10 HOH   184  1584 527  HOH   HOH A . 
V 10 HOH   185  1585 83   HOH   HOH A . 
V 10 HOH   186  1586 785  HOH   HOH A . 
V 10 HOH   187  1587 440  HOH   HOH A . 
V 10 HOH   188  1588 1403 HOH   HOH A . 
V 10 HOH   189  1589 1526 HOH   HOH A . 
V 10 HOH   190  1590 2186 HOH   HOH A . 
V 10 HOH   191  1591 67   HOH   HOH A . 
V 10 HOH   192  1592 918  HOH   HOH A . 
V 10 HOH   193  1593 52   HOH   HOH A . 
V 10 HOH   194  1594 580  HOH   HOH A . 
V 10 HOH   195  1595 113  HOH   HOH A . 
V 10 HOH   196  1596 1312 HOH   HOH A . 
V 10 HOH   197  1597 652  HOH   HOH A . 
V 10 HOH   198  1598 232  HOH   HOH A . 
V 10 HOH   199  1599 2584 HOH   HOH A . 
V 10 HOH   200  1600 1803 HOH   HOH A . 
V 10 HOH   201  1601 1062 HOH   HOH A . 
V 10 HOH   202  1602 525  HOH   HOH A . 
V 10 HOH   203  1603 1621 HOH   HOH A . 
V 10 HOH   204  1604 1732 HOH   HOH A . 
V 10 HOH   205  1605 432  HOH   HOH A . 
V 10 HOH   206  1606 227  HOH   HOH A . 
V 10 HOH   207  1607 722  HOH   HOH A . 
V 10 HOH   208  1608 123  HOH   HOH A . 
V 10 HOH   209  1609 320  HOH   HOH A . 
V 10 HOH   210  1610 551  HOH   HOH A . 
V 10 HOH   211  1611 4    HOH   HOH A . 
V 10 HOH   212  1612 773  HOH   HOH A . 
V 10 HOH   213  1613 637  HOH   HOH A . 
V 10 HOH   214  1614 1509 HOH   HOH A . 
V 10 HOH   215  1615 649  HOH   HOH A . 
V 10 HOH   216  1616 145  HOH   HOH A . 
V 10 HOH   217  1617 974  HOH   HOH A . 
V 10 HOH   218  1618 2314 HOH   HOH A . 
V 10 HOH   219  1619 162  HOH   HOH A . 
V 10 HOH   220  1620 1901 HOH   HOH A . 
V 10 HOH   221  1621 488  HOH   HOH A . 
V 10 HOH   222  1622 282  HOH   HOH A . 
V 10 HOH   223  1623 469  HOH   HOH A . 
V 10 HOH   224  1624 2028 HOH   HOH A . 
V 10 HOH   225  1625 1317 HOH   HOH A . 
V 10 HOH   226  1626 2122 HOH   HOH A . 
V 10 HOH   227  1627 1556 HOH   HOH A . 
V 10 HOH   228  1628 490  HOH   HOH A . 
V 10 HOH   229  1629 29   HOH   HOH A . 
V 10 HOH   230  1630 1053 HOH   HOH A . 
V 10 HOH   231  1631 456  HOH   HOH A . 
V 10 HOH   232  1632 2199 HOH   HOH A . 
V 10 HOH   233  1633 1264 HOH   HOH A . 
V 10 HOH   234  1634 522  HOH   HOH A . 
V 10 HOH   235  1635 1842 HOH   HOH A . 
V 10 HOH   236  1636 35   HOH   HOH A . 
V 10 HOH   237  1637 1496 HOH   HOH A . 
V 10 HOH   238  1638 308  HOH   HOH A . 
V 10 HOH   239  1639 173  HOH   HOH A . 
V 10 HOH   240  1640 2189 HOH   HOH A . 
V 10 HOH   241  1641 2135 HOH   HOH A . 
V 10 HOH   242  1642 306  HOH   HOH A . 
V 10 HOH   243  1643 1459 HOH   HOH A . 
V 10 HOH   244  1644 1337 HOH   HOH A . 
V 10 HOH   245  1645 1438 HOH   HOH A . 
V 10 HOH   246  1646 1590 HOH   HOH A . 
V 10 HOH   247  1647 1755 HOH   HOH A . 
V 10 HOH   248  1648 542  HOH   HOH A . 
V 10 HOH   249  1649 1063 HOH   HOH A . 
V 10 HOH   250  1650 226  HOH   HOH A . 
V 10 HOH   251  1651 1240 HOH   HOH A . 
V 10 HOH   252  1652 2479 HOH   HOH A . 
V 10 HOH   253  1653 1828 HOH   HOH A . 
V 10 HOH   254  1654 140  HOH   HOH A . 
V 10 HOH   255  1655 2151 HOH   HOH A . 
V 10 HOH   256  1656 656  HOH   HOH A . 
V 10 HOH   257  1657 299  HOH   HOH A . 
V 10 HOH   258  1658 465  HOH   HOH A . 
V 10 HOH   259  1659 1119 HOH   HOH A . 
V 10 HOH   260  1660 2313 HOH   HOH A . 
V 10 HOH   261  1661 1010 HOH   HOH A . 
V 10 HOH   262  1662 2489 HOH   HOH A . 
V 10 HOH   263  1663 2162 HOH   HOH A . 
V 10 HOH   264  1664 534  HOH   HOH A . 
V 10 HOH   265  1665 1164 HOH   HOH A . 
V 10 HOH   266  1666 50   HOH   HOH A . 
V 10 HOH   267  1667 1779 HOH   HOH A . 
V 10 HOH   268  1668 748  HOH   HOH A . 
V 10 HOH   269  1669 1008 HOH   HOH A . 
V 10 HOH   270  1670 190  HOH   HOH A . 
V 10 HOH   271  1671 187  HOH   HOH A . 
V 10 HOH   272  1672 476  HOH   HOH A . 
V 10 HOH   273  1673 578  HOH   HOH A . 
V 10 HOH   274  1674 1413 HOH   HOH A . 
V 10 HOH   275  1675 557  HOH   HOH A . 
V 10 HOH   276  1676 236  HOH   HOH A . 
V 10 HOH   277  1677 1615 HOH   HOH A . 
V 10 HOH   278  1678 1950 HOH   HOH A . 
V 10 HOH   279  1679 385  HOH   HOH A . 
V 10 HOH   280  1680 1984 HOH   HOH A . 
V 10 HOH   281  1681 738  HOH   HOH A . 
V 10 HOH   282  1682 1208 HOH   HOH A . 
V 10 HOH   283  1683 186  HOH   HOH A . 
V 10 HOH   284  1684 648  HOH   HOH A . 
V 10 HOH   285  1685 605  HOH   HOH A . 
V 10 HOH   286  1686 36   HOH   HOH A . 
V 10 HOH   287  1687 238  HOH   HOH A . 
V 10 HOH   288  1688 805  HOH   HOH A . 
V 10 HOH   289  1689 627  HOH   HOH A . 
V 10 HOH   290  1690 995  HOH   HOH A . 
V 10 HOH   291  1691 138  HOH   HOH A . 
V 10 HOH   292  1692 341  HOH   HOH A . 
V 10 HOH   293  1693 1029 HOH   HOH A . 
V 10 HOH   294  1694 1543 HOH   HOH A . 
V 10 HOH   295  1695 82   HOH   HOH A . 
V 10 HOH   296  1696 2402 HOH   HOH A . 
V 10 HOH   297  1697 1077 HOH   HOH A . 
V 10 HOH   298  1698 216  HOH   HOH A . 
V 10 HOH   299  1699 1449 HOH   HOH A . 
V 10 HOH   300  1700 41   HOH   HOH A . 
V 10 HOH   301  1701 200  HOH   HOH A . 
V 10 HOH   302  1702 1335 HOH   HOH A . 
V 10 HOH   303  1703 1407 HOH   HOH A . 
V 10 HOH   304  1704 417  HOH   HOH A . 
V 10 HOH   305  1705 199  HOH   HOH A . 
V 10 HOH   306  1706 1217 HOH   HOH A . 
V 10 HOH   307  1707 844  HOH   HOH A . 
V 10 HOH   308  1708 2458 HOH   HOH A . 
V 10 HOH   309  1709 47   HOH   HOH A . 
V 10 HOH   310  1710 623  HOH   HOH A . 
V 10 HOH   311  1711 1570 HOH   HOH A . 
V 10 HOH   312  1712 673  HOH   HOH A . 
V 10 HOH   313  1713 413  HOH   HOH A . 
V 10 HOH   314  1714 814  HOH   HOH A . 
V 10 HOH   315  1715 590  HOH   HOH A . 
V 10 HOH   316  1716 347  HOH   HOH A . 
V 10 HOH   317  1717 786  HOH   HOH A . 
V 10 HOH   318  1718 2112 HOH   HOH A . 
V 10 HOH   319  1719 205  HOH   HOH A . 
V 10 HOH   320  1720 1619 HOH   HOH A . 
V 10 HOH   321  1721 899  HOH   HOH A . 
V 10 HOH   322  1722 2428 HOH   HOH A . 
V 10 HOH   323  1723 391  HOH   HOH A . 
V 10 HOH   324  1724 193  HOH   HOH A . 
V 10 HOH   325  1725 77   HOH   HOH A . 
V 10 HOH   326  1726 804  HOH   HOH A . 
V 10 HOH   327  1727 1    HOH   HOH A . 
V 10 HOH   328  1728 1108 HOH   HOH A . 
V 10 HOH   329  1729 2064 HOH   HOH A . 
V 10 HOH   330  1730 889  HOH   HOH A . 
V 10 HOH   331  1731 1295 HOH   HOH A . 
V 10 HOH   332  1732 363  HOH   HOH A . 
V 10 HOH   333  1733 684  HOH   HOH A . 
V 10 HOH   334  1734 176  HOH   HOH A . 
V 10 HOH   335  1735 500  HOH   HOH A . 
V 10 HOH   336  1736 535  HOH   HOH A . 
V 10 HOH   337  1737 826  HOH   HOH A . 
V 10 HOH   338  1738 165  HOH   HOH A . 
V 10 HOH   339  1739 671  HOH   HOH A . 
V 10 HOH   340  1740 1311 HOH   HOH A . 
V 10 HOH   341  1741 1373 HOH   HOH A . 
V 10 HOH   342  1742 1116 HOH   HOH A . 
V 10 HOH   343  1743 231  HOH   HOH A . 
V 10 HOH   344  1744 1060 HOH   HOH A . 
V 10 HOH   345  1745 2294 HOH   HOH A . 
V 10 HOH   346  1746 1606 HOH   HOH A . 
V 10 HOH   347  1747 757  HOH   HOH A . 
V 10 HOH   348  1748 1435 HOH   HOH A . 
V 10 HOH   349  1749 2531 HOH   HOH A . 
V 10 HOH   350  1750 966  HOH   HOH A . 
V 10 HOH   351  1751 1160 HOH   HOH A . 
V 10 HOH   352  1752 478  HOH   HOH A . 
V 10 HOH   353  1753 1054 HOH   HOH A . 
V 10 HOH   354  1754 528  HOH   HOH A . 
V 10 HOH   355  1755 420  HOH   HOH A . 
V 10 HOH   356  1756 342  HOH   HOH A . 
V 10 HOH   357  1757 121  HOH   HOH A . 
V 10 HOH   358  1758 739  HOH   HOH A . 
V 10 HOH   359  1759 1225 HOH   HOH A . 
V 10 HOH   360  1760 1052 HOH   HOH A . 
V 10 HOH   361  1761 784  HOH   HOH A . 
V 10 HOH   362  1762 399  HOH   HOH A . 
V 10 HOH   363  1763 553  HOH   HOH A . 
V 10 HOH   364  1764 374  HOH   HOH A . 
V 10 HOH   365  1765 1218 HOH   HOH A . 
V 10 HOH   366  1766 1362 HOH   HOH A . 
V 10 HOH   367  1767 457  HOH   HOH A . 
V 10 HOH   368  1768 1494 HOH   HOH A . 
V 10 HOH   369  1769 20   HOH   HOH A . 
V 10 HOH   370  1770 464  HOH   HOH A . 
V 10 HOH   371  1771 941  HOH   HOH A . 
V 10 HOH   372  1772 646  HOH   HOH A . 
V 10 HOH   373  1773 164  HOH   HOH A . 
V 10 HOH   374  1774 874  HOH   HOH A . 
V 10 HOH   375  1775 608  HOH   HOH A . 
V 10 HOH   376  1776 214  HOH   HOH A . 
V 10 HOH   377  1777 659  HOH   HOH A . 
V 10 HOH   378  1778 110  HOH   HOH A . 
V 10 HOH   379  1779 505  HOH   HOH A . 
V 10 HOH   380  1780 390  HOH   HOH A . 
V 10 HOH   381  1781 936  HOH   HOH A . 
V 10 HOH   382  1782 144  HOH   HOH A . 
V 10 HOH   383  1783 2248 HOH   HOH A . 
V 10 HOH   384  1784 486  HOH   HOH A . 
V 10 HOH   385  1785 1038 HOH   HOH A . 
V 10 HOH   386  1786 660  HOH   HOH A . 
V 10 HOH   387  1787 127  HOH   HOH A . 
V 10 HOH   388  1788 2226 HOH   HOH A . 
V 10 HOH   389  1789 1370 HOH   HOH A . 
V 10 HOH   390  1790 998  HOH   HOH A . 
V 10 HOH   391  1791 516  HOH   HOH A . 
V 10 HOH   392  1792 170  HOH   HOH A . 
V 10 HOH   393  1793 1061 HOH   HOH A . 
V 10 HOH   394  1794 455  HOH   HOH A . 
V 10 HOH   395  1795 1815 HOH   HOH A . 
V 10 HOH   396  1796 1743 HOH   HOH A . 
V 10 HOH   397  1797 981  HOH   HOH A . 
V 10 HOH   398  1798 665  HOH   HOH A . 
V 10 HOH   399  1799 2141 HOH   HOH A . 
V 10 HOH   400  1800 74   HOH   HOH A . 
V 10 HOH   401  1801 92   HOH   HOH A . 
V 10 HOH   402  1802 1106 HOH   HOH A . 
V 10 HOH   403  1803 480  HOH   HOH A . 
V 10 HOH   404  1804 512  HOH   HOH A . 
V 10 HOH   405  1805 517  HOH   HOH A . 
V 10 HOH   406  1806 1767 HOH   HOH A . 
V 10 HOH   407  1807 1289 HOH   HOH A . 
V 10 HOH   408  1808 412  HOH   HOH A . 
V 10 HOH   409  1809 108  HOH   HOH A . 
V 10 HOH   410  1810 2473 HOH   HOH A . 
V 10 HOH   411  1811 923  HOH   HOH A . 
V 10 HOH   412  1812 894  HOH   HOH A . 
V 10 HOH   413  1813 1999 HOH   HOH A . 
V 10 HOH   414  1814 475  HOH   HOH A . 
V 10 HOH   415  1815 606  HOH   HOH A . 
V 10 HOH   416  1816 357  HOH   HOH A . 
V 10 HOH   417  1817 1634 HOH   HOH A . 
V 10 HOH   418  1818 906  HOH   HOH A . 
V 10 HOH   419  1819 387  HOH   HOH A . 
V 10 HOH   420  1820 734  HOH   HOH A . 
V 10 HOH   421  1821 1910 HOH   HOH A . 
V 10 HOH   422  1822 812  HOH   HOH A . 
V 10 HOH   423  1823 2286 HOH   HOH A . 
V 10 HOH   424  1824 1810 HOH   HOH A . 
V 10 HOH   425  1825 436  HOH   HOH A . 
V 10 HOH   426  1826 242  HOH   HOH A . 
V 10 HOH   427  1827 33   HOH   HOH A . 
V 10 HOH   428  1828 1243 HOH   HOH A . 
V 10 HOH   429  1829 249  HOH   HOH A . 
V 10 HOH   430  1830 725  HOH   HOH A . 
V 10 HOH   431  1831 204  HOH   HOH A . 
V 10 HOH   432  1832 1262 HOH   HOH A . 
V 10 HOH   433  1833 37   HOH   HOH A . 
V 10 HOH   434  1834 620  HOH   HOH A . 
V 10 HOH   435  1835 398  HOH   HOH A . 
V 10 HOH   436  1836 1086 HOH   HOH A . 
V 10 HOH   437  1837 1050 HOH   HOH A . 
V 10 HOH   438  1838 286  HOH   HOH A . 
V 10 HOH   439  1839 159  HOH   HOH A . 
V 10 HOH   440  1840 1640 HOH   HOH A . 
V 10 HOH   441  1841 868  HOH   HOH A . 
V 10 HOH   442  1842 745  HOH   HOH A . 
V 10 HOH   443  1843 1101 HOH   HOH A . 
V 10 HOH   444  1844 262  HOH   HOH A . 
V 10 HOH   445  1845 280  HOH   HOH A . 
V 10 HOH   446  1846 474  HOH   HOH A . 
V 10 HOH   447  1847 2176 HOH   HOH A . 
V 10 HOH   448  1848 407  HOH   HOH A . 
V 10 HOH   449  1849 168  HOH   HOH A . 
V 10 HOH   450  1850 1152 HOH   HOH A . 
V 10 HOH   451  1851 1684 HOH   HOH A . 
V 10 HOH   452  1852 787  HOH   HOH A . 
V 10 HOH   453  1853 443  HOH   HOH A . 
V 10 HOH   454  1854 1275 HOH   HOH A . 
V 10 HOH   455  1855 62   HOH   HOH A . 
V 10 HOH   456  1856 1553 HOH   HOH A . 
V 10 HOH   457  1857 297  HOH   HOH A . 
V 10 HOH   458  1858 1579 HOH   HOH A . 
V 10 HOH   459  1859 422  HOH   HOH A . 
V 10 HOH   460  1860 702  HOH   HOH A . 
V 10 HOH   461  1861 326  HOH   HOH A . 
V 10 HOH   462  1862 1540 HOH   HOH A . 
V 10 HOH   463  1863 1065 HOH   HOH A . 
V 10 HOH   464  1864 1738 HOH   HOH A . 
V 10 HOH   465  1865 2266 HOH   HOH A . 
V 10 HOH   466  1866 622  HOH   HOH A . 
V 10 HOH   467  1867 233  HOH   HOH A . 
V 10 HOH   468  1868 1772 HOH   HOH A . 
V 10 HOH   469  1869 736  HOH   HOH A . 
V 10 HOH   470  1870 2553 HOH   HOH A . 
V 10 HOH   471  1871 2178 HOH   HOH A . 
V 10 HOH   472  1872 831  HOH   HOH A . 
V 10 HOH   473  1873 724  HOH   HOH A . 
V 10 HOH   474  1874 1417 HOH   HOH A . 
V 10 HOH   475  1875 591  HOH   HOH A . 
V 10 HOH   476  1876 349  HOH   HOH A . 
V 10 HOH   477  1877 487  HOH   HOH A . 
V 10 HOH   478  1878 171  HOH   HOH A . 
V 10 HOH   479  1879 1635 HOH   HOH A . 
V 10 HOH   480  1880 922  HOH   HOH A . 
V 10 HOH   481  1881 541  HOH   HOH A . 
V 10 HOH   482  1882 1138 HOH   HOH A . 
V 10 HOH   483  1883 2016 HOH   HOH A . 
V 10 HOH   484  1884 460  HOH   HOH A . 
V 10 HOH   485  1885 160  HOH   HOH A . 
V 10 HOH   486  1886 1741 HOH   HOH A . 
V 10 HOH   487  1887 709  HOH   HOH A . 
V 10 HOH   488  1888 1109 HOH   HOH A . 
V 10 HOH   489  1889 2347 HOH   HOH A . 
V 10 HOH   490  1890 549  HOH   HOH A . 
V 10 HOH   491  1891 774  HOH   HOH A . 
V 10 HOH   492  1892 1418 HOH   HOH A . 
V 10 HOH   493  1893 491  HOH   HOH A . 
V 10 HOH   494  1894 688  HOH   HOH A . 
V 10 HOH   495  1895 1223 HOH   HOH A . 
V 10 HOH   496  1896 220  HOH   HOH A . 
V 10 HOH   497  1897 1247 HOH   HOH A . 
V 10 HOH   498  1898 2046 HOH   HOH A . 
V 10 HOH   499  1899 970  HOH   HOH A . 
V 10 HOH   500  1900 415  HOH   HOH A . 
V 10 HOH   501  1901 2161 HOH   HOH A . 
V 10 HOH   502  1902 191  HOH   HOH A . 
V 10 HOH   503  1903 1365 HOH   HOH A . 
V 10 HOH   504  1904 253  HOH   HOH A . 
V 10 HOH   505  1905 2443 HOH   HOH A . 
V 10 HOH   506  1906 836  HOH   HOH A . 
V 10 HOH   507  1907 1157 HOH   HOH A . 
V 10 HOH   508  1908 969  HOH   HOH A . 
V 10 HOH   509  1909 687  HOH   HOH A . 
V 10 HOH   510  1910 1557 HOH   HOH A . 
V 10 HOH   511  1911 61   HOH   HOH A . 
V 10 HOH   512  1912 1974 HOH   HOH A . 
V 10 HOH   513  1913 1723 HOH   HOH A . 
V 10 HOH   514  1914 1239 HOH   HOH A . 
V 10 HOH   515  1915 1252 HOH   HOH A . 
V 10 HOH   516  1916 2503 HOH   HOH A . 
V 10 HOH   517  1917 1094 HOH   HOH A . 
V 10 HOH   518  1918 1588 HOH   HOH A . 
V 10 HOH   519  1919 1774 HOH   HOH A . 
V 10 HOH   520  1920 1681 HOH   HOH A . 
V 10 HOH   521  1921 504  HOH   HOH A . 
V 10 HOH   522  1922 1920 HOH   HOH A . 
V 10 HOH   523  1923 508  HOH   HOH A . 
V 10 HOH   524  1924 765  HOH   HOH A . 
V 10 HOH   525  1925 642  HOH   HOH A . 
V 10 HOH   526  1926 1483 HOH   HOH A . 
V 10 HOH   527  1927 1988 HOH   HOH A . 
V 10 HOH   528  1928 2523 HOH   HOH A . 
V 10 HOH   529  1929 1668 HOH   HOH A . 
V 10 HOH   530  1930 209  HOH   HOH A . 
V 10 HOH   531  1931 259  HOH   HOH A . 
V 10 HOH   532  1932 1066 HOH   HOH A . 
V 10 HOH   533  1933 893  HOH   HOH A . 
V 10 HOH   534  1934 1277 HOH   HOH A . 
V 10 HOH   535  1935 1051 HOH   HOH A . 
V 10 HOH   536  1936 993  HOH   HOH A . 
V 10 HOH   537  1937 1523 HOH   HOH A . 
V 10 HOH   538  1938 683  HOH   HOH A . 
V 10 HOH   539  1939 1013 HOH   HOH A . 
V 10 HOH   540  1940 834  HOH   HOH A . 
V 10 HOH   541  1941 102  HOH   HOH A . 
V 10 HOH   542  1942 1209 HOH   HOH A . 
V 10 HOH   543  1943 489  HOH   HOH A . 
V 10 HOH   544  1944 962  HOH   HOH A . 
V 10 HOH   545  1945 424  HOH   HOH A . 
V 10 HOH   546  1946 1258 HOH   HOH A . 
V 10 HOH   547  1947 1219 HOH   HOH A . 
V 10 HOH   548  1948 225  HOH   HOH A . 
V 10 HOH   549  1949 1919 HOH   HOH A . 
V 10 HOH   550  1950 1702 HOH   HOH A . 
V 10 HOH   551  1951 1746 HOH   HOH A . 
V 10 HOH   552  1952 997  HOH   HOH A . 
V 10 HOH   553  1953 2053 HOH   HOH A . 
V 10 HOH   554  1954 1469 HOH   HOH A . 
V 10 HOH   555  1955 1693 HOH   HOH A . 
V 10 HOH   556  1956 870  HOH   HOH A . 
V 10 HOH   557  1957 617  HOH   HOH A . 
V 10 HOH   558  1958 31   HOH   HOH A . 
V 10 HOH   559  1959 944  HOH   HOH A . 
V 10 HOH   560  1960 378  HOH   HOH A . 
V 10 HOH   561  1961 645  HOH   HOH A . 
V 10 HOH   562  1962 1967 HOH   HOH A . 
V 10 HOH   563  1963 2179 HOH   HOH A . 
V 10 HOH   564  1964 555  HOH   HOH A . 
V 10 HOH   565  1965 34   HOH   HOH A . 
V 10 HOH   566  1966 1084 HOH   HOH A . 
V 10 HOH   567  1967 2499 HOH   HOH A . 
V 10 HOH   568  1968 294  HOH   HOH A . 
V 10 HOH   569  1969 582  HOH   HOH A . 
V 10 HOH   570  1970 2524 HOH   HOH A . 
V 10 HOH   571  1971 1316 HOH   HOH A . 
V 10 HOH   572  1972 1462 HOH   HOH A . 
V 10 HOH   573  1973 72   HOH   HOH A . 
V 10 HOH   574  1974 502  HOH   HOH A . 
V 10 HOH   575  1975 1652 HOH   HOH A . 
V 10 HOH   576  1976 819  HOH   HOH A . 
V 10 HOH   577  1977 2014 HOH   HOH A . 
V 10 HOH   578  1978 400  HOH   HOH A . 
V 10 HOH   579  1979 971  HOH   HOH A . 
V 10 HOH   580  1980 563  HOH   HOH A . 
V 10 HOH   581  1981 916  HOH   HOH A . 
V 10 HOH   582  1982 614  HOH   HOH A . 
V 10 HOH   583  1983 194  HOH   HOH A . 
V 10 HOH   584  1984 142  HOH   HOH A . 
V 10 HOH   585  1985 1479 HOH   HOH A . 
V 10 HOH   586  1986 1882 HOH   HOH A . 
V 10 HOH   587  1987 1991 HOH   HOH A . 
V 10 HOH   588  1988 1857 HOH   HOH A . 
V 10 HOH   589  1989 479  HOH   HOH A . 
V 10 HOH   590  1990 2306 HOH   HOH A . 
V 10 HOH   591  1991 783  HOH   HOH A . 
V 10 HOH   592  1992 130  HOH   HOH A . 
V 10 HOH   593  1993 867  HOH   HOH A . 
V 10 HOH   594  1994 268  HOH   HOH A . 
V 10 HOH   595  1995 343  HOH   HOH A . 
V 10 HOH   596  1996 716  HOH   HOH A . 
V 10 HOH   597  1997 1037 HOH   HOH A . 
V 10 HOH   598  1998 976  HOH   HOH A . 
V 10 HOH   599  1999 1907 HOH   HOH A . 
V 10 HOH   600  2000 778  HOH   HOH A . 
V 10 HOH   601  2001 331  HOH   HOH A . 
V 10 HOH   602  2002 2386 HOH   HOH A . 
V 10 HOH   603  2003 201  HOH   HOH A . 
V 10 HOH   604  2004 2    HOH   HOH A . 
V 10 HOH   605  2005 703  HOH   HOH A . 
V 10 HOH   606  2006 830  HOH   HOH A . 
V 10 HOH   607  2007 2279 HOH   HOH A . 
V 10 HOH   608  2008 332  HOH   HOH A . 
V 10 HOH   609  2009 483  HOH   HOH A . 
V 10 HOH   610  2010 1422 HOH   HOH A . 
V 10 HOH   611  2011 1878 HOH   HOH A . 
V 10 HOH   612  2012 1244 HOH   HOH A . 
V 10 HOH   613  2013 1130 HOH   HOH A . 
V 10 HOH   614  2014 1638 HOH   HOH A . 
V 10 HOH   615  2015 1005 HOH   HOH A . 
V 10 HOH   616  2016 91   HOH   HOH A . 
V 10 HOH   617  2017 1833 HOH   HOH A . 
V 10 HOH   618  2018 1006 HOH   HOH A . 
V 10 HOH   619  2019 1319 HOH   HOH A . 
V 10 HOH   620  2020 835  HOH   HOH A . 
V 10 HOH   621  2021 1731 HOH   HOH A . 
V 10 HOH   622  2022 1482 HOH   HOH A . 
V 10 HOH   623  2023 2147 HOH   HOH A . 
V 10 HOH   624  2024 524  HOH   HOH A . 
V 10 HOH   625  2025 1636 HOH   HOH A . 
V 10 HOH   626  2026 510  HOH   HOH A . 
V 10 HOH   627  2027 1254 HOH   HOH A . 
V 10 HOH   628  2028 260  HOH   HOH A . 
V 10 HOH   629  2029 454  HOH   HOH A . 
V 10 HOH   630  2030 977  HOH   HOH A . 
V 10 HOH   631  2031 364  HOH   HOH A . 
V 10 HOH   632  2032 1211 HOH   HOH A . 
V 10 HOH   633  2033 571  HOH   HOH A . 
V 10 HOH   634  2034 1953 HOH   HOH A . 
V 10 HOH   635  2035 1808 HOH   HOH A . 
V 10 HOH   636  2036 2180 HOH   HOH A . 
V 10 HOH   637  2037 183  HOH   HOH A . 
V 10 HOH   638  2038 1234 HOH   HOH A . 
V 10 HOH   639  2039 1287 HOH   HOH A . 
V 10 HOH   640  2040 2074 HOH   HOH A . 
V 10 HOH   641  2041 1133 HOH   HOH A . 
V 10 HOH   642  2042 289  HOH   HOH A . 
V 10 HOH   643  2043 1113 HOH   HOH A . 
V 10 HOH   644  2044 863  HOH   HOH A . 
V 10 HOH   645  2045 2004 HOH   HOH A . 
V 10 HOH   646  2046 639  HOH   HOH A . 
V 10 HOH   647  2047 2595 HOH   HOH A . 
V 10 HOH   648  2048 111  HOH   HOH A . 
V 10 HOH   649  2049 581  HOH   HOH A . 
V 10 HOH   650  2050 1531 HOH   HOH A . 
V 10 HOH   651  2051 1864 HOH   HOH A . 
V 10 HOH   652  2052 230  HOH   HOH A . 
V 10 HOH   653  2053 2455 HOH   HOH A . 
V 10 HOH   654  2054 207  HOH   HOH A . 
V 10 HOH   655  2055 2493 HOH   HOH A . 
V 10 HOH   656  2056 1587 HOH   HOH A . 
V 10 HOH   657  2057 876  HOH   HOH A . 
V 10 HOH   658  2058 1653 HOH   HOH A . 
V 10 HOH   659  2059 1491 HOH   HOH A . 
V 10 HOH   660  2060 1184 HOH   HOH A . 
V 10 HOH   661  2061 403  HOH   HOH A . 
V 10 HOH   662  2062 453  HOH   HOH A . 
V 10 HOH   663  2063 2060 HOH   HOH A . 
V 10 HOH   664  2064 300  HOH   HOH A . 
V 10 HOH   665  2065 2170 HOH   HOH A . 
V 10 HOH   666  2066 610  HOH   HOH A . 
V 10 HOH   667  2067 1822 HOH   HOH A . 
V 10 HOH   668  2068 839  HOH   HOH A . 
V 10 HOH   669  2069 2230 HOH   HOH A . 
V 10 HOH   670  2070 1074 HOH   HOH A . 
V 10 HOH   671  2071 1097 HOH   HOH A . 
V 10 HOH   672  2072 523  HOH   HOH A . 
V 10 HOH   673  2073 1574 HOH   HOH A . 
V 10 HOH   674  2074 1082 HOH   HOH A . 
V 10 HOH   675  2075 381  HOH   HOH A . 
V 10 HOH   676  2076 1487 HOH   HOH A . 
V 10 HOH   677  2077 1150 HOH   HOH A . 
V 10 HOH   678  2078 1571 HOH   HOH A . 
V 10 HOH   679  2079 1303 HOH   HOH A . 
V 10 HOH   680  2080 692  HOH   HOH A . 
V 10 HOH   681  2081 925  HOH   HOH A . 
V 10 HOH   682  2082 1451 HOH   HOH A . 
V 10 HOH   683  2083 1719 HOH   HOH A . 
V 10 HOH   684  2084 338  HOH   HOH A . 
V 10 HOH   685  2085 1318 HOH   HOH A . 
V 10 HOH   686  2086 1831 HOH   HOH A . 
V 10 HOH   687  2087 279  HOH   HOH A . 
V 10 HOH   688  2088 1034 HOH   HOH A . 
V 10 HOH   689  2089 1242 HOH   HOH A . 
V 10 HOH   690  2090 781  HOH   HOH A . 
V 10 HOH   691  2091 1555 HOH   HOH A . 
V 10 HOH   692  2092 589  HOH   HOH A . 
V 10 HOH   693  2093 2225 HOH   HOH A . 
V 10 HOH   694  2094 583  HOH   HOH A . 
V 10 HOH   695  2095 1047 HOH   HOH A . 
V 10 HOH   696  2096 1131 HOH   HOH A . 
V 10 HOH   697  2097 208  HOH   HOH A . 
V 10 HOH   698  2098 813  HOH   HOH A . 
V 10 HOH   699  2099 929  HOH   HOH A . 
V 10 HOH   700  2100 389  HOH   HOH A . 
V 10 HOH   701  2101 594  HOH   HOH A . 
V 10 HOH   702  2102 258  HOH   HOH A . 
V 10 HOH   703  2103 353  HOH   HOH A . 
V 10 HOH   704  2104 1786 HOH   HOH A . 
V 10 HOH   705  2105 494  HOH   HOH A . 
V 10 HOH   706  2106 574  HOH   HOH A . 
V 10 HOH   707  2107 1665 HOH   HOH A . 
V 10 HOH   708  2108 632  HOH   HOH A . 
V 10 HOH   709  2109 1016 HOH   HOH A . 
V 10 HOH   710  2110 1267 HOH   HOH A . 
V 10 HOH   711  2111 945  HOH   HOH A . 
V 10 HOH   712  2112 1026 HOH   HOH A . 
V 10 HOH   713  2113 263  HOH   HOH A . 
V 10 HOH   714  2114 951  HOH   HOH A . 
V 10 HOH   715  2115 513  HOH   HOH A . 
V 10 HOH   716  2116 1159 HOH   HOH A . 
V 10 HOH   717  2117 351  HOH   HOH A . 
V 10 HOH   718  2118 818  HOH   HOH A . 
V 10 HOH   719  2119 1296 HOH   HOH A . 
V 10 HOH   720  2120 1445 HOH   HOH A . 
V 10 HOH   721  2121 1811 HOH   HOH A . 
V 10 HOH   722  2122 1728 HOH   HOH A . 
V 10 HOH   723  2123 1607 HOH   HOH A . 
V 10 HOH   724  2124 1306 HOH   HOH A . 
V 10 HOH   725  2125 1409 HOH   HOH A . 
V 10 HOH   726  2126 871  HOH   HOH A . 
V 10 HOH   727  2127 2008 HOH   HOH A . 
V 10 HOH   728  2128 761  HOH   HOH A . 
V 10 HOH   729  2129 1667 HOH   HOH A . 
V 10 HOH   730  2130 539  HOH   HOH A . 
V 10 HOH   731  2131 882  HOH   HOH A . 
V 10 HOH   732  2132 1273 HOH   HOH A . 
V 10 HOH   733  2133 446  HOH   HOH A . 
V 10 HOH   734  2134 496  HOH   HOH A . 
V 10 HOH   735  2135 2011 HOH   HOH A . 
V 10 HOH   736  2136 2045 HOH   HOH A . 
V 10 HOH   737  2137 2146 HOH   HOH A . 
V 10 HOH   738  2138 1506 HOH   HOH A . 
V 10 HOH   739  2139 2212 HOH   HOH A . 
V 10 HOH   740  2140 2431 HOH   HOH A . 
V 10 HOH   741  2141 2063 HOH   HOH A . 
V 10 HOH   742  2142 744  HOH   HOH A . 
V 10 HOH   743  2143 607  HOH   HOH A . 
V 10 HOH   744  2144 388  HOH   HOH A . 
V 10 HOH   745  2145 2145 HOH   HOH A . 
V 10 HOH   746  2146 1474 HOH   HOH A . 
V 10 HOH   747  2147 1753 HOH   HOH A . 
V 10 HOH   748  2148 1136 HOH   HOH A . 
V 10 HOH   749  2149 720  HOH   HOH A . 
V 10 HOH   750  2150 2071 HOH   HOH A . 
V 10 HOH   751  2151 2322 HOH   HOH A . 
V 10 HOH   752  2152 900  HOH   HOH A . 
V 10 HOH   753  2153 1799 HOH   HOH A . 
V 10 HOH   754  2154 76   HOH   HOH A . 
V 10 HOH   755  2155 912  HOH   HOH A . 
V 10 HOH   756  2156 346  HOH   HOH A . 
V 10 HOH   757  2157 1575 HOH   HOH A . 
V 10 HOH   758  2158 373  HOH   HOH A . 
V 10 HOH   759  2159 2481 HOH   HOH A . 
V 10 HOH   760  2160 1647 HOH   HOH A . 
V 10 HOH   761  2161 676  HOH   HOH A . 
V 10 HOH   762  2162 1880 HOH   HOH A . 
V 10 HOH   763  2163 664  HOH   HOH A . 
V 10 HOH   764  2164 1659 HOH   HOH A . 
V 10 HOH   765  2165 468  HOH   HOH A . 
V 10 HOH   766  2166 1841 HOH   HOH A . 
V 10 HOH   767  2167 817  HOH   HOH A . 
V 10 HOH   768  2168 842  HOH   HOH A . 
V 10 HOH   769  2169 585  HOH   HOH A . 
V 10 HOH   770  2170 275  HOH   HOH A . 
V 10 HOH   771  2171 548  HOH   HOH A . 
V 10 HOH   772  2172 2148 HOH   HOH A . 
V 10 HOH   773  2173 1956 HOH   HOH A . 
V 10 HOH   774  2174 2364 HOH   HOH A . 
V 10 HOH   775  2175 2134 HOH   HOH A . 
V 10 HOH   776  2176 921  HOH   HOH A . 
V 10 HOH   777  2177 188  HOH   HOH A . 
V 10 HOH   778  2178 181  HOH   HOH A . 
V 10 HOH   779  2179 2315 HOH   HOH A . 
V 10 HOH   780  2180 281  HOH   HOH A . 
V 10 HOH   781  2181 376  HOH   HOH A . 
V 10 HOH   782  2182 1172 HOH   HOH A . 
V 10 HOH   783  2183 1332 HOH   HOH A . 
V 10 HOH   784  2184 2369 HOH   HOH A . 
V 10 HOH   785  2185 1452 HOH   HOH A . 
V 10 HOH   786  2186 1102 HOH   HOH A . 
V 10 HOH   787  2187 366  HOH   HOH A . 
V 10 HOH   788  2188 942  HOH   HOH A . 
V 10 HOH   789  2189 2081 HOH   HOH A . 
V 10 HOH   790  2190 450  HOH   HOH A . 
V 10 HOH   791  2191 2054 HOH   HOH A . 
V 10 HOH   792  2192 1673 HOH   HOH A . 
V 10 HOH   793  2193 1269 HOH   HOH A . 
V 10 HOH   794  2194 1179 HOH   HOH A . 
V 10 HOH   795  2195 1994 HOH   HOH A . 
V 10 HOH   796  2196 1952 HOH   HOH A . 
V 10 HOH   797  2197 1364 HOH   HOH A . 
V 10 HOH   798  2198 2091 HOH   HOH A . 
V 10 HOH   799  2199 1961 HOH   HOH A . 
V 10 HOH   800  2200 1835 HOH   HOH A . 
V 10 HOH   801  2201 1591 HOH   HOH A . 
V 10 HOH   802  2202 855  HOH   HOH A . 
V 10 HOH   803  2203 1817 HOH   HOH A . 
V 10 HOH   804  2204 1154 HOH   HOH A . 
V 10 HOH   805  2205 2129 HOH   HOH A . 
V 10 HOH   806  2206 2128 HOH   HOH A . 
V 10 HOH   807  2207 1182 HOH   HOH A . 
V 10 HOH   808  2208 45   HOH   HOH A . 
V 10 HOH   809  2209 1393 HOH   HOH A . 
V 10 HOH   810  2210 1997 HOH   HOH A . 
V 10 HOH   811  2211 988  HOH   HOH A . 
V 10 HOH   812  2212 1820 HOH   HOH A . 
V 10 HOH   813  2213 2249 HOH   HOH A . 
V 10 HOH   814  2214 1055 HOH   HOH A . 
V 10 HOH   815  2215 1088 HOH   HOH A . 
V 10 HOH   816  2216 959  HOH   HOH A . 
V 10 HOH   817  2217 1354 HOH   HOH A . 
V 10 HOH   818  2218 1112 HOH   HOH A . 
V 10 HOH   819  2219 847  HOH   HOH A . 
V 10 HOH   820  2220 2358 HOH   HOH A . 
V 10 HOH   821  2221 1682 HOH   HOH A . 
V 10 HOH   822  2222 2263 HOH   HOH A . 
V 10 HOH   823  2223 255  HOH   HOH A . 
V 10 HOH   824  2224 2181 HOH   HOH A . 
V 10 HOH   825  2225 989  HOH   HOH A . 
V 10 HOH   826  2226 2344 HOH   HOH A . 
V 10 HOH   827  2227 1140 HOH   HOH A . 
V 10 HOH   828  2228 792  HOH   HOH A . 
V 10 HOH   829  2229 2566 HOH   HOH A . 
V 10 HOH   830  2230 1735 HOH   HOH A . 
V 10 HOH   831  2231 2047 HOH   HOH A . 
V 10 HOH   832  2232 1341 HOH   HOH A . 
V 10 HOH   833  2233 1514 HOH   HOH A . 
V 10 HOH   834  2234 2323 HOH   HOH A . 
V 10 HOH   835  2235 2376 HOH   HOH A . 
V 10 HOH   836  2236 2127 HOH   HOH A . 
V 10 HOH   837  2237 1168 HOH   HOH A . 
V 10 HOH   838  2238 2451 HOH   HOH A . 
V 10 HOH   839  2239 2391 HOH   HOH A . 
V 10 HOH   840  2240 859  HOH   HOH A . 
V 10 HOH   841  2241 2462 HOH   HOH A . 
V 10 HOH   842  2242 1599 HOH   HOH A . 
V 10 HOH   843  2243 1489 HOH   HOH A . 
V 10 HOH   844  2244 435  HOH   HOH A . 
V 10 HOH   845  2245 1522 HOH   HOH A . 
V 10 HOH   846  2246 1464 HOH   HOH A . 
V 10 HOH   847  2247 1945 HOH   HOH A . 
V 10 HOH   848  2248 1935 HOH   HOH A . 
V 10 HOH   849  2249 1850 HOH   HOH A . 
V 10 HOH   850  2250 1827 HOH   HOH A . 
V 10 HOH   851  2251 776  HOH   HOH A . 
V 10 HOH   852  2252 2267 HOH   HOH A . 
V 10 HOH   853  2253 1722 HOH   HOH A . 
V 10 HOH   854  2254 1292 HOH   HOH A . 
V 10 HOH   855  2255 2392 HOH   HOH A . 
V 10 HOH   856  2256 1875 HOH   HOH A . 
V 10 HOH   857  2257 1713 HOH   HOH A . 
V 10 HOH   858  2258 1886 HOH   HOH A . 
V 10 HOH   859  2259 782  HOH   HOH A . 
V 10 HOH   860  2260 592  HOH   HOH A . 
V 10 HOH   861  2261 643  HOH   HOH A . 
V 10 HOH   862  2262 2144 HOH   HOH A . 
V 10 HOH   863  2263 1323 HOH   HOH A . 
V 10 HOH   864  2264 1492 HOH   HOH A . 
V 10 HOH   865  2265 633  HOH   HOH A . 
V 10 HOH   866  2266 2338 HOH   HOH A . 
V 10 HOH   867  2267 5    HOH   HOH A . 
V 10 HOH   868  2268 1115 HOH   HOH A . 
V 10 HOH   869  2269 501  HOH   HOH A . 
V 10 HOH   870  2270 2024 HOH   HOH A . 
V 10 HOH   871  2271 2255 HOH   HOH A . 
V 10 HOH   872  2272 1705 HOH   HOH A . 
V 10 HOH   873  2273 1406 HOH   HOH A . 
V 10 HOH   874  2274 2471 HOH   HOH A . 
V 10 HOH   875  2275 2456 HOH   HOH A . 
V 10 HOH   876  2276 1801 HOH   HOH A . 
V 10 HOH   877  2277 1165 HOH   HOH A . 
V 10 HOH   878  2278 2137 HOH   HOH A . 
V 10 HOH   879  2279 2320 HOH   HOH A . 
V 10 HOH   880  2280 1442 HOH   HOH A . 
V 10 HOH   881  2281 1025 HOH   HOH A . 
V 10 HOH   882  2282 2036 HOH   HOH A . 
V 10 HOH   883  2283 1837 HOH   HOH A . 
V 10 HOH   884  2284 1117 HOH   HOH A . 
V 10 HOH   885  2285 2198 HOH   HOH A . 
V 10 HOH   886  2286 520  HOH   HOH A . 
V 10 HOH   887  2287 2113 HOH   HOH A . 
V 10 HOH   888  2288 2508 HOH   HOH A . 
V 10 HOH   889  2289 2221 HOH   HOH A . 
V 10 HOH   890  2290 1628 HOH   HOH A . 
V 10 HOH   891  2291 832  HOH   HOH A . 
V 10 HOH   892  2292 1089 HOH   HOH A . 
V 10 HOH   893  2293 2268 HOH   HOH A . 
V 10 HOH   894  2294 329  HOH   HOH A . 
V 10 HOH   895  2295 2288 HOH   HOH A . 
V 10 HOH   896  2296 700  HOH   HOH A . 
V 10 HOH   897  2297 1717 HOH   HOH A . 
V 10 HOH   898  2298 1795 HOH   HOH A . 
V 10 HOH   899  2299 2254 HOH   HOH A . 
V 10 HOH   900  2300 1651 HOH   HOH A . 
V 10 HOH   901  2301 2500 HOH   HOH A . 
V 10 HOH   902  2302 2423 HOH   HOH A . 
V 10 HOH   903  2303 2084 HOH   HOH A . 
V 10 HOH   904  2304 2213 HOH   HOH A . 
V 10 HOH   905  2305 1073 HOH   HOH A . 
V 10 HOH   906  2306 861  HOH   HOH A . 
V 10 HOH   907  2307 2410 HOH   HOH A . 
V 10 HOH   908  2308 2483 HOH   HOH A . 
V 10 HOH   909  2309 2549 HOH   HOH A . 
V 10 HOH   910  2310 1558 HOH   HOH A . 
V 10 HOH   911  2311 1807 HOH   HOH A . 
V 10 HOH   912  2312 1276 HOH   HOH A . 
V 10 HOH   913  2313 1773 HOH   HOH A . 
V 10 HOH   914  2314 2556 HOH   HOH A . 
V 10 HOH   915  2315 1739 HOH   HOH A . 
V 10 HOH   916  2316 2260 HOH   HOH A . 
V 10 HOH   917  2317 1973 HOH   HOH A . 
V 10 HOH   918  2318 2581 HOH   HOH A . 
V 10 HOH   919  2319 2450 HOH   HOH A . 
V 10 HOH   920  2320 2143 HOH   HOH A . 
V 10 HOH   921  2321 1536 HOH   HOH A . 
V 10 HOH   922  2322 2361 HOH   HOH A . 
V 10 HOH   923  2323 537  HOH   HOH A . 
V 10 HOH   924  2324 1507 HOH   HOH A . 
V 10 HOH   925  2325 2177 HOH   HOH A . 
V 10 HOH   926  2326 1002 HOH   HOH A . 
V 10 HOH   927  2327 1446 HOH   HOH A . 
V 10 HOH   928  2328 1854 HOH   HOH A . 
V 10 HOH   929  2329 1664 HOH   HOH A . 
V 10 HOH   930  2330 2378 HOH   HOH A . 
V 10 HOH   931  2331 550  HOH   HOH A . 
V 10 HOH   932  2332 1436 HOH   HOH A . 
V 10 HOH   933  2333 957  HOH   HOH A . 
V 10 HOH   934  2334 1700 HOH   HOH A . 
V 10 HOH   935  2335 961  HOH   HOH A . 
V 10 HOH   936  2336 2224 HOH   HOH A . 
V 10 HOH   937  2337 2569 HOH   HOH A . 
V 10 HOH   938  2338 2258 HOH   HOH A . 
V 10 HOH   939  2339 1622 HOH   HOH A . 
V 10 HOH   940  2340 2366 HOH   HOH A . 
V 10 HOH   941  2341 2592 HOH   HOH A . 
V 10 HOH   942  2342 1340 HOH   HOH A . 
V 10 HOH   943  2343 1926 HOH   HOH A . 
V 10 HOH   944  2344 984  HOH   HOH A . 
V 10 HOH   945  2345 2587 HOH   HOH A . 
V 10 HOH   946  2346 2191 HOH   HOH A . 
V 10 HOH   947  2347 2245 HOH   HOH A . 
V 10 HOH   948  2348 1308 HOH   HOH A . 
V 10 HOH   949  2349 2023 HOH   HOH A . 
V 10 HOH   950  2350 2000 HOH   HOH A . 
V 10 HOH   951  2351 2406 HOH   HOH A . 
V 10 HOH   952  2352 2197 HOH   HOH A . 
V 10 HOH   953  2353 919  HOH   HOH A . 
V 10 HOH   954  2354 1049 HOH   HOH A . 
V 10 HOH   955  2355 1176 HOH   HOH A . 
V 10 HOH   956  2356 2474 HOH   HOH A . 
V 10 HOH   957  2357 2570 HOH   HOH A . 
V 10 HOH   958  2358 1972 HOH   HOH A . 
V 10 HOH   959  2359 1800 HOH   HOH A . 
V 10 HOH   960  2360 1434 HOH   HOH A . 
V 10 HOH   961  2361 1818 HOH   HOH A . 
V 10 HOH   962  2362 2182 HOH   HOH A . 
V 10 HOH   963  2363 1363 HOH   HOH A . 
V 10 HOH   964  2364 1415 HOH   HOH A . 
V 10 HOH   965  2365 987  HOH   HOH A . 
V 10 HOH   966  2366 2484 HOH   HOH A . 
V 10 HOH   967  2367 1995 HOH   HOH A . 
V 10 HOH   968  2368 2085 HOH   HOH A . 
V 10 HOH   969  2369 728  HOH   HOH A . 
V 10 HOH   970  2370 1990 HOH   HOH A . 
V 10 HOH   971  2371 1650 HOH   HOH A . 
V 10 HOH   972  2372 1408 HOH   HOH A . 
V 10 HOH   973  2373 865  HOH   HOH A . 
V 10 HOH   974  2374 2529 HOH   HOH A . 
V 10 HOH   975  2375 1153 HOH   HOH A . 
V 10 HOH   976  2376 2228 HOH   HOH A . 
V 10 HOH   977  2377 1923 HOH   HOH A . 
V 10 HOH   978  2378 2365 HOH   HOH A . 
V 10 HOH   979  2379 1473 HOH   HOH A . 
V 10 HOH   980  2380 686  HOH   HOH A . 
V 10 HOH   981  2381 2287 HOH   HOH A . 
V 10 HOH   982  2382 2324 HOH   HOH A . 
V 10 HOH   983  2383 2259 HOH   HOH A . 
V 10 HOH   984  2384 1908 HOH   HOH A . 
V 10 HOH   985  2385 1349 HOH   HOH A . 
V 10 HOH   986  2386 2236 HOH   HOH A . 
V 10 HOH   987  2387 2543 HOH   HOH A . 
V 10 HOH   988  2388 2360 HOH   HOH A . 
V 10 HOH   989  2389 2418 HOH   HOH A . 
V 10 HOH   990  2390 2476 HOH   HOH A . 
V 10 HOH   991  2391 2475 HOH   HOH A . 
V 10 HOH   992  2392 953  HOH   HOH A . 
V 10 HOH   993  2393 2175 HOH   HOH A . 
V 10 HOH   994  2394 1400 HOH   HOH A . 
V 10 HOH   995  2395 2577 HOH   HOH A . 
V 10 HOH   996  2396 2271 HOH   HOH A . 
V 10 HOH   997  2397 3    HOH   HOH A . 
V 10 HOH   998  2398 1245 HOH   HOH A . 
V 10 HOH   999  2399 1648 HOH   HOH A . 
V 10 HOH   1000 2400 1843 HOH   HOH A . 
V 10 HOH   1001 2401 1661 HOH   HOH A . 
V 10 HOH   1002 2402 1193 HOH   HOH A . 
V 10 HOH   1003 2403 2040 HOH   HOH A . 
V 10 HOH   1004 2404 1458 HOH   HOH A . 
V 10 HOH   1005 2405 1488 HOH   HOH A . 
V 10 HOH   1006 2406 1573 HOH   HOH A . 
V 10 HOH   1007 2407 2291 HOH   HOH A . 
V 10 HOH   1008 2408 2070 HOH   HOH A . 
V 10 HOH   1009 2409 1630 HOH   HOH A . 
V 10 HOH   1010 2410 1524 HOH   HOH A . 
V 10 HOH   1011 2411 2237 HOH   HOH A . 
V 10 HOH   1012 2412 1385 HOH   HOH A . 
V 10 HOH   1013 2413 943  HOH   HOH A . 
V 10 HOH   1014 2414 1177 HOH   HOH A . 
V 10 HOH   1015 2415 2136 HOH   HOH A . 
V 10 HOH   1016 2416 350  HOH   HOH A . 
V 10 HOH   1017 2417 1884 HOH   HOH A . 
V 10 HOH   1018 2418 2073 HOH   HOH A . 
V 10 HOH   1019 2419 217  HOH   HOH A . 
V 10 HOH   1020 2420 1862 HOH   HOH A . 
V 10 HOH   1021 2421 635  HOH   HOH A . 
V 10 HOH   1022 2422 1567 HOH   HOH A . 
V 10 HOH   1023 2423 1983 HOH   HOH A . 
V 10 HOH   1024 2424 2517 HOH   HOH A . 
V 10 HOH   1025 2425 2264 HOH   HOH A . 
V 10 HOH   1026 2426 1214 HOH   HOH A . 
V 10 HOH   1027 2427 1568 HOH   HOH A . 
V 10 HOH   1028 2428 1928 HOH   HOH A . 
V 10 HOH   1029 2429 1505 HOH   HOH A . 
V 10 HOH   1030 2430 2359 HOH   HOH A . 
V 10 HOH   1031 2431 1031 HOH   HOH A . 
V 10 HOH   1032 2432 1672 HOH   HOH A . 
V 10 HOH   1033 2433 1941 HOH   HOH A . 
V 10 HOH   1034 2434 2142 HOH   HOH A . 
V 10 HOH   1035 2435 1216 HOH   HOH A . 
V 10 HOH   1036 2436 1911 HOH   HOH A . 
V 10 HOH   1037 2437 2433 HOH   HOH A . 
V 10 HOH   1038 2438 1327 HOH   HOH A . 
V 10 HOH   1039 2439 2096 HOH   HOH A . 
V 10 HOH   1040 2440 1329 HOH   HOH A . 
V 10 HOH   1041 2441 2504 HOH   HOH A . 
V 10 HOH   1042 2442 2069 HOH   HOH A . 
V 10 HOH   1043 2443 1892 HOH   HOH A . 
V 10 HOH   1044 2444 1942 HOH   HOH A . 
V 10 HOH   1045 2445 404  HOH   HOH A . 
V 10 HOH   1046 2446 1490 HOH   HOH A . 
V 10 HOH   1047 2447 2472 HOH   HOH A . 
V 10 HOH   1048 2448 2292 HOH   HOH A . 
V 10 HOH   1049 2449 1612 HOH   HOH A . 
V 10 HOH   1050 2450 2374 HOH   HOH A . 
V 10 HOH   1051 2451 2545 HOH   HOH A . 
V 10 HOH   1052 2452 2332 HOH   HOH A . 
V 10 HOH   1053 2453 1981 HOH   HOH A . 
V 10 HOH   1054 2454 2012 HOH   HOH A . 
V 10 HOH   1055 2455 2416 HOH   HOH A . 
V 10 HOH   1056 2456 568  HOH   HOH A . 
V 10 HOH   1057 2457 1384 HOH   HOH A . 
V 10 HOH   1058 2458 2568 HOH   HOH A . 
V 10 HOH   1059 2459 2468 HOH   HOH A . 
V 10 HOH   1060 2460 1076 HOH   HOH A . 
V 10 HOH   1061 2461 1309 HOH   HOH A . 
V 10 HOH   1062 2462 1227 HOH   HOH A . 
V 10 HOH   1063 2463 1826 HOH   HOH A . 
V 10 HOH   1064 2464 2215 HOH   HOH A . 
V 10 HOH   1065 2465 1191 HOH   HOH A . 
V 10 HOH   1066 2466 1471 HOH   HOH A . 
V 10 HOH   1067 2467 1516 HOH   HOH A . 
V 10 HOH   1068 2468 2123 HOH   HOH A . 
V 10 HOH   1069 2469 2409 HOH   HOH A . 
V 10 HOH   1070 2470 2167 HOH   HOH A . 
V 10 HOH   1071 2471 1745 HOH   HOH A . 
V 10 HOH   1072 2472 567  HOH   HOH A . 
V 10 HOH   1073 2473 1989 HOH   HOH A . 
V 10 HOH   1074 2474 1484 HOH   HOH A . 
V 10 HOH   1075 2475 851  HOH   HOH A . 
V 10 HOH   1076 2476 1105 HOH   HOH A . 
V 10 HOH   1077 2477 2220 HOH   HOH A . 
V 10 HOH   1078 2478 2261 HOH   HOH A . 
V 10 HOH   1079 2479 1343 HOH   HOH A . 
V 10 HOH   1080 2480 1513 HOH   HOH A . 
V 10 HOH   1081 2481 2412 HOH   HOH A . 
V 10 HOH   1082 2482 361  HOH   HOH A . 
V 10 HOH   1083 2483 1320 HOH   HOH A . 
V 10 HOH   1084 2484 935  HOH   HOH A . 
V 10 HOH   1085 2485 2552 HOH   HOH A . 
V 10 HOH   1086 2486 1782 HOH   HOH A . 
V 10 HOH   1087 2487 1396 HOH   HOH A . 
V 10 HOH   1088 2488 2457 HOH   HOH A . 
V 10 HOH   1089 2489 1425 HOH   HOH A . 
V 10 HOH   1090 2490 2241 HOH   HOH A . 
V 10 HOH   1091 2491 1456 HOH   HOH A . 
V 10 HOH   1092 2492 1155 HOH   HOH A . 
V 10 HOH   1093 2493 1058 HOH   HOH A . 
V 10 HOH   1094 2494 1777 HOH   HOH A . 
V 10 HOH   1095 2495 2078 HOH   HOH A . 
V 10 HOH   1096 2496 1692 HOH   HOH A . 
V 10 HOH   1097 2497 1966 HOH   HOH A . 
V 10 HOH   1098 2498 2211 HOH   HOH A . 
V 10 HOH   1099 2499 1922 HOH   HOH A . 
V 10 HOH   1100 2500 2375 HOH   HOH A . 
V 10 HOH   1101 2501 1865 HOH   HOH A . 
V 10 HOH   1102 2502 1899 HOH   HOH A . 
V 10 HOH   1103 2503 1078 HOH   HOH A . 
V 10 HOH   1104 2504 1301 HOH   HOH A . 
V 10 HOH   1105 2505 1613 HOH   HOH A . 
V 10 HOH   1106 2506 1948 HOH   HOH A . 
V 10 HOH   1107 2507 1780 HOH   HOH A . 
V 10 HOH   1108 2508 1890 HOH   HOH A . 
V 10 HOH   1109 2509 2498 HOH   HOH A . 
V 10 HOH   1110 2510 2515 HOH   HOH A . 
V 10 HOH   1111 2511 1443 HOH   HOH A . 
V 10 HOH   1112 2512 2480 HOH   HOH A . 
V 10 HOH   1113 2513 1175 HOH   HOH A . 
V 10 HOH   1114 2514 2214 HOH   HOH A . 
V 10 HOH   1115 2515 1215 HOH   HOH A . 
V 10 HOH   1116 2516 1701 HOH   HOH A . 
V 10 HOH   1117 2517 1090 HOH   HOH A . 
V 10 HOH   1118 2518 616  HOH   HOH A . 
V 10 HOH   1119 2519 1372 HOH   HOH A . 
V 10 HOH   1120 2520 1231 HOH   HOH A . 
V 10 HOH   1121 2521 1929 HOH   HOH A . 
V 10 HOH   1122 2522 1504 HOH   HOH A . 
V 10 HOH   1123 2523 2065 HOH   HOH A . 
V 10 HOH   1124 2524 1618 HOH   HOH A . 
V 10 HOH   1125 2525 1392 HOH   HOH A . 
V 10 HOH   1126 2526 2571 HOH   HOH A . 
V 10 HOH   1127 2527 2093 HOH   HOH A . 
V 10 HOH   1128 2528 1059 HOH   HOH A . 
V 10 HOH   1129 2529 668  HOH   HOH A . 
V 10 HOH   1130 2530 1080 HOH   HOH A . 
V 10 HOH   1131 2531 2371 HOH   HOH A . 
V 10 HOH   1132 2532 1118 HOH   HOH A . 
V 10 HOH   1133 2533 1975 HOH   HOH A . 
V 10 HOH   1134 2534 1969 HOH   HOH A . 
V 10 HOH   1135 2535 521  HOH   HOH A . 
V 10 HOH   1136 2536 1716 HOH   HOH A . 
V 10 HOH   1137 2537 1737 HOH   HOH A . 
V 10 HOH   1138 2538 2100 HOH   HOH A . 
V 10 HOH   1139 2539 2589 HOH   HOH A . 
V 10 HOH   1140 2540 2528 HOH   HOH A . 
V 10 HOH   1141 2541 2307 HOH   HOH A . 
V 10 HOH   1142 2542 2265 HOH   HOH A . 
V 10 HOH   1143 2543 1260 HOH   HOH A . 
V 10 HOH   1144 2544 1813 HOH   HOH A . 
V 10 HOH   1145 2545 2337 HOH   HOH A . 
V 10 HOH   1146 2546 2190 HOH   HOH A . 
V 10 HOH   1147 2547 1611 HOH   HOH A . 
V 10 HOH   1148 2548 1535 HOH   HOH A . 
V 10 HOH   1149 2549 2522 HOH   HOH A . 
V 10 HOH   1150 2550 2427 HOH   HOH A . 
V 10 HOH   1151 2551 2217 HOH   HOH A . 
V 10 HOH   1152 2552 1798 HOH   HOH A . 
V 10 HOH   1153 2553 1980 HOH   HOH A . 
V 10 HOH   1154 2554 2125 HOH   HOH A . 
V 10 HOH   1155 2555 2579 HOH   HOH A . 
V 10 HOH   1156 2556 2296 HOH   HOH A . 
V 10 HOH   1157 2557 1754 HOH   HOH A . 
V 10 HOH   1158 2558 1481 HOH   HOH A . 
V 10 HOH   1159 2559 2269 HOH   HOH A . 
V 10 HOH   1160 2560 2387 HOH   HOH A . 
V 10 HOH   1161 2561 1124 HOH   HOH A . 
V 10 HOH   1162 2562 2530 HOH   HOH A . 
V 10 HOH   1163 2563 1918 HOH   HOH A . 
V 10 HOH   1164 2564 2563 HOH   HOH A . 
V 10 HOH   1165 2565 2171 HOH   HOH A . 
V 10 HOH   1166 2566 1070 HOH   HOH A . 
V 10 HOH   1167 2567 1764 HOH   HOH A . 
V 10 HOH   1168 2568 1534 HOH   HOH A . 
V 10 HOH   1169 2569 2058 HOH   HOH A . 
V 10 HOH   1170 2570 2585 HOH   HOH A . 
V 10 HOH   1171 2571 727  HOH   HOH A . 
V 10 HOH   1172 2572 1454 HOH   HOH A . 
V 10 HOH   1173 2573 820  HOH   HOH A . 
V 10 HOH   1174 2574 1298 HOH   HOH A . 
V 10 HOH   1175 2575 1614 HOH   HOH A . 
V 10 HOH   1176 2576 1024 HOH   HOH A . 
V 10 HOH   1177 2577 2496 HOH   HOH A . 
V 10 HOH   1178 2578 1734 HOH   HOH A . 
V 10 HOH   1179 2579 2099 HOH   HOH A . 
V 10 HOH   1180 2580 1889 HOH   HOH A . 
V 10 HOH   1181 2581 362  HOH   HOH A . 
V 10 HOH   1182 2582 1328 HOH   HOH A . 
V 10 HOH   1183 2583 2042 HOH   HOH A . 
V 10 HOH   1184 2584 1426 HOH   HOH A . 
V 10 HOH   1185 2585 1149 HOH   HOH A . 
V 10 HOH   1186 2586 1205 HOH   HOH A . 
V 10 HOH   1187 2587 1190 HOH   HOH A . 
V 10 HOH   1188 2588 1914 HOH   HOH A . 
V 10 HOH   1189 2589 1963 HOH   HOH A . 
V 10 HOH   1190 2590 2280 HOH   HOH A . 
V 10 HOH   1191 2591 1383 HOH   HOH A . 
V 10 HOH   1192 2592 1423 HOH   HOH A . 
V 10 HOH   1193 2593 2097 HOH   HOH A . 
V 10 HOH   1194 2594 2022 HOH   HOH A . 
V 10 HOH   1195 2595 2270 HOH   HOH A . 
V 10 HOH   1196 2596 1830 HOH   HOH A . 
V 10 HOH   1197 2597 2356 HOH   HOH A . 
V 10 HOH   1198 2598 1600 HOH   HOH A . 
V 10 HOH   1199 2599 2032 HOH   HOH A . 
V 10 HOH   1200 2600 2031 HOH   HOH A . 
V 10 HOH   1201 2601 1873 HOH   HOH A . 
V 10 HOH   1202 2602 1542 HOH   HOH A . 
V 10 HOH   1203 2603 1921 HOH   HOH A . 
V 10 HOH   1204 2604 1859 HOH   HOH A . 
V 10 HOH   1205 2605 1602 HOH   HOH A . 
V 10 HOH   1206 2606 1750 HOH   HOH A . 
V 10 HOH   1207 2607 2502 HOH   HOH A . 
V 10 HOH   1208 2608 2009 HOH   HOH A . 
V 10 HOH   1209 2609 1718 HOH   HOH A . 
V 10 HOH   1210 2610 1546 HOH   HOH A . 
V 10 HOH   1211 2611 1943 HOH   HOH A . 
V 10 HOH   1212 2612 1107 HOH   HOH A . 
V 10 HOH   1213 2613 2095 HOH   HOH A . 
V 10 HOH   1214 2614 1871 HOH   HOH A . 
V 10 HOH   1215 2615 1299 HOH   HOH A . 
V 10 HOH   1216 2616 1617 HOH   HOH A . 
V 10 HOH   1217 2617 1868 HOH   HOH A . 
V 10 HOH   1218 2618 2425 HOH   HOH A . 
V 10 HOH   1219 2619 1706 HOH   HOH A . 
V 10 HOH   1220 2620 1968 HOH   HOH A . 
V 10 HOH   1221 2621 2168 HOH   HOH A . 
V 10 HOH   1222 2622 1577 HOH   HOH A . 
V 10 HOH   1223 2623 1178 HOH   HOH A . 
V 10 HOH   1224 2624 1849 HOH   HOH A . 
V 10 HOH   1225 2625 2048 HOH   HOH A . 
V 10 HOH   1226 2626 2013 HOH   HOH A . 
V 10 HOH   1227 2627 1949 HOH   HOH A . 
V 10 HOH   1228 2628 2546 HOH   HOH A . 
V 10 HOH   1229 2629 2169 HOH   HOH A . 
V 10 HOH   1230 2630 2090 HOH   HOH A . 
V 10 HOH   1231 2631 1046 HOH   HOH A . 
V 10 HOH   1232 2632 2124 HOH   HOH A . 
V 10 HOH   1233 2633 1342 HOH   HOH A . 
V 10 HOH   1234 2634 1856 HOH   HOH A . 
W 10 HOH   1    1401 2114 HOH   HOH B . 
W 10 HOH   2    1402 2107 HOH   HOH B . 
W 10 HOH   3    1403 1633 HOH   HOH B . 
W 10 HOH   4    1404 708  HOH   HOH B . 
W 10 HOH   5    1405 2505 HOH   HOH B . 
W 10 HOH   6    1406 1712 HOH   HOH B . 
W 10 HOH   7    1407 2304 HOH   HOH B . 
W 10 HOH   8    1408 1528 HOH   HOH B . 
W 10 HOH   9    1409 2380 HOH   HOH B . 
W 10 HOH   10   1410 2233 HOH   HOH B . 
W 10 HOH   11   1411 1041 HOH   HOH B . 
W 10 HOH   12   1412 1162 HOH   HOH B . 
W 10 HOH   13   1413 1834 HOH   HOH B . 
W 10 HOH   14   1414 815  HOH   HOH B . 
W 10 HOH   15   1415 1872 HOH   HOH B . 
W 10 HOH   16   1416 2370 HOH   HOH B . 
W 10 HOH   17   1417 1480 HOH   HOH B . 
W 10 HOH   18   1418 1867 HOH   HOH B . 
W 10 HOH   19   1419 674  HOH   HOH B . 
W 10 HOH   20   1420 837  HOH   HOH B . 
W 10 HOH   21   1421 1729 HOH   HOH B . 
W 10 HOH   22   1422 2253 HOH   HOH B . 
W 10 HOH   23   1423 1068 HOH   HOH B . 
W 10 HOH   24   1424 2558 HOH   HOH B . 
W 10 HOH   25   1425 1707 HOH   HOH B . 
W 10 HOH   26   1426 892  HOH   HOH B . 
W 10 HOH   27   1427 694  HOH   HOH B . 
W 10 HOH   28   1428 543  HOH   HOH B . 
W 10 HOH   29   1429 663  HOH   HOH B . 
W 10 HOH   30   1430 1521 HOH   HOH B . 
W 10 HOH   31   1431 650  HOH   HOH B . 
W 10 HOH   32   1432 2310 HOH   HOH B . 
W 10 HOH   33   1433 1758 HOH   HOH B . 
W 10 HOH   34   1434 1271 HOH   HOH B . 
W 10 HOH   35   1435 94   HOH   HOH B . 
W 10 HOH   36   1436 1397 HOH   HOH B . 
W 10 HOH   37   1437 1690 HOH   HOH B . 
W 10 HOH   38   1438 1663 HOH   HOH B . 
W 10 HOH   39   1439 1858 HOH   HOH B . 
W 10 HOH   40   1440 325  HOH   HOH B . 
W 10 HOH   41   1441 1816 HOH   HOH B . 
W 10 HOH   42   1442 2395 HOH   HOH B . 
W 10 HOH   43   1443 1004 HOH   HOH B . 
W 10 HOH   44   1444 1394 HOH   HOH B . 
W 10 HOH   45   1445 735  HOH   HOH B . 
W 10 HOH   46   1446 431  HOH   HOH B . 
W 10 HOH   47   1447 1001 HOH   HOH B . 
W 10 HOH   48   1448 1596 HOH   HOH B . 
W 10 HOH   49   1449 1793 HOH   HOH B . 
W 10 HOH   50   1450 2111 HOH   HOH B . 
W 10 HOH   51   1451 296  HOH   HOH B . 
W 10 HOH   52   1452 1359 HOH   HOH B . 
W 10 HOH   53   1453 1748 HOH   HOH B . 
W 10 HOH   54   1454 895  HOH   HOH B . 
W 10 HOH   55   1455 1170 HOH   HOH B . 
W 10 HOH   56   1456 677  HOH   HOH B . 
W 10 HOH   57   1457 954  HOH   HOH B . 
W 10 HOH   58   1458 1147 HOH   HOH B . 
W 10 HOH   59   1459 119  HOH   HOH B . 
W 10 HOH   60   1460 1580 HOH   HOH B . 
W 10 HOH   61   1461 301  HOH   HOH B . 
W 10 HOH   62   1462 2297 HOH   HOH B . 
W 10 HOH   63   1463 235  HOH   HOH B . 
W 10 HOH   64   1464 624  HOH   HOH B . 
W 10 HOH   65   1465 1146 HOH   HOH B . 
W 10 HOH   66   1466 2208 HOH   HOH B . 
W 10 HOH   67   1467 530  HOH   HOH B . 
W 10 HOH   68   1468 81   HOH   HOH B . 
W 10 HOH   69   1469 562  HOH   HOH B . 
W 10 HOH   70   1470 1863 HOH   HOH B . 
W 10 HOH   71   1471 1230 HOH   HOH B . 
W 10 HOH   72   1472 1126 HOH   HOH B . 
W 10 HOH   73   1473 1785 HOH   HOH B . 
W 10 HOH   74   1474 1906 HOH   HOH B . 
W 10 HOH   75   1475 1727 HOH   HOH B . 
W 10 HOH   76   1476 2414 HOH   HOH B . 
W 10 HOH   77   1477 1173 HOH   HOH B . 
W 10 HOH   78   1478 621  HOH   HOH B . 
W 10 HOH   79   1479 1649 HOH   HOH B . 
W 10 HOH   80   1480 295  HOH   HOH B . 
W 10 HOH   81   1481 1207 HOH   HOH B . 
W 10 HOH   82   1482 1510 HOH   HOH B . 
W 10 HOH   83   1483 493  HOH   HOH B . 
W 10 HOH   84   1484 1129 HOH   HOH B . 
W 10 HOH   85   1485 1092 HOH   HOH B . 
W 10 HOH   86   1486 441  HOH   HOH B . 
W 10 HOH   87   1487 55   HOH   HOH B . 
W 10 HOH   88   1488 2501 HOH   HOH B . 
W 10 HOH   89   1489 1726 HOH   HOH B . 
W 10 HOH   90   1490 367  HOH   HOH B . 
W 10 HOH   91   1491 2510 HOH   HOH B . 
W 10 HOH   92   1492 89   HOH   HOH B . 
W 10 HOH   93   1493 355  HOH   HOH B . 
W 10 HOH   94   1494 24   HOH   HOH B . 
W 10 HOH   95   1495 795  HOH   HOH B . 
W 10 HOH   96   1496 825  HOH   HOH B . 
W 10 HOH   97   1497 212  HOH   HOH B . 
W 10 HOH   98   1498 1325 HOH   HOH B . 
W 10 HOH   99   1499 1099 HOH   HOH B . 
W 10 HOH   100  1500 234  HOH   HOH B . 
W 10 HOH   101  1501 1962 HOH   HOH B . 
W 10 HOH   102  1502 328  HOH   HOH B . 
W 10 HOH   103  1503 2275 HOH   HOH B . 
W 10 HOH   104  1504 274  HOH   HOH B . 
W 10 HOH   105  1505 1410 HOH   HOH B . 
W 10 HOH   106  1506 1476 HOH   HOH B . 
W 10 HOH   107  1507 1569 HOH   HOH B . 
W 10 HOH   108  1508 1011 HOH   HOH B . 
W 10 HOH   109  1509 2026 HOH   HOH B . 
W 10 HOH   110  1510 40   HOH   HOH B . 
W 10 HOH   111  1511 1326 HOH   HOH B . 
W 10 HOH   112  1512 1253 HOH   HOH B . 
W 10 HOH   113  1513 30   HOH   HOH B . 
W 10 HOH   114  1514 1334 HOH   HOH B . 
W 10 HOH   115  1515 125  HOH   HOH B . 
W 10 HOH   116  1516 1300 HOH   HOH B . 
W 10 HOH   117  1517 438  HOH   HOH B . 
W 10 HOH   118  1518 1694 HOH   HOH B . 
W 10 HOH   119  1519 64   HOH   HOH B . 
W 10 HOH   120  1520 324  HOH   HOH B . 
W 10 HOH   121  1521 696  HOH   HOH B . 
W 10 HOH   122  1522 963  HOH   HOH B . 
W 10 HOH   123  1523 749  HOH   HOH B . 
W 10 HOH   124  1524 1643 HOH   HOH B . 
W 10 HOH   125  1525 1802 HOH   HOH B . 
W 10 HOH   126  1526 547  HOH   HOH B . 
W 10 HOH   127  1527 955  HOH   HOH B . 
W 10 HOH   128  1528 2424 HOH   HOH B . 
W 10 HOH   129  1529 888  HOH   HOH B . 
W 10 HOH   130  1530 322  HOH   HOH B . 
W 10 HOH   131  1531 2240 HOH   HOH B . 
W 10 HOH   132  1532 277  HOH   HOH B . 
W 10 HOH   133  1533 1221 HOH   HOH B . 
W 10 HOH   134  1534 2463 HOH   HOH B . 
W 10 HOH   135  1535 379  HOH   HOH B . 
W 10 HOH   136  1536 241  HOH   HOH B . 
W 10 HOH   137  1537 1936 HOH   HOH B . 
W 10 HOH   138  1538 221  HOH   HOH B . 
W 10 HOH   139  1539 2203 HOH   HOH B . 
W 10 HOH   140  1540 1386 HOH   HOH B . 
W 10 HOH   141  1541 526  HOH   HOH B . 
W 10 HOH   142  1542 416  HOH   HOH B . 
W 10 HOH   143  1543 599  HOH   HOH B . 
W 10 HOH   144  1544 2494 HOH   HOH B . 
W 10 HOH   145  1545 278  HOH   HOH B . 
W 10 HOH   146  1546 16   HOH   HOH B . 
W 10 HOH   147  1547 303  HOH   HOH B . 
W 10 HOH   148  1548 2355 HOH   HOH B . 
W 10 HOH   149  1549 1478 HOH   HOH B . 
W 10 HOH   150  1550 806  HOH   HOH B . 
W 10 HOH   151  1551 1181 HOH   HOH B . 
W 10 HOH   152  1552 1183 HOH   HOH B . 
W 10 HOH   153  1553 340  HOH   HOH B . 
W 10 HOH   154  1554 99   HOH   HOH B . 
W 10 HOH   155  1555 1733 HOH   HOH B . 
W 10 HOH   156  1556 406  HOH   HOH B . 
W 10 HOH   157  1557 1740 HOH   HOH B . 
W 10 HOH   158  1558 759  HOH   HOH B . 
W 10 HOH   159  1559 715  HOH   HOH B . 
W 10 HOH   160  1560 179  HOH   HOH B . 
W 10 HOH   161  1561 175  HOH   HOH B . 
W 10 HOH   162  1562 1279 HOH   HOH B . 
W 10 HOH   163  1563 828  HOH   HOH B . 
W 10 HOH   164  1564 2126 HOH   HOH B . 
W 10 HOH   165  1565 445  HOH   HOH B . 
W 10 HOH   166  1566 1114 HOH   HOH B . 
W 10 HOH   167  1567 667  HOH   HOH B . 
W 10 HOH   168  1568 1825 HOH   HOH B . 
W 10 HOH   169  1569 2486 HOH   HOH B . 
W 10 HOH   170  1570 467  HOH   HOH B . 
W 10 HOH   171  1571 751  HOH   HOH B . 
W 10 HOH   172  1572 2139 HOH   HOH B . 
W 10 HOH   173  1573 421  HOH   HOH B . 
W 10 HOH   174  1574 1468 HOH   HOH B . 
W 10 HOH   175  1575 51   HOH   HOH B . 
W 10 HOH   176  1576 983  HOH   HOH B . 
W 10 HOH   177  1577 2534 HOH   HOH B . 
W 10 HOH   178  1578 1757 HOH   HOH B . 
W 10 HOH   179  1579 932  HOH   HOH B . 
W 10 HOH   180  1580 758  HOH   HOH B . 
W 10 HOH   181  1581 7    HOH   HOH B . 
W 10 HOH   182  1582 307  HOH   HOH B . 
W 10 HOH   183  1583 311  HOH   HOH B . 
W 10 HOH   184  1584 146  HOH   HOH B . 
W 10 HOH   185  1585 801  HOH   HOH B . 
W 10 HOH   186  1586 631  HOH   HOH B . 
W 10 HOH   187  1587 38   HOH   HOH B . 
W 10 HOH   188  1588 1601 HOH   HOH B . 
W 10 HOH   189  1589 546  HOH   HOH B . 
W 10 HOH   190  1590 1212 HOH   HOH B . 
W 10 HOH   191  1591 1198 HOH   HOH B . 
W 10 HOH   192  1592 192  HOH   HOH B . 
W 10 HOH   193  1593 1581 HOH   HOH B . 
W 10 HOH   194  1594 2077 HOH   HOH B . 
W 10 HOH   195  1595 95   HOH   HOH B . 
W 10 HOH   196  1596 185  HOH   HOH B . 
W 10 HOH   197  1597 1866 HOH   HOH B . 
W 10 HOH   198  1598 1009 HOH   HOH B . 
W 10 HOH   199  1599 1603 HOH   HOH B . 
W 10 HOH   200  1600 103  HOH   HOH B . 
W 10 HOH   201  1601 2154 HOH   HOH B . 
W 10 HOH   202  1602 1144 HOH   HOH B . 
W 10 HOH   203  1603 579  HOH   HOH B . 
W 10 HOH   204  1604 1925 HOH   HOH B . 
W 10 HOH   205  1605 352  HOH   HOH B . 
W 10 HOH   206  1606 1917 HOH   HOH B . 
W 10 HOH   207  1607 1691 HOH   HOH B . 
W 10 HOH   208  1608 2461 HOH   HOH B . 
W 10 HOH   209  1609 63   HOH   HOH B . 
W 10 HOH   210  1610 2509 HOH   HOH B . 
W 10 HOH   211  1611 59   HOH   HOH B . 
W 10 HOH   212  1612 2021 HOH   HOH B . 
W 10 HOH   213  1613 335  HOH   HOH B . 
W 10 HOH   214  1614 141  HOH   HOH B . 
W 10 HOH   215  1615 1398 HOH   HOH B . 
W 10 HOH   216  1616 1330 HOH   HOH B . 
W 10 HOH   217  1617 587  HOH   HOH B . 
W 10 HOH   218  1618 283  HOH   HOH B . 
W 10 HOH   219  1619 1695 HOH   HOH B . 
W 10 HOH   220  1620 2596 HOH   HOH B . 
W 10 HOH   221  1621 747  HOH   HOH B . 
W 10 HOH   222  1622 629  HOH   HOH B . 
W 10 HOH   223  1623 2316 HOH   HOH B . 
W 10 HOH   224  1624 877  HOH   HOH B . 
W 10 HOH   225  1625 1608 HOH   HOH B . 
W 10 HOH   226  1626 1135 HOH   HOH B . 
W 10 HOH   227  1627 2232 HOH   HOH B . 
W 10 HOH   228  1628 1582 HOH   HOH B . 
W 10 HOH   229  1629 161  HOH   HOH B . 
W 10 HOH   230  1630 1195 HOH   HOH B . 
W 10 HOH   231  1631 1043 HOH   HOH B . 
W 10 HOH   232  1632 1964 HOH   HOH B . 
W 10 HOH   233  1633 2329 HOH   HOH B . 
W 10 HOH   234  1634 433  HOH   HOH B . 
W 10 HOH   235  1635 576  HOH   HOH B . 
W 10 HOH   236  1636 711  HOH   HOH B . 
W 10 HOH   237  1637 447  HOH   HOH B . 
W 10 HOH   238  1638 682  HOH   HOH B . 
W 10 HOH   239  1639 695  HOH   HOH B . 
W 10 HOH   240  1640 2075 HOH   HOH B . 
W 10 HOH   241  1641 248  HOH   HOH B . 
W 10 HOH   242  1642 559  HOH   HOH B . 
W 10 HOH   243  1643 264  HOH   HOH B . 
W 10 HOH   244  1644 1302 HOH   HOH B . 
W 10 HOH   245  1645 1180 HOH   HOH B . 
W 10 HOH   246  1646 411  HOH   HOH B . 
W 10 HOH   247  1647 2593 HOH   HOH B . 
W 10 HOH   248  1648 28   HOH   HOH B . 
W 10 HOH   249  1649 184  HOH   HOH B . 
W 10 HOH   250  1650 222  HOH   HOH B . 
W 10 HOH   251  1651 1246 HOH   HOH B . 
W 10 HOH   252  1652 150  HOH   HOH B . 
W 10 HOH   253  1653 393  HOH   HOH B . 
W 10 HOH   254  1654 229  HOH   HOH B . 
W 10 HOH   255  1655 1087 HOH   HOH B . 
W 10 HOH   256  1656 463  HOH   HOH B . 
W 10 HOH   257  1657 1249 HOH   HOH B . 
W 10 HOH   258  1658 327  HOH   HOH B . 
W 10 HOH   259  1659 1344 HOH   HOH B . 
W 10 HOH   260  1660 65   HOH   HOH B . 
W 10 HOH   261  1661 538  HOH   HOH B . 
W 10 HOH   262  1662 1100 HOH   HOH B . 
W 10 HOH   263  1663 1887 HOH   HOH B . 
W 10 HOH   264  1664 288  HOH   HOH B . 
W 10 HOH   265  1665 996  HOH   HOH B . 
W 10 HOH   266  1666 2005 HOH   HOH B . 
W 10 HOH   267  1667 291  HOH   HOH B . 
W 10 HOH   268  1668 979  HOH   HOH B . 
W 10 HOH   269  1669 655  HOH   HOH B . 
W 10 HOH   270  1670 49   HOH   HOH B . 
W 10 HOH   271  1671 1860 HOH   HOH B . 
W 10 HOH   272  1672 206  HOH   HOH B . 
W 10 HOH   273  1673 337  HOH   HOH B . 
W 10 HOH   274  1674 2305 HOH   HOH B . 
W 10 HOH   275  1675 202  HOH   HOH B . 
W 10 HOH   276  1676 1770 HOH   HOH B . 
W 10 HOH   277  1677 149  HOH   HOH B . 
W 10 HOH   278  1678 640  HOH   HOH B . 
W 10 HOH   279  1679 154  HOH   HOH B . 
W 10 HOH   280  1680 883  HOH   HOH B . 
W 10 HOH   281  1681 42   HOH   HOH B . 
W 10 HOH   282  1682 840  HOH   HOH B . 
W 10 HOH   283  1683 838  HOH   HOH B . 
W 10 HOH   284  1684 139  HOH   HOH B . 
W 10 HOH   285  1685 730  HOH   HOH B . 
W 10 HOH   286  1686 1310 HOH   HOH B . 
W 10 HOH   287  1687 1951 HOH   HOH B . 
W 10 HOH   288  1688 1894 HOH   HOH B . 
W 10 HOH   289  1689 409  HOH   HOH B . 
W 10 HOH   290  1690 79   HOH   HOH B . 
W 10 HOH   291  1691 2196 HOH   HOH B . 
W 10 HOH   292  1692 569  HOH   HOH B . 
W 10 HOH   293  1693 354  HOH   HOH B . 
W 10 HOH   294  1694 2417 HOH   HOH B . 
W 10 HOH   295  1695 775  HOH   HOH B . 
W 10 HOH   296  1696 1395 HOH   HOH B . 
W 10 HOH   297  1697 218  HOH   HOH B . 
W 10 HOH   298  1698 1185 HOH   HOH B . 
W 10 HOH   299  1699 2121 HOH   HOH B . 
W 10 HOH   300  1700 1625 HOH   HOH B . 
W 10 HOH   301  1701 869  HOH   HOH B . 
W 10 HOH   302  1702 78   HOH   HOH B . 
W 10 HOH   303  1703 2327 HOH   HOH B . 
W 10 HOH   304  1704 964  HOH   HOH B . 
W 10 HOH   305  1705 803  HOH   HOH B . 
W 10 HOH   306  1706 22   HOH   HOH B . 
W 10 HOH   307  1707 777  HOH   HOH B . 
W 10 HOH   308  1708 1012 HOH   HOH B . 
W 10 HOH   309  1709 485  HOH   HOH B . 
W 10 HOH   310  1710 133  HOH   HOH B . 
W 10 HOH   311  1711 1529 HOH   HOH B . 
W 10 HOH   312  1712 21   HOH   HOH B . 
W 10 HOH   313  1713 1367 HOH   HOH B . 
W 10 HOH   314  1714 1023 HOH   HOH B . 
W 10 HOH   315  1715 1699 HOH   HOH B . 
W 10 HOH   316  1716 1374 HOH   HOH B . 
W 10 HOH   317  1717 96   HOH   HOH B . 
W 10 HOH   318  1718 2218 HOH   HOH B . 
W 10 HOH   319  1719 2445 HOH   HOH B . 
W 10 HOH   320  1720 691  HOH   HOH B . 
W 10 HOH   321  1721 654  HOH   HOH B . 
W 10 HOH   322  1722 529  HOH   HOH B . 
W 10 HOH   323  1723 609  HOH   HOH B . 
W 10 HOH   324  1724 12   HOH   HOH B . 
W 10 HOH   325  1725 1128 HOH   HOH B . 
W 10 HOH   326  1726 1662 HOH   HOH B . 
W 10 HOH   327  1727 1669 HOH   HOH B . 
W 10 HOH   328  1728 309  HOH   HOH B . 
W 10 HOH   329  1729 1530 HOH   HOH B . 
W 10 HOH   330  1730 2041 HOH   HOH B . 
W 10 HOH   331  1731 808  HOH   HOH B . 
W 10 HOH   332  1732 410  HOH   HOH B . 
W 10 HOH   333  1733 132  HOH   HOH B . 
W 10 HOH   334  1734 601  HOH   HOH B . 
W 10 HOH   335  1735 1768 HOH   HOH B . 
W 10 HOH   336  1736 1934 HOH   HOH B . 
W 10 HOH   337  1737 372  HOH   HOH B . 
W 10 HOH   338  1738 39   HOH   HOH B . 
W 10 HOH   339  1739 2295 HOH   HOH B . 
W 10 HOH   340  1740 392  HOH   HOH B . 
W 10 HOH   341  1741 2335 HOH   HOH B . 
W 10 HOH   342  1742 14   HOH   HOH B . 
W 10 HOH   343  1743 1631 HOH   HOH B . 
W 10 HOH   344  1744 19   HOH   HOH B . 
W 10 HOH   345  1745 321  HOH   HOH B . 
W 10 HOH   346  1746 2157 HOH   HOH B . 
W 10 HOH   347  1747 920  HOH   HOH B . 
W 10 HOH   348  1748 151  HOH   HOH B . 
W 10 HOH   349  1749 1976 HOH   HOH B . 
W 10 HOH   350  1750 732  HOH   HOH B . 
W 10 HOH   351  1751 339  HOH   HOH B . 
W 10 HOH   352  1752 383  HOH   HOH B . 
W 10 HOH   353  1753 397  HOH   HOH B . 
W 10 HOH   354  1754 2044 HOH   HOH B . 
W 10 HOH   355  1755 1268 HOH   HOH B . 
W 10 HOH   356  1756 1847 HOH   HOH B . 
W 10 HOH   357  1757 482  HOH   HOH B . 
W 10 HOH   358  1758 1888 HOH   HOH B . 
W 10 HOH   359  1759 358  HOH   HOH B . 
W 10 HOH   360  1760 1937 HOH   HOH B . 
W 10 HOH   361  1761 1467 HOH   HOH B . 
W 10 HOH   362  1762 678  HOH   HOH B . 
W 10 HOH   363  1763 46   HOH   HOH B . 
W 10 HOH   364  1764 926  HOH   HOH B . 
W 10 HOH   365  1765 1366 HOH   HOH B . 
W 10 HOH   366  1766 934  HOH   HOH B . 
W 10 HOH   367  1767 564  HOH   HOH B . 
W 10 HOH   368  1768 369  HOH   HOH B . 
W 10 HOH   369  1769 157  HOH   HOH B . 
W 10 HOH   370  1770 1986 HOH   HOH B . 
W 10 HOH   371  1771 290  HOH   HOH B . 
W 10 HOH   372  1772 2430 HOH   HOH B . 
W 10 HOH   373  1773 147  HOH   HOH B . 
W 10 HOH   374  1774 117  HOH   HOH B . 
W 10 HOH   375  1775 313  HOH   HOH B . 
W 10 HOH   376  1776 1241 HOH   HOH B . 
W 10 HOH   377  1777 928  HOH   HOH B . 
W 10 HOH   378  1778 2229 HOH   HOH B . 
W 10 HOH   379  1779 1905 HOH   HOH B . 
W 10 HOH   380  1780 484  HOH   HOH B . 
W 10 HOH   381  1781 143  HOH   HOH B . 
W 10 HOH   382  1782 975  HOH   HOH B . 
W 10 HOH   383  1783 53   HOH   HOH B . 
W 10 HOH   384  1784 1350 HOH   HOH B . 
W 10 HOH   385  1785 641  HOH   HOH B . 
W 10 HOH   386  1786 66   HOH   HOH B . 
W 10 HOH   387  1787 841  HOH   HOH B . 
W 10 HOH   388  1788 2331 HOH   HOH B . 
W 10 HOH   389  1789 1281 HOH   HOH B . 
W 10 HOH   390  1790 903  HOH   HOH B . 
W 10 HOH   391  1791 986  HOH   HOH B . 
W 10 HOH   392  1792 891  HOH   HOH B . 
W 10 HOH   393  1793 44   HOH   HOH B . 
W 10 HOH   394  1794 2076 HOH   HOH B . 
W 10 HOH   395  1795 864  HOH   HOH B . 
W 10 HOH   396  1796 452  HOH   HOH B . 
W 10 HOH   397  1797 681  HOH   HOH B . 
W 10 HOH   398  1798 712  HOH   HOH B . 
W 10 HOH   399  1799 917  HOH   HOH B . 
W 10 HOH   400  1800 401  HOH   HOH B . 
W 10 HOH   401  1801 158  HOH   HOH B . 
W 10 HOH   402  1802 104  HOH   HOH B . 
W 10 HOH   403  1803 2352 HOH   HOH B . 
W 10 HOH   404  1804 471  HOH   HOH B . 
W 10 HOH   405  1805 470  HOH   HOH B . 
W 10 HOH   406  1806 978  HOH   HOH B . 
W 10 HOH   407  1807 287  HOH   HOH B . 
W 10 HOH   408  1808 1904 HOH   HOH B . 
W 10 HOH   409  1809 1056 HOH   HOH B . 
W 10 HOH   410  1810 1656 HOH   HOH B . 
W 10 HOH   411  1811 70   HOH   HOH B . 
W 10 HOH   412  1812 1288 HOH   HOH B . 
W 10 HOH   413  1813 250  HOH   HOH B . 
W 10 HOH   414  1814 843  HOH   HOH B . 
W 10 HOH   415  1815 270  HOH   HOH B . 
W 10 HOH   416  1816 333  HOH   HOH B . 
W 10 HOH   417  1817 2299 HOH   HOH B . 
W 10 HOH   418  1818 336  HOH   HOH B . 
W 10 HOH   419  1819 196  HOH   HOH B . 
W 10 HOH   420  1820 405  HOH   HOH B . 
W 10 HOH   421  1821 18   HOH   HOH B . 
W 10 HOH   422  1822 148  HOH   HOH B . 
W 10 HOH   423  1823 904  HOH   HOH B . 
W 10 HOH   424  1824 60   HOH   HOH B . 
W 10 HOH   425  1825 2408 HOH   HOH B . 
W 10 HOH   426  1826 136  HOH   HOH B . 
W 10 HOH   427  1827 901  HOH   HOH B . 
W 10 HOH   428  1828 661  HOH   HOH B . 
W 10 HOH   429  1829 2289 HOH   HOH B . 
W 10 HOH   430  1830 419  HOH   HOH B . 
W 10 HOH   431  1831 824  HOH   HOH B . 
W 10 HOH   432  1832 163  HOH   HOH B . 
W 10 HOH   433  1833 1189 HOH   HOH B . 
W 10 HOH   434  1834 856  HOH   HOH B . 
W 10 HOH   435  1835 1045 HOH   HOH B . 
W 10 HOH   436  1836 1720 HOH   HOH B . 
W 10 HOH   437  1837 1033 HOH   HOH B . 
W 10 HOH   438  1838 1829 HOH   HOH B . 
W 10 HOH   439  1839 1597 HOH   HOH B . 
W 10 HOH   440  1840 2243 HOH   HOH B . 
W 10 HOH   441  1841 1028 HOH   HOH B . 
W 10 HOH   442  1842 994  HOH   HOH B . 
W 10 HOH   443  1843 540  HOH   HOH B . 
W 10 HOH   444  1844 2363 HOH   HOH B . 
W 10 HOH   445  1845 75   HOH   HOH B . 
W 10 HOH   446  1846 382  HOH   HOH B . 
W 10 HOH   447  1847 497  HOH   HOH B . 
W 10 HOH   448  1848 586  HOH   HOH B . 
W 10 HOH   449  1849 672  HOH   HOH B . 
W 10 HOH   450  1850 1637 HOH   HOH B . 
W 10 HOH   451  1851 1202 HOH   HOH B . 
W 10 HOH   452  1852 1331 HOH   HOH B . 
W 10 HOH   453  1853 492  HOH   HOH B . 
W 10 HOH   454  1854 737  HOH   HOH B . 
W 10 HOH   455  1855 25   HOH   HOH B . 
W 10 HOH   456  1856 73   HOH   HOH B . 
W 10 HOH   457  1857 6    HOH   HOH B . 
W 10 HOH   458  1858 90   HOH   HOH B . 
W 10 HOH   459  1859 56   HOH   HOH B . 
W 10 HOH   460  1860 13   HOH   HOH B . 
W 10 HOH   461  1861 669  HOH   HOH B . 
W 10 HOH   462  1862 1123 HOH   HOH B . 
W 10 HOH   463  1863 348  HOH   HOH B . 
W 10 HOH   464  1864 689  HOH   HOH B . 
W 10 HOH   465  1865 80   HOH   HOH B . 
W 10 HOH   466  1866 1465 HOH   HOH B . 
W 10 HOH   467  1867 1433 HOH   HOH B . 
W 10 HOH   468  1868 822  HOH   HOH B . 
W 10 HOH   469  1869 2478 HOH   HOH B . 
W 10 HOH   470  1870 498  HOH   HOH B . 
W 10 HOH   471  1871 395  HOH   HOH B . 
W 10 HOH   472  1872 762  HOH   HOH B . 
W 10 HOH   473  1873 570  HOH   HOH B . 
W 10 HOH   474  1874 515  HOH   HOH B . 
W 10 HOH   475  1875 1687 HOH   HOH B . 
W 10 HOH   476  1876 991  HOH   HOH B . 
W 10 HOH   477  1877 2354 HOH   HOH B . 
W 10 HOH   478  1878 23   HOH   HOH B . 
W 10 HOH   479  1879 1313 HOH   HOH B . 
W 10 HOH   480  1880 1032 HOH   HOH B . 
W 10 HOH   481  1881 380  HOH   HOH B . 
W 10 HOH   482  1882 1248 HOH   HOH B . 
W 10 HOH   483  1883 272  HOH   HOH B . 
W 10 HOH   484  1884 772  HOH   HOH B . 
W 10 HOH   485  1885 105  HOH   HOH B . 
W 10 HOH   486  1886 285  HOH   HOH B . 
W 10 HOH   487  1887 952  HOH   HOH B . 
W 10 HOH   488  1888 1358 HOH   HOH B . 
W 10 HOH   489  1889 240  HOH   HOH B . 
W 10 HOH   490  1890 1199 HOH   HOH B . 
W 10 HOH   491  1891 43   HOH   HOH B . 
W 10 HOH   492  1892 1794 HOH   HOH B . 
W 10 HOH   493  1893 1576 HOH   HOH B . 
W 10 HOH   494  1894 245  HOH   HOH B . 
W 10 HOH   495  1895 1200 HOH   HOH B . 
W 10 HOH   496  1896 167  HOH   HOH B . 
W 10 HOH   497  1897 793  HOH   HOH B . 
W 10 HOH   498  1898 152  HOH   HOH B . 
W 10 HOH   499  1899 644  HOH   HOH B . 
W 10 HOH   500  1900 2056 HOH   HOH B . 
W 10 HOH   501  1901 1204 HOH   HOH B . 
W 10 HOH   502  1902 251  HOH   HOH B . 
W 10 HOH   503  1903 1376 HOH   HOH B . 
W 10 HOH   504  1904 1677 HOH   HOH B . 
W 10 HOH   505  1905 107  HOH   HOH B . 
W 10 HOH   506  1906 968  HOH   HOH B . 
W 10 HOH   507  1907 1187 HOH   HOH B . 
W 10 HOH   508  1908 2051 HOH   HOH B . 
W 10 HOH   509  1909 58   HOH   HOH B . 
W 10 HOH   510  1910 429  HOH   HOH B . 
W 10 HOH   511  1911 156  HOH   HOH B . 
W 10 HOH   512  1912 1965 HOH   HOH B . 
W 10 HOH   513  1913 120  HOH   HOH B . 
W 10 HOH   514  1914 1520 HOH   HOH B . 
W 10 HOH   515  1915 1751 HOH   HOH B . 
W 10 HOH   516  1916 305  HOH   HOH B . 
W 10 HOH   517  1917 794  HOH   HOH B . 
W 10 HOH   518  1918 1428 HOH   HOH B . 
W 10 HOH   519  1919 334  HOH   HOH B . 
W 10 HOH   520  1920 368  HOH   HOH B . 
W 10 HOH   521  1921 1421 HOH   HOH B . 
W 10 HOH   522  1922 560  HOH   HOH B . 
W 10 HOH   523  1923 1036 HOH   HOH B . 
W 10 HOH   524  1924 210  HOH   HOH B . 
W 10 HOH   525  1925 875  HOH   HOH B . 
W 10 HOH   526  1926 666  HOH   HOH B . 
W 10 HOH   527  1927 887  HOH   HOH B . 
W 10 HOH   528  1928 992  HOH   HOH B . 
W 10 HOH   529  1929 733  HOH   HOH B . 
W 10 HOH   530  1930 1679 HOH   HOH B . 
W 10 HOH   531  1931 2444 HOH   HOH B . 
W 10 HOH   532  1932 2173 HOH   HOH B . 
W 10 HOH   533  1933 126  HOH   HOH B . 
W 10 HOH   534  1934 790  HOH   HOH B . 
W 10 HOH   535  1935 223  HOH   HOH B . 
W 10 HOH   536  1936 519  HOH   HOH B . 
W 10 HOH   537  1937 619  HOH   HOH B . 
W 10 HOH   538  1938 2513 HOH   HOH B . 
W 10 HOH   539  1939 1290 HOH   HOH B . 
W 10 HOH   540  1940 284  HOH   HOH B . 
W 10 HOH   541  1941 854  HOH   HOH B . 
W 10 HOH   542  1942 1095 HOH   HOH B . 
W 10 HOH   543  1943 1554 HOH   HOH B . 
W 10 HOH   544  1944 933  HOH   HOH B . 
W 10 HOH   545  1945 1548 HOH   HOH B . 
W 10 HOH   546  1946 2541 HOH   HOH B . 
W 10 HOH   547  1947 462  HOH   HOH B . 
W 10 HOH   548  1948 1270 HOH   HOH B . 
W 10 HOH   549  1949 1450 HOH   HOH B . 
W 10 HOH   550  1950 461  HOH   HOH B . 
W 10 HOH   551  1951 898  HOH   HOH B . 
W 10 HOH   552  1952 427  HOH   HOH B . 
W 10 HOH   553  1953 878  HOH   HOH B . 
W 10 HOH   554  1954 769  HOH   HOH B . 
W 10 HOH   555  1955 98   HOH   HOH B . 
W 10 HOH   556  1956 1378 HOH   HOH B . 
W 10 HOH   557  1957 434  HOH   HOH B . 
W 10 HOH   558  1958 679  HOH   HOH B . 
W 10 HOH   559  1959 169  HOH   HOH B . 
W 10 HOH   560  1960 118  HOH   HOH B . 
W 10 HOH   561  1961 705  HOH   HOH B . 
W 10 HOH   562  1962 2038 HOH   HOH B . 
W 10 HOH   563  1963 244  HOH   HOH B . 
W 10 HOH   564  1964 1232 HOH   HOH B . 
W 10 HOH   565  1965 1539 HOH   HOH B . 
W 10 HOH   566  1966 100  HOH   HOH B . 
W 10 HOH   567  1967 428  HOH   HOH B . 
W 10 HOH   568  1968 166  HOH   HOH B . 
W 10 HOH   569  1969 1163 HOH   HOH B . 
W 10 HOH   570  1970 849  HOH   HOH B . 
W 10 HOH   571  1971 1194 HOH   HOH B . 
W 10 HOH   572  1972 1466 HOH   HOH B . 
W 10 HOH   573  1973 596  HOH   HOH B . 
W 10 HOH   574  1974 2210 HOH   HOH B . 
W 10 HOH   575  1975 155  HOH   HOH B . 
W 10 HOH   576  1976 84   HOH   HOH B . 
W 10 HOH   577  1977 54   HOH   HOH B . 
W 10 HOH   578  1978 213  HOH   HOH B . 
W 10 HOH   579  1979 1030 HOH   HOH B . 
W 10 HOH   580  1980 195  HOH   HOH B . 
W 10 HOH   581  1981 1840 HOH   HOH B . 
W 10 HOH   582  1982 365  HOH   HOH B . 
W 10 HOH   583  1983 180  HOH   HOH B . 
W 10 HOH   584  1984 756  HOH   HOH B . 
W 10 HOH   585  1985 247  HOH   HOH B . 
W 10 HOH   586  1986 448  HOH   HOH B . 
W 10 HOH   587  1987 86   HOH   HOH B . 
W 10 HOH   588  1988 884  HOH   HOH B . 
W 10 HOH   589  1989 273  HOH   HOH B . 
W 10 HOH   590  1990 1345 HOH   HOH B . 
W 10 HOH   591  1991 2438 HOH   HOH B . 
W 10 HOH   592  1992 2194 HOH   HOH B . 
W 10 HOH   593  1993 1391 HOH   HOH B . 
W 10 HOH   594  1994 293  HOH   HOH B . 
W 10 HOH   595  1995 615  HOH   HOH B . 
W 10 HOH   596  1996 211  HOH   HOH B . 
W 10 HOH   597  1997 533  HOH   HOH B . 
W 10 HOH   598  1998 256  HOH   HOH B . 
W 10 HOH   599  1999 1044 HOH   HOH B . 
W 10 HOH   600  2000 1379 HOH   HOH B . 
W 10 HOH   601  2001 27   HOH   HOH B . 
W 10 HOH   602  2002 2506 HOH   HOH B . 
W 10 HOH   603  2003 699  HOH   HOH B . 
W 10 HOH   604  2004 317  HOH   HOH B . 
W 10 HOH   605  2005 69   HOH   HOH B . 
W 10 HOH   606  2006 252  HOH   HOH B . 
W 10 HOH   607  2007 1439 HOH   HOH B . 
W 10 HOH   608  2008 698  HOH   HOH B . 
W 10 HOH   609  2009 1071 HOH   HOH B . 
W 10 HOH   610  2010 862  HOH   HOH B . 
W 10 HOH   611  2011 1891 HOH   HOH B . 
W 10 HOH   612  2012 128  HOH   HOH B . 
W 10 HOH   613  2013 116  HOH   HOH B . 
W 10 HOH   614  2014 2067 HOH   HOH B . 
W 10 HOH   615  2015 1401 HOH   HOH B . 
W 10 HOH   616  2016 2098 HOH   HOH B . 
W 10 HOH   617  2017 1789 HOH   HOH B . 
W 10 HOH   618  2018 2209 HOH   HOH B . 
W 10 HOH   619  2019 1351 HOH   HOH B . 
W 10 HOH   620  2020 752  HOH   HOH B . 
W 10 HOH   621  2021 1186 HOH   HOH B . 
W 10 HOH   622  2022 1429 HOH   HOH B . 
W 10 HOH   623  2023 1265 HOH   HOH B . 
W 10 HOH   624  2024 2470 HOH   HOH B . 
W 10 HOH   625  2025 597  HOH   HOH B . 
W 10 HOH   626  2026 685  HOH   HOH B . 
W 10 HOH   627  2027 276  HOH   HOH B . 
W 10 HOH   628  2028 129  HOH   HOH B . 
W 10 HOH   629  2029 731  HOH   HOH B . 
W 10 HOH   630  2030 2106 HOH   HOH B . 
W 10 HOH   631  2031 1660 HOH   HOH B . 
W 10 HOH   632  2032 71   HOH   HOH B . 
W 10 HOH   633  2033 1671 HOH   HOH B . 
W 10 HOH   634  2034 423  HOH   HOH B . 
W 10 HOH   635  2035 860  HOH   HOH B . 
W 10 HOH   636  2036 2572 HOH   HOH B . 
W 10 HOH   637  2037 2349 HOH   HOH B . 
W 10 HOH   638  2038 1747 HOH   HOH B . 
W 10 HOH   639  2039 17   HOH   HOH B . 
W 10 HOH   640  2040 1003 HOH   HOH B . 
W 10 HOH   641  2041 967  HOH   HOH B . 
W 10 HOH   642  2042 697  HOH   HOH B . 
W 10 HOH   643  2043 198  HOH   HOH B . 
W 10 HOH   644  2044 588  HOH   HOH B . 
W 10 HOH   645  2045 137  HOH   HOH B . 
W 10 HOH   646  2046 182  HOH   HOH B . 
W 10 HOH   647  2047 1166 HOH   HOH B . 
W 10 HOH   648  2048 85   HOH   HOH B . 
W 10 HOH   649  2049 2239 HOH   HOH B . 
W 10 HOH   650  2050 11   HOH   HOH B . 
W 10 HOH   651  2051 386  HOH   HOH B . 
W 10 HOH   652  2052 1069 HOH   HOH B . 
W 10 HOH   653  2053 1419 HOH   HOH B . 
W 10 HOH   654  2054 902  HOH   HOH B . 
W 10 HOH   655  2055 2290 HOH   HOH B . 
W 10 HOH   656  2056 573  HOH   HOH B . 
W 10 HOH   657  2057 1645 HOH   HOH B . 
W 10 HOH   658  2058 1736 HOH   HOH B . 
W 10 HOH   659  2059 506  HOH   HOH B . 
W 10 HOH   660  2060 908  HOH   HOH B . 
W 10 HOH   661  2061 302  HOH   HOH B . 
W 10 HOH   662  2062 2020 HOH   HOH B . 
W 10 HOH   663  2063 552  HOH   HOH B . 
W 10 HOH   664  2064 511  HOH   HOH B . 
W 10 HOH   665  2065 940  HOH   HOH B . 
W 10 HOH   666  2066 701  HOH   HOH B . 
W 10 HOH   667  2067 215  HOH   HOH B . 
W 10 HOH   668  2068 1057 HOH   HOH B . 
W 10 HOH   669  2069 1424 HOH   HOH B . 
W 10 HOH   670  2070 109  HOH   HOH B . 
W 10 HOH   671  2071 88   HOH   HOH B . 
W 10 HOH   672  2072 2578 HOH   HOH B . 
W 10 HOH   673  2073 292  HOH   HOH B . 
W 10 HOH   674  2074 8    HOH   HOH B . 
W 10 HOH   675  2075 1987 HOH   HOH B . 
W 10 HOH   676  2076 507  HOH   HOH B . 
W 10 HOH   677  2077 2594 HOH   HOH B . 
W 10 HOH   678  2078 254  HOH   HOH B . 
W 10 HOH   679  2079 1470 HOH   HOH B . 
W 10 HOH   680  2080 1993 HOH   HOH B . 
W 10 HOH   681  2081 930  HOH   HOH B . 
W 10 HOH   682  2082 1356 HOH   HOH B . 
W 10 HOH   683  2083 1457 HOH   HOH B . 
W 10 HOH   684  2084 203  HOH   HOH B . 
W 10 HOH   685  2085 1093 HOH   HOH B . 
W 10 HOH   686  2086 799  HOH   HOH B . 
W 10 HOH   687  2087 2277 HOH   HOH B . 
W 10 HOH   688  2088 1688 HOH   HOH B . 
W 10 HOH   689  2089 318  HOH   HOH B . 
W 10 HOH   690  2090 680  HOH   HOH B . 
W 10 HOH   691  2091 763  HOH   HOH B . 
W 10 HOH   692  2092 174  HOH   HOH B . 
W 10 HOH   693  2093 1    HOH   HOH B . 
W 10 HOH   694  2094 1742 HOH   HOH B . 
W 10 HOH   695  2095 418  HOH   HOH B . 
W 10 HOH   696  2096 1790 HOH   HOH B . 
W 10 HOH   697  2097 1261 HOH   HOH B . 
W 10 HOH   698  2098 228  HOH   HOH B . 
W 10 HOH   699  2099 2401 HOH   HOH B . 
W 10 HOH   700  2100 603  HOH   HOH B . 
W 10 HOH   701  2101 115  HOH   HOH B . 
W 10 HOH   702  2102 872  HOH   HOH B . 
W 10 HOH   703  2103 630  HOH   HOH B . 
W 10 HOH   704  2104 848  HOH   HOH B . 
W 10 HOH   705  2105 257  HOH   HOH B . 
W 10 HOH   706  2106 2538 HOH   HOH B . 
W 10 HOH   707  2107 356  HOH   HOH B . 
W 10 HOH   708  2108 514  HOH   HOH B . 
W 10 HOH   709  2109 330  HOH   HOH B . 
W 10 HOH   710  2110 430  HOH   HOH B . 
W 10 HOH   711  2111 572  HOH   HOH B . 
W 10 HOH   712  2112 598  HOH   HOH B . 
W 10 HOH   713  2113 1776 HOH   HOH B . 
W 10 HOH   714  2114 1213 HOH   HOH B . 
W 10 HOH   715  2115 503  HOH   HOH B . 
W 10 HOH   716  2116 1333 HOH   HOH B . 
W 10 HOH   717  2117 2437 HOH   HOH B . 
W 10 HOH   718  2118 584  HOH   HOH B . 
W 10 HOH   719  2119 1075 HOH   HOH B . 
W 10 HOH   720  2120 1192 HOH   HOH B . 
W 10 HOH   721  2121 729  HOH   HOH B . 
W 10 HOH   722  2122 2576 HOH   HOH B . 
W 10 HOH   723  2123 2367 HOH   HOH B . 
W 10 HOH   724  2124 1499 HOH   HOH B . 
W 10 HOH   725  2125 518  HOH   HOH B . 
W 10 HOH   726  2126 886  HOH   HOH B . 
W 10 HOH   727  2127 134  HOH   HOH B . 
W 10 HOH   728  2128 402  HOH   HOH B . 
W 10 HOH   729  2129 1414 HOH   HOH B . 
W 10 HOH   730  2130 1912 HOH   HOH B . 
W 10 HOH   731  2131 2034 HOH   HOH B . 
W 10 HOH   732  2132 178  HOH   HOH B . 
W 10 HOH   733  2133 1169 HOH   HOH B . 
W 10 HOH   734  2134 2130 HOH   HOH B . 
W 10 HOH   735  2135 1121 HOH   HOH B . 
W 10 HOH   736  2136 394  HOH   HOH B . 
W 10 HOH   737  2137 2072 HOH   HOH B . 
W 10 HOH   738  2138 742  HOH   HOH B . 
W 10 HOH   739  2139 1544 HOH   HOH B . 
W 10 HOH   740  2140 1266 HOH   HOH B . 
W 10 HOH   741  2141 653  HOH   HOH B . 
W 10 HOH   742  2142 1127 HOH   HOH B . 
W 10 HOH   743  2143 544  HOH   HOH B . 
W 10 HOH   744  2144 634  HOH   HOH B . 
W 10 HOH   745  2145 1035 HOH   HOH B . 
W 10 HOH   746  2146 473  HOH   HOH B . 
W 10 HOH   747  2147 558  HOH   HOH B . 
W 10 HOH   748  2148 1954 HOH   HOH B . 
W 10 HOH   749  2149 565  HOH   HOH B . 
W 10 HOH   750  2150 1017 HOH   HOH B . 
W 10 HOH   751  2151 833  HOH   HOH B . 
W 10 HOH   752  2152 707  HOH   HOH B . 
W 10 HOH   753  2153 315  HOH   HOH B . 
W 10 HOH   754  2154 1322 HOH   HOH B . 
W 10 HOH   755  2155 999  HOH   HOH B . 
W 10 HOH   756  2156 764  HOH   HOH B . 
W 10 HOH   757  2157 910  HOH   HOH B . 
W 10 HOH   758  2158 753  HOH   HOH B . 
W 10 HOH   759  2159 112  HOH   HOH B . 
W 10 HOH   760  2160 26   HOH   HOH B . 
W 10 HOH   761  2161 740  HOH   HOH B . 
W 10 HOH   762  2162 271  HOH   HOH B . 
W 10 HOH   763  2163 359  HOH   HOH B . 
W 10 HOH   764  2164 2394 HOH   HOH B . 
W 10 HOH   765  2165 1874 HOH   HOH B . 
W 10 HOH   766  2166 439  HOH   HOH B . 
W 10 HOH   767  2167 1388 HOH   HOH B . 
W 10 HOH   768  2168 1353 HOH   HOH B . 
W 10 HOH   769  2169 726  HOH   HOH B . 
W 10 HOH   770  2170 1646 HOH   HOH B . 
W 10 HOH   771  2171 1836 HOH   HOH B . 
W 10 HOH   772  2172 2373 HOH   HOH B . 
W 10 HOH   773  2173 1508 HOH   HOH B . 
W 10 HOH   774  2174 1977 HOH   HOH B . 
W 10 HOH   775  2175 298  HOH   HOH B . 
W 10 HOH   776  2176 1533 HOH   HOH B . 
W 10 HOH   777  2177 106  HOH   HOH B . 
W 10 HOH   778  2178 1042 HOH   HOH B . 
W 10 HOH   779  2179 1565 HOH   HOH B . 
W 10 HOH   780  2180 2583 HOH   HOH B . 
W 10 HOH   781  2181 595  HOH   HOH B . 
W 10 HOH   782  2182 495  HOH   HOH B . 
W 10 HOH   783  2183 960  HOH   HOH B . 
W 10 HOH   784  2184 1111 HOH   HOH B . 
W 10 HOH   785  2185 2246 HOH   HOH B . 
W 10 HOH   786  2186 1411 HOH   HOH B . 
W 10 HOH   787  2187 1251 HOH   HOH B . 
W 10 HOH   788  2188 1670 HOH   HOH B . 
W 10 HOH   789  2189 2382 HOH   HOH B . 
W 10 HOH   790  2190 2293 HOH   HOH B . 
W 10 HOH   791  2191 1156 HOH   HOH B . 
W 10 HOH   792  2192 269  HOH   HOH B . 
W 10 HOH   793  2193 1122 HOH   HOH B . 
W 10 HOH   794  2194 743  HOH   HOH B . 
W 10 HOH   795  2195 1518 HOH   HOH B . 
W 10 HOH   796  2196 2018 HOH   HOH B . 
W 10 HOH   797  2197 2564 HOH   HOH B . 
W 10 HOH   798  2198 670  HOH   HOH B . 
W 10 HOH   799  2199 1495 HOH   HOH B . 
W 10 HOH   800  2200 396  HOH   HOH B . 
W 10 HOH   801  2201 408  HOH   HOH B . 
W 10 HOH   802  2202 2542 HOH   HOH B . 
W 10 HOH   803  2203 1007 HOH   HOH B . 
W 10 HOH   804  2204 1924 HOH   HOH B . 
W 10 HOH   805  2205 1550 HOH   HOH B . 
W 10 HOH   806  2206 965  HOH   HOH B . 
W 10 HOH   807  2207 97   HOH   HOH B . 
W 10 HOH   808  2208 1982 HOH   HOH B . 
W 10 HOH   809  2209 197  HOH   HOH B . 
W 10 HOH   810  2210 371  HOH   HOH B . 
W 10 HOH   811  2211 310  HOH   HOH B . 
W 10 HOH   812  2212 15   HOH   HOH B . 
W 10 HOH   813  2213 1019 HOH   HOH B . 
W 10 HOH   814  2214 927  HOH   HOH B . 
W 10 HOH   815  2215 1348 HOH   HOH B . 
W 10 HOH   816  2216 266  HOH   HOH B . 
W 10 HOH   817  2217 896  HOH   HOH B . 
W 10 HOH   818  2218 319  HOH   HOH B . 
W 10 HOH   819  2219 1566 HOH   HOH B . 
W 10 HOH   820  2220 802  HOH   HOH B . 
W 10 HOH   821  2221 2353 HOH   HOH B . 
W 10 HOH   822  2222 1812 HOH   HOH B . 
W 10 HOH   823  2223 604  HOH   HOH B . 
W 10 HOH   824  2224 706  HOH   HOH B . 
W 10 HOH   825  2225 1294 HOH   HOH B . 
W 10 HOH   826  2226 857  HOH   HOH B . 
W 10 HOH   827  2227 57   HOH   HOH B . 
W 10 HOH   828  2228 809  HOH   HOH B . 
W 10 HOH   829  2229 2257 HOH   HOH B . 
W 10 HOH   830  2230 2514 HOH   HOH B . 
W 10 HOH   831  2231 1538 HOH   HOH B . 
W 10 HOH   832  2232 1839 HOH   HOH B . 
W 10 HOH   833  2233 360  HOH   HOH B . 
W 10 HOH   834  2234 1685 HOH   HOH B . 
W 10 HOH   835  2235 556  HOH   HOH B . 
W 10 HOH   836  2236 2080 HOH   HOH B . 
W 10 HOH   837  2237 304  HOH   HOH B . 
W 10 HOH   838  2238 626  HOH   HOH B . 
W 10 HOH   839  2239 1399 HOH   HOH B . 
W 10 HOH   840  2240 577  HOH   HOH B . 
W 10 HOH   841  2241 2109 HOH   HOH B . 
W 10 HOH   842  2242 2539 HOH   HOH B . 
W 10 HOH   843  2243 2413 HOH   HOH B . 
W 10 HOH   844  2244 2345 HOH   HOH B . 
W 10 HOH   845  2245 2200 HOH   HOH B . 
W 10 HOH   846  2246 905  HOH   HOH B . 
W 10 HOH   847  2247 2330 HOH   HOH B . 
W 10 HOH   848  2248 2019 HOH   HOH B . 
W 10 HOH   849  2249 93   HOH   HOH B . 
W 10 HOH   850  2250 1654 HOH   HOH B . 
W 10 HOH   851  2251 370  HOH   HOH B . 
W 10 HOH   852  2252 2055 HOH   HOH B . 
W 10 HOH   853  2253 1375 HOH   HOH B . 
W 10 HOH   854  2254 647  HOH   HOH B . 
W 10 HOH   855  2255 2216 HOH   HOH B . 
W 10 HOH   856  2256 2325 HOH   HOH B . 
W 10 HOH   857  2257 2201 HOH   HOH B . 
W 10 HOH   858  2258 566  HOH   HOH B . 
W 10 HOH   859  2259 1583 HOH   HOH B . 
W 10 HOH   860  2260 1592 HOH   HOH B . 
W 10 HOH   861  2261 1819 HOH   HOH B . 
W 10 HOH   862  2262 1404 HOH   HOH B . 
W 10 HOH   863  2263 2035 HOH   HOH B . 
W 10 HOH   864  2264 911  HOH   HOH B . 
W 10 HOH   865  2265 267  HOH   HOH B . 
W 10 HOH   866  2266 1346 HOH   HOH B . 
W 10 HOH   867  2267 1930 HOH   HOH B . 
W 10 HOH   868  2268 414  HOH   HOH B . 
W 10 HOH   869  2269 1778 HOH   HOH B . 
W 10 HOH   870  2270 1188 HOH   HOH B . 
W 10 HOH   871  2271 947  HOH   HOH B . 
W 10 HOH   872  2272 1463 HOH   HOH B . 
W 10 HOH   873  2273 2442 HOH   HOH B . 
W 10 HOH   874  2274 1014 HOH   HOH B . 
W 10 HOH   875  2275 931  HOH   HOH B . 
W 10 HOH   876  2276 2591 HOH   HOH B . 
W 10 HOH   877  2277 509  HOH   HOH B . 
W 10 HOH   878  2278 1593 HOH   HOH B . 
W 10 HOH   879  2279 1838 HOH   HOH B . 
W 10 HOH   880  2280 1846 HOH   HOH B . 
W 10 HOH   881  2281 2163 HOH   HOH B . 
W 10 HOH   882  2282 1472 HOH   HOH B . 
W 10 HOH   883  2283 897  HOH   HOH B . 
W 10 HOH   884  2284 2533 HOH   HOH B . 
W 10 HOH   885  2285 2234 HOH   HOH B . 
W 10 HOH   886  2286 2346 HOH   HOH B . 
W 10 HOH   887  2287 1708 HOH   HOH B . 
W 10 HOH   888  2288 2464 HOH   HOH B . 
W 10 HOH   889  2289 766  HOH   HOH B . 
W 10 HOH   890  2290 2050 HOH   HOH B . 
W 10 HOH   891  2291 714  HOH   HOH B . 
W 10 HOH   892  2292 2422 HOH   HOH B . 
W 10 HOH   893  2293 1027 HOH   HOH B . 
W 10 HOH   894  2294 2251 HOH   HOH B . 
W 10 HOH   895  2295 2204 HOH   HOH B . 
W 10 HOH   896  2296 1151 HOH   HOH B . 
W 10 HOH   897  2297 9    HOH   HOH B . 
W 10 HOH   898  2298 2159 HOH   HOH B . 
W 10 HOH   899  2299 1709 HOH   HOH B . 
W 10 HOH   900  2300 2185 HOH   HOH B . 
W 10 HOH   901  2301 1525 HOH   HOH B . 
W 10 HOH   902  2302 1238 HOH   HOH B . 
W 10 HOH   903  2303 1167 HOH   HOH B . 
W 10 HOH   904  2304 1946 HOH   HOH B . 
W 10 HOH   905  2305 1021 HOH   HOH B . 
W 10 HOH   906  2306 2512 HOH   HOH B . 
W 10 HOH   907  2307 2582 HOH   HOH B . 
W 10 HOH   908  2308 1784 HOH   HOH B . 
W 10 HOH   909  2309 1852 HOH   HOH B . 
W 10 HOH   910  2310 375  HOH   HOH B . 
W 10 HOH   911  2311 2298 HOH   HOH B . 
W 10 HOH   912  2312 2117 HOH   HOH B . 
W 10 HOH   913  2313 1876 HOH   HOH B . 
W 10 HOH   914  2314 2052 HOH   HOH B . 
W 10 HOH   915  2315 2548 HOH   HOH B . 
W 10 HOH   916  2316 846  HOH   HOH B . 
W 10 HOH   917  2317 1979 HOH   HOH B . 
W 10 HOH   918  2318 636  HOH   HOH B . 
W 10 HOH   919  2319 2272 HOH   HOH B . 
W 10 HOH   920  2320 2188 HOH   HOH B . 
W 10 HOH   921  2321 377  HOH   HOH B . 
W 10 HOH   922  2322 2550 HOH   HOH B . 
W 10 HOH   923  2323 2083 HOH   HOH B . 
W 10 HOH   924  2324 946  HOH   HOH B . 
W 10 HOH   925  2325 2119 HOH   HOH B . 
W 10 HOH   926  2326 2381 HOH   HOH B . 
W 10 HOH   927  2327 1584 HOH   HOH B . 
W 10 HOH   928  2328 1412 HOH   HOH B . 
W 10 HOH   929  2329 1805 HOH   HOH B . 
W 10 HOH   930  2330 2318 HOH   HOH B . 
W 10 HOH   931  2331 658  HOH   HOH B . 
W 10 HOH   932  2332 800  HOH   HOH B . 
W 10 HOH   933  2333 1503 HOH   HOH B . 
W 10 HOH   934  2334 1148 HOH   HOH B . 
W 10 HOH   935  2335 2207 HOH   HOH B . 
W 10 HOH   936  2336 1171 HOH   HOH B . 
W 10 HOH   937  2337 2193 HOH   HOH B . 
W 10 HOH   938  2338 2273 HOH   HOH B . 
W 10 HOH   939  2339 850  HOH   HOH B . 
W 10 HOH   940  2340 1724 HOH   HOH B . 
W 10 HOH   941  2341 2487 HOH   HOH B . 
W 10 HOH   942  2342 1944 HOH   HOH B . 
W 10 HOH   943  2343 2235 HOH   HOH B . 
W 10 HOH   944  2344 1079 HOH   HOH B . 
W 10 HOH   945  2345 2561 HOH   HOH B . 
W 10 HOH   946  2346 1697 HOH   HOH B . 
W 10 HOH   947  2347 1898 HOH   HOH B . 
W 10 HOH   948  2348 1272 HOH   HOH B . 
W 10 HOH   949  2349 2339 HOH   HOH B . 
W 10 HOH   950  2350 1502 HOH   HOH B . 
W 10 HOH   951  2351 2006 HOH   HOH B . 
W 10 HOH   952  2352 1210 HOH   HOH B . 
W 10 HOH   953  2353 2187 HOH   HOH B . 
W 10 HOH   954  2354 2166 HOH   HOH B . 
W 10 HOH   955  2355 2223 HOH   HOH B . 
W 10 HOH   956  2356 2033 HOH   HOH B . 
W 10 HOH   957  2357 1752 HOH   HOH B . 
W 10 HOH   958  2358 2312 HOH   HOH B . 
W 10 HOH   959  2359 2390 HOH   HOH B . 
W 10 HOH   960  2360 122  HOH   HOH B . 
W 10 HOH   961  2361 2551 HOH   HOH B . 
W 10 HOH   962  2362 2440 HOH   HOH B . 
W 10 HOH   963  2363 1792 HOH   HOH B . 
W 10 HOH   964  2364 789  HOH   HOH B . 
W 10 HOH   965  2365 2559 HOH   HOH B . 
W 10 HOH   966  2366 1971 HOH   HOH B . 
W 10 HOH   967  2367 2535 HOH   HOH B . 
W 10 HOH   968  2368 1233 HOH   HOH B . 
W 10 HOH   969  2369 1620 HOH   HOH B . 
W 10 HOH   970  2370 913  HOH   HOH B . 
W 10 HOH   971  2371 1226 HOH   HOH B . 
W 10 HOH   972  2372 1551 HOH   HOH B . 
W 10 HOH   973  2373 1939 HOH   HOH B . 
W 10 HOH   974  2374 2001 HOH   HOH B . 
W 10 HOH   975  2375 938  HOH   HOH B . 
W 10 HOH   976  2376 2300 HOH   HOH B . 
W 10 HOH   977  2377 1430 HOH   HOH B . 
W 10 HOH   978  2378 1804 HOH   HOH B . 
W 10 HOH   979  2379 2590 HOH   HOH B . 
W 10 HOH   980  2380 810  HOH   HOH B . 
W 10 HOH   981  2381 1915 HOH   HOH B . 
W 10 HOH   982  2382 449  HOH   HOH B . 
W 10 HOH   983  2383 536  HOH   HOH B . 
W 10 HOH   984  2384 1783 HOH   HOH B . 
W 10 HOH   985  2385 1578 HOH   HOH B . 
W 10 HOH   986  2386 791  HOH   HOH B . 
W 10 HOH   987  2387 2419 HOH   HOH B . 
W 10 HOH   988  2388 741  HOH   HOH B . 
W 10 HOH   989  2389 2138 HOH   HOH B . 
W 10 HOH   990  2390 1371 HOH   HOH B . 
W 10 HOH   991  2391 845  HOH   HOH B . 
W 10 HOH   992  2392 1823 HOH   HOH B . 
W 10 HOH   993  2393 477  HOH   HOH B . 
W 10 HOH   994  2394 2192 HOH   HOH B . 
W 10 HOH   995  2395 950  HOH   HOH B . 
W 10 HOH   996  2396 2164 HOH   HOH B . 
W 10 HOH   997  2397 2532 HOH   HOH B . 
W 10 HOH   998  2398 602  HOH   HOH B . 
W 10 HOH   999  2399 1845 HOH   HOH B . 
W 10 HOH   1000 2400 2027 HOH   HOH B . 
W 10 HOH   1001 2401 1380 HOH   HOH B . 
W 10 HOH   1002 2402 1885 HOH   HOH B . 
W 10 HOH   1003 2403 1896 HOH   HOH B . 
W 10 HOH   1004 2404 124  HOH   HOH B . 
W 10 HOH   1005 2405 2507 HOH   HOH B . 
W 10 HOH   1006 2406 823  HOH   HOH B . 
W 10 HOH   1007 2407 2222 HOH   HOH B . 
W 10 HOH   1008 2408 980  HOH   HOH B . 
W 10 HOH   1009 2409 2308 HOH   HOH B . 
W 10 HOH   1010 2410 924  HOH   HOH B . 
W 10 HOH   1011 2411 1224 HOH   HOH B . 
W 10 HOH   1012 2412 1900 HOH   HOH B . 
W 10 HOH   1013 2413 2407 HOH   HOH B . 
W 10 HOH   1014 2414 2244 HOH   HOH B . 
W 10 HOH   1015 2415 481  HOH   HOH B . 
W 10 HOH   1016 2416 1236 HOH   HOH B . 
W 10 HOH   1017 2417 1547 HOH   HOH B . 
W 10 HOH   1018 2418 2536 HOH   HOH B . 
W 10 HOH   1019 2419 1537 HOH   HOH B . 
W 10 HOH   1020 2420 1305 HOH   HOH B . 
W 10 HOH   1021 2421 1970 HOH   HOH B . 
W 10 HOH   1022 2422 710  HOH   HOH B . 
W 10 HOH   1023 2423 990  HOH   HOH B . 
W 10 HOH   1024 2424 1096 HOH   HOH B . 
W 10 HOH   1025 2425 2575 HOH   HOH B . 
W 10 HOH   1026 2426 1632 HOH   HOH B . 
W 10 HOH   1027 2427 2    HOH   HOH B . 
W 10 HOH   1028 2428 2068 HOH   HOH B . 
W 10 HOH   1029 2429 2278 HOH   HOH B . 
W 10 HOH   1030 2430 2560 HOH   HOH B . 
W 10 HOH   1031 2431 612  HOH   HOH B . 
W 10 HOH   1032 2432 2103 HOH   HOH B . 
W 10 HOH   1033 2433 2285 HOH   HOH B . 
W 10 HOH   1034 2434 2043 HOH   HOH B . 
W 10 HOH   1035 2435 1222 HOH   HOH B . 
W 10 HOH   1036 2436 1861 HOH   HOH B . 
W 10 HOH   1037 2437 2115 HOH   HOH B . 
W 10 HOH   1038 2438 2562 HOH   HOH B . 
W 10 HOH   1039 2439 1756 HOH   HOH B . 
W 10 HOH   1040 2440 1806 HOH   HOH B . 
W 10 HOH   1041 2441 638  HOH   HOH B . 
W 10 HOH   1042 2442 2282 HOH   HOH B . 
W 10 HOH   1043 2443 2195 HOH   HOH B . 
W 10 HOH   1044 2444 2527 HOH   HOH B . 
W 10 HOH   1045 2445 1382 HOH   HOH B . 
W 10 HOH   1046 2446 2284 HOH   HOH B . 
W 10 HOH   1047 2447 858  HOH   HOH B . 
W 10 HOH   1048 2448 1229 HOH   HOH B . 
W 10 HOH   1049 2449 2015 HOH   HOH B . 
W 10 HOH   1050 2450 2388 HOH   HOH B . 
W 10 HOH   1051 2451 2477 HOH   HOH B . 
W 10 HOH   1052 2452 1304 HOH   HOH B . 
W 10 HOH   1053 2453 873  HOH   HOH B . 
W 10 HOH   1054 2454 1641 HOH   HOH B . 
W 10 HOH   1055 2455 2441 HOH   HOH B . 
W 10 HOH   1056 2456 2485 HOH   HOH B . 
W 10 HOH   1057 2457 1913 HOH   HOH B . 
W 10 HOH   1058 2458 1511 HOH   HOH B . 
W 10 HOH   1059 2459 1250 HOH   HOH B . 
W 10 HOH   1060 2460 2449 HOH   HOH B . 
W 10 HOH   1061 2461 1655 HOH   HOH B . 
W 10 HOH   1062 2462 2118 HOH   HOH B . 
W 10 HOH   1063 2463 1931 HOH   HOH B . 
W 10 HOH   1064 2464 2281 HOH   HOH B . 
W 10 HOH   1065 2465 973  HOH   HOH B . 
W 10 HOH   1066 2466 1642 HOH   HOH B . 
W 10 HOH   1067 2467 1848 HOH   HOH B . 
W 10 HOH   1068 2468 10   HOH   HOH B . 
W 10 HOH   1069 2469 2580 HOH   HOH B . 
W 10 HOH   1070 2470 2108 HOH   HOH B . 
W 10 HOH   1071 2471 1958 HOH   HOH B . 
W 10 HOH   1072 2472 816  HOH   HOH B . 
W 10 HOH   1073 2473 1877 HOH   HOH B . 
W 10 HOH   1074 2474 2301 HOH   HOH B . 
W 10 HOH   1075 2475 1098 HOH   HOH B . 
W 10 HOH   1076 2476 2488 HOH   HOH B . 
W 10 HOH   1077 2477 2586 HOH   HOH B . 
W 10 HOH   1078 2478 2309 HOH   HOH B . 
W 10 HOH   1079 2479 1519 HOH   HOH B . 
W 10 HOH   1080 2480 1361 HOH   HOH B . 
W 10 HOH   1081 2481 1255 HOH   HOH B . 
W 10 HOH   1082 2482 2372 HOH   HOH B . 
W 10 HOH   1083 2483 1781 HOH   HOH B . 
W 10 HOH   1084 2484 1455 HOH   HOH B . 
W 10 HOH   1085 2485 1626 HOH   HOH B . 
W 10 HOH   1086 2486 768  HOH   HOH B . 
W 10 HOH   1087 2487 1338 HOH   HOH B . 
W 10 HOH   1088 2488 1064 HOH   HOH B . 
W 10 HOH   1089 2489 821  HOH   HOH B . 
W 10 HOH   1090 2490 1448 HOH   HOH B . 
W 10 HOH   1091 2491 1263 HOH   HOH B . 
W 10 HOH   1092 2492 1763 HOH   HOH B . 
W 10 HOH   1093 2493 1744 HOH   HOH B . 
W 10 HOH   1094 2494 2520 HOH   HOH B . 
W 10 HOH   1095 2495 2469 HOH   HOH B . 
W 10 HOH   1096 2496 4    HOH   HOH B . 
W 10 HOH   1097 2497 2079 HOH   HOH B . 
W 10 HOH   1098 2498 811  HOH   HOH B . 
W 10 HOH   1099 2499 1844 HOH   HOH B . 
W 10 HOH   1100 2500 2104 HOH   HOH B . 
W 10 HOH   1101 2501 2184 HOH   HOH B . 
W 10 HOH   1102 2502 1498 HOH   HOH B . 
W 10 HOH   1103 2503 1220 HOH   HOH B . 
W 10 HOH   1104 2504 2116 HOH   HOH B . 
W 10 HOH   1105 2505 2340 HOH   HOH B . 
W 10 HOH   1106 2506 1040 HOH   HOH B . 
W 10 HOH   1107 2507 1501 HOH   HOH B . 
W 10 HOH   1108 2508 2007 HOH   HOH B . 
W 10 HOH   1109 2509 2283 HOH   HOH B . 
W 10 HOH   1110 2510 625  HOH   HOH B . 
W 10 HOH   1111 2511 2242 HOH   HOH B . 
W 10 HOH   1112 2512 1497 HOH   HOH B . 
W 10 HOH   1113 2513 1143 HOH   HOH B . 
W 10 HOH   1114 2514 2454 HOH   HOH B . 
W 10 HOH   1115 2515 2399 HOH   HOH B . 
W 10 HOH   1116 2516 2334 HOH   HOH B . 
W 10 HOH   1117 2517 1824 HOH   HOH B . 
W 10 HOH   1118 2518 1453 HOH   HOH B . 
W 10 HOH   1119 2519 1903 HOH   HOH B . 
W 10 HOH   1120 2520 1297 HOH   HOH B . 
W 10 HOH   1121 2521 425  HOH   HOH B . 
W 10 HOH   1122 2522 1381 HOH   HOH B . 
W 10 HOH   1123 2523 1585 HOH   HOH B . 
W 10 HOH   1124 2524 1081 HOH   HOH B . 
W 10 HOH   1125 2525 2029 HOH   HOH B . 
W 10 HOH   1126 2526 1791 HOH   HOH B . 
W 10 HOH   1127 2527 1698 HOH   HOH B . 
W 10 HOH   1128 2528 2039 HOH   HOH B . 
W 10 HOH   1129 2529 2059 HOH   HOH B . 
W 10 HOH   1130 2530 1293 HOH   HOH B . 
W 10 HOH   1131 2531 1769 HOH   HOH B . 
W 10 HOH   1132 2532 1545 HOH   HOH B . 
W 10 HOH   1133 2533 2460 HOH   HOH B . 
W 10 HOH   1134 2534 1686 HOH   HOH B . 
W 10 HOH   1135 2535 2037 HOH   HOH B . 
W 10 HOH   1136 2536 2160 HOH   HOH B . 
W 10 HOH   1137 2537 746  HOH   HOH B . 
W 10 HOH   1138 2538 767  HOH   HOH B . 
W 10 HOH   1139 2539 135  HOH   HOH B . 
W 10 HOH   1140 2540 948  HOH   HOH B . 
W 10 HOH   1141 2541 1377 HOH   HOH B . 
W 10 HOH   1142 2542 1762 HOH   HOH B . 
W 10 HOH   1143 2543 2519 HOH   HOH B . 
W 10 HOH   1144 2544 1355 HOH   HOH B . 
W 10 HOH   1145 2545 890  HOH   HOH B . 
W 10 HOH   1146 2546 1237 HOH   HOH B . 
W 10 HOH   1147 2547 2415 HOH   HOH B . 
W 10 HOH   1148 2548 770  HOH   HOH B . 
W 10 HOH   1149 2549 1658 HOH   HOH B . 
W 10 HOH   1150 2550 717  HOH   HOH B . 
W 10 HOH   1151 2551 2491 HOH   HOH B . 
W 10 HOH   1152 2552 788  HOH   HOH B . 
W 10 HOH   1153 2553 1527 HOH   HOH B . 
W 10 HOH   1154 2554 1765 HOH   HOH B . 
W 10 HOH   1155 2555 458  HOH   HOH B . 
W 10 HOH   1156 2556 2102 HOH   HOH B . 
W 10 HOH   1157 2557 1895 HOH   HOH B . 
W 10 HOH   1158 2558 1696 HOH   HOH B . 
W 10 HOH   1159 2559 2411 HOH   HOH B . 
W 10 HOH   1160 2560 958  HOH   HOH B . 
W 10 HOH   1161 2561 690  HOH   HOH B . 
W 10 HOH   1162 2562 1853 HOH   HOH B . 
W 10 HOH   1163 2563 1315 HOH   HOH B . 
W 10 HOH   1164 2564 2429 HOH   HOH B . 
W 10 HOH   1165 2565 2049 HOH   HOH B . 
W 10 HOH   1166 2566 472  HOH   HOH B . 
W 10 HOH   1167 2567 2010 HOH   HOH B . 
W 10 HOH   1168 2568 2131 HOH   HOH B . 
W 10 HOH   1169 2569 1683 HOH   HOH B . 
W 10 HOH   1170 2570 2250 HOH   HOH B . 
W 10 HOH   1171 2571 1282 HOH   HOH B . 
W 10 HOH   1172 2572 243  HOH   HOH B . 
W 10 HOH   1173 2573 1357 HOH   HOH B . 
W 10 HOH   1174 2574 1879 HOH   HOH B . 
W 10 HOH   1175 2575 2082 HOH   HOH B . 
W 10 HOH   1176 2576 2231 HOH   HOH B . 
W 10 HOH   1177 2577 1938 HOH   HOH B . 
W 10 HOH   1178 2578 1437 HOH   HOH B . 
W 10 HOH   1179 2579 1336 HOH   HOH B . 
W 10 HOH   1180 2580 1851 HOH   HOH B . 
W 10 HOH   1181 2581 1500 HOH   HOH B . 
W 10 HOH   1182 2582 881  HOH   HOH B . 
W 10 HOH   1183 2583 1955 HOH   HOH B . 
W 10 HOH   1184 2584 1560 HOH   HOH B . 
W 10 HOH   1185 2585 2495 HOH   HOH B . 
W 10 HOH   1186 2586 1797 HOH   HOH B . 
W 10 HOH   1187 2587 2404 HOH   HOH B . 
W 10 HOH   1188 2588 1960 HOH   HOH B . 
W 10 HOH   1189 2589 1235 HOH   HOH B . 
W 10 HOH   1190 2590 593  HOH   HOH B . 
W 10 HOH   1191 2591 2276 HOH   HOH B . 
W 10 HOH   1192 2592 1321 HOH   HOH B . 
W 10 HOH   1193 2593 1947 HOH   HOH B . 
W 10 HOH   1194 2594 1809 HOH   HOH B . 
W 10 HOH   1195 2595 2447 HOH   HOH B . 
W 10 HOH   1196 2596 939  HOH   HOH B . 
W 10 HOH   1197 2597 1725 HOH   HOH B . 
W 10 HOH   1198 2598 2092 HOH   HOH B . 
W 10 HOH   1199 2599 1137 HOH   HOH B . 
W 10 HOH   1200 2600 1048 HOH   HOH B . 
W 10 HOH   1201 2601 1132 HOH   HOH B . 
W 10 HOH   1202 2602 1477 HOH   HOH B . 
W 10 HOH   1203 2603 545  HOH   HOH B . 
W 10 HOH   1204 2604 2379 HOH   HOH B . 
W 10 HOH   1205 2605 2389 HOH   HOH B . 
W 10 HOH   1206 2606 2396 HOH   HOH B . 
W 10 HOH   1207 2607 2302 HOH   HOH B . 
W 10 HOH   1208 2608 1881 HOH   HOH B . 
W 10 HOH   1209 2609 1067 HOH   HOH B . 
W 10 HOH   1210 2610 1940 HOH   HOH B . 
W 10 HOH   1211 2611 2311 HOH   HOH B . 
W 10 HOH   1212 2612 907  HOH   HOH B . 
W 10 HOH   1213 2613 1998 HOH   HOH B . 
W 10 HOH   1214 2614 1564 HOH   HOH B . 
W 10 HOH   1215 2615 1259 HOH   HOH B . 
W 10 HOH   1216 2616 2448 HOH   HOH B . 
W 10 HOH   1217 2617 1201 HOH   HOH B . 
W 10 HOH   1218 2618 1280 HOH   HOH B . 
W 10 HOH   1219 2619 1512 HOH   HOH B . 
W 10 HOH   1220 2620 2348 HOH   HOH B . 
W 10 HOH   1221 2621 1158 HOH   HOH B . 
W 10 HOH   1222 2622 1039 HOH   HOH B . 
W 10 HOH   1223 2623 798  HOH   HOH B . 
W 10 HOH   1224 2624 1629 HOH   HOH B . 
W 10 HOH   1225 2625 1680 HOH   HOH B . 
W 10 HOH   1226 2626 1689 HOH   HOH B . 
W 10 HOH   1227 2627 675  HOH   HOH B . 
W 10 HOH   1228 2628 1444 HOH   HOH B . 
W 10 HOH   1229 2629 2588 HOH   HOH B . 
W 10 HOH   1230 2630 651  HOH   HOH B . 
W 10 HOH   1231 2631 1676 HOH   HOH B . 
W 10 HOH   1232 2632 1775 HOH   HOH B . 
W 10 HOH   1233 2633 1405 HOH   HOH B . 
W 10 HOH   1234 2634 1515 HOH   HOH B . 
W 10 HOH   1235 2635 1485 HOH   HOH B . 
W 10 HOH   1236 2636 1352 HOH   HOH B . 
W 10 HOH   1237 2637 2086 HOH   HOH B . 
W 10 HOH   1238 2638 2326 HOH   HOH B . 
W 10 HOH   1239 2639 1639 HOH   HOH B . 
W 10 HOH   1240 2640 1902 HOH   HOH B . 
W 10 HOH   1241 2641 1788 HOH   HOH B . 
W 10 HOH   1242 2642 771  HOH   HOH B . 
W 10 HOH   1243 2643 177  HOH   HOH B . 
W 10 HOH   1244 2644 1203 HOH   HOH B . 
W 10 HOH   1245 2645 796  HOH   HOH B . 
W 10 HOH   1246 2646 1623 HOH   HOH B . 
W 10 HOH   1247 2647 2120 HOH   HOH B . 
W 10 HOH   1248 2648 1431 HOH   HOH B . 
W 10 HOH   1249 2649 807  HOH   HOH B . 
W 10 HOH   1250 2650 2165 HOH   HOH B . 
W 10 HOH   1251 2651 1197 HOH   HOH B . 
W 10 HOH   1252 2652 1291 HOH   HOH B . 
W 10 HOH   1253 2653 2341 HOH   HOH B . 
W 10 HOH   1254 2654 1390 HOH   HOH B . 
W 10 HOH   1255 2655 2274 HOH   HOH B . 
W 10 HOH   1256 2656 1996 HOH   HOH B . 
W 10 HOH   1257 2657 531  HOH   HOH B . 
W 10 HOH   1258 2658 2336 HOH   HOH B . 
W 10 HOH   1259 2659 1432 HOH   HOH B . 
W 10 HOH   1260 2660 2446 HOH   HOH B . 
W 10 HOH   1261 2661 2101 HOH   HOH B . 
W 10 HOH   1262 2662 2453 HOH   HOH B . 
W 10 HOH   1263 2663 1985 HOH   HOH B . 
W 10 HOH   1264 2664 1627 HOH   HOH B . 
W 10 HOH   1265 2665 2110 HOH   HOH B . 
W 10 HOH   1266 2666 2105 HOH   HOH B . 
W 10 HOH   1267 2667 2206 HOH   HOH B . 
W 10 HOH   1268 2668 852  HOH   HOH B . 
W 10 HOH   1269 2669 2061 HOH   HOH B . 
W 10 HOH   1270 2670 2452 HOH   HOH B . 
W 10 HOH   1271 2671 1832 HOH   HOH B . 
W 10 HOH   1272 2672 1552 HOH   HOH B . 
W 10 HOH   1273 2673 2333 HOH   HOH B . 
W 10 HOH   1274 2674 2057 HOH   HOH B . 
W 10 HOH   1275 2675 1347 HOH   HOH B . 
W 10 HOH   1276 2676 1666 HOH   HOH B . 
W 10 HOH   1277 2677 1339 HOH   HOH B . 
W 10 HOH   1278 2678 1796 HOH   HOH B . 
W 10 HOH   1279 2679 1933 HOH   HOH B . 
W 10 HOH   1280 2680 1141 HOH   HOH B . 
W 10 HOH   1281 2681 1161 HOH   HOH B . 
W 10 HOH   1282 2682 1897 HOH   HOH B . 
W 10 HOH   1283 2683 1324 HOH   HOH B . 
W 10 HOH   1284 2684 1916 HOH   HOH B . 
W 10 HOH   1285 2685 2420 HOH   HOH B . 
W 10 HOH   1286 2686 2439 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 52   ? CG  ? A GLU 54   CG  
2   1 Y 1 A GLU 52   ? CD  ? A GLU 54   CD  
3   1 Y 1 A GLU 52   ? OE1 ? A GLU 54   OE1 
4   1 Y 1 A GLU 52   ? OE2 ? A GLU 54   OE2 
5   1 Y 1 A GLU 59   ? CG  ? A GLU 61   CG  
6   1 Y 1 A GLU 59   ? CD  ? A GLU 61   CD  
7   1 Y 1 A GLU 59   ? OE1 ? A GLU 61   OE1 
8   1 Y 1 A GLU 59   ? OE2 ? A GLU 61   OE2 
9   1 Y 1 A HIS 79   ? CG  ? A HIS 81   CG  
10  1 Y 1 A HIS 79   ? ND1 ? A HIS 81   ND1 
11  1 Y 1 A HIS 79   ? CD2 ? A HIS 81   CD2 
12  1 Y 1 A HIS 79   ? CE1 ? A HIS 81   CE1 
13  1 Y 1 A HIS 79   ? NE2 ? A HIS 81   NE2 
14  1 Y 1 A SER 82   ? OG  ? A SER 84   OG  
15  1 Y 1 A GLU 85   ? CG  ? A GLU 87   CG  
16  1 Y 1 A GLU 85   ? CD  ? A GLU 87   CD  
17  1 Y 1 A GLU 85   ? OE1 ? A GLU 87   OE1 
18  1 Y 1 A GLU 85   ? OE2 ? A GLU 87   OE2 
19  1 Y 1 A GLN 89   ? CG  ? A GLN 91   CG  
20  1 Y 1 A GLN 89   ? CD  ? A GLN 91   CD  
21  1 Y 1 A GLN 89   ? OE1 ? A GLN 91   OE1 
22  1 Y 1 A GLN 89   ? NE2 ? A GLN 91   NE2 
23  1 Y 1 A ASP 113  ? CG  ? A ASP 115  CG  
24  1 Y 1 A ASP 113  ? OD1 ? A ASP 115  OD1 
25  1 Y 1 A ASP 113  ? OD2 ? A ASP 115  OD2 
26  1 Y 1 A ARG 122  ? CG  ? A ARG 124  CG  
27  1 Y 1 A ARG 122  ? CD  ? A ARG 124  CD  
28  1 Y 1 A ARG 122  ? NE  ? A ARG 124  NE  
29  1 Y 1 A ARG 122  ? CZ  ? A ARG 124  CZ  
30  1 Y 1 A ARG 122  ? NH1 ? A ARG 124  NH1 
31  1 Y 1 A ARG 122  ? NH2 ? A ARG 124  NH2 
32  1 Y 1 A ASP 127  ? CG  ? A ASP 129  CG  
33  1 Y 1 A ASP 127  ? OD1 ? A ASP 129  OD1 
34  1 Y 1 A ASP 127  ? OD2 ? A ASP 129  OD2 
35  1 Y 1 A ASN 129  ? CG  ? A ASN 131  CG  
36  1 Y 1 A ASN 129  ? OD1 ? A ASN 131  OD1 
37  1 Y 1 A ASN 129  ? ND2 ? A ASN 131  ND2 
38  1 Y 1 A LYS 131  ? CG  ? A LYS 133  CG  
39  1 Y 1 A LYS 131  ? CD  ? A LYS 133  CD  
40  1 Y 1 A LYS 131  ? CE  ? A LYS 133  CE  
41  1 Y 1 A LYS 131  ? NZ  ? A LYS 133  NZ  
42  1 Y 1 A SER 132  ? OG  ? A SER 134  OG  
43  1 Y 1 A SER 137  ? OG  ? A SER 139  OG  
44  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
45  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
46  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
47  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
48  1 Y 1 A THR 156  ? OG1 ? A THR 158  OG1 
49  1 Y 1 A THR 156  ? CG2 ? A THR 158  CG2 
50  1 Y 1 A GLN 194  ? CG  ? A GLN 196  CG  
51  1 Y 1 A GLN 194  ? CD  ? A GLN 196  CD  
52  1 Y 1 A GLN 194  ? OE1 ? A GLN 196  OE1 
53  1 Y 1 A GLN 194  ? NE2 ? A GLN 196  NE2 
54  1 Y 1 A LYS 206  ? CG  ? A LYS 208  CG  
55  1 Y 1 A LYS 206  ? CD  ? A LYS 208  CD  
56  1 Y 1 A LYS 206  ? CE  ? A LYS 208  CE  
57  1 Y 1 A LYS 206  ? NZ  ? A LYS 208  NZ  
58  1 Y 1 A LYS 209  ? CG  ? A LYS 211  CG  
59  1 Y 1 A LYS 209  ? CD  ? A LYS 211  CD  
60  1 Y 1 A LYS 209  ? CE  ? A LYS 211  CE  
61  1 Y 1 A LYS 209  ? NZ  ? A LYS 211  NZ  
62  1 Y 1 A GLU 213  ? CG  ? A GLU 215  CG  
63  1 Y 1 A GLU 213  ? CD  ? A GLU 215  CD  
64  1 Y 1 A GLU 213  ? OE1 ? A GLU 215  OE1 
65  1 Y 1 A GLU 213  ? OE2 ? A GLU 215  OE2 
66  1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
67  1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
68  1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
69  1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
70  1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
71  1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
72  1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
73  1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
74  1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
75  1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
76  1 Y 1 A GLU 480  ? CG  ? A GLU 482  CG  
77  1 Y 1 A GLU 480  ? CD  ? A GLU 482  CD  
78  1 Y 1 A GLU 480  ? OE1 ? A GLU 482  OE1 
79  1 Y 1 A GLU 480  ? OE2 ? A GLU 482  OE2 
80  1 Y 1 A ARG 489  ? CG  ? A ARG 491  CG  
81  1 Y 1 A ARG 489  ? CD  ? A ARG 491  CD  
82  1 Y 1 A ARG 489  ? NE  ? A ARG 491  NE  
83  1 Y 1 A ARG 489  ? CZ  ? A ARG 491  CZ  
84  1 Y 1 A ARG 489  ? NH1 ? A ARG 491  NH1 
85  1 Y 1 A ARG 489  ? NH2 ? A ARG 491  NH2 
86  1 Y 1 A ASN 496  ? CG  ? A ASN 498  CG  
87  1 Y 1 A ASN 496  ? OD1 ? A ASN 498  OD1 
88  1 Y 1 A ASN 496  ? ND2 ? A ASN 498  ND2 
89  1 Y 1 A LYS 507  ? CG  ? A LYS 509  CG  
90  1 Y 1 A LYS 507  ? CD  ? A LYS 509  CD  
91  1 Y 1 A LYS 507  ? CE  ? A LYS 509  CE  
92  1 Y 1 A LYS 507  ? NZ  ? A LYS 509  NZ  
93  1 Y 1 A ARG 533  ? CG  ? A ARG 535  CG  
94  1 Y 1 A ARG 533  ? CD  ? A ARG 535  CD  
95  1 Y 1 A ARG 533  ? NE  ? A ARG 535  NE  
96  1 Y 1 A ARG 533  ? CZ  ? A ARG 535  CZ  
97  1 Y 1 A ARG 533  ? NH1 ? A ARG 535  NH1 
98  1 Y 1 A ARG 533  ? NH2 ? A ARG 535  NH2 
99  1 Y 1 A LYS 573  ? CG  ? A LYS 575  CG  
100 1 Y 1 A LYS 573  ? CD  ? A LYS 575  CD  
101 1 Y 1 A LYS 573  ? CE  ? A LYS 575  CE  
102 1 Y 1 A LYS 573  ? NZ  ? A LYS 575  NZ  
103 1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
104 1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
105 1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
106 1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
107 1 Y 1 A GLU 611  ? CG  ? A GLU 613  CG  
108 1 Y 1 A GLU 611  ? CD  ? A GLU 613  CD  
109 1 Y 1 A GLU 611  ? OE1 ? A GLU 613  OE1 
110 1 Y 1 A GLU 611  ? OE2 ? A GLU 613  OE2 
111 1 Y 1 A SER 633  ? OG  ? A SER 635  OG  
112 1 Y 1 A GLU 785  ? CG  ? A GLU 787  CG  
113 1 Y 1 A GLU 785  ? CD  ? A GLU 787  CD  
114 1 Y 1 A GLU 785  ? OE1 ? A GLU 787  OE1 
115 1 Y 1 A GLU 785  ? OE2 ? A GLU 787  OE2 
116 1 Y 1 A LEU 824  ? CG  ? A LEU 826  CG  
117 1 Y 1 A LEU 824  ? CD1 ? A LEU 826  CD1 
118 1 Y 1 A LEU 824  ? CD2 ? A LEU 826  CD2 
119 1 Y 1 A ASP 855  ? CG  ? A ASP 857  CG  
120 1 Y 1 A ASP 855  ? OD1 ? A ASP 857  OD1 
121 1 Y 1 A ASP 855  ? OD2 ? A ASP 857  OD2 
122 1 Y 1 A LYS 897  ? CG  ? A LYS 899  CG  
123 1 Y 1 A LYS 897  ? CD  ? A LYS 899  CD  
124 1 Y 1 A LYS 897  ? CE  ? A LYS 899  CE  
125 1 Y 1 A LYS 897  ? NZ  ? A LYS 899  NZ  
126 1 Y 1 A GLU 932  ? CG  ? A GLU 934  CG  
127 1 Y 1 A GLU 932  ? CD  ? A GLU 934  CD  
128 1 Y 1 A GLU 932  ? OE1 ? A GLU 934  OE1 
129 1 Y 1 A GLU 932  ? OE2 ? A GLU 934  OE2 
130 1 Y 1 A LYS 933  ? CG  ? A LYS 935  CG  
131 1 Y 1 A LYS 933  ? CD  ? A LYS 935  CD  
132 1 Y 1 A LYS 933  ? CE  ? A LYS 935  CE  
133 1 Y 1 A LYS 933  ? NZ  ? A LYS 935  NZ  
134 1 Y 1 A GLN 938  ? CG  ? A GLN 940  CG  
135 1 Y 1 A GLN 938  ? CD  ? A GLN 940  CD  
136 1 Y 1 A GLN 938  ? OE1 ? A GLN 940  OE1 
137 1 Y 1 A GLN 938  ? NE2 ? A GLN 940  NE2 
138 1 Y 1 A ARG 939  ? CG  ? A ARG 941  CG  
139 1 Y 1 A ARG 939  ? CD  ? A ARG 941  CD  
140 1 Y 1 A ARG 939  ? NE  ? A ARG 941  NE  
141 1 Y 1 A ARG 939  ? CZ  ? A ARG 941  CZ  
142 1 Y 1 A ARG 939  ? NH1 ? A ARG 941  NH1 
143 1 Y 1 A ARG 939  ? NH2 ? A ARG 941  NH2 
144 1 Y 1 A ARG 952  ? CG  ? A ARG 954  CG  
145 1 Y 1 A ARG 952  ? CD  ? A ARG 954  CD  
146 1 Y 1 A ARG 952  ? NE  ? A ARG 954  NE  
147 1 Y 1 A ARG 952  ? CZ  ? A ARG 954  CZ  
148 1 Y 1 A ARG 952  ? NH1 ? A ARG 954  NH1 
149 1 Y 1 A ARG 952  ? NH2 ? A ARG 954  NH2 
150 1 Y 1 A ARG 1063 ? CG  ? A ARG 1065 CG  
151 1 Y 1 A ARG 1063 ? CD  ? A ARG 1065 CD  
152 1 Y 1 A ARG 1063 ? NE  ? A ARG 1065 NE  
153 1 Y 1 A ARG 1063 ? CZ  ? A ARG 1065 CZ  
154 1 Y 1 A ARG 1063 ? NH1 ? A ARG 1065 NH1 
155 1 Y 1 A ARG 1063 ? NH2 ? A ARG 1065 NH2 
156 1 Y 1 A LYS 1139 ? CG  ? A LYS 1141 CG  
157 1 Y 1 A LYS 1139 ? CD  ? A LYS 1141 CD  
158 1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
159 1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
160 1 Y 1 A GLN 1143 ? CG  ? A GLN 1145 CG  
161 1 Y 1 A GLN 1143 ? CD  ? A GLN 1145 CD  
162 1 Y 1 A GLN 1143 ? OE1 ? A GLN 1145 OE1 
163 1 Y 1 A GLN 1143 ? NE2 ? A GLN 1145 NE2 
164 1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
165 1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
166 1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
167 1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
168 1 Y 1 A SER 1228 ? OG  ? A SER 1230 OG  
169 1 Y 1 A MET 1230 ? CG  ? A MET 1232 CG  
170 1 Y 1 A MET 1230 ? SD  ? A MET 1232 SD  
171 1 Y 1 A MET 1230 ? CE  ? A MET 1232 CE  
172 1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
173 1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
174 1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
175 1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
176 1 Y 1 B LYS 58   ? CG  ? B LYS 60   CG  
177 1 Y 1 B LYS 58   ? CD  ? B LYS 60   CD  
178 1 Y 1 B LYS 58   ? CE  ? B LYS 60   CE  
179 1 Y 1 B LYS 58   ? NZ  ? B LYS 60   NZ  
180 1 Y 1 B GLU 59   ? CG  ? B GLU 61   CG  
181 1 Y 1 B GLU 59   ? CD  ? B GLU 61   CD  
182 1 Y 1 B GLU 59   ? OE1 ? B GLU 61   OE1 
183 1 Y 1 B GLU 59   ? OE2 ? B GLU 61   OE2 
184 1 Y 1 B SER 66   ? OG  ? B SER 68   OG  
185 1 Y 1 B GLU 85   ? CG  ? B GLU 87   CG  
186 1 Y 1 B GLU 85   ? CD  ? B GLU 87   CD  
187 1 Y 1 B GLU 85   ? OE1 ? B GLU 87   OE1 
188 1 Y 1 B GLU 85   ? OE2 ? B GLU 87   OE2 
189 1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
190 1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
191 1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
192 1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
193 1 Y 1 B THR 114  ? OG1 ? B THR 116  OG1 
194 1 Y 1 B THR 114  ? CG2 ? B THR 116  CG2 
195 1 Y 1 B ARG 122  ? CG  ? B ARG 124  CG  
196 1 Y 1 B ARG 122  ? CD  ? B ARG 124  CD  
197 1 Y 1 B ARG 122  ? NE  ? B ARG 124  NE  
198 1 Y 1 B ARG 122  ? CZ  ? B ARG 124  CZ  
199 1 Y 1 B ARG 122  ? NH1 ? B ARG 124  NH1 
200 1 Y 1 B ARG 122  ? NH2 ? B ARG 124  NH2 
201 1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
202 1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
203 1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
204 1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
205 1 Y 1 B ASP 127  ? CG  ? B ASP 129  CG  
206 1 Y 1 B ASP 127  ? OD1 ? B ASP 129  OD1 
207 1 Y 1 B ASP 127  ? OD2 ? B ASP 129  OD2 
208 1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
209 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
210 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
211 1 Y 1 B LYS 131  ? CG  ? B LYS 133  CG  
212 1 Y 1 B LYS 131  ? CD  ? B LYS 133  CD  
213 1 Y 1 B LYS 131  ? CE  ? B LYS 133  CE  
214 1 Y 1 B LYS 131  ? NZ  ? B LYS 133  NZ  
215 1 Y 1 B SER 132  ? OG  ? B SER 134  OG  
216 1 Y 1 B HIS 133  ? CG  ? B HIS 135  CG  
217 1 Y 1 B HIS 133  ? ND1 ? B HIS 135  ND1 
218 1 Y 1 B HIS 133  ? CD2 ? B HIS 135  CD2 
219 1 Y 1 B HIS 133  ? CE1 ? B HIS 135  CE1 
220 1 Y 1 B HIS 133  ? NE2 ? B HIS 135  NE2 
221 1 Y 1 B ARG 138  ? CG  ? B ARG 140  CG  
222 1 Y 1 B ARG 138  ? CD  ? B ARG 140  CD  
223 1 Y 1 B ARG 138  ? NE  ? B ARG 140  NE  
224 1 Y 1 B ARG 138  ? CZ  ? B ARG 140  CZ  
225 1 Y 1 B ARG 138  ? NH1 ? B ARG 140  NH1 
226 1 Y 1 B ARG 138  ? NH2 ? B ARG 140  NH2 
227 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
228 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
229 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
230 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
231 1 Y 1 B ARG 189  ? CG  ? B ARG 191  CG  
232 1 Y 1 B ARG 189  ? CD  ? B ARG 191  CD  
233 1 Y 1 B ARG 189  ? NE  ? B ARG 191  NE  
234 1 Y 1 B ARG 189  ? CZ  ? B ARG 191  CZ  
235 1 Y 1 B ARG 189  ? NH1 ? B ARG 191  NH1 
236 1 Y 1 B ARG 189  ? NH2 ? B ARG 191  NH2 
237 1 Y 1 B GLN 194  ? CG  ? B GLN 196  CG  
238 1 Y 1 B GLN 194  ? CD  ? B GLN 196  CD  
239 1 Y 1 B GLN 194  ? OE1 ? B GLN 196  OE1 
240 1 Y 1 B GLN 194  ? NE2 ? B GLN 196  NE2 
241 1 Y 1 B LYS 206  ? CG  ? B LYS 208  CG  
242 1 Y 1 B LYS 206  ? CD  ? B LYS 208  CD  
243 1 Y 1 B LYS 206  ? CE  ? B LYS 208  CE  
244 1 Y 1 B LYS 206  ? NZ  ? B LYS 208  NZ  
245 1 Y 1 B LYS 249  ? CG  ? B LYS 251  CG  
246 1 Y 1 B LYS 249  ? CD  ? B LYS 251  CD  
247 1 Y 1 B LYS 249  ? CE  ? B LYS 251  CE  
248 1 Y 1 B LYS 249  ? NZ  ? B LYS 251  NZ  
249 1 Y 1 B LYS 437  ? CG  ? B LYS 439  CG  
250 1 Y 1 B LYS 437  ? CD  ? B LYS 439  CD  
251 1 Y 1 B LYS 437  ? CE  ? B LYS 439  CE  
252 1 Y 1 B LYS 437  ? NZ  ? B LYS 439  NZ  
253 1 Y 1 B ASP 438  ? CG  ? B ASP 440  CG  
254 1 Y 1 B ASP 438  ? OD1 ? B ASP 440  OD1 
255 1 Y 1 B ASP 438  ? OD2 ? B ASP 440  OD2 
256 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
257 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
258 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
259 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
260 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
261 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
262 1 Y 1 B GLU 480  ? CG  ? B GLU 482  CG  
263 1 Y 1 B GLU 480  ? CD  ? B GLU 482  CD  
264 1 Y 1 B GLU 480  ? OE1 ? B GLU 482  OE1 
265 1 Y 1 B GLU 480  ? OE2 ? B GLU 482  OE2 
266 1 Y 1 B THR 481  ? OG1 ? B THR 483  OG1 
267 1 Y 1 B THR 481  ? CG2 ? B THR 483  CG2 
268 1 Y 1 B VAL 487  ? CG1 ? B VAL 489  CG1 
269 1 Y 1 B VAL 487  ? CG2 ? B VAL 489  CG2 
270 1 Y 1 B ARG 489  ? CG  ? B ARG 491  CG  
271 1 Y 1 B ARG 489  ? CD  ? B ARG 491  CD  
272 1 Y 1 B ARG 489  ? NE  ? B ARG 491  NE  
273 1 Y 1 B ARG 489  ? CZ  ? B ARG 491  CZ  
274 1 Y 1 B ARG 489  ? NH1 ? B ARG 491  NH1 
275 1 Y 1 B ARG 489  ? NH2 ? B ARG 491  NH2 
276 1 Y 1 B LEU 490  ? CG  ? B LEU 492  CG  
277 1 Y 1 B LEU 490  ? CD1 ? B LEU 492  CD1 
278 1 Y 1 B LEU 490  ? CD2 ? B LEU 492  CD2 
279 1 Y 1 B GLU 492  ? CG  ? B GLU 494  CG  
280 1 Y 1 B GLU 492  ? CD  ? B GLU 494  CD  
281 1 Y 1 B GLU 492  ? OE1 ? B GLU 494  OE1 
282 1 Y 1 B GLU 492  ? OE2 ? B GLU 494  OE2 
283 1 Y 1 B ASN 496  ? CG  ? B ASN 498  CG  
284 1 Y 1 B ASN 496  ? OD1 ? B ASN 498  OD1 
285 1 Y 1 B ASN 496  ? ND2 ? B ASN 498  ND2 
286 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
287 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
288 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
289 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
290 1 Y 1 B VAL 508  ? CG1 ? B VAL 510  CG1 
291 1 Y 1 B VAL 508  ? CG2 ? B VAL 510  CG2 
292 1 Y 1 B ARG 533  ? CG  ? B ARG 535  CG  
293 1 Y 1 B ARG 533  ? CD  ? B ARG 535  CD  
294 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
295 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
296 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
297 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
298 1 Y 1 B GLU 611  ? CG  ? B GLU 613  CG  
299 1 Y 1 B GLU 611  ? CD  ? B GLU 613  CD  
300 1 Y 1 B GLU 611  ? OE1 ? B GLU 613  OE1 
301 1 Y 1 B GLU 611  ? OE2 ? B GLU 613  OE2 
302 1 Y 1 B GLU 785  ? CG  ? B GLU 787  CG  
303 1 Y 1 B GLU 785  ? CD  ? B GLU 787  CD  
304 1 Y 1 B GLU 785  ? OE1 ? B GLU 787  OE1 
305 1 Y 1 B GLU 785  ? OE2 ? B GLU 787  OE2 
306 1 Y 1 B GLN 827  ? CG  ? B GLN 829  CG  
307 1 Y 1 B GLN 827  ? CD  ? B GLN 829  CD  
308 1 Y 1 B GLN 827  ? OE1 ? B GLN 829  OE1 
309 1 Y 1 B GLN 827  ? NE2 ? B GLN 829  NE2 
310 1 Y 1 B GLU 854  ? CG  ? B GLU 856  CG  
311 1 Y 1 B GLU 854  ? CD  ? B GLU 856  CD  
312 1 Y 1 B GLU 854  ? OE1 ? B GLU 856  OE1 
313 1 Y 1 B GLU 854  ? OE2 ? B GLU 856  OE2 
314 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
315 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
316 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
317 1 Y 1 B GLU 890  ? CG  ? B GLU 892  CG  
318 1 Y 1 B GLU 890  ? CD  ? B GLU 892  CD  
319 1 Y 1 B GLU 890  ? OE1 ? B GLU 892  OE1 
320 1 Y 1 B GLU 890  ? OE2 ? B GLU 892  OE2 
321 1 Y 1 B LEU 914  ? CG  ? B LEU 916  CG  
322 1 Y 1 B LEU 914  ? CD1 ? B LEU 916  CD1 
323 1 Y 1 B LEU 914  ? CD2 ? B LEU 916  CD2 
324 1 Y 1 B SER 916  ? OG  ? B SER 918  OG  
325 1 Y 1 B GLU 917  ? CG  ? B GLU 919  CG  
326 1 Y 1 B GLU 917  ? CD  ? B GLU 919  CD  
327 1 Y 1 B GLU 917  ? OE1 ? B GLU 919  OE1 
328 1 Y 1 B GLU 917  ? OE2 ? B GLU 919  OE2 
329 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
330 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
331 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
332 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
333 1 Y 1 B LYS 933  ? CG  ? B LYS 935  CG  
334 1 Y 1 B LYS 933  ? CD  ? B LYS 935  CD  
335 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
336 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
337 1 Y 1 B GLN 938  ? CG  ? B GLN 940  CG  
338 1 Y 1 B GLN 938  ? CD  ? B GLN 940  CD  
339 1 Y 1 B GLN 938  ? OE1 ? B GLN 940  OE1 
340 1 Y 1 B GLN 938  ? NE2 ? B GLN 940  NE2 
341 1 Y 1 B ARG 952  ? CG  ? B ARG 954  CG  
342 1 Y 1 B ARG 952  ? CD  ? B ARG 954  CD  
343 1 Y 1 B ARG 952  ? NE  ? B ARG 954  NE  
344 1 Y 1 B ARG 952  ? CZ  ? B ARG 954  CZ  
345 1 Y 1 B ARG 952  ? NH1 ? B ARG 954  NH1 
346 1 Y 1 B ARG 952  ? NH2 ? B ARG 954  NH2 
347 1 Y 1 B ARG 958  ? CG  ? B ARG 960  CG  
348 1 Y 1 B ARG 958  ? CD  ? B ARG 960  CD  
349 1 Y 1 B ARG 958  ? NE  ? B ARG 960  NE  
350 1 Y 1 B ARG 958  ? CZ  ? B ARG 960  CZ  
351 1 Y 1 B ARG 958  ? NH1 ? B ARG 960  NH1 
352 1 Y 1 B ARG 958  ? NH2 ? B ARG 960  NH2 
353 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
354 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
355 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
356 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
357 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
358 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
359 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
360 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
361 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
362 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
363 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
364 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
365 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
366 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
367 1 Y 1 B LEU 1147 ? CG  ? B LEU 1149 CG  
368 1 Y 1 B LEU 1147 ? CD1 ? B LEU 1149 CD1 
369 1 Y 1 B LEU 1147 ? CD2 ? B LEU 1149 CD2 
370 1 Y 1 B LYS 1153 ? CG  ? B LYS 1155 CG  
371 1 Y 1 B LYS 1153 ? CD  ? B LYS 1155 CD  
372 1 Y 1 B LYS 1153 ? CE  ? B LYS 1155 CE  
373 1 Y 1 B LYS 1153 ? NZ  ? B LYS 1155 NZ  
374 1 Y 1 B SER 1228 ? OG  ? B SER 1230 OG  
375 1 Y 1 B MET 1230 ? CG  ? B MET 1232 CG  
376 1 Y 1 B MET 1230 ? SD  ? B MET 1232 SD  
377 1 Y 1 B MET 1230 ? CE  ? B MET 1232 CE  
# 
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                     9E0A 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.715 
_cell.length_a_esd                 ? 
_cell.length_b                     102.066 
_cell.length_b_esd                 ? 
_cell.length_c                     126.176 
_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                         9E0A 
_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                   9E0A 
_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             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.83 
_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 18% (w/v) PEG 3350. Enzyme was incubated with 24 mM 1,4-benzenedimethanol. Crystal was soaked in cryobuffer containing 50 mM 1,4-benzenedimethanol 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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-16 
_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   1.00008 
_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 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00008 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9E0A 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.39 
_reflns.d_resolution_low                               48.31 
_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                                     946557 
_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                           98.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.96 
_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                                0.080 
_reflns.pdbx_Rpim_I_all                                0.030 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.074 
_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                                    1.39 
_reflns_shell.d_res_low                                     1.41 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           161024 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             23190 
_reflns_shell.percent_possible_obs                          95.9 
_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                               6.9 
_reflns_shell.pdbx_chi_squared                              0.66 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.7 
_reflns_shell.pdbx_Rrim_I_all                               2.694 
_reflns_shell.pdbx_Rpim_I_all                               1.009 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.332 
_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                                  2.493 
_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                                 9E0A 
_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                            1.39 
_refine.ls_d_res_low                             47.03 
_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                     946557 
_refine.ls_number_reflns_R_free                  47595 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.54 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1728 
_refine.ls_R_factor_R_free                       0.1909 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1718 
_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                 21.74 
_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                            0.17 
_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        17877 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         273 
_refine_hist.number_atoms_solvent             2520 
_refine_hist.number_atoms_total               20670 
_refine_hist.d_res_high                       1.39 
_refine_hist.d_res_low                        47.03 
# 
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' ? 0.005  ? 18865 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.912  ? 25783 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.526 ? 7084  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.069  ? 3021  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3338  ? 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' 1.39 1.41  . . 1529 29082 95.00  . . . . 0.3340 . . . . . . . . . . . 0.3399 
'X-RAY DIFFRACTION' 1.41 1.42  . . 1529 29641 96.00  . . . . 0.3183 . . . . . . . . . . . 0.3310 
'X-RAY DIFFRACTION' 1.42 1.44  . . 1540 29916 97.00  . . . . 0.3120 . . . . . . . . . . . 0.3152 
'X-RAY DIFFRACTION' 1.44 1.46  . . 1523 30050 98.00  . . . . 0.3013 . . . . . . . . . . . 0.3055 
'X-RAY DIFFRACTION' 1.46 1.48  . . 1638 30164 98.00  . . . . 0.2954 . . . . . . . . . . . 0.3210 
'X-RAY DIFFRACTION' 1.48 1.50  . . 1624 30040 98.00  . . . . 0.2898 . . . . . . . . . . . 0.3130 
'X-RAY DIFFRACTION' 1.50 1.52  . . 1565 30187 98.00  . . . . 0.2713 . . . . . . . . . . . 0.2972 
'X-RAY DIFFRACTION' 1.52 1.54  . . 1685 30073 98.00  . . . . 0.2542 . . . . . . . . . . . 0.2632 
'X-RAY DIFFRACTION' 1.54 1.57  . . 1693 30086 98.00  . . . . 0.2500 . . . . . . . . . . . 0.2683 
'X-RAY DIFFRACTION' 1.57 1.59  . . 1551 30387 99.00  . . . . 0.2327 . . . . . . . . . . . 0.2584 
'X-RAY DIFFRACTION' 1.59 1.62  . . 1663 30113 98.00  . . . . 0.2258 . . . . . . . . . . . 0.2481 
'X-RAY DIFFRACTION' 1.62 1.65  . . 1676 30145 98.00  . . . . 0.2156 . . . . . . . . . . . 0.2363 
'X-RAY DIFFRACTION' 1.65 1.68  . . 1606 30180 98.00  . . . . 0.2111 . . . . . . . . . . . 0.2332 
'X-RAY DIFFRACTION' 1.68 1.71  . . 1644 30270 99.00  . . . . 0.2133 . . . . . . . . . . . 0.2362 
'X-RAY DIFFRACTION' 1.71 1.75  . . 1668 30259 99.00  . . . . 0.2024 . . . . . . . . . . . 0.2140 
'X-RAY DIFFRACTION' 1.75 1.79  . . 1495 30109 98.00  . . . . 0.1980 . . . . . . . . . . . 0.2269 
'X-RAY DIFFRACTION' 1.79 1.84  . . 1470 28715 93.00  . . . . 0.1861 . . . . . . . . . . . 0.2069 
'X-RAY DIFFRACTION' 1.84 1.89  . . 1601 29230 95.00  . . . . 0.1858 . . . . . . . . . . . 0.2196 
'X-RAY DIFFRACTION' 1.89 1.94  . . 1507 30345 98.00  . . . . 0.1856 . . . . . . . . . . . 0.2050 
'X-RAY DIFFRACTION' 1.94 2.00  . . 1537 30410 99.00  . . . . 0.1793 . . . . . . . . . . . 0.1967 
'X-RAY DIFFRACTION' 2.00 2.08  . . 1640 30167 98.00  . . . . 0.1692 . . . . . . . . . . . 0.1950 
'X-RAY DIFFRACTION' 2.08 2.16  . . 1661 30274 99.00  . . . . 0.1647 . . . . . . . . . . . 0.1949 
'X-RAY DIFFRACTION' 2.16 2.26  . . 1569 30196 98.00  . . . . 0.1621 . . . . . . . . . . . 0.1802 
'X-RAY DIFFRACTION' 2.26 2.38  . . 1515 30373 98.00  . . . . 0.1641 . . . . . . . . . . . 0.1942 
'X-RAY DIFFRACTION' 2.38 2.53  . . 1682 30094 98.00  . . . . 0.1599 . . . . . . . . . . . 0.1762 
'X-RAY DIFFRACTION' 2.53 2.72  . . 1547 30208 98.00  . . . . 0.1596 . . . . . . . . . . . 0.1762 
'X-RAY DIFFRACTION' 2.72 2.99  . . 1558 29770 97.00  . . . . 0.1622 . . . . . . . . . . . 0.1911 
'X-RAY DIFFRACTION' 2.99 3.43  . . 1450 27536 90.00  . . . . 0.1575 . . . . . . . . . . . 0.1748 
'X-RAY DIFFRACTION' 3.43 4.32  . . 1573 30310 99.00  . . . . 0.1340 . . . . . . . . . . . 0.1470 
'X-RAY DIFFRACTION' 4.32 47.03 . . 1656 30632 100.00 . . . . 0.1372 . . . . . . . . . . . 0.1500 
# 
_struct.entry_id                     9E0A 
_struct.title                        'Structure of proline utilization A complexed with 1,4-benzenedimethanol' 
_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        9E0A 
_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 4  ? 
G N N 5  ? 
H N N 6  ? 
I N N 6  ? 
J N N 6  ? 
K N N 6  ? 
L N N 6  ? 
M N N 7  ? 
N N N 2  ? 
O N N 8  ? 
P N N 3  ? 
Q N N 9  ? 
R N N 4  ? 
S N N 5  ? 
T N N 6  ? 
U N N 7  ? 
V N N 10 ? 
W N N 10 ? 
# 
_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 9E0A A 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
2 1 9E0A 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 9E0A SER A 1 ? UNP F7X6I3 ? ? 'expression tag' -1 1 
1 9E0A MET A 2 ? UNP F7X6I3 ? ? 'expression tag' 0  2 
2 9E0A SER B 1 ? UNP F7X6I3 ? ? 'expression tag' -1 3 
2 9E0A 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)' 11230 ? 
1 MORE         -139  ? 
1 'SSA (A^2)'  77170 ? 
# 
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 
2 1 A,C,D,E,F,G,H,I,J,K,L,M,V                     
3 1 B,N,O,P,Q,R,S,T,U,W                           
# 
_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   ? THR A 57   ? PRO A 42   THR A 55   1 ? 14 
HELX_P HELX_P3   AA3 SER A 59   ? HIS A 81   ? SER A 57   HIS A 79   1 ? 23 
HELX_P HELX_P4   AA4 GLY A 85   ? TYR A 93   ? GLY A 83   TYR A 91   1 ? 9  
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 ASN A 131  ? LEU A 136  ? ASN A 129  LEU A 134  1 ? 6  
HELX_P HELX_P8   AA8 ASN A 145  ? GLY A 155  ? ASN A 143  GLY A 153  1 ? 11 
HELX_P HELX_P9   AA9 ASN A 162  ? GLN A 196  ? ASN A 160  GLN A 194  1 ? 35 
HELX_P HELX_P10  AB1 THR A 202  ? GLU A 215  ? THR A 200  GLU A 213  1 ? 14 
HELX_P HELX_P11  AB2 THR A 231  ? ALA A 254  ? THR A 229  ALA A 252  1 ? 24 
HELX_P HELX_P12  AB3 ARG A 256  ? GLY A 261  ? ARG A 254  GLY A 259  1 ? 6  
HELX_P HELX_P13  AB4 LYS A 267  ? LEU A 271  ? LYS A 265  LEU A 269  5 ? 5  
HELX_P HELX_P14  AB5 SER A 276  ? ALA A 278  ? SER A 274  ALA A 276  5 ? 3  
HELX_P HELX_P15  AB6 GLN A 279  ? ASP A 302  ? GLN A 277  ASP A 300  1 ? 24 
HELX_P HELX_P16  AB7 GLU A 311  ? ASP A 313  ? GLU A 309  ASP A 311  5 ? 3  
HELX_P HELX_P17  AB8 ARG A 314  ? ASP A 328  ? ARG A 312  ASP A 326  1 ? 15 
HELX_P HELX_P18  AB9 GLY A 329  ? SER A 332  ? GLY A 327  SER A 330  5 ? 4  
HELX_P HELX_P19  AC1 ARG A 347  ? GLY A 363  ? ARG A 345  GLY A 361  1 ? 17 
HELX_P HELX_P20  AC2 TYR A 375  ? GLY A 387  ? TYR A 373  GLY A 385  1 ? 13 
HELX_P HELX_P21  AC3 ARG A 396  ? ALA A 413  ? ARG A 394  ALA A 411  1 ? 18 
HELX_P HELX_P22  AC4 ASN A 426  ? GLY A 438  ? ASN A 424  GLY A 436  1 ? 13 
HELX_P HELX_P23  AC5 GLY A 455  ? GLU A 460  ? GLY A 453  GLU A 458  1 ? 6  
HELX_P HELX_P24  AC6 THR A 480  ? ALA A 486  ? THR A 478  ALA A 484  1 ? 7  
HELX_P HELX_P25  AC7 TYR A 487  ? ALA A 497  ? TYR A 485  ALA A 495  1 ? 11 
HELX_P HELX_P26  AC8 SER A 500  ? ASN A 506  ? SER A 498  ASN A 504  1 ? 7  
HELX_P HELX_P27  AC9 SER A 511  ? ILE A 516  ? SER A 509  ILE A 514  1 ? 6  
HELX_P HELX_P28  AD1 ASP A 518  ? ALA A 525  ? ASP A 516  ALA A 523  1 ? 8  
HELX_P HELX_P29  AD2 LEU A 538  ? LEU A 542  ? LEU A 536  LEU A 540  5 ? 5  
HELX_P HELX_P30  AD3 PHE A 543  ? ARG A 547  ? PHE A 541  ARG A 545  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  ? ASP A 798  ? SER A 783  ASP A 796  1 ? 14 
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 ? LYS A 1062 ? ASP A 1047 LYS A 1060 1 ? 14 
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 1171 ? ALA A 1184 ? ASP A 1169 ALA A 1182 1 ? 14 
HELX_P HELX_P58  AG4 SER A 1196 ? ASN A 1203 ? SER A 1194 ASN A 1201 1 ? 8  
HELX_P HELX_P59  AG5 CYS A 1208 ? TRP A 1211 ? CYS A 1206 TRP A 1209 5 ? 4  
HELX_P HELX_P60  AG6 ALA A 1229 ? ILE A 1234 ? ALA A 1227 ILE A 1232 5 ? 6  
HELX_P HELX_P61  AG7 SER B 31   ? ALA B 40   ? SER B 29   ALA B 38   1 ? 10 
HELX_P HELX_P62  AG8 PRO B 44   ? THR B 57   ? PRO B 42   THR B 55   1 ? 14 
HELX_P HELX_P63  AG9 SER B 59   ? LYS B 80   ? SER B 57   LYS B 78   1 ? 22 
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 ASN B 131  ? LEU B 136  ? ASN B 129  LEU B 134  1 ? 6  
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  ? GLY B 217  ? THR B 200  GLY B 215  1 ? 16 
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  ? HIS B 272  ? LYS B 265  HIS B 270  5 ? 6  
HELX_P HELX_P74  AI2 SER B 276  ? ALA B 278  ? SER B 274  ALA B 276  5 ? 3  
HELX_P HELX_P75  AI3 GLN B 279  ? ASP B 302  ? GLN B 277  ASP B 300  1 ? 24 
HELX_P HELX_P76  AI4 GLU B 311  ? ASP B 313  ? GLU B 309  ASP B 311  5 ? 3  
HELX_P HELX_P77  AI5 ARG B 314  ? ASP B 328  ? ARG B 312  ASP B 326  1 ? 15 
HELX_P HELX_P78  AI6 GLY B 329  ? SER B 332  ? GLY B 327  SER B 330  5 ? 4  
HELX_P HELX_P79  AI7 ARG B 347  ? GLY B 363  ? ARG B 345  GLY B 361  1 ? 17 
HELX_P HELX_P80  AI8 TYR B 375  ? GLY B 387  ? TYR B 373  GLY B 385  1 ? 13 
HELX_P HELX_P81  AI9 ARG B 396  ? ALA B 413  ? ARG B 394  ALA B 411  1 ? 18 
HELX_P HELX_P82  AJ1 ASN B 426  ? ALA B 437  ? ASN B 424  ALA B 435  1 ? 12 
HELX_P HELX_P83  AJ2 GLY B 455  ? GLU B 460  ? GLY B 453  GLU B 458  1 ? 6  
HELX_P HELX_P84  AJ3 THR B 480  ? ALA B 486  ? THR B 478  ALA B 484  1 ? 7  
HELX_P HELX_P85  AJ4 TYR B 487  ? GLU B 494  ? TYR B 485  GLU B 492  1 ? 8  
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  ? ILE B 516  ? SER B 509  ILE B 514  1 ? 6  
HELX_P HELX_P88  AJ7 ASP B 518  ? ALA B 525  ? ASP B 516  ALA B 523  1 ? 8  
HELX_P HELX_P89  AJ8 LEU B 538  ? LEU B 542  ? LEU B 536  LEU B 540  5 ? 5  
HELX_P HELX_P90  AJ9 PHE B 543  ? ARG B 547  ? PHE B 541  ARG B 545  5 ? 5  
HELX_P HELX_P91  AK1 ASN B 557  ? ALA B 573  ? ASN B 555  ALA B 571  1 ? 17 
HELX_P HELX_P92  AK2 SER B 611  ? ALA B 631  ? SER B 609  ALA B 629  1 ? 21 
HELX_P HELX_P93  AK3 PRO B 633  ? ARG B 651  ? PRO B 631  ARG B 649  1 ? 19 
HELX_P HELX_P94  AK4 ARG B 651  ? GLY B 664  ? ARG B 649  GLY B 662  1 ? 14 
HELX_P HELX_P95  AK5 SER B 666  ? LEU B 692  ? SER B 664  LEU B 690  1 ? 27 
HELX_P HELX_P96  AK6 LEU B 712  ? ALA B 725  ? LEU B 710  ALA B 723  1 ? 14 
HELX_P HELX_P97  AK7 THR B 737  ? ALA B 751  ? THR B 735  ALA B 749  1 ? 15 
HELX_P HELX_P98  AK8 PRO B 754  ? SER B 756  ? PRO B 752  SER B 754  5 ? 3  
HELX_P HELX_P99  AK9 ASP B 764  ? ALA B 774  ? ASP B 762  ALA B 772  1 ? 11 
HELX_P HELX_P100 AL1 SER B 785  ? ASP B 798  ? SER B 783  ASP B 796  1 ? 14 
HELX_P HELX_P101 AL2 LEU B 826  ? ASP B 840  ? LEU B 824  ASP B 838  1 ? 15 
HELX_P HELX_P102 AL3 SER B 841  ? GLN B 844  ? SER B 839  GLN B 842  5 ? 4  
HELX_P HELX_P103 AL4 GLU B 856  ? HIS B 871  ? GLU B 854  HIS B 869  1 ? 16 
HELX_P HELX_P104 AL5 THR B 890  ? LEU B 907  ? THR B 888  LEU B 905  1 ? 18 
HELX_P HELX_P105 AL6 ALA B 917  ? GLY B 923  ? ALA B 915  GLY B 921  5 ? 7  
HELX_P HELX_P106 AL7 LYS B 935  ? LEU B 939  ? LYS B 933  LEU B 937  5 ? 5  
HELX_P HELX_P107 AL8 ARG B 954  ? ASP B 956  ? ARG B 952  ASP B 954  5 ? 3  
HELX_P HELX_P108 AL9 ASP B 957  ? ALA B 967  ? ASP B 955  ALA B 965  1 ? 11 
HELX_P HELX_P109 AM1 LEU B 980  ? ILE B 991  ? LEU B 978  ILE B 989  1 ? 12 
HELX_P HELX_P110 AM2 ARG B 1015 ? GLY B 1019 ? ARG B 1013 GLY B 1017 5 ? 5  
HELX_P HELX_P111 AM3 TYR B 1029 ? VAL B 1034 ? TYR B 1027 VAL B 1032 5 ? 6  
HELX_P HELX_P112 AM4 ASP B 1049 ? LYS B 1062 ? ASP B 1047 LYS B 1060 1 ? 14 
HELX_P HELX_P113 AM5 ALA B 1064 ? SER B 1078 ? ALA B 1062 SER B 1076 1 ? 15 
HELX_P HELX_P114 AM6 THR B 1110 ? THR B 1124 ? THR B 1108 THR B 1122 1 ? 15 
HELX_P HELX_P115 AM7 ALA B 1133 ? GLY B 1135 ? ALA B 1131 GLY B 1133 5 ? 3  
HELX_P HELX_P116 AM8 LEU B 1136 ? LYS B 1141 ? LEU B 1134 LYS B 1139 5 ? 6  
HELX_P HELX_P117 AM9 PRO B 1144 ? LEU B 1149 ? PRO B 1142 LEU B 1147 1 ? 6  
HELX_P HELX_P118 AN1 ASP B 1156 ? GLY B 1161 ? ASP B 1154 GLY B 1159 1 ? 6  
HELX_P HELX_P119 AN2 ASP B 1171 ? ALA B 1184 ? ASP B 1169 ALA B 1182 1 ? 14 
HELX_P HELX_P120 AN3 SER B 1196 ? ASN B 1203 ? SER B 1194 ASN B 1201 1 ? 8  
HELX_P HELX_P121 AN4 CYS B 1208 ? TRP B 1211 ? CYS B 1206 TRP B 1209 5 ? 4  
HELX_P HELX_P122 AN5 ALA B 1229 ? ALA B 1233 ? ALA B 1227 ALA B 1231 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? G NAD . O2A ? ? ? 1_555 M MG  . MG ? ? A NAD 1305 A MG  1311 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc2  metalc ? ? M MG  . MG  ? ? ? 1_555 V HOH . O  ? ? A MG  1311 A HOH 1611 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc3  metalc ? ? M MG  . MG  ? ? ? 1_555 V HOH . O  ? ? A MG  1311 A HOH 1727 1_555 ? ? ? ? ? ? ? 2.148 ? ? 
metalc4  metalc ? ? M MG  . MG  ? ? ? 1_555 V HOH . O  ? ? A MG  1311 A HOH 2004 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc5  metalc ? ? M MG  . MG  ? ? ? 1_555 V HOH . O  ? ? A MG  1311 A HOH 2267 1_555 ? ? ? ? ? ? ? 2.155 ? ? 
metalc6  metalc ? ? M MG  . MG  ? ? ? 1_555 V HOH . O  ? ? A MG  1311 A HOH 2397 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc7  metalc ? ? S NAD . O2A ? ? ? 1_555 U MG  . MG ? ? B NAD 1306 B MG  1308 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc8  metalc ? ? U MG  . MG  ? ? ? 1_555 W HOH . O  ? ? B MG  1308 B HOH 1581 1_555 ? ? ? ? ? ? ? 1.971 ? ? 
metalc9  metalc ? ? U MG  . MG  ? ? ? 1_555 W HOH . O  ? ? B MG  1308 B HOH 1857 1_555 ? ? ? ? ? ? ? 1.905 ? ? 
metalc10 metalc ? ? U MG  . MG  ? ? ? 1_555 W HOH . O  ? ? B MG  1308 B HOH 2074 1_555 ? ? ? ? ? ? ? 2.256 ? ? 
metalc11 metalc ? ? U MG  . MG  ? ? ? 1_555 W HOH . O  ? ? B MG  1308 B HOH 2297 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc12 metalc ? ? U MG  . MG  ? ? ? 1_555 W HOH . O  ? ? B MG  1308 B HOH 2468 1_555 ? ? ? ? ? ? ? 1.946 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? G NAD . ? A NAD 1305 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 1611 ? 1_555 86.5  ? 
2  O2A ? G NAD . ? A NAD 1305 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 1727 ? 1_555 90.4  ? 
3  O   ? V HOH . ? A HOH 1611 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 1727 ? 1_555 92.0  ? 
4  O2A ? G NAD . ? A NAD 1305 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2004 ? 1_555 88.3  ? 
5  O   ? V HOH . ? A HOH 1611 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2004 ? 1_555 93.1  ? 
6  O   ? V HOH . ? A HOH 1727 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2004 ? 1_555 174.6 ? 
7  O2A ? G NAD . ? A NAD 1305 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2267 ? 1_555 93.9  ? 
8  O   ? V HOH . ? A HOH 1611 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2267 ? 1_555 179.6 ? 
9  O   ? V HOH . ? A HOH 1727 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2267 ? 1_555 88.1  ? 
10 O   ? V HOH . ? A HOH 2004 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2267 ? 1_555 86.8  ? 
11 O2A ? G NAD . ? A NAD 1305 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2397 ? 1_555 176.3 ? 
12 O   ? V HOH . ? A HOH 1611 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2397 ? 1_555 89.8  ? 
13 O   ? V HOH . ? A HOH 1727 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2397 ? 1_555 89.4  ? 
14 O   ? V HOH . ? A HOH 2004 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2397 ? 1_555 92.2  ? 
15 O   ? V HOH . ? A HOH 2267 ? 1_555 MG ? M MG . ? A MG 1311 ? 1_555 O ? V HOH . ? A HOH 2397 ? 1_555 89.7  ? 
16 O2A ? S NAD . ? B NAD 1306 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 1581 ? 1_555 93.4  ? 
17 O2A ? S NAD . ? B NAD 1306 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 1857 ? 1_555 96.3  ? 
18 O   ? W HOH . ? B HOH 1581 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 1857 ? 1_555 106.3 ? 
19 O2A ? S NAD . ? B NAD 1306 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2074 ? 1_555 83.2  ? 
20 O   ? W HOH . ? B HOH 1581 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2074 ? 1_555 87.3  ? 
21 O   ? W HOH . ? B HOH 1857 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2074 ? 1_555 166.3 ? 
22 O2A ? S NAD . ? B NAD 1306 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2297 ? 1_555 89.4  ? 
23 O   ? W HOH . ? B HOH 1581 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2297 ? 1_555 167.6 ? 
24 O   ? W HOH . ? B HOH 1857 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2297 ? 1_555 85.3  ? 
25 O   ? W HOH . ? B HOH 2074 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2297 ? 1_555 81.0  ? 
26 O2A ? S NAD . ? B NAD 1306 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2468 ? 1_555 166.6 ? 
27 O   ? W HOH . ? B HOH 1581 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2468 ? 1_555 93.4  ? 
28 O   ? W HOH . ? B HOH 1857 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2468 ? 1_555 92.8  ? 
29 O   ? W HOH . ? B HOH 2074 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2468 ? 1_555 85.6  ? 
30 O   ? W HOH . ? B HOH 2297 ? 1_555 MG ? U MG . ? B MG 1308 ? 1_555 O ? W HOH . ? B HOH 2468 ? 1_555 81.7  ? 
# 
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 -3.42 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 0.73  
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -3.21 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 2.58  
# 
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  LYS A 910  ? GLN A 913  ? LYS A 908  GLN A 911  
AA5 2  THR A 929  ? GLU A 932  ? THR A 927  GLU A 930  
AA5 3  VAL A 947  ? TYR A 953  ? VAL A 945  TYR A 951  
AA5 4  LEU A 849  ? GLN A 855  ? LEU A 847  GLN A 853  
AA5 5  ASN A 817  ? VAL A 821  ? ASN A 815  VAL A 819  
AA5 6  THR A 973  ? HIS A 977  ? THR A 971  HIS A 975  
AA5 7  ASN A 995  ? ILE A 998  ? ASN A 993  ILE A 996  
AA5 8  VAL A 1213 ? ASN A 1221 ? VAL A 1211 ASN A 1219 
AA5 9  GLU A 1092 ? ALA A 1100 ? GLU A 1090 ALA A 1098 
AA5 10 ASP A 1083 ? LEU A 1086 ? ASP A 1081 LEU A 1084 
AA6 1  VAL A 1151 ? SER A 1154 ? VAL A 1149 SER A 1152 
AA6 2  SER A 1127 ? ASP A 1131 ? SER A 1125 ASP A 1129 
AA6 3  ARG A 1103 ? VAL A 1107 ? ARG A 1101 VAL A 1105 
AA6 4  GLY A 1165 ? GLU A 1169 ? GLY A 1163 GLU A 1167 
AA6 5  VAL A 1192 ? ALA A 1195 ? VAL A 1190 ALA A 1193 
AA7 1  PHE B 218  ? ASP B 223  ? PHE B 216  ASP B 221  
AA7 2  GLY B 263  ? ILE B 266  ? GLY B 261  ILE B 264  
AA7 3  LEU B 305  ? ILE B 307  ? LEU B 303  ILE B 305  
AA7 4  MET B 337  ? GLN B 342  ? MET B 335  GLN B 340  
AA7 5  ILE B 366  ? VAL B 371  ? ILE B 364  VAL B 369  
AA7 6  VAL B 418  ? ALA B 423  ? VAL B 416  ALA B 421  
AA7 7  GLU B 447  ? LEU B 451  ? GLU B 445  LEU B 449  
AA7 8  CYS B 472  ? PRO B 477  ? CYS B 470  PRO B 475  
AA7 9  PHE B 218  ? ASP B 223  ? PHE B 216  ASP B 221  
AA8 1  TRP B 576  ? ALA B 578  ? TRP B 574  ALA B 576  
AA8 2  ASP B 599  ? GLU B 609  ? ASP B 597  GLU B 607  
AA8 3  GLU B 590  ? ASN B 596  ? GLU B 588  ASN B 594  
AA9 1  GLN B 581  ? LEU B 582  ? GLN B 579  LEU B 580  
AA9 2  GLY B 585  ? PRO B 586  ? GLY B 583  PRO B 584  
AB1 1  LEU B 758  ? LEU B 760  ? LEU B 756  LEU B 758  
AB1 2  VAL B 729  ? LYS B 732  ? VAL B 727  LYS B 730  
AB1 3  ILE B 702  ? ILE B 705  ? ILE B 700  ILE B 703  
AB1 4  GLY B 779  ? THR B 783  ? GLY B 777  THR B 781  
AB1 5  LEU B 809  ? GLU B 812  ? LEU B 807  GLU B 810  
AB2 1  VAL B 911  ? GLN B 913  ? VAL B 909  GLN B 911  
AB2 2  THR B 929  ? GLU B 932  ? THR B 927  GLU B 930  
AB2 3  VAL B 947  ? TYR B 953  ? VAL B 945  TYR B 951  
AB2 4  LEU B 849  ? GLN B 855  ? LEU B 847  GLN B 853  
AB2 5  ASN B 817  ? VAL B 821  ? ASN B 815  VAL B 819  
AB2 6  THR B 973  ? HIS B 977  ? THR B 971  HIS B 975  
AB2 7  ASN B 995  ? ILE B 998  ? ASN B 993  ILE B 996  
AB2 8  VAL B 1213 ? ASN B 1221 ? VAL B 1211 ASN B 1219 
AB2 9  GLU B 1092 ? ALA B 1100 ? GLU B 1090 ALA B 1098 
AB2 10 ASP B 1083 ? 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 SER A 265  ? O SER A 263  
AA1 2 3  N ILE A 266  ? N ILE A 264  O ASN A 306  ? O ASN A 304  
AA1 3 4  N LEU A 305  ? N LEU A 303  O GLY A 338  ? O GLY A 336  
AA1 4 5  N PHE A 339  ? N PHE A 337  O MET A 367  ? O MET A 365  
AA1 5 6  N VAL A 368  ? N VAL A 366  O GLN A 421  ? O GLN A 419  
AA1 6 7  N PHE A 422  ? N PHE A 420  O GLU A 447  ? O GLU A 445  
AA1 7 8  N CYS A 450  ? N CYS A 448  O TYR A 475  ? O TYR A 473  
AA1 8 9  O ILE A 474  ? O ILE A 472  N SER A 219  ? N SER A 217  
AA2 1 2  N ALA A 578  ? N ALA A 576  O THR A 608  ? O THR A 606  
AA2 2 3  O GLU A 609  ? O GLU A 607  N GLU A 590  ? N GLU A 588  
AA3 1 2  N LEU A 582  ? N LEU A 580  O GLY A 585  ? O GLY A 583  
AA4 1 2  O GLN A 759  ? O GLN A 757  N ALA A 731  ? N ALA A 729  
AA4 2 3  O LYS A 732  ? O LYS A 730  N CYS A 704  ? N CYS A 702  
AA4 3 4  N ILE A 705  ? N ILE A 703  O MET A 781  ? O MET A 779  
AA4 4 5  N PHE A 782  ? N PHE A 780  O ILE A 810  ? O ILE A 808  
AA5 1 2  N GLU A 912  ? N GLU A 910  O ILE A 930  ? O ILE A 928  
AA5 2 3  N ILE A 931  ? N ILE A 929  O LEU A 948  ? O LEU A 946  
AA5 3 4  O HIS A 949  ? O HIS A 947  N LEU A 852  ? N LEU A 850  
AA5 4 5  O CYS A 853  ? O CYS A 851  N MET A 819  ? N MET A 817  
AA5 5 6  N ILE A 820  ? N ILE A 818  O HIS A 977  ? O HIS A 975  
AA5 6 7  N LEU A 976  ? N LEU A 974  O TYR A 997  ? O TYR A 995  
AA5 7 8  N LEU A 996  ? N LEU A 994  O SER A 1217 ? O SER A 1215 
AA5 8 9  O ALA A 1218 ? O ALA A 1216 N LEU A 1095 ? N LEU A 1093 
AA5 9 10 O ASN A 1094 ? O ASN A 1092 N LEU A 1086 ? N LEU A 1084 
AA6 1 2  O SER A 1154 ? O SER A 1152 N ILE A 1130 ? N ILE A 1128 
AA6 2 3  O ALA A 1129 ? O ALA A 1127 N LEU A 1106 ? N LEU A 1104 
AA6 3 4  N VAL A 1107 ? N VAL A 1105 O LEU A 1167 ? O LEU A 1165 
AA6 4 5  N VAL A 1168 ? N VAL A 1166 O GLN A 1193 ? O GLN A 1191 
AA7 1 2  N TYR B 222  ? N TYR B 220  O SER B 265  ? O SER B 263  
AA7 2 3  N ILE B 266  ? N ILE B 264  O ASN B 306  ? O ASN B 304  
AA7 3 4  N LEU B 305  ? N LEU B 303  O GLY B 338  ? O GLY B 336  
AA7 4 5  N MET B 337  ? N MET B 335  O MET B 367  ? O MET B 365  
AA7 5 6  N VAL B 368  ? N VAL B 366  O GLN B 421  ? O GLN B 419  
AA7 6 7  N PHE B 422  ? N PHE B 420  O GLU B 447  ? O GLU B 445  
AA7 7 8  N CYS B 450  ? N CYS B 448  O TYR B 475  ? O TYR B 473  
AA7 8 9  O ILE B 474  ? O ILE B 472  N SER B 219  ? N SER B 217  
AA8 1 2  N ALA B 578  ? N ALA B 576  O THR B 608  ? O THR B 606  
AA8 2 3  O GLU B 609  ? O GLU B 607  N GLU B 590  ? N GLU B 588  
AA9 1 2  N LEU B 582  ? N LEU B 580  O GLY B 585  ? O GLY B 583  
AB1 1 2  O GLN B 759  ? O GLN B 757  N ALA B 731  ? N ALA B 729  
AB1 2 3  O LYS B 732  ? O LYS B 730  N CYS B 704  ? N CYS B 702  
AB1 3 4  N ILE B 705  ? N ILE B 703  O MET B 781  ? O MET B 779  
AB1 4 5  N PHE B 782  ? N PHE B 780  O ILE B 810  ? O ILE B 808  
AB2 1 2  N GLU B 912  ? N GLU B 910  O ILE B 930  ? O ILE B 928  
AB2 2 3  N THR B 929  ? N THR B 927  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 LEU B 976  ? N LEU B 974  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 1154 ? O SER B 1152 N ILE B 1130 ? N ILE B 1128 
AB3 2 3  O ALA B 1129 ? O ALA B 1127 N LEU B 1106 ? N LEU B 1104 
AB3 3 4  N VAL B 1107 ? N VAL B 1105 O LEU B 1167 ? O LEU B 1165 
AB3 4 5  N VAL B 1168 ? N VAL B 1166 O GLN B 1193 ? O GLN B 1191 
# 
_pdbx_entry_details.entry_id                   9E0A 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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 GLN 793  ? ? O A HOH 1401 ? ? 2.12 
2  1 O   B HOH 2134 ? ? O B HOH 2365 ? ? 2.12 
3  1 O   A HOH 2412 ? ? O A HOH 2537 ? ? 2.14 
4  1 OE1 B GLN 793  ? ? O B HOH 1401 ? ? 2.14 
5  1 O   A LEU 1183 ? ? O A HOH 1402 ? ? 2.14 
6  1 OE1 B GLU 539  ? ? O B HOH 1402 ? ? 2.15 
7  1 O   A HOH 1575 ? ? O A HOH 1620 ? ? 2.15 
8  1 O   B HOH 2243 ? ? O B HOH 2536 ? ? 2.16 
9  1 O   A HOH 2151 ? ? O A HOH 2483 ? ? 2.17 
10 1 OH  A TYR 995  ? ? O A HOH 1403 ? ? 2.17 
11 1 O2  A SO4 1308 ? ? O A HOH 1404 ? ? 2.18 
12 1 O   B HOH 1518 ? ? O B HOH 2457 ? ? 2.19 
# 
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   ? ? -156.54 57.62   
2  1 LYS A 124  ? ? -125.15 -52.88  
3  1 ASN A 129  ? ? -62.27  78.50   
4  1 GLU A 225  ? ? -171.68 140.45  
5  1 GLU A 308  ? ? -120.07 -136.09 
6  1 MET A 452  ? ? -149.28 -49.82  
7  1 LYS A 465  ? ? -119.23 -126.28 
8  1 ASP A 597  ? ? -172.78 97.28   
9  1 THR A 811  ? ? -125.53 -154.91 
10 1 GLN A 842  ? ? -92.56  53.36   
11 1 GLN A 938  ? ? -104.33 -63.51  
12 1 LEU A 970  ? ? -98.54  -86.62  
13 1 ALA A 1003 ? A -141.01 37.24   
14 1 GLN A 1008 ? ? -118.84 78.49   
15 1 ALA B 22   ? ? -156.03 60.74   
16 1 ASN B 129  ? ? -76.30  48.57   
17 1 GLU B 308  ? ? -118.66 -134.68 
18 1 MET B 452  ? ? -138.64 -45.54  
19 1 VAL B 460  ? ? -122.63 -52.66  
20 1 LYS B 465  ? ? -115.18 -125.20 
21 1 ASP B 597  ? ? -167.79 100.30  
22 1 HIS B 694  ? ? -101.36 76.77   
23 1 THR B 811  ? ? -124.34 -153.83 
24 1 GLN B 842  ? ? -94.17  54.39   
25 1 LEU B 970  ? ? -97.94  -87.39  
26 1 GLN B 1008 ? ? -114.87 76.91   
27 1 ASP B 1154 ? ? -160.27 88.53   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ILE 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    912 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    913 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -142.45 
# 
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 -25.6529 66.0586 92.7845 0.1672 ? 0.0205 ? 0.0129  ? 0.1291 ? 0.0053  ? 0.1354 ? 0.6288 ? -0.0143 
? 0.1643 ? 0.0990 ? -0.0005 ? 0.1372 ? -0.0351 ? -0.1169 ? -0.0051 ? 0.0305 ? 0.0332 ? 0.0173  ? -0.0114 ? -0.0133 ? 0.0022  ? 
2 'X-RAY DIFFRACTION' ? refined 5.6737   31.3574 91.3171 0.1322 ? 0.0056 ? -0.0007 ? 0.1485 ? -0.0191 ? 0.1353 ? 0.1468 ? 0.0052  
? 0.0346 ? 0.2283 ? -0.0475 ? 0.2885 ? 0.0038  ? -0.0344 ? 0.0002  ? 0.0449 ? 0.0018 ? -0.0002 ? 0.0168  ? -0.0650 ? -0.0099 ? 
# 
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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2632 ? 5.81 . 
2 1 O ? A HOH 2633 ? 5.82 . 
3 1 O ? A HOH 2634 ? 5.87 . 
4 1 O ? B HOH 2684 ? 6.03 . 
5 1 O ? B HOH 2685 ? 6.12 . 
6 1 O ? B HOH 2686 ? 6.28 . 
# 
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 SER 80  ? A SER 82  
17 1 Y 1 A GLY 81  ? A GLY 83  
18 1 Y 1 A GLY 135 ? A GLY 137 
19 1 Y 1 A GLY 136 ? A GLY 138 
20 1 Y 1 B SER -1  ? B SER 1   
21 1 Y 1 B MET 0   ? B MET 2   
22 1 Y 1 B MET 1   ? B MET 3   
23 1 Y 1 B SER 2   ? B SER 4   
24 1 Y 1 B PRO 3   ? B PRO 5   
25 1 Y 1 B ASN 4   ? B ASN 6   
26 1 Y 1 B PRO 5   ? B PRO 7   
27 1 Y 1 B LEU 6   ? B LEU 8   
28 1 Y 1 B GLN 7   ? B GLN 9   
29 1 Y 1 B LYS 8   ? B LYS 10  
30 1 Y 1 B PRO 9   ? B PRO 11  
31 1 Y 1 B ALA 10  ? B ALA 12  
32 1 Y 1 B ILE 11  ? B ILE 13  
33 1 Y 1 B ASP 12  ? B ASP 14  
34 1 Y 1 B ALA 13  ? B ALA 15  
35 1 Y 1 B HIS 79  ? B HIS 81  
36 1 Y 1 B SER 80  ? B SER 82  
37 1 Y 1 B GLY 81  ? B GLY 83  
38 1 Y 1 B SER 82  ? B SER 84  
39 1 Y 1 B GLY 135 ? B GLY 137 
40 1 Y 1 B GLY 136 ? B GLY 138 
41 1 Y 1 B SER 137 ? B SER 139 
42 1 Y 1 B ASN 493 ? B ASN 495 
# 
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 
A1BDW C10    C  Y N 1   
A1BDW C02    C  N N 2   
A1BDW C03    C  Y N 3   
A1BDW C04    C  Y N 4   
A1BDW C05    C  Y N 5   
A1BDW C06    C  Y N 6   
A1BDW C07    C  N N 7   
A1BDW C09    C  Y N 8   
A1BDW O01    O  N N 9   
A1BDW O08    O  N N 10  
A1BDW H1     H  N N 11  
A1BDW H2     H  N N 12  
A1BDW H3     H  N N 13  
A1BDW H4     H  N N 14  
A1BDW H5     H  N N 15  
A1BDW H6     H  N N 16  
A1BDW H7     H  N N 17  
A1BDW H8     H  N N 18  
A1BDW H9     H  N N 19  
A1BDW H10    H  N N 20  
ALA   N      N  N N 21  
ALA   CA     C  N S 22  
ALA   C      C  N N 23  
ALA   O      O  N N 24  
ALA   CB     C  N N 25  
ALA   OXT    O  N N 26  
ALA   H      H  N N 27  
ALA   H2     H  N N 28  
ALA   HA     H  N N 29  
ALA   HB1    H  N N 30  
ALA   HB2    H  N N 31  
ALA   HB3    H  N N 32  
ALA   HXT    H  N N 33  
ARG   N      N  N N 34  
ARG   CA     C  N S 35  
ARG   C      C  N N 36  
ARG   O      O  N N 37  
ARG   CB     C  N N 38  
ARG   CG     C  N N 39  
ARG   CD     C  N N 40  
ARG   NE     N  N N 41  
ARG   CZ     C  N N 42  
ARG   NH1    N  N N 43  
ARG   NH2    N  N N 44  
ARG   OXT    O  N N 45  
ARG   H      H  N N 46  
ARG   H2     H  N N 47  
ARG   HA     H  N N 48  
ARG   HB2    H  N N 49  
ARG   HB3    H  N N 50  
ARG   HG2    H  N N 51  
ARG   HG3    H  N N 52  
ARG   HD2    H  N N 53  
ARG   HD3    H  N N 54  
ARG   HE     H  N N 55  
ARG   HH11   H  N N 56  
ARG   HH12   H  N N 57  
ARG   HH21   H  N N 58  
ARG   HH22   H  N N 59  
ARG   HXT    H  N N 60  
ASN   N      N  N N 61  
ASN   CA     C  N S 62  
ASN   C      C  N N 63  
ASN   O      O  N N 64  
ASN   CB     C  N N 65  
ASN   CG     C  N N 66  
ASN   OD1    O  N N 67  
ASN   ND2    N  N N 68  
ASN   OXT    O  N N 69  
ASN   H      H  N N 70  
ASN   H2     H  N N 71  
ASN   HA     H  N N 72  
ASN   HB2    H  N N 73  
ASN   HB3    H  N N 74  
ASN   HD21   H  N N 75  
ASN   HD22   H  N N 76  
ASN   HXT    H  N N 77  
ASP   N      N  N N 78  
ASP   CA     C  N S 79  
ASP   C      C  N N 80  
ASP   O      O  N N 81  
ASP   CB     C  N N 82  
ASP   CG     C  N N 83  
ASP   OD1    O  N N 84  
ASP   OD2    O  N N 85  
ASP   OXT    O  N N 86  
ASP   H      H  N N 87  
ASP   H2     H  N N 88  
ASP   HA     H  N N 89  
ASP   HB2    H  N N 90  
ASP   HB3    H  N N 91  
ASP   HD2    H  N N 92  
ASP   HXT    H  N N 93  
CYS   N      N  N N 94  
CYS   CA     C  N R 95  
CYS   C      C  N N 96  
CYS   O      O  N N 97  
CYS   CB     C  N N 98  
CYS   SG     S  N N 99  
CYS   OXT    O  N N 100 
CYS   H      H  N N 101 
CYS   H2     H  N N 102 
CYS   HA     H  N N 103 
CYS   HB2    H  N N 104 
CYS   HB3    H  N N 105 
CYS   HG     H  N N 106 
CYS   HXT    H  N N 107 
FAD   PA     P  N R 108 
FAD   O1A    O  N N 109 
FAD   O2A    O  N N 110 
FAD   O5B    O  N N 111 
FAD   C5B    C  N N 112 
FAD   C4B    C  N R 113 
FAD   O4B    O  N N 114 
FAD   C3B    C  N S 115 
FAD   O3B    O  N N 116 
FAD   C2B    C  N R 117 
FAD   O2B    O  N N 118 
FAD   C1B    C  N R 119 
FAD   N9A    N  Y N 120 
FAD   C8A    C  Y N 121 
FAD   N7A    N  Y N 122 
FAD   C5A    C  Y N 123 
FAD   C6A    C  Y N 124 
FAD   N6A    N  N N 125 
FAD   N1A    N  Y N 126 
FAD   C2A    C  Y N 127 
FAD   N3A    N  Y N 128 
FAD   C4A    C  Y N 129 
FAD   N1     N  N N 130 
FAD   C2     C  N N 131 
FAD   O2     O  N N 132 
FAD   N3     N  N N 133 
FAD   C4     C  N N 134 
FAD   O4     O  N N 135 
FAD   C4X    C  N N 136 
FAD   N5     N  N N 137 
FAD   C5X    C  Y N 138 
FAD   C6     C  Y N 139 
FAD   C7     C  Y N 140 
FAD   C7M    C  N N 141 
FAD   C8     C  Y N 142 
FAD   C8M    C  N N 143 
FAD   C9     C  Y N 144 
FAD   C9A    C  Y N 145 
FAD   N10    N  N N 146 
FAD   C10    C  N N 147 
FAD   "C1'"  C  N N 148 
FAD   "C2'"  C  N S 149 
FAD   "O2'"  O  N N 150 
FAD   "C3'"  C  N S 151 
FAD   "O3'"  O  N N 152 
FAD   "C4'"  C  N R 153 
FAD   "O4'"  O  N N 154 
FAD   "C5'"  C  N N 155 
FAD   "O5'"  O  N N 156 
FAD   P      P  N R 157 
FAD   O1P    O  N N 158 
FAD   O2P    O  N N 159 
FAD   O3P    O  N N 160 
FAD   HOA2   H  N N 161 
FAD   H51A   H  N N 162 
FAD   H52A   H  N N 163 
FAD   H4B    H  N N 164 
FAD   H3B    H  N N 165 
FAD   HO3A   H  N N 166 
FAD   H2B    H  N N 167 
FAD   HO2A   H  N N 168 
FAD   H1B    H  N N 169 
FAD   H8A    H  N N 170 
FAD   H61A   H  N N 171 
FAD   H62A   H  N N 172 
FAD   H2A    H  N N 173 
FAD   HN3    H  N N 174 
FAD   H6     H  N N 175 
FAD   HM71   H  N N 176 
FAD   HM72   H  N N 177 
FAD   HM73   H  N N 178 
FAD   HM81   H  N N 179 
FAD   HM82   H  N N 180 
FAD   HM83   H  N N 181 
FAD   H9     H  N N 182 
FAD   "H1'1" H  N N 183 
FAD   "H1'2" H  N N 184 
FAD   "H2'"  H  N N 185 
FAD   "HO2'" H  N N 186 
FAD   "H3'"  H  N N 187 
FAD   "HO3'" H  N N 188 
FAD   "H4'"  H  N N 189 
FAD   "HO4'" H  N N 190 
FAD   "H5'1" H  N N 191 
FAD   "H5'2" H  N N 192 
FAD   HOP2   H  N N 193 
FMT   C      C  N N 194 
FMT   O1     O  N N 195 
FMT   O2     O  N N 196 
FMT   H      H  N N 197 
FMT   HO2    H  N N 198 
GLN   N      N  N N 199 
GLN   CA     C  N S 200 
GLN   C      C  N N 201 
GLN   O      O  N N 202 
GLN   CB     C  N N 203 
GLN   CG     C  N N 204 
GLN   CD     C  N N 205 
GLN   OE1    O  N N 206 
GLN   NE2    N  N N 207 
GLN   OXT    O  N N 208 
GLN   H      H  N N 209 
GLN   H2     H  N N 210 
GLN   HA     H  N N 211 
GLN   HB2    H  N N 212 
GLN   HB3    H  N N 213 
GLN   HG2    H  N N 214 
GLN   HG3    H  N N 215 
GLN   HE21   H  N N 216 
GLN   HE22   H  N N 217 
GLN   HXT    H  N N 218 
GLU   N      N  N N 219 
GLU   CA     C  N S 220 
GLU   C      C  N N 221 
GLU   O      O  N N 222 
GLU   CB     C  N N 223 
GLU   CG     C  N N 224 
GLU   CD     C  N N 225 
GLU   OE1    O  N N 226 
GLU   OE2    O  N N 227 
GLU   OXT    O  N N 228 
GLU   H      H  N N 229 
GLU   H2     H  N N 230 
GLU   HA     H  N N 231 
GLU   HB2    H  N N 232 
GLU   HB3    H  N N 233 
GLU   HG2    H  N N 234 
GLU   HG3    H  N N 235 
GLU   HE2    H  N N 236 
GLU   HXT    H  N N 237 
GLY   N      N  N N 238 
GLY   CA     C  N N 239 
GLY   C      C  N N 240 
GLY   O      O  N N 241 
GLY   OXT    O  N N 242 
GLY   H      H  N N 243 
GLY   H2     H  N N 244 
GLY   HA2    H  N N 245 
GLY   HA3    H  N N 246 
GLY   HXT    H  N N 247 
HIS   N      N  N N 248 
HIS   CA     C  N S 249 
HIS   C      C  N N 250 
HIS   O      O  N N 251 
HIS   CB     C  N N 252 
HIS   CG     C  Y N 253 
HIS   ND1    N  Y N 254 
HIS   CD2    C  Y N 255 
HIS   CE1    C  Y N 256 
HIS   NE2    N  Y N 257 
HIS   OXT    O  N N 258 
HIS   H      H  N N 259 
HIS   H2     H  N N 260 
HIS   HA     H  N N 261 
HIS   HB2    H  N N 262 
HIS   HB3    H  N N 263 
HIS   HD1    H  N N 264 
HIS   HD2    H  N N 265 
HIS   HE1    H  N N 266 
HIS   HE2    H  N N 267 
HIS   HXT    H  N N 268 
HOH   O      O  N N 269 
HOH   H1     H  N N 270 
HOH   H2     H  N N 271 
ILE   N      N  N N 272 
ILE   CA     C  N S 273 
ILE   C      C  N N 274 
ILE   O      O  N N 275 
ILE   CB     C  N S 276 
ILE   CG1    C  N N 277 
ILE   CG2    C  N N 278 
ILE   CD1    C  N N 279 
ILE   OXT    O  N N 280 
ILE   H      H  N N 281 
ILE   H2     H  N N 282 
ILE   HA     H  N N 283 
ILE   HB     H  N N 284 
ILE   HG12   H  N N 285 
ILE   HG13   H  N N 286 
ILE   HG21   H  N N 287 
ILE   HG22   H  N N 288 
ILE   HG23   H  N N 289 
ILE   HD11   H  N N 290 
ILE   HD12   H  N N 291 
ILE   HD13   H  N N 292 
ILE   HXT    H  N N 293 
LEU   N      N  N N 294 
LEU   CA     C  N S 295 
LEU   C      C  N N 296 
LEU   O      O  N N 297 
LEU   CB     C  N N 298 
LEU   CG     C  N N 299 
LEU   CD1    C  N N 300 
LEU   CD2    C  N N 301 
LEU   OXT    O  N N 302 
LEU   H      H  N N 303 
LEU   H2     H  N N 304 
LEU   HA     H  N N 305 
LEU   HB2    H  N N 306 
LEU   HB3    H  N N 307 
LEU   HG     H  N N 308 
LEU   HD11   H  N N 309 
LEU   HD12   H  N N 310 
LEU   HD13   H  N N 311 
LEU   HD21   H  N N 312 
LEU   HD22   H  N N 313 
LEU   HD23   H  N N 314 
LEU   HXT    H  N N 315 
LYS   N      N  N N 316 
LYS   CA     C  N S 317 
LYS   C      C  N N 318 
LYS   O      O  N N 319 
LYS   CB     C  N N 320 
LYS   CG     C  N N 321 
LYS   CD     C  N N 322 
LYS   CE     C  N N 323 
LYS   NZ     N  N N 324 
LYS   OXT    O  N N 325 
LYS   H      H  N N 326 
LYS   H2     H  N N 327 
LYS   HA     H  N N 328 
LYS   HB2    H  N N 329 
LYS   HB3    H  N N 330 
LYS   HG2    H  N N 331 
LYS   HG3    H  N N 332 
LYS   HD2    H  N N 333 
LYS   HD3    H  N N 334 
LYS   HE2    H  N N 335 
LYS   HE3    H  N N 336 
LYS   HZ1    H  N N 337 
LYS   HZ2    H  N N 338 
LYS   HZ3    H  N N 339 
LYS   HXT    H  N N 340 
MET   N      N  N N 341 
MET   CA     C  N S 342 
MET   C      C  N N 343 
MET   O      O  N N 344 
MET   CB     C  N N 345 
MET   CG     C  N N 346 
MET   SD     S  N N 347 
MET   CE     C  N N 348 
MET   OXT    O  N N 349 
MET   H      H  N N 350 
MET   H2     H  N N 351 
MET   HA     H  N N 352 
MET   HB2    H  N N 353 
MET   HB3    H  N N 354 
MET   HG2    H  N N 355 
MET   HG3    H  N N 356 
MET   HE1    H  N N 357 
MET   HE2    H  N N 358 
MET   HE3    H  N N 359 
MET   HXT    H  N N 360 
MG    MG     MG N N 361 
NAD   PA     P  N S 362 
NAD   O1A    O  N N 363 
NAD   O2A    O  N N 364 
NAD   O5B    O  N N 365 
NAD   C5B    C  N N 366 
NAD   C4B    C  N R 367 
NAD   O4B    O  N N 368 
NAD   C3B    C  N S 369 
NAD   O3B    O  N N 370 
NAD   C2B    C  N R 371 
NAD   O2B    O  N N 372 
NAD   C1B    C  N R 373 
NAD   N9A    N  Y N 374 
NAD   C8A    C  Y N 375 
NAD   N7A    N  Y N 376 
NAD   C5A    C  Y N 377 
NAD   C6A    C  Y N 378 
NAD   N6A    N  N N 379 
NAD   N1A    N  Y N 380 
NAD   C2A    C  Y N 381 
NAD   N3A    N  Y N 382 
NAD   C4A    C  Y N 383 
NAD   O3     O  N N 384 
NAD   PN     P  N N 385 
NAD   O1N    O  N N 386 
NAD   O2N    O  N N 387 
NAD   O5D    O  N N 388 
NAD   C5D    C  N N 389 
NAD   C4D    C  N R 390 
NAD   O4D    O  N N 391 
NAD   C3D    C  N S 392 
NAD   O3D    O  N N 393 
NAD   C2D    C  N R 394 
NAD   O2D    O  N N 395 
NAD   C1D    C  N R 396 
NAD   N1N    N  Y N 397 
NAD   C2N    C  Y N 398 
NAD   C3N    C  Y N 399 
NAD   C7N    C  N N 400 
NAD   O7N    O  N N 401 
NAD   N7N    N  N N 402 
NAD   C4N    C  Y N 403 
NAD   C5N    C  Y N 404 
NAD   C6N    C  Y N 405 
NAD   HOA2   H  N N 406 
NAD   H51A   H  N N 407 
NAD   H52A   H  N N 408 
NAD   H4B    H  N N 409 
NAD   H3B    H  N N 410 
NAD   HO3A   H  N N 411 
NAD   H2B    H  N N 412 
NAD   HO2A   H  N N 413 
NAD   H1B    H  N N 414 
NAD   H8A    H  N N 415 
NAD   H61A   H  N N 416 
NAD   H62A   H  N N 417 
NAD   H2A    H  N N 418 
NAD   H51N   H  N N 419 
NAD   H52N   H  N N 420 
NAD   H4D    H  N N 421 
NAD   H3D    H  N N 422 
NAD   HO3N   H  N N 423 
NAD   H2D    H  N N 424 
NAD   HO2N   H  N N 425 
NAD   H1D    H  N N 426 
NAD   H2N    H  N N 427 
NAD   H71N   H  N N 428 
NAD   H72N   H  N N 429 
NAD   H4N    H  N N 430 
NAD   H5N    H  N N 431 
NAD   H6N    H  N N 432 
PEG   C1     C  N N 433 
PEG   O1     O  N N 434 
PEG   C2     C  N N 435 
PEG   O2     O  N N 436 
PEG   C3     C  N N 437 
PEG   C4     C  N N 438 
PEG   O4     O  N N 439 
PEG   H11    H  N N 440 
PEG   H12    H  N N 441 
PEG   HO1    H  N N 442 
PEG   H21    H  N N 443 
PEG   H22    H  N N 444 
PEG   H31    H  N N 445 
PEG   H32    H  N N 446 
PEG   H41    H  N N 447 
PEG   H42    H  N N 448 
PEG   HO4    H  N N 449 
PGE   C1     C  N N 450 
PGE   O1     O  N N 451 
PGE   C2     C  N N 452 
PGE   O2     O  N N 453 
PGE   C3     C  N N 454 
PGE   C4     C  N N 455 
PGE   O4     O  N N 456 
PGE   C6     C  N N 457 
PGE   C5     C  N N 458 
PGE   O3     O  N N 459 
PGE   H1     H  N N 460 
PGE   H12    H  N N 461 
PGE   HO1    H  N N 462 
PGE   H2     H  N N 463 
PGE   H22    H  N N 464 
PGE   H3     H  N N 465 
PGE   H32    H  N N 466 
PGE   H4     H  N N 467 
PGE   H42    H  N N 468 
PGE   HO4    H  N N 469 
PGE   H6     H  N N 470 
PGE   H62    H  N N 471 
PGE   H5     H  N N 472 
PGE   H52    H  N N 473 
PHE   N      N  N N 474 
PHE   CA     C  N S 475 
PHE   C      C  N N 476 
PHE   O      O  N N 477 
PHE   CB     C  N N 478 
PHE   CG     C  Y N 479 
PHE   CD1    C  Y N 480 
PHE   CD2    C  Y N 481 
PHE   CE1    C  Y N 482 
PHE   CE2    C  Y N 483 
PHE   CZ     C  Y N 484 
PHE   OXT    O  N N 485 
PHE   H      H  N N 486 
PHE   H2     H  N N 487 
PHE   HA     H  N N 488 
PHE   HB2    H  N N 489 
PHE   HB3    H  N N 490 
PHE   HD1    H  N N 491 
PHE   HD2    H  N N 492 
PHE   HE1    H  N N 493 
PHE   HE2    H  N N 494 
PHE   HZ     H  N N 495 
PHE   HXT    H  N N 496 
PRO   N      N  N N 497 
PRO   CA     C  N S 498 
PRO   C      C  N N 499 
PRO   O      O  N N 500 
PRO   CB     C  N N 501 
PRO   CG     C  N N 502 
PRO   CD     C  N N 503 
PRO   OXT    O  N N 504 
PRO   H      H  N N 505 
PRO   HA     H  N N 506 
PRO   HB2    H  N N 507 
PRO   HB3    H  N N 508 
PRO   HG2    H  N N 509 
PRO   HG3    H  N N 510 
PRO   HD2    H  N N 511 
PRO   HD3    H  N N 512 
PRO   HXT    H  N N 513 
SER   N      N  N N 514 
SER   CA     C  N S 515 
SER   C      C  N N 516 
SER   O      O  N N 517 
SER   CB     C  N N 518 
SER   OG     O  N N 519 
SER   OXT    O  N N 520 
SER   H      H  N N 521 
SER   H2     H  N N 522 
SER   HA     H  N N 523 
SER   HB2    H  N N 524 
SER   HB3    H  N N 525 
SER   HG     H  N N 526 
SER   HXT    H  N N 527 
SO4   S      S  N N 528 
SO4   O1     O  N N 529 
SO4   O2     O  N N 530 
SO4   O3     O  N N 531 
SO4   O4     O  N N 532 
THR   N      N  N N 533 
THR   CA     C  N S 534 
THR   C      C  N N 535 
THR   O      O  N N 536 
THR   CB     C  N R 537 
THR   OG1    O  N N 538 
THR   CG2    C  N N 539 
THR   OXT    O  N N 540 
THR   H      H  N N 541 
THR   H2     H  N N 542 
THR   HA     H  N N 543 
THR   HB     H  N N 544 
THR   HG1    H  N N 545 
THR   HG21   H  N N 546 
THR   HG22   H  N N 547 
THR   HG23   H  N N 548 
THR   HXT    H  N N 549 
TRP   N      N  N N 550 
TRP   CA     C  N S 551 
TRP   C      C  N N 552 
TRP   O      O  N N 553 
TRP   CB     C  N N 554 
TRP   CG     C  Y N 555 
TRP   CD1    C  Y N 556 
TRP   CD2    C  Y N 557 
TRP   NE1    N  Y N 558 
TRP   CE2    C  Y N 559 
TRP   CE3    C  Y N 560 
TRP   CZ2    C  Y N 561 
TRP   CZ3    C  Y N 562 
TRP   CH2    C  Y N 563 
TRP   OXT    O  N N 564 
TRP   H      H  N N 565 
TRP   H2     H  N N 566 
TRP   HA     H  N N 567 
TRP   HB2    H  N N 568 
TRP   HB3    H  N N 569 
TRP   HD1    H  N N 570 
TRP   HE1    H  N N 571 
TRP   HE3    H  N N 572 
TRP   HZ2    H  N N 573 
TRP   HZ3    H  N N 574 
TRP   HH2    H  N N 575 
TRP   HXT    H  N N 576 
TYR   N      N  N N 577 
TYR   CA     C  N S 578 
TYR   C      C  N N 579 
TYR   O      O  N N 580 
TYR   CB     C  N N 581 
TYR   CG     C  Y N 582 
TYR   CD1    C  Y N 583 
TYR   CD2    C  Y N 584 
TYR   CE1    C  Y N 585 
TYR   CE2    C  Y N 586 
TYR   CZ     C  Y N 587 
TYR   OH     O  N N 588 
TYR   OXT    O  N N 589 
TYR   H      H  N N 590 
TYR   H2     H  N N 591 
TYR   HA     H  N N 592 
TYR   HB2    H  N N 593 
TYR   HB3    H  N N 594 
TYR   HD1    H  N N 595 
TYR   HD2    H  N N 596 
TYR   HE1    H  N N 597 
TYR   HE2    H  N N 598 
TYR   HH     H  N N 599 
TYR   HXT    H  N N 600 
VAL   N      N  N N 601 
VAL   CA     C  N S 602 
VAL   C      C  N N 603 
VAL   O      O  N N 604 
VAL   CB     C  N N 605 
VAL   CG1    C  N N 606 
VAL   CG2    C  N N 607 
VAL   OXT    O  N N 608 
VAL   H      H  N N 609 
VAL   H2     H  N N 610 
VAL   HA     H  N N 611 
VAL   HB     H  N N 612 
VAL   HG11   H  N N 613 
VAL   HG12   H  N N 614 
VAL   HG13   H  N N 615 
VAL   HG21   H  N N 616 
VAL   HG22   H  N N 617 
VAL   HG23   H  N N 618 
VAL   HXT    H  N N 619 
# 
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 
A1BDW O01   C02    sing N N 1   
A1BDW C02   C03    sing N N 2   
A1BDW C04   C03    doub Y N 3   
A1BDW C04   C05    sing Y N 4   
A1BDW C03   C10    sing Y N 5   
A1BDW C05   C06    doub Y N 6   
A1BDW C10   C09    doub Y N 7   
A1BDW C06   C09    sing Y N 8   
A1BDW C06   C07    sing N N 9   
A1BDW C07   O08    sing N N 10  
A1BDW C10   H1     sing N N 11  
A1BDW C02   H2     sing N N 12  
A1BDW C02   H3     sing N N 13  
A1BDW C04   H4     sing N N 14  
A1BDW C05   H5     sing N N 15  
A1BDW C07   H6     sing N N 16  
A1BDW C07   H7     sing N N 17  
A1BDW C09   H8     sing N N 18  
A1BDW O01   H9     sing N N 19  
A1BDW O08   H10    sing N N 20  
ALA   N     CA     sing N N 21  
ALA   N     H      sing N N 22  
ALA   N     H2     sing N N 23  
ALA   CA    C      sing N N 24  
ALA   CA    CB     sing N N 25  
ALA   CA    HA     sing N N 26  
ALA   C     O      doub N N 27  
ALA   C     OXT    sing N N 28  
ALA   CB    HB1    sing N N 29  
ALA   CB    HB2    sing N N 30  
ALA   CB    HB3    sing N N 31  
ALA   OXT   HXT    sing N N 32  
ARG   N     CA     sing N N 33  
ARG   N     H      sing N N 34  
ARG   N     H2     sing N N 35  
ARG   CA    C      sing N N 36  
ARG   CA    CB     sing N N 37  
ARG   CA    HA     sing N N 38  
ARG   C     O      doub N N 39  
ARG   C     OXT    sing N N 40  
ARG   CB    CG     sing N N 41  
ARG   CB    HB2    sing N N 42  
ARG   CB    HB3    sing N N 43  
ARG   CG    CD     sing N N 44  
ARG   CG    HG2    sing N N 45  
ARG   CG    HG3    sing N N 46  
ARG   CD    NE     sing N N 47  
ARG   CD    HD2    sing N N 48  
ARG   CD    HD3    sing N N 49  
ARG   NE    CZ     sing N N 50  
ARG   NE    HE     sing N N 51  
ARG   CZ    NH1    sing N N 52  
ARG   CZ    NH2    doub N N 53  
ARG   NH1   HH11   sing N N 54  
ARG   NH1   HH12   sing N N 55  
ARG   NH2   HH21   sing N N 56  
ARG   NH2   HH22   sing N N 57  
ARG   OXT   HXT    sing N N 58  
ASN   N     CA     sing N N 59  
ASN   N     H      sing N N 60  
ASN   N     H2     sing N N 61  
ASN   CA    C      sing N N 62  
ASN   CA    CB     sing N N 63  
ASN   CA    HA     sing N N 64  
ASN   C     O      doub N N 65  
ASN   C     OXT    sing N N 66  
ASN   CB    CG     sing N N 67  
ASN   CB    HB2    sing N N 68  
ASN   CB    HB3    sing N N 69  
ASN   CG    OD1    doub N N 70  
ASN   CG    ND2    sing N N 71  
ASN   ND2   HD21   sing N N 72  
ASN   ND2   HD22   sing N N 73  
ASN   OXT   HXT    sing N N 74  
ASP   N     CA     sing N N 75  
ASP   N     H      sing N N 76  
ASP   N     H2     sing N N 77  
ASP   CA    C      sing N N 78  
ASP   CA    CB     sing N N 79  
ASP   CA    HA     sing N N 80  
ASP   C     O      doub N N 81  
ASP   C     OXT    sing N N 82  
ASP   CB    CG     sing N N 83  
ASP   CB    HB2    sing N N 84  
ASP   CB    HB3    sing N N 85  
ASP   CG    OD1    doub N N 86  
ASP   CG    OD2    sing N N 87  
ASP   OD2   HD2    sing N N 88  
ASP   OXT   HXT    sing N N 89  
CYS   N     CA     sing N N 90  
CYS   N     H      sing N N 91  
CYS   N     H2     sing N N 92  
CYS   CA    C      sing N N 93  
CYS   CA    CB     sing N N 94  
CYS   CA    HA     sing N N 95  
CYS   C     O      doub N N 96  
CYS   C     OXT    sing N N 97  
CYS   CB    SG     sing N N 98  
CYS   CB    HB2    sing N N 99  
CYS   CB    HB3    sing N N 100 
CYS   SG    HG     sing N N 101 
CYS   OXT   HXT    sing N N 102 
FAD   PA    O1A    doub N N 103 
FAD   PA    O2A    sing N N 104 
FAD   PA    O5B    sing N N 105 
FAD   PA    O3P    sing N N 106 
FAD   O2A   HOA2   sing N N 107 
FAD   O5B   C5B    sing N N 108 
FAD   C5B   C4B    sing N N 109 
FAD   C5B   H51A   sing N N 110 
FAD   C5B   H52A   sing N N 111 
FAD   C4B   O4B    sing N N 112 
FAD   C4B   C3B    sing N N 113 
FAD   C4B   H4B    sing N N 114 
FAD   O4B   C1B    sing N N 115 
FAD   C3B   O3B    sing N N 116 
FAD   C3B   C2B    sing N N 117 
FAD   C3B   H3B    sing N N 118 
FAD   O3B   HO3A   sing N N 119 
FAD   C2B   O2B    sing N N 120 
FAD   C2B   C1B    sing N N 121 
FAD   C2B   H2B    sing N N 122 
FAD   O2B   HO2A   sing N N 123 
FAD   C1B   N9A    sing N N 124 
FAD   C1B   H1B    sing N N 125 
FAD   N9A   C8A    sing Y N 126 
FAD   N9A   C4A    sing Y N 127 
FAD   C8A   N7A    doub Y N 128 
FAD   C8A   H8A    sing N N 129 
FAD   N7A   C5A    sing Y N 130 
FAD   C5A   C6A    sing Y N 131 
FAD   C5A   C4A    doub Y N 132 
FAD   C6A   N6A    sing N N 133 
FAD   C6A   N1A    doub Y N 134 
FAD   N6A   H61A   sing N N 135 
FAD   N6A   H62A   sing N N 136 
FAD   N1A   C2A    sing Y N 137 
FAD   C2A   N3A    doub Y N 138 
FAD   C2A   H2A    sing N N 139 
FAD   N3A   C4A    sing Y N 140 
FAD   N1    C2     sing N N 141 
FAD   N1    C10    doub N N 142 
FAD   C2    O2     doub N N 143 
FAD   C2    N3     sing N N 144 
FAD   N3    C4     sing N N 145 
FAD   N3    HN3    sing N N 146 
FAD   C4    O4     doub N N 147 
FAD   C4    C4X    sing N N 148 
FAD   C4X   N5     doub N N 149 
FAD   C4X   C10    sing N N 150 
FAD   N5    C5X    sing N N 151 
FAD   C5X   C6     doub Y N 152 
FAD   C5X   C9A    sing Y N 153 
FAD   C6    C7     sing Y N 154 
FAD   C6    H6     sing N N 155 
FAD   C7    C7M    sing N N 156 
FAD   C7    C8     doub Y N 157 
FAD   C7M   HM71   sing N N 158 
FAD   C7M   HM72   sing N N 159 
FAD   C7M   HM73   sing N N 160 
FAD   C8    C8M    sing N N 161 
FAD   C8    C9     sing Y N 162 
FAD   C8M   HM81   sing N N 163 
FAD   C8M   HM82   sing N N 164 
FAD   C8M   HM83   sing N N 165 
FAD   C9    C9A    doub Y N 166 
FAD   C9    H9     sing N N 167 
FAD   C9A   N10    sing N N 168 
FAD   N10   C10    sing N N 169 
FAD   N10   "C1'"  sing N N 170 
FAD   "C1'" "C2'"  sing N N 171 
FAD   "C1'" "H1'1" sing N N 172 
FAD   "C1'" "H1'2" sing N N 173 
FAD   "C2'" "O2'"  sing N N 174 
FAD   "C2'" "C3'"  sing N N 175 
FAD   "C2'" "H2'"  sing N N 176 
FAD   "O2'" "HO2'" sing N N 177 
FAD   "C3'" "O3'"  sing N N 178 
FAD   "C3'" "C4'"  sing N N 179 
FAD   "C3'" "H3'"  sing N N 180 
FAD   "O3'" "HO3'" sing N N 181 
FAD   "C4'" "O4'"  sing N N 182 
FAD   "C4'" "C5'"  sing N N 183 
FAD   "C4'" "H4'"  sing N N 184 
FAD   "O4'" "HO4'" sing N N 185 
FAD   "C5'" "O5'"  sing N N 186 
FAD   "C5'" "H5'1" sing N N 187 
FAD   "C5'" "H5'2" sing N N 188 
FAD   "O5'" P      sing N N 189 
FAD   P     O1P    doub N N 190 
FAD   P     O2P    sing N N 191 
FAD   P     O3P    sing N N 192 
FAD   O2P   HOP2   sing N N 193 
FMT   C     O1     doub N N 194 
FMT   C     O2     sing N N 195 
FMT   C     H      sing N N 196 
FMT   O2    HO2    sing N N 197 
GLN   N     CA     sing N N 198 
GLN   N     H      sing N N 199 
GLN   N     H2     sing N N 200 
GLN   CA    C      sing N N 201 
GLN   CA    CB     sing N N 202 
GLN   CA    HA     sing N N 203 
GLN   C     O      doub N N 204 
GLN   C     OXT    sing N N 205 
GLN   CB    CG     sing N N 206 
GLN   CB    HB2    sing N N 207 
GLN   CB    HB3    sing N N 208 
GLN   CG    CD     sing N N 209 
GLN   CG    HG2    sing N N 210 
GLN   CG    HG3    sing N N 211 
GLN   CD    OE1    doub N N 212 
GLN   CD    NE2    sing N N 213 
GLN   NE2   HE21   sing N N 214 
GLN   NE2   HE22   sing N N 215 
GLN   OXT   HXT    sing N N 216 
GLU   N     CA     sing N N 217 
GLU   N     H      sing N N 218 
GLU   N     H2     sing N N 219 
GLU   CA    C      sing N N 220 
GLU   CA    CB     sing N N 221 
GLU   CA    HA     sing N N 222 
GLU   C     O      doub N N 223 
GLU   C     OXT    sing N N 224 
GLU   CB    CG     sing N N 225 
GLU   CB    HB2    sing N N 226 
GLU   CB    HB3    sing N N 227 
GLU   CG    CD     sing N N 228 
GLU   CG    HG2    sing N N 229 
GLU   CG    HG3    sing N N 230 
GLU   CD    OE1    doub N N 231 
GLU   CD    OE2    sing N N 232 
GLU   OE2   HE2    sing N N 233 
GLU   OXT   HXT    sing N N 234 
GLY   N     CA     sing N N 235 
GLY   N     H      sing N N 236 
GLY   N     H2     sing N N 237 
GLY   CA    C      sing N N 238 
GLY   CA    HA2    sing N N 239 
GLY   CA    HA3    sing N N 240 
GLY   C     O      doub N N 241 
GLY   C     OXT    sing N N 242 
GLY   OXT   HXT    sing N N 243 
HIS   N     CA     sing N N 244 
HIS   N     H      sing N N 245 
HIS   N     H2     sing N N 246 
HIS   CA    C      sing N N 247 
HIS   CA    CB     sing N N 248 
HIS   CA    HA     sing N N 249 
HIS   C     O      doub N N 250 
HIS   C     OXT    sing N N 251 
HIS   CB    CG     sing N N 252 
HIS   CB    HB2    sing N N 253 
HIS   CB    HB3    sing N N 254 
HIS   CG    ND1    sing Y N 255 
HIS   CG    CD2    doub Y N 256 
HIS   ND1   CE1    doub Y N 257 
HIS   ND1   HD1    sing N N 258 
HIS   CD2   NE2    sing Y N 259 
HIS   CD2   HD2    sing N N 260 
HIS   CE1   NE2    sing Y N 261 
HIS   CE1   HE1    sing N N 262 
HIS   NE2   HE2    sing N N 263 
HIS   OXT   HXT    sing N N 264 
HOH   O     H1     sing N N 265 
HOH   O     H2     sing N N 266 
ILE   N     CA     sing N N 267 
ILE   N     H      sing N N 268 
ILE   N     H2     sing N N 269 
ILE   CA    C      sing N N 270 
ILE   CA    CB     sing N N 271 
ILE   CA    HA     sing N N 272 
ILE   C     O      doub N N 273 
ILE   C     OXT    sing N N 274 
ILE   CB    CG1    sing N N 275 
ILE   CB    CG2    sing N N 276 
ILE   CB    HB     sing N N 277 
ILE   CG1   CD1    sing N N 278 
ILE   CG1   HG12   sing N N 279 
ILE   CG1   HG13   sing N N 280 
ILE   CG2   HG21   sing N N 281 
ILE   CG2   HG22   sing N N 282 
ILE   CG2   HG23   sing N N 283 
ILE   CD1   HD11   sing N N 284 
ILE   CD1   HD12   sing N N 285 
ILE   CD1   HD13   sing N N 286 
ILE   OXT   HXT    sing N N 287 
LEU   N     CA     sing N N 288 
LEU   N     H      sing N N 289 
LEU   N     H2     sing N N 290 
LEU   CA    C      sing N N 291 
LEU   CA    CB     sing N N 292 
LEU   CA    HA     sing N N 293 
LEU   C     O      doub N N 294 
LEU   C     OXT    sing N N 295 
LEU   CB    CG     sing N N 296 
LEU   CB    HB2    sing N N 297 
LEU   CB    HB3    sing N N 298 
LEU   CG    CD1    sing N N 299 
LEU   CG    CD2    sing N N 300 
LEU   CG    HG     sing N N 301 
LEU   CD1   HD11   sing N N 302 
LEU   CD1   HD12   sing N N 303 
LEU   CD1   HD13   sing N N 304 
LEU   CD2   HD21   sing N N 305 
LEU   CD2   HD22   sing N N 306 
LEU   CD2   HD23   sing N N 307 
LEU   OXT   HXT    sing N N 308 
LYS   N     CA     sing N N 309 
LYS   N     H      sing N N 310 
LYS   N     H2     sing N N 311 
LYS   CA    C      sing N N 312 
LYS   CA    CB     sing N N 313 
LYS   CA    HA     sing N N 314 
LYS   C     O      doub N N 315 
LYS   C     OXT    sing N N 316 
LYS   CB    CG     sing N N 317 
LYS   CB    HB2    sing N N 318 
LYS   CB    HB3    sing N N 319 
LYS   CG    CD     sing N N 320 
LYS   CG    HG2    sing N N 321 
LYS   CG    HG3    sing N N 322 
LYS   CD    CE     sing N N 323 
LYS   CD    HD2    sing N N 324 
LYS   CD    HD3    sing N N 325 
LYS   CE    NZ     sing N N 326 
LYS   CE    HE2    sing N N 327 
LYS   CE    HE3    sing N N 328 
LYS   NZ    HZ1    sing N N 329 
LYS   NZ    HZ2    sing N N 330 
LYS   NZ    HZ3    sing N N 331 
LYS   OXT   HXT    sing N N 332 
MET   N     CA     sing N N 333 
MET   N     H      sing N N 334 
MET   N     H2     sing N N 335 
MET   CA    C      sing N N 336 
MET   CA    CB     sing N N 337 
MET   CA    HA     sing N N 338 
MET   C     O      doub N N 339 
MET   C     OXT    sing N N 340 
MET   CB    CG     sing N N 341 
MET   CB    HB2    sing N N 342 
MET   CB    HB3    sing N N 343 
MET   CG    SD     sing N N 344 
MET   CG    HG2    sing N N 345 
MET   CG    HG3    sing N N 346 
MET   SD    CE     sing N N 347 
MET   CE    HE1    sing N N 348 
MET   CE    HE2    sing N N 349 
MET   CE    HE3    sing N N 350 
MET   OXT   HXT    sing N N 351 
NAD   PA    O1A    doub N N 352 
NAD   PA    O2A    sing N N 353 
NAD   PA    O5B    sing N N 354 
NAD   PA    O3     sing N N 355 
NAD   O2A   HOA2   sing N N 356 
NAD   O5B   C5B    sing N N 357 
NAD   C5B   C4B    sing N N 358 
NAD   C5B   H51A   sing N N 359 
NAD   C5B   H52A   sing N N 360 
NAD   C4B   O4B    sing N N 361 
NAD   C4B   C3B    sing N N 362 
NAD   C4B   H4B    sing N N 363 
NAD   O4B   C1B    sing N N 364 
NAD   C3B   O3B    sing N N 365 
NAD   C3B   C2B    sing N N 366 
NAD   C3B   H3B    sing N N 367 
NAD   O3B   HO3A   sing N N 368 
NAD   C2B   O2B    sing N N 369 
NAD   C2B   C1B    sing N N 370 
NAD   C2B   H2B    sing N N 371 
NAD   O2B   HO2A   sing N N 372 
NAD   C1B   N9A    sing N N 373 
NAD   C1B   H1B    sing N N 374 
NAD   N9A   C8A    sing Y N 375 
NAD   N9A   C4A    sing Y N 376 
NAD   C8A   N7A    doub Y N 377 
NAD   C8A   H8A    sing N N 378 
NAD   N7A   C5A    sing Y N 379 
NAD   C5A   C6A    sing Y N 380 
NAD   C5A   C4A    doub Y N 381 
NAD   C6A   N6A    sing N N 382 
NAD   C6A   N1A    doub Y N 383 
NAD   N6A   H61A   sing N N 384 
NAD   N6A   H62A   sing N N 385 
NAD   N1A   C2A    sing Y N 386 
NAD   C2A   N3A    doub Y N 387 
NAD   C2A   H2A    sing N N 388 
NAD   N3A   C4A    sing Y N 389 
NAD   O3    PN     sing N N 390 
NAD   PN    O1N    doub N N 391 
NAD   PN    O2N    sing N N 392 
NAD   PN    O5D    sing N N 393 
NAD   O5D   C5D    sing N N 394 
NAD   C5D   C4D    sing N N 395 
NAD   C5D   H51N   sing N N 396 
NAD   C5D   H52N   sing N N 397 
NAD   C4D   O4D    sing N N 398 
NAD   C4D   C3D    sing N N 399 
NAD   C4D   H4D    sing N N 400 
NAD   O4D   C1D    sing N N 401 
NAD   C3D   O3D    sing N N 402 
NAD   C3D   C2D    sing N N 403 
NAD   C3D   H3D    sing N N 404 
NAD   O3D   HO3N   sing N N 405 
NAD   C2D   O2D    sing N N 406 
NAD   C2D   C1D    sing N N 407 
NAD   C2D   H2D    sing N N 408 
NAD   O2D   HO2N   sing N N 409 
NAD   C1D   N1N    sing N N 410 
NAD   C1D   H1D    sing N N 411 
NAD   N1N   C2N    sing Y N 412 
NAD   N1N   C6N    doub Y N 413 
NAD   C2N   C3N    doub Y N 414 
NAD   C2N   H2N    sing N N 415 
NAD   C3N   C7N    sing N N 416 
NAD   C3N   C4N    sing Y N 417 
NAD   C7N   O7N    doub N N 418 
NAD   C7N   N7N    sing N N 419 
NAD   N7N   H71N   sing N N 420 
NAD   N7N   H72N   sing N N 421 
NAD   C4N   C5N    doub Y N 422 
NAD   C4N   H4N    sing N N 423 
NAD   C5N   C6N    sing Y N 424 
NAD   C5N   H5N    sing N N 425 
NAD   C6N   H6N    sing N N 426 
PEG   C1    O1     sing N N 427 
PEG   C1    C2     sing N N 428 
PEG   C1    H11    sing N N 429 
PEG   C1    H12    sing N N 430 
PEG   O1    HO1    sing N N 431 
PEG   C2    O2     sing N N 432 
PEG   C2    H21    sing N N 433 
PEG   C2    H22    sing N N 434 
PEG   O2    C3     sing N N 435 
PEG   C3    C4     sing N N 436 
PEG   C3    H31    sing N N 437 
PEG   C3    H32    sing N N 438 
PEG   C4    O4     sing N N 439 
PEG   C4    H41    sing N N 440 
PEG   C4    H42    sing N N 441 
PEG   O4    HO4    sing N N 442 
PGE   C1    O1     sing N N 443 
PGE   C1    C2     sing N N 444 
PGE   C1    H1     sing N N 445 
PGE   C1    H12    sing N N 446 
PGE   O1    HO1    sing N N 447 
PGE   C2    O2     sing N N 448 
PGE   C2    H2     sing N N 449 
PGE   C2    H22    sing N N 450 
PGE   O2    C3     sing N N 451 
PGE   C3    C4     sing N N 452 
PGE   C3    H3     sing N N 453 
PGE   C3    H32    sing N N 454 
PGE   C4    O3     sing N N 455 
PGE   C4    H4     sing N N 456 
PGE   C4    H42    sing N N 457 
PGE   O4    C6     sing N N 458 
PGE   O4    HO4    sing N N 459 
PGE   C6    C5     sing N N 460 
PGE   C6    H6     sing N N 461 
PGE   C6    H62    sing N N 462 
PGE   C5    O3     sing N N 463 
PGE   C5    H5     sing N N 464 
PGE   C5    H52    sing N N 465 
PHE   N     CA     sing N N 466 
PHE   N     H      sing N N 467 
PHE   N     H2     sing N N 468 
PHE   CA    C      sing N N 469 
PHE   CA    CB     sing N N 470 
PHE   CA    HA     sing N N 471 
PHE   C     O      doub N N 472 
PHE   C     OXT    sing N N 473 
PHE   CB    CG     sing N N 474 
PHE   CB    HB2    sing N N 475 
PHE   CB    HB3    sing N N 476 
PHE   CG    CD1    doub Y N 477 
PHE   CG    CD2    sing Y N 478 
PHE   CD1   CE1    sing Y N 479 
PHE   CD1   HD1    sing N N 480 
PHE   CD2   CE2    doub Y N 481 
PHE   CD2   HD2    sing N N 482 
PHE   CE1   CZ     doub Y N 483 
PHE   CE1   HE1    sing N N 484 
PHE   CE2   CZ     sing Y N 485 
PHE   CE2   HE2    sing N N 486 
PHE   CZ    HZ     sing N N 487 
PHE   OXT   HXT    sing N N 488 
PRO   N     CA     sing N N 489 
PRO   N     CD     sing N N 490 
PRO   N     H      sing N N 491 
PRO   CA    C      sing N N 492 
PRO   CA    CB     sing N N 493 
PRO   CA    HA     sing N N 494 
PRO   C     O      doub N N 495 
PRO   C     OXT    sing N N 496 
PRO   CB    CG     sing N N 497 
PRO   CB    HB2    sing N N 498 
PRO   CB    HB3    sing N N 499 
PRO   CG    CD     sing N N 500 
PRO   CG    HG2    sing N N 501 
PRO   CG    HG3    sing N N 502 
PRO   CD    HD2    sing N N 503 
PRO   CD    HD3    sing N N 504 
PRO   OXT   HXT    sing N N 505 
SER   N     CA     sing N N 506 
SER   N     H      sing N N 507 
SER   N     H2     sing N N 508 
SER   CA    C      sing N N 509 
SER   CA    CB     sing N N 510 
SER   CA    HA     sing N N 511 
SER   C     O      doub N N 512 
SER   C     OXT    sing N N 513 
SER   CB    OG     sing N N 514 
SER   CB    HB2    sing N N 515 
SER   CB    HB3    sing N N 516 
SER   OG    HG     sing N N 517 
SER   OXT   HXT    sing N N 518 
SO4   S     O1     doub N N 519 
SO4   S     O2     doub N N 520 
SO4   S     O3     sing N N 521 
SO4   S     O4     sing N N 522 
THR   N     CA     sing N N 523 
THR   N     H      sing N N 524 
THR   N     H2     sing N N 525 
THR   CA    C      sing N N 526 
THR   CA    CB     sing N N 527 
THR   CA    HA     sing N N 528 
THR   C     O      doub N N 529 
THR   C     OXT    sing N N 530 
THR   CB    OG1    sing N N 531 
THR   CB    CG2    sing N N 532 
THR   CB    HB     sing N N 533 
THR   OG1   HG1    sing N N 534 
THR   CG2   HG21   sing N N 535 
THR   CG2   HG22   sing N N 536 
THR   CG2   HG23   sing N N 537 
THR   OXT   HXT    sing N N 538 
TRP   N     CA     sing N N 539 
TRP   N     H      sing N N 540 
TRP   N     H2     sing N N 541 
TRP   CA    C      sing N N 542 
TRP   CA    CB     sing N N 543 
TRP   CA    HA     sing N N 544 
TRP   C     O      doub N N 545 
TRP   C     OXT    sing N N 546 
TRP   CB    CG     sing N N 547 
TRP   CB    HB2    sing N N 548 
TRP   CB    HB3    sing N N 549 
TRP   CG    CD1    doub Y N 550 
TRP   CG    CD2    sing Y N 551 
TRP   CD1   NE1    sing Y N 552 
TRP   CD1   HD1    sing N N 553 
TRP   CD2   CE2    doub Y N 554 
TRP   CD2   CE3    sing Y N 555 
TRP   NE1   CE2    sing Y N 556 
TRP   NE1   HE1    sing N N 557 
TRP   CE2   CZ2    sing Y N 558 
TRP   CE3   CZ3    doub Y N 559 
TRP   CE3   HE3    sing N N 560 
TRP   CZ2   CH2    doub Y N 561 
TRP   CZ2   HZ2    sing N N 562 
TRP   CZ3   CH2    sing Y N 563 
TRP   CZ3   HZ3    sing N N 564 
TRP   CH2   HH2    sing N N 565 
TRP   OXT   HXT    sing N N 566 
TYR   N     CA     sing N N 567 
TYR   N     H      sing N N 568 
TYR   N     H2     sing N N 569 
TYR   CA    C      sing N N 570 
TYR   CA    CB     sing N N 571 
TYR   CA    HA     sing N N 572 
TYR   C     O      doub N N 573 
TYR   C     OXT    sing N N 574 
TYR   CB    CG     sing N N 575 
TYR   CB    HB2    sing N N 576 
TYR   CB    HB3    sing N N 577 
TYR   CG    CD1    doub Y N 578 
TYR   CG    CD2    sing Y N 579 
TYR   CD1   CE1    sing Y N 580 
TYR   CD1   HD1    sing N N 581 
TYR   CD2   CE2    doub Y N 582 
TYR   CD2   HD2    sing N N 583 
TYR   CE1   CZ     doub Y N 584 
TYR   CE1   HE1    sing N N 585 
TYR   CE2   CZ     sing Y N 586 
TYR   CE2   HE2    sing N N 587 
TYR   CZ    OH     sing N N 588 
TYR   OH    HH     sing N N 589 
TYR   OXT   HXT    sing N N 590 
VAL   N     CA     sing N N 591 
VAL   N     H      sing N N 592 
VAL   N     H2     sing N N 593 
VAL   CA    C      sing N N 594 
VAL   CA    CB     sing N N 595 
VAL   CA    HA     sing N N 596 
VAL   C     O      doub N N 597 
VAL   C     OXT    sing N N 598 
VAL   CB    CG1    sing N N 599 
VAL   CB    CG2    sing N N 600 
VAL   CB    HB     sing N N 601 
VAL   CG1   HG11   sing N N 602 
VAL   CG1   HG12   sing N N 603 
VAL   CG1   HG13   sing N N 604 
VAL   CG2   HG21   sing N N 605 
VAL   CG2   HG22   sing N N 606 
VAL   CG2   HG23   sing N N 607 
VAL   OXT   HXT    sing N N 608 
# 
_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 
# 
_atom_sites.entry_id                    9E0A 
_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]   0.009929 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002918 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009798 
_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]   0.008261 
_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  
MG 
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   ? -49.128 93.629  103.740 1.00 51.24 ? 14   ALA   A N     1 
ATOM   2     C  CA    . ALA   A 1  16   ? -48.090 92.602  103.700 1.00 51.37 ? 14   ALA   A CA    1 
ATOM   3     C  C     . ALA   A 1  16   ? -48.696 91.212  103.863 1.00 48.09 ? 14   ALA   A C     1 
ATOM   4     O  O     . ALA   A 1  16   ? -49.433 90.963  104.815 1.00 44.25 ? 14   ALA   A O     1 
ATOM   5     C  CB    . ALA   A 1  16   ? -47.046 92.859  104.780 1.00 51.73 ? 14   ALA   A CB    1 
ATOM   6     N  N     . PRO   A 1  17   ? -48.381 90.302  102.940 1.00 46.78 ? 15   PRO   A N     1 
ATOM   7     C  CA    . PRO   A 1  17   ? -48.957 88.954  103.014 1.00 35.73 ? 15   PRO   A CA    1 
ATOM   8     C  C     . PRO   A 1  17   ? -48.446 88.207  104.235 1.00 37.92 ? 15   PRO   A C     1 
ATOM   9     O  O     . PRO   A 1  17   ? -47.278 88.324  104.615 1.00 36.31 ? 15   PRO   A O     1 
ATOM   10    C  CB    . PRO   A 1  17   ? -48.479 88.290  101.717 1.00 37.81 ? 15   PRO   A CB    1 
ATOM   11    C  CG    . PRO   A 1  17   ? -47.246 89.041  101.350 1.00 44.28 ? 15   PRO   A CG    1 
ATOM   12    C  CD    . PRO   A 1  17   ? -47.479 90.458  101.786 1.00 40.07 ? 15   PRO   A CD    1 
ATOM   13    N  N     . ALA   A 1  18   ? -49.339 87.444  104.855 1.00 34.52 ? 16   ALA   A N     1 
ATOM   14    C  CA    . ALA   A 1  18   ? -48.972 86.721  106.058 1.00 30.93 ? 16   ALA   A CA    1 
ATOM   15    C  C     . ALA   A 1  18   ? -47.923 85.669  105.712 1.00 28.71 ? 16   ALA   A C     1 
ATOM   16    O  O     . ALA   A 1  18   ? -47.989 85.061  104.639 1.00 30.02 ? 16   ALA   A O     1 
ATOM   17    C  CB    . ALA   A 1  18   ? -50.204 86.050  106.664 1.00 36.29 ? 16   ALA   A CB    1 
ATOM   18    N  N     . PRO   A 1  19   ? -46.938 85.447  106.578 1.00 26.60 ? 17   PRO   A N     1 
ATOM   19    C  CA    . PRO   A 1  19   ? -45.881 84.480  106.260 1.00 26.67 ? 17   PRO   A CA    1 
ATOM   20    C  C     . PRO   A 1  19   ? -46.464 83.096  106.038 1.00 25.99 ? 17   PRO   A C     1 
ATOM   21    O  O     . PRO   A 1  19   ? -47.278 82.609  106.829 1.00 30.37 ? 17   PRO   A O     1 
ATOM   22    C  CB    . PRO   A 1  19   ? -44.979 84.520  107.500 1.00 30.92 ? 17   PRO   A CB    1 
ATOM   23    C  CG    . PRO   A 1  19   ? -45.264 85.842  108.140 1.00 35.16 ? 17   PRO   A CG    1 
ATOM   24    C  CD    . PRO   A 1  19   ? -46.711 86.117  107.870 1.00 29.52 ? 17   PRO   A CD    1 
ATOM   25    N  N     . PHE   A 1  20   ? -46.064 82.480  104.928 1.00 24.96 ? 18   PHE   A N     1 
ATOM   26    C  CA    . PHE   A 1  20   ? -46.406 81.111  104.569 1.00 25.24 ? 18   PHE   A CA    1 
ATOM   27    C  C     . PHE   A 1  20   ? -47.886 80.921  104.278 1.00 24.77 ? 18   PHE   A C     1 
ATOM   28    O  O     . PHE   A 1  20   ? -48.344 79.778  104.177 1.00 25.67 ? 18   PHE   A O     1 
ATOM   29    C  CB    . PHE   A 1  20   ? -45.932 80.102  105.619 1.00 24.38 ? 18   PHE   A CB    1 
ATOM   30    C  CG    . PHE   A 1  20   ? -44.460 80.181  105.901 1.00 26.33 ? 18   PHE   A CG    1 
ATOM   31    C  CD1   . PHE   A 1  20   ? -43.544 79.685  104.992 1.00 24.17 ? 18   PHE   A CD1   1 
ATOM   32    C  CD2   . PHE   A 1  20   ? -43.992 80.763  107.068 1.00 26.67 ? 18   PHE   A CD2   1 
ATOM   33    C  CE1   . PHE   A 1  20   ? -42.179 79.761  105.247 1.00 23.66 ? 18   PHE   A CE1   1 
ATOM   34    C  CE2   . PHE   A 1  20   ? -42.641 80.841  107.327 1.00 27.25 ? 18   PHE   A CE2   1 
ATOM   35    C  CZ    . PHE   A 1  20   ? -41.732 80.336  106.419 1.00 26.81 ? 18   PHE   A CZ    1 
ATOM   36    N  N     . ALA   A 1  21   ? -48.644 82.008  104.136 1.00 28.59 ? 19   ALA   A N     1 
ATOM   37    C  CA    . ALA   A 1  21   ? -50.065 81.887  103.838 1.00 29.16 ? 19   ALA   A CA    1 
ATOM   38    C  C     . ALA   A 1  21   ? -50.319 81.321  102.451 1.00 29.14 ? 19   ALA   A C     1 
ATOM   39    O  O     . ALA   A 1  21   ? -51.418 80.824  102.193 1.00 30.12 ? 19   ALA   A O     1 
ATOM   40    C  CB    . ALA   A 1  21   ? -50.756 83.241  104.003 1.00 33.40 ? 19   ALA   A CB    1 
ATOM   41    N  N     . ASP   A 1  22   ? -49.337 81.380  101.559 1.00 26.64 ? 20   ASP   A N     1 
ATOM   42    C  CA    . ASP   A 1  22   ? -49.454 80.836  100.210 1.00 30.14 ? 20   ASP   A CA    1 
ATOM   43    C  C     . ASP   A 1  22   ? -48.288 79.911  99.907  1.00 25.17 ? 20   ASP   A C     1 
ATOM   44    O  O     . ASP   A 1  22   ? -47.754 79.904  98.796  1.00 24.61 ? 20   ASP   A O     1 
ATOM   45    C  CB    . ASP   A 1  22   ? -49.511 81.950  99.168  1.00 31.12 ? 20   ASP   A CB    1 
ATOM   46    C  CG    . ASP   A 1  22   ? -50.734 82.837  99.320  1.00 45.91 ? 20   ASP   A CG    1 
ATOM   47    O  OD1   . ASP   A 1  22   ? -51.741 82.381  99.901  1.00 49.93 ? 20   ASP   A OD1   1 
ATOM   48    O  OD2   . ASP   A 1  22   ? -50.688 83.992  98.848  1.00 59.07 ? 20   ASP   A OD2   1 
ATOM   49    N  N     . PHE   A 1  23   ? -47.867 79.117  100.891 1.00 21.30 ? 21   PHE   A N     1 
ATOM   50    C  CA    . PHE   A 1  23   ? -46.599 78.405  100.754 1.00 20.34 ? 21   PHE   A CA    1 
ATOM   51    C  C     . PHE   A 1  23   ? -46.640 77.371  99.635  1.00 22.59 ? 21   PHE   A C     1 
ATOM   52    O  O     . PHE   A 1  23   ? -45.797 77.383  98.734  1.00 20.18 ? 21   PHE   A O     1 
ATOM   53    C  CB    . PHE   A 1  23   ? -46.195 77.749  102.072 1.00 21.95 ? 21   PHE   A CB    1 
ATOM   54    C  CG    . PHE   A 1  23   ? -44.982 76.879  101.943 1.00 18.96 ? 21   PHE   A CG    1 
ATOM   55    C  CD1   . PHE   A 1  23   ? -43.755 77.430  101.607 1.00 21.40 ? 21   PHE   A CD1   1 
ATOM   56    C  CD2   . PHE   A 1  23   ? -45.066 75.505  102.130 1.00 22.32 ? 21   PHE   A CD2   1 
ATOM   57    C  CE1   . PHE   A 1  23   ? -42.629 76.629  101.466 1.00 21.31 ? 21   PHE   A CE1   1 
ATOM   58    C  CE2   . PHE   A 1  23   ? -43.942 74.702  102.000 1.00 24.09 ? 21   PHE   A CE2   1 
ATOM   59    C  CZ    . PHE   A 1  23   ? -42.725 75.266  101.663 1.00 20.69 ? 21   PHE   A CZ    1 
ATOM   60    N  N     . ALA   A 1  24   ? -47.587 76.448  99.691  1.00 21.85 ? 22   ALA   A N     1 
ATOM   61    C  CA    . ALA   A 1  24   ? -47.631 75.389  98.694  1.00 21.97 ? 22   ALA   A CA    1 
ATOM   62    C  C     . ALA   A 1  24   ? -49.038 74.819  98.582  1.00 19.92 ? 22   ALA   A C     1 
ATOM   63    O  O     . ALA   A 1  24   ? -49.235 73.608  98.740  1.00 20.17 ? 22   ALA   A O     1 
ATOM   64    C  CB    . ALA   A 1  24   ? -46.629 74.284  99.038  1.00 23.54 ? 22   ALA   A CB    1 
ATOM   65    N  N     . PRO   A 1  25   ? -50.034 75.640  98.280  1.00 23.01 ? 23   PRO   A N     1 
ATOM   66    C  CA    . PRO   A 1  25   ? -51.394 75.125  98.191  1.00 21.81 ? 23   PRO   A CA    1 
ATOM   67    C  C     . PRO   A 1  25   ? -51.498 74.133  97.050  1.00 23.35 ? 23   PRO   A C     1 
ATOM   68    O  O     . PRO   A 1  25   ? -50.942 74.360  95.965  1.00 21.75 ? 23   PRO   A O     1 
ATOM   69    C  CB    . PRO   A 1  25   ? -52.226 76.384  97.907  1.00 25.38 ? 23   PRO   A CB    1 
ATOM   70    C  CG    . PRO   A 1  25   ? -51.296 77.287  97.204  1.00 25.87 ? 23   PRO   A CG    1 
ATOM   71    C  CD    . PRO   A 1  25   ? -49.951 77.049  97.850  1.00 24.62 ? 23   PRO   A CD    1 
ATOM   72    N  N     . PRO   A 1  26   ? -52.168 73.007  97.268  1.00 21.40 ? 24   PRO   A N     1 
ATOM   73    C  CA    . PRO   A 1  26   ? -52.319 72.024  96.194  1.00 20.92 ? 24   PRO   A CA    1 
ATOM   74    C  C     . PRO   A 1  26   ? -53.137 72.589  95.044  1.00 21.00 ? 24   PRO   A C     1 
ATOM   75    O  O     . PRO   A 1  26   ? -53.929 73.526  95.200  1.00 23.56 ? 24   PRO   A O     1 
ATOM   76    C  CB    . PRO   A 1  26   ? -53.051 70.862  96.874  1.00 24.99 ? 24   PRO   A CB    1 
ATOM   77    C  CG    . PRO   A 1  26   ? -53.766 71.493  98.027  1.00 30.77 ? 24   PRO   A CG    1 
ATOM   78    C  CD    . PRO   A 1  26   ? -52.890 72.627  98.494  1.00 24.34 ? 24   PRO   A CD    1 
ATOM   79    N  N     . VAL   A 1  27   ? -52.932 71.988  93.869  1.00 20.65 ? 25   VAL   A N     1 
ATOM   80    C  CA    . VAL   A 1  27   ? -53.691 72.354  92.675  1.00 23.18 ? 25   VAL   A CA    1 
ATOM   81    C  C     . VAL   A 1  27   ? -55.183 72.245  92.933  1.00 21.84 ? 25   VAL   A C     1 
ATOM   82    O  O     . VAL   A 1  27   ? -55.965 73.111  92.521  1.00 23.73 ? 25   VAL   A O     1 
ATOM   83    C  CB    . VAL   A 1  27   ? -53.265 71.468  91.491  1.00 22.72 ? 25   VAL   A CB    1 
ATOM   84    C  CG1   . VAL   A 1  27   ? -54.239 71.632  90.338  1.00 23.39 ? 25   VAL   A CG1   1 
ATOM   85    C  CG2   . VAL   A 1  27   ? -51.854 71.824  91.065  1.00 22.57 ? 25   VAL   A CG2   1 
ATOM   86    N  N     . ARG   A 1  28   ? -55.599 71.184  93.617  1.00 24.01 ? 26   ARG   A N     1 
ATOM   87    C  CA    . ARG   A 1  28   ? -56.998 70.933  93.931  1.00 26.29 ? 26   ARG   A CA    1 
ATOM   88    C  C     . ARG   A 1  28   ? -57.061 70.246  95.284  1.00 29.39 ? 26   ARG   A C     1 
ATOM   89    O  O     . ARG   A 1  28   ? -56.060 69.680  95.742  1.00 26.14 ? 26   ARG   A O     1 
ATOM   90    C  CB    . ARG   A 1  28   ? -57.634 70.031  92.864  1.00 28.18 ? 26   ARG   A CB    1 
ATOM   91    C  CG    . ARG   A 1  28   ? -57.130 68.589  92.886  1.00 28.32 ? 26   ARG   A CG    1 
ATOM   92    C  CD    . ARG   A 1  28   ? -57.647 67.785  91.696  1.00 31.04 ? 26   ARG   A CD    1 
ATOM   93    N  NE    . ARG   A 1  28   ? -57.010 68.203  90.451  1.00 31.28 ? 26   ARG   A NE    1 
ATOM   94    C  CZ    . ARG   A 1  28   ? -57.552 69.032  89.572  1.00 37.82 ? 26   ARG   A CZ    1 
ATOM   95    N  NH1   . ARG   A 1  28   ? -58.781 69.495  89.723  1.00 36.43 ? 26   ARG   A NH1   1 
ATOM   96    N  NH2   . ARG   A 1  28   ? -56.837 69.418  88.522  1.00 32.20 ? 26   ARG   A NH2   1 
ATOM   97    N  N     . PRO   A 1  29   ? -58.215 70.280  95.958  1.00 26.54 ? 27   PRO   A N     1 
ATOM   98    C  CA    . PRO   A 1  29   ? -58.337 69.507  97.198  1.00 27.11 ? 27   PRO   A CA    1 
ATOM   99    C  C     . PRO   A 1  29   ? -58.146 68.032  96.887  1.00 24.67 ? 27   PRO   A C     1 
ATOM   100   O  O     . PRO   A 1  29   ? -58.604 67.530  95.860  1.00 28.32 ? 27   PRO   A O     1 
ATOM   101   C  CB    . PRO   A 1  29   ? -59.766 69.800  97.670  1.00 27.02 ? 27   PRO   A CB    1 
ATOM   102   C  CG    . PRO   A 1  29   ? -60.138 71.083  96.996  1.00 30.31 ? 27   PRO   A CG    1 
ATOM   103   C  CD    . PRO   A 1  29   ? -59.446 71.039  95.666  1.00 28.46 ? 27   PRO   A CD    1 
ATOM   104   N  N     . GLN   A 1  30   ? -57.452 67.339  97.779  1.00 26.09 ? 28   GLN   A N     1 
ATOM   105   C  CA    . GLN   A 1  30   ? -57.062 65.963  97.508  1.00 26.58 ? 28   GLN   A CA    1 
ATOM   106   C  C     . GLN   A 1  30   ? -58.213 65.031  97.864  1.00 25.82 ? 28   GLN   A C     1 
ATOM   107   O  O     . GLN   A 1  30   ? -58.624 64.959  99.026  1.00 28.11 ? 28   GLN   A O     1 
ATOM   108   C  CB    . GLN   A 1  30   ? -55.810 65.627  98.311  1.00 25.03 ? 28   GLN   A CB    1 
ATOM   109   C  CG    . GLN   A 1  30   ? -54.668 66.588  98.033  1.00 21.77 ? 28   GLN   A CG    1 
ATOM   110   C  CD    . GLN   A 1  30   ? -54.097 66.410  96.643  1.00 24.62 ? 28   GLN   A CD    1 
ATOM   111   O  OE1   . GLN   A 1  30   ? -53.398 65.436  96.380  1.00 22.16 ? 28   GLN   A OE1   1 
ATOM   112   N  NE2   . GLN   A 1  30   ? -54.403 67.338  95.742  1.00 22.50 ? 28   GLN   A NE2   1 
ATOM   113   N  N     . SER   A 1  31   ? -58.727 64.323  96.862  1.00 22.74 ? 29   SER   A N     1 
ATOM   114   C  CA    . SER   A 1  31   ? -59.817 63.379  97.066  1.00 21.92 ? 29   SER   A CA    1 
ATOM   115   C  C     . SER   A 1  31   ? -59.324 62.185  97.875  1.00 25.20 ? 29   SER   A C     1 
ATOM   116   O  O     . SER   A 1  31   ? -58.123 61.994  98.081  1.00 23.37 ? 29   SER   A O     1 
ATOM   117   C  CB    . SER   A 1  31   ? -60.328 62.879  95.719  1.00 23.31 ? 29   SER   A CB    1 
ATOM   118   O  OG    . SER   A 1  31   ? -59.333 62.073  95.091  1.00 21.50 ? 29   SER   A OG    1 
ATOM   119   N  N     . THR   A 1  32   ? -60.274 61.363  98.336  1.00 22.94 ? 30   THR   A N     1 
ATOM   120   C  CA    . THR   A 1  32   ? -59.905 60.123  99.008  1.00 23.21 ? 30   THR   A CA    1 
ATOM   121   C  C     . THR   A 1  32   ? -58.962 59.294  98.147  1.00 21.82 ? 30   THR   A C     1 
ATOM   122   O  O     . THR   A 1  32   ? -57.970 58.756  98.643  1.00 22.99 ? 30   THR   A O     1 
ATOM   123   C  CB    . THR   A 1  32   ? -61.161 59.317  99.350  1.00 24.46 ? 30   THR   A CB    1 
ATOM   124   O  OG1   . THR   A 1  32   ? -61.995 60.095  100.215 1.00 30.45 ? 30   THR   A OG1   1 
ATOM   125   C  CG2   . THR   A 1  32   ? -60.787 58.025  100.041 1.00 26.70 ? 30   THR   A CG2   1 
ATOM   126   N  N     . LEU   A 1  33   ? -59.250 59.195  96.850  1.00 21.72 ? 31   LEU   A N     1 
ATOM   127   C  CA    . LEU   A 1  33   ? -58.399 58.402  95.975  1.00 20.68 ? 31   LEU   A CA    1 
ATOM   128   C  C     . LEU   A 1  33   ? -57.026 59.033  95.819  1.00 20.83 ? 31   LEU   A C     1 
ATOM   129   O  O     . LEU   A 1  33   ? -56.015 58.327  95.806  1.00 20.41 ? 31   LEU   A O     1 
ATOM   130   C  CB    . LEU   A 1  33   ? -59.066 58.221  94.616  1.00 23.52 ? 31   LEU   A CB    1 
ATOM   131   C  CG    . LEU   A 1  33   ? -60.211 57.215  94.698  1.00 24.15 ? 31   LEU   A CG    1 
ATOM   132   C  CD1   . LEU   A 1  33   ? -61.088 57.287  93.465  1.00 25.91 ? 31   LEU   A CD1   1 
ATOM   133   C  CD2   . LEU   A 1  33   ? -59.654 55.806  94.886  1.00 28.90 ? 31   LEU   A CD2   1 
ATOM   134   N  N     . ARG   A 1  34   ? -56.964 60.358  95.693  1.00 19.73 ? 32   ARG   A N     1 
ATOM   135   C  CA    . ARG   A 1  34   ? -55.654 60.995  95.583  1.00 19.32 ? 32   ARG   A CA    1 
ATOM   136   C  C     . ARG   A 1  34   ? -54.865 60.837  96.869  1.00 20.48 ? 32   ARG   A C     1 
ATOM   137   O  O     . ARG   A 1  34   ? -53.651 60.620  96.831  1.00 21.62 ? 32   ARG   A O     1 
ATOM   138   C  CB    . ARG   A 1  34   ? -55.802 62.470  95.227  1.00 22.24 ? 32   ARG   A CB    1 
ATOM   139   C  CG    . ARG   A 1  34   ? -56.243 62.730  93.797  1.00 22.22 ? 32   ARG   A CG    1 
ATOM   140   C  CD    . ARG   A 1  34   ? -55.115 62.466  92.809  1.00 19.37 ? 32   ARG   A CD    1 
ATOM   141   N  NE    . ARG   A 1  34   ? -54.000 63.394  92.969  1.00 20.22 ? 32   ARG   A NE    1 
ATOM   142   C  CZ    . ARG   A 1  34   ? -53.898 64.558  92.340  1.00 24.71 ? 32   ARG   A CZ    1 
ATOM   143   N  NH1   . ARG   A 1  34   ? -54.842 64.983  91.513  1.00 23.32 ? 32   ARG   A NH1   1 
ATOM   144   N  NH2   . ARG   A 1  34   ? -52.820 65.313  92.540  1.00 24.35 ? 32   ARG   A NH2   1 
ATOM   145   N  N     . ARG   A 1  35   ? -55.535 60.927  98.021  1.00 20.40 ? 33   ARG   A N     1 
ATOM   146   C  CA    . ARG   A 1  35   ? -54.818 60.798  99.283  1.00 20.46 ? 33   ARG   A CA    1 
ATOM   147   C  C     . ARG   A 1  35   ? -54.265 59.393  99.465  1.00 20.17 ? 33   ARG   A C     1 
ATOM   148   O  O     . ARG   A 1  35   ? -53.202 59.223  100.072 1.00 22.31 ? 33   ARG   A O     1 
ATOM   149   C  CB    . ARG   A 1  35   ? -55.716 61.194  100.459 1.00 24.26 ? 33   ARG   A CB    1 
ATOM   150   C  CG    . ARG   A 1  35   ? -56.033 62.675  100.470 1.00 23.99 ? 33   ARG   A CG    1 
ATOM   151   C  CD    . ARG   A 1  35   ? -56.990 63.040  101.599 1.00 31.42 ? 33   ARG   A CD    1 
ATOM   152   N  NE    . ARG   A 1  35   ? -57.329 64.455  101.533 1.00 41.55 ? 33   ARG   A NE    1 
ATOM   153   C  CZ    . ARG   A 1  35   ? -56.606 65.421  102.083 1.00 49.29 ? 33   ARG   A CZ    1 
ATOM   154   N  NH1   . ARG   A 1  35   ? -55.523 65.153  102.794 1.00 53.48 ? 33   ARG   A NH1   1 
ATOM   155   N  NH2   . ARG   A 1  35   ? -56.974 66.688  101.911 1.00 46.28 ? 33   ARG   A NH2   1 
ATOM   156   N  N     . ALA   A 1  36   ? -54.959 58.384  98.935  1.00 20.77 ? 34   ALA   A N     1 
ATOM   157   C  CA    . ALA   A 1  36   ? -54.445 57.024  99.034  1.00 21.42 ? 34   ALA   A CA    1 
ATOM   158   C  C     . ALA   A 1  36   ? -53.192 56.854  98.197  1.00 21.25 ? 34   ALA   A C     1 
ATOM   159   O  O     . ALA   A 1  36   ? -52.302 56.079  98.562  1.00 22.26 ? 34   ALA   A O     1 
ATOM   160   C  CB    . ALA   A 1  36   ? -55.514 56.021  98.610  1.00 22.80 ? 34   ALA   A CB    1 
ATOM   161   N  N     . ILE   A 1  37   ? -53.100 57.585  97.088  1.00 20.12 ? 35   ILE   A N     1 
ATOM   162   C  CA    . ILE   A 1  37   ? -51.865 57.600  96.322  1.00 18.35 ? 35   ILE   A CA    1 
ATOM   163   C  C     . ILE   A 1  37   ? -50.735 58.178  97.153  1.00 18.09 ? 35   ILE   A C     1 
ATOM   164   O  O     . ILE   A 1  37   ? -49.677 57.558  97.317  1.00 18.42 ? 35   ILE   A O     1 
ATOM   165   C  CB    . ILE   A 1  37   ? -52.065 58.393  95.025  1.00 18.42 ? 35   ILE   A CB    1 
ATOM   166   C  CG1   . ILE   A 1  37   ? -53.033 57.667  94.108  1.00 19.40 ? 35   ILE   A CG1   1 
ATOM   167   C  CG2   . ILE   A 1  37   ? -50.722 58.604  94.341  1.00 17.94 ? 35   ILE   A CG2   1 
ATOM   168   C  CD1   . ILE   A 1  37   ? -53.477 58.521  92.925  1.00 20.62 ? 35   ILE   A CD1   1 
ATOM   169   N  N     . THR   A 1  38   ? -50.933 59.386  97.679  1.00 18.56 ? 36   THR   A N     1 
ATOM   170   C  CA    . THR   A 1  38   ? -49.866 60.041  98.416  1.00 19.73 ? 36   THR   A CA    1 
ATOM   171   C  C     . THR   A 1  38   ? -49.445 59.212  99.619  1.00 19.42 ? 36   THR   A C     1 
ATOM   172   O  O     . THR   A 1  38   ? -48.256 59.143  99.943  1.00 20.35 ? 36   THR   A O     1 
ATOM   173   C  CB    . THR   A 1  38   ? -50.332 61.431  98.840  1.00 20.24 ? 36   THR   A CB    1 
ATOM   174   O  OG1   . THR   A 1  38   ? -50.830 62.131  97.692  1.00 21.24 ? 36   THR   A OG1   1 
ATOM   175   C  CG2   . THR   A 1  38   ? -49.193 62.213  99.462  1.00 21.72 ? 36   THR   A CG2   1 
ATOM   176   N  N     . ALA   A 1  39   ? -50.400 58.533  100.252 1.00 21.15 ? 37   ALA   A N     1 
ATOM   177   C  CA    . ALA   A 1  39   ? -50.094 57.731  101.428 1.00 23.02 ? 37   ALA   A CA    1 
ATOM   178   C  C     . ALA   A 1  39   ? -49.123 56.601  101.116 1.00 25.50 ? 37   ALA   A C     1 
ATOM   179   O  O     . ALA   A 1  39   ? -48.389 56.157  102.005 1.00 26.00 ? 37   ALA   A O     1 
ATOM   180   C  CB    . ALA   A 1  39   ? -51.391 57.161  102.003 1.00 22.39 ? 37   ALA   A CB    1 
ATOM   181   N  N     . ALA   A 1  40   ? -49.095 56.129  99.872  1.00 20.28 ? 38   ALA   A N     1 
ATOM   182   C  CA    . ALA   A 1  40   ? -48.264 54.991  99.502  1.00 21.52 ? 38   ALA   A CA    1 
ATOM   183   C  C     . ALA   A 1  40   ? -46.900 55.397  98.969  1.00 21.61 ? 38   ALA   A C     1 
ATOM   184   O  O     . ALA   A 1  40   ? -46.087 54.515  98.662  1.00 22.18 ? 38   ALA   A O     1 
ATOM   185   C  CB    . ALA   A 1  40   ? -48.975 54.121  98.465  1.00 20.57 ? 38   ALA   A CB    1 
ATOM   186   N  N     . TYR   A 1  41   ? -46.627 56.702  98.896  1.00 19.71 ? 39   TYR   A N     1 
ATOM   187   C  CA    . TYR   A 1  41   ? -45.456 57.220  98.186  1.00 19.21 ? 39   TYR   A CA    1 
ATOM   188   C  C     . TYR   A 1  41   ? -44.179 56.479  98.566  1.00 20.31 ? 39   TYR   A C     1 
ATOM   189   O  O     . TYR   A 1  41   ? -43.435 56.007  97.699  1.00 19.95 ? 39   TYR   A O     1 
ATOM   190   C  CB    . TYR   A 1  41   ? -45.339 58.717  98.482  1.00 20.24 ? 39   TYR   A CB    1 
ATOM   191   C  CG    . TYR   A 1  41   ? -44.579 59.578  97.487  1.00 18.81 ? 39   TYR   A CG    1 
ATOM   192   C  CD1   . TYR   A 1  41   ? -43.490 59.094  96.782  1.00 20.00 ? 39   TYR   A CD1   1 
ATOM   193   C  CD2   . TYR   A 1  41   ? -44.956 60.901  97.282  1.00 19.64 ? 39   TYR   A CD2   1 
ATOM   194   C  CE1   . TYR   A 1  41   ? -42.801 59.908  95.895  1.00 17.80 ? 39   TYR   A CE1   1 
ATOM   195   C  CE2   . TYR   A 1  41   ? -44.279 61.713  96.400  1.00 19.91 ? 39   TYR   A CE2   1 
ATOM   196   C  CZ    . TYR   A 1  41   ? -43.194 61.217  95.720  1.00 18.27 ? 39   TYR   A CZ    1 
ATOM   197   O  OH    . TYR   A 1  41   ? -42.512 62.031  94.835  1.00 18.87 ? 39   TYR   A OH    1 
ATOM   198   N  N     . ARG   A 1  42   ? -43.913 56.355  99.860  1.00 21.17 ? 40   ARG   A N     1 
ATOM   199   C  CA    . ARG   A 1  42   ? -42.689 55.708  100.312 1.00 21.68 ? 40   ARG   A CA    1 
ATOM   200   C  C     . ARG   A 1  42   ? -42.996 54.598  101.304 1.00 20.40 ? 40   ARG   A C     1 
ATOM   201   O  O     . ARG   A 1  42   ? -42.213 54.340  102.229 1.00 25.59 ? 40   ARG   A O     1 
ATOM   202   C  CB    . ARG   A 1  42   ? -41.703 56.730  100.872 1.00 25.43 ? 40   ARG   A CB    1 
ATOM   203   C  CG    . ARG   A 1  42   ? -41.188 57.649  99.783  1.00 23.64 ? 40   ARG   A CG    1 
ATOM   204   C  CD    . ARG   A 1  42   ? -40.413 58.813  100.313 1.00 24.52 ? 40   ARG   A CD    1 
ATOM   205   N  NE    . ARG   A 1  42   ? -40.408 59.857  99.302  1.00 22.84 ? 40   ARG   A NE    1 
ATOM   206   C  CZ    . ARG   A 1  42   ? -39.583 59.886  98.267  1.00 21.69 ? 40   ARG   A CZ    1 
ATOM   207   N  NH1   . ARG   A 1  42   ? -38.599 59.003  98.139  1.00 22.41 ? 40   ARG   A NH1   1 
ATOM   208   N  NH2   . ARG   A 1  42   ? -39.743 60.825  97.340  1.00 21.45 ? 40   ARG   A NH2   1 
ATOM   209   N  N     . ARG   A 1  43   ? -44.122 53.932  101.100 1.00 22.44 ? 41   ARG   A N     1 
ATOM   210   C  CA    . ARG   A 1  43   ? -44.563 52.881  102.001 1.00 24.32 ? 41   ARG   A CA    1 
ATOM   211   C  C     . ARG   A 1  43   ? -43.507 51.782  102.071 1.00 26.76 ? 41   ARG   A C     1 
ATOM   212   O  O     . ARG   A 1  43   ? -42.938 51.400  101.042 1.00 23.91 ? 41   ARG   A O     1 
ATOM   213   C  CB    . ARG   A 1  43   ? -45.870 52.299  101.475 1.00 23.87 ? 41   ARG   A CB    1 
ATOM   214   C  CG    . ARG   A 1  43   ? -46.382 51.096  102.233 1.00 23.62 ? 41   ARG   A CG    1 
ATOM   215   C  CD    . ARG   A 1  43   ? -47.805 50.827  101.831 1.00 26.74 ? 41   ARG   A CD    1 
ATOM   216   N  NE    . ARG   A 1  43   ? -48.657 51.955  102.184 1.00 25.43 ? 41   ARG   A NE    1 
ATOM   217   C  CZ    . ARG   A 1  43   ? -49.795 52.256  101.577 1.00 22.89 ? 41   ARG   A CZ    1 
ATOM   218   N  NH1   . ARG   A 1  43   ? -50.235 51.554  100.550 1.00 25.94 ? 41   ARG   A NH1   1 
ATOM   219   N  NH2   . ARG   A 1  43   ? -50.513 53.283  102.022 1.00 26.19 ? 41   ARG   A NH2   1 
ATOM   220   N  N     . PRO   A 1  44   ? -43.205 51.268  103.261 1.00 25.14 ? 42   PRO   A N     1 
ATOM   221   C  CA    . PRO   A 1  44   ? -42.230 50.180  103.362 1.00 25.42 ? 42   PRO   A CA    1 
ATOM   222   C  C     . PRO   A 1  44   ? -42.563 49.041  102.408 1.00 21.29 ? 42   PRO   A C     1 
ATOM   223   O  O     . PRO   A 1  44   ? -43.725 48.696  102.188 1.00 25.98 ? 42   PRO   A O     1 
ATOM   224   C  CB    . PRO   A 1  44   ? -42.343 49.744  104.828 1.00 27.47 ? 42   PRO   A CB    1 
ATOM   225   C  CG    . PRO   A 1  44   ? -42.760 50.999  105.537 1.00 30.28 ? 42   PRO   A CG    1 
ATOM   226   C  CD    . PRO   A 1  44   ? -43.701 51.693  104.583 1.00 29.86 ? 42   PRO   A CD    1 
ATOM   227   N  N     . GLU   A 1  45   ? -41.508 48.485  101.807 1.00 25.08 ? 43   GLU   A N     1 
ATOM   228   C  CA    . GLU   A 1  45   ? -41.681 47.470  100.777 1.00 25.56 ? 43   GLU   A CA    1 
ATOM   229   C  C     . GLU   A 1  45   ? -42.398 46.233  101.315 1.00 25.77 ? 43   GLU   A C     1 
ATOM   230   O  O     . GLU   A 1  45   ? -43.209 45.615  100.612 1.00 27.43 ? 43   GLU   A O     1 
ATOM   231   C  CB    . GLU   A 1  45   ? -40.307 47.128  100.195 1.00 29.10 ? 43   GLU   A CB    1 
ATOM   232   C  CG    . GLU   A 1  45   ? -40.327 46.919  98.706  1.00 30.14 ? 43   GLU   A CG    1 
ATOM   233   C  CD    . GLU   A 1  45   ? -38.961 46.967  98.052  1.00 23.75 ? 43   GLU   A CD    1 
ATOM   234   O  OE1   . GLU   A 1  45   ? -38.025 47.608  98.588  1.00 23.76 ? 43   GLU   A OE1   1 
ATOM   235   O  OE2   . GLU   A 1  45   ? -38.841 46.349  96.979  1.00 24.71 ? 43   GLU   A OE2   1 
ATOM   236   N  N     . THR   A 1  46   ? -42.114 45.851  102.566 1.00 28.64 ? 44   THR   A N     1 
ATOM   237   C  CA    . THR   A 1  46   ? -42.813 44.722  103.178 1.00 32.60 ? 44   THR   A CA    1 
ATOM   238   C  C     . THR   A 1  46   ? -44.312 44.956  103.297 1.00 31.10 ? 44   THR   A C     1 
ATOM   239   O  O     . THR   A 1  46   ? -45.076 43.987  103.375 1.00 33.84 ? 44   THR   A O     1 
ATOM   240   C  CB    . THR   A 1  46   ? -42.239 44.417  104.563 1.00 31.40 ? 44   THR   A CB    1 
ATOM   241   O  OG1   . THR   A 1  46   ? -42.227 45.615  105.349 1.00 31.62 ? 44   THR   A OG1   1 
ATOM   242   C  CG2   . THR   A 1  46   ? -40.816 43.871  104.451 1.00 29.79 ? 44   THR   A CG2   1 
ATOM   243   N  N     . GLU   A 1  47   ? -44.751 46.214  103.321 1.00 28.09 ? 45   GLU   A N     1 
ATOM   244   C  CA    . GLU   A 1  47   ? -46.176 46.507  103.387 1.00 27.97 ? 45   GLU   A CA    1 
ATOM   245   C  C     . GLU   A 1  47   ? -46.826 46.495  102.006 1.00 27.11 ? 45   GLU   A C     1 
ATOM   246   O  O     . GLU   A 1  47   ? -48.008 46.153  101.881 1.00 29.93 ? 45   GLU   A O     1 
ATOM   247   C  CB    . GLU   A 1  47   ? -46.393 47.850  104.086 1.00 30.40 ? 45   GLU   A CB    1 
ATOM   248   C  CG    . GLU   A 1  47   ? -45.586 47.988  105.368 1.00 42.05 ? 45   GLU   A CG    1 
ATOM   249   C  CD    . GLU   A 1  47   ? -45.991 49.184  106.208 1.00 45.96 ? 45   GLU   A CD    1 
ATOM   250   O  OE1   . GLU   A 1  47   ? -46.923 49.914  105.806 1.00 48.13 ? 45   GLU   A OE1   1 
ATOM   251   O  OE2   . GLU   A 1  47   ? -45.376 49.388  107.278 1.00 53.65 ? 45   GLU   A OE2   1 
ATOM   252   N  N     . CYS   A 1  48   ? -46.071 46.853  100.963 1.00 24.74 ? 46   CYS   A N     1 
ATOM   253   C  CA    . CYS   A 1  48   ? -46.638 46.927  99.620  1.00 24.73 ? 46   CYS   A CA    1 
ATOM   254   C  C     . CYS   A 1  48   ? -46.903 45.546  99.037  1.00 19.82 ? 46   CYS   A C     1 
ATOM   255   O  O     . CYS   A 1  48   ? -47.875 45.352  98.303  1.00 23.90 ? 46   CYS   A O     1 
ATOM   256   C  CB    . CYS   A 1  48   ? -45.670 47.662  98.691  1.00 27.33 ? 46   CYS   A CB    1 
ATOM   257   S  SG    . CYS   A 1  48   ? -45.330 49.366  99.124  1.00 26.58 ? 46   CYS   A SG    1 
ATOM   258   N  N     . LEU   A 1  49   ? -46.011 44.585  99.304  1.00 26.07 ? 47   LEU   A N     1 
ATOM   259   C  CA    . LEU   A 1  49   ? -46.025 43.344  98.529  1.00 26.79 ? 47   LEU   A CA    1 
ATOM   260   C  C     . LEU   A 1  49   ? -47.221 42.436  98.794  1.00 23.80 ? 47   LEU   A C     1 
ATOM   261   O  O     . LEU   A 1  49   ? -47.789 41.910  97.821  1.00 27.06 ? 47   LEU   A O     1 
ATOM   262   C  CB    . LEU   A 1  49   ? -44.680 42.621  98.651  1.00 27.19 ? 47   LEU   A CB    1 
ATOM   263   C  CG    . LEU   A 1  49   ? -43.704 42.906  97.504  1.00 27.88 ? 47   LEU   A CG    1 
ATOM   264   C  CD1   . LEU   A 1  49   ? -44.272 42.406  96.192  1.00 28.08 ? 47   LEU   A CD1   1 
ATOM   265   C  CD2   . LEU   A 1  49   ? -43.391 44.392  97.403  1.00 27.58 ? 47   LEU   A CD2   1 
ATOM   266   N  N     . PRO   A 1  50   ? -47.635 42.173  100.035 1.00 29.00 ? 48   PRO   A N     1 
ATOM   267   C  CA    . PRO   A 1  50   ? -48.695 41.168  100.272 1.00 30.35 ? 48   PRO   A CA    1 
ATOM   268   C  C     . PRO   A 1  50   ? -49.960 41.423  99.464  1.00 26.86 ? 48   PRO   A C     1 
ATOM   269   O  O     . PRO   A 1  50   ? -50.474 40.487  98.833  1.00 31.80 ? 48   PRO   A O     1 
ATOM   270   C  CB    . PRO   A 1  50   ? -48.942 41.258  101.786 1.00 30.13 ? 48   PRO   A CB    1 
ATOM   271   C  CG    . PRO   A 1  50   ? -47.619 41.661  102.331 1.00 28.96 ? 48   PRO   A CG    1 
ATOM   272   C  CD    . PRO   A 1  50   ? -47.030 42.622  101.303 1.00 27.75 ? 48   PRO   A CD    1 
ATOM   273   N  N     . PRO   A 1  51   ? -50.511 42.649  99.435  1.00 27.45 ? 49   PRO   A N     1 
ATOM   274   C  CA    . PRO   A 1  51   ? -51.697 42.850  98.586  1.00 31.04 ? 49   PRO   A CA    1 
ATOM   275   C  C     . PRO   A 1  51   ? -51.422 42.657  97.103  1.00 24.35 ? 49   PRO   A C     1 
ATOM   276   O  O     . PRO   A 1  51   ? -52.329 42.257  96.359  1.00 29.49 ? 49   PRO   A O     1 
ATOM   277   C  CB    . PRO   A 1  51   ? -52.154 44.278  98.924  1.00 29.15 ? 49   PRO   A CB    1 
ATOM   278   C  CG    . PRO   A 1  51   ? -50.972 44.941  99.454  1.00 29.74 ? 49   PRO   A CG    1 
ATOM   279   C  CD    . PRO   A 1  51   ? -50.171 43.884  100.167 1.00 28.46 ? 49   PRO   A CD    1 
ATOM   280   N  N     . LEU   A 1  52   ? -50.196 42.926  96.649  1.00 27.92 ? 50   LEU   A N     1 
ATOM   281   C  CA    . LEU   A 1  52   ? -49.867 42.682  95.248  1.00 26.81 ? 50   LEU   A CA    1 
ATOM   282   C  C     . LEU   A 1  52   ? -49.806 41.189  94.959  1.00 23.66 ? 50   LEU   A C     1 
ATOM   283   O  O     . LEU   A 1  52   ? -50.328 40.722  93.938  1.00 25.67 ? 50   LEU   A O     1 
ATOM   284   C  CB    . LEU   A 1  52   ? -48.546 43.362  94.899  1.00 26.18 ? 50   LEU   A CB    1 
ATOM   285   C  CG    . LEU   A 1  52   ? -48.502 44.889  95.020  1.00 27.65 ? 50   LEU   A CG    1 
ATOM   286   C  CD1   . LEU   A 1  52   ? -47.083 45.403  94.797  1.00 23.68 ? 50   LEU   A CD1   1 
ATOM   287   C  CD2   . LEU   A 1  52   ? -49.453 45.545  94.028  1.00 24.62 ? 50   LEU   A CD2   1 
ATOM   288   N  N     . VAL   A 1  53   ? -49.194 40.421  95.864  1.00 25.95 ? 51   VAL   A N     1 
ATOM   289   C  CA    . VAL   A 1  53   ? -49.184 38.965  95.727  1.00 29.02 ? 51   VAL   A CA    1 
ATOM   290   C  C     . VAL   A 1  53   ? -50.602 38.419  95.657  1.00 24.56 ? 51   VAL   A C     1 
ATOM   291   O  O     . VAL   A 1  53   ? -50.918 37.575  94.807  1.00 29.66 ? 51   VAL   A O     1 
ATOM   292   C  CB    . VAL   A 1  53   ? -48.388 38.325  96.875  1.00 28.51 ? 51   VAL   A CB    1 
ATOM   293   C  CG1   . VAL   A 1  53   ? -48.552 36.810  96.851  1.00 29.94 ? 51   VAL   A CG1   1 
ATOM   294   C  CG2   . VAL   A 1  53   ? -46.927 38.704  96.779  1.00 27.11 ? 51   VAL   A CG2   1 
ATOM   295   N  N     . GLU   A 1  54   ? -51.488 38.907  96.530  1.00 28.36 ? 52   GLU   A N     1 
ATOM   296   C  CA    . GLU   A 1  54   ? -52.869 38.436  96.503  1.00 32.64 ? 52   GLU   A CA    1 
ATOM   297   C  C     . GLU   A 1  54   ? -53.541 38.776  95.179  1.00 28.45 ? 52   GLU   A C     1 
ATOM   298   O  O     . GLU   A 1  54   ? -54.196 37.921  94.570  1.00 32.03 ? 52   GLU   A O     1 
ATOM   299   C  CB    . GLU   A 1  54   ? -53.655 39.001  97.689  1.00 35.58 ? 52   GLU   A CB    1 
ATOM   300   N  N     . ALA   A 1  55   ? -53.356 40.013  94.692  1.00 29.15 ? 53   ALA   A N     1 
ATOM   301   C  CA    . ALA   A 1  55   ? -54.029 40.434  93.466  1.00 28.70 ? 53   ALA   A CA    1 
ATOM   302   C  C     . ALA   A 1  55   ? -53.482 39.707  92.243  1.00 27.86 ? 53   ALA   A C     1 
ATOM   303   O  O     . ALA   A 1  55   ? -54.207 39.511  91.260  1.00 27.28 ? 53   ALA   A O     1 
ATOM   304   C  CB    . ALA   A 1  55   ? -53.882 41.946  93.291  1.00 29.58 ? 53   ALA   A CB    1 
ATOM   305   N  N     . ALA   A 1  56   ? -52.219 39.294  92.290  1.00 26.85 ? 54   ALA   A N     1 
ATOM   306   C  CA    . ALA   A 1  56   ? -51.567 38.655  91.158  1.00 28.25 ? 54   ALA   A CA    1 
ATOM   307   C  C     . ALA   A 1  56   ? -51.728 37.141  91.148  1.00 31.43 ? 54   ALA   A C     1 
ATOM   308   O  O     . ALA   A 1  56   ? -51.317 36.494  90.178  1.00 28.65 ? 54   ALA   A O     1 
ATOM   309   C  CB    . ALA   A 1  56   ? -50.074 39.002  91.162  1.00 22.96 ? 54   ALA   A CB    1 
ATOM   310   N  N     . THR   A 1  57   ? -52.305 36.565  92.194  1.00 30.88 ? 55   THR   A N     1 
ATOM   311   C  CA    . THR   A 1  57   ? -52.442 35.118  92.271  1.00 29.29 ? 55   THR   A CA    1 
ATOM   312   C  C     . THR   A 1  57   ? -53.382 34.610  91.184  1.00 30.13 ? 55   THR   A C     1 
ATOM   313   O  O     . THR   A 1  57   ? -54.410 35.224  90.890  1.00 32.96 ? 55   THR   A O     1 
ATOM   314   C  CB    . THR   A 1  57   ? -52.965 34.745  93.656  1.00 36.61 ? 55   THR   A CB    1 
ATOM   315   O  OG1   . THR   A 1  57   ? -51.988 35.123  94.634  1.00 33.71 ? 55   THR   A OG1   1 
ATOM   316   C  CG2   . THR   A 1  57   ? -53.246 33.245  93.760  1.00 35.18 ? 55   THR   A CG2   1 
ATOM   317   N  N     . GLN   A 1  58   ? -53.014 33.487  90.567  1.00 31.50 ? 56   GLN   A N     1 
ATOM   318   C  CA    . GLN   A 1  58   ? -53.846 32.832  89.569  1.00 31.28 ? 56   GLN   A CA    1 
ATOM   319   C  C     . GLN   A 1  58   ? -53.896 31.338  89.862  1.00 28.47 ? 56   GLN   A C     1 
ATOM   320   O  O     . GLN   A 1  58   ? -53.098 30.810  90.637  1.00 33.47 ? 56   GLN   A O     1 
ATOM   321   C  CB    . GLN   A 1  58   ? -53.333 33.087  88.146  1.00 34.35 ? 56   GLN   A CB    1 
ATOM   322   C  CG    . GLN   A 1  58   ? -53.250 34.564  87.764  1.00 28.56 ? 56   GLN   A CG    1 
ATOM   323   C  CD    . GLN   A 1  58   ? -53.051 34.766  86.281  1.00 27.98 ? 56   GLN   A CD    1 
ATOM   324   O  OE1   . GLN   A 1  58   ? -54.002 34.681  85.508  1.00 31.12 ? 56   GLN   A OE1   1 
ATOM   325   N  NE2   . GLN   A 1  58   ? -51.811 35.032  85.871  1.00 30.94 ? 56   GLN   A NE2   1 
ATOM   326   N  N     . SER   A 1  59   ? -54.849 30.660  89.229  1.00 30.93 ? 57   SER   A N     1 
ATOM   327   C  CA    . SER   A 1  59   ? -55.040 29.237  89.470  1.00 30.63 ? 57   SER   A CA    1 
ATOM   328   C  C     . SER   A 1  59   ? -53.823 28.448  89.001  1.00 34.00 ? 57   SER   A C     1 
ATOM   329   O  O     . SER   A 1  59   ? -53.074 28.879  88.117  1.00 30.02 ? 57   SER   A O     1 
ATOM   330   C  CB    . SER   A 1  59   ? -56.267 28.739  88.718  1.00 34.67 ? 57   SER   A CB    1 
ATOM   331   O  OG    . SER   A 1  59   ? -56.030 28.754  87.320  1.00 34.97 ? 57   SER   A OG    1 
ATOM   332   N  N     . LYS   A 1  60   ? -53.636 27.270  89.603  1.00 32.45 ? 58   LYS   A N     1 
ATOM   333   C  CA    . LYS   A 1  60   ? -52.540 26.401  89.191  1.00 33.59 ? 58   LYS   A CA    1 
ATOM   334   C  C     . LYS   A 1  60   ? -52.626 26.081  87.705  1.00 32.99 ? 58   LYS   A C     1 
ATOM   335   O  O     . LYS   A 1  60   ? -51.605 26.058  87.008  1.00 37.16 ? 58   LYS   A O     1 
ATOM   336   C  CB    . LYS   A 1  60   ? -52.548 25.119  90.031  1.00 34.74 ? 58   LYS   A CB    1 
ATOM   337   C  CG    . LYS   A 1  60   ? -51.421 24.146  89.704  1.00 36.48 ? 58   LYS   A CG    1 
ATOM   338   C  CD    . LYS   A 1  60   ? -50.061 24.803  89.871  1.00 41.75 ? 58   LYS   A CD    1 
ATOM   339   C  CE    . LYS   A 1  60   ? -48.952 23.777  90.078  1.00 46.21 ? 58   LYS   A CE    1 
ATOM   340   N  NZ    . LYS   A 1  60   ? -48.826 22.841  88.929  1.00 48.77 ? 58   LYS   A NZ    1 
ATOM   341   N  N     . GLU   A 1  61   ? -53.841 25.850  87.200  1.00 34.81 ? 59   GLU   A N     1 
ATOM   342   C  CA    . GLU   A 1  61   ? -54.018 25.581  85.777  1.00 36.38 ? 59   GLU   A CA    1 
ATOM   343   C  C     . GLU   A 1  61   ? -53.533 26.749  84.928  1.00 39.75 ? 59   GLU   A C     1 
ATOM   344   O  O     . GLU   A 1  61   ? -52.899 26.547  83.886  1.00 37.19 ? 59   GLU   A O     1 
ATOM   345   C  CB    . GLU   A 1  61   ? -55.484 25.274  85.479  1.00 35.93 ? 59   GLU   A CB    1 
ATOM   346   N  N     . ILE   A 1  62   ? -53.822 27.980  85.357  1.00 34.53 ? 60   ILE   A N     1 
ATOM   347   C  CA    . ILE   A 1  62   ? -53.366 29.150  84.612  1.00 31.85 ? 60   ILE   A CA    1 
ATOM   348   C  C     . ILE   A 1  62   ? -51.853 29.293  84.701  1.00 35.44 ? 60   ILE   A C     1 
ATOM   349   O  O     . ILE   A 1  62   ? -51.186 29.593  83.702  1.00 31.10 ? 60   ILE   A O     1 
ATOM   350   C  CB    . ILE   A 1  62   ? -54.099 30.417  85.085  1.00 32.46 ? 60   ILE   A CB    1 
ATOM   351   C  CG1   . ILE   A 1  62   ? -55.528 30.422  84.549  1.00 37.53 ? 60   ILE   A CG1   1 
ATOM   352   C  CG2   . ILE   A 1  62   ? -53.343 31.666  84.649  1.00 32.33 ? 60   ILE   A CG2   1 
ATOM   353   C  CD1   . ILE   A 1  62   ? -56.229 31.720  84.744  1.00 37.42 ? 60   ILE   A CD1   1 
ATOM   354   N  N     . ARG   A 1  63   ? -51.285 29.088  85.892  1.00 30.58 ? 61   ARG   A N     1 
ATOM   355   C  CA    . ARG   A 1  63   ? -49.837 29.198  86.045  1.00 33.21 ? 61   ARG   A CA    1 
ATOM   356   C  C     . ARG   A 1  63   ? -49.103 28.184  85.175  1.00 35.48 ? 61   ARG   A C     1 
ATOM   357   O  O     . ARG   A 1  63   ? -48.088 28.513  84.551  1.00 31.39 ? 61   ARG   A O     1 
ATOM   358   C  CB    . ARG   A 1  63   ? -49.449 29.071  87.517  1.00 34.30 ? 61   ARG   A CB    1 
ATOM   359   C  CG    . ARG   A 1  63   ? -49.923 30.258  88.332  1.00 37.36 ? 61   ARG   A CG    1 
ATOM   360   C  CD    . ARG   A 1  63   ? -49.398 30.242  89.750  1.00 45.52 ? 61   ARG   A CD    1 
ATOM   361   N  NE    . ARG   A 1  63   ? -50.116 29.300  90.593  1.00 47.61 ? 61   ARG   A NE    1 
ATOM   362   C  CZ    . ARG   A 1  63   ? -49.614 28.152  91.021  1.00 48.22 ? 61   ARG   A CZ    1 
ATOM   363   N  NH1   . ARG   A 1  63   ? -48.386 27.776  90.705  1.00 50.87 ? 61   ARG   A NH1   1 
ATOM   364   N  NH2   . ARG   A 1  63   ? -50.359 27.368  91.793  1.00 46.79 ? 61   ARG   A NH2   1 
ATOM   365   N  N     . ASP   A 1  64   ? -49.612 26.953  85.104  1.00 36.11 ? 62   ASP   A N     1 
ATOM   366   C  CA    . ASP   A 1  64   ? -49.007 25.958  84.224  1.00 35.96 ? 62   ASP   A CA    1 
ATOM   367   C  C     . ASP   A 1  64   ? -49.133 26.364  82.759  1.00 37.18 ? 62   ASP   A C     1 
ATOM   368   O  O     . ASP   A 1  64   ? -48.176 26.240  81.988  1.00 34.59 ? 62   ASP   A O     1 
ATOM   369   C  CB    . ASP   A 1  64   ? -49.646 24.590  84.468  1.00 35.82 ? 62   ASP   A CB    1 
ATOM   370   C  CG    . ASP   A 1  64   ? -49.301 24.019  85.838  1.00 38.12 ? 62   ASP   A CG    1 
ATOM   371   O  OD1   . ASP   A 1  64   ? -48.463 24.614  86.551  1.00 37.35 ? 62   ASP   A OD1   1 
ATOM   372   O  OD2   . ASP   A 1  64   ? -49.872 22.967  86.202  1.00 44.75 ? 62   ASP   A OD2   1 
ATOM   373   N  N     . ALA   A 1  65   ? -50.305 26.858  82.356  1.00 30.56 ? 63   ALA   A N     1 
ATOM   374   C  CA    . ALA   A 1  65   ? -50.483 27.291  80.973  1.00 31.78 ? 63   ALA   A CA    1 
ATOM   375   C  C     . ALA   A 1  65   ? -49.616 28.504  80.660  1.00 34.00 ? 63   ALA   A C     1 
ATOM   376   O  O     . ALA   A 1  65   ? -49.062 28.611  79.560  1.00 33.32 ? 63   ALA   A O     1 
ATOM   377   C  CB    . ALA   A 1  65   ? -51.955 27.593  80.691  1.00 34.29 ? 63   ALA   A CB    1 
ATOM   378   N  N     . ALA   A 1  66   ? -49.484 29.423  81.618  1.00 29.33 ? 64   ALA   A N     1 
ATOM   379   C  CA    . ALA   A 1  66   ? -48.630 30.589  81.410  1.00 30.84 ? 64   ALA   A CA    1 
ATOM   380   C  C     . ALA   A 1  66   ? -47.173 30.177  81.267  1.00 32.49 ? 64   ALA   A C     1 
ATOM   381   O  O     . ALA   A 1  66   ? -46.451 30.701  80.408  1.00 29.10 ? 64   ALA   A O     1 
ATOM   382   C  CB    . ALA   A 1  66   ? -48.782 31.567  82.574  1.00 30.28 ? 64   ALA   A CB    1 
ATOM   383   N  N     . ALA   A 1  67   ? -46.720 29.247  82.109  1.00 27.13 ? 65   ALA   A N     1 
ATOM   384   C  CA    . ALA   A 1  67   ? -45.345 28.777  82.004  1.00 32.03 ? 65   ALA   A CA    1 
ATOM   385   C  C     . ALA   A 1  67   ? -45.112 28.093  80.664  1.00 32.09 ? 65   ALA   A C     1 
ATOM   386   O  O     . ALA   A 1  67   ? -44.060 28.272  80.039  1.00 31.89 ? 65   ALA   A O     1 
ATOM   387   C  CB    . ALA   A 1  67   ? -45.019 27.837  83.166  1.00 34.97 ? 65   ALA   A CB    1 
ATOM   388   N  N     . SER   A 1  68   ? -46.096 27.329  80.194  1.00 33.22 ? 66   SER   A N     1 
ATOM   389   C  CA    . SER   A 1  68   ? -45.965 26.679  78.896  1.00 35.00 ? 66   SER   A CA    1 
ATOM   390   C  C     . SER   A 1  68   ? -45.920 27.702  77.769  1.00 36.77 ? 66   SER   A C     1 
ATOM   391   O  O     . SER   A 1  68   ? -45.099 27.587  76.851  1.00 34.05 ? 66   SER   A O     1 
ATOM   392   C  CB    . SER   A 1  68   ? -47.103 25.681  78.690  1.00 39.52 ? 66   SER   A CB    1 
ATOM   393   O  OG    . SER   A 1  68   ? -47.088 25.164  77.375  1.00 43.76 ? 66   SER   A OG    1 
ATOM   394   N  N     . THR   A 1  69   ? -46.787 28.717  77.824  1.00 33.67 ? 67   THR   A N     1 
ATOM   395   C  CA    . THR   A 1  69   ? -46.744 29.771  76.817  1.00 30.88 ? 67   THR   A CA    1 
ATOM   396   C  C     . THR   A 1  69   ? -45.425 30.526  76.868  1.00 27.34 ? 67   THR   A C     1 
ATOM   397   O  O     . THR   A 1  69   ? -44.817 30.796  75.827  1.00 29.64 ? 67   THR   A O     1 
ATOM   398   C  CB    . THR   A 1  69   ? -47.916 30.728  77.024  1.00 31.75 ? 67   THR   A CB    1 
ATOM   399   O  OG1   . THR   A 1  69   ? -49.141 30.048  76.733  1.00 30.47 ? 67   THR   A OG1   1 
ATOM   400   C  CG2   . THR   A 1  69   ? -47.785 31.954  76.120  1.00 28.03 ? 67   THR   A CG2   1 
ATOM   401   N  N     . ALA   A 1  70   ? -44.972 30.880  78.072  1.00 28.65 ? 68   ALA   A N     1 
ATOM   402   C  CA    . ALA   A 1  70   ? -43.710 31.593  78.219  1.00 29.20 ? 68   ALA   A CA    1 
ATOM   403   C  C     . ALA   A 1  70   ? -42.556 30.780  77.654  1.00 31.95 ? 68   ALA   A C     1 
ATOM   404   O  O     . ALA   A 1  70   ? -41.706 31.310  76.930  1.00 29.47 ? 68   ALA   A O     1 
ATOM   405   C  CB    . ALA   A 1  70   ? -43.463 31.929  79.691  1.00 29.48 ? 68   ALA   A CB    1 
ATOM   406   N  N     . ARG   A 1  71   ? -42.510 29.484  77.981  1.00 30.50 ? 69   ARG   A N     1 
ATOM   407   C  CA    . ARG   A 1  71   ? -41.457 28.625  77.449  1.00 32.15 ? 69   ARG   A CA    1 
ATOM   408   C  C     . ARG   A 1  71   ? -41.510 28.576  75.929  1.00 30.72 ? 69   ARG   A C     1 
ATOM   409   O  O     . ARG   A 1  71   ? -40.471 28.656  75.261  1.00 33.35 ? 69   ARG   A O     1 
ATOM   410   C  CB    . ARG   A 1  71   ? -41.583 27.220  78.040  1.00 34.08 ? 69   ARG   A CB    1 
ATOM   411   C  CG    . ARG   A 1  71   ? -40.792 26.166  77.288  1.00 35.27 ? 69   ARG   A CG    1 
ATOM   412   C  CD    . ARG   A 1  71   ? -40.841 24.807  77.980  1.00 36.58 ? 69   ARG   A CD    1 
ATOM   413   N  NE    . ARG   A 1  71   ? -40.061 24.814  79.209  1.00 39.93 ? 69   ARG   A NE    1 
ATOM   414   C  CZ    . ARG   A 1  71   ? -38.737 24.747  79.250  1.00 40.06 ? 69   ARG   A CZ    1 
ATOM   415   N  NH1   . ARG   A 1  71   ? -38.014 24.659  78.144  1.00 40.35 ? 69   ARG   A NH1   1 
ATOM   416   N  NH2   . ARG   A 1  71   ? -38.123 24.786  80.429  1.00 40.22 ? 69   ARG   A NH2   1 
ATOM   417   N  N     . LYS   A 1  72   ? -42.715 28.470  75.364  1.00 29.80 ? 70   LYS   A N     1 
ATOM   418   C  CA    . LYS   A 1  72   ? -42.857 28.448  73.912  1.00 32.74 ? 70   LYS   A CA    1 
ATOM   419   C  C     . LYS   A 1  72   ? -42.345 29.743  73.286  1.00 35.58 ? 70   LYS   A C     1 
ATOM   420   O  O     . LYS   A 1  72   ? -41.629 29.712  72.277  1.00 31.06 ? 70   LYS   A O     1 
ATOM   421   C  CB    . LYS   A 1  72   ? -44.314 28.199  73.536  1.00 32.14 ? 70   LYS   A CB    1 
ATOM   422   C  CG    . LYS   A 1  72   ? -44.583 28.222  72.043  1.00 38.60 ? 70   LYS   A CG    1 
ATOM   423   C  CD    . LYS   A 1  72   ? -46.049 27.963  71.758  1.00 38.26 ? 70   LYS   A CD    1 
ATOM   424   C  CE    . LYS   A 1  72   ? -46.335 27.899  70.270  1.00 46.57 ? 70   LYS   A CE    1 
ATOM   425   N  NZ    . LYS   A 1  72   ? -45.740 26.681  69.650  1.00 52.94 ? 70   LYS   A NZ    1 
ATOM   426   N  N     . LEU   A 1  73   ? -42.692 30.890  73.877  1.00 31.29 ? 71   LEU   A N     1 
ATOM   427   C  CA    . LEU   A 1  73   ? -42.188 32.165  73.374  1.00 29.23 ? 71   LEU   A CA    1 
ATOM   428   C  C     . LEU   A 1  73   ? -40.671 32.249  73.490  1.00 31.26 ? 71   LEU   A C     1 
ATOM   429   O  O     . LEU   A 1  73   ? -39.997 32.725  72.571  1.00 32.29 ? 71   LEU   A O     1 
ATOM   430   C  CB    . LEU   A 1  73   ? -42.817 33.326  74.146  1.00 26.95 ? 71   LEU   A CB    1 
ATOM   431   C  CG    . LEU   A 1  73   ? -44.330 33.490  74.035  1.00 29.72 ? 71   LEU   A CG    1 
ATOM   432   C  CD1   . LEU   A 1  73   ? -44.795 34.536  75.026  1.00 27.67 ? 71   LEU   A CD1   1 
ATOM   433   C  CD2   . LEU   A 1  73   ? -44.732 33.872  72.623  1.00 30.80 ? 71   LEU   A CD2   1 
ATOM   434   N  N     . ILE   A 1  74   ? -40.117 31.805  74.620  1.00 28.95 ? 72   ILE   A N     1 
ATOM   435   C  CA    . ILE   A 1  74   ? -38.677 31.906  74.832  1.00 29.36 ? 72   ILE   A CA    1 
ATOM   436   C  C     . ILE   A 1  74   ? -37.927 30.953  73.908  1.00 31.55 ? 72   ILE   A C     1 
ATOM   437   O  O     . ILE   A 1  74   ? -36.853 31.284  73.392  1.00 31.95 ? 72   ILE   A O     1 
ATOM   438   C  CB    . ILE   A 1  74   ? -38.347 31.678  76.317  1.00 30.80 ? 72   ILE   A CB    1 
ATOM   439   C  CG1   . ILE   A 1  74   ? -38.885 32.844  77.149  1.00 30.60 ? 72   ILE   A CG1   1 
ATOM   440   C  CG2   . ILE   A 1  74   ? -36.847 31.501  76.531  1.00 30.50 ? 72   ILE   A CG2   1 
ATOM   441   C  CD1   . ILE   A 1  74   ? -38.997 32.539  78.613  1.00 29.38 ? 72   ILE   A CD1   1 
ATOM   442   N  N     . GLU   A 1  75   ? -38.481 29.762  73.673  1.00 33.55 ? 73   GLU   A N     1 
ATOM   443   C  CA    . GLU   A 1  75   ? -37.850 28.842  72.732  1.00 34.73 ? 73   GLU   A CA    1 
ATOM   444   C  C     . GLU   A 1  75   ? -37.840 29.420  71.323  1.00 38.00 ? 73   GLU   A C     1 
ATOM   445   O  O     . GLU   A 1  75   ? -36.853 29.279  70.592  1.00 35.06 ? 73   GLU   A O     1 
ATOM   446   C  CB    . GLU   A 1  75   ? -38.538 27.477  72.780  1.00 37.83 ? 73   GLU   A CB    1 
ATOM   447   C  CG    . GLU   A 1  75   ? -38.063 26.632  73.946  1.00 40.15 ? 73   GLU   A CG    1 
ATOM   448   C  CD    . GLU   A 1  75   ? -38.969 25.457  74.257  1.00 44.61 ? 73   GLU   A CD    1 
ATOM   449   O  OE1   . GLU   A 1  75   ? -40.034 25.324  73.612  1.00 43.85 ? 73   GLU   A OE1   1 
ATOM   450   O  OE2   . GLU   A 1  75   ? -38.609 24.668  75.160  1.00 46.97 ? 73   GLU   A OE2   1 
ATOM   451   N  N     . ALA   A 1  76   ? -38.922 30.096  70.931  1.00 36.89 ? 74   ALA   A N     1 
ATOM   452   C  CA    . ALA   A 1  76   ? -38.935 30.780  69.643  1.00 33.01 ? 74   ALA   A CA    1 
ATOM   453   C  C     . ALA   A 1  76   ? -37.905 31.903  69.603  1.00 35.26 ? 74   ALA   A C     1 
ATOM   454   O  O     . ALA   A 1  76   ? -37.212 32.080  68.595  1.00 39.42 ? 74   ALA   A O     1 
ATOM   455   C  CB    . ALA   A 1  76   ? -40.336 31.320  69.352  1.00 39.34 ? 74   ALA   A CB    1 
ATOM   456   N  N     . LEU   A 1  77   ? -37.789 32.672  70.690  1.00 34.04 ? 75   LEU   A N     1 
ATOM   457   C  CA    . LEU   A 1  77   ? -36.839 33.782  70.722  1.00 31.96 ? 75   LEU   A CA    1 
ATOM   458   C  C     . LEU   A 1  77   ? -35.409 33.284  70.578  1.00 36.96 ? 75   LEU   A C     1 
ATOM   459   O  O     . LEU   A 1  77   ? -34.635 33.802  69.764  1.00 39.95 ? 75   LEU   A O     1 
ATOM   460   C  CB    . LEU   A 1  77   ? -36.981 34.558  72.029  1.00 31.63 ? 75   LEU   A CB    1 
ATOM   461   C  CG    . LEU   A 1  77   ? -38.094 35.597  72.097  1.00 34.04 ? 75   LEU   A CG    1 
ATOM   462   C  CD1   . LEU   A 1  77   ? -38.071 36.275  73.449  1.00 31.66 ? 75   LEU   A CD1   1 
ATOM   463   C  CD2   . LEU   A 1  77   ? -37.891 36.605  70.990  1.00 31.72 ? 75   LEU   A CD2   1 
ATOM   464   N  N     . ARG   A 1  78   ? -35.035 32.287  71.379  1.00 32.82 ? 76   ARG   A N     1 
ATOM   465   C  CA    . ARG   A 1  78   ? -33.680 31.758  71.313  1.00 32.15 ? 76   ARG   A CA    1 
ATOM   466   C  C     . ARG   A 1  78   ? -33.425 30.973  70.038  1.00 34.91 ? 76   ARG   A C     1 
ATOM   467   O  O     . ARG   A 1  78   ? -32.265 30.813  69.649  1.00 41.63 ? 76   ARG   A O     1 
ATOM   468   C  CB    . ARG   A 1  78   ? -33.399 30.907  72.548  1.00 31.57 ? 76   ARG   A CB    1 
ATOM   469   C  CG    . ARG   A 1  78   ? -33.308 31.740  73.805  1.00 34.75 ? 76   ARG   A CG    1 
ATOM   470   C  CD    . ARG   A 1  78   ? -32.929 30.914  75.008  1.00 32.91 ? 76   ARG   A CD    1 
ATOM   471   N  NE    . ARG   A 1  78   ? -32.375 31.766  76.048  1.00 31.68 ? 76   ARG   A NE    1 
ATOM   472   C  CZ    . ARG   A 1  78   ? -31.926 31.328  77.214  1.00 33.40 ? 76   ARG   A CZ    1 
ATOM   473   N  NH1   . ARG   A 1  78   ? -32.011 30.053  77.551  1.00 35.84 ? 76   ARG   A NH1   1 
ATOM   474   N  NH2   . ARG   A 1  78   ? -31.375 32.192  78.062  1.00 35.52 ? 76   ARG   A NH2   1 
ATOM   475   N  N     . GLY   A 1  79   ? -34.479 30.494  69.375  1.00 36.85 ? 77   GLY   A N     1 
ATOM   476   C  CA    . GLY   A 1  79   ? -34.313 29.729  68.154  1.00 42.59 ? 77   GLY   A CA    1 
ATOM   477   C  C     . GLY   A 1  79   ? -34.017 30.560  66.926  1.00 47.68 ? 77   GLY   A C     1 
ATOM   478   O  O     . GLY   A 1  79   ? -33.451 30.039  65.961  1.00 47.85 ? 77   GLY   A O     1 
ATOM   479   N  N     . LYS   A 1  80   ? -34.384 31.838  66.937  1.00 44.96 ? 78   LYS   A N     1 
ATOM   480   C  CA    . LYS   A 1  80   ? -34.130 32.722  65.810  1.00 45.33 ? 78   LYS   A CA    1 
ATOM   481   C  C     . LYS   A 1  80   ? -33.096 33.794  66.117  1.00 43.77 ? 78   LYS   A C     1 
ATOM   482   O  O     . LYS   A 1  80   ? -32.833 34.642  65.258  1.00 51.42 ? 78   LYS   A O     1 
ATOM   483   C  CB    . LYS   A 1  80   ? -35.437 33.367  65.339  1.00 44.74 ? 78   LYS   A CB    1 
ATOM   484   C  CG    . LYS   A 1  80   ? -36.150 34.165  66.416  1.00 46.78 ? 78   LYS   A CG    1 
ATOM   485   C  CD    . LYS   A 1  80   ? -37.541 34.560  65.960  1.00 43.97 ? 78   LYS   A CD    1 
ATOM   486   C  CE    . LYS   A 1  80   ? -38.263 35.369  67.018  1.00 43.39 ? 78   LYS   A CE    1 
ATOM   487   N  NZ    . LYS   A 1  80   ? -39.632 35.746  66.558  1.00 31.40 ? 78   LYS   A NZ    1 
ATOM   488   N  N     . HIS   A 1  81   ? -32.503 33.775  67.309  1.00 44.96 ? 79   HIS   A N     1 
ATOM   489   C  CA    . HIS   A 1  81   ? -31.555 34.800  67.739  1.00 47.27 ? 79   HIS   A CA    1 
ATOM   490   C  C     . HIS   A 1  81   ? -30.387 34.973  66.769  1.00 51.95 ? 79   HIS   A C     1 
ATOM   491   O  O     . HIS   A 1  81   ? -29.523 34.107  66.667  1.00 56.05 ? 79   HIS   A O     1 
ATOM   492   C  CB    . HIS   A 1  81   ? -31.023 34.474  69.136  1.00 50.69 ? 79   HIS   A CB    1 
ATOM   493   N  N     . SER   A 1  84   ? -26.268 41.172  66.886  1.00 51.32 ? 82   SER   A N     1 
ATOM   494   C  CA    . SER   A 1  84   ? -25.408 40.315  66.081  1.00 50.15 ? 82   SER   A CA    1 
ATOM   495   C  C     . SER   A 1  84   ? -24.682 41.119  65.007  1.00 44.66 ? 82   SER   A C     1 
ATOM   496   O  O     . SER   A 1  84   ? -23.648 40.689  64.506  1.00 43.29 ? 82   SER   A O     1 
ATOM   497   C  CB    . SER   A 1  84   ? -26.214 39.180  65.439  1.00 47.48 ? 82   SER   A CB    1 
ATOM   498   N  N     . GLY   A 1  85   ? -25.232 42.279  64.651  1.00 46.73 ? 83   GLY   A N     1 
ATOM   499   C  CA    . GLY   A 1  85   ? -24.590 43.149  63.684  1.00 40.28 ? 83   GLY   A CA    1 
ATOM   500   C  C     . GLY   A 1  85   ? -23.243 43.656  64.165  1.00 31.13 ? 83   GLY   A C     1 
ATOM   501   O  O     . GLY   A 1  85   ? -22.219 43.464  63.497  1.00 31.27 ? 83   GLY   A O     1 
ATOM   502   N  N     . VAL   A 1  86   ? -23.240 44.318  65.325  1.00 33.27 ? 84   VAL   A N     1 
ATOM   503   C  CA    . VAL   A 1  86   ? -21.984 44.747  65.935  1.00 31.63 ? 84   VAL   A CA    1 
ATOM   504   C  C     . VAL   A 1  86   ? -21.123 43.539  66.271  1.00 33.45 ? 84   VAL   A C     1 
ATOM   505   O  O     . VAL   A 1  86   ? -19.906 43.540  66.043  1.00 26.99 ? 84   VAL   A O     1 
ATOM   506   C  CB    . VAL   A 1  86   ? -22.261 45.627  67.169  1.00 38.27 ? 84   VAL   A CB    1 
ATOM   507   C  CG1   . VAL   A 1  86   ? -20.981 45.864  67.960  1.00 37.48 ? 84   VAL   A CG1   1 
ATOM   508   C  CG2   . VAL   A 1  86   ? -22.873 46.947  66.739  1.00 39.00 ? 84   VAL   A CG2   1 
ATOM   509   N  N     . GLU   A 1  87   ? -21.742 42.484  66.805  1.00 34.07 ? 85   GLU   A N     1 
ATOM   510   C  CA    . GLU   A 1  87   ? -21.002 41.269  67.125  1.00 37.69 ? 85   GLU   A CA    1 
ATOM   511   C  C     . GLU   A 1  87   ? -20.336 40.682  65.888  1.00 35.49 ? 85   GLU   A C     1 
ATOM   512   O  O     . GLU   A 1  87   ? -19.175 40.259  65.942  1.00 36.09 ? 85   GLU   A O     1 
ATOM   513   C  CB    . GLU   A 1  87   ? -21.928 40.245  67.783  1.00 40.90 ? 85   GLU   A CB    1 
ATOM   514   N  N     . GLY   A 1  88   ? -21.048 40.655  64.759  1.00 31.86 ? 86   GLY   A N     1 
ATOM   515   C  CA    . GLY   A 1  88   ? -20.460 40.113  63.544  1.00 29.36 ? 86   GLY   A CA    1 
ATOM   516   C  C     . GLY   A 1  88   ? -19.315 40.963  63.028  1.00 29.40 ? 86   GLY   A C     1 
ATOM   517   O  O     . GLY   A 1  88   ? -18.335 40.443  62.486  1.00 31.74 ? 86   GLY   A O     1 
ATOM   518   N  N     . LEU   A 1  89   ? -19.425 42.280  63.195  1.00 29.27 ? 87   LEU   A N     1 
ATOM   519   C  CA    . LEU   A 1  89   ? -18.364 43.188  62.784  1.00 27.36 ? 87   LEU   A CA    1 
ATOM   520   C  C     . LEU   A 1  89   ? -17.125 42.990  63.648  1.00 25.65 ? 87   LEU   A C     1 
ATOM   521   O  O     . LEU   A 1  89   ? -16.008 42.848  63.135  1.00 25.46 ? 87   LEU   A O     1 
ATOM   522   C  CB    . LEU   A 1  89   ? -18.891 44.619  62.890  1.00 28.75 ? 87   LEU   A CB    1 
ATOM   523   C  CG    . LEU   A 1  89   ? -18.008 45.782  62.465  1.00 37.18 ? 87   LEU   A CG    1 
ATOM   524   C  CD1   . LEU   A 1  89   ? -17.595 45.579  61.046  1.00 37.04 ? 87   LEU   A CD1   1 
ATOM   525   C  CD2   . LEU   A 1  89   ? -18.772 47.090  62.623  1.00 36.65 ? 87   LEU   A CD2   1 
ATOM   526   N  N     . VAL   A 1  90   ? -17.317 42.957  64.969  1.00 26.60 ? 88   VAL   A N     1 
ATOM   527   C  CA    . VAL   A 1  90   ? -16.226 42.671  65.897  1.00 27.19 ? 88   VAL   A CA    1 
ATOM   528   C  C     . VAL   A 1  90   ? -15.548 41.355  65.543  1.00 27.14 ? 88   VAL   A C     1 
ATOM   529   O  O     . VAL   A 1  90   ? -14.315 41.247  65.571  1.00 27.51 ? 88   VAL   A O     1 
ATOM   530   C  CB    . VAL   A 1  90   ? -16.763 42.677  67.340  1.00 26.87 ? 88   VAL   A CB    1 
ATOM   531   C  CG1   . VAL   A 1  90   ? -15.750 42.085  68.293  1.00 30.72 ? 88   VAL   A CG1   1 
ATOM   532   C  CG2   . VAL   A 1  90   ? -17.135 44.089  67.763  1.00 28.00 ? 88   VAL   A CG2   1 
ATOM   533   N  N     . GLN   A 1  91   ? -16.339 40.331  65.207  1.00 29.69 ? 89   GLN   A N     1 
ATOM   534   C  CA    . GLN   A 1  91   ? -15.767 39.032  64.860  1.00 30.78 ? 89   GLN   A CA    1 
ATOM   535   C  C     . GLN   A 1  91   ? -14.984 39.098  63.554  1.00 31.14 ? 89   GLN   A C     1 
ATOM   536   O  O     . GLN   A 1  91   ? -13.850 38.610  63.472  1.00 31.82 ? 89   GLN   A O     1 
ATOM   537   C  CB    . GLN   A 1  91   ? -16.876 37.977  64.771  1.00 32.48 ? 89   GLN   A CB    1 
ATOM   538   N  N     . GLU   A 1  92   ? -15.571 39.702  62.517  1.00 27.77 ? 90   GLU   A N     1 
ATOM   539   C  CA    . GLU   A 1  92   ? -14.951 39.666  61.194  1.00 28.06 ? 90   GLU   A CA    1 
ATOM   540   C  C     . GLU   A 1  92   ? -13.587 40.343  61.197  1.00 28.65 ? 90   GLU   A C     1 
ATOM   541   O  O     . GLU   A 1  92   ? -12.653 39.885  60.527  1.00 29.07 ? 90   GLU   A O     1 
ATOM   542   C  CB    . GLU   A 1  92   ? -15.876 40.322  60.166  1.00 28.93 ? 90   GLU   A CB    1 
ATOM   543   C  CG    . GLU   A 1  92   ? -15.236 40.479  58.793  1.00 30.89 ? 90   GLU   A CG    1 
ATOM   544   C  CD    . GLU   A 1  92   ? -16.165 41.119  57.778  1.00 37.93 ? 90   GLU   A CD    1 
ATOM   545   O  OE1   . GLU   A 1  92   ? -17.269 41.552  58.168  1.00 41.49 ? 90   GLU   A OE1   1 
ATOM   546   O  OE2   . GLU   A 1  92   ? -15.787 41.191  56.590  1.00 39.95 ? 90   GLU   A OE2   1 
ATOM   547   N  N     . TYR   A 1  93   ? -13.445 41.425  61.957  1.00 27.79 ? 91   TYR   A N     1 
ATOM   548   C  CA    . TYR   A 1  93   ? -12.206 42.187  61.986  1.00 28.49 ? 91   TYR   A CA    1 
ATOM   549   C  C     . TYR   A 1  93   ? -11.399 41.970  63.259  1.00 26.64 ? 91   TYR   A C     1 
ATOM   550   O  O     . TYR   A 1  93   ? -10.425 42.696  63.493  1.00 25.94 ? 91   TYR   A O     1 
ATOM   551   C  CB    . TYR   A 1  93   ? -12.492 43.668  61.755  1.00 25.70 ? 91   TYR   A CB    1 
ATOM   552   C  CG    . TYR   A 1  93   ? -12.987 43.917  60.360  1.00 26.76 ? 91   TYR   A CG    1 
ATOM   553   C  CD1   . TYR   A 1  93   ? -12.092 44.077  59.313  1.00 25.64 ? 91   TYR   A CD1   1 
ATOM   554   C  CD2   . TYR   A 1  93   ? -14.344 43.950  60.079  1.00 29.10 ? 91   TYR   A CD2   1 
ATOM   555   C  CE1   . TYR   A 1  93   ? -12.538 44.283  58.022  1.00 27.32 ? 91   TYR   A CE1   1 
ATOM   556   C  CE2   . TYR   A 1  93   ? -14.796 44.162  58.793  1.00 31.11 ? 91   TYR   A CE2   1 
ATOM   557   C  CZ    . TYR   A 1  93   ? -13.886 44.335  57.775  1.00 27.33 ? 91   TYR   A CZ    1 
ATOM   558   O  OH    . TYR   A 1  93   ? -14.320 44.535  56.485  1.00 34.51 ? 91   TYR   A OH    1 
ATOM   559   N  N     . SER   A 1  94   ? -11.768 40.977  64.066  1.00 25.16 ? 92   SER   A N     1 
ATOM   560   C  CA    . SER   A 1  94   ? -11.022 40.632  65.277  1.00 26.06 ? 92   SER   A CA    1 
ATOM   561   C  C     . SER   A 1  94   ? -10.811 41.858  66.161  1.00 22.50 ? 92   SER   A C     1 
ATOM   562   O  O     . SER   A 1  94   ? -9.715  42.109  66.668  1.00 25.49 ? 92   SER   A O     1 
ATOM   563   C  CB    . SER   A 1  94   ? -9.697  39.938  64.947  1.00 27.64 ? 92   SER   A CB    1 
ATOM   564   O  OG    . SER   A 1  94   ? -9.913  38.862  64.044  1.00 33.29 ? 92   SER   A OG    1 
ATOM   565   N  N     . LEU   A 1  95   ? -11.874 42.639  66.333  1.00 20.49 ? 93   LEU   A N     1 
ATOM   566   C  CA    . LEU   A 1  95   ? -11.780 43.866  67.105  1.00 21.92 ? 93   LEU   A CA    1 
ATOM   567   C  C     . LEU   A 1  95   ? -11.804 43.563  68.593  1.00 21.50 ? 93   LEU   A C     1 
ATOM   568   O  O     . LEU   A 1  95   ? -12.577 42.724  69.062  1.00 23.12 ? 93   LEU   A O     1 
ATOM   569   C  CB    . LEU   A 1  95   ? -12.959 44.784  66.786  1.00 19.17 ? 93   LEU   A CB    1 
ATOM   570   C  CG    . LEU   A 1  95   ? -13.091 45.179  65.314  1.00 18.21 ? 93   LEU   A CG    1 
ATOM   571   C  CD1   . LEU   A 1  95   ? -14.233 46.182  65.167  1.00 22.47 ? 93   LEU   A CD1   1 
ATOM   572   C  CD2   . LEU   A 1  95   ? -11.784 45.747  64.785  1.00 21.95 ? 93   LEU   A CD2   1 
ATOM   573   N  N     . SER   A 1  96   ? -10.966 44.269  69.339  1.00 20.08 ? 94   SER   A N     1 
ATOM   574   C  CA    . SER   A 1  96   ? -11.163 44.335  70.773  1.00 19.23 ? 94   SER   A CA    1 
ATOM   575   C  C     . SER   A 1  96   ? -12.413 45.167  71.071  1.00 20.20 ? 94   SER   A C     1 
ATOM   576   O  O     . SER   A 1  96   ? -12.972 45.834  70.197  1.00 19.94 ? 94   SER   A O     1 
ATOM   577   C  CB    . SER   A 1  96   ? -9.965  45.007  71.428  1.00 20.51 ? 94   SER   A CB    1 
ATOM   578   O  OG    . SER   A 1  96   ? -9.903  46.361  71.025  1.00 18.71 ? 94   SER   A OG    1 
ATOM   579   N  N     . SER   A 1  97   ? -12.838 45.146  72.332  1.00 20.89 ? 95   SER   A N     1 
ATOM   580   C  CA    . SER   A 1  97   ? -13.983 45.958  72.731  1.00 20.98 ? 95   SER   A CA    1 
ATOM   581   C  C     . SER   A 1  97   ? -13.716 47.436  72.490  1.00 17.86 ? 95   SER   A C     1 
ATOM   582   O  O     . SER   A 1  97   ? -14.569 48.156  71.958  1.00 17.65 ? 95   SER   A O     1 
ATOM   583   C  CB    . SER   A 1  97   ? -14.312 45.704  74.202  1.00 25.01 ? 95   SER   A CB    1 
ATOM   584   O  OG    . SER   A 1  97   ? -14.920 44.435  74.342  1.00 33.76 ? 95   SER   A OG    1 
ATOM   585   N  N     . GLN   A 1  98   ? -12.534 47.911  72.876  1.00 16.75 ? 96   GLN   A N     1 
ATOM   586   C  CA    . GLN   A 1  98   ? -12.230 49.321  72.672  1.00 17.22 ? 96   GLN   A CA    1 
ATOM   587   C  C     . GLN   A 1  98   ? -12.191 49.663  71.193  1.00 15.91 ? 96   GLN   A C     1 
ATOM   588   O  O     . GLN   A 1  98   ? -12.617 50.753  70.798  1.00 17.09 ? 96   GLN   A O     1 
ATOM   589   C  CB    . GLN   A 1  98   ? -10.921 49.696  73.360  1.00 18.30 ? 96   GLN   A CB    1 
ATOM   590   C  CG    . GLN   A 1  98   ? -11.062 49.762  74.880  1.00 17.35 ? 96   GLN   A CG    1 
ATOM   591   C  CD    . GLN   A 1  98   ? -12.005 50.862  75.331  1.00 18.34 ? 96   GLN   A CD    1 
ATOM   592   O  OE1   . GLN   A 1  98   ? -13.227 50.684  75.353  1.00 20.17 ? 96   GLN   A OE1   1 
ATOM   593   N  NE2   . GLN   A 1  98   ? -11.448 52.011  75.689  1.00 20.50 ? 96   GLN   A NE2   1 
ATOM   594   N  N     . GLU   A 1  99   ? -11.673 48.751  70.363  1.00 16.43 ? 97   GLU   A N     1 
ATOM   595   C  CA    . GLU   A 1  99   ? -11.679 48.978  68.922  1.00 16.08 ? 97   GLU   A CA    1 
ATOM   596   C  C     . GLU   A 1  99   ? -13.099 49.072  68.390  1.00 17.80 ? 97   GLU   A C     1 
ATOM   597   O  O     . GLU   A 1  99   ? -13.414 49.961  67.593  1.00 16.86 ? 97   GLU   A O     1 
ATOM   598   C  CB    . GLU   A 1  99   ? -10.898 47.877  68.220  1.00 15.92 ? 97   GLU   A CB    1 
ATOM   599   C  CG    . GLU   A 1  99   ? -9.408  48.060  68.442  1.00 16.14 ? 97   GLU   A CG    1 
ATOM   600   C  CD    . GLU   A 1  99   ? -8.598  46.892  67.955  1.00 19.27 ? 97   GLU   A CD    1 
ATOM   601   O  OE1   . GLU   A 1  99   ? -9.210  45.888  67.531  1.00 18.86 ? 97   GLU   A OE1   1 
ATOM   602   O  OE2   . GLU   A 1  99   ? -7.351  46.969  68.004  1.00 19.98 ? 97   GLU   A OE2   1 
ATOM   603   N  N     . GLY   A 1  100  ? -13.971 48.158  68.818  1.00 16.84 ? 98   GLY   A N     1 
ATOM   604   C  CA    . GLY   A 1  100  ? -15.365 48.231  68.406  1.00 16.40 ? 98   GLY   A CA    1 
ATOM   605   C  C     . GLY   A 1  100  ? -16.001 49.553  68.784  1.00 17.78 ? 98   GLY   A C     1 
ATOM   606   O  O     . GLY   A 1  100  ? -16.676 50.186  67.973  1.00 17.59 ? 98   GLY   A O     1 
ATOM   607   N  N     . VAL   A 1  101  ? -15.787 49.993  70.025  1.00 16.10 ? 99   VAL   A N     1 
ATOM   608   C  CA    . VAL   A 1  101  ? -16.349 51.264  70.470  1.00 15.73 ? 99   VAL   A CA    1 
ATOM   609   C  C     . VAL   A 1  101  ? -15.782 52.408  69.647  1.00 16.34 ? 99   VAL   A C     1 
ATOM   610   O  O     . VAL   A 1  101  ? -16.521 53.275  69.160  1.00 17.09 ? 99   VAL   A O     1 
ATOM   611   C  CB    . VAL   A 1  101  ? -16.082 51.474  71.968  1.00 16.41 ? 99   VAL   A CB    1 
ATOM   612   C  CG1   . VAL   A 1  101  ? -16.493 52.875  72.371  1.00 17.83 ? 99   VAL   A CG1   1 
ATOM   613   C  CG2   . VAL   A 1  101  ? -16.842 50.435  72.794  1.00 18.73 ? 99   VAL   A CG2   1 
ATOM   614   N  N     . ALA   A 1  102  ? -14.452 52.424  69.479  1.00 15.17 ? 100  ALA   A N     1 
ATOM   615   C  CA    . ALA   A 1  102  ? -13.822 53.515  68.746  1.00 16.45 ? 100  ALA   A CA    1 
ATOM   616   C  C     . ALA   A 1  102  ? -14.306 53.549  67.310  1.00 14.98 ? 100  ALA   A C     1 
ATOM   617   O  O     . ALA   A 1  102  ? -14.538 54.628  66.757  1.00 17.54 ? 100  ALA   A O     1 
ATOM   618   C  CB    . ALA   A 1  102  ? -12.299 53.374  68.793  1.00 17.01 ? 100  ALA   A CB    1 
ATOM   619   N  N     . LEU   A 1  103  ? -14.457 52.374  66.694  1.00 15.02 ? 101  LEU   A N     1 
ATOM   620   C  CA    . LEU   A 1  103  ? -14.982 52.298  65.338  1.00 15.96 ? 101  LEU   A CA    1 
ATOM   621   C  C     . LEU   A 1  103  ? -16.375 52.898  65.257  1.00 16.70 ? 101  LEU   A C     1 
ATOM   622   O  O     . LEU   A 1  103  ? -16.681 53.645  64.322  1.00 18.75 ? 101  LEU   A O     1 
ATOM   623   C  CB    . LEU   A 1  103  ? -15.015 50.845  64.882  1.00 16.27 ? 101  LEU   A CB    1 
ATOM   624   C  CG    . LEU   A 1  103  ? -15.638 50.658  63.501  1.00 18.39 ? 101  LEU   A CG    1 
ATOM   625   C  CD1   . LEU   A 1  103  ? -14.831 51.399  62.437  1.00 19.73 ? 101  LEU   A CD1   1 
ATOM   626   C  CD2   . LEU   A 1  103  ? -15.749 49.198  63.187  1.00 20.45 ? 101  LEU   A CD2   1 
ATOM   627   N  N     . MET   A 1  104  ? -17.243 52.581  66.218  1.00 15.67 ? 102  MET   A N     1 
ATOM   628   C  CA    . MET   A 1  104  ? -18.589 53.132  66.136  1.00 17.40 ? 102  MET   A CA    1 
ATOM   629   C  C     . MET   A 1  104  ? -18.585 54.633  66.362  1.00 17.68 ? 102  MET   A C     1 
ATOM   630   O  O     . MET   A 1  104  ? -19.385 55.351  65.753  1.00 18.75 ? 102  MET   A O     1 
ATOM   631   C  CB    . MET   A 1  104  ? -19.515 52.421  67.116  1.00 18.55 ? 102  MET   A CB    1 
ATOM   632   C  CG    . MET   A 1  104  ? -19.629 50.933  66.820  1.00 19.03 ? 102  MET   A CG    1 
ATOM   633   S  SD    . MET   A 1  104  ? -20.098 50.567  65.098  1.00 26.40 ? 102  MET   A SD    1 
ATOM   634   C  CE    . MET   A 1  104  ? -21.746 51.246  65.058  1.00 27.22 ? 102  MET   A CE    1 
ATOM   635   N  N     . CYS   A 1  105  ? -17.677 55.130  67.203  1.00 15.65 ? 103  CYS   A N     1 
ATOM   636   C  CA    . CYS   A 1  105  ? -17.563 56.573  67.377  1.00 16.18 ? 103  CYS   A CA    1 
ATOM   637   C  C     . CYS   A 1  105  ? -17.098 57.238  66.096  1.00 20.54 ? 103  CYS   A C     1 
ATOM   638   O  O     . CYS   A 1  105  ? -17.603 58.303  65.722  1.00 20.34 ? 103  CYS   A O     1 
ATOM   639   C  CB    . CYS   A 1  105  ? -16.579 56.893  68.497  1.00 17.59 ? 103  CYS   A CB    1 
ATOM   640   S  SG    . CYS   A 1  105  ? -17.140 56.419  70.111  1.00 19.45 ? 103  CYS   A SG    1 
ATOM   641   N  N     . LEU   A 1  106  ? -16.116 56.638  65.425  1.00 17.74 ? 104  LEU   A N     1 
ATOM   642   C  CA    . LEU   A 1  106  ? -15.697 57.155  64.129  1.00 19.33 ? 104  LEU   A CA    1 
ATOM   643   C  C     . LEU   A 1  106  ? -16.857 57.132  63.151  1.00 21.03 ? 104  LEU   A C     1 
ATOM   644   O  O     . LEU   A 1  106  ? -17.066 58.096  62.407  1.00 20.07 ? 104  LEU   A O     1 
ATOM   645   C  CB    . LEU   A 1  106  ? -14.543 56.322  63.575  1.00 19.62 ? 104  LEU   A CB    1 
ATOM   646   C  CG    . LEU   A 1  106  ? -14.168 56.669  62.129  1.00 19.94 ? 104  LEU   A CG    1 
ATOM   647   C  CD1   . LEU   A 1  106  ? -13.632 58.095  62.042  1.00 25.10 ? 104  LEU   A CD1   1 
ATOM   648   C  CD2   . LEU   A 1  106  ? -13.157 55.678  61.595  1.00 22.80 ? 104  LEU   A CD2   1 
ATOM   649   N  N     . ALA   A 1  107  ? -17.612 56.035  63.129  1.00 18.31 ? 105  ALA   A N     1 
ATOM   650   C  CA    . ALA   A 1  107  ? -18.719 55.944  62.190  1.00 20.09 ? 105  ALA   A CA    1 
ATOM   651   C  C     . ALA   A 1  107  ? -19.735 57.039  62.474  1.00 23.23 ? 105  ALA   A C     1 
ATOM   652   O  O     . ALA   A 1  107  ? -20.203 57.716  61.554  1.00 22.07 ? 105  ALA   A O     1 
ATOM   653   C  CB    . ALA   A 1  107  ? -19.357 54.557  62.264  1.00 18.44 ? 105  ALA   A CB    1 
ATOM   654   N  N     . GLU   A 1  108  ? -20.058 57.248  63.754  1.00 20.09 ? 106  GLU   A N     1 
ATOM   655   C  CA    . GLU   A 1  108  ? -20.968 58.325  64.138  1.00 21.43 ? 106  GLU   A CA    1 
ATOM   656   C  C     . GLU   A 1  108  ? -20.472 59.678  63.625  1.00 26.08 ? 106  GLU   A C     1 
ATOM   657   O  O     . GLU   A 1  108  ? -21.249 60.470  63.075  1.00 26.10 ? 106  GLU   A O     1 
ATOM   658   C  CB    . GLU   A 1  108  ? -21.114 58.333  65.663  1.00 22.95 ? 106  GLU   A CB    1 
ATOM   659   C  CG    . GLU   A 1  108  ? -21.924 59.500  66.232  1.00 24.93 ? 106  GLU   A CG    1 
ATOM   660   C  CD    . GLU   A 1  108  ? -21.634 59.757  67.697  1.00 26.34 ? 106  GLU   A CD    1 
ATOM   661   O  OE1   . GLU   A 1  108  ? -21.127 58.843  68.394  1.00 25.77 ? 106  GLU   A OE1   1 
ATOM   662   O  OE2   . GLU   A 1  108  ? -21.898 60.888  68.154  1.00 28.34 ? 106  GLU   A OE2   1 
ATOM   663   N  N     . ALA   A 1  109  ? -19.174 59.946  63.773  1.00 23.14 ? 107  ALA   A N     1 
ATOM   664   C  CA    . ALA   A 1  109  ? -18.606 61.212  63.316  1.00 24.07 ? 107  ALA   A CA    1 
ATOM   665   C  C     . ALA   A 1  109  ? -18.666 61.334  61.801  1.00 27.13 ? 107  ALA   A C     1 
ATOM   666   O  O     . ALA   A 1  109  ? -18.982 62.408  61.271  1.00 28.84 ? 107  ALA   A O     1 
ATOM   667   C  CB    . ALA   A 1  109  ? -17.160 61.335  63.794  1.00 25.89 ? 107  ALA   A CB    1 
ATOM   668   N  N     . LEU   A 1  110  ? -18.359 60.248  61.087  1.00 23.29 ? 108  LEU   A N     1 
ATOM   669   C  CA    . LEU   A 1  110  ? -18.438 60.266  59.631  1.00 23.29 ? 108  LEU   A CA    1 
ATOM   670   C  C     . LEU   A 1  110  ? -19.861 60.509  59.155  1.00 26.94 ? 108  LEU   A C     1 
ATOM   671   O  O     . LEU   A 1  110  ? -20.066 61.120  58.098  1.00 29.37 ? 108  LEU   A O     1 
ATOM   672   C  CB    . LEU   A 1  110  ? -17.900 58.951  59.063  1.00 23.17 ? 108  LEU   A CB    1 
ATOM   673   C  CG    . LEU   A 1  110  ? -16.380 58.821  59.185  1.00 25.33 ? 108  LEU   A CG    1 
ATOM   674   C  CD1   . LEU   A 1  110  ? -15.926 57.412  58.876  1.00 23.59 ? 108  LEU   A CD1   1 
ATOM   675   C  CD2   . LEU   A 1  110  ? -15.683 59.815  58.248  1.00 28.29 ? 108  LEU   A CD2   1 
ATOM   676   N  N     . LEU   A 1  111  ? -20.853 60.045  59.914  1.00 25.22 ? 109  LEU   A N     1 
ATOM   677   C  CA    . LEU   A 1  111  ? -22.246 60.257  59.553  1.00 28.16 ? 109  LEU   A CA    1 
ATOM   678   C  C     . LEU   A 1  111  ? -22.727 61.672  59.841  1.00 34.14 ? 109  LEU   A C     1 
ATOM   679   O  O     . LEU   A 1  111  ? -23.812 62.042  59.378  1.00 34.47 ? 109  LEU   A O     1 
ATOM   680   C  CB    . LEU   A 1  111  ? -23.123 59.223  60.264  1.00 27.39 ? 109  LEU   A CB    1 
ATOM   681   C  CG    . LEU   A 1  111  ? -22.900 57.806  59.720  1.00 25.95 ? 109  LEU   A CG    1 
ATOM   682   C  CD1   . LEU   A 1  111  ? -23.545 56.769  60.611  1.00 28.88 ? 109  LEU   A CD1   1 
ATOM   683   C  CD2   . LEU   A 1  111  ? -23.402 57.677  58.290  1.00 27.59 ? 109  LEU   A CD2   1 
ATOM   684   N  N     . ARG   A 1  112  ? -21.960 62.463  60.595  1.00 32.25 ? 110  ARG   A N     1 
ATOM   685   C  CA    . ARG   A 1  112  ? -22.244 63.886  60.725  1.00 35.38 ? 110  ARG   A CA    1 
ATOM   686   C  C     . ARG   A 1  112  ? -21.863 64.661  59.472  1.00 40.07 ? 110  ARG   A C     1 
ATOM   687   O  O     . ARG   A 1  112  ? -22.258 65.824  59.338  1.00 40.70 ? 110  ARG   A O     1 
ATOM   688   C  CB    . ARG   A 1  112  ? -21.530 64.472  61.944  1.00 32.47 ? 110  ARG   A CB    1 
ATOM   689   C  CG    . ARG   A 1  112  ? -22.023 63.926  63.282  1.00 32.12 ? 110  ARG   A CG    1 
ATOM   690   C  CD    . ARG   A 1  112  ? -21.005 64.154  64.402  1.00 36.98 ? 110  ARG   A CD    1 
ATOM   691   N  NE    . ARG   A 1  112  ? -20.911 65.550  64.812  1.00 43.45 ? 110  ARG   A NE    1 
ATOM   692   C  CZ    . ARG   A 1  112  ? -21.667 66.113  65.746  1.00 53.54 ? 110  ARG   A CZ    1 
ATOM   693   N  NH1   . ARG   A 1  112  ? -22.607 65.430  66.381  1.00 51.41 ? 110  ARG   A NH1   1 
ATOM   694   N  NH2   . ARG   A 1  112  ? -21.476 67.393  66.052  1.00 55.40 ? 110  ARG   A NH2   1 
ATOM   695   N  N     . ILE   A 1  113  ? -21.099 64.054  58.570  1.00 36.60 ? 111  ILE   A N     1 
ATOM   696   C  CA    . ILE   A 1  113  ? -20.849 64.612  57.244  1.00 37.32 ? 111  ILE   A CA    1 
ATOM   697   C  C     . ILE   A 1  113  ? -22.066 64.325  56.375  1.00 38.75 ? 111  ILE   A C     1 
ATOM   698   O  O     . ILE   A 1  113  ? -22.354 63.157  56.078  1.00 42.40 ? 111  ILE   A O     1 
ATOM   699   C  CB    . ILE   A 1  113  ? -19.568 64.027  56.635  1.00 34.19 ? 111  ILE   A CB    1 
ATOM   700   C  CG1   . ILE   A 1  113  ? -18.349 64.513  57.415  1.00 34.59 ? 111  ILE   A CG1   1 
ATOM   701   C  CG2   . ILE   A 1  113  ? -19.457 64.397  55.165  1.00 41.20 ? 111  ILE   A CG2   1 
ATOM   702   C  CD1   . ILE   A 1  113  ? -17.092 63.785  57.062  1.00 36.23 ? 111  ILE   A CD1   1 
ATOM   703   N  N     . PRO   A 1  114  ? -22.809 65.350  55.945  1.00 47.21 ? 112  PRO   A N     1 
ATOM   704   C  CA    . PRO   A 1  114  ? -24.081 65.103  55.249  1.00 41.59 ? 112  PRO   A CA    1 
ATOM   705   C  C     . PRO   A 1  114  ? -23.952 64.510  53.852  1.00 41.62 ? 112  PRO   A C     1 
ATOM   706   O  O     . PRO   A 1  114  ? -24.630 63.527  53.535  1.00 49.85 ? 112  PRO   A O     1 
ATOM   707   C  CB    . PRO   A 1  114  ? -24.737 66.491  55.212  1.00 42.48 ? 112  PRO   A CB    1 
ATOM   708   C  CG    . PRO   A 1  114  ? -24.044 67.276  56.291  1.00 48.61 ? 112  PRO   A CG    1 
ATOM   709   C  CD    . PRO   A 1  114  ? -22.634 66.770  56.285  1.00 47.14 ? 112  PRO   A CD    1 
ATOM   710   N  N     . ASP   A 1  115  ? -23.105 65.095  53.005  1.00 49.83 ? 113  ASP   A N     1 
ATOM   711   C  CA    . ASP   A 1  115  ? -22.984 64.641  51.622  1.00 48.94 ? 113  ASP   A CA    1 
ATOM   712   C  C     . ASP   A 1  115  ? -22.305 63.277  51.578  1.00 46.80 ? 113  ASP   A C     1 
ATOM   713   O  O     . ASP   A 1  115  ? -21.173 63.125  52.048  1.00 45.64 ? 113  ASP   A O     1 
ATOM   714   C  CB    . ASP   A 1  115  ? -22.190 65.655  50.803  1.00 45.37 ? 113  ASP   A CB    1 
ATOM   715   N  N     . THR   A 1  116  ? -22.992 62.292  50.995  1.00 46.22 ? 114  THR   A N     1 
ATOM   716   C  CA    . THR   A 1  116  ? -22.479 60.924  50.986  1.00 40.40 ? 114  THR   A CA    1 
ATOM   717   C  C     . THR   A 1  116  ? -21.172 60.816  50.207  1.00 46.35 ? 114  THR   A C     1 
ATOM   718   O  O     . THR   A 1  116  ? -20.236 60.138  50.646  1.00 40.25 ? 114  THR   A O     1 
ATOM   719   C  CB    . THR   A 1  116  ? -23.531 59.978  50.409  1.00 42.88 ? 114  THR   A CB    1 
ATOM   720   O  OG1   . THR   A 1  116  ? -24.673 59.953  51.273  1.00 48.77 ? 114  THR   A OG1   1 
ATOM   721   C  CG2   . THR   A 1  116  ? -22.970 58.570  50.274  1.00 45.69 ? 114  THR   A CG2   1 
ATOM   722   N  N     . ALA   A 1  117  ? -21.089 61.469  49.047  1.00 41.29 ? 115  ALA   A N     1 
ATOM   723   C  CA    . ALA   A 1  117  ? -19.860 61.406  48.264  1.00 41.83 ? 115  ALA   A CA    1 
ATOM   724   C  C     . ALA   A 1  117  ? -18.707 62.068  49.002  1.00 39.54 ? 115  ALA   A C     1 
ATOM   725   O  O     . ALA   A 1  117  ? -17.560 61.616  48.910  1.00 37.75 ? 115  ALA   A O     1 
ATOM   726   C  CB    . ALA   A 1  117  ? -20.067 62.041  46.887  1.00 45.30 ? 115  ALA   A CB    1 
ATOM   727   N  N     . THR   A 1  118  ? -18.989 63.145  49.739  1.00 38.66 ? 116  THR   A N     1 
ATOM   728   C  CA    . THR   A 1  118  ? -17.937 63.793  50.512  1.00 39.45 ? 116  THR   A CA    1 
ATOM   729   C  C     . THR   A 1  118  ? -17.417 62.864  51.599  1.00 36.07 ? 116  THR   A C     1 
ATOM   730   O  O     . THR   A 1  118  ? -16.204 62.759  51.812  1.00 38.65 ? 116  THR   A O     1 
ATOM   731   C  CB    . THR   A 1  118  ? -18.459 65.085  51.140  1.00 38.82 ? 116  THR   A CB    1 
ATOM   732   O  OG1   . THR   A 1  118  ? -19.018 65.924  50.121  1.00 51.13 ? 116  THR   A OG1   1 
ATOM   733   C  CG2   . THR   A 1  118  ? -17.330 65.822  51.832  1.00 39.39 ? 116  THR   A CG2   1 
ATOM   734   N  N     . ARG   A 1  119  ? -18.324 62.178  52.293  1.00 35.56 ? 117  ARG   A N     1 
ATOM   735   C  CA    . ARG   A 1  119  ? -17.914 61.267  53.357  1.00 35.91 ? 117  ARG   A CA    1 
ATOM   736   C  C     . ARG   A 1  119  ? -17.056 60.135  52.803  1.00 33.23 ? 117  ARG   A C     1 
ATOM   737   O  O     . ARG   A 1  119  ? -16.002 59.807  53.360  1.00 34.04 ? 117  ARG   A O     1 
ATOM   738   C  CB    . ARG   A 1  119  ? -19.158 60.712  54.047  1.00 33.78 ? 117  ARG   A CB    1 
ATOM   739   C  CG    . ARG   A 1  119  ? -18.870 59.795  55.225  1.00 29.76 ? 117  ARG   A CG    1 
ATOM   740   C  CD    . ARG   A 1  119  ? -20.128 59.040  55.628  1.00 32.37 ? 117  ARG   A CD    1 
ATOM   741   N  NE    . ARG   A 1  119  ? -21.272 59.927  55.804  1.00 34.38 ? 117  ARG   A NE    1 
ATOM   742   C  CZ    . ARG   A 1  119  ? -22.437 59.779  55.189  1.00 31.28 ? 117  ARG   A CZ    1 
ATOM   743   N  NH1   . ARG   A 1  119  ? -22.662 58.768  54.366  1.00 35.42 ? 117  ARG   A NH1   1 
ATOM   744   N  NH2   . ARG   A 1  119  ? -23.405 60.663  55.414  1.00 42.77 ? 117  ARG   A NH2   1 
ATOM   745   N  N     . ASP   A 1  120  ? -17.495 59.529  51.696  1.00 36.06 ? 118  ASP   A N     1 
ATOM   746   C  CA    . ASP   A 1  120  ? -16.761 58.408  51.117  1.00 35.46 ? 118  ASP   A CA    1 
ATOM   747   C  C     . ASP   A 1  120  ? -15.371 58.833  50.666  1.00 38.55 ? 118  ASP   A C     1 
ATOM   748   O  O     . ASP   A 1  120  ? -14.409 58.063  50.786  1.00 37.63 ? 118  ASP   A O     1 
ATOM   749   C  CB    . ASP   A 1  120  ? -17.553 57.798  49.961  1.00 35.29 ? 118  ASP   A CB    1 
ATOM   750   C  CG    . ASP   A 1  120  ? -18.903 57.278  50.402  1.00 42.58 ? 118  ASP   A CG    1 
ATOM   751   O  OD1   . ASP   A 1  120  ? -19.206 57.383  51.607  1.00 42.95 ? 118  ASP   A OD1   1 
ATOM   752   O  OD2   . ASP   A 1  120  ? -19.663 56.766  49.552  1.00 42.78 ? 118  ASP   A OD2   1 
ATOM   753   N  N     . ALA   A 1  121  ? -15.242 60.059  50.149  1.00 39.90 ? 119  ALA   A N     1 
ATOM   754   C  CA    . ALA   A 1  121  ? -13.934 60.555  49.730  1.00 40.39 ? 119  ALA   A CA    1 
ATOM   755   C  C     . ALA   A 1  121  ? -13.010 60.761  50.924  1.00 37.39 ? 119  ALA   A C     1 
ATOM   756   O  O     . ALA   A 1  121  ? -11.822 60.418  50.867  1.00 41.96 ? 119  ALA   A O     1 
ATOM   757   C  CB    . ALA   A 1  121  ? -14.096 61.855  48.943  1.00 37.21 ? 119  ALA   A CB    1 
ATOM   758   N  N     . LEU   A 1  122  ? -13.536 61.328  52.012  1.00 41.51 ? 120  LEU   A N     1 
ATOM   759   C  CA    . LEU   A 1  122  ? -12.737 61.475  53.223  1.00 38.28 ? 120  LEU   A CA    1 
ATOM   760   C  C     . LEU   A 1  122  ? -12.288 60.117  53.746  1.00 37.23 ? 120  LEU   A C     1 
ATOM   761   O  O     . LEU   A 1  122  ? -11.136 59.952  54.161  1.00 37.24 ? 120  LEU   A O     1 
ATOM   762   C  CB    . LEU   A 1  122  ? -13.540 62.221  54.286  1.00 39.33 ? 120  LEU   A CB    1 
ATOM   763   C  CG    . LEU   A 1  122  ? -12.727 62.711  55.484  1.00 34.06 ? 120  LEU   A CG    1 
ATOM   764   C  CD1   . LEU   A 1  122  ? -11.808 63.848  55.073  1.00 40.99 ? 120  LEU   A CD1   1 
ATOM   765   C  CD2   . LEU   A 1  122  ? -13.624 63.130  56.632  1.00 34.66 ? 120  LEU   A CD2   1 
ATOM   766   N  N     . ILE   A 1  123  ? -13.182 59.128  53.716  1.00 35.59 ? 121  ILE   A N     1 
ATOM   767   C  CA    . ILE   A 1  123  ? -12.833 57.783  54.166  1.00 36.31 ? 121  ILE   A CA    1 
ATOM   768   C  C     . ILE   A 1  123  ? -11.711 57.211  53.310  1.00 38.02 ? 121  ILE   A C     1 
ATOM   769   O  O     . ILE   A 1  123  ? -10.657 56.812  53.818  1.00 36.88 ? 121  ILE   A O     1 
ATOM   770   C  CB    . ILE   A 1  123  ? -14.071 56.870  54.153  1.00 33.88 ? 121  ILE   A CB    1 
ATOM   771   C  CG1   . ILE   A 1  123  ? -15.079 57.299  55.224  1.00 29.98 ? 121  ILE   A CG1   1 
ATOM   772   C  CG2   . ILE   A 1  123  ? -13.654 55.405  54.307  1.00 31.58 ? 121  ILE   A CG2   1 
ATOM   773   C  CD1   . ILE   A 1  123  ? -16.396 56.591  55.109  1.00 29.53 ? 121  ILE   A CD1   1 
ATOM   774   N  N     . ARG   A 1  124  ? -11.923 57.172  51.991  1.00 37.93 ? 122  ARG   A N     1 
ATOM   775   C  CA    . ARG   A 1  124  ? -10.985 56.486  51.106  1.00 34.29 ? 122  ARG   A CA    1 
ATOM   776   C  C     . ARG   A 1  124  ? -9.642  57.203  51.043  1.00 41.16 ? 122  ARG   A C     1 
ATOM   777   O  O     . ARG   A 1  124  ? -8.587  56.556  51.040  1.00 44.65 ? 122  ARG   A O     1 
ATOM   778   C  CB    . ARG   A 1  124  ? -11.587 56.352  49.707  1.00 38.46 ? 122  ARG   A CB    1 
ATOM   779   N  N     . ASP   A 1  125  ? -9.654  58.535  51.010  1.00 44.31 ? 123  ASP   A N     1 
ATOM   780   C  CA    . ASP   A 1  125  ? -8.440  59.293  50.734  1.00 49.83 ? 123  ASP   A CA    1 
ATOM   781   C  C     . ASP   A 1  125  ? -7.750  59.839  51.976  1.00 49.93 ? 123  ASP   A C     1 
ATOM   782   O  O     . ASP   A 1  125  ? -6.555  60.150  51.908  1.00 53.12 ? 123  ASP   A O     1 
ATOM   783   C  CB    . ASP   A 1  125  ? -8.740  60.450  49.770  1.00 53.24 ? 123  ASP   A CB    1 
ATOM   784   C  CG    . ASP   A 1  125  ? -9.368  59.979  48.472  1.00 55.44 ? 123  ASP   A CG    1 
ATOM   785   O  OD1   . ASP   A 1  125  ? -8.979  58.898  47.979  1.00 57.03 ? 123  ASP   A OD1   1 
ATOM   786   O  OD2   . ASP   A 1  125  ? -10.254 60.687  47.946  1.00 56.47 ? 123  ASP   A OD2   1 
ATOM   787   N  N     . LYS   A 1  126  ? -8.453  59.956  53.102  1.00 46.05 ? 124  LYS   A N     1 
ATOM   788   C  CA    . LYS   A 1  126  ? -7.881  60.598  54.281  1.00 42.60 ? 124  LYS   A CA    1 
ATOM   789   C  C     . LYS   A 1  126  ? -7.933  59.713  55.525  1.00 45.19 ? 124  LYS   A C     1 
ATOM   790   O  O     . LYS   A 1  126  ? -6.908  59.506  56.183  1.00 48.94 ? 124  LYS   A O     1 
ATOM   791   C  CB    . LYS   A 1  126  ? -8.574  61.937  54.551  1.00 49.60 ? 124  LYS   A CB    1 
ATOM   792   C  CG    . LYS   A 1  126  ? -8.469  62.945  53.411  1.00 51.97 ? 124  LYS   A CG    1 
ATOM   793   C  CD    . LYS   A 1  126  ? -7.025  63.366  53.170  1.00 53.21 ? 124  LYS   A CD    1 
ATOM   794   C  CE    . LYS   A 1  126  ? -6.946  64.594  52.272  1.00 59.86 ? 124  LYS   A CE    1 
ATOM   795   N  NZ    . LYS   A 1  126  ? -5.555  65.119  52.158  1.00 61.18 ? 124  LYS   A NZ    1 
ATOM   796   N  N     . ILE   A 1  127  ? -9.116  59.196  55.862  1.00 41.07 ? 125  ILE   A N     1 
ATOM   797   C  CA    . ILE   A 1  127  ? -9.262  58.420  57.094  1.00 37.55 ? 125  ILE   A CA    1 
ATOM   798   C  C     . ILE   A 1  127  ? -8.506  57.102  56.992  1.00 40.79 ? 125  ILE   A C     1 
ATOM   799   O  O     . ILE   A 1  127  ? -7.721  56.747  57.880  1.00 44.30 ? 125  ILE   A O     1 
ATOM   800   C  CB    . ILE   A 1  127  ? -10.746 58.190  57.428  1.00 36.12 ? 125  ILE   A CB    1 
ATOM   801   C  CG1   . ILE   A 1  127  ? -11.516 59.514  57.443  1.00 39.87 ? 125  ILE   A CG1   1 
ATOM   802   C  CG2   . ILE   A 1  127  ? -10.881 57.482  58.774  1.00 34.96 ? 125  ILE   A CG2   1 
ATOM   803   C  CD1   . ILE   A 1  127  ? -10.941 60.545  58.377  1.00 40.26 ? 125  ILE   A CD1   1 
ATOM   804   N  N     . ALA   A 1  128  ? -8.749  56.348  55.918  1.00 34.98 ? 126  ALA   A N     1 
ATOM   805   C  CA    . ALA   A 1  128  ? -8.120  55.041  55.770  1.00 37.43 ? 126  ALA   A CA    1 
ATOM   806   C  C     . ALA   A 1  128  ? -6.609  55.157  55.660  1.00 44.48 ? 126  ALA   A C     1 
ATOM   807   O  O     . ALA   A 1  128  ? -5.886  54.282  56.148  1.00 42.41 ? 126  ALA   A O     1 
ATOM   808   C  CB    . ALA   A 1  128  ? -8.693  54.313  54.553  1.00 35.79 ? 126  ALA   A CB    1 
ATOM   809   N  N     . ASP   A 1  129  ? -6.120  56.237  55.041  1.00 55.63 ? 127  ASP   A N     1 
ATOM   810   C  CA    . ASP   A 1  129  ? -4.692  56.451  54.837  1.00 59.78 ? 127  ASP   A CA    1 
ATOM   811   C  C     . ASP   A 1  129  ? -3.929  56.676  56.136  1.00 57.36 ? 127  ASP   A C     1 
ATOM   812   O  O     . ASP   A 1  129  ? -2.695  56.596  56.130  1.00 64.59 ? 127  ASP   A O     1 
ATOM   813   C  CB    . ASP   A 1  129  ? -4.465  57.625  53.879  1.00 57.95 ? 127  ASP   A CB    1 
ATOM   814   N  N     . GLY   A 1  130  ? -4.618  56.955  57.239  1.00 60.66 ? 128  GLY   A N     1 
ATOM   815   C  CA    . GLY   A 1  130  ? -3.947  57.044  58.518  1.00 59.70 ? 128  GLY   A CA    1 
ATOM   816   C  C     . GLY   A 1  130  ? -4.486  58.116  59.440  1.00 62.12 ? 128  GLY   A C     1 
ATOM   817   O  O     . GLY   A 1  130  ? -5.296  57.831  60.327  1.00 59.98 ? 128  GLY   A O     1 
ATOM   818   N  N     . ASN   A 1  131  ? -4.043  59.355  59.231  1.00 64.26 ? 129  ASN   A N     1 
ATOM   819   C  CA    . ASN   A 1  131  ? -4.318  60.450  60.155  1.00 63.24 ? 129  ASN   A CA    1 
ATOM   820   C  C     . ASN   A 1  131  ? -5.808  60.745  60.282  1.00 50.24 ? 129  ASN   A C     1 
ATOM   821   O  O     . ASN   A 1  131  ? -6.306  61.707  59.690  1.00 58.75 ? 129  ASN   A O     1 
ATOM   822   C  CB    . ASN   A 1  131  ? -3.562  61.710  59.721  1.00 60.56 ? 129  ASN   A CB    1 
ATOM   823   N  N     . TRP   A 1  132  ? -6.530  59.929  61.058  1.00 48.03 ? 130  TRP   A N     1 
ATOM   824   C  CA    . TRP   A 1  132  ? -7.940  60.219  61.304  1.00 38.07 ? 130  TRP   A CA    1 
ATOM   825   C  C     . TRP   A 1  132  ? -8.111  61.439  62.197  1.00 36.76 ? 130  TRP   A C     1 
ATOM   826   O  O     . TRP   A 1  132  ? -9.110  62.158  62.079  1.00 44.72 ? 130  TRP   A O     1 
ATOM   827   C  CB    . TRP   A 1  132  ? -8.643  59.012  61.929  1.00 38.87 ? 130  TRP   A CB    1 
ATOM   828   C  CG    . TRP   A 1  132  ? -8.090  58.606  63.271  1.00 32.13 ? 130  TRP   A CG    1 
ATOM   829   C  CD1   . TRP   A 1  132  ? -7.166  57.629  63.510  1.00 29.72 ? 130  TRP   A CD1   1 
ATOM   830   C  CD2   . TRP   A 1  132  ? -8.430  59.157  64.554  1.00 25.72 ? 130  TRP   A CD2   1 
ATOM   831   N  NE1   . TRP   A 1  132  ? -6.912  57.537  64.858  1.00 29.13 ? 130  TRP   A NE1   1 
ATOM   832   C  CE2   . TRP   A 1  132  ? -7.668  58.466  65.521  1.00 24.98 ? 130  TRP   A CE2   1 
ATOM   833   C  CE3   . TRP   A 1  132  ? -9.297  60.165  64.979  1.00 28.72 ? 130  TRP   A CE3   1 
ATOM   834   C  CZ2   . TRP   A 1  132  ? -7.744  58.754  66.880  1.00 24.73 ? 130  TRP   A CZ2   1 
ATOM   835   C  CZ3   . TRP   A 1  132  ? -9.373  60.450  66.332  1.00 24.83 ? 130  TRP   A CZ3   1 
ATOM   836   C  CH2   . TRP   A 1  132  ? -8.609  59.741  67.269  1.00 24.16 ? 130  TRP   A CH2   1 
ATOM   837   N  N     . LYS   A 1  133  ? -7.161  61.675  63.105  1.00 42.17 ? 131  LYS   A N     1 
ATOM   838   C  CA    . LYS   A 1  133  ? -7.259  62.828  63.993  1.00 48.19 ? 131  LYS   A CA    1 
ATOM   839   C  C     . LYS   A 1  133  ? -7.142  64.131  63.214  1.00 55.41 ? 131  LYS   A C     1 
ATOM   840   O  O     . LYS   A 1  133  ? -7.852  65.100  63.504  1.00 60.10 ? 131  LYS   A O     1 
ATOM   841   C  CB    . LYS   A 1  133  ? -6.186  62.743  65.078  1.00 44.07 ? 131  LYS   A CB    1 
ATOM   842   N  N     . SER   A 1  134  ? -6.266  64.162  62.206  1.00 55.70 ? 132  SER   A N     1 
ATOM   843   C  CA    . SER   A 1  134  ? -6.051  65.377  61.431  1.00 60.13 ? 132  SER   A CA    1 
ATOM   844   C  C     . SER   A 1  134  ? -7.307  65.837  60.701  1.00 62.48 ? 132  SER   A C     1 
ATOM   845   O  O     . SER   A 1  134  ? -7.420  67.024  60.379  1.00 68.09 ? 132  SER   A O     1 
ATOM   846   C  CB    . SER   A 1  134  ? -4.907  65.168  60.435  1.00 55.16 ? 132  SER   A CB    1 
ATOM   847   N  N     . HIS   A 1  135  ? -8.259  64.936  60.444  1.00 61.44 ? 133  HIS   A N     1 
ATOM   848   C  CA    . HIS   A 1  135  ? -9.438  65.275  59.660  1.00 58.88 ? 133  HIS   A CA    1 
ATOM   849   C  C     . HIS   A 1  135  ? -10.739 65.287  60.450  1.00 60.04 ? 133  HIS   A C     1 
ATOM   850   O  O     . HIS   A 1  135  ? -11.711 65.892  59.988  1.00 61.38 ? 133  HIS   A O     1 
ATOM   851   C  CB    . HIS   A 1  135  ? -9.581  64.325  58.460  1.00 56.41 ? 133  HIS   A CB    1 
ATOM   852   C  CG    . HIS   A 1  135  ? -8.345  64.221  57.621  1.00 62.99 ? 133  HIS   A CG    1 
ATOM   853   N  ND1   . HIS   A 1  135  ? -7.406  63.227  57.799  1.00 63.29 ? 133  HIS   A ND1   1 
ATOM   854   C  CD2   . HIS   A 1  135  ? -7.887  64.994  56.608  1.00 59.18 ? 133  HIS   A CD2   1 
ATOM   855   C  CE1   . HIS   A 1  135  ? -6.425  63.389  56.929  1.00 68.40 ? 133  HIS   A CE1   1 
ATOM   856   N  NE2   . HIS   A 1  135  ? -6.692  64.455  56.195  1.00 69.15 ? 133  HIS   A NE2   1 
ATOM   857   N  N     . LEU   A 1  136  ? -10.789 64.647  61.613  1.00 54.78 ? 134  LEU   A N     1 
ATOM   858   C  CA    . LEU   A 1  136  ? -12.011 64.643  62.415  1.00 55.26 ? 134  LEU   A CA    1 
ATOM   859   C  C     . LEU   A 1  136  ? -11.718 64.918  63.888  1.00 59.26 ? 134  LEU   A C     1 
ATOM   860   O  O     . LEU   A 1  136  ? -12.629 65.204  64.668  1.00 59.88 ? 134  LEU   A O     1 
ATOM   861   C  CB    . LEU   A 1  136  ? -12.759 63.312  62.267  1.00 52.82 ? 134  LEU   A CB    1 
ATOM   862   C  CG    . LEU   A 1  136  ? -13.410 62.977  60.922  1.00 46.99 ? 134  LEU   A CG    1 
ATOM   863   C  CD1   . LEU   A 1  136  ? -13.801 61.514  60.886  1.00 37.45 ? 134  LEU   A CD1   1 
ATOM   864   C  CD2   . LEU   A 1  136  ? -14.627 63.849  60.660  1.00 35.82 ? 134  LEU   A CD2   1 
ATOM   865   N  N     . SER   A 1  139  ? -12.532 70.147  67.372  1.00 45.78 ? 137  SER   A N     1 
ATOM   866   C  CA    . SER   A 1  139  ? -13.258 70.944  68.360  1.00 49.03 ? 137  SER   A CA    1 
ATOM   867   C  C     . SER   A 1  139  ? -14.200 70.085  69.207  1.00 48.38 ? 137  SER   A C     1 
ATOM   868   O  O     . SER   A 1  139  ? -14.799 70.564  70.175  1.00 46.82 ? 137  SER   A O     1 
ATOM   869   C  CB    . SER   A 1  139  ? -14.047 72.060  67.670  1.00 53.59 ? 137  SER   A CB    1 
ATOM   870   N  N     . ARG   A 1  140  ? -14.331 68.816  68.830  1.00 37.20 ? 138  ARG   A N     1 
ATOM   871   C  CA    . ARG   A 1  140  ? -15.200 67.877  69.532  1.00 30.43 ? 138  ARG   A CA    1 
ATOM   872   C  C     . ARG   A 1  140  ? -14.555 66.506  69.431  1.00 32.42 ? 138  ARG   A C     1 
ATOM   873   O  O     . ARG   A 1  140  ? -14.277 66.035  68.323  1.00 31.31 ? 138  ARG   A O     1 
ATOM   874   C  CB    . ARG   A 1  140  ? -16.592 67.857  68.895  1.00 35.92 ? 138  ARG   A CB    1 
ATOM   875   C  CG    . ARG   A 1  140  ? -17.492 66.690  69.306  1.00 38.51 ? 138  ARG   A CG    1 
ATOM   876   C  CD    . ARG   A 1  140  ? -18.666 66.554  68.333  1.00 44.03 ? 138  ARG   A CD    1 
ATOM   877   N  NE    . ARG   A 1  140  ? -19.573 65.461  68.672  1.00 45.21 ? 138  ARG   A NE    1 
ATOM   878   C  CZ    . ARG   A 1  140  ? -19.463 64.221  68.213  1.00 51.85 ? 138  ARG   A CZ    1 
ATOM   879   N  NH1   . ARG   A 1  140  ? -18.476 63.867  67.402  1.00 45.73 ? 138  ARG   A NH1   1 
ATOM   880   N  NH2   . ARG   A 1  140  ? -20.366 63.312  68.574  1.00 47.77 ? 138  ARG   A NH2   1 
ATOM   881   N  N     . SER   A 1  141  ? -14.301 65.886  70.580  1.00 26.75 ? 139  SER   A N     1 
ATOM   882   C  CA    . SER   A 1  141  ? -13.735 64.548  70.593  1.00 24.21 ? 139  SER   A CA    1 
ATOM   883   C  C     . SER   A 1  141  ? -14.603 63.613  69.768  1.00 22.80 ? 139  SER   A C     1 
ATOM   884   O  O     . SER   A 1  141  ? -15.835 63.675  69.805  1.00 24.27 ? 139  SER   A O     1 
ATOM   885   C  CB    . SER   A 1  141  ? -13.677 64.030  72.028  1.00 25.64 ? 139  SER   A CB    1 
ATOM   886   O  OG    . SER   A 1  141  ? -13.192 62.696  72.078  1.00 23.20 ? 139  SER   A OG    1 
ATOM   887   N  N     . LEU   A 1  142  ? -13.949 62.732  69.014  1.00 22.94 ? 140  LEU   A N     1 
ATOM   888   C  CA    . LEU   A 1  142  ? -14.685 61.681  68.334  1.00 22.58 ? 140  LEU   A CA    1 
ATOM   889   C  C     . LEU   A 1  142  ? -15.465 60.824  69.316  1.00 19.20 ? 140  LEU   A C     1 
ATOM   890   O  O     . LEU   A 1  142  ? -16.454 60.190  68.936  1.00 20.30 ? 140  LEU   A O     1 
ATOM   891   C  CB    . LEU   A 1  142  ? -13.682 60.792  67.608  1.00 23.10 ? 140  LEU   A CB    1 
ATOM   892   C  CG    . LEU   A 1  142  ? -14.001 60.435  66.174  1.00 28.64 ? 140  LEU   A CG    1 
ATOM   893   C  CD1   . LEU   A 1  142  ? -13.922 61.670  65.310  1.00 33.96 ? 140  LEU   A CD1   1 
ATOM   894   C  CD2   . LEU   A 1  142  ? -13.000 59.411  65.724  1.00 28.70 ? 140  LEU   A CD2   1 
ATOM   895   N  N     . PHE   A 1  143  ? -15.061 60.825  70.582  1.00 19.22 ? 141  PHE   A N     1 
ATOM   896   C  CA    . PHE   A 1  143  ? -15.486 59.830  71.545  1.00 18.41 ? 141  PHE   A CA    1 
ATOM   897   C  C     . PHE   A 1  143  ? -16.498 60.381  72.542  1.00 19.65 ? 141  PHE   A C     1 
ATOM   898   O  O     . PHE   A 1  143  ? -16.749 59.748  73.562  1.00 19.73 ? 141  PHE   A O     1 
ATOM   899   C  CB    . PHE   A 1  143  ? -14.250 59.230  72.224  1.00 17.19 ? 141  PHE   A CB    1 
ATOM   900   C  CG    . PHE   A 1  143  ? -13.233 58.741  71.233  1.00 17.00 ? 141  PHE   A CG    1 
ATOM   901   C  CD1   . PHE   A 1  143  ? -13.574 57.745  70.327  1.00 16.36 ? 141  PHE   A CD1   1 
ATOM   902   C  CD2   . PHE   A 1  143  ? -11.968 59.305  71.165  1.00 18.34 ? 141  PHE   A CD2   1 
ATOM   903   C  CE1   . PHE   A 1  143  ? -12.677 57.307  69.400  1.00 17.12 ? 141  PHE   A CE1   1 
ATOM   904   C  CE2   . PHE   A 1  143  ? -11.066 58.859  70.234  1.00 18.57 ? 141  PHE   A CE2   1 
ATOM   905   C  CZ    . PHE   A 1  143  ? -11.414 57.867  69.347  1.00 16.35 ? 141  PHE   A CZ    1 
ATOM   906   N  N     . VAL   A 1  144  ? -17.120 61.524  72.223  1.00 18.52 ? 142  VAL   A N     1 
ATOM   907   C  CA    . VAL   A 1  144  ? -18.077 62.157  73.133  1.00 20.63 ? 142  VAL   A CA    1 
ATOM   908   C  C     . VAL   A 1  144  ? -19.163 61.181  73.557  1.00 21.58 ? 142  VAL   A C     1 
ATOM   909   O  O     . VAL   A 1  144  ? -19.579 61.163  74.722  1.00 23.16 ? 142  VAL   A O     1 
ATOM   910   C  CB    . VAL   A 1  144  ? -18.664 63.437  72.502  1.00 23.02 ? 142  VAL   A CB    1 
ATOM   911   C  CG1   . VAL   A 1  144  ? -19.868 63.940  73.301  1.00 26.67 ? 142  VAL   A CG1   1 
ATOM   912   C  CG2   . VAL   A 1  144  ? -17.601 64.520  72.410  1.00 23.84 ? 142  VAL   A CG2   1 
ATOM   913   N  N     . ASN   A 1  145  ? -19.644 60.357  72.628  1.00 19.99 ? 143  ASN   A N     1 
ATOM   914   C  CA    . ASN   A 1  145  ? -20.709 59.407  72.924  1.00 22.38 ? 143  ASN   A CA    1 
ATOM   915   C  C     . ASN   A 1  145  ? -20.195 57.990  73.122  1.00 22.56 ? 143  ASN   A C     1 
ATOM   916   O  O     . ASN   A 1  145  ? -20.960 57.032  72.986  1.00 20.61 ? 143  ASN   A O     1 
ATOM   917   C  CB    . ASN   A 1  145  ? -21.783 59.445  71.836  1.00 22.34 ? 143  ASN   A CB    1 
ATOM   918   C  CG    . ASN   A 1  145  ? -22.554 60.738  71.843  1.00 22.97 ? 143  ASN   A CG    1 
ATOM   919   O  OD1   . ASN   A 1  145  ? -23.051 61.156  72.888  1.00 29.95 ? 143  ASN   A OD1   1 
ATOM   920   N  ND2   . ASN   A 1  145  ? -22.629 61.395  70.696  1.00 27.81 ? 143  ASN   A ND2   1 
ATOM   921   N  N     . ALA   A 1  146  ? -18.918 57.832  73.471  1.00 18.29 ? 144  ALA   A N     1 
ATOM   922   C  CA    . ALA   A 1  146  ? -18.372 56.486  73.583  1.00 19.34 ? 144  ALA   A CA    1 
ATOM   923   C  C     . ALA   A 1  146  ? -18.999 55.671  74.708  1.00 17.51 ? 144  ALA   A C     1 
ATOM   924   O  O     . ALA   A 1  146  ? -18.991 54.437  74.641  1.00 22.40 ? 144  ALA   A O     1 
ATOM   925   C  CB    . ALA   A 1  146  ? -16.859 56.539  73.761  1.00 18.47 ? 144  ALA   A CB    1 
ATOM   926   N  N     . ALA   A 1  147  ? -19.547 56.314  75.743  1.00 19.42 ? 145  ALA   A N     1 
ATOM   927   C  CA    . ALA   A 1  147  ? -20.214 55.531  76.779  1.00 23.34 ? 145  ALA   A CA    1 
ATOM   928   C  C     . ALA   A 1  147  ? -21.422 54.814  76.205  1.00 24.09 ? 145  ALA   A C     1 
ATOM   929   O  O     . ALA   A 1  147  ? -21.709 53.662  76.562  1.00 22.94 ? 145  ALA   A O     1 
ATOM   930   C  CB    . ALA   A 1  147  ? -20.616 56.422  77.955  1.00 25.39 ? 145  ALA   A CB    1 
ATOM   931   N  N     . THR   A 1  148  ? -22.131 55.475  75.291  1.00 20.70 ? 146  THR   A N     1 
ATOM   932   C  CA    . THR   A 1  148  ? -23.276 54.852  74.646  1.00 21.06 ? 146  THR   A CA    1 
ATOM   933   C  C     . THR   A 1  148  ? -22.829 53.706  73.753  1.00 19.89 ? 146  THR   A C     1 
ATOM   934   O  O     . THR   A 1  148  ? -23.369 52.597  73.825  1.00 21.59 ? 146  THR   A O     1 
ATOM   935   C  CB    . THR   A 1  148  ? -24.028 55.908  73.844  1.00 24.87 ? 146  THR   A CB    1 
ATOM   936   O  OG1   . THR   A 1  148  ? -24.435 56.956  74.729  1.00 25.80 ? 146  THR   A OG1   1 
ATOM   937   C  CG2   . THR   A 1  148  ? -25.253 55.301  73.175  1.00 30.29 ? 146  THR   A CG2   1 
ATOM   938   N  N     . TRP   A 1  149  ? -21.825 53.949  72.909  1.00 19.66 ? 147  TRP   A N     1 
ATOM   939   C  CA    . TRP   A 1  149  ? -21.346 52.865  72.065  1.00 19.71 ? 147  TRP   A CA    1 
ATOM   940   C  C     . TRP   A 1  149  ? -20.722 51.752  72.886  1.00 18.48 ? 147  TRP   A C     1 
ATOM   941   O  O     . TRP   A 1  149  ? -20.774 50.592  72.475  1.00 19.40 ? 147  TRP   A O     1 
ATOM   942   C  CB    . TRP   A 1  149  ? -20.350 53.382  71.029  1.00 19.90 ? 147  TRP   A CB    1 
ATOM   943   C  CG    . TRP   A 1  149  ? -20.988 54.281  70.037  1.00 19.32 ? 147  TRP   A CG    1 
ATOM   944   C  CD1   . TRP   A 1  149  ? -20.765 55.611  69.878  1.00 21.81 ? 147  TRP   A CD1   1 
ATOM   945   C  CD2   . TRP   A 1  149  ? -21.994 53.921  69.087  1.00 20.78 ? 147  TRP   A CD2   1 
ATOM   946   N  NE1   . TRP   A 1  149  ? -21.553 56.105  68.859  1.00 22.19 ? 147  TRP   A NE1   1 
ATOM   947   C  CE2   . TRP   A 1  149  ? -22.320 55.083  68.364  1.00 21.86 ? 147  TRP   A CE2   1 
ATOM   948   C  CE3   . TRP   A 1  149  ? -22.634 52.720  68.763  1.00 21.48 ? 147  TRP   A CE3   1 
ATOM   949   C  CZ2   . TRP   A 1  149  ? -23.270 55.085  67.339  1.00 23.81 ? 147  TRP   A CZ2   1 
ATOM   950   C  CZ3   . TRP   A 1  149  ? -23.579 52.720  67.743  1.00 25.29 ? 147  TRP   A CZ3   1 
ATOM   951   C  CH2   . TRP   A 1  149  ? -23.883 53.897  67.044  1.00 26.59 ? 147  TRP   A CH2   1 
ATOM   952   N  N     . GLY   A 1  150  ? -20.140 52.078  74.044  1.00 18.07 ? 148  GLY   A N     1 
ATOM   953   C  CA    . GLY   A 1  150  ? -19.648 51.028  74.917  1.00 20.38 ? 148  GLY   A CA    1 
ATOM   954   C  C     . GLY   A 1  150  ? -20.764 50.124  75.390  1.00 21.20 ? 148  GLY   A C     1 
ATOM   955   O  O     . GLY   A 1  150  ? -20.604 48.905  75.469  1.00 22.03 ? 148  GLY   A O     1 
ATOM   956   N  N     . LEU   A 1  151  ? -21.926 50.710  75.685  1.00 20.32 ? 149  LEU   A N     1 
ATOM   957   C  CA    . LEU   A 1  151  ? -23.069 49.891  76.056  1.00 23.59 ? 149  LEU   A CA    1 
ATOM   958   C  C     . LEU   A 1  151  ? -23.506 49.017  74.887  1.00 21.61 ? 149  LEU   A C     1 
ATOM   959   O  O     . LEU   A 1  151  ? -23.795 47.830  75.067  1.00 25.88 ? 149  LEU   A O     1 
ATOM   960   C  CB    . LEU   A 1  151  ? -24.197 50.796  76.549  1.00 26.73 ? 149  LEU   A CB    1 
ATOM   961   C  CG    . LEU   A 1  151  ? -25.315 50.206  77.398  1.00 30.74 ? 149  LEU   A CG    1 
ATOM   962   C  CD1   . LEU   A 1  151  ? -24.763 49.407  78.565  1.00 27.95 ? 149  LEU   A CD1   1 
ATOM   963   C  CD2   . LEU   A 1  151  ? -26.163 51.354  77.914  1.00 35.46 ? 149  LEU   A CD2   1 
ATOM   964   N  N     . VAL   A 1  152  ? -23.511 49.576  73.674  1.00 21.42 ? 150  VAL   A N     1 
ATOM   965   C  CA    . VAL   A 1  152  ? -23.876 48.807  72.484  1.00 22.99 ? 150  VAL   A CA    1 
ATOM   966   C  C     . VAL   A 1  152  ? -22.905 47.653  72.262  1.00 24.90 ? 150  VAL   A C     1 
ATOM   967   O  O     . VAL   A 1  152  ? -23.312 46.518  71.983  1.00 27.39 ? 150  VAL   A O     1 
ATOM   968   C  CB    . VAL   A 1  152  ? -23.940 49.737  71.258  1.00 24.19 ? 150  VAL   A CB    1 
ATOM   969   C  CG1   . VAL   A 1  152  ? -24.051 48.932  69.980  1.00 27.11 ? 150  VAL   A CG1   1 
ATOM   970   C  CG2   . VAL   A 1  152  ? -25.090 50.724  71.395  1.00 25.59 ? 150  VAL   A CG2   1 
ATOM   971   N  N     . VAL   A 1  153  ? -21.608 47.922  72.382  1.00 23.62 ? 151  VAL   A N     1 
ATOM   972   C  CA    . VAL   A 1  153  ? -20.605 46.929  72.022  1.00 25.45 ? 151  VAL   A CA    1 
ATOM   973   C  C     . VAL   A 1  153  ? -20.409 45.907  73.133  1.00 23.58 ? 151  VAL   A C     1 
ATOM   974   O  O     . VAL   A 1  153  ? -20.327 44.700  72.871  1.00 26.99 ? 151  VAL   A O     1 
ATOM   975   C  CB    . VAL   A 1  153  ? -19.291 47.634  71.650  1.00 22.90 ? 151  VAL   A CB    1 
ATOM   976   C  CG1   . VAL   A 1  153  ? -18.196 46.616  71.432  1.00 26.24 ? 151  VAL   A CG1   1 
ATOM   977   C  CG2   . VAL   A 1  153  ? -19.489 48.487  70.419  1.00 21.04 ? 151  VAL   A CG2   1 
ATOM   978   N  N     . THR   A 1  154  ? -20.321 46.367  74.382  1.00 24.16 ? 152  THR   A N     1 
ATOM   979   C  CA    . THR   A 1  154  ? -19.911 45.525  75.495  1.00 24.50 ? 152  THR   A CA    1 
ATOM   980   C  C     . THR   A 1  154  ? -21.049 45.178  76.440  1.00 27.64 ? 152  THR   A C     1 
ATOM   981   O  O     . THR   A 1  154  ? -20.878 44.295  77.285  1.00 30.50 ? 152  THR   A O     1 
ATOM   982   C  CB    . THR   A 1  154  ? -18.791 46.207  76.303  1.00 27.98 ? 152  THR   A CB    1 
ATOM   983   O  OG1   . THR   A 1  154  ? -19.341 47.254  77.117  1.00 28.34 ? 152  THR   A OG1   1 
ATOM   984   C  CG2   . THR   A 1  154  ? -17.750 46.805  75.372  1.00 27.33 ? 152  THR   A CG2   1 
ATOM   985   N  N     . GLY   A 1  155  ? -22.192 45.848  76.335  1.00 28.86 ? 153  GLY   A N     1 
ATOM   986   C  CA    . GLY   A 1  155  ? -23.249 45.653  77.306  1.00 26.29 ? 153  GLY   A CA    1 
ATOM   987   C  C     . GLY   A 1  155  ? -22.989 46.267  78.661  1.00 34.10 ? 153  GLY   A C     1 
ATOM   988   O  O     . GLY   A 1  155  ? -23.810 46.090  79.569  1.00 31.72 ? 153  GLY   A O     1 
ATOM   989   N  N     . LYS   A 1  156  ? -21.878 46.981  78.828  1.00 27.99 ? 154  LYS   A N     1 
ATOM   990   C  CA    . LYS   A 1  156  ? -21.502 47.596  80.092  1.00 30.27 ? 154  LYS   A CA    1 
ATOM   991   C  C     . LYS   A 1  156  ? -21.504 49.109  79.942  1.00 31.58 ? 154  LYS   A C     1 
ATOM   992   O  O     . LYS   A 1  156  ? -21.145 49.641  78.887  1.00 27.49 ? 154  LYS   A O     1 
ATOM   993   C  CB    . LYS   A 1  156  ? -20.108 47.133  80.536  1.00 35.46 ? 154  LYS   A CB    1 
ATOM   994   N  N     . LEU   A 1  157  ? -21.908 49.800  81.000  1.00 27.35 ? 155  LEU   A N     1 
ATOM   995   C  CA    . LEU   A 1  157  ? -21.925 51.253  81.022  1.00 29.48 ? 155  LEU   A CA    1 
ATOM   996   C  C     . LEU   A 1  157  ? -20.707 51.741  81.795  1.00 38.48 ? 155  LEU   A C     1 
ATOM   997   O  O     . LEU   A 1  157  ? -20.498 51.342  82.946  1.00 37.89 ? 155  LEU   A O     1 
ATOM   998   C  CB    . LEU   A 1  157  ? -23.204 51.764  81.679  1.00 29.29 ? 155  LEU   A CB    1 
ATOM   999   C  CG    . LEU   A 1  157  ? -23.292 53.284  81.785  1.00 37.89 ? 155  LEU   A CG    1 
ATOM   1000  C  CD1   . LEU   A 1  157  ? -23.301 53.925  80.402  1.00 35.43 ? 155  LEU   A CD1   1 
ATOM   1001  C  CD2   . LEU   A 1  157  ? -24.534 53.660  82.559  1.00 40.38 ? 155  LEU   A CD2   1 
ATOM   1002  N  N     . THR   A 1  158  ? -19.898 52.582  81.158  1.00 41.91 ? 156  THR   A N     1 
ATOM   1003  C  CA    . THR   A 1  158  ? -18.782 53.261  81.805  1.00 43.51 ? 156  THR   A CA    1 
ATOM   1004  C  C     . THR   A 1  158  ? -19.067 54.753  81.738  1.00 42.94 ? 156  THR   A C     1 
ATOM   1005  O  O     . THR   A 1  158  ? -19.204 55.308  80.643  1.00 50.80 ? 156  THR   A O     1 
ATOM   1006  C  CB    . THR   A 1  158  ? -17.460 52.925  81.108  1.00 43.14 ? 156  THR   A CB    1 
ATOM   1007  N  N     . SER   A 1  159  ? -19.154 55.395  82.906  1.00 38.41 ? 157  SER   A N     1 
ATOM   1008  C  CA    . SER   A 1  159  ? -19.704 56.748  82.993  1.00 25.04 ? 157  SER   A CA    1 
ATOM   1009  C  C     . SER   A 1  159  ? -18.872 57.769  82.217  1.00 31.69 ? 157  SER   A C     1 
ATOM   1010  O  O     . SER   A 1  159  ? -19.419 58.694  81.606  1.00 33.58 ? 157  SER   A O     1 
ATOM   1011  C  CB    . SER   A 1  159  ? -19.827 57.156  84.461  1.00 41.77 ? 157  SER   A CB    1 
ATOM   1012  O  OG    . SER   A 1  159  ? -18.693 56.730  85.200  1.00 42.54 ? 157  SER   A OG    1 
ATOM   1013  N  N     . THR   A 1  160  ? -17.557 57.646  82.258  1.00 30.85 ? 158  THR   A N     1 
ATOM   1014  C  CA    . THR   A 1  160  ? -16.682 58.503  81.479  1.00 26.98 ? 158  THR   A CA    1 
ATOM   1015  C  C     . THR   A 1  160  ? -15.942 57.647  80.465  1.00 23.49 ? 158  THR   A C     1 
ATOM   1016  O  O     . THR   A 1  160  ? -15.945 56.418  80.536  1.00 27.01 ? 158  THR   A O     1 
ATOM   1017  C  CB    . THR   A 1  160  ? -15.697 59.250  82.383  1.00 23.67 ? 158  THR   A CB    1 
ATOM   1018  O  OG1   . THR   A 1  160  ? -14.907 58.300  83.105  1.00 32.00 ? 158  THR   A OG1   1 
ATOM   1019  C  CG2   . THR   A 1  160  ? -16.439 60.155  83.352  1.00 35.01 ? 158  THR   A CG2   1 
ATOM   1020  N  N     . VAL   A 1  161  ? -15.300 58.330  79.521  1.00 18.24 ? 159  VAL   A N     1 
ATOM   1021  C  CA    . VAL   A 1  161  ? -14.736 57.730  78.319  1.00 19.31 ? 159  VAL   A CA    1 
ATOM   1022  C  C     . VAL   A 1  161  ? -13.222 57.774  78.436  1.00 18.12 ? 159  VAL   A C     1 
ATOM   1023  O  O     . VAL   A 1  161  ? -12.653 58.845  78.658  1.00 17.45 ? 159  VAL   A O     1 
ATOM   1024  C  CB    . VAL   A 1  161  ? -15.183 58.548  77.095  1.00 20.96 ? 159  VAL   A CB    1 
ATOM   1025  C  CG1   . VAL   A 1  161  ? -14.441 58.149  75.877  1.00 24.20 ? 159  VAL   A CG1   1 
ATOM   1026  C  CG2   . VAL   A 1  161  ? -16.708 58.452  76.908  1.00 25.91 ? 159  VAL   A CG2   1 
ATOM   1027  N  N     . ASN   A 1  162  ? -12.565 56.629  78.243  1.00 15.47 ? 160  ASN   A N     1 
ATOM   1028  C  CA    . ASN   A 1  162  ? -11.101 56.651  78.183  1.00 15.65 ? 160  ASN   A CA    1 
ATOM   1029  C  C     . ASN   A 1  162  ? -10.726 56.996  76.749  1.00 15.08 ? 160  ASN   A C     1 
ATOM   1030  O  O     . ASN   A 1  162  ? -10.504 56.124  75.902  1.00 16.80 ? 160  ASN   A O     1 
ATOM   1031  C  CB    . ASN   A 1  162  ? -10.499 55.334  78.647  1.00 16.70 ? 160  ASN   A CB    1 
ATOM   1032  C  CG    . ASN   A 1  162  ? -8.978  55.404  78.706  1.00 17.56 ? 160  ASN   A CG    1 
ATOM   1033  O  OD1   . ASN   A 1  162  ? -8.373  56.258  78.054  1.00 17.60 ? 160  ASN   A OD1   1 
ATOM   1034  N  ND2   . ASN   A 1  162  ? -8.363  54.513  79.475  1.00 21.83 ? 160  ASN   A ND2   1 
ATOM   1035  N  N     . ASP   A 1  163  ? -10.656 58.302  76.476  1.00 15.25 ? 161  ASP   A N     1 
ATOM   1036  C  CA    . ASP   A 1  163  ? -10.476 58.762  75.108  1.00 15.89 ? 161  ASP   A CA    1 
ATOM   1037  C  C     . ASP   A 1  163  ? -9.084  58.462  74.574  1.00 14.81 ? 161  ASP   A C     1 
ATOM   1038  O  O     . ASP   A 1  163  ? -8.903  58.340  73.366  1.00 16.38 ? 161  ASP   A O     1 
ATOM   1039  C  CB    . ASP   A 1  163  ? -10.834 60.244  74.955  1.00 18.28 ? 161  ASP   A CB    1 
ATOM   1040  C  CG    . ASP   A 1  163  ? -10.199 61.140  76.001  1.00 19.25 ? 161  ASP   A CG    1 
ATOM   1041  O  OD1   . ASP   A 1  163  ? -10.108 60.758  77.189  1.00 18.19 ? 161  ASP   A OD1   1 
ATOM   1042  O  OD2   . ASP   A 1  163  ? -9.848  62.276  75.615  1.00 21.60 ? 161  ASP   A OD2   1 
ATOM   1043  N  N     . ARG   A 1  164  ? -8.089  58.341  75.451  1.00 15.80 ? 162  ARG   A N     1 
ATOM   1044  C  CA    A ARG   A 1  164  ? -6.765  57.962  74.978  0.56 15.62 ? 162  ARG   A CA    1 
ATOM   1045  C  CA    B ARG   A 1  164  ? -6.761  57.959  74.989  0.44 15.65 ? 162  ARG   A CA    1 
ATOM   1046  C  C     . ARG   A 1  164  ? -6.725  56.493  74.578  1.00 14.92 ? 162  ARG   A C     1 
ATOM   1047  O  O     . ARG   A 1  164  ? -6.069  56.132  73.591  1.00 16.34 ? 162  ARG   A O     1 
ATOM   1048  C  CB    A ARG   A 1  164  ? -5.711  58.293  76.034  0.56 17.53 ? 162  ARG   A CB    1 
ATOM   1049  C  CB    B ARG   A 1  164  ? -5.731  58.264  76.077  0.44 17.50 ? 162  ARG   A CB    1 
ATOM   1050  C  CG    A ARG   A 1  164  ? -5.527  59.792  76.276  0.56 17.14 ? 162  ARG   A CG    1 
ATOM   1051  C  CG    B ARG   A 1  164  ? -5.652  59.743  76.442  0.44 17.21 ? 162  ARG   A CG    1 
ATOM   1052  C  CD    A ARG   A 1  164  ? -5.556  60.613  74.984  0.56 21.86 ? 162  ARG   A CD    1 
ATOM   1053  C  CD    B ARG   A 1  164  ? -4.699  60.534  75.540  0.44 19.29 ? 162  ARG   A CD    1 
ATOM   1054  N  NE    A ARG   A 1  164  ? -4.610  60.159  73.967  0.56 26.75 ? 162  ARG   A NE    1 
ATOM   1055  N  NE    B ARG   A 1  164  ? -5.077  60.512  74.132  0.44 25.77 ? 162  ARG   A NE    1 
ATOM   1056  C  CZ    A ARG   A 1  164  ? -4.697  60.468  72.678  0.56 24.70 ? 162  ARG   A CZ    1 
ATOM   1057  C  CZ    B ARG   A 1  164  ? -6.126  61.143  73.621  0.44 24.02 ? 162  ARG   A CZ    1 
ATOM   1058  N  NH1   A ARG   A 1  164  ? -5.661  61.246  72.218  0.56 25.21 ? 162  ARG   A NH1   1 
ATOM   1059  N  NH1   B ARG   A 1  164  ? -6.945  61.851  74.379  0.44 26.52 ? 162  ARG   A NH1   1 
ATOM   1060  N  NH2   A ARG   A 1  164  ? -3.800  59.977  71.829  0.56 22.94 ? 162  ARG   A NH2   1 
ATOM   1061  N  NH2   B ARG   A 1  164  ? -6.360  61.058  72.315  0.44 28.00 ? 162  ARG   A NH2   1 
ATOM   1062  N  N     . SER   A 1  165  ? -7.427  55.634  75.319  1.00 14.01 ? 163  SER   A N     1 
ATOM   1063  C  CA    . SER   A 1  165  ? -7.517  54.230  74.928  1.00 13.42 ? 163  SER   A CA    1 
ATOM   1064  C  C     . SER   A 1  165  ? -8.269  54.085  73.614  1.00 15.29 ? 163  SER   A C     1 
ATOM   1065  O  O     . SER   A 1  165  ? -7.874  53.308  72.739  1.00 14.60 ? 163  SER   A O     1 
ATOM   1066  C  CB    . SER   A 1  165  ? -8.216  53.435  76.035  1.00 16.55 ? 163  SER   A CB    1 
ATOM   1067  O  OG    . SER   A 1  165  ? -8.551  52.129  75.594  1.00 18.08 ? 163  SER   A OG    1 
ATOM   1068  N  N     . LEU   A 1  166  ? -9.360  54.840  73.458  1.00 15.08 ? 164  LEU   A N     1 
ATOM   1069  C  CA    . LEU   A 1  166  ? -10.122 54.783  72.220  1.00 15.49 ? 164  LEU   A CA    1 
ATOM   1070  C  C     . LEU   A 1  166  ? -9.325  55.331  71.046  1.00 14.49 ? 164  LEU   A C     1 
ATOM   1071  O  O     . LEU   A 1  166  ? -9.405  54.789  69.941  1.00 15.16 ? 164  LEU   A O     1 
ATOM   1072  C  CB    . LEU   A 1  166  ? -11.426 55.552  72.399  1.00 14.21 ? 164  LEU   A CB    1 
ATOM   1073  C  CG    . LEU   A 1  166  ? -12.367 54.856  73.366  1.00 15.17 ? 164  LEU   A CG    1 
ATOM   1074  C  CD1   . LEU   A 1  166  ? -13.529 55.757  73.636  1.00 16.77 ? 164  LEU   A CD1   1 
ATOM   1075  C  CD2   . LEU   A 1  166  ? -12.871 53.549  72.760  1.00 17.47 ? 164  LEU   A CD2   1 
ATOM   1076  N  N     . ALA   A 1  167  ? -8.577  56.421  71.250  1.00 14.49 ? 165  ALA   A N     1 
ATOM   1077  C  CA    . ALA   A 1  167  ? -7.771  56.946  70.150  1.00 15.57 ? 165  ALA   A CA    1 
ATOM   1078  C  C     . ALA   A 1  167  ? -6.728  55.930  69.722  1.00 14.90 ? 165  ALA   A C     1 
ATOM   1079  O  O     . ALA   A 1  167  ? -6.500  55.731  68.527  1.00 16.37 ? 165  ALA   A O     1 
ATOM   1080  C  CB    . ALA   A 1  167  ? -7.089  58.243  70.574  1.00 17.34 ? 165  ALA   A CB    1 
ATOM   1081  N  N     . ALA   A 1  168  ? -6.063  55.301  70.690  1.00 15.70 ? 166  ALA   A N     1 
ATOM   1082  C  CA    . ALA   A 1  168  ? -5.089  54.265  70.357  1.00 16.05 ? 166  ALA   A CA    1 
ATOM   1083  C  C     . ALA   A 1  168  ? -5.747  53.114  69.612  1.00 15.74 ? 166  ALA   A C     1 
ATOM   1084  O  O     . ALA   A 1  168  ? -5.215  52.620  68.610  1.00 16.05 ? 166  ALA   A O     1 
ATOM   1085  C  CB    . ALA   A 1  168  ? -4.433  53.771  71.647  1.00 16.33 ? 166  ALA   A CB    1 
ATOM   1086  N  N     . ALA   A 1  169  ? -6.924  52.693  70.068  1.00 14.95 ? 167  ALA   A N     1 
ATOM   1087  C  CA    . ALA   A 1  169  ? -7.621  51.580  69.438  1.00 14.69 ? 167  ALA   A CA    1 
ATOM   1088  C  C     . ALA   A 1  169  ? -8.048  51.921  68.021  1.00 16.00 ? 167  ALA   A C     1 
ATOM   1089  O  O     . ALA   A 1  169  ? -7.996  51.071  67.133  1.00 16.13 ? 167  ALA   A O     1 
ATOM   1090  C  CB    . ALA   A 1  169  ? -8.846  51.201  70.275  1.00 16.31 ? 167  ALA   A CB    1 
ATOM   1091  N  N     . LEU   A 1  170  ? -8.496  53.152  67.804  1.00 14.36 ? 168  LEU   A N     1 
ATOM   1092  C  CA    . LEU   A 1  170  ? -8.905  53.555  66.466  1.00 14.11 ? 168  LEU   A CA    1 
ATOM   1093  C  C     . LEU   A 1  170  ? -7.718  53.607  65.516  1.00 15.86 ? 168  LEU   A C     1 
ATOM   1094  O  O     . LEU   A 1  170  ? -7.804  53.121  64.383  1.00 17.18 ? 168  LEU   A O     1 
ATOM   1095  C  CB    . LEU   A 1  170  ? -9.593  54.911  66.549  1.00 16.06 ? 168  LEU   A CB    1 
ATOM   1096  C  CG    . LEU   A 1  170  ? -10.204 55.389  65.238  1.00 15.47 ? 168  LEU   A CG    1 
ATOM   1097  C  CD1   . LEU   A 1  170  ? -11.162 54.337  64.732  1.00 18.60 ? 168  LEU   A CD1   1 
ATOM   1098  C  CD2   . LEU   A 1  170  ? -10.926 56.684  65.479  1.00 18.60 ? 168  LEU   A CD2   1 
ATOM   1099  N  N     . THR   A 1  171  ? -6.600  54.187  65.958  1.00 16.36 ? 169  THR   A N     1 
ATOM   1100  C  CA    . THR   A 1  171  ? -5.402  54.161  65.133  1.00 17.46 ? 169  THR   A CA    1 
ATOM   1101  C  C     . THR   A 1  171  ? -5.010  52.726  64.815  1.00 16.65 ? 169  THR   A C     1 
ATOM   1102  O  O     . THR   A 1  171  ? -4.739  52.378  63.662  1.00 17.03 ? 169  THR   A O     1 
ATOM   1103  C  CB    . THR   A 1  171  ? -4.277  54.871  65.873  1.00 19.72 ? 169  THR   A CB    1 
ATOM   1104  O  OG1   . THR   A 1  171  ? -4.640  56.239  66.082  1.00 20.94 ? 169  THR   A OG1   1 
ATOM   1105  C  CG2   . THR   A 1  171  ? -2.961  54.791  65.108  1.00 21.20 ? 169  THR   A CG2   1 
ATOM   1106  N  N     . ARG   A 1  172  ? -5.045  51.864  65.823  1.00 16.85 ? 170  ARG   A N     1 
ATOM   1107  C  CA    . ARG   A 1  172  ? -4.641  50.479  65.631  1.00 16.53 ? 170  ARG   A CA    1 
ATOM   1108  C  C     . ARG   A 1  172  ? -5.543  49.774  64.630  1.00 16.26 ? 170  ARG   A C     1 
ATOM   1109  O  O     . ARG   A 1  172  ? -5.060  49.087  63.721  1.00 17.31 ? 170  ARG   A O     1 
ATOM   1110  C  CB    . ARG   A 1  172  ? -4.659  49.748  66.975  1.00 17.12 ? 170  ARG   A CB    1 
ATOM   1111  C  CG    . ARG   A 1  172  ? -3.973  48.382  66.901  1.00 16.41 ? 170  ARG   A CG    1 
ATOM   1112  C  CD    . ARG   A 1  172  ? -4.120  47.596  68.206  1.00 18.14 ? 170  ARG   A CD    1 
ATOM   1113  N  NE    . ARG   A 1  172  ? -3.859  48.413  69.383  1.00 16.57 ? 170  ARG   A NE    1 
ATOM   1114  C  CZ    . ARG   A 1  172  ? -4.794  48.879  70.203  1.00 16.55 ? 170  ARG   A CZ    1 
ATOM   1115  N  NH1   . ARG   A 1  172  ? -6.078  48.623  70.008  1.00 15.86 ? 170  ARG   A NH1   1 
ATOM   1116  N  NH2   . ARG   A 1  172  ? -4.433  49.637  71.228  1.00 16.31 ? 170  ARG   A NH2   1 
ATOM   1117  N  N     . LEU   A 1  173  ? -6.864  49.942  64.763  1.00 17.04 ? 171  LEU   A N     1 
ATOM   1118  C  CA    . LEU   A 1  173  ? -7.759  49.187  63.898  1.00 16.02 ? 171  LEU   A CA    1 
ATOM   1119  C  C     . LEU   A 1  173  ? -7.709  49.709  62.469  1.00 16.68 ? 171  LEU   A C     1 
ATOM   1120  O  O     . LEU   A 1  173  ? -7.794  48.928  61.516  1.00 19.00 ? 171  LEU   A O     1 
ATOM   1121  C  CB    . LEU   A 1  173  ? -9.185  49.183  64.457  1.00 18.94 ? 171  LEU   A CB    1 
ATOM   1122  C  CG    . LEU   A 1  173  ? -10.056 50.437  64.373  1.00 17.78 ? 171  LEU   A CG    1 
ATOM   1123  C  CD1   . LEU   A 1  173  ? -10.827 50.487  63.059  1.00 20.88 ? 171  LEU   A CD1   1 
ATOM   1124  C  CD2   . LEU   A 1  173  ? -11.042 50.455  65.528  1.00 18.20 ? 171  LEU   A CD2   1 
ATOM   1125  N  N     . ILE   A 1  174  ? -7.558  51.024  62.303  1.00 18.30 ? 172  ILE   A N     1 
ATOM   1126  C  CA    . ILE   A 1  174  ? -7.478  51.570  60.952  1.00 17.40 ? 172  ILE   A CA    1 
ATOM   1127  C  C     . ILE   A 1  174  ? -6.174  51.151  60.294  1.00 19.04 ? 172  ILE   A C     1 
ATOM   1128  O  O     . ILE   A 1  174  ? -6.147  50.768  59.117  1.00 19.99 ? 172  ILE   A O     1 
ATOM   1129  C  CB    . ILE   A 1  174  ? -7.627  53.100  60.978  1.00 18.39 ? 172  ILE   A CB    1 
ATOM   1130  C  CG1   . ILE   A 1  174  ? -9.049  53.492  61.348  1.00 20.46 ? 172  ILE   A CG1   1 
ATOM   1131  C  CG2   . ILE   A 1  174  ? -7.256  53.680  59.602  1.00 23.11 ? 172  ILE   A CG2   1 
ATOM   1132  C  CD1   . ILE   A 1  174  ? -9.210  54.967  61.596  1.00 22.14 ? 172  ILE   A CD1   1 
ATOM   1133  N  N     . SER   A 1  175  ? -5.076  51.198  61.042  1.00 18.57 ? 173  SER   A N     1 
ATOM   1134  C  CA    . SER   A 1  175  ? -3.810  50.797  60.449  1.00 18.13 ? 173  SER   A CA    1 
ATOM   1135  C  C     . SER   A 1  175  ? -3.761  49.311  60.163  1.00 20.58 ? 173  SER   A C     1 
ATOM   1136  O  O     . SER   A 1  175  ? -3.021  48.888  59.272  1.00 22.95 ? 173  SER   A O     1 
ATOM   1137  C  CB    . SER   A 1  175  ? -2.660  51.162  61.377  1.00 21.82 ? 173  SER   A CB    1 
ATOM   1138  O  OG    . SER   A 1  175  ? -2.537  52.562  61.477  1.00 24.33 ? 173  SER   A OG    1 
ATOM   1139  N  N     . ARG   A 1  176  ? -4.553  48.517  60.871  1.00 19.43 ? 174  ARG   A N     1 
ATOM   1140  C  CA    . ARG   A 1  176  ? -4.538  47.083  60.641  1.00 19.32 ? 174  ARG   A CA    1 
ATOM   1141  C  C     . ARG   A 1  176  ? -5.495  46.690  59.526  1.00 22.90 ? 174  ARG   A C     1 
ATOM   1142  O  O     . ARG   A 1  176  ? -5.150  45.860  58.681  1.00 25.45 ? 174  ARG   A O     1 
ATOM   1143  C  CB    . ARG   A 1  176  ? -4.921  46.366  61.944  1.00 22.94 ? 174  ARG   A CB    1 
ATOM   1144  C  CG    . ARG   A 1  176  ? -4.753  44.849  61.926  1.00 24.15 ? 174  ARG   A CG    1 
ATOM   1145  C  CD    . ARG   A 1  176  ? -5.031  44.268  63.318  1.00 23.14 ? 174  ARG   A CD    1 
ATOM   1146  N  NE    . ARG   A 1  176  ? -6.450  44.317  63.661  1.00 22.19 ? 174  ARG   A NE    1 
ATOM   1147  C  CZ    . ARG   A 1  176  ? -7.002  45.026  64.643  1.00 22.99 ? 174  ARG   A CZ    1 
ATOM   1148  N  NH1   . ARG   A 1  176  ? -6.278  45.764  65.481  1.00 20.27 ? 174  ARG   A NH1   1 
ATOM   1149  N  NH2   . ARG   A 1  176  ? -8.324  44.996  64.790  1.00 24.01 ? 174  ARG   A NH2   1 
ATOM   1150  N  N     . CYS   A 1  177  ? -6.686  47.294  59.488  1.00 21.43 ? 175  CYS   A N     1 
ATOM   1151  C  CA    . CYS   A 1  177  ? -7.753  46.819  58.628  1.00 22.79 ? 175  CYS   A CA    1 
ATOM   1152  C  C     . CYS   A 1  177  ? -8.200  47.803  57.559  1.00 25.11 ? 175  CYS   A C     1 
ATOM   1153  O  O     . CYS   A 1  177  ? -8.899  47.388  56.633  1.00 27.92 ? 175  CYS   A O     1 
ATOM   1154  C  CB    . CYS   A 1  177  ? -8.983  46.432  59.460  1.00 24.85 ? 175  CYS   A CB    1 
ATOM   1155  S  SG    . CYS   A 1  177  ? -8.620  45.241  60.774  1.00 27.43 ? 175  CYS   A SG    1 
ATOM   1156  N  N     . GLY   A 1  178  ? -7.867  49.080  57.683  1.00 24.16 ? 176  GLY   A N     1 
ATOM   1157  C  CA    . GLY   A 1  178  ? -8.052  49.999  56.578  1.00 23.90 ? 176  GLY   A CA    1 
ATOM   1158  C  C     . GLY   A 1  178  ? -9.497  50.353  56.258  1.00 21.26 ? 176  GLY   A C     1 
ATOM   1159  O  O     . GLY   A 1  178  ? -10.415 50.241  57.073  1.00 23.55 ? 176  GLY   A O     1 
ATOM   1160  N  N     . GLU   A 1  179  ? -9.676  50.799  55.020  1.00 23.43 ? 177  GLU   A N     1 
ATOM   1161  C  CA    . GLU   A 1  179  ? -10.993 51.239  54.572  1.00 23.77 ? 177  GLU   A CA    1 
ATOM   1162  C  C     . GLU   A 1  179  ? -12.096 50.208  54.776  1.00 21.60 ? 177  GLU   A C     1 
ATOM   1163  O  O     . GLU   A 1  179  ? -13.205 50.611  55.167  1.00 23.21 ? 177  GLU   A O     1 
ATOM   1164  C  CB    . GLU   A 1  179  ? -10.917 51.716  53.112  1.00 24.01 ? 177  GLU   A CB    1 
ATOM   1165  C  CG    . GLU   A 1  179  ? -12.187 52.405  52.625  1.00 31.84 ? 177  GLU   A CG    1 
ATOM   1166  C  CD    . GLU   A 1  179  ? -13.172 51.461  51.947  1.00 46.17 ? 177  GLU   A CD    1 
ATOM   1167  O  OE1   . GLU   A 1  179  ? -12.786 50.321  51.603  1.00 43.21 ? 177  GLU   A OE1   1 
ATOM   1168  O  OE2   . GLU   A 1  179  ? -14.341 51.868  51.750  1.00 46.28 ? 177  GLU   A OE2   1 
ATOM   1169  N  N     . PRO   A 1  180  ? -11.894 48.908  54.534  1.00 21.87 ? 178  PRO   A N     1 
ATOM   1170  C  CA    . PRO   A 1  180  ? -13.020 47.974  54.688  1.00 23.40 ? 178  PRO   A CA    1 
ATOM   1171  C  C     . PRO   A 1  180  ? -13.666 47.989  56.061  1.00 23.49 ? 178  PRO   A C     1 
ATOM   1172  O  O     . PRO   A 1  180  ? -14.898 47.924  56.154  1.00 23.66 ? 178  PRO   A O     1 
ATOM   1173  C  CB    . PRO   A 1  180  ? -12.401 46.618  54.338  1.00 25.38 ? 178  PRO   A CB    1 
ATOM   1174  C  CG    . PRO   A 1  180  ? -11.328 46.959  53.374  1.00 25.87 ? 178  PRO   A CG    1 
ATOM   1175  C  CD    . PRO   A 1  180  ? -10.750 48.254  53.877  1.00 24.47 ? 178  PRO   A CD    1 
ATOM   1176  N  N     . VAL   A 1  181  ? -12.881 48.091  57.135  1.00 22.03 ? 179  VAL   A N     1 
ATOM   1177  C  CA    . VAL   A 1  181  ? -13.496 48.121  58.455  1.00 21.29 ? 179  VAL   A CA    1 
ATOM   1178  C  C     . VAL   A 1  181  ? -14.233 49.434  58.684  1.00 20.81 ? 179  VAL   A C     1 
ATOM   1179  O  O     . VAL   A 1  181  ? -15.275 49.456  59.343  1.00 20.17 ? 179  VAL   A O     1 
ATOM   1180  C  CB    . VAL   A 1  181  ? -12.478 47.791  59.567  1.00 21.54 ? 179  VAL   A CB    1 
ATOM   1181  C  CG1   . VAL   A 1  181  ? -11.478 48.928  59.762  1.00 19.85 ? 179  VAL   A CG1   1 
ATOM   1182  C  CG2   . VAL   A 1  181  ? -13.211 47.471  60.857  1.00 23.97 ? 179  VAL   A CG2   1 
ATOM   1183  N  N     . ILE   A 1  182  ? -13.716 50.544  58.151  1.00 20.21 ? 180  ILE   A N     1 
ATOM   1184  C  CA    . ILE   A 1  182  ? -14.392 51.826  58.297  1.00 20.76 ? 180  ILE   A CA    1 
ATOM   1185  C  C     . ILE   A 1  182  ? -15.719 51.795  57.567  1.00 23.45 ? 180  ILE   A C     1 
ATOM   1186  O  O     . ILE   A 1  182  ? -16.747 52.231  58.094  1.00 22.01 ? 180  ILE   A O     1 
ATOM   1187  C  CB    . ILE   A 1  182  ? -13.507 52.970  57.776  1.00 20.39 ? 180  ILE   A CB    1 
ATOM   1188  C  CG1   . ILE   A 1  182  ? -12.181 53.011  58.528  1.00 21.63 ? 180  ILE   A CG1   1 
ATOM   1189  C  CG2   . ILE   A 1  182  ? -14.261 54.297  57.857  1.00 21.22 ? 180  ILE   A CG2   1 
ATOM   1190  C  CD1   . ILE   A 1  182  ? -11.148 53.934  57.893  1.00 26.02 ? 180  ILE   A CD1   1 
ATOM   1191  N  N     . ARG   A 1  183  ? -15.700 51.294  56.331  1.00 22.09 ? 181  ARG   A N     1 
ATOM   1192  C  CA    A ARG   A 1  183  ? -16.928 51.174  55.553  0.41 25.63 ? 181  ARG   A CA    1 
ATOM   1193  C  CA    B ARG   A 1  183  ? -16.920 51.155  55.541  0.59 25.63 ? 181  ARG   A CA    1 
ATOM   1194  C  C     . ARG   A 1  183  ? -17.970 50.353  56.300  1.00 25.59 ? 181  ARG   A C     1 
ATOM   1195  O  O     . ARG   A 1  183  ? -19.145 50.739  56.373  1.00 24.89 ? 181  ARG   A O     1 
ATOM   1196  C  CB    A ARG   A 1  183  ? -16.616 50.553  54.191  0.41 25.35 ? 181  ARG   A CB    1 
ATOM   1197  C  CB    B ARG   A 1  183  ? -16.562 50.458  54.226  0.59 25.27 ? 181  ARG   A CB    1 
ATOM   1198  C  CG    A ARG   A 1  183  ? -17.842 50.223  53.349  0.41 30.28 ? 181  ARG   A CG    1 
ATOM   1199  C  CG    B ARG   A 1  183  ? -17.708 50.222  53.254  0.59 30.37 ? 181  ARG   A CG    1 
ATOM   1200  C  CD    A ARG   A 1  183  ? -18.752 51.433  53.205  0.41 30.88 ? 181  ARG   A CD    1 
ATOM   1201  C  CD    B ARG   A 1  183  ? -18.119 51.515  52.579  0.59 32.39 ? 181  ARG   A CD    1 
ATOM   1202  N  NE    A ARG   A 1  183  ? -18.022 52.612  52.755  0.41 30.02 ? 181  ARG   A NE    1 
ATOM   1203  N  NE    B ARG   A 1  183  ? -19.210 52.168  53.292  0.59 29.77 ? 181  ARG   A NE    1 
ATOM   1204  C  CZ    A ARG   A 1  183  ? -18.494 53.849  52.816  0.41 32.27 ? 181  ARG   A CZ    1 
ATOM   1205  C  CZ    B ARG   A 1  183  ? -19.434 53.474  53.283  0.59 33.74 ? 181  ARG   A CZ    1 
ATOM   1206  N  NH1   A ARG   A 1  183  ? -19.686 54.109  53.330  0.41 33.92 ? 181  ARG   A NH1   1 
ATOM   1207  N  NH1   B ARG   A 1  183  ? -18.632 54.308  52.642  0.59 33.56 ? 181  ARG   A NH1   1 
ATOM   1208  N  NH2   A ARG   A 1  183  ? -17.751 54.850  52.353  0.41 34.55 ? 181  ARG   A NH2   1 
ATOM   1209  N  NH2   B ARG   A 1  183  ? -20.483 53.956  53.941  0.59 31.32 ? 181  ARG   A NH2   1 
ATOM   1210  N  N     . ARG   A 1  184  ? -17.555 49.226  56.875  1.00 23.48 ? 182  ARG   A N     1 
ATOM   1211  C  CA    . ARG   A 1  184  ? -18.497 48.380  57.594  1.00 24.11 ? 182  ARG   A CA    1 
ATOM   1212  C  C     . ARG   A 1  184  ? -19.007 49.070  58.846  1.00 23.22 ? 182  ARG   A C     1 
ATOM   1213  O  O     . ARG   A 1  184  ? -20.187 48.945  59.194  1.00 22.63 ? 182  ARG   A O     1 
ATOM   1214  C  CB    . ARG   A 1  184  ? -17.830 47.052  57.931  1.00 26.00 ? 182  ARG   A CB    1 
ATOM   1215  C  CG    . ARG   A 1  184  ? -17.712 46.126  56.736  1.00 31.37 ? 182  ARG   A CG    1 
ATOM   1216  C  CD    . ARG   A 1  184  ? -18.916 45.192  56.651  1.00 33.04 ? 182  ARG   A CD    1 
ATOM   1217  N  NE    . ARG   A 1  184  ? -18.771 44.049  57.545  1.00 33.54 ? 182  ARG   A NE    1 
ATOM   1218  C  CZ    . ARG   A 1  184  ? -19.576 43.776  58.562  1.00 32.36 ? 182  ARG   A CZ    1 
ATOM   1219  N  NH1   . ARG   A 1  184  ? -20.629 44.530  58.835  1.00 33.91 ? 182  ARG   A NH1   1 
ATOM   1220  N  NH2   . ARG   A 1  184  ? -19.327 42.708  59.316  1.00 28.15 ? 182  ARG   A NH2   1 
ATOM   1221  N  N     . GLY   A 1  185  ? -18.136 49.795  59.545  1.00 21.18 ? 183  GLY   A N     1 
ATOM   1222  C  CA    . GLY   A 1  185  ? -18.584 50.536  60.708  1.00 19.95 ? 183  GLY   A CA    1 
ATOM   1223  C  C     . GLY   A 1  185  ? -19.589 51.614  60.347  1.00 22.66 ? 183  GLY   A C     1 
ATOM   1224  O  O     . GLY   A 1  185  ? -20.612 51.772  61.011  1.00 20.44 ? 183  GLY   A O     1 
ATOM   1225  N  N     . VAL   A 1  186  ? -19.311 52.366  59.280  1.00 21.51 ? 184  VAL   A N     1 
ATOM   1226  C  CA    . VAL   A 1  186  ? -20.226 53.423  58.855  1.00 23.72 ? 184  VAL   A CA    1 
ATOM   1227  C  C     . VAL   A 1  186  ? -21.580 52.840  58.496  1.00 23.71 ? 184  VAL   A C     1 
ATOM   1228  O  O     . VAL   A 1  186  ? -22.629 53.372  58.884  1.00 21.39 ? 184  VAL   A O     1 
ATOM   1229  C  CB    . VAL   A 1  186  ? -19.616 54.197  57.675  1.00 22.44 ? 184  VAL   A CB    1 
ATOM   1230  C  CG1   . VAL   A 1  186  ? -20.688 55.073  56.998  1.00 23.91 ? 184  VAL   A CG1   1 
ATOM   1231  C  CG2   . VAL   A 1  186  ? -18.468 55.036  58.162  1.00 22.38 ? 184  VAL   A CG2   1 
ATOM   1232  N  N     . ASP   A 1  187  ? -21.580 51.732  57.768  1.00 21.40 ? 185  ASP   A N     1 
ATOM   1233  C  CA    . ASP   A 1  187  ? -22.848 51.149  57.344  1.00 25.21 ? 185  ASP   A CA    1 
ATOM   1234  C  C     . ASP   A 1  187  ? -23.617 50.602  58.537  1.00 29.08 ? 185  ASP   A C     1 
ATOM   1235  O  O     . ASP   A 1  187  ? -24.848 50.708  58.591  1.00 27.67 ? 185  ASP   A O     1 
ATOM   1236  C  CB    . ASP   A 1  187  ? -22.602 50.067  56.297  1.00 26.08 ? 185  ASP   A CB    1 
ATOM   1237  C  CG    . ASP   A 1  187  ? -22.103 50.637  54.970  1.00 30.25 ? 185  ASP   A CG    1 
ATOM   1238  O  OD1   . ASP   A 1  187  ? -22.228 51.862  54.756  1.00 33.61 ? 185  ASP   A OD1   1 
ATOM   1239  O  OD2   . ASP   A 1  187  ? -21.597 49.858  54.139  1.00 33.21 ? 185  ASP   A OD2   1 
ATOM   1240  N  N     . MET   A 1  188  ? -22.904 50.029  59.507  1.00 26.31 ? 186  MET   A N     1 
ATOM   1241  C  CA    . MET   A 1  188  ? -23.541 49.532  60.723  1.00 24.89 ? 186  MET   A CA    1 
ATOM   1242  C  C     . MET   A 1  188  ? -24.141 50.667  61.537  1.00 25.81 ? 186  MET   A C     1 
ATOM   1243  O  O     . MET   A 1  188  ? -25.296 50.587  61.978  1.00 24.71 ? 186  MET   A O     1 
ATOM   1244  C  CB    . MET   A 1  188  ? -22.510 48.776  61.561  1.00 27.11 ? 186  MET   A CB    1 
ATOM   1245  C  CG    . MET   A 1  188  ? -23.075 48.140  62.812  1.00 34.52 ? 186  MET   A CG    1 
ATOM   1246  S  SD    . MET   A 1  188  ? -24.260 46.859  62.374  1.00 42.35 ? 186  MET   A SD    1 
ATOM   1247  C  CE    . MET   A 1  188  ? -23.233 45.831  61.315  1.00 34.22 ? 186  MET   A CE    1 
ATOM   1248  N  N     . ALA   A 1  189  ? -23.359 51.720  61.784  1.00 22.61 ? 187  ALA   A N     1 
ATOM   1249  C  CA    . ALA   A 1  189  ? -23.868 52.854  62.543  1.00 22.31 ? 187  ALA   A CA    1 
ATOM   1250  C  C     . ALA   A 1  189  ? -25.045 53.499  61.831  1.00 24.52 ? 187  ALA   A C     1 
ATOM   1251  O  O     . ALA   A 1  189  ? -26.017 53.905  62.474  1.00 23.38 ? 187  ALA   A O     1 
ATOM   1252  C  CB    . ALA   A 1  189  ? -22.764 53.883  62.773  1.00 23.01 ? 187  ALA   A CB    1 
ATOM   1253  N  N     . MET   A 1  190  ? -24.977 53.598  60.504  1.00 22.84 ? 188  MET   A N     1 
ATOM   1254  C  CA    . MET   A 1  190  ? -26.070 54.206  59.747  1.00 23.29 ? 188  MET   A CA    1 
ATOM   1255  C  C     . MET   A 1  190  ? -27.364 53.428  59.938  1.00 24.42 ? 188  MET   A C     1 
ATOM   1256  O  O     . MET   A 1  190  ? -28.430 54.012  60.178  1.00 25.55 ? 188  MET   A O     1 
ATOM   1257  C  CB    . MET   A 1  190  ? -25.695 54.251  58.266  1.00 24.48 ? 188  MET   A CB    1 
ATOM   1258  C  CG    . MET   A 1  190  ? -26.644 55.077  57.422  1.00 32.32 ? 188  MET   A CG    1 
ATOM   1259  S  SD    . MET   A 1  190  ? -26.255 54.947  55.668  1.00 39.44 ? 188  MET   A SD    1 
ATOM   1260  C  CE    . MET   A 1  190  ? -24.485 55.214  55.686  1.00 33.14 ? 188  MET   A CE    1 
ATOM   1261  N  N     . ARG   A 1  191  ? -27.285 52.103  59.834  1.00 21.51 ? 189  ARG   A N     1 
ATOM   1262  C  CA    . ARG   A 1  191  ? -28.457 51.266  60.042  1.00 25.34 ? 189  ARG   A CA    1 
ATOM   1263  C  C     . ARG   A 1  191  ? -28.952 51.352  61.478  1.00 25.31 ? 189  ARG   A C     1 
ATOM   1264  O  O     . ARG   A 1  191  ? -30.162 51.439  61.721  1.00 25.03 ? 189  ARG   A O     1 
ATOM   1265  C  CB    . ARG   A 1  191  ? -28.122 49.820  59.687  1.00 26.66 ? 189  ARG   A CB    1 
ATOM   1266  C  CG    . ARG   A 1  191  ? -29.311 48.881  59.733  1.00 36.39 ? 189  ARG   A CG    1 
ATOM   1267  C  CD    . ARG   A 1  191  ? -28.938 47.477  59.284  1.00 45.62 ? 189  ARG   A CD    1 
ATOM   1268  N  NE    . ARG   A 1  191  ? -27.947 46.866  60.161  1.00 53.95 ? 189  ARG   A NE    1 
ATOM   1269  C  CZ    . ARG   A 1  191  ? -28.220 46.349  61.352  1.00 62.68 ? 189  ARG   A CZ    1 
ATOM   1270  N  NH1   . ARG   A 1  191  ? -29.445 46.376  61.853  1.00 70.57 ? 189  ARG   A NH1   1 
ATOM   1271  N  NH2   . ARG   A 1  191  ? -27.239 45.795  62.060  1.00 59.82 ? 189  ARG   A NH2   1 
ATOM   1272  N  N     . MET   A 1  192  ? -28.040 51.317  62.451  1.00 22.94 ? 190  MET   A N     1 
ATOM   1273  C  CA    . MET   A 1  192  ? -28.480 51.323  63.842  1.00 23.92 ? 190  MET   A CA    1 
ATOM   1274  C  C     . MET   A 1  192  ? -29.125 52.648  64.202  1.00 25.21 ? 190  MET   A C     1 
ATOM   1275  O  O     . MET   A 1  192  ? -30.198 52.685  64.814  1.00 24.51 ? 190  MET   A O     1 
ATOM   1276  C  CB    . MET   A 1  192  ? -27.301 51.040  64.771  1.00 25.82 ? 190  MET   A CB    1 
ATOM   1277  C  CG    . MET   A 1  192  ? -26.784 49.631  64.642  1.00 25.34 ? 190  MET   A CG    1 
ATOM   1278  S  SD    . MET   A 1  192  ? -25.414 49.353  65.766  1.00 34.42 ? 190  MET   A SD    1 
ATOM   1279  C  CE    . MET   A 1  192  ? -26.301 49.168  67.297  1.00 31.59 ? 190  MET   A CE    1 
ATOM   1280  N  N     . MET   A 1  193  ? -28.492 53.751  63.822  1.00 23.16 ? 191  MET   A N     1 
ATOM   1281  C  CA    A MET   A 1  193  ? -28.996 55.067  64.186  0.55 24.73 ? 191  MET   A CA    1 
ATOM   1282  C  CA    B MET   A 1  193  ? -29.014 55.054  64.200  0.45 24.74 ? 191  MET   A CA    1 
ATOM   1283  C  C     . MET   A 1  193  ? -30.186 55.497  63.340  1.00 26.00 ? 191  MET   A C     1 
ATOM   1284  O  O     . MET   A 1  193  ? -30.952 56.363  63.771  1.00 28.05 ? 191  MET   A O     1 
ATOM   1285  C  CB    A MET   A 1  193  ? -27.878 56.104  64.077  0.55 23.39 ? 191  MET   A CB    1 
ATOM   1286  C  CB    B MET   A 1  193  ? -27.902 56.099  64.190  0.45 23.46 ? 191  MET   A CB    1 
ATOM   1287  C  CG    A MET   A 1  193  ? -26.625 55.730  64.854  0.55 24.28 ? 191  MET   A CG    1 
ATOM   1288  C  CG    B MET   A 1  193  ? -26.911 55.899  65.317  0.45 24.57 ? 191  MET   A CG    1 
ATOM   1289  S  SD    A MET   A 1  193  ? -25.329 56.973  64.711  0.55 27.20 ? 191  MET   A SD    1 
ATOM   1290  S  SD    B MET   A 1  193  ? -25.900 57.354  65.602  0.45 28.10 ? 191  MET   A SD    1 
ATOM   1291  C  CE    A MET   A 1  193  ? -25.874 58.142  65.954  0.55 31.13 ? 191  MET   A CE    1 
ATOM   1292  C  CE    B MET   A 1  193  ? -25.029 57.454  64.035  0.45 29.81 ? 191  MET   A CE    1 
ATOM   1293  N  N     . GLY   A 1  194  ? -30.359 54.916  62.161  1.00 25.17 ? 192  GLY   A N     1 
ATOM   1294  C  CA    . GLY   A 1  194  ? -31.444 55.321  61.290  1.00 29.22 ? 192  GLY   A CA    1 
ATOM   1295  C  C     . GLY   A 1  194  ? -32.633 54.383  61.266  1.00 28.57 ? 192  GLY   A C     1 
ATOM   1296  O  O     . GLY   A 1  194  ? -33.736 54.798  60.884  1.00 28.65 ? 192  GLY   A O     1 
ATOM   1297  N  N     . GLU   A 1  195  ? -32.434 53.121  61.667  1.00 25.19 ? 193  GLU   A N     1 
ATOM   1298  C  CA    . GLU   A 1  195  ? -33.476 52.105  61.555  1.00 24.73 ? 193  GLU   A CA    1 
ATOM   1299  C  C     . GLU   A 1  195  ? -33.723 51.284  62.809  1.00 22.90 ? 193  GLU   A C     1 
ATOM   1300  O  O     . GLU   A 1  195  ? -34.790 50.663  62.897  1.00 23.22 ? 193  GLU   A O     1 
ATOM   1301  C  CB    . GLU   A 1  195  ? -33.168 51.126  60.417  1.00 28.67 ? 193  GLU   A CB    1 
ATOM   1302  C  CG    . GLU   A 1  195  ? -32.767 51.760  59.113  1.00 36.36 ? 193  GLU   A CG    1 
ATOM   1303  C  CD    . GLU   A 1  195  ? -32.198 50.733  58.160  1.00 46.37 ? 193  GLU   A CD    1 
ATOM   1304  O  OE1   . GLU   A 1  195  ? -32.530 49.539  58.323  1.00 47.40 ? 193  GLU   A OE1   1 
ATOM   1305  O  OE2   . GLU   A 1  195  ? -31.409 51.111  57.269  1.00 55.78 ? 193  GLU   A OE2   1 
ATOM   1306  N  N     . GLN   A 1  196  ? -32.786 51.225  63.759  1.00 25.92 ? 194  GLN   A N     1 
ATOM   1307  C  CA    . GLN   A 1  196  ? -32.945 50.395  64.952  1.00 24.50 ? 194  GLN   A CA    1 
ATOM   1308  C  C     . GLN   A 1  196  ? -33.254 51.205  66.205  1.00 25.92 ? 194  GLN   A C     1 
ATOM   1309  O  O     . GLN   A 1  196  ? -34.244 50.937  66.894  1.00 29.41 ? 194  GLN   A O     1 
ATOM   1310  C  CB    . GLN   A 1  196  ? -31.695 49.529  65.177  1.00 25.93 ? 194  GLN   A CB    1 
ATOM   1311  N  N     . PHE   A 1  197  ? -32.425 52.196  66.523  1.00 22.47 ? 195  PHE   A N     1 
ATOM   1312  C  CA    . PHE   A 1  197  ? -32.694 53.039  67.676  1.00 24.33 ? 195  PHE   A CA    1 
ATOM   1313  C  C     . PHE   A 1  197  ? -33.855 53.975  67.419  1.00 25.12 ? 195  PHE   A C     1 
ATOM   1314  O  O     . PHE   A 1  197  ? -34.455 54.475  68.376  1.00 27.83 ? 195  PHE   A O     1 
ATOM   1315  C  CB    . PHE   A 1  197  ? -31.465 53.868  68.016  1.00 27.08 ? 195  PHE   A CB    1 
ATOM   1316  C  CG    . PHE   A 1  197  ? -30.272 53.046  68.384  1.00 31.10 ? 195  PHE   A CG    1 
ATOM   1317  C  CD1   . PHE   A 1  197  ? -30.419 51.901  69.147  1.00 31.60 ? 195  PHE   A CD1   1 
ATOM   1318  C  CD2   . PHE   A 1  197  ? -29.006 53.420  67.976  1.00 29.08 ? 195  PHE   A CD2   1 
ATOM   1319  C  CE1   . PHE   A 1  197  ? -29.322 51.140  69.498  1.00 37.42 ? 195  PHE   A CE1   1 
ATOM   1320  C  CE2   . PHE   A 1  197  ? -27.901 52.656  68.324  1.00 30.79 ? 195  PHE   A CE2   1 
ATOM   1321  C  CZ    . PHE   A 1  197  ? -28.071 51.518  69.086  1.00 27.91 ? 195  PHE   A CZ    1 
ATOM   1322  N  N     . VAL   A 1  198  ? -34.151 54.259  66.159  1.00 21.25 ? 196  VAL   A N     1 
ATOM   1323  C  CA    . VAL   A 1  198  ? -35.340 55.021  65.804  1.00 21.27 ? 196  VAL   A CA    1 
ATOM   1324  C  C     . VAL   A 1  198  ? -36.053 54.281  64.691  1.00 20.87 ? 196  VAL   A C     1 
ATOM   1325  O  O     . VAL   A 1  198  ? -35.445 53.525  63.929  1.00 25.43 ? 196  VAL   A O     1 
ATOM   1326  C  CB    . VAL   A 1  198  ? -35.044 56.480  65.380  1.00 20.51 ? 196  VAL   A CB    1 
ATOM   1327  C  CG1   . VAL   A 1  198  ? -34.391 57.249  66.521  1.00 23.92 ? 196  VAL   A CG1   1 
ATOM   1328  C  CG2   . VAL   A 1  198  ? -34.181 56.510  64.124  1.00 23.83 ? 196  VAL   A CG2   1 
ATOM   1329  N  N     . THR   A 1  199  ? -37.365 54.480  64.616  1.00 20.18 ? 197  THR   A N     1 
ATOM   1330  C  CA    . THR   A 1  199  ? -38.099 53.956  63.477  1.00 21.10 ? 197  THR   A CA    1 
ATOM   1331  C  C     . THR   A 1  199  ? -37.787 54.766  62.231  1.00 24.90 ? 197  THR   A C     1 
ATOM   1332  O  O     . THR   A 1  199  ? -37.721 54.213  61.133  1.00 27.43 ? 197  THR   A O     1 
ATOM   1333  C  CB    . THR   A 1  199  ? -39.594 53.949  63.794  1.00 22.56 ? 197  THR   A CB    1 
ATOM   1334  O  OG1   . THR   A 1  199  ? -39.804 53.217  65.010  1.00 24.39 ? 197  THR   A OG1   1 
ATOM   1335  C  CG2   . THR   A 1  199  ? -40.378 53.285  62.681  1.00 26.95 ? 197  THR   A CG2   1 
ATOM   1336  N  N     . GLY   A 1  200  ? -37.550 56.061  62.394  1.00 21.63 ? 198  GLY   A N     1 
ATOM   1337  C  CA    . GLY   A 1  200  ? -37.137 56.915  61.296  1.00 22.56 ? 198  GLY   A CA    1 
ATOM   1338  C  C     . GLY   A 1  200  ? -36.598 58.209  61.852  1.00 20.58 ? 198  GLY   A C     1 
ATOM   1339  O  O     . GLY   A 1  200  ? -36.794 58.544  63.022  1.00 20.01 ? 198  GLY   A O     1 
ATOM   1340  N  N     . GLU   A 1  201  ? -35.893 58.938  60.988  1.00 21.68 ? 199  GLU   A N     1 
ATOM   1341  C  CA    . GLU   A 1  201  ? -35.327 60.215  61.401  1.00 21.57 ? 199  GLU   A CA    1 
ATOM   1342  C  C     . GLU   A 1  201  ? -36.398 61.289  61.513  1.00 23.05 ? 199  GLU   A C     1 
ATOM   1343  O  O     . GLU   A 1  201  ? -36.270 62.211  62.325  1.00 24.61 ? 199  GLU   A O     1 
ATOM   1344  C  CB    . GLU   A 1  201  ? -34.267 60.648  60.391  1.00 24.99 ? 199  GLU   A CB    1 
ATOM   1345  C  CG    . GLU   A 1  201  ? -33.598 61.970  60.689  1.00 34.88 ? 199  GLU   A CG    1 
ATOM   1346  C  CD    . GLU   A 1  201  ? -32.549 62.319  59.649  1.00 46.47 ? 199  GLU   A CD    1 
ATOM   1347  O  OE1   . GLU   A 1  201  ? -32.423 61.563  58.661  1.00 49.83 ? 199  GLU   A OE1   1 
ATOM   1348  O  OE2   . GLU   A 1  201  ? -31.850 63.341  59.820  1.00 54.52 ? 199  GLU   A OE2   1 
ATOM   1349  N  N     . THR   A 1  202  ? -37.455 61.182  60.712  1.00 20.87 ? 200  THR   A N     1 
ATOM   1350  C  CA    . THR   A 1  202  ? -38.558 62.123  60.726  1.00 20.11 ? 200  THR   A CA    1 
ATOM   1351  C  C     . THR   A 1  202  ? -39.853 61.336  60.808  1.00 18.74 ? 200  THR   A C     1 
ATOM   1352  O  O     . THR   A 1  202  ? -39.899 60.140  60.509  1.00 19.92 ? 200  THR   A O     1 
ATOM   1353  C  CB    . THR   A 1  202  ? -38.622 62.908  59.426  1.00 22.57 ? 200  THR   A CB    1 
ATOM   1354  O  OG1   . THR   A 1  202  ? -38.853 61.984  58.360  1.00 24.44 ? 200  THR   A OG1   1 
ATOM   1355  C  CG2   . THR   A 1  202  ? -37.307 63.657  59.173  1.00 25.16 ? 200  THR   A CG2   1 
ATOM   1356  N  N     . ILE   A 1  203  ? -40.920 62.030  61.195  1.00 19.28 ? 201  ILE   A N     1 
ATOM   1357  C  CA    . ILE   A 1  203  ? -42.196 61.336  61.339  1.00 20.32 ? 201  ILE   A CA    1 
ATOM   1358  C  C     . ILE   A 1  203  ? -42.644 60.742  60.010  1.00 20.42 ? 201  ILE   A C     1 
ATOM   1359  O  O     . ILE   A 1  203  ? -43.189 59.635  59.967  1.00 20.23 ? 201  ILE   A O     1 
ATOM   1360  C  CB    . ILE   A 1  203  ? -43.261 62.227  62.007  1.00 18.72 ? 201  ILE   A CB    1 
ATOM   1361  C  CG1   . ILE   A 1  203  ? -44.509 61.396  62.308  1.00 17.24 ? 201  ILE   A CG1   1 
ATOM   1362  C  CG2   . ILE   A 1  203  ? -43.602 63.451  61.139  1.00 19.88 ? 201  ILE   A CG2   1 
ATOM   1363  C  CD1   . ILE   A 1  203  ? -44.261 60.235  63.260  1.00 17.36 ? 201  ILE   A CD1   1 
ATOM   1364  N  N     . ARG   A 1  204  ? -42.380 61.439  58.898  1.00 20.06 ? 202  ARG   A N     1 
ATOM   1365  C  CA    . ARG   A 1  204  ? -42.755 60.898  57.593  1.00 21.38 ? 202  ARG   A CA    1 
ATOM   1366  C  C     . ARG   A 1  204  ? -42.001 59.617  57.277  1.00 19.99 ? 202  ARG   A C     1 
ATOM   1367  O  O     . ARG   A 1  204  ? -42.588 58.653  56.768  1.00 22.01 ? 202  ARG   A O     1 
ATOM   1368  C  CB    . ARG   A 1  204  ? -42.514 61.940  56.504  1.00 25.75 ? 202  ARG   A CB    1 
ATOM   1369  C  CG    . ARG   A 1  204  ? -43.643 62.933  56.396  1.00 32.59 ? 202  ARG   A CG    1 
ATOM   1370  C  CD    . ARG   A 1  204  ? -43.218 64.193  55.667  1.00 35.01 ? 202  ARG   A CD    1 
ATOM   1371  N  NE    . ARG   A 1  204  ? -44.336 65.122  55.550  1.00 35.44 ? 202  ARG   A NE    1 
ATOM   1372  C  CZ    . ARG   A 1  204  ? -44.818 65.842  56.554  1.00 34.45 ? 202  ARG   A CZ    1 
ATOM   1373  N  NH1   . ARG   A 1  204  ? -44.302 65.764  57.776  1.00 27.81 ? 202  ARG   A NH1   1 
ATOM   1374  N  NH2   . ARG   A 1  204  ? -45.846 66.658  56.329  1.00 29.67 ? 202  ARG   A NH2   1 
ATOM   1375  N  N     . GLU   A 1  205  ? -40.695 59.593  57.544  1.00 20.79 ? 203  GLU   A N     1 
ATOM   1376  C  CA    . GLU   A 1  205  ? -39.939 58.366  57.343  1.00 22.06 ? 203  GLU   A CA    1 
ATOM   1377  C  C     . GLU   A 1  205  ? -40.453 57.259  58.248  1.00 21.59 ? 203  GLU   A C     1 
ATOM   1378  O  O     . GLU   A 1  205  ? -40.642 56.122  57.802  1.00 21.82 ? 203  GLU   A O     1 
ATOM   1379  C  CB    . GLU   A 1  205  ? -38.457 58.625  57.598  1.00 23.21 ? 203  GLU   A CB    1 
ATOM   1380  C  CG    . GLU   A 1  205  ? -37.559 57.453  57.259  1.00 26.99 ? 203  GLU   A CG    1 
ATOM   1381  C  CD    . GLU   A 1  205  ? -36.088 57.833  57.308  1.00 37.78 ? 203  GLU   A CD    1 
ATOM   1382  O  OE1   . GLU   A 1  205  ? -35.566 58.071  58.419  1.00 32.00 ? 203  GLU   A OE1   1 
ATOM   1383  O  OE2   . GLU   A 1  205  ? -35.457 57.909  56.232  1.00 39.95 ? 203  GLU   A OE2   1 
ATOM   1384  N  N     . ALA   A 1  206  ? -40.718 57.583  59.517  1.00 19.11 ? 204  ALA   A N     1 
ATOM   1385  C  CA    . ALA   A 1  206  ? -41.199 56.572  60.449  1.00 19.70 ? 204  ALA   A CA    1 
ATOM   1386  C  C     . ALA   A 1  206  ? -42.537 56.013  59.998  1.00 20.72 ? 204  ALA   A C     1 
ATOM   1387  O  O     . ALA   A 1  206  ? -42.771 54.801  60.077  1.00 21.40 ? 204  ALA   A O     1 
ATOM   1388  C  CB    . ALA   A 1  206  ? -41.317 57.167  61.853  1.00 20.35 ? 204  ALA   A CB    1 
ATOM   1389  N  N     . LEU   A 1  207  ? -43.425 56.884  59.511  1.00 18.70 ? 205  LEU   A N     1 
ATOM   1390  C  CA    . LEU   A 1  207  ? -44.727 56.421  59.049  1.00 18.92 ? 205  LEU   A CA    1 
ATOM   1391  C  C     . LEU   A 1  207  ? -44.591 55.492  57.850  1.00 22.45 ? 205  LEU   A C     1 
ATOM   1392  O  O     . LEU   A 1  207  ? -45.289 54.473  57.763  1.00 22.56 ? 205  LEU   A O     1 
ATOM   1393  C  CB    . LEU   A 1  207  ? -45.622 57.615  58.721  1.00 19.43 ? 205  LEU   A CB    1 
ATOM   1394  C  CG    . LEU   A 1  207  ? -46.135 58.347  59.958  1.00 20.00 ? 205  LEU   A CG    1 
ATOM   1395  C  CD1   . LEU   A 1  207  ? -46.696 59.702  59.574  1.00 20.10 ? 205  LEU   A CD1   1 
ATOM   1396  C  CD2   . LEU   A 1  207  ? -47.204 57.509  60.664  1.00 19.91 ? 205  LEU   A CD2   1 
ATOM   1397  N  N     . LYS   A 1  208  ? -43.684 55.813  56.922  1.00 20.55 ? 206  LYS   A N     1 
ATOM   1398  C  CA    . LYS   A 1  208  ? -43.502 54.956  55.753  1.00 22.02 ? 206  LYS   A CA    1 
ATOM   1399  C  C     . LYS   A 1  208  ? -43.034 53.568  56.164  1.00 26.08 ? 206  LYS   A C     1 
ATOM   1400  O  O     . LYS   A 1  208  ? -43.492 52.558  55.614  1.00 29.35 ? 206  LYS   A O     1 
ATOM   1401  C  CB    . LYS   A 1  208  ? -42.496 55.596  54.794  1.00 27.99 ? 206  LYS   A CB    1 
ATOM   1402  N  N     . ARG   A 1  209  ? -42.138 53.500  57.144  1.00 22.60 ? 207  ARG   A N     1 
ATOM   1403  C  CA    . ARG   A 1  209  ? -41.584 52.237  57.611  1.00 25.41 ? 207  ARG   A CA    1 
ATOM   1404  C  C     . ARG   A 1  209  ? -42.528 51.464  58.519  1.00 26.24 ? 207  ARG   A C     1 
ATOM   1405  O  O     . ARG   A 1  209  ? -42.233 50.312  58.852  1.00 30.20 ? 207  ARG   A O     1 
ATOM   1406  C  CB    . ARG   A 1  209  ? -40.269 52.499  58.332  1.00 25.04 ? 207  ARG   A CB    1 
ATOM   1407  C  CG    . ARG   A 1  209  ? -39.201 53.007  57.389  1.00 27.55 ? 207  ARG   A CG    1 
ATOM   1408  C  CD    . ARG   A 1  209  ? -37.983 53.455  58.145  1.00 28.42 ? 207  ARG   A CD    1 
ATOM   1409  N  NE    . ARG   A 1  209  ? -36.955 53.977  57.257  1.00 32.41 ? 207  ARG   A NE    1 
ATOM   1410  C  CZ    . ARG   A 1  209  ? -35.800 54.470  57.679  1.00 37.98 ? 207  ARG   A CZ    1 
ATOM   1411  N  NH1   . ARG   A 1  209  ? -35.507 54.531  58.968  1.00 32.11 ? 207  ARG   A NH1   1 
ATOM   1412  N  NH2   . ARG   A 1  209  ? -34.922 54.920  56.787  1.00 41.66 ? 207  ARG   A NH2   1 
ATOM   1413  N  N     . SER   A 1  210  ? -43.642 52.062  58.930  1.00 23.82 ? 208  SER   A N     1 
ATOM   1414  C  CA    . SER   A 1  210  ? -44.577 51.392  59.824  1.00 21.75 ? 208  SER   A CA    1 
ATOM   1415  C  C     . SER   A 1  210  ? -45.577 50.504  59.099  1.00 24.39 ? 208  SER   A C     1 
ATOM   1416  O  O     . SER   A 1  210  ? -46.211 49.663  59.742  1.00 24.12 ? 208  SER   A O     1 
ATOM   1417  C  CB    . SER   A 1  210  ? -45.346 52.433  60.642  1.00 21.50 ? 208  SER   A CB    1 
ATOM   1418  O  OG    . SER   A 1  210  ? -44.454 53.156  61.480  1.00 24.60 ? 208  SER   A OG    1 
ATOM   1419  N  N     . LYS   A 1  211  ? -45.720 50.665  57.781  1.00 24.95 ? 209  LYS   A N     1 
ATOM   1420  C  CA    . LYS   A 1  211  ? -46.763 49.957  57.047  1.00 25.01 ? 209  LYS   A CA    1 
ATOM   1421  C  C     . LYS   A 1  211  ? -46.570 48.447  57.112  1.00 26.65 ? 209  LYS   A C     1 
ATOM   1422  O  O     . LYS   A 1  211  ? -47.549 47.698  57.217  1.00 27.56 ? 209  LYS   A O     1 
ATOM   1423  C  CB    . LYS   A 1  211  ? -46.787 50.437  55.596  1.00 30.44 ? 209  LYS   A CB    1 
ATOM   1424  N  N     . GLU   A 1  212  ? -45.317 47.986  57.065  1.00 27.23 ? 210  GLU   A N     1 
ATOM   1425  C  CA    . GLU   A 1  212  ? -45.048 46.550  57.000  1.00 30.03 ? 210  GLU   A CA    1 
ATOM   1426  C  C     . GLU   A 1  212  ? -45.627 45.820  58.206  1.00 30.46 ? 210  GLU   A C     1 
ATOM   1427  O  O     . GLU   A 1  212  ? -46.336 44.818  58.059  1.00 31.39 ? 210  GLU   A O     1 
ATOM   1428  C  CB    . GLU   A 1  212  ? -43.545 46.297  56.890  1.00 33.93 ? 210  GLU   A CB    1 
ATOM   1429  C  CG    . GLU   A 1  212  ? -43.180 44.821  56.885  1.00 41.53 ? 210  GLU   A CG    1 
ATOM   1430  C  CD    . GLU   A 1  212  ? -41.686 44.586  56.853  1.00 54.26 ? 210  GLU   A CD    1 
ATOM   1431  O  OE1   . GLU   A 1  212  ? -40.932 45.575  56.738  1.00 58.25 ? 210  GLU   A OE1   1 
ATOM   1432  O  OE2   . GLU   A 1  212  ? -41.267 43.413  56.944  1.00 60.89 ? 210  GLU   A OE2   1 
ATOM   1433  N  N     . LEU   A 1  213  ? -45.344 46.314  59.412  1.00 26.34 ? 211  LEU   A N     1 
ATOM   1434  C  CA    . LEU   A 1  213  ? -45.840 45.640  60.606  1.00 26.40 ? 211  LEU   A CA    1 
ATOM   1435  C  C     . LEU   A 1  213  ? -47.302 45.964  60.890  1.00 25.67 ? 211  LEU   A C     1 
ATOM   1436  O  O     . LEU   A 1  213  ? -48.014 45.133  61.463  1.00 25.09 ? 211  LEU   A O     1 
ATOM   1437  C  CB    . LEU   A 1  213  ? -44.953 45.952  61.809  1.00 22.98 ? 211  LEU   A CB    1 
ATOM   1438  C  CG    . LEU   A 1  213  ? -43.579 45.277  61.744  1.00 28.27 ? 211  LEU   A CG    1 
ATOM   1439  C  CD1   . LEU   A 1  213  ? -42.729 45.583  62.974  1.00 27.81 ? 211  LEU   A CD1   1 
ATOM   1440  C  CD2   . LEU   A 1  213  ? -43.748 43.775  61.567  1.00 31.39 ? 211  LEU   A CD2   1 
ATOM   1441  N  N     . GLU   A 1  214  ? -47.782 47.140  60.484  1.00 22.60 ? 212  GLU   A N     1 
ATOM   1442  C  CA    . GLU   A 1  214  ? -49.215 47.396  60.591  1.00 23.47 ? 212  GLU   A CA    1 
ATOM   1443  C  C     . GLU   A 1  214  ? -50.015 46.377  59.792  1.00 26.26 ? 212  GLU   A C     1 
ATOM   1444  O  O     . GLU   A 1  214  ? -51.072 45.919  60.241  1.00 28.84 ? 212  GLU   A O     1 
ATOM   1445  C  CB    . GLU   A 1  214  ? -49.547 48.813  60.141  1.00 23.06 ? 212  GLU   A CB    1 
ATOM   1446  C  CG    . GLU   A 1  214  ? -49.084 49.856  61.141  1.00 23.74 ? 212  GLU   A CG    1 
ATOM   1447  C  CD    . GLU   A 1  214  ? -49.486 51.258  60.751  1.00 24.67 ? 212  GLU   A CD    1 
ATOM   1448  O  OE1   . GLU   A 1  214  ? -49.799 51.494  59.563  1.00 27.32 ? 212  GLU   A OE1   1 
ATOM   1449  O  OE2   . GLU   A 1  214  ? -49.480 52.131  61.640  1.00 28.51 ? 212  GLU   A OE2   1 
ATOM   1450  N  N     . GLU   A 1  215  ? -49.513 45.989  58.617  1.00 26.66 ? 213  GLU   A N     1 
ATOM   1451  C  CA    . GLU   A 1  215  ? -50.218 45.016  57.794  1.00 30.94 ? 213  GLU   A CA    1 
ATOM   1452  C  C     . GLU   A 1  215  ? -50.298 43.652  58.464  1.00 35.31 ? 213  GLU   A C     1 
ATOM   1453  O  O     . GLU   A 1  215  ? -51.166 42.847  58.111  1.00 36.22 ? 213  GLU   A O     1 
ATOM   1454  C  CB    . GLU   A 1  215  ? -49.543 44.897  56.426  1.00 32.38 ? 213  GLU   A CB    1 
ATOM   1455  N  N     . LYS   A 1  216  ? -49.430 43.387  59.432  1.00 33.64 ? 214  LYS   A N     1 
ATOM   1456  C  CA    . LYS   A 1  216  ? -49.410 42.129  60.162  1.00 32.50 ? 214  LYS   A CA    1 
ATOM   1457  C  C     . LYS   A 1  216  ? -50.199 42.182  61.464  1.00 35.41 ? 214  LYS   A C     1 
ATOM   1458  O  O     . LYS   A 1  216  ? -50.355 41.149  62.122  1.00 38.76 ? 214  LYS   A O     1 
ATOM   1459  C  CB    . LYS   A 1  216  ? -47.964 41.712  60.425  1.00 29.99 ? 214  LYS   A CB    1 
ATOM   1460  C  CG    . LYS   A 1  216  ? -47.188 41.506  59.138  1.00 40.23 ? 214  LYS   A CG    1 
ATOM   1461  C  CD    . LYS   A 1  216  ? -45.738 41.124  59.374  1.00 51.95 ? 214  LYS   A CD    1 
ATOM   1462  C  CE    . LYS   A 1  216  ? -45.060 40.802  58.048  1.00 50.55 ? 214  LYS   A CE    1 
ATOM   1463  N  NZ    . LYS   A 1  216  ? -43.580 40.732  58.171  1.00 63.99 ? 214  LYS   A NZ    1 
ATOM   1464  N  N     . GLY   A 1  217  ? -50.714 43.348  61.847  1.00 28.08 ? 215  GLY   A N     1 
ATOM   1465  C  CA    . GLY   A 1  217  ? -51.523 43.477  63.042  1.00 27.34 ? 215  GLY   A CA    1 
ATOM   1466  C  C     . GLY   A 1  217  ? -50.899 44.306  64.139  1.00 24.37 ? 215  GLY   A C     1 
ATOM   1467  O  O     . GLY   A 1  217  ? -51.501 44.438  65.210  1.00 28.64 ? 215  GLY   A O     1 
ATOM   1468  N  N     . PHE   A 1  218  ? -49.713 44.854  63.923  1.00 24.49 ? 216  PHE   A N     1 
ATOM   1469  C  CA    . PHE   A 1  218  ? -49.155 45.762  64.904  1.00 20.17 ? 216  PHE   A CA    1 
ATOM   1470  C  C     . PHE   A 1  218  ? -49.751 47.146  64.715  1.00 21.77 ? 216  PHE   A C     1 
ATOM   1471  O  O     . PHE   A 1  218  ? -50.279 47.490  63.656  1.00 22.04 ? 216  PHE   A O     1 
ATOM   1472  C  CB    . PHE   A 1  218  ? -47.638 45.884  64.731  1.00 20.16 ? 216  PHE   A CB    1 
ATOM   1473  C  CG    . PHE   A 1  218  ? -46.865 44.674  65.169  1.00 22.64 ? 216  PHE   A CG    1 
ATOM   1474  C  CD1   . PHE   A 1  218  ? -46.710 43.585  64.324  1.00 25.85 ? 216  PHE   A CD1   1 
ATOM   1475  C  CD2   . PHE   A 1  218  ? -46.260 44.644  66.413  1.00 21.65 ? 216  PHE   A CD2   1 
ATOM   1476  C  CE1   . PHE   A 1  218  ? -45.976 42.480  64.727  1.00 24.62 ? 216  PHE   A CE1   1 
ATOM   1477  C  CE2   . PHE   A 1  218  ? -45.526 43.539  66.824  1.00 24.46 ? 216  PHE   A CE2   1 
ATOM   1478  C  CZ    . PHE   A 1  218  ? -45.388 42.457  65.978  1.00 24.63 ? 216  PHE   A CZ    1 
ATOM   1479  N  N     . SER   A 1  219  ? -49.636 47.956  65.756  1.00 20.20 ? 217  SER   A N     1 
ATOM   1480  C  CA    . SER   A 1  219  ? -49.922 49.378  65.677  1.00 19.56 ? 217  SER   A CA    1 
ATOM   1481  C  C     . SER   A 1  219  ? -48.695 50.123  66.177  1.00 19.90 ? 217  SER   A C     1 
ATOM   1482  O  O     . SER   A 1  219  ? -47.702 49.518  66.588  1.00 17.96 ? 217  SER   A O     1 
ATOM   1483  C  CB    . SER   A 1  219  ? -51.159 49.747  66.495  1.00 21.60 ? 217  SER   A CB    1 
ATOM   1484  O  OG    . SER   A 1  219  ? -50.957 49.411  67.850  1.00 23.65 ? 217  SER   A OG    1 
ATOM   1485  N  N     . TYR   A 1  220  ? -48.773 51.450  66.154  1.00 17.79 ? 218  TYR   A N     1 
ATOM   1486  C  CA    . TYR   A 1  220  ? -47.640 52.291  66.506  1.00 17.55 ? 218  TYR   A CA    1 
ATOM   1487  C  C     . TYR   A 1  220  ? -48.049 53.422  67.431  1.00 17.54 ? 218  TYR   A C     1 
ATOM   1488  O  O     . TYR   A 1  220  ? -49.164 53.943  67.360  1.00 17.13 ? 218  TYR   A O     1 
ATOM   1489  C  CB    . TYR   A 1  220  ? -46.993 52.899  65.254  1.00 18.70 ? 218  TYR   A CB    1 
ATOM   1490  C  CG    . TYR   A 1  220  ? -46.080 51.921  64.583  1.00 17.52 ? 218  TYR   A CG    1 
ATOM   1491  C  CD1   . TYR   A 1  220  ? -46.578 50.972  63.695  1.00 21.66 ? 218  TYR   A CD1   1 
ATOM   1492  C  CD2   . TYR   A 1  220  ? -44.726 51.933  64.848  1.00 19.11 ? 218  TYR   A CD2   1 
ATOM   1493  C  CE1   . TYR   A 1  220  ? -45.735 50.055  63.094  1.00 20.31 ? 218  TYR   A CE1   1 
ATOM   1494  C  CE2   . TYR   A 1  220  ? -43.877 51.028  64.252  1.00 19.67 ? 218  TYR   A CE2   1 
ATOM   1495  C  CZ    . TYR   A 1  220  ? -44.384 50.099  63.374  1.00 20.89 ? 218  TYR   A CZ    1 
ATOM   1496  O  OH    . TYR   A 1  220  ? -43.522 49.200  62.795  1.00 22.50 ? 218  TYR   A OH    1 
ATOM   1497  N  N     . SER   A 1  221  ? -47.108 53.814  68.284  1.00 17.27 ? 219  SER   A N     1 
ATOM   1498  C  CA    . SER   A 1  221  ? -47.173 55.071  69.018  1.00 17.39 ? 219  SER   A CA    1 
ATOM   1499  C  C     . SER   A 1  221  ? -45.827 55.748  68.835  1.00 16.07 ? 219  SER   A C     1 
ATOM   1500  O  O     . SER   A 1  221  ? -44.800 55.195  69.234  1.00 19.90 ? 219  SER   A O     1 
ATOM   1501  C  CB    . SER   A 1  221  ? -47.412 54.827  70.508  1.00 20.14 ? 219  SER   A CB    1 
ATOM   1502  O  OG    . SER   A 1  221  ? -47.540 56.074  71.183  1.00 19.79 ? 219  SER   A OG    1 
ATOM   1503  N  N     . TYR   A 1  222  ? -45.830 56.950  68.286  1.00 14.87 ? 220  TYR   A N     1 
ATOM   1504  C  CA    . TYR   A 1  222  ? -44.579 57.609  67.928  1.00 15.81 ? 220  TYR   A CA    1 
ATOM   1505  C  C     . TYR   A 1  222  ? -44.093 58.506  69.051  1.00 18.93 ? 220  TYR   A C     1 
ATOM   1506  O  O     . TYR   A 1  222  ? -44.856 59.303  69.603  1.00 18.88 ? 220  TYR   A O     1 
ATOM   1507  C  CB    . TYR   A 1  222  ? -44.739 58.387  66.621  1.00 16.75 ? 220  TYR   A CB    1 
ATOM   1508  C  CG    . TYR   A 1  222  ? -45.068 57.454  65.494  1.00 15.58 ? 220  TYR   A CG    1 
ATOM   1509  C  CD1   . TYR   A 1  222  ? -44.077 56.706  64.874  1.00 16.46 ? 220  TYR   A CD1   1 
ATOM   1510  C  CD2   . TYR   A 1  222  ? -46.377 57.282  65.078  1.00 15.59 ? 220  TYR   A CD2   1 
ATOM   1511  C  CE1   . TYR   A 1  222  ? -44.386 55.823  63.857  1.00 17.78 ? 220  TYR   A CE1   1 
ATOM   1512  C  CE2   . TYR   A 1  222  ? -46.692 56.413  64.074  1.00 17.53 ? 220  TYR   A CE2   1 
ATOM   1513  C  CZ    . TYR   A 1  222  ? -45.699 55.686  63.465  1.00 17.69 ? 220  TYR   A CZ    1 
ATOM   1514  O  OH    . TYR   A 1  222  ? -46.051 54.819  62.459  1.00 20.98 ? 220  TYR   A OH    1 
ATOM   1515  N  N     . ASP   A 1  223  ? -42.805 58.384  69.354  1.00 19.60 ? 221  ASP   A N     1 
ATOM   1516  C  CA    . ASP   A 1  223  ? -42.116 59.161  70.374  1.00 23.35 ? 221  ASP   A CA    1 
ATOM   1517  C  C     . ASP   A 1  223  ? -41.161 60.110  69.660  1.00 24.42 ? 221  ASP   A C     1 
ATOM   1518  O  O     . ASP   A 1  223  ? -40.143 59.672  69.106  1.00 20.93 ? 221  ASP   A O     1 
ATOM   1519  C  CB    . ASP   A 1  223  ? -41.331 58.197  71.249  1.00 24.31 ? 221  ASP   A CB    1 
ATOM   1520  C  CG    . ASP   A 1  223  ? -40.414 58.904  72.227  1.00 27.11 ? 221  ASP   A CG    1 
ATOM   1521  O  OD1   . ASP   A 1  223  ? -40.630 60.104  72.495  1.00 29.57 ? 221  ASP   A OD1   1 
ATOM   1522  O  OD2   . ASP   A 1  223  ? -39.481 58.241  72.719  1.00 36.12 ? 221  ASP   A OD2   1 
ATOM   1523  N  N     . MET   A 1  224  ? -41.480 61.402  69.676  1.00 21.71 ? 222  MET   A N     1 
ATOM   1524  C  CA    . MET   A 1  224  ? -40.634 62.405  69.044  1.00 24.70 ? 222  MET   A CA    1 
ATOM   1525  C  C     . MET   A 1  224  ? -39.379 62.715  69.859  1.00 25.89 ? 222  MET   A C     1 
ATOM   1526  O  O     . MET   A 1  224  ? -38.628 63.621  69.491  1.00 34.25 ? 222  MET   A O     1 
ATOM   1527  C  CB    . MET   A 1  224  ? -41.432 63.675  68.730  1.00 24.75 ? 222  MET   A CB    1 
ATOM   1528  C  CG    . MET   A 1  224  ? -42.644 63.437  67.823  1.00 29.00 ? 222  MET   A CG    1 
ATOM   1529  S  SD    . MET   A 1  224  ? -42.274 62.481  66.329  1.00 31.69 ? 222  MET   A SD    1 
ATOM   1530  C  CE    . MET   A 1  224  ? -41.222 63.631  65.466  1.00 33.58 ? 222  MET   A CE    1 
ATOM   1531  N  N     . LEU   A 1  225  ? -39.146 61.988  70.946  1.00 30.60 ? 223  LEU   A N     1 
ATOM   1532  C  CA    . LEU   A 1  225  ? -37.893 61.996  71.692  1.00 28.43 ? 223  LEU   A CA    1 
ATOM   1533  C  C     . LEU   A 1  225  ? -37.640 63.300  72.439  1.00 36.02 ? 223  LEU   A C     1 
ATOM   1534  O  O     . LEU   A 1  225  ? -36.540 63.498  72.960  1.00 36.73 ? 223  LEU   A O     1 
ATOM   1535  C  CB    . LEU   A 1  225  ? -36.692 61.605  70.821  1.00 30.37 ? 223  LEU   A CB    1 
ATOM   1536  C  CG    . LEU   A 1  225  ? -36.590 60.137  70.389  1.00 29.46 ? 223  LEU   A CG    1 
ATOM   1537  C  CD1   . LEU   A 1  225  ? -35.436 59.946  69.412  1.00 31.70 ? 223  LEU   A CD1   1 
ATOM   1538  C  CD2   . LEU   A 1  225  ? -36.417 59.227  71.601  1.00 30.54 ? 223  LEU   A CD2   1 
ATOM   1539  N  N     . GLY   A 1  226  ? -38.625 64.190  72.512  1.00 33.30 ? 224  GLY   A N     1 
ATOM   1540  C  CA    . GLY   A 1  226  ? -38.473 65.384  73.317  1.00 34.32 ? 224  GLY   A CA    1 
ATOM   1541  C  C     . GLY   A 1  226  ? -38.569 65.075  74.799  1.00 33.09 ? 224  GLY   A C     1 
ATOM   1542  O  O     . GLY   A 1  226  ? -39.304 64.187  75.231  1.00 30.24 ? 224  GLY   A O     1 
ATOM   1543  N  N     . GLU   A 1  227  ? -37.820 65.834  75.593  1.00 29.10 ? 225  GLU   A N     1 
ATOM   1544  C  CA    . GLU   A 1  227  ? -37.726 65.527  77.011  1.00 32.51 ? 225  GLU   A CA    1 
ATOM   1545  C  C     . GLU   A 1  227  ? -36.987 66.657  77.703  1.00 27.88 ? 225  GLU   A C     1 
ATOM   1546  O  O     . GLU   A 1  227  ? -36.025 67.194  77.155  1.00 25.38 ? 225  GLU   A O     1 
ATOM   1547  C  CB    . GLU   A 1  227  ? -36.947 64.222  77.183  1.00 40.50 ? 225  GLU   A CB    1 
ATOM   1548  C  CG    . GLU   A 1  227  ? -36.769 63.758  78.591  1.00 44.88 ? 225  GLU   A CG    1 
ATOM   1549  C  CD    . GLU   A 1  227  ? -36.133 62.390  78.636  1.00 45.07 ? 225  GLU   A CD    1 
ATOM   1550  O  OE1   . GLU   A 1  227  ? -36.161 61.694  77.593  1.00 36.13 ? 225  GLU   A OE1   1 
ATOM   1551  O  OE2   . GLU   A 1  227  ? -35.608 62.016  79.704  1.00 48.35 ? 225  GLU   A OE2   1 
ATOM   1552  N  N     . ALA   A 1  228  ? -37.451 67.014  78.898  1.00 24.88 ? 226  ALA   A N     1 
ATOM   1553  C  CA    . ALA   A 1  228  ? -36.743 67.920  79.795  1.00 25.77 ? 226  ALA   A CA    1 
ATOM   1554  C  C     . ALA   A 1  228  ? -36.345 69.219  79.086  1.00 21.89 ? 226  ALA   A C     1 
ATOM   1555  O  O     . ALA   A 1  228  ? -35.169 69.532  78.908  1.00 25.81 ? 226  ALA   A O     1 
ATOM   1556  C  CB    . ALA   A 1  228  ? -35.532 67.212  80.410  1.00 29.38 ? 226  ALA   A CB    1 
ATOM   1557  N  N     . ALA   A 1  229  ? -37.365 69.982  78.703  1.00 19.34 ? 227  ALA   A N     1 
ATOM   1558  C  CA    . ALA   A 1  229  ? -37.131 71.333  78.213  1.00 18.23 ? 227  ALA   A CA    1 
ATOM   1559  C  C     . ALA   A 1  229  ? -36.392 72.146  79.267  1.00 17.94 ? 227  ALA   A C     1 
ATOM   1560  O  O     . ALA   A 1  229  ? -36.744 72.127  80.450  1.00 18.02 ? 227  ALA   A O     1 
ATOM   1561  C  CB    . ALA   A 1  229  ? -38.457 72.015  77.892  1.00 19.82 ? 227  ALA   A CB    1 
ATOM   1562  N  N     . THR   A 1  230  ? -35.367 72.863  78.830  1.00 17.41 ? 228  THR   A N     1 
ATOM   1563  C  CA    . THR   A 1  230  ? -34.599 73.736  79.708  1.00 19.20 ? 228  THR   A CA    1 
ATOM   1564  C  C     . THR   A 1  230  ? -35.022 75.188  79.589  1.00 16.75 ? 228  THR   A C     1 
ATOM   1565  O  O     . THR   A 1  230  ? -34.867 75.959  80.543  1.00 17.80 ? 228  THR   A O     1 
ATOM   1566  C  CB    . THR   A 1  230  ? -33.112 73.607  79.348  1.00 19.84 ? 228  THR   A CB    1 
ATOM   1567  O  OG1   . THR   A 1  230  ? -32.721 72.230  79.470  1.00 26.34 ? 228  THR   A OG1   1 
ATOM   1568  C  CG2   . THR   A 1  230  ? -32.252 74.427  80.279  1.00 23.65 ? 228  THR   A CG2   1 
ATOM   1569  N  N     . THR   A 1  231  ? -35.567 75.579  78.446  1.00 17.44 ? 229  THR   A N     1 
ATOM   1570  C  CA    . THR   A 1  231  ? -35.927 76.959  78.178  1.00 16.08 ? 229  THR   A CA    1 
ATOM   1571  C  C     . THR   A 1  231  ? -37.317 76.985  77.568  1.00 17.40 ? 229  THR   A C     1 
ATOM   1572  O  O     . THR   A 1  231  ? -37.830 75.962  77.107  1.00 17.05 ? 229  THR   A O     1 
ATOM   1573  C  CB    . THR   A 1  231  ? -34.962 77.610  77.174  1.00 17.99 ? 229  THR   A CB    1 
ATOM   1574  O  OG1   . THR   A 1  231  ? -35.160 77.024  75.880  1.00 18.35 ? 229  THR   A OG1   1 
ATOM   1575  C  CG2   . THR   A 1  231  ? -33.492 77.424  77.597  1.00 17.62 ? 229  THR   A CG2   1 
ATOM   1576  N  N     . ALA   A 1  232  ? -37.917 78.173  77.591  1.00 18.10 ? 230  ALA   A N     1 
ATOM   1577  C  CA    . ALA   A 1  232  ? -39.182 78.373  76.899  1.00 17.37 ? 230  ALA   A CA    1 
ATOM   1578  C  C     . ALA   A 1  232  ? -39.061 77.998  75.431  1.00 20.34 ? 230  ALA   A C     1 
ATOM   1579  O  O     . ALA   A 1  232  ? -39.956 77.354  74.872  1.00 19.82 ? 230  ALA   A O     1 
ATOM   1580  C  CB    . ALA   A 1  232  ? -39.619 79.828  77.044  1.00 18.88 ? 230  ALA   A CB    1 
ATOM   1581  N  N     . ALA   A 1  233  ? -37.950 78.364  74.794  1.00 20.09 ? 231  ALA   A N     1 
ATOM   1582  C  CA    . ALA   A 1  233  ? -37.780 78.053  73.378  1.00 22.95 ? 231  ALA   A CA    1 
ATOM   1583  C  C     . ALA   A 1  233  ? -37.721 76.550  73.136  1.00 20.66 ? 231  ALA   A C     1 
ATOM   1584  O  O     . ALA   A 1  233  ? -38.282 76.056  72.149  1.00 23.33 ? 231  ALA   A O     1 
ATOM   1585  C  CB    . ALA   A 1  233  ? -36.533 78.745  72.823  1.00 24.67 ? 231  ALA   A CB    1 
ATOM   1586  N  N     . ASP   A 1  234  ? -37.066 75.800  74.026  1.00 19.69 ? 232  ASP   A N     1 
ATOM   1587  C  CA    . ASP   A 1  234  ? -37.084 74.343  73.918  1.00 21.38 ? 232  ASP   A CA    1 
ATOM   1588  C  C     . ASP   A 1  234  ? -38.507 73.834  73.982  1.00 20.83 ? 232  ASP   A C     1 
ATOM   1589  O  O     . ASP   A 1  234  ? -38.906 72.958  73.211  1.00 21.03 ? 232  ASP   A O     1 
ATOM   1590  C  CB    . ASP   A 1  234  ? -36.357 73.697  75.098  1.00 24.09 ? 232  ASP   A CB    1 
ATOM   1591  C  CG    . ASP   A 1  234  ? -34.871 73.835  75.042  1.00 32.39 ? 232  ASP   A CG    1 
ATOM   1592  O  OD1   . ASP   A 1  234  ? -34.315 74.099  73.957  1.00 31.75 ? 232  ASP   A OD1   1 
ATOM   1593  O  OD2   . ASP   A 1  234  ? -34.259 73.647  76.117  1.00 30.82 ? 232  ASP   A OD2   1 
ATOM   1594  N  N     . ALA   A 1  235  ? -39.264 74.320  74.963  1.00 18.27 ? 233  ALA   A N     1 
ATOM   1595  C  CA    . ALA   A 1  235  ? -40.618 73.826  75.141  1.00 17.90 ? 233  ALA   A CA    1 
ATOM   1596  C  C     . ALA   A 1  235  ? -41.463 74.142  73.922  1.00 20.27 ? 233  ALA   A C     1 
ATOM   1597  O  O     . ALA   A 1  235  ? -42.283 73.320  73.495  1.00 19.63 ? 233  ALA   A O     1 
ATOM   1598  C  CB    . ALA   A 1  235  ? -41.230 74.425  76.408  1.00 19.49 ? 233  ALA   A CB    1 
ATOM   1599  N  N     . GLU   A 1  236  ? -41.269 75.326  73.339  1.00 20.57 ? 234  GLU   A N     1 
ATOM   1600  C  CA    . GLU   A 1  236  ? -41.997 75.671  72.123  1.00 20.87 ? 234  GLU   A CA    1 
ATOM   1601  C  C     . GLU   A 1  236  ? -41.588 74.771  70.965  1.00 19.23 ? 234  GLU   A C     1 
ATOM   1602  O  O     . GLU   A 1  236  ? -42.435 74.361  70.160  1.00 19.62 ? 234  GLU   A O     1 
ATOM   1603  C  CB    . GLU   A 1  236  ? -41.748 77.140  71.776  1.00 24.33 ? 234  GLU   A CB    1 
ATOM   1604  C  CG    . GLU   A 1  236  ? -42.525 78.116  72.636  1.00 34.43 ? 234  GLU   A CG    1 
ATOM   1605  C  CD    . GLU   A 1  236  ? -41.771 79.413  72.898  1.00 45.30 ? 234  GLU   A CD    1 
ATOM   1606  O  OE1   . GLU   A 1  236  ? -40.772 79.678  72.194  1.00 48.83 ? 234  GLU   A OE1   1 
ATOM   1607  O  OE2   . GLU   A 1  236  ? -42.177 80.162  73.815  1.00 46.37 ? 234  GLU   A OE2   1 
ATOM   1608  N  N     . ARG   A 1  237  ? -40.293 74.468  70.856  1.00 18.54 ? 235  ARG   A N     1 
ATOM   1609  C  CA    . ARG   A 1  237  ? -39.813 73.566  69.812  1.00 20.77 ? 235  ARG   A CA    1 
ATOM   1610  C  C     . ARG   A 1  237  ? -40.429 72.180  69.956  1.00 22.70 ? 235  ARG   A C     1 
ATOM   1611  O  O     . ARG   A 1  237  ? -40.911 71.598  68.982  1.00 21.08 ? 235  ARG   A O     1 
ATOM   1612  C  CB    . ARG   A 1  237  ? -38.283 73.502  69.820  1.00 21.88 ? 235  ARG   A CB    1 
ATOM   1613  C  CG    . ARG   A 1  237  ? -37.701 72.476  68.857  1.00 30.04 ? 235  ARG   A CG    1 
ATOM   1614  C  CD    . ARG   A 1  237  ? -36.193 72.656  68.683  1.00 39.14 ? 235  ARG   A CD    1 
ATOM   1615  N  NE    . ARG   A 1  237  ? -35.495 72.606  69.962  1.00 41.87 ? 235  ARG   A NE    1 
ATOM   1616  C  CZ    . ARG   A 1  237  ? -35.099 71.490  70.557  1.00 45.94 ? 235  ARG   A CZ    1 
ATOM   1617  N  NH1   . ARG   A 1  237  ? -35.300 70.303  70.005  1.00 49.03 ? 235  ARG   A NH1   1 
ATOM   1618  N  NH2   . ARG   A 1  237  ? -34.486 71.565  71.736  1.00 41.56 ? 235  ARG   A NH2   1 
ATOM   1619  N  N     . TYR   A 1  238  ? -40.434 71.635  71.172  1.00 18.29 ? 236  TYR   A N     1 
ATOM   1620  C  CA    . TYR   A 1  238  ? -41.044 70.328  71.357  1.00 19.50 ? 236  TYR   A CA    1 
ATOM   1621  C  C     . TYR   A 1  238  ? -42.535 70.385  71.063  1.00 17.11 ? 236  TYR   A C     1 
ATOM   1622  O  O     . TYR   A 1  238  ? -43.094 69.446  70.481  1.00 19.29 ? 236  TYR   A O     1 
ATOM   1623  C  CB    . TYR   A 1  238  ? -40.771 69.822  72.774  1.00 17.53 ? 236  TYR   A CB    1 
ATOM   1624  C  CG    . TYR   A 1  238  ? -39.324 69.466  73.011  1.00 19.06 ? 236  TYR   A CG    1 
ATOM   1625  C  CD1   . TYR   A 1  238  ? -38.587 68.771  72.059  1.00 25.94 ? 236  TYR   A CD1   1 
ATOM   1626  C  CD2   . TYR   A 1  238  ? -38.690 69.831  74.186  1.00 20.36 ? 236  TYR   A CD2   1 
ATOM   1627  C  CE1   . TYR   A 1  238  ? -37.249 68.449  72.279  1.00 26.31 ? 236  TYR   A CE1   1 
ATOM   1628  C  CE2   . TYR   A 1  238  ? -37.365 69.511  74.417  1.00 25.31 ? 236  TYR   A CE2   1 
ATOM   1629  C  CZ    . TYR   A 1  238  ? -36.651 68.821  73.465  1.00 29.31 ? 236  TYR   A CZ    1 
ATOM   1630  O  OH    . TYR   A 1  238  ? -35.332 68.509  73.711  1.00 31.77 ? 236  TYR   A OH    1 
ATOM   1631  N  N     . TYR   A 1  239  ? -43.197 71.479  71.452  1.00 16.81 ? 237  TYR   A N     1 
ATOM   1632  C  CA    . TYR   A 1  239  ? -44.612 71.637  71.140  1.00 16.58 ? 237  TYR   A CA    1 
ATOM   1633  C  C     . TYR   A 1  239  ? -44.852 71.548  69.640  1.00 18.67 ? 237  TYR   A C     1 
ATOM   1634  O  O     . TYR   A 1  239  ? -45.670 70.745  69.177  1.00 18.23 ? 237  TYR   A O     1 
ATOM   1635  C  CB    . TYR   A 1  239  ? -45.156 72.956  71.678  1.00 18.92 ? 237  TYR   A CB    1 
ATOM   1636  C  CG    . TYR   A 1  239  ? -46.610 73.074  71.338  1.00 19.85 ? 237  TYR   A CG    1 
ATOM   1637  C  CD1   . TYR   A 1  239  ? -47.013 73.640  70.137  1.00 21.04 ? 237  TYR   A CD1   1 
ATOM   1638  C  CD2   . TYR   A 1  239  ? -47.584 72.556  72.179  1.00 19.96 ? 237  TYR   A CD2   1 
ATOM   1639  C  CE1   . TYR   A 1  239  ? -48.345 73.715  69.790  1.00 23.99 ? 237  TYR   A CE1   1 
ATOM   1640  C  CE2   . TYR   A 1  239  ? -48.910 72.635  71.847  1.00 21.58 ? 237  TYR   A CE2   1 
ATOM   1641  C  CZ    . TYR   A 1  239  ? -49.289 73.210  70.656  1.00 22.83 ? 237  TYR   A CZ    1 
ATOM   1642  O  OH    . TYR   A 1  239  ? -50.614 73.287  70.308  1.00 26.83 ? 237  TYR   A OH    1 
ATOM   1643  N  N     . ARG   A 1  240  ? -44.158 72.379  68.864  1.00 17.71 ? 238  ARG   A N     1 
ATOM   1644  C  CA    . ARG   A 1  240  ? -44.426 72.360  67.431  1.00 17.51 ? 238  ARG   A CA    1 
ATOM   1645  C  C     . ARG   A 1  240  ? -44.012 71.038  66.792  1.00 18.52 ? 238  ARG   A C     1 
ATOM   1646  O  O     . ARG   A 1  240  ? -44.601 70.644  65.785  1.00 17.92 ? 238  ARG   A O     1 
ATOM   1647  C  CB    . ARG   A 1  240  ? -43.823 73.586  66.733  1.00 22.31 ? 238  ARG   A CB    1 
ATOM   1648  C  CG    . ARG   A 1  240  ? -42.341 73.636  66.779  1.00 24.66 ? 238  ARG   A CG    1 
ATOM   1649  C  CD    . ARG   A 1  240  ? -41.803 74.786  65.935  1.00 21.74 ? 238  ARG   A CD    1 
ATOM   1650  N  NE    . ARG   A 1  240  ? -40.362 74.907  66.120  1.00 22.65 ? 238  ARG   A NE    1 
ATOM   1651  C  CZ    . ARG   A 1  240  ? -39.783 75.689  67.026  1.00 27.13 ? 238  ARG   A CZ    1 
ATOM   1652  N  NH1   . ARG   A 1  240  ? -40.487 76.512  67.787  1.00 21.94 ? 238  ARG   A NH1   1 
ATOM   1653  N  NH2   . ARG   A 1  240  ? -38.462 75.644  67.171  1.00 28.88 ? 238  ARG   A NH2   1 
ATOM   1654  N  N     . ASP   A 1  241  ? -43.019 70.334  67.353  1.00 17.33 ? 239  ASP   A N     1 
ATOM   1655  C  CA    . ASP   A 1  241  ? -42.693 68.991  66.873  1.00 16.93 ? 239  ASP   A CA    1 
ATOM   1656  C  C     . ASP   A 1  241  ? -43.839 68.015  67.134  1.00 18.96 ? 239  ASP   A C     1 
ATOM   1657  O  O     . ASP   A 1  241  ? -44.181 67.194  66.273  1.00 18.45 ? 239  ASP   A O     1 
ATOM   1658  C  CB    . ASP   A 1  241  ? -41.432 68.461  67.555  1.00 21.32 ? 239  ASP   A CB    1 
ATOM   1659  C  CG    . ASP   A 1  241  ? -40.169 69.159  67.102  1.00 32.65 ? 239  ASP   A CG    1 
ATOM   1660  O  OD1   . ASP   A 1  241  ? -40.219 69.947  66.132  1.00 38.47 ? 239  ASP   A OD1   1 
ATOM   1661  O  OD2   . ASP   A 1  241  ? -39.120 68.917  67.743  1.00 44.70 ? 239  ASP   A OD2   1 
ATOM   1662  N  N     . TYR   A 1  242  ? -44.423 68.059  68.331  1.00 16.78 ? 240  TYR   A N     1 
ATOM   1663  C  CA    . TYR   A 1  242  ? -45.574 67.200  68.605  1.00 16.53 ? 240  TYR   A CA    1 
ATOM   1664  C  C     . TYR   A 1  242  ? -46.752 67.554  67.710  1.00 15.62 ? 240  TYR   A C     1 
ATOM   1665  O  O     . TYR   A 1  242  ? -47.431 66.666  67.179  1.00 15.55 ? 240  TYR   A O     1 
ATOM   1666  C  CB    . TYR   A 1  242  ? -46.001 67.346  70.062  1.00 15.02 ? 240  TYR   A CB    1 
ATOM   1667  C  CG    . TYR   A 1  242  ? -45.118 66.695  71.094  1.00 15.26 ? 240  TYR   A CG    1 
ATOM   1668  C  CD1   . TYR   A 1  242  ? -44.470 65.493  70.856  1.00 16.87 ? 240  TYR   A CD1   1 
ATOM   1669  C  CD2   . TYR   A 1  242  ? -44.973 67.281  72.330  1.00 17.15 ? 240  TYR   A CD2   1 
ATOM   1670  C  CE1   . TYR   A 1  242  ? -43.682 64.911  71.845  1.00 19.60 ? 240  TYR   A CE1   1 
ATOM   1671  C  CE2   . TYR   A 1  242  ? -44.186 66.724  73.299  1.00 16.18 ? 240  TYR   A CE2   1 
ATOM   1672  C  CZ    . TYR   A 1  242  ? -43.562 65.542  73.064  1.00 15.35 ? 240  TYR   A CZ    1 
ATOM   1673  O  OH    . TYR   A 1  242  ? -42.786 65.005  74.074  1.00 17.11 ? 240  TYR   A OH    1 
ATOM   1674  N  N     . GLU   A 1  243  ? -47.007 68.846  67.532  1.00 15.21 ? 241  GLU   A N     1 
ATOM   1675  C  CA    . GLU   A 1  243  ? -48.133 69.267  66.709  1.00 16.29 ? 241  GLU   A CA    1 
ATOM   1676  C  C     . GLU   A 1  243  ? -47.945 68.792  65.274  1.00 16.58 ? 241  GLU   A C     1 
ATOM   1677  O  O     . GLU   A 1  243  ? -48.857 68.215  64.673  1.00 16.71 ? 241  GLU   A O     1 
ATOM   1678  C  CB    . GLU   A 1  243  ? -48.267 70.789  66.792  1.00 18.23 ? 241  GLU   A CB    1 
ATOM   1679  C  CG    . GLU   A 1  243  ? -49.376 71.387  65.969  1.00 21.46 ? 241  GLU   A CG    1 
ATOM   1680  C  CD    . GLU   A 1  243  ? -49.248 72.906  65.860  1.00 23.41 ? 241  GLU   A CD    1 
ATOM   1681  O  OE1   . GLU   A 1  243  ? -48.109 73.448  65.892  1.00 30.06 ? 241  GLU   A OE1   1 
ATOM   1682  O  OE2   . GLU   A 1  243  ? -50.287 73.555  65.729  1.00 22.62 ? 241  GLU   A OE2   1 
ATOM   1683  N  N     . SER   A 1  244  ? -46.743 68.976  64.728  1.00 16.76 ? 242  SER   A N     1 
ATOM   1684  C  CA    . SER   A 1  244  ? -46.492 68.534  63.360  1.00 16.31 ? 242  SER   A CA    1 
ATOM   1685  C  C     . SER   A 1  244  ? -46.569 67.016  63.245  1.00 16.77 ? 242  SER   A C     1 
ATOM   1686  O  O     . SER   A 1  244  ? -47.067 66.488  62.245  1.00 18.69 ? 242  SER   A O     1 
ATOM   1687  C  CB    . SER   A 1  244  ? -45.137 69.050  62.869  1.00 18.14 ? 242  SER   A CB    1 
ATOM   1688  O  OG    . SER   A 1  244  ? -44.067 68.438  63.572  1.00 23.63 ? 242  SER   A OG    1 
ATOM   1689  N  N     . ALA   A 1  245  ? -46.102 66.294  64.266  1.00 16.39 ? 243  ALA   A N     1 
ATOM   1690  C  CA    . ALA   A 1  245  ? -46.217 64.840  64.235  1.00 15.50 ? 243  ALA   A CA    1 
ATOM   1691  C  C     . ALA   A 1  245  ? -47.674 64.394  64.290  1.00 16.45 ? 243  ALA   A C     1 
ATOM   1692  O  O     . ALA   A 1  245  ? -48.071 63.458  63.590  1.00 17.03 ? 243  ALA   A O     1 
ATOM   1693  C  CB    . ALA   A 1  245  ? -45.404 64.213  65.369  1.00 17.80 ? 243  ALA   A CB    1 
ATOM   1694  N  N     . ILE   A 1  246  ? -48.484 65.032  65.135  1.00 15.46 ? 244  ILE   A N     1 
ATOM   1695  C  CA    . ILE   A 1  246  ? -49.898 64.667  65.199  1.00 16.22 ? 244  ILE   A CA    1 
ATOM   1696  C  C     . ILE   A 1  246  ? -50.554 64.818  63.834  1.00 16.64 ? 244  ILE   A C     1 
ATOM   1697  O  O     . ILE   A 1  246  ? -51.330 63.957  63.409  1.00 16.12 ? 244  ILE   A O     1 
ATOM   1698  C  CB    . ILE   A 1  246  ? -50.616 65.480  66.282  1.00 15.54 ? 244  ILE   A CB    1 
ATOM   1699  C  CG1   . ILE   A 1  246  ? -50.166 64.996  67.657  1.00 16.19 ? 244  ILE   A CG1   1 
ATOM   1700  C  CG2   . ILE   A 1  246  ? -52.126 65.327  66.136  1.00 16.36 ? 244  ILE   A CG2   1 
ATOM   1701  C  CD1   . ILE   A 1  246  ? -50.566 65.927  68.786  1.00 16.59 ? 244  ILE   A CD1   1 
ATOM   1702  N  N     . HIS   A 1  247  ? -50.240 65.899  63.116  1.00 15.59 ? 245  HIS   A N     1 
ATOM   1703  C  CA    . HIS   A 1  247  ? -50.810 66.053  61.778  1.00 16.00 ? 245  HIS   A CA    1 
ATOM   1704  C  C     . HIS   A 1  247  ? -50.394 64.907  60.875  1.00 16.86 ? 245  HIS   A C     1 
ATOM   1705  O  O     . HIS   A 1  247  ? -51.229 64.324  60.178  1.00 17.52 ? 245  HIS   A O     1 
ATOM   1706  C  CB    . HIS   A 1  247  ? -50.396 67.386  61.160  1.00 16.47 ? 245  HIS   A CB    1 
ATOM   1707  C  CG    . HIS   A 1  247  ? -51.117 68.556  61.729  1.00 18.66 ? 245  HIS   A CG    1 
ATOM   1708  N  ND1   . HIS   A 1  247  ? -52.475 68.732  61.591  1.00 19.51 ? 245  HIS   A ND1   1 
ATOM   1709  C  CD2   . HIS   A 1  247  ? -50.664 69.626  62.425  1.00 20.87 ? 245  HIS   A CD2   1 
ATOM   1710  C  CE1   . HIS   A 1  247  ? -52.833 69.854  62.188  1.00 21.90 ? 245  HIS   A CE1   1 
ATOM   1711  N  NE2   . HIS   A 1  247  ? -51.754 70.409  62.709  1.00 20.07 ? 245  HIS   A NE2   1 
ATOM   1712  N  N     . ALA   A 1  248  ? -49.107 64.564  60.876  1.00 16.74 ? 246  ALA   A N     1 
ATOM   1713  C  CA    . ALA   A 1  248  ? -48.646 63.499  59.995  1.00 16.62 ? 246  ALA   A CA    1 
ATOM   1714  C  C     . ALA   A 1  248  ? -49.253 62.168  60.396  1.00 17.04 ? 246  ALA   A C     1 
ATOM   1715  O  O     . ALA   A 1  248  ? -49.714 61.409  59.543  1.00 17.05 ? 246  ALA   A O     1 
ATOM   1716  C  CB    . ALA   A 1  248  ? -47.117 63.438  59.996  1.00 18.07 ? 246  ALA   A CB    1 
ATOM   1717  N  N     . ILE   A 1  249  ? -49.287 61.881  61.697  1.00 16.19 ? 247  ILE   A N     1 
ATOM   1718  C  CA    . ILE   A 1  249  ? -49.861 60.629  62.174  1.00 14.23 ? 247  ILE   A CA    1 
ATOM   1719  C  C     . ILE   A 1  249  ? -51.354 60.587  61.892  1.00 16.48 ? 247  ILE   A C     1 
ATOM   1720  O  O     . ILE   A 1  249  ? -51.893 59.555  61.475  1.00 17.91 ? 247  ILE   A O     1 
ATOM   1721  C  CB    . ILE   A 1  249  ? -49.574 60.475  63.677  1.00 15.53 ? 247  ILE   A CB    1 
ATOM   1722  C  CG1   . ILE   A 1  249  ? -48.071 60.353  63.926  1.00 16.22 ? 247  ILE   A CG1   1 
ATOM   1723  C  CG2   . ILE   A 1  249  ? -50.310 59.266  64.252  1.00 17.10 ? 247  ILE   A CG2   1 
ATOM   1724  C  CD1   . ILE   A 1  249  ? -47.677 60.636  65.375  1.00 17.41 ? 247  ILE   A CD1   1 
ATOM   1725  N  N     . GLY   A 1  250  ? -52.048 61.697  62.136  1.00 15.40 ? 248  GLY   A N     1 
ATOM   1726  C  CA    . GLY   A 1  250  ? -53.474 61.730  61.886  1.00 16.91 ? 248  GLY   A CA    1 
ATOM   1727  C  C     . GLY   A 1  250  ? -53.811 61.608  60.416  1.00 16.79 ? 248  GLY   A C     1 
ATOM   1728  O  O     . GLY   A 1  250  ? -54.790 60.954  60.057  1.00 17.71 ? 248  GLY   A O     1 
ATOM   1729  N  N     . LYS   A 1  251  ? -53.026 62.253  59.549  1.00 17.11 ? 249  LYS   A N     1 
ATOM   1730  C  CA    . LYS   A 1  251  ? -53.247 62.086  58.116  1.00 16.90 ? 249  LYS   A CA    1 
ATOM   1731  C  C     . LYS   A 1  251  ? -53.064 60.635  57.712  1.00 18.97 ? 249  LYS   A C     1 
ATOM   1732  O  O     . LYS   A 1  251  ? -53.820 60.116  56.882  1.00 19.96 ? 249  LYS   A O     1 
ATOM   1733  C  CB    . LYS   A 1  251  ? -52.264 62.943  57.327  1.00 19.37 ? 249  LYS   A CB    1 
ATOM   1734  C  CG    . LYS   A 1  251  ? -52.527 64.429  57.366  1.00 19.60 ? 249  LYS   A CG    1 
ATOM   1735  C  CD    . LYS   A 1  251  ? -51.296 65.118  56.809  1.00 21.05 ? 249  LYS   A CD    1 
ATOM   1736  C  CE    . LYS   A 1  251  ? -51.414 66.625  56.818  1.00 21.65 ? 249  LYS   A CE    1 
ATOM   1737  N  NZ    . LYS   A 1  251  ? -50.154 67.215  56.251  1.00 20.80 ? 249  LYS   A NZ    1 
ATOM   1738  N  N     . ALA   A 1  252  ? -52.047 59.976  58.285  1.00 18.13 ? 250  ALA   A N     1 
ATOM   1739  C  CA    . ALA   A 1  252  ? -51.751 58.585  57.957  1.00 16.98 ? 250  ALA   A CA    1 
ATOM   1740  C  C     . ALA   A 1  252  ? -52.766 57.646  58.568  1.00 19.21 ? 250  ALA   A C     1 
ATOM   1741  O  O     . ALA   A 1  252  ? -53.113 56.626  57.963  1.00 20.65 ? 250  ALA   A O     1 
ATOM   1742  C  CB    . ALA   A 1  252  ? -50.361 58.201  58.458  1.00 20.04 ? 250  ALA   A CB    1 
ATOM   1743  N  N     . SER   A 1  253  ? -53.233 57.963  59.776  1.00 18.91 ? 251  SER   A N     1 
ATOM   1744  C  CA    . SER   A 1  253  ? -54.225 57.112  60.409  1.00 18.60 ? 251  SER   A CA    1 
ATOM   1745  C  C     . SER   A 1  253  ? -55.438 56.964  59.515  1.00 20.57 ? 251  SER   A C     1 
ATOM   1746  O  O     . SER   A 1  253  ? -55.980 55.864  59.371  1.00 20.29 ? 251  SER   A O     1 
ATOM   1747  C  CB    . SER   A 1  253  ? -54.633 57.713  61.744  1.00 18.02 ? 251  SER   A CB    1 
ATOM   1748  O  OG    . SER   A 1  253  ? -55.615 56.903  62.331  1.00 19.31 ? 251  SER   A OG    1 
ATOM   1749  N  N     . ALA   A 1  254  ? -55.855 58.064  58.892  1.00 19.67 ? 252  ALA   A N     1 
ATOM   1750  C  CA    . ALA   A 1  254  ? -56.927 58.068  57.898  1.00 21.45 ? 252  ALA   A CA    1 
ATOM   1751  C  C     . ALA   A 1  254  ? -58.178 57.369  58.418  1.00 22.38 ? 252  ALA   A C     1 
ATOM   1752  O  O     . ALA   A 1  254  ? -58.774 56.517  57.755  1.00 22.84 ? 252  ALA   A O     1 
ATOM   1753  C  CB    . ALA   A 1  254  ? -56.457 57.489  56.561  1.00 24.57 ? 252  ALA   A CB    1 
ATOM   1754  N  N     . GLY   A 1  255  ? -58.562 57.718  59.640  1.00 20.44 ? 253  GLY   A N     1 
ATOM   1755  C  CA    . GLY   A 1  255  ? -59.799 57.215  60.194  1.00 22.47 ? 253  GLY   A CA    1 
ATOM   1756  C  C     . GLY   A 1  255  ? -59.742 55.819  60.768  1.00 20.04 ? 253  GLY   A C     1 
ATOM   1757  O  O     . GLY   A 1  255  ? -60.792 55.265  61.097  1.00 23.95 ? 253  GLY   A O     1 
ATOM   1758  N  N     . ARG   A 1  256  ? -58.552 55.232  60.924  1.00 20.92 ? 254  ARG   A N     1 
ATOM   1759  C  CA    . ARG   A 1  256  ? -58.469 53.905  61.520  1.00 20.02 ? 254  ARG   A CA    1 
ATOM   1760  C  C     . ARG   A 1  256  ? -58.841 53.899  62.993  1.00 20.71 ? 254  ARG   A C     1 
ATOM   1761  O  O     . ARG   A 1  256  ? -59.122 52.829  63.539  1.00 21.79 ? 254  ARG   A O     1 
ATOM   1762  C  CB    . ARG   A 1  256  ? -57.078 53.311  61.334  1.00 19.61 ? 254  ARG   A CB    1 
ATOM   1763  C  CG    . ARG   A 1  256  ? -56.891 52.700  59.960  1.00 22.39 ? 254  ARG   A CG    1 
ATOM   1764  C  CD    . ARG   A 1  256  ? -55.486 52.186  59.800  1.00 24.64 ? 254  ARG   A CD    1 
ATOM   1765  N  NE    . ARG   A 1  256  ? -54.543 53.281  59.628  1.00 21.97 ? 254  ARG   A NE    1 
ATOM   1766  C  CZ    . ARG   A 1  256  ? -53.227 53.127  59.614  1.00 25.40 ? 254  ARG   A CZ    1 
ATOM   1767  N  NH1   . ARG   A 1  256  ? -52.669 51.954  59.866  1.00 24.29 ? 254  ARG   A NH1   1 
ATOM   1768  N  NH2   . ARG   A 1  256  ? -52.452 54.171  59.333  1.00 23.06 ? 254  ARG   A NH2   1 
ATOM   1769  N  N     . GLY   A 1  257  ? -58.842 55.055  63.645  1.00 19.31 ? 255  GLY   A N     1 
ATOM   1770  C  CA    . GLY   A 1  257  ? -59.227 55.125  65.038  1.00 18.32 ? 255  GLY   A CA    1 
ATOM   1771  C  C     . GLY   A 1  257  ? -58.077 54.842  65.983  1.00 18.03 ? 255  GLY   A C     1 
ATOM   1772  O  O     . GLY   A 1  257  ? -56.940 54.568  65.596  1.00 18.82 ? 255  GLY   A O     1 
ATOM   1773  N  N     . ILE   A 1  258  ? -58.400 54.887  67.270  1.00 16.36 ? 256  ILE   A N     1 
ATOM   1774  C  CA    . ILE   A 1  258  ? -57.356 54.909  68.287  1.00 16.56 ? 256  ILE   A CA    1 
ATOM   1775  C  C     . ILE   A 1  258  ? -56.759 53.542  68.583  1.00 17.86 ? 256  ILE   A C     1 
ATOM   1776  O  O     . ILE   A 1  258  ? -55.677 53.471  69.174  1.00 18.71 ? 256  ILE   A O     1 
ATOM   1777  C  CB    . ILE   A 1  258  ? -57.862 55.569  69.575  1.00 16.98 ? 256  ILE   A CB    1 
ATOM   1778  C  CG1   . ILE   A 1  258  ? -58.999 54.743  70.183  1.00 19.31 ? 256  ILE   A CG1   1 
ATOM   1779  C  CG2   . ILE   A 1  258  ? -58.298 57.010  69.299  1.00 17.23 ? 256  ILE   A CG2   1 
ATOM   1780  C  CD1   . ILE   A 1  258  ? -59.543 55.338  71.467  1.00 19.52 ? 256  ILE   A CD1   1 
ATOM   1781  N  N     . TYR   A 1  259  ? -57.426 52.452  68.206  1.00 19.39 ? 257  TYR   A N     1 
ATOM   1782  C  CA    . TYR   A 1  259  ? -56.914 51.122  68.509  1.00 18.35 ? 257  TYR   A CA    1 
ATOM   1783  C  C     . TYR   A 1  259  ? -56.114 50.533  67.354  1.00 21.80 ? 257  TYR   A C     1 
ATOM   1784  O  O     . TYR   A 1  259  ? -54.968 50.114  67.542  1.00 23.71 ? 257  TYR   A O     1 
ATOM   1785  C  CB    . TYR   A 1  259  ? -58.056 50.191  68.939  1.00 19.88 ? 257  TYR   A CB    1 
ATOM   1786  C  CG    . TYR   A 1  259  ? -58.864 50.782  70.056  1.00 21.33 ? 257  TYR   A CG    1 
ATOM   1787  C  CD1   . TYR   A 1  259  ? -58.282 51.061  71.288  1.00 21.41 ? 257  TYR   A CD1   1 
ATOM   1788  C  CD2   . TYR   A 1  259  ? -60.206 51.097  69.882  1.00 21.61 ? 257  TYR   A CD2   1 
ATOM   1789  C  CE1   . TYR   A 1  259  ? -59.018 51.621  72.315  1.00 21.99 ? 257  TYR   A CE1   1 
ATOM   1790  C  CE2   . TYR   A 1  259  ? -60.944 51.666  70.904  1.00 22.17 ? 257  TYR   A CE2   1 
ATOM   1791  C  CZ    . TYR   A 1  259  ? -60.340 51.929  72.115  1.00 21.83 ? 257  TYR   A CZ    1 
ATOM   1792  O  OH    . TYR   A 1  259  ? -61.068 52.499  73.129  1.00 20.54 ? 257  TYR   A OH    1 
ATOM   1793  N  N     . GLU   A 1  260  ? -56.690 50.517  66.154  1.00 19.07 ? 258  GLU   A N     1 
ATOM   1794  C  CA    . GLU   A 1  260  ? -55.956 50.022  64.999  1.00 21.19 ? 258  GLU   A CA    1 
ATOM   1795  C  C     . GLU   A 1  260  ? -54.945 51.038  64.505  1.00 24.04 ? 258  GLU   A C     1 
ATOM   1796  O  O     . GLU   A 1  260  ? -53.864 50.664  64.028  1.00 26.56 ? 258  GLU   A O     1 
ATOM   1797  C  CB    . GLU   A 1  260  ? -56.920 49.705  63.852  1.00 24.76 ? 258  GLU   A CB    1 
ATOM   1798  C  CG    . GLU   A 1  260  ? -56.201 49.175  62.619  1.00 33.68 ? 258  GLU   A CG    1 
ATOM   1799  C  CD    . GLU   A 1  260  ? -57.091 49.026  61.399  1.00 39.54 ? 258  GLU   A CD    1 
ATOM   1800  O  OE1   . GLU   A 1  260  ? -58.332 49.040  61.543  1.00 39.91 ? 258  GLU   A OE1   1 
ATOM   1801  O  OE2   . GLU   A 1  260  ? -56.537 48.893  60.286  1.00 35.35 ? 258  GLU   A OE2   1 
ATOM   1802  N  N     . GLY   A 1  261  ? -55.267 52.318  64.623  1.00 19.10 ? 259  GLY   A N     1 
ATOM   1803  C  CA    . GLY   A 1  261  ? -54.455 53.345  64.037  1.00 19.73 ? 259  GLY   A CA    1 
ATOM   1804  C  C     . GLY   A 1  261  ? -53.369 53.826  64.969  1.00 19.05 ? 259  GLY   A C     1 
ATOM   1805  O  O     . GLY   A 1  261  ? -53.379 53.578  66.178  1.00 18.43 ? 259  GLY   A O     1 
ATOM   1806  N  N     . PRO   A 1  262  ? -52.406 54.534  64.402  1.00 17.00 ? 260  PRO   A N     1 
ATOM   1807  C  CA    . PRO   A 1  262  ? -51.261 55.000  65.184  1.00 18.18 ? 260  PRO   A CA    1 
ATOM   1808  C  C     . PRO   A 1  262  ? -51.644 56.152  66.092  1.00 17.03 ? 260  PRO   A C     1 
ATOM   1809  O  O     . PRO   A 1  262  ? -52.659 56.826  65.912  1.00 18.93 ? 260  PRO   A O     1 
ATOM   1810  C  CB    . PRO   A 1  262  ? -50.282 55.472  64.108  1.00 19.24 ? 260  PRO   A CB    1 
ATOM   1811  C  CG    . PRO   A 1  262  ? -51.182 55.886  62.971  1.00 19.49 ? 260  PRO   A CG    1 
ATOM   1812  C  CD    . PRO   A 1  262  ? -52.294 54.886  62.978  1.00 18.33 ? 260  PRO   A CD    1 
ATOM   1813  N  N     . GLY   A 1  263  ? -50.791 56.369  67.084  1.00 17.59 ? 261  GLY   A N     1 
ATOM   1814  C  CA    . GLY   A 1  263  ? -50.941 57.464  68.013  1.00 17.28 ? 261  GLY   A CA    1 
ATOM   1815  C  C     . GLY   A 1  263  ? -49.604 58.110  68.299  1.00 15.64 ? 261  GLY   A C     1 
ATOM   1816  O  O     . GLY   A 1  263  ? -48.597 57.784  67.656  1.00 16.38 ? 261  GLY   A O     1 
ATOM   1817  N  N     . ILE   A 1  264  ? -49.589 59.026  69.258  1.00 14.68 ? 262  ILE   A N     1 
ATOM   1818  C  CA    . ILE   A 1  264  ? -48.384 59.736  69.645  1.00 16.06 ? 262  ILE   A CA    1 
ATOM   1819  C  C     . ILE   A 1  264  ? -48.213 59.597  71.149  1.00 16.56 ? 262  ILE   A C     1 
ATOM   1820  O  O     . ILE   A 1  264  ? -49.188 59.435  71.890  1.00 16.43 ? 262  ILE   A O     1 
ATOM   1821  C  CB    . ILE   A 1  264  ? -48.450 61.218  69.209  1.00 15.15 ? 262  ILE   A CB    1 
ATOM   1822  C  CG1   . ILE   A 1  264  ? -47.067 61.851  69.265  1.00 18.71 ? 262  ILE   A CG1   1 
ATOM   1823  C  CG2   . ILE   A 1  264  ? -49.492 61.987  70.045  1.00 17.18 ? 262  ILE   A CG2   1 
ATOM   1824  C  CD1   . ILE   A 1  264  ? -47.030 63.259  68.715  1.00 18.60 ? 262  ILE   A CD1   1 
ATOM   1825  N  N     . SER   A 1  265  ? -46.964 59.627  71.593  1.00 15.10 ? 263  SER   A N     1 
ATOM   1826  C  CA    . SER   A 1  265  ? -46.637 59.711  73.007  1.00 15.07 ? 263  SER   A CA    1 
ATOM   1827  C  C     . SER   A 1  265  ? -45.900 61.015  73.254  1.00 18.41 ? 263  SER   A C     1 
ATOM   1828  O  O     . SER   A 1  265  ? -45.055 61.416  72.448  1.00 20.10 ? 263  SER   A O     1 
ATOM   1829  C  CB    . SER   A 1  265  ? -45.754 58.548  73.449  1.00 16.82 ? 263  SER   A CB    1 
ATOM   1830  O  OG    . SER   A 1  265  ? -46.487 57.334  73.472  1.00 19.89 ? 263  SER   A OG    1 
ATOM   1831  N  N     . ILE   A 1  266  ? -46.216 61.672  74.368  1.00 15.45 ? 264  ILE   A N     1 
ATOM   1832  C  CA    . ILE   A 1  266  ? -45.588 62.935  74.736  1.00 15.11 ? 264  ILE   A CA    1 
ATOM   1833  C  C     . ILE   A 1  266  ? -45.043 62.823  76.149  1.00 14.48 ? 264  ILE   A C     1 
ATOM   1834  O  O     . ILE   A 1  266  ? -45.500 62.009  76.954  1.00 16.48 ? 264  ILE   A O     1 
ATOM   1835  C  CB    . ILE   A 1  266  ? -46.547 64.140  74.638  1.00 16.90 ? 264  ILE   A CB    1 
ATOM   1836  C  CG1   . ILE   A 1  266  ? -47.680 64.036  75.659  1.00 17.23 ? 264  ILE   A CG1   1 
ATOM   1837  C  CG2   . ILE   A 1  266  ? -47.128 64.262  73.222  1.00 18.37 ? 264  ILE   A CG2   1 
ATOM   1838  C  CD1   . ILE   A 1  266  ? -48.525 65.323  75.751  1.00 17.48 ? 264  ILE   A CD1   1 
ATOM   1839  N  N     . LYS   A 1  267  ? -44.058 63.662  76.448  1.00 15.48 ? 265  LYS   A N     1 
ATOM   1840  C  CA    . LYS   A 1  267  ? -43.565 63.817  77.805  1.00 14.12 ? 265  LYS   A CA    1 
ATOM   1841  C  C     . LYS   A 1  267  ? -43.885 65.223  78.265  1.00 16.20 ? 265  LYS   A C     1 
ATOM   1842  O  O     . LYS   A 1  267  ? -43.555 66.191  77.581  1.00 16.42 ? 265  LYS   A O     1 
ATOM   1843  C  CB    . LYS   A 1  267  ? -42.052 63.607  77.853  1.00 17.08 ? 265  LYS   A CB    1 
ATOM   1844  C  CG    . LYS   A 1  267  ? -41.670 62.143  77.771  1.00 19.30 ? 265  LYS   A CG    1 
ATOM   1845  C  CD    . LYS   A 1  267  ? -40.155 61.983  77.857  1.00 23.75 ? 265  LYS   A CD    1 
ATOM   1846  C  CE    . LYS   A 1  267  ? -39.774 60.525  78.026  1.00 30.70 ? 265  LYS   A CE    1 
ATOM   1847  N  NZ    . LYS   A 1  267  ? -40.350 59.671  76.952  1.00 33.85 ? 265  LYS   A NZ    1 
ATOM   1848  N  N     . LEU   A 1  268  ? -44.546 65.337  79.417  1.00 14.69 ? 266  LEU   A N     1 
ATOM   1849  C  CA    . LEU   A 1  268  ? -44.889 66.661  79.918  1.00 14.70 ? 266  LEU   A CA    1 
ATOM   1850  C  C     . LEU   A 1  268  ? -43.653 67.511  80.150  1.00 15.49 ? 266  LEU   A C     1 
ATOM   1851  O  O     . LEU   A 1  268  ? -43.701 68.729  79.965  1.00 16.51 ? 266  LEU   A O     1 
ATOM   1852  C  CB    . LEU   A 1  268  ? -45.726 66.556  81.192  1.00 15.51 ? 266  LEU   A CB    1 
ATOM   1853  C  CG    . LEU   A 1  268  ? -47.057 65.838  80.974  1.00 16.99 ? 266  LEU   A CG    1 
ATOM   1854  C  CD1   . LEU   A 1  268  ? -47.849 65.760  82.259  1.00 17.72 ? 266  LEU   A CD1   1 
ATOM   1855  C  CD2   . LEU   A 1  268  ? -47.841 66.550  79.890  1.00 19.54 ? 266  LEU   A CD2   1 
ATOM   1856  N  N     . SER   A 1  269  ? -42.537 66.893  80.529  1.00 15.08 ? 267  SER   A N     1 
ATOM   1857  C  CA    . SER   A 1  269  ? -41.334 67.674  80.778  1.00 17.48 ? 267  SER   A CA    1 
ATOM   1858  C  C     . SER   A 1  269  ? -40.803 68.325  79.516  1.00 17.81 ? 267  SER   A C     1 
ATOM   1859  O  O     . SER   A 1  269  ? -40.014 69.264  79.610  1.00 17.83 ? 267  SER   A O     1 
ATOM   1860  C  CB    . SER   A 1  269  ? -40.234 66.808  81.379  1.00 16.76 ? 267  SER   A CB    1 
ATOM   1861  O  OG    . SER   A 1  269  ? -39.718 65.909  80.426  1.00 17.61 ? 267  SER   A OG    1 
ATOM   1862  N  N     . ALA   A 1  270  ? -41.202 67.836  78.338  1.00 14.68 ? 268  ALA   A N     1 
ATOM   1863  C  CA    . ALA   A 1  270  ? -40.793 68.491  77.104  1.00 15.70 ? 268  ALA   A CA    1 
ATOM   1864  C  C     . ALA   A 1  270  ? -41.559 69.778  76.859  1.00 15.27 ? 268  ALA   A C     1 
ATOM   1865  O  O     . ALA   A 1  270  ? -41.118 70.610  76.062  1.00 17.01 ? 268  ALA   A O     1 
ATOM   1866  C  CB    . ALA   A 1  270  ? -41.043 67.559  75.919  1.00 17.50 ? 268  ALA   A CB    1 
ATOM   1867  N  N     . LEU   A 1  271  ? -42.709 69.955  77.499  1.00 15.19 ? 269  LEU   A N     1 
ATOM   1868  C  CA    . LEU   A 1  271  ? -43.603 71.037  77.132  1.00 15.78 ? 269  LEU   A CA    1 
ATOM   1869  C  C     . LEU   A 1  271  ? -43.544 72.214  78.085  1.00 15.20 ? 269  LEU   A C     1 
ATOM   1870  O  O     . LEU   A 1  271  ? -44.251 73.200  77.876  1.00 16.90 ? 269  LEU   A O     1 
ATOM   1871  C  CB    . LEU   A 1  271  ? -45.028 70.511  77.020  1.00 17.09 ? 269  LEU   A CB    1 
ATOM   1872  C  CG    . LEU   A 1  271  ? -45.173 69.547  75.852  1.00 17.92 ? 269  LEU   A CG    1 
ATOM   1873  C  CD1   . LEU   A 1  271  ? -46.531 68.880  75.926  1.00 21.57 ? 269  LEU   A CD1   1 
ATOM   1874  C  CD2   . LEU   A 1  271  ? -45.071 70.349  74.577  1.00 19.29 ? 269  LEU   A CD2   1 
ATOM   1875  N  N     . HIS   A 1  272  ? -42.716 72.137  79.124  1.00 17.87 ? 270  HIS   A N     1 
ATOM   1876  C  CA    . HIS   A 1  272  ? -42.570 73.299  79.973  1.00 16.40 ? 270  HIS   A CA    1 
ATOM   1877  C  C     . HIS   A 1  272  ? -41.228 73.184  80.659  1.00 16.24 ? 270  HIS   A C     1 
ATOM   1878  O  O     . HIS   A 1  272  ? -40.884 72.093  81.122  1.00 17.32 ? 270  HIS   A O     1 
ATOM   1879  C  CB    . HIS   A 1  272  ? -43.677 73.360  81.027  1.00 18.44 ? 270  HIS   A CB    1 
ATOM   1880  C  CG    . HIS   A 1  272  ? -43.819 74.708  81.645  1.00 19.64 ? 270  HIS   A CG    1 
ATOM   1881  N  ND1   . HIS   A 1  272  ? -42.907 75.217  82.547  1.00 21.08 ? 270  HIS   A ND1   1 
ATOM   1882  C  CD2   . HIS   A 1  272  ? -44.753 75.670  81.465  1.00 20.91 ? 270  HIS   A CD2   1 
ATOM   1883  C  CE1   . HIS   A 1  272  ? -43.276 76.437  82.894  1.00 22.89 ? 270  HIS   A CE1   1 
ATOM   1884  N  NE2   . HIS   A 1  272  ? -44.392 76.736  82.252  1.00 23.89 ? 270  HIS   A NE2   1 
ATOM   1885  N  N     . PRO   A 1  273  ? -40.447 74.266  80.740  1.00 17.46 ? 271  PRO   A N     1 
ATOM   1886  C  CA    . PRO   A 1  273  ? -39.130 74.171  81.374  1.00 16.94 ? 271  PRO   A CA    1 
ATOM   1887  C  C     . PRO   A 1  273  ? -39.182 74.085  82.883  1.00 17.30 ? 271  PRO   A C     1 
ATOM   1888  O  O     . PRO   A 1  273  ? -38.144 73.804  83.495  1.00 19.21 ? 271  PRO   A O     1 
ATOM   1889  C  CB    . PRO   A 1  273  ? -38.436 75.462  80.927  1.00 17.93 ? 271  PRO   A CB    1 
ATOM   1890  C  CG    . PRO   A 1  273  ? -39.545 76.424  80.781  1.00 18.17 ? 271  PRO   A CG    1 
ATOM   1891  C  CD    . PRO   A 1  273  ? -40.704 75.617  80.215  1.00 19.61 ? 271  PRO   A CD    1 
ATOM   1892  N  N     . ARG   A 1  274  ? -40.334 74.320  83.508  1.00 16.30 ? 272  ARG   A N     1 
ATOM   1893  C  CA    . ARG   A 1  274  ? -40.420 74.195  84.957  1.00 17.01 ? 272  ARG   A CA    1 
ATOM   1894  C  C     . ARG   A 1  274  ? -41.533 73.235  85.341  1.00 16.75 ? 272  ARG   A C     1 
ATOM   1895  O  O     . ARG   A 1  274  ? -42.435 73.578  86.113  1.00 18.92 ? 272  ARG   A O     1 
ATOM   1896  C  CB    . ARG   A 1  274  ? -40.645 75.560  85.608  1.00 17.80 ? 272  ARG   A CB    1 
ATOM   1897  C  CG    . ARG   A 1  274  ? -39.512 76.556  85.355  1.00 17.23 ? 272  ARG   A CG    1 
ATOM   1898  C  CD    . ARG   A 1  274  ? -38.166 76.048  85.902  1.00 17.91 ? 272  ARG   A CD    1 
ATOM   1899  N  NE    . ARG   A 1  274  ? -38.225 75.644  87.304  1.00 19.04 ? 272  ARG   A NE    1 
ATOM   1900  C  CZ    . ARG   A 1  274  ? -38.197 76.494  88.325  1.00 18.57 ? 272  ARG   A CZ    1 
ATOM   1901  N  NH1   . ARG   A 1  274  ? -38.152 77.802  88.132  1.00 19.34 ? 272  ARG   A NH1   1 
ATOM   1902  N  NH2   . ARG   A 1  274  ? -38.236 76.021  89.567  1.00 20.40 ? 272  ARG   A NH2   1 
ATOM   1903  N  N     . TYR   A 1  275  ? -41.469 72.024  84.805  1.00 16.27 ? 273  TYR   A N     1 
ATOM   1904  C  CA    . TYR   A 1  275  ? -42.484 71.018  85.081  1.00 15.24 ? 273  TYR   A CA    1 
ATOM   1905  C  C     . TYR   A 1  275  ? -42.113 70.360  86.406  1.00 16.49 ? 273  TYR   A C     1 
ATOM   1906  O  O     . TYR   A 1  275  ? -41.314 69.427  86.468  1.00 17.76 ? 273  TYR   A O     1 
ATOM   1907  C  CB    . TYR   A 1  275  ? -42.560 70.032  83.921  1.00 15.78 ? 273  TYR   A CB    1 
ATOM   1908  C  CG    . TYR   A 1  275  ? -43.502 68.907  84.200  1.00 15.80 ? 273  TYR   A CG    1 
ATOM   1909  C  CD1   . TYR   A 1  275  ? -44.795 69.159  84.611  1.00 16.10 ? 273  TYR   A CD1   1 
ATOM   1910  C  CD2   . TYR   A 1  275  ? -43.088 67.590  84.074  1.00 15.35 ? 273  TYR   A CD2   1 
ATOM   1911  C  CE1   . TYR   A 1  275  ? -45.660 68.121  84.889  1.00 18.02 ? 273  TYR   A CE1   1 
ATOM   1912  C  CE2   . TYR   A 1  275  ? -43.942 66.549  84.348  1.00 16.18 ? 273  TYR   A CE2   1 
ATOM   1913  C  CZ    . TYR   A 1  275  ? -45.220 66.822  84.760  1.00 16.82 ? 273  TYR   A CZ    1 
ATOM   1914  O  OH    . TYR   A 1  275  ? -46.065 65.776  85.033  1.00 18.37 ? 273  TYR   A OH    1 
ATOM   1915  N  N     . SER   A 1  276  ? -42.682 70.879  87.489  1.00 15.99 ? 274  SER   A N     1 
ATOM   1916  C  CA    . SER   A 1  276  ? -42.376 70.366  88.815  1.00 15.04 ? 274  SER   A CA    1 
ATOM   1917  C  C     . SER   A 1  276  ? -43.481 70.803  89.754  1.00 16.47 ? 274  SER   A C     1 
ATOM   1918  O  O     . SER   A 1  276  ? -44.185 71.781  89.499  1.00 16.77 ? 274  SER   A O     1 
ATOM   1919  C  CB    . SER   A 1  276  ? -41.046 70.914  89.325  1.00 20.20 ? 274  SER   A CB    1 
ATOM   1920  O  OG    . SER   A 1  276  ? -41.175 72.287  89.639  1.00 23.59 ? 274  SER   A OG    1 
ATOM   1921  N  N     . ARG   A 1  277  ? -43.620 70.055  90.851  1.00 15.72 ? 275  ARG   A N     1 
ATOM   1922  C  CA    . ARG   A 1  277  ? -44.609 70.404  91.863  1.00 16.62 ? 275  ARG   A CA    1 
ATOM   1923  C  C     . ARG   A 1  277  ? -44.355 71.790  92.434  1.00 16.78 ? 275  ARG   A C     1 
ATOM   1924  O  O     . ARG   A 1  277  ? -45.305 72.514  92.730  1.00 17.00 ? 275  ARG   A O     1 
ATOM   1925  C  CB    . ARG   A 1  277  ? -44.618 69.351  92.977  1.00 16.53 ? 275  ARG   A CB    1 
ATOM   1926  C  CG    . ARG   A 1  277  ? -45.458 69.719  94.198  1.00 17.95 ? 275  ARG   A CG    1 
ATOM   1927  C  CD    . ARG   A 1  277  ? -46.943 69.893  93.844  1.00 18.16 ? 275  ARG   A CD    1 
ATOM   1928  N  NE    . ARG   A 1  277  ? -47.753 70.218  95.012  1.00 18.27 ? 275  ARG   A NE    1 
ATOM   1929  C  CZ    . ARG   A 1  277  ? -47.927 71.449  95.470  1.00 16.71 ? 275  ARG   A CZ    1 
ATOM   1930  N  NH1   . ARG   A 1  277  ? -47.278 72.479  94.951  1.00 17.87 ? 275  ARG   A NH1   1 
ATOM   1931  N  NH2   . ARG   A 1  277  ? -48.775 71.655  96.478  1.00 18.53 ? 275  ARG   A NH2   1 
ATOM   1932  N  N     . ALA   A 1  278  ? -43.088 72.191  92.570  1.00 17.07 ? 276  ALA   A N     1 
ATOM   1933  C  CA    . ALA   A 1  278  ? -42.806 73.521  93.104  1.00 19.13 ? 276  ALA   A CA    1 
ATOM   1934  C  C     . ALA   A 1  278  ? -43.398 74.611  92.232  1.00 17.95 ? 276  ALA   A C     1 
ATOM   1935  O  O     . ALA   A 1  278  ? -43.680 75.710  92.716  1.00 19.73 ? 276  ALA   A O     1 
ATOM   1936  C  CB    . ALA   A 1  278  ? -41.299 73.736  93.230  1.00 20.02 ? 276  ALA   A CB    1 
ATOM   1937  N  N     . GLN   A 1  279  ? -43.565 74.336  90.944  1.00 16.63 ? 277  GLN   A N     1 
ATOM   1938  C  CA    . GLN   A 1  279  ? -44.098 75.296  89.991  1.00 16.76 ? 277  GLN   A CA    1 
ATOM   1939  C  C     . GLN   A 1  279  ? -45.472 74.872  89.494  1.00 18.10 ? 277  GLN   A C     1 
ATOM   1940  O  O     . GLN   A 1  279  ? -45.834 75.153  88.353  1.00 18.03 ? 277  GLN   A O     1 
ATOM   1941  C  CB    . GLN   A 1  279  ? -43.133 75.452  88.817  1.00 18.70 ? 277  GLN   A CB    1 
ATOM   1942  C  CG    . GLN   A 1  279  ? -41.746 75.936  89.225  1.00 19.33 ? 277  GLN   A CG    1 
ATOM   1943  C  CD    . GLN   A 1  279  ? -41.802 77.314  89.834  1.00 21.85 ? 277  GLN   A CD    1 
ATOM   1944  O  OE1   . GLN   A 1  279  ? -42.614 78.153  89.437  1.00 28.53 ? 277  GLN   A OE1   1 
ATOM   1945  N  NE2   . GLN   A 1  279  ? -40.983 77.543  90.843  1.00 21.05 ? 277  GLN   A NE2   1 
ATOM   1946  N  N     . ALA   A 1  280  ? -46.249 74.208  90.351  1.00 17.72 ? 278  ALA   A N     1 
ATOM   1947  C  CA    . ALA   A 1  280  ? -47.520 73.638  89.904  1.00 16.41 ? 278  ALA   A CA    1 
ATOM   1948  C  C     . ALA   A 1  280  ? -48.441 74.687  89.307  1.00 18.04 ? 278  ALA   A C     1 
ATOM   1949  O  O     . ALA   A 1  280  ? -49.154 74.405  88.342  1.00 17.52 ? 278  ALA   A O     1 
ATOM   1950  C  CB    . ALA   A 1  280  ? -48.217 72.926  91.061  1.00 19.10 ? 278  ALA   A CB    1 
ATOM   1951  N  N     . ALA   A 1  281  ? -48.465 75.893  89.870  1.00 17.39 ? 279  ALA   A N     1 
ATOM   1952  C  CA    . ALA   A 1  281  ? -49.344 76.918  89.314  1.00 17.68 ? 279  ALA   A CA    1 
ATOM   1953  C  C     . ALA   A 1  281  ? -48.959 77.250  87.878  1.00 19.04 ? 279  ALA   A C     1 
ATOM   1954  O  O     . ALA   A 1  281  ? -49.830 77.404  87.009  1.00 19.81 ? 279  ALA   A O     1 
ATOM   1955  C  CB    . ALA   A 1  281  ? -49.344 78.175  90.189  1.00 20.71 ? 279  ALA   A CB    1 
ATOM   1956  N  N     . ARG   A 1  282  ? -47.658 77.347  87.599  1.00 17.06 ? 280  ARG   A N     1 
ATOM   1957  C  CA    . ARG   A 1  282  ? -47.251 77.603  86.222  1.00 17.02 ? 280  ARG   A CA    1 
ATOM   1958  C  C     . ARG   A 1  282  ? -47.558 76.407  85.338  1.00 18.47 ? 280  ARG   A C     1 
ATOM   1959  O  O     . ARG   A 1  282  ? -47.922 76.570  84.168  1.00 17.90 ? 280  ARG   A O     1 
ATOM   1960  C  CB    . ARG   A 1  282  ? -45.758 77.934  86.151  1.00 18.55 ? 280  ARG   A CB    1 
ATOM   1961  C  CG    . ARG   A 1  282  ? -45.374 79.287  86.716  1.00 19.91 ? 280  ARG   A CG    1 
ATOM   1962  C  CD    . ARG   A 1  282  ? -43.925 79.603  86.341  1.00 21.15 ? 280  ARG   A CD    1 
ATOM   1963  N  NE    . ARG   A 1  282  ? -43.817 79.734  84.894  1.00 19.87 ? 280  ARG   A NE    1 
ATOM   1964  C  CZ    . ARG   A 1  282  ? -42.681 79.689  84.216  1.00 20.14 ? 280  ARG   A CZ    1 
ATOM   1965  N  NH1   . ARG   A 1  282  ? -41.513 79.524  84.827  1.00 20.18 ? 280  ARG   A NH1   1 
ATOM   1966  N  NH2   . ARG   A 1  282  ? -42.716 79.815  82.892  1.00 22.87 ? 280  ARG   A NH2   1 
ATOM   1967  N  N     . VAL   A 1  283  ? -47.410 75.197  85.877  1.00 17.00 ? 281  VAL   A N     1 
ATOM   1968  C  CA    . VAL   A 1  283  ? -47.733 74.000  85.114  1.00 16.04 ? 281  VAL   A CA    1 
ATOM   1969  C  C     . VAL   A 1  283  ? -49.202 74.007  84.706  1.00 16.63 ? 281  VAL   A C     1 
ATOM   1970  O  O     . VAL   A 1  283  ? -49.542 73.779  83.540  1.00 17.32 ? 281  VAL   A O     1 
ATOM   1971  C  CB    . VAL   A 1  283  ? -47.370 72.748  85.927  1.00 15.30 ? 281  VAL   A CB    1 
ATOM   1972  C  CG1   . VAL   A 1  283  ? -47.932 71.505  85.261  1.00 20.17 ? 281  VAL   A CG1   1 
ATOM   1973  C  CG2   . VAL   A 1  283  ? -45.861 72.658  86.055  1.00 17.98 ? 281  VAL   A CG2   1 
ATOM   1974  N  N     . MET   A 1  284  ? -50.096 74.278  85.653  1.00 16.44 ? 282  MET   A N     1 
ATOM   1975  C  CA    . MET   A 1  284  ? -51.512 74.255  85.314  1.00 16.70 ? 282  MET   A CA    1 
ATOM   1976  C  C     . MET   A 1  284  ? -51.886 75.425  84.425  1.00 18.66 ? 282  MET   A C     1 
ATOM   1977  O  O     . MET   A 1  284  ? -52.779 75.300  83.580  1.00 21.00 ? 282  MET   A O     1 
ATOM   1978  C  CB    . MET   A 1  284  ? -52.350 74.251  86.589  1.00 17.90 ? 282  MET   A CB    1 
ATOM   1979  C  CG    . MET   A 1  284  ? -52.028 73.077  87.493  1.00 19.91 ? 282  MET   A CG    1 
ATOM   1980  S  SD    . MET   A 1  284  ? -52.300 71.468  86.730  1.00 22.10 ? 282  MET   A SD    1 
ATOM   1981  C  CE    . MET   A 1  284  ? -54.050 71.558  86.389  1.00 21.58 ? 282  MET   A CE    1 
ATOM   1982  N  N     . GLY   A 1  285  ? -51.212 76.563  84.587  1.00 18.10 ? 283  GLY   A N     1 
ATOM   1983  C  CA    . GLY   A 1  285  ? -51.570 77.729  83.804  1.00 18.59 ? 283  GLY   A CA    1 
ATOM   1984  C  C     . GLY   A 1  285  ? -50.987 77.723  82.410  1.00 19.40 ? 283  GLY   A C     1 
ATOM   1985  O  O     . GLY   A 1  285  ? -51.601 78.252  81.479  1.00 21.69 ? 283  GLY   A O     1 
ATOM   1986  N  N     . GLU   A 1  286  ? -49.815 77.129  82.238  1.00 17.67 ? 284  GLU   A N     1 
ATOM   1987  C  CA    . GLU   A 1  286  ? -49.057 77.260  81.000  1.00 16.80 ? 284  GLU   A CA    1 
ATOM   1988  C  C     . GLU   A 1  286  ? -48.850 75.944  80.281  1.00 19.13 ? 284  GLU   A C     1 
ATOM   1989  O  O     . GLU   A 1  286  ? -48.866 75.909  79.050  1.00 21.62 ? 284  GLU   A O     1 
ATOM   1990  C  CB    . GLU   A 1  286  ? -47.679 77.863  81.292  1.00 17.93 ? 284  GLU   A CB    1 
ATOM   1991  C  CG    . GLU   A 1  286  ? -47.744 79.201  81.984  1.00 20.81 ? 284  GLU   A CG    1 
ATOM   1992  C  CD    . GLU   A 1  286  ? -46.397 79.647  82.513  1.00 21.88 ? 284  GLU   A CD    1 
ATOM   1993  O  OE1   . GLU   A 1  286  ? -45.372 79.261  81.923  1.00 23.25 ? 284  GLU   A OE1   1 
ATOM   1994  O  OE2   . GLU   A 1  286  ? -46.373 80.393  83.515  1.00 25.09 ? 284  GLU   A OE2   1 
ATOM   1995  N  N     . LEU   A 1  287  ? -48.610 74.864  81.011  1.00 15.90 ? 285  LEU   A N     1 
ATOM   1996  C  CA    A LEU   A 1  287  ? -48.404 73.572  80.372  0.55 16.85 ? 285  LEU   A CA    1 
ATOM   1997  C  CA    B LEU   A 1  287  ? -48.407 73.575  80.371  0.45 16.87 ? 285  LEU   A CA    1 
ATOM   1998  C  C     . LEU   A 1  287  ? -49.737 72.956  79.971  1.00 18.48 ? 285  LEU   A C     1 
ATOM   1999  O  O     . LEU   A 1  287  ? -49.889 72.470  78.848  1.00 18.35 ? 285  LEU   A O     1 
ATOM   2000  C  CB    A LEU   A 1  287  ? -47.624 72.643  81.315  0.55 16.66 ? 285  LEU   A CB    1 
ATOM   2001  C  CB    B LEU   A 1  287  ? -47.636 72.646  81.310  0.45 16.68 ? 285  LEU   A CB    1 
ATOM   2002  C  CG    A LEU   A 1  287  ? -46.742 71.520  80.746  0.55 17.65 ? 285  LEU   A CG    1 
ATOM   2003  C  CG    B LEU   A 1  287  ? -47.645 71.165  80.940  0.45 18.17 ? 285  LEU   A CG    1 
ATOM   2004  C  CD1   A LEU   A 1  287  ? -45.962 70.809  81.839  0.55 17.50 ? 285  LEU   A CD1   1 
ATOM   2005  C  CD1   B LEU   A 1  287  ? -47.136 70.990  79.539  0.45 22.15 ? 285  LEU   A CD1   1 
ATOM   2006  C  CD2   A LEU   A 1  287  ? -47.554 70.511  79.980  0.55 21.56 ? 285  LEU   A CD2   1 
ATOM   2007  C  CD2   B LEU   A 1  287  ? -46.798 70.372  81.915  0.45 17.68 ? 285  LEU   A CD2   1 
ATOM   2008  N  N     . LEU   A 1  288  ? -50.708 72.971  80.879  1.00 17.28 ? 286  LEU   A N     1 
ATOM   2009  C  CA    . LEU   A 1  288  ? -52.012 72.377  80.600  1.00 17.07 ? 286  LEU   A CA    1 
ATOM   2010  C  C     . LEU   A 1  288  ? -52.625 72.850  79.287  1.00 17.71 ? 286  LEU   A C     1 
ATOM   2011  O  O     . LEU   A 1  288  ? -53.032 71.994  78.486  1.00 18.13 ? 286  LEU   A O     1 
ATOM   2012  C  CB    . LEU   A 1  288  ? -52.944 72.585  81.799  1.00 20.07 ? 286  LEU   A CB    1 
ATOM   2013  C  CG    . LEU   A 1  288  ? -54.393 72.164  81.568  1.00 25.93 ? 286  LEU   A CG    1 
ATOM   2014  C  CD1   . LEU   A 1  288  ? -54.459 70.671  81.297  1.00 22.53 ? 286  LEU   A CD1   1 
ATOM   2015  C  CD2   . LEU   A 1  288  ? -55.207 72.548  82.783  1.00 32.56 ? 286  LEU   A CD2   1 
ATOM   2016  N  N     . PRO   A 1  289  ? -52.710 74.153  78.989  1.00 17.65 ? 287  PRO   A N     1 
ATOM   2017  C  CA    . PRO   A 1  289  ? -53.294 74.559  77.700  1.00 19.21 ? 287  PRO   A CA    1 
ATOM   2018  C  C     . PRO   A 1  289  ? -52.559 74.003  76.507  1.00 19.59 ? 287  PRO   A C     1 
ATOM   2019  O  O     . PRO   A 1  289  ? -53.184 73.774  75.465  1.00 17.42 ? 287  PRO   A O     1 
ATOM   2020  C  CB    . PRO   A 1  289  ? -53.211 76.091  77.735  1.00 22.10 ? 287  PRO   A CB    1 
ATOM   2021  C  CG    . PRO   A 1  289  ? -53.151 76.435  79.174  1.00 25.99 ? 287  PRO   A CG    1 
ATOM   2022  C  CD    . PRO   A 1  289  ? -52.373 75.325  79.820  1.00 18.86 ? 287  PRO   A CD    1 
ATOM   2023  N  N     . ARG   A 1  290  ? -51.250 73.791  76.619  1.00 16.82 ? 288  ARG   A N     1 
ATOM   2024  C  CA    . ARG   A 1  290  ? -50.505 73.219  75.504  1.00 16.28 ? 288  ARG   A CA    1 
ATOM   2025  C  C     . ARG   A 1  290  ? -50.886 71.766  75.291  1.00 15.27 ? 288  ARG   A C     1 
ATOM   2026  O  O     . ARG   A 1  290  ? -51.072 71.327  74.151  1.00 16.55 ? 288  ARG   A O     1 
ATOM   2027  C  CB    . ARG   A 1  290  ? -49.003 73.355  75.737  1.00 18.44 ? 288  ARG   A CB    1 
ATOM   2028  C  CG    . ARG   A 1  290  ? -48.557 74.785  75.775  1.00 21.71 ? 288  ARG   A CG    1 
ATOM   2029  C  CD    . ARG   A 1  290  ? -47.126 74.898  76.257  1.00 26.31 ? 288  ARG   A CD    1 
ATOM   2030  N  NE    . ARG   A 1  290  ? -46.762 76.298  76.442  1.00 30.52 ? 288  ARG   A NE    1 
ATOM   2031  C  CZ    . ARG   A 1  290  ? -45.764 76.717  77.208  1.00 31.45 ? 288  ARG   A CZ    1 
ATOM   2032  N  NH1   . ARG   A 1  290  ? -45.003 75.868  77.878  1.00 24.35 ? 288  ARG   A NH1   1 
ATOM   2033  N  NH2   . ARG   A 1  290  ? -45.527 78.023  77.307  1.00 35.90 ? 288  ARG   A NH2   1 
ATOM   2034  N  N     . VAL   A 1  291  ? -50.993 70.999  76.374  1.00 15.46 ? 289  VAL   A N     1 
ATOM   2035  C  CA    . VAL   A 1  291  ? -51.433 69.618  76.232  1.00 15.18 ? 289  VAL   A CA    1 
ATOM   2036  C  C     . VAL   A 1  291  ? -52.839 69.575  75.671  1.00 15.79 ? 289  VAL   A C     1 
ATOM   2037  O  O     . VAL   A 1  291  ? -53.159 68.736  74.816  1.00 15.85 ? 289  VAL   A O     1 
ATOM   2038  C  CB    . VAL   A 1  291  ? -51.345 68.874  77.576  1.00 15.74 ? 289  VAL   A CB    1 
ATOM   2039  C  CG1   . VAL   A 1  291  ? -51.734 67.434  77.375  1.00 17.92 ? 289  VAL   A CG1   1 
ATOM   2040  C  CG2   . VAL   A 1  291  ? -49.946 68.950  78.093  1.00 19.45 ? 289  VAL   A CG2   1 
ATOM   2041  N  N     . LYS   A 1  292  ? -53.702 70.474  76.144  1.00 16.01 ? 290  LYS   A N     1 
ATOM   2042  C  CA    . LYS   A 1  292  ? -55.065 70.500  75.641  1.00 13.94 ? 290  LYS   A CA    1 
ATOM   2043  C  C     . LYS   A 1  292  ? -55.083 70.769  74.148  1.00 16.73 ? 290  LYS   A C     1 
ATOM   2044  O  O     . LYS   A 1  292  ? -55.839 70.138  73.402  1.00 15.00 ? 290  LYS   A O     1 
ATOM   2045  C  CB    . LYS   A 1  292  ? -55.892 71.548  76.371  1.00 16.04 ? 290  LYS   A CB    1 
ATOM   2046  C  CG    . LYS   A 1  292  ? -57.299 71.643  75.791  1.00 17.46 ? 290  LYS   A CG    1 
ATOM   2047  C  CD    . LYS   A 1  292  ? -58.168 72.648  76.496  1.00 19.05 ? 290  LYS   A CD    1 
ATOM   2048  C  CE    . LYS   A 1  292  ? -59.536 72.724  75.829  1.00 21.22 ? 290  LYS   A CE    1 
ATOM   2049  N  NZ    . LYS   A 1  292  ? -60.463 73.561  76.625  1.00 20.74 ? 290  LYS   A NZ    1 
ATOM   2050  N  N     . ALA   A 1  293  ? -54.262 71.712  73.691  1.00 15.96 ? 291  ALA   A N     1 
ATOM   2051  C  CA    . ALA   A 1  293  ? -54.245 72.015  72.267  1.00 16.02 ? 291  ALA   A CA    1 
ATOM   2052  C  C     . ALA   A 1  293  ? -53.792 70.807  71.453  1.00 14.69 ? 291  ALA   A C     1 
ATOM   2053  O  O     . ALA   A 1  293  ? -54.362 70.507  70.390  1.00 16.87 ? 291  ALA   A O     1 
ATOM   2054  C  CB    . ALA   A 1  293  ? -53.369 73.246  72.015  1.00 15.71 ? 291  ALA   A CB    1 
ATOM   2055  N  N     . LEU   A 1  294  ? -52.771 70.089  71.928  1.00 14.62 ? 292  LEU   A N     1 
ATOM   2056  C  CA    . LEU   A 1  294  ? -52.356 68.882  71.225  1.00 14.18 ? 292  LEU   A CA    1 
ATOM   2057  C  C     . LEU   A 1  294  ? -53.445 67.825  71.284  1.00 13.70 ? 292  LEU   A C     1 
ATOM   2058  O  O     . LEU   A 1  294  ? -53.686 67.114  70.300  1.00 15.14 ? 292  LEU   A O     1 
ATOM   2059  C  CB    . LEU   A 1  294  ? -51.069 68.328  71.828  1.00 15.89 ? 292  LEU   A CB    1 
ATOM   2060  C  CG    . LEU   A 1  294  ? -49.879 69.264  71.745  1.00 15.18 ? 292  LEU   A CG    1 
ATOM   2061  C  CD1   . LEU   A 1  294  ? -48.750 68.716  72.591  1.00 17.87 ? 292  LEU   A CD1   1 
ATOM   2062  C  CD2   . LEU   A 1  294  ? -49.450 69.413  70.289  1.00 17.33 ? 292  LEU   A CD2   1 
ATOM   2063  N  N     . ALA   A 1  295  ? -54.113 67.708  72.432  1.00 13.54 ? 293  ALA   A N     1 
ATOM   2064  C  CA    . ALA   A 1  295  ? -55.171 66.711  72.566  1.00 14.92 ? 293  ALA   A CA    1 
ATOM   2065  C  C     . ALA   A 1  295  ? -56.349 67.030  71.663  1.00 15.27 ? 293  ALA   A C     1 
ATOM   2066  O  O     . ALA   A 1  295  ? -56.963 66.117  71.108  1.00 15.26 ? 293  ALA   A O     1 
ATOM   2067  C  CB    . ALA   A 1  295  ? -55.614 66.618  74.023  1.00 15.81 ? 293  ALA   A CB    1 
ATOM   2068  N  N     . LEU   A 1  296  ? -56.678 68.312  71.503  1.00 14.47 ? 294  LEU   A N     1 
ATOM   2069  C  CA    . LEU   A 1  296  ? -57.751 68.678  70.582  1.00 14.50 ? 294  LEU   A CA    1 
ATOM   2070  C  C     . LEU   A 1  296  ? -57.421 68.239  69.166  1.00 15.70 ? 294  LEU   A C     1 
ATOM   2071  O  O     . LEU   A 1  296  ? -58.304 67.804  68.421  1.00 15.95 ? 294  LEU   A O     1 
ATOM   2072  C  CB    . LEU   A 1  296  ? -57.998 70.186  70.613  1.00 15.50 ? 294  LEU   A CB    1 
ATOM   2073  C  CG    . LEU   A 1  296  ? -58.680 70.710  71.873  1.00 17.63 ? 294  LEU   A CG    1 
ATOM   2074  C  CD1   . LEU   A 1  296  ? -58.586 72.223  71.922  1.00 19.11 ? 294  LEU   A CD1   1 
ATOM   2075  C  CD2   . LEU   A 1  296  ? -60.149 70.272  71.921  1.00 21.86 ? 294  LEU   A CD2   1 
ATOM   2076  N  N     . LEU   A 1  297  ? -56.156 68.368  68.767  1.00 15.22 ? 295  LEU   A N     1 
ATOM   2077  C  CA    . LEU   A 1  297  ? -55.779 67.938  67.429  1.00 16.38 ? 295  LEU   A CA    1 
ATOM   2078  C  C     . LEU   A 1  297  ? -55.832 66.419  67.317  1.00 15.27 ? 295  LEU   A C     1 
ATOM   2079  O  O     . LEU   A 1  297  ? -56.323 65.882  66.320  1.00 15.82 ? 295  LEU   A O     1 
ATOM   2080  C  CB    . LEU   A 1  297  ? -54.392 68.471  67.085  1.00 17.68 ? 295  LEU   A CB    1 
ATOM   2081  C  CG    . LEU   A 1  297  ? -54.032 68.357  65.604  1.00 19.75 ? 295  LEU   A CG    1 
ATOM   2082  C  CD1   . LEU   A 1  297  ? -54.998 69.164  64.719  1.00 25.27 ? 295  LEU   A CD1   1 
ATOM   2083  C  CD2   . LEU   A 1  297  ? -52.598 68.814  65.429  1.00 23.54 ? 295  LEU   A CD2   1 
ATOM   2084  N  N     . ALA   A 1  298  ? -55.350 65.708  68.343  1.00 14.42 ? 296  ALA   A N     1 
ATOM   2085  C  CA    . ALA   A 1  298  ? -55.455 64.255  68.335  1.00 14.84 ? 296  ALA   A CA    1 
ATOM   2086  C  C     . ALA   A 1  298  ? -56.905 63.813  68.259  1.00 15.43 ? 296  ALA   A C     1 
ATOM   2087  O  O     . ALA   A 1  298  ? -57.232 62.852  67.550  1.00 15.85 ? 296  ALA   A O     1 
ATOM   2088  C  CB    . ALA   A 1  298  ? -54.791 63.679  69.580  1.00 16.14 ? 296  ALA   A CB    1 
ATOM   2089  N  N     . LYS   A 1  299  ? -57.788 64.513  68.982  1.00 15.48 ? 297  LYS   A N     1 
ATOM   2090  C  CA    A LYS   A 1  299  ? -59.218 64.235  68.910  0.60 16.01 ? 297  LYS   A CA    1 
ATOM   2091  C  CA    B LYS   A 1  299  ? -59.215 64.230  68.909  0.40 16.02 ? 297  LYS   A CA    1 
ATOM   2092  C  C     . LYS   A 1  299  ? -59.738 64.409  67.491  1.00 17.59 ? 297  LYS   A C     1 
ATOM   2093  O  O     . LYS   A 1  299  ? -60.519 63.587  67.004  1.00 16.50 ? 297  LYS   A O     1 
ATOM   2094  C  CB    A LYS   A 1  299  ? -59.966 65.165  69.864  0.60 16.00 ? 297  LYS   A CB    1 
ATOM   2095  C  CB    B LYS   A 1  299  ? -59.957 65.145  69.880  0.40 16.01 ? 297  LYS   A CB    1 
ATOM   2096  C  CG    A LYS   A 1  299  ? -61.460 65.250  69.579  0.60 17.20 ? 297  LYS   A CG    1 
ATOM   2097  C  CG    B LYS   A 1  299  ? -61.461 65.161  69.699  0.40 17.20 ? 297  LYS   A CG    1 
ATOM   2098  C  CD    A LYS   A 1  299  ? -62.179 66.169  70.556  0.60 18.63 ? 297  LYS   A CD    1 
ATOM   2099  C  CD    B LYS   A 1  299  ? -62.128 65.937  70.822  0.40 17.70 ? 297  LYS   A CD    1 
ATOM   2100  C  CE    A LYS   A 1  299  ? -63.599 66.458  70.074  0.60 18.05 ? 297  LYS   A CE    1 
ATOM   2101  C  CE    B LYS   A 1  299  ? -63.570 66.253  70.477  0.40 19.84 ? 297  LYS   A CE    1 
ATOM   2102  N  NZ    A LYS   A 1  299  ? -64.444 67.101  71.124  0.60 19.48 ? 297  LYS   A NZ    1 
ATOM   2103  N  NZ    B LYS   A 1  299  ? -63.689 67.069  69.247  0.40 21.11 ? 297  LYS   A NZ    1 
ATOM   2104  N  N     . ASN   A 1  300  ? -59.308 65.466  66.804  1.00 16.17 ? 298  ASN   A N     1 
ATOM   2105  C  CA    . ASN   A 1  300  ? -59.870 65.700  65.479  1.00 15.56 ? 298  ASN   A CA    1 
ATOM   2106  C  C     . ASN   A 1  300  ? -59.482 64.606  64.495  1.00 16.19 ? 298  ASN   A C     1 
ATOM   2107  O  O     . ASN   A 1  300  ? -60.295 64.212  63.647  1.00 20.35 ? 298  ASN   A O     1 
ATOM   2108  C  CB    . ASN   A 1  300  ? -59.501 67.071  64.931  1.00 20.38 ? 298  ASN   A CB    1 
ATOM   2109  C  CG    . ASN   A 1  300  ? -60.330 67.419  63.718  1.00 28.97 ? 298  ASN   A CG    1 
ATOM   2110  O  OD1   . ASN   A 1  300  ? -61.484 67.854  63.839  1.00 33.46 ? 298  ASN   A OD1   1 
ATOM   2111  N  ND2   . ASN   A 1  300  ? -59.775 67.183  62.545  1.00 25.41 ? 298  ASN   A ND2   1 
ATOM   2112  N  N     . TYR   A 1  301  ? -58.256 64.103  64.589  1.00 16.36 ? 299  TYR   A N     1 
ATOM   2113  C  CA    . TYR   A 1  301  ? -57.826 62.987  63.768  1.00 17.42 ? 299  TYR   A CA    1 
ATOM   2114  C  C     . TYR   A 1  301  ? -58.212 61.637  64.357  1.00 17.29 ? 299  TYR   A C     1 
ATOM   2115  O  O     . TYR   A 1  301  ? -58.073 60.617  63.677  1.00 18.94 ? 299  TYR   A O     1 
ATOM   2116  C  CB    . TYR   A 1  301  ? -56.310 63.024  63.626  1.00 16.21 ? 299  TYR   A CB    1 
ATOM   2117  C  CG    . TYR   A 1  301  ? -55.775 64.097  62.721  1.00 16.38 ? 299  TYR   A CG    1 
ATOM   2118  C  CD1   . TYR   A 1  301  ? -55.980 64.046  61.348  1.00 17.27 ? 299  TYR   A CD1   1 
ATOM   2119  C  CD2   . TYR   A 1  301  ? -55.016 65.128  63.231  1.00 16.42 ? 299  TYR   A CD2   1 
ATOM   2120  C  CE1   . TYR   A 1  301  ? -55.438 65.011  60.517  1.00 18.75 ? 299  TYR   A CE1   1 
ATOM   2121  C  CE2   . TYR   A 1  301  ? -54.474 66.086  62.423  1.00 17.34 ? 299  TYR   A CE2   1 
ATOM   2122  C  CZ    . TYR   A 1  301  ? -54.686 66.032  61.062  1.00 18.83 ? 299  TYR   A CZ    1 
ATOM   2123  O  OH    . TYR   A 1  301  ? -54.122 67.007  60.265  1.00 19.38 ? 299  TYR   A OH    1 
ATOM   2124  N  N     . ASP   A 1  302  ? -58.699 61.614  65.598  1.00 15.43 ? 300  ASP   A N     1 
ATOM   2125  C  CA    . ASP   A 1  302  ? -59.053 60.390  66.305  1.00 15.71 ? 300  ASP   A CA    1 
ATOM   2126  C  C     . ASP   A 1  302  ? -57.870 59.430  66.406  1.00 16.33 ? 300  ASP   A C     1 
ATOM   2127  O  O     . ASP   A 1  302  ? -57.932 58.270  66.004  1.00 16.74 ? 300  ASP   A O     1 
ATOM   2128  C  CB    . ASP   A 1  302  ? -60.299 59.710  65.725  1.00 17.19 ? 300  ASP   A CB    1 
ATOM   2129  C  CG    . ASP   A 1  302  ? -60.924 58.744  66.700  1.00 19.37 ? 300  ASP   A CG    1 
ATOM   2130  O  OD1   . ASP   A 1  302  ? -60.922 59.051  67.911  1.00 20.23 ? 300  ASP   A OD1   1 
ATOM   2131  O  OD2   . ASP   A 1  302  ? -61.428 57.683  66.269  1.00 23.32 ? 300  ASP   A OD2   1 
ATOM   2132  N  N     . ILE   A 1  303  ? -56.786 59.943  66.978  1.00 14.78 ? 301  ILE   A N     1 
ATOM   2133  C  CA    . ILE   A 1  303  ? -55.595 59.150  67.267  1.00 15.20 ? 301  ILE   A CA    1 
ATOM   2134  C  C     . ILE   A 1  303  ? -55.354 59.163  68.769  1.00 15.83 ? 301  ILE   A C     1 
ATOM   2135  O  O     . ILE   A 1  303  ? -55.860 60.017  69.496  1.00 15.05 ? 301  ILE   A O     1 
ATOM   2136  C  CB    . ILE   A 1  303  ? -54.339 59.652  66.519  1.00 15.67 ? 301  ILE   A CB    1 
ATOM   2137  C  CG1   . ILE   A 1  303  ? -53.839 60.987  67.089  1.00 15.47 ? 301  ILE   A CG1   1 
ATOM   2138  C  CG2   . ILE   A 1  303  ? -54.629 59.757  65.016  1.00 17.09 ? 301  ILE   A CG2   1 
ATOM   2139  C  CD1   . ILE   A 1  303  ? -52.477 61.402  66.530  1.00 17.54 ? 301  ILE   A CD1   1 
ATOM   2140  N  N     . GLY   A 1  304  ? -54.554 58.206  69.228  1.00 15.83 ? 302  GLY   A N     1 
ATOM   2141  C  CA    . GLY   A 1  304  ? -54.175 58.182  70.626  1.00 15.90 ? 302  GLY   A CA    1 
ATOM   2142  C  C     . GLY   A 1  304  ? -53.144 59.250  70.932  1.00 15.64 ? 302  GLY   A C     1 
ATOM   2143  O  O     . GLY   A 1  304  ? -52.306 59.594  70.105  1.00 15.39 ? 302  GLY   A O     1 
ATOM   2144  N  N     . LEU   A 1  305  ? -53.229 59.803  72.135  1.00 15.35 ? 303  LEU   A N     1 
ATOM   2145  C  CA    . LEU   A 1  305  ? -52.227 60.728  72.649  1.00 14.44 ? 303  LEU   A CA    1 
ATOM   2146  C  C     . LEU   A 1  305  ? -51.910 60.267  74.057  1.00 15.09 ? 303  LEU   A C     1 
ATOM   2147  O  O     . LEU   A 1  305  ? -52.753 60.388  74.949  1.00 15.65 ? 303  LEU   A O     1 
ATOM   2148  C  CB    . LEU   A 1  305  ? -52.749 62.160  72.667  1.00 16.10 ? 303  LEU   A CB    1 
ATOM   2149  C  CG    . LEU   A 1  305  ? -51.686 63.194  73.051  1.00 20.01 ? 303  LEU   A CG    1 
ATOM   2150  C  CD1   . LEU   A 1  305  ? -51.976 64.499  72.361  1.00 22.16 ? 303  LEU   A CD1   1 
ATOM   2151  C  CD2   . LEU   A 1  305  ? -51.615 63.420  74.554  1.00 27.67 ? 303  LEU   A CD2   1 
ATOM   2152  N  N     . ASN   A 1  306  ? -50.709 59.739  74.252  1.00 15.58 ? 304  ASN   A N     1 
ATOM   2153  C  CA    . ASN   A 1  306  ? -50.320 59.130  75.510  1.00 16.22 ? 304  ASN   A CA    1 
ATOM   2154  C  C     . ASN   A 1  306  ? -49.369 60.057  76.249  1.00 15.24 ? 304  ASN   A C     1 
ATOM   2155  O  O     . ASN   A 1  306  ? -48.419 60.587  75.658  1.00 16.11 ? 304  ASN   A O     1 
ATOM   2156  C  CB    . ASN   A 1  306  ? -49.579 57.827  75.248  1.00 15.83 ? 304  ASN   A CB    1 
ATOM   2157  C  CG    . ASN   A 1  306  ? -48.972 57.278  76.496  1.00 17.38 ? 304  ASN   A CG    1 
ATOM   2158  O  OD1   . ASN   A 1  306  ? -47.779 57.464  76.765  1.00 21.46 ? 304  ASN   A OD1   1 
ATOM   2159  N  ND2   . ASN   A 1  306  ? -49.785 56.610  77.287  1.00 16.14 ? 304  ASN   A ND2   1 
ATOM   2160  N  N     . ILE   A 1  307  ? -49.594 60.211  77.548  1.00 14.75 ? 305  ILE   A N     1 
ATOM   2161  C  CA    . ILE   A 1  307  ? -48.680 60.946  78.414  1.00 14.57 ? 305  ILE   A CA    1 
ATOM   2162  C  C     . ILE   A 1  307  ? -47.731 59.949  79.064  1.00 14.73 ? 305  ILE   A C     1 
ATOM   2163  O  O     . ILE   A 1  307  ? -48.135 59.139  79.912  1.00 15.85 ? 305  ILE   A O     1 
ATOM   2164  C  CB    . ILE   A 1  307  ? -49.438 61.759  79.463  1.00 14.93 ? 305  ILE   A CB    1 
ATOM   2165  C  CG1   . ILE   A 1  307  ? -50.329 62.786  78.754  1.00 17.52 ? 305  ILE   A CG1   1 
ATOM   2166  C  CG2   . ILE   A 1  307  ? -48.434 62.404  80.445  1.00 19.24 ? 305  ILE   A CG2   1 
ATOM   2167  C  CD1   . ILE   A 1  307  ? -51.347 63.441  79.674  1.00 23.21 ? 305  ILE   A CD1   1 
ATOM   2168  N  N     . ASP   A 1  308  ? -46.457 60.014  78.673  1.00 14.62 ? 306  ASP   A N     1 
ATOM   2169  C  CA    . ASP   A 1  308  ? -45.433 59.145  79.225  1.00 15.89 ? 306  ASP   A CA    1 
ATOM   2170  C  C     . ASP   A 1  308  ? -45.205 59.485  80.694  1.00 15.98 ? 306  ASP   A C     1 
ATOM   2171  O  O     . ASP   A 1  308  ? -45.422 60.613  81.132  1.00 17.00 ? 306  ASP   A O     1 
ATOM   2172  C  CB    . ASP   A 1  308  ? -44.117 59.339  78.463  1.00 16.98 ? 306  ASP   A CB    1 
ATOM   2173  C  CG    . ASP   A 1  308  ? -44.109 58.661  77.100  1.00 21.42 ? 306  ASP   A CG    1 
ATOM   2174  O  OD1   . ASP   A 1  308  ? -45.051 57.913  76.772  1.00 20.22 ? 306  ASP   A OD1   1 
ATOM   2175  O  OD2   . ASP   A 1  308  ? -43.131 58.867  76.347  1.00 22.06 ? 306  ASP   A OD2   1 
ATOM   2176  N  N     . ALA   A 1  309  ? -44.784 58.488  81.461  1.00 14.19 ? 307  ALA   A N     1 
ATOM   2177  C  CA    . ALA   A 1  309  ? -44.506 58.687  82.876  1.00 13.29 ? 307  ALA   A CA    1 
ATOM   2178  C  C     . ALA   A 1  309  ? -43.020 58.927  83.081  1.00 16.22 ? 307  ALA   A C     1 
ATOM   2179  O  O     . ALA   A 1  309  ? -42.175 58.258  82.473  1.00 16.02 ? 307  ALA   A O     1 
ATOM   2180  C  CB    . ALA   A 1  309  ? -44.949 57.487  83.706  1.00 16.11 ? 307  ALA   A CB    1 
ATOM   2181  N  N     . GLU   A 1  310  ? -42.712 59.858  83.975  1.00 15.30 ? 308  GLU   A N     1 
ATOM   2182  C  CA    . GLU   A 1  310  ? -41.333 60.284  84.146  1.00 14.94 ? 308  GLU   A CA    1 
ATOM   2183  C  C     . GLU   A 1  310  ? -40.887 60.016  85.575  1.00 14.34 ? 308  GLU   A C     1 
ATOM   2184  O  O     . GLU   A 1  310  ? -41.151 58.931  86.102  1.00 16.01 ? 308  GLU   A O     1 
ATOM   2185  C  CB    . GLU   A 1  310  ? -41.197 61.734  83.695  1.00 16.32 ? 308  GLU   A CB    1 
ATOM   2186  C  CG    . GLU   A 1  310  ? -41.541 61.874  82.202  1.00 18.89 ? 308  GLU   A CG    1 
ATOM   2187  C  CD    . GLU   A 1  310  ? -41.267 63.260  81.659  1.00 19.17 ? 308  GLU   A CD    1 
ATOM   2188  O  OE1   . GLU   A 1  310  ? -40.071 63.577  81.443  1.00 21.21 ? 308  GLU   A OE1   1 
ATOM   2189  O  OE2   . GLU   A 1  310  ? -42.247 64.017  81.458  1.00 17.85 ? 308  GLU   A OE2   1 
ATOM   2190  N  N     . GLU   A 1  311  ? -40.197 60.966  86.198  1.00 15.65 ? 309  GLU   A N     1 
ATOM   2191  C  CA    . GLU   A 1  311  ? -39.679 60.742  87.540  1.00 16.98 ? 309  GLU   A CA    1 
ATOM   2192  C  C     . GLU   A 1  311  ? -40.806 60.649  88.567  1.00 15.12 ? 309  GLU   A C     1 
ATOM   2193  O  O     . GLU   A 1  311  ? -41.917 61.160  88.382  1.00 15.25 ? 309  GLU   A O     1 
ATOM   2194  C  CB    . GLU   A 1  311  ? -38.739 61.876  87.930  1.00 17.41 ? 309  GLU   A CB    1 
ATOM   2195  C  CG    . GLU   A 1  311  ? -37.466 61.949  87.073  1.00 18.52 ? 309  GLU   A CG    1 
ATOM   2196  C  CD    . GLU   A 1  311  ? -37.620 62.817  85.843  1.00 23.27 ? 309  GLU   A CD    1 
ATOM   2197  O  OE1   . GLU   A 1  311  ? -38.756 63.170  85.472  1.00 18.51 ? 309  GLU   A OE1   1 
ATOM   2198  O  OE2   . GLU   A 1  311  ? -36.591 63.159  85.233  1.00 27.42 ? 309  GLU   A OE2   1 
ATOM   2199  N  N     . ALA   A 1  312  ? -40.496 60.002  89.688  1.00 14.84 ? 310  ALA   A N     1 
ATOM   2200  C  CA    . ALA   A 1  312  ? -41.508 59.772  90.710  1.00 14.44 ? 310  ALA   A CA    1 
ATOM   2201  C  C     . ALA   A 1  312  ? -42.095 61.072  91.243  1.00 14.44 ? 310  ALA   A C     1 
ATOM   2202  O  O     . ALA   A 1  312  ? -43.283 61.120  91.580  1.00 16.45 ? 310  ALA   A O     1 
ATOM   2203  C  CB    . ALA   A 1  312  ? -40.906 58.944  91.846  1.00 16.14 ? 310  ALA   A CB    1 
ATOM   2204  N  N     . ASP   A 1  313  ? -41.297 62.138  91.328  1.00 15.73 ? 311  ASP   A N     1 
ATOM   2205  C  CA    . ASP   A 1  313  ? -41.819 63.394  91.858  1.00 16.09 ? 311  ASP   A CA    1 
ATOM   2206  C  C     . ASP   A 1  313  ? -42.690 64.153  90.871  1.00 15.47 ? 311  ASP   A C     1 
ATOM   2207  O  O     . ASP   A 1  313  ? -43.138 65.252  91.200  1.00 18.20 ? 311  ASP   A O     1 
ATOM   2208  C  CB    . ASP   A 1  313  ? -40.715 64.282  92.457  1.00 18.22 ? 311  ASP   A CB    1 
ATOM   2209  C  CG    . ASP   A 1  313  ? -39.723 64.790  91.424  1.00 23.52 ? 311  ASP   A CG    1 
ATOM   2210  O  OD1   . ASP   A 1  313  ? -39.879 64.493  90.223  1.00 19.96 ? 311  ASP   A OD1   1 
ATOM   2211  O  OD2   . ASP   A 1  313  ? -38.775 65.499  91.826  1.00 25.40 ? 311  ASP   A OD2   1 
ATOM   2212  N  N     . ARG   A 1  314  ? -42.941 63.590  89.693  1.00 15.04 ? 312  ARG   A N     1 
ATOM   2213  C  CA    . ARG   A 1  314  ? -43.841 64.187  88.720  1.00 14.19 ? 312  ARG   A CA    1 
ATOM   2214  C  C     . ARG   A 1  314  ? -45.132 63.406  88.573  1.00 15.72 ? 312  ARG   A C     1 
ATOM   2215  O  O     . ARG   A 1  314  ? -46.071 63.903  87.940  1.00 16.88 ? 312  ARG   A O     1 
ATOM   2216  C  CB    . ARG   A 1  314  ? -43.146 64.315  87.357  1.00 16.09 ? 312  ARG   A CB    1 
ATOM   2217  C  CG    . ARG   A 1  314  ? -42.143 65.453  87.367  1.00 18.14 ? 312  ARG   A CG    1 
ATOM   2218  C  CD    . ARG   A 1  314  ? -41.145 65.341  86.250  1.00 19.90 ? 312  ARG   A CD    1 
ATOM   2219  N  NE    . ARG   A 1  314  ? -40.557 66.644  85.981  1.00 19.63 ? 312  ARG   A NE    1 
ATOM   2220  C  CZ    . ARG   A 1  314  ? -39.557 66.838  85.133  1.00 18.29 ? 312  ARG   A CZ    1 
ATOM   2221  N  NH1   . ARG   A 1  314  ? -38.960 65.822  84.536  1.00 19.91 ? 312  ARG   A NH1   1 
ATOM   2222  N  NH2   . ARG   A 1  314  ? -39.160 68.083  84.871  1.00 20.34 ? 312  ARG   A NH2   1 
ATOM   2223  N  N     . LEU   A 1  315  ? -45.221 62.225  89.185  1.00 15.43 ? 313  LEU   A N     1 
ATOM   2224  C  CA    . LEU   A 1  315  ? -46.399 61.381  89.015  1.00 15.80 ? 313  LEU   A CA    1 
ATOM   2225  C  C     . LEU   A 1  315  ? -47.660 62.113  89.440  1.00 16.74 ? 313  LEU   A C     1 
ATOM   2226  O  O     . LEU   A 1  315  ? -48.605 62.267  88.654  1.00 16.73 ? 313  LEU   A O     1 
ATOM   2227  C  CB    . LEU   A 1  315  ? -46.228 60.117  89.857  1.00 16.42 ? 313  LEU   A CB    1 
ATOM   2228  C  CG    . LEU   A 1  315  ? -47.030 58.881  89.437  1.00 16.14 ? 313  LEU   A CG    1 
ATOM   2229  C  CD1   . LEU   A 1  315  ? -46.652 57.709  90.332  1.00 17.32 ? 313  LEU   A CD1   1 
ATOM   2230  C  CD2   . LEU   A 1  315  ? -48.531 59.095  89.470  1.00 19.74 ? 313  LEU   A CD2   1 
ATOM   2231  N  N     . GLU   A 1  316  ? -47.710 62.553  90.694  1.00 16.37 ? 314  GLU   A N     1 
ATOM   2232  C  CA    . GLU   A 1  316  ? -48.966 63.106  91.184  1.00 16.56 ? 314  GLU   A CA    1 
ATOM   2233  C  C     . GLU   A 1  316  ? -49.316 64.414  90.486  1.00 19.04 ? 314  GLU   A C     1 
ATOM   2234  O  O     . GLU   A 1  316  ? -50.492 64.673  90.200  1.00 17.84 ? 314  GLU   A O     1 
ATOM   2235  C  CB    . GLU   A 1  316  ? -48.951 63.216  92.706  1.00 18.20 ? 314  GLU   A CB    1 
ATOM   2236  C  CG    . GLU   A 1  316  ? -49.037 61.838  93.334  1.00 18.10 ? 314  GLU   A CG    1 
ATOM   2237  C  CD    . GLU   A 1  316  ? -49.011 61.845  94.840  1.00 18.42 ? 314  GLU   A CD    1 
ATOM   2238  O  OE1   . GLU   A 1  316  ? -49.737 62.656  95.430  1.00 21.10 ? 314  GLU   A OE1   1 
ATOM   2239  O  OE2   . GLU   A 1  316  ? -48.271 61.026  95.425  1.00 19.67 ? 314  GLU   A OE2   1 
ATOM   2240  N  N     . LEU   A 1  317  ? -48.312 65.233  90.164  1.00 17.58 ? 315  LEU   A N     1 
ATOM   2241  C  CA    . LEU   A 1  317  ? -48.577 66.453  89.407  1.00 17.98 ? 315  LEU   A CA    1 
ATOM   2242  C  C     . LEU   A 1  317  ? -49.226 66.137  88.065  1.00 17.51 ? 315  LEU   A C     1 
ATOM   2243  O  O     . LEU   A 1  317  ? -50.178 66.808  87.649  1.00 17.38 ? 315  LEU   A O     1 
ATOM   2244  C  CB    . LEU   A 1  317  ? -47.274 67.211  89.197  1.00 19.22 ? 315  LEU   A CB    1 
ATOM   2245  C  CG    . LEU   A 1  317  ? -47.401 68.469  88.343  1.00 20.00 ? 315  LEU   A CG    1 
ATOM   2246  C  CD1   . LEU   A 1  317  ? -48.382 69.441  88.978  1.00 23.28 ? 315  LEU   A CD1   1 
ATOM   2247  C  CD2   . LEU   A 1  317  ? -46.032 69.110  88.184  1.00 23.58 ? 315  LEU   A CD2   1 
ATOM   2248  N  N     . SER   A 1  318  ? -48.745 65.096  87.386  1.00 14.98 ? 316  SER   A N     1 
ATOM   2249  C  CA    . SER   A 1  318  ? -49.314 64.745  86.091  1.00 15.19 ? 316  SER   A CA    1 
ATOM   2250  C  C     . SER   A 1  318  ? -50.772 64.340  86.216  1.00 17.05 ? 316  SER   A C     1 
ATOM   2251  O  O     . SER   A 1  318  ? -51.541 64.527  85.269  1.00 16.41 ? 316  SER   A O     1 
ATOM   2252  C  CB    . SER   A 1  318  ? -48.521 63.612  85.435  1.00 14.65 ? 316  SER   A CB    1 
ATOM   2253  O  OG    . SER   A 1  318  ? -48.724 62.384  86.103  1.00 16.74 ? 316  SER   A OG    1 
ATOM   2254  N  N     . LEU   A 1  319  ? -51.169 63.797  87.372  1.00 16.38 ? 317  LEU   A N     1 
ATOM   2255  C  CA    . LEU   A 1  319  ? -52.563 63.416  87.573  1.00 15.97 ? 317  LEU   A CA    1 
ATOM   2256  C  C     . LEU   A 1  319  ? -53.468 64.627  87.566  1.00 17.08 ? 317  LEU   A C     1 
ATOM   2257  O  O     . LEU   A 1  319  ? -54.625 64.531  87.143  1.00 16.94 ? 317  LEU   A O     1 
ATOM   2258  C  CB    . LEU   A 1  319  ? -52.721 62.663  88.893  1.00 17.51 ? 317  LEU   A CB    1 
ATOM   2259  C  CG    . LEU   A 1  319  ? -52.007 61.319  88.961  1.00 18.78 ? 317  LEU   A CG    1 
ATOM   2260  C  CD1   . LEU   A 1  319  ? -52.195 60.722  90.354  1.00 18.83 ? 317  LEU   A CD1   1 
ATOM   2261  C  CD2   . LEU   A 1  319  ? -52.527 60.374  87.905  1.00 18.78 ? 317  LEU   A CD2   1 
ATOM   2262  N  N     . ASP   A 1  320  ? -52.980 65.772  88.038  1.00 16.89 ? 318  ASP   A N     1 
ATOM   2263  C  CA    . ASP   A 1  320  ? -53.811 66.967  87.985  1.00 20.10 ? 318  ASP   A CA    1 
ATOM   2264  C  C     . ASP   A 1  320  ? -54.071 67.405  86.558  1.00 19.42 ? 318  ASP   A C     1 
ATOM   2265  O  O     . ASP   A 1  320  ? -55.158 67.905  86.251  1.00 20.85 ? 318  ASP   A O     1 
ATOM   2266  C  CB    . ASP   A 1  320  ? -53.193 68.090  88.808  1.00 19.55 ? 318  ASP   A CB    1 
ATOM   2267  C  CG    . ASP   A 1  320  ? -53.362 67.867  90.277  1.00 23.52 ? 318  ASP   A CG    1 
ATOM   2268  O  OD1   . ASP   A 1  320  ? -54.525 67.666  90.707  1.00 24.73 ? 318  ASP   A OD1   1 
ATOM   2269  O  OD2   . ASP   A 1  320  ? -52.337 67.866  90.991  1.00 26.12 ? 318  ASP   A OD2   1 
ATOM   2270  N  N     . LEU   A 1  321  ? -53.101 67.213  85.672  1.00 16.42 ? 319  LEU   A N     1 
ATOM   2271  C  CA    . LEU   A 1  321  ? -53.340 67.511  84.268  1.00 17.12 ? 319  LEU   A CA    1 
ATOM   2272  C  C     . LEU   A 1  321  ? -54.288 66.495  83.655  1.00 16.99 ? 319  LEU   A C     1 
ATOM   2273  O  O     . LEU   A 1  321  ? -55.209 66.871  82.919  1.00 17.93 ? 319  LEU   A O     1 
ATOM   2274  C  CB    . LEU   A 1  321  ? -52.020 67.540  83.497  1.00 17.20 ? 319  LEU   A CB    1 
ATOM   2275  C  CG    . LEU   A 1  321  ? -51.171 68.790  83.707  1.00 20.43 ? 319  LEU   A CG    1 
ATOM   2276  C  CD1   . LEU   A 1  321  ? -50.225 68.585  84.863  1.00 24.54 ? 319  LEU   A CD1   1 
ATOM   2277  C  CD2   . LEU   A 1  321  ? -50.391 69.125  82.431  1.00 25.13 ? 319  LEU   A CD2   1 
ATOM   2278  N  N     . LEU   A 1  322  ? -54.072 65.207  83.938  1.00 16.08 ? 320  LEU   A N     1 
ATOM   2279  C  CA    . LEU   A 1  322  ? -54.958 64.172  83.418  1.00 16.60 ? 320  LEU   A CA    1 
ATOM   2280  C  C     . LEU   A 1  322  ? -56.391 64.420  83.861  1.00 17.21 ? 320  LEU   A C     1 
ATOM   2281  O  O     . LEU   A 1  322  ? -57.325 64.275  83.065  1.00 17.90 ? 320  LEU   A O     1 
ATOM   2282  C  CB    . LEU   A 1  322  ? -54.485 62.794  83.887  1.00 17.09 ? 320  LEU   A CB    1 
ATOM   2283  C  CG    . LEU   A 1  322  ? -55.329 61.612  83.403  1.00 18.83 ? 320  LEU   A CG    1 
ATOM   2284  C  CD1   . LEU   A 1  322  ? -55.154 61.404  81.913  1.00 17.33 ? 320  LEU   A CD1   1 
ATOM   2285  C  CD2   . LEU   A 1  322  ? -54.981 60.345  84.173  1.00 16.95 ? 320  LEU   A CD2   1 
ATOM   2286  N  N     . GLU   A 1  323  ? -56.578 64.824  85.118  1.00 15.85 ? 321  GLU   A N     1 
ATOM   2287  C  CA    . GLU   A 1  323  ? -57.922 65.099  85.626  1.00 18.37 ? 321  GLU   A CA    1 
ATOM   2288  C  C     . GLU   A 1  323  ? -58.586 66.216  84.833  1.00 21.51 ? 321  GLU   A C     1 
ATOM   2289  O  O     . GLU   A 1  323  ? -59.718 66.065  84.355  1.00 18.86 ? 321  GLU   A O     1 
ATOM   2290  C  CB    . GLU   A 1  323  ? -57.857 65.456  87.112  1.00 19.48 ? 321  GLU   A CB    1 
ATOM   2291  C  CG    . GLU   A 1  323  ? -59.169 66.014  87.681  1.00 25.18 ? 321  GLU   A CG    1 
ATOM   2292  C  CD    . GLU   A 1  323  ? -59.862 65.058  88.626  1.00 27.61 ? 321  GLU   A CD    1 
ATOM   2293  O  OE1   . GLU   A 1  323  ? -59.277 64.017  88.955  1.00 30.78 ? 321  GLU   A OE1   1 
ATOM   2294  O  OE2   . GLU   A 1  323  ? -61.008 65.342  89.039  1.00 27.81 ? 321  GLU   A OE2   1 
ATOM   2295  N  N     . VAL   A 1  324  ? -57.898 67.352  84.679  1.00 17.29 ? 322  VAL   A N     1 
ATOM   2296  C  CA    . VAL   A 1  324  ? -58.512 68.478  83.983  1.00 16.11 ? 322  VAL   A CA    1 
ATOM   2297  C  C     . VAL   A 1  324  ? -58.832 68.103  82.548  1.00 17.67 ? 322  VAL   A C     1 
ATOM   2298  O  O     . VAL   A 1  324  ? -59.907 68.424  82.032  1.00 17.77 ? 322  VAL   A O     1 
ATOM   2299  C  CB    . VAL   A 1  324  ? -57.610 69.722  84.044  1.00 21.25 ? 322  VAL   A CB    1 
ATOM   2300  C  CG1   . VAL   A 1  324  ? -58.246 70.856  83.245  1.00 21.70 ? 322  VAL   A CG1   1 
ATOM   2301  C  CG2   . VAL   A 1  324  ? -57.399 70.150  85.473  1.00 21.81 ? 322  VAL   A CG2   1 
ATOM   2302  N  N     . LEU   A 1  325  ? -57.911 67.408  81.885  1.00 15.28 ? 323  LEU   A N     1 
ATOM   2303  C  CA    . LEU   A 1  325  ? -58.124 67.070  80.481  1.00 16.51 ? 323  LEU   A CA    1 
ATOM   2304  C  C     . LEU   A 1  325  ? -59.311 66.131  80.321  1.00 16.52 ? 323  LEU   A C     1 
ATOM   2305  O  O     . LEU   A 1  325  ? -60.136 66.302  79.411  1.00 16.00 ? 323  LEU   A O     1 
ATOM   2306  C  CB    . LEU   A 1  325  ? -56.862 66.433  79.904  1.00 18.00 ? 323  LEU   A CB    1 
ATOM   2307  C  CG    . LEU   A 1  325  ? -55.681 67.397  79.798  1.00 18.03 ? 323  LEU   A CG    1 
ATOM   2308  C  CD1   . LEU   A 1  325  ? -54.393 66.605  79.640  1.00 19.70 ? 323  LEU   A CD1   1 
ATOM   2309  C  CD2   . LEU   A 1  325  ? -55.902 68.302  78.615  1.00 18.45 ? 323  LEU   A CD2   1 
ATOM   2310  N  N     . CYS   A 1  326  ? -59.415 65.133  81.199  1.00 16.32 ? 324  CYS   A N     1 
ATOM   2311  C  CA    . CYS   A 1  326  ? -60.516 64.189  81.072  1.00 16.59 ? 324  CYS   A CA    1 
ATOM   2312  C  C     . CYS   A 1  326  ? -61.862 64.800  81.420  1.00 19.49 ? 324  CYS   A C     1 
ATOM   2313  O  O     . CYS   A 1  326  ? -62.881 64.278  80.967  1.00 18.04 ? 324  CYS   A O     1 
ATOM   2314  C  CB    . CYS   A 1  326  ? -60.259 62.956  81.928  1.00 17.66 ? 324  CYS   A CB    1 
ATOM   2315  S  SG    . CYS   A 1  326  ? -58.916 61.954  81.267  1.00 19.73 ? 324  CYS   A SG    1 
ATOM   2316  N  N     . LEU   A 1  327  ? -61.889 65.877  82.201  1.00 18.65 ? 325  LEU   A N     1 
ATOM   2317  C  CA    . LEU   A 1  327  ? -63.126 66.563  82.551  1.00 16.43 ? 325  LEU   A CA    1 
ATOM   2318  C  C     . LEU   A 1  327  ? -63.448 67.712  81.606  1.00 16.66 ? 325  LEU   A C     1 
ATOM   2319  O  O     . LEU   A 1  327  ? -64.511 68.320  81.739  1.00 18.82 ? 325  LEU   A O     1 
ATOM   2320  C  CB    . LEU   A 1  327  ? -63.055 67.084  83.992  1.00 17.52 ? 325  LEU   A CB    1 
ATOM   2321  C  CG    . LEU   A 1  327  ? -62.910 66.003  85.066  1.00 24.69 ? 325  LEU   A CG    1 
ATOM   2322  C  CD1   . LEU   A 1  327  ? -62.823 66.624  86.453  1.00 24.97 ? 325  LEU   A CD1   1 
ATOM   2323  C  CD2   . LEU   A 1  327  ? -64.037 64.992  85.002  1.00 25.65 ? 325  LEU   A CD2   1 
ATOM   2324  N  N     . ASP   A 1  328  ? -62.568 68.014  80.657  1.00 16.49 ? 326  ASP   A N     1 
ATOM   2325  C  CA    . ASP   A 1  328  ? -62.749 69.157  79.770  1.00 17.56 ? 326  ASP   A CA    1 
ATOM   2326  C  C     . ASP   A 1  328  ? -63.690 68.771  78.641  1.00 19.17 ? 326  ASP   A C     1 
ATOM   2327  O  O     . ASP   A 1  328  ? -63.358 67.916  77.817  1.00 17.59 ? 326  ASP   A O     1 
ATOM   2328  C  CB    . ASP   A 1  328  ? -61.392 69.556  79.196  1.00 17.98 ? 326  ASP   A CB    1 
ATOM   2329  C  CG    . ASP   A 1  328  ? -61.439 70.879  78.476  1.00 23.13 ? 326  ASP   A CG    1 
ATOM   2330  O  OD1   . ASP   A 1  328  ? -62.431 71.144  77.771  1.00 21.80 ? 326  ASP   A OD1   1 
ATOM   2331  O  OD2   . ASP   A 1  328  ? -60.498 71.674  78.635  1.00 25.22 ? 326  ASP   A OD2   1 
ATOM   2332  N  N     . GLY   A 1  329  ? -64.855 69.417  78.592  1.00 18.09 ? 327  GLY   A N     1 
ATOM   2333  C  CA    . GLY   A 1  329  ? -65.850 69.060  77.598  1.00 18.79 ? 327  GLY   A CA    1 
ATOM   2334  C  C     . GLY   A 1  329  ? -65.394 69.264  76.173  1.00 18.73 ? 327  GLY   A C     1 
ATOM   2335  O  O     . GLY   A 1  329  ? -65.915 68.607  75.275  1.00 18.03 ? 327  GLY   A O     1 
ATOM   2336  N  N     . ASP   A 1  330  ? -64.412 70.136  75.942  1.00 17.68 ? 328  ASP   A N     1 
ATOM   2337  C  CA    . ASP   A 1  330  ? -63.926 70.326  74.581  1.00 17.97 ? 328  ASP   A CA    1 
ATOM   2338  C  C     . ASP   A 1  330  ? -63.282 69.065  74.028  1.00 17.26 ? 328  ASP   A C     1 
ATOM   2339  O  O     . ASP   A 1  330  ? -63.176 68.926  72.808  1.00 18.35 ? 328  ASP   A O     1 
ATOM   2340  C  CB    . ASP   A 1  330  ? -62.898 71.456  74.518  1.00 17.98 ? 328  ASP   A CB    1 
ATOM   2341  C  CG    . ASP   A 1  330  ? -63.507 72.825  74.751  1.00 25.53 ? 328  ASP   A CG    1 
ATOM   2342  O  OD1   . ASP   A 1  330  ? -64.720 72.992  74.530  1.00 26.60 ? 328  ASP   A OD1   1 
ATOM   2343  O  OD2   . ASP   A 1  330  ? -62.764 73.742  75.149  1.00 22.02 ? 328  ASP   A OD2   1 
ATOM   2344  N  N     . LEU   A 1  331  ? -62.859 68.145  74.890  1.00 15.70 ? 329  LEU   A N     1 
ATOM   2345  C  CA    . LEU   A 1  331  ? -62.233 66.911  74.447  1.00 16.43 ? 329  LEU   A CA    1 
ATOM   2346  C  C     . LEU   A 1  331  ? -63.201 65.743  74.414  1.00 17.86 ? 329  LEU   A C     1 
ATOM   2347  O  O     . LEU   A 1  331  ? -62.783 64.617  74.152  1.00 18.35 ? 329  LEU   A O     1 
ATOM   2348  C  CB    . LEU   A 1  331  ? -61.042 66.570  75.336  1.00 15.84 ? 329  LEU   A CB    1 
ATOM   2349  C  CG    . LEU   A 1  331  ? -59.827 67.459  75.090  1.00 15.53 ? 329  LEU   A CG    1 
ATOM   2350  C  CD1   . LEU   A 1  331  ? -58.815 67.265  76.191  1.00 16.82 ? 329  LEU   A CD1   1 
ATOM   2351  C  CD2   . LEU   A 1  331  ? -59.203 67.182  73.729  1.00 18.44 ? 329  LEU   A CD2   1 
ATOM   2352  N  N     . SER   A 1  332  ? -64.483 65.983  74.681  1.00 17.46 ? 330  SER   A N     1 
ATOM   2353  C  CA    . SER   A 1  332  ? -65.406 64.867  74.794  1.00 19.47 ? 330  SER   A CA    1 
ATOM   2354  C  C     . SER   A 1  332  ? -65.621 64.203  73.441  1.00 17.91 ? 330  SER   A C     1 
ATOM   2355  O  O     . SER   A 1  332  ? -65.465 64.818  72.384  1.00 21.68 ? 330  SER   A O     1 
ATOM   2356  C  CB    . SER   A 1  332  ? -66.740 65.321  75.384  1.00 19.55 ? 330  SER   A CB    1 
ATOM   2357  O  OG    . SER   A 1  332  ? -67.418 66.175  74.496  1.00 22.74 ? 330  SER   A OG    1 
ATOM   2358  N  N     . GLY   A 1  333  ? -65.954 62.918  73.489  1.00 16.80 ? 331  GLY   A N     1 
ATOM   2359  C  CA    . GLY   A 1  333  ? -66.178 62.139  72.295  1.00 19.27 ? 331  GLY   A CA    1 
ATOM   2360  C  C     . GLY   A 1  333  ? -64.950 61.418  71.793  1.00 18.44 ? 331  GLY   A C     1 
ATOM   2361  O  O     . GLY   A 1  333  ? -65.050 60.642  70.833  1.00 21.06 ? 331  GLY   A O     1 
ATOM   2362  N  N     . TRP   A 1  334  ? -63.797 61.651  72.407  1.00 17.87 ? 332  TRP   A N     1 
ATOM   2363  C  CA    . TRP   A 1  334  ? -62.540 61.059  71.985  1.00 17.69 ? 332  TRP   A CA    1 
ATOM   2364  C  C     . TRP   A 1  334  ? -61.997 60.256  73.149  1.00 16.82 ? 332  TRP   A C     1 
ATOM   2365  O  O     . TRP   A 1  334  ? -61.914 60.766  74.269  1.00 17.61 ? 332  TRP   A O     1 
ATOM   2366  C  CB    . TRP   A 1  334  ? -61.586 62.188  71.646  1.00 17.38 ? 332  TRP   A CB    1 
ATOM   2367  C  CG    . TRP   A 1  334  ? -60.157 61.833  71.467  1.00 15.50 ? 332  TRP   A CG    1 
ATOM   2368  C  CD1   . TRP   A 1  334  ? -59.610 61.070  70.480  1.00 16.05 ? 332  TRP   A CD1   1 
ATOM   2369  C  CD2   . TRP   A 1  334  ? -59.079 62.306  72.263  1.00 14.84 ? 332  TRP   A CD2   1 
ATOM   2370  N  NE1   . TRP   A 1  334  ? -58.245 61.029  70.621  1.00 16.25 ? 332  TRP   A NE1   1 
ATOM   2371  C  CE2   . TRP   A 1  334  ? -57.892 61.780  71.712  1.00 15.06 ? 332  TRP   A CE2   1 
ATOM   2372  C  CE3   . TRP   A 1  334  ? -58.999 63.119  73.398  1.00 17.81 ? 332  TRP   A CE3   1 
ATOM   2373  C  CZ2   . TRP   A 1  334  ? -56.633 62.041  72.255  1.00 16.55 ? 332  TRP   A CZ2   1 
ATOM   2374  C  CZ3   . TRP   A 1  334  ? -57.751 63.376  73.943  1.00 17.43 ? 332  TRP   A CZ3   1 
ATOM   2375  C  CH2   . TRP   A 1  334  ? -56.579 62.839  73.366  1.00 17.50 ? 332  TRP   A CH2   1 
ATOM   2376  N  N     . ASN   A 1  335  ? -61.660 58.995  72.886  1.00 15.73 ? 333  ASN   A N     1 
ATOM   2377  C  CA    . ASN   A 1  335  ? -61.135 58.090  73.898  1.00 15.05 ? 333  ASN   A CA    1 
ATOM   2378  C  C     . ASN   A 1  335  ? -59.639 57.870  73.745  1.00 15.60 ? 333  ASN   A C     1 
ATOM   2379  O  O     . ASN   A 1  335  ? -59.095 56.917  74.308  1.00 16.36 ? 333  ASN   A O     1 
ATOM   2380  C  CB    . ASN   A 1  335  ? -61.854 56.742  73.853  1.00 17.05 ? 333  ASN   A CB    1 
ATOM   2381  C  CG    . ASN   A 1  335  ? -63.204 56.784  74.510  1.00 19.37 ? 333  ASN   A CG    1 
ATOM   2382  O  OD1   . ASN   A 1  335  ? -63.451 57.578  75.419  1.00 18.02 ? 333  ASN   A OD1   1 
ATOM   2383  N  ND2   . ASN   A 1  335  ? -64.095 55.919  74.050  1.00 23.10 ? 333  ASN   A ND2   1 
ATOM   2384  N  N     . GLY   A 1  336  ? -58.969 58.730  72.984  1.00 16.51 ? 334  GLY   A N     1 
ATOM   2385  C  CA    . GLY   A 1  336  ? -57.559 58.527  72.727  1.00 15.28 ? 334  GLY   A CA    1 
ATOM   2386  C  C     . GLY   A 1  336  ? -56.605 59.026  73.793  1.00 16.04 ? 334  GLY   A C     1 
ATOM   2387  O  O     . GLY   A 1  336  ? -55.407 58.785  73.658  1.00 16.00 ? 334  GLY   A O     1 
ATOM   2388  N  N     . MET   A 1  337  ? -57.067 59.710  74.833  1.00 15.86 ? 335  MET   A N     1 
ATOM   2389  C  CA    A MET   A 1  337  ? -56.144 60.153  75.871  0.56 16.73 ? 335  MET   A CA    1 
ATOM   2390  C  CA    B MET   A 1  337  ? -56.150 60.152  75.876  0.44 16.74 ? 335  MET   A CA    1 
ATOM   2391  C  C     . MET   A 1  337  ? -55.573 58.944  76.600  1.00 15.05 ? 335  MET   A C     1 
ATOM   2392  O  O     . MET   A 1  337  ? -56.315 58.069  77.062  1.00 16.23 ? 335  MET   A O     1 
ATOM   2393  C  CB    A MET   A 1  337  ? -56.848 61.082  76.855  0.56 17.10 ? 335  MET   A CB    1 
ATOM   2394  C  CB    B MET   A 1  337  ? -56.872 61.052  76.869  0.44 17.13 ? 335  MET   A CB    1 
ATOM   2395  C  CG    A MET   A 1  337  ? -55.914 61.698  77.871  0.56 20.38 ? 335  MET   A CG    1 
ATOM   2396  C  CG    B MET   A 1  337  ? -56.066 61.359  78.108  0.44 22.12 ? 335  MET   A CG    1 
ATOM   2397  S  SD    A MET   A 1  337  ? -54.792 62.873  77.110  0.56 26.84 ? 335  MET   A SD    1 
ATOM   2398  S  SD    B MET   A 1  337  ? -55.997 63.127  78.372  0.44 21.88 ? 335  MET   A SD    1 
ATOM   2399  C  CE    A MET   A 1  337  ? -55.878 64.277  76.856  0.56 21.93 ? 335  MET   A CE    1 
ATOM   2400  C  CE    B MET   A 1  337  ? -55.201 63.616  76.841  0.44 15.79 ? 335  MET   A CE    1 
ATOM   2401  N  N     . GLY   A 1  338  ? -54.244 58.892  76.693  1.00 15.34 ? 336  GLY   A N     1 
ATOM   2402  C  CA    . GLY   A 1  338  ? -53.570 57.776  77.317  1.00 15.88 ? 336  GLY   A CA    1 
ATOM   2403  C  C     . GLY   A 1  338  ? -52.610 58.254  78.389  1.00 15.01 ? 336  GLY   A C     1 
ATOM   2404  O  O     . GLY   A 1  338  ? -52.216 59.414  78.425  1.00 14.90 ? 336  GLY   A O     1 
ATOM   2405  N  N     . PHE   A 1  339  ? -52.272 57.340  79.291  1.00 15.22 ? 337  PHE   A N     1 
ATOM   2406  C  CA    . PHE   A 1  339  ? -51.485 57.713  80.456  1.00 15.49 ? 337  PHE   A CA    1 
ATOM   2407  C  C     . PHE   A 1  339  ? -50.729 56.493  80.948  1.00 15.53 ? 337  PHE   A C     1 
ATOM   2408  O  O     . PHE   A 1  339  ? -51.308 55.409  81.072  1.00 16.24 ? 337  PHE   A O     1 
ATOM   2409  C  CB    . PHE   A 1  339  ? -52.444 58.217  81.535  1.00 16.72 ? 337  PHE   A CB    1 
ATOM   2410  C  CG    . PHE   A 1  339  ? -51.771 58.866  82.702  1.00 15.68 ? 337  PHE   A CG    1 
ATOM   2411  C  CD1   . PHE   A 1  339  ? -51.462 60.221  82.682  1.00 17.79 ? 337  PHE   A CD1   1 
ATOM   2412  C  CD2   . PHE   A 1  339  ? -51.469 58.124  83.836  1.00 16.18 ? 337  PHE   A CD2   1 
ATOM   2413  C  CE1   . PHE   A 1  339  ? -50.874 60.820  83.788  1.00 16.71 ? 337  PHE   A CE1   1 
ATOM   2414  C  CE2   . PHE   A 1  339  ? -50.875 58.720  84.937  1.00 18.54 ? 337  PHE   A CE2   1 
ATOM   2415  C  CZ    . PHE   A 1  339  ? -50.576 60.068  84.902  1.00 18.18 ? 337  PHE   A CZ    1 
ATOM   2416  N  N     . VAL   A 1  340  ? -49.431 56.672  81.214  1.00 15.23 ? 338  VAL   A N     1 
ATOM   2417  C  CA    . VAL   A 1  340  ? -48.567 55.587  81.654  1.00 14.85 ? 338  VAL   A CA    1 
ATOM   2418  C  C     . VAL   A 1  340  ? -48.576 55.519  83.167  1.00 16.25 ? 338  VAL   A C     1 
ATOM   2419  O  O     . VAL   A 1  340  ? -48.543 56.551  83.847  1.00 16.39 ? 338  VAL   A O     1 
ATOM   2420  C  CB    . VAL   A 1  340  ? -47.142 55.834  81.151  1.00 15.04 ? 338  VAL   A CB    1 
ATOM   2421  C  CG1   . VAL   A 1  340  ? -46.203 54.731  81.636  1.00 15.82 ? 338  VAL   A CG1   1 
ATOM   2422  C  CG2   . VAL   A 1  340  ? -47.149 55.902  79.644  1.00 15.73 ? 338  VAL   A CG2   1 
ATOM   2423  N  N     . VAL   A 1  341  ? -48.599 54.304  83.700  1.00 15.60 ? 339  VAL   A N     1 
ATOM   2424  C  CA    . VAL   A 1  341  ? -48.358 54.080  85.117  1.00 15.29 ? 339  VAL   A CA    1 
ATOM   2425  C  C     . VAL   A 1  341  ? -47.226 53.076  85.264  1.00 15.78 ? 339  VAL   A C     1 
ATOM   2426  O  O     . VAL   A 1  341  ? -47.155 52.087  84.524  1.00 17.85 ? 339  VAL   A O     1 
ATOM   2427  C  CB    . VAL   A 1  341  ? -49.614 53.622  85.881  1.00 17.82 ? 339  VAL   A CB    1 
ATOM   2428  C  CG1   . VAL   A 1  341  ? -49.361 53.757  87.354  1.00 24.31 ? 339  VAL   A CG1   1 
ATOM   2429  C  CG2   . VAL   A 1  341  ? -50.794 54.493  85.522  1.00 20.40 ? 339  VAL   A CG2   1 
ATOM   2430  N  N     . GLN   A 1  342  ? -46.337 53.340  86.217  1.00 15.67 ? 340  GLN   A N     1 
ATOM   2431  C  CA    . GLN   A 1  342  ? -45.097 52.590  86.375  1.00 16.53 ? 340  GLN   A CA    1 
ATOM   2432  C  C     . GLN   A 1  342  ? -45.256 51.601  87.524  1.00 15.94 ? 340  GLN   A C     1 
ATOM   2433  O  O     . GLN   A 1  342  ? -45.339 52.004  88.689  1.00 17.04 ? 340  GLN   A O     1 
ATOM   2434  C  CB    . GLN   A 1  342  ? -43.949 53.556  86.648  1.00 16.21 ? 340  GLN   A CB    1 
ATOM   2435  C  CG    . GLN   A 1  342  ? -43.696 54.539  85.500  1.00 14.68 ? 340  GLN   A CG    1 
ATOM   2436  C  CD    . GLN   A 1  342  ? -43.096 55.823  85.985  1.00 16.22 ? 340  GLN   A CD    1 
ATOM   2437  O  OE1   . GLN   A 1  342  ? -43.586 56.427  86.931  1.00 16.63 ? 340  GLN   A OE1   1 
ATOM   2438  N  NE2   . GLN   A 1  342  ? -42.036 56.269  85.323  1.00 14.64 ? 340  GLN   A NE2   1 
ATOM   2439  N  N     . ALA   A 1  343  ? -45.271 50.305  87.192  1.00 14.73 ? 341  ALA   A N     1 
ATOM   2440  C  CA    . ALA   A 1  343  ? -45.447 49.258  88.197  1.00 17.46 ? 341  ALA   A CA    1 
ATOM   2441  C  C     . ALA   A 1  343  ? -44.265 49.141  89.147  1.00 18.14 ? 341  ALA   A C     1 
ATOM   2442  O  O     . ALA   A 1  343  ? -44.407 48.533  90.215  1.00 18.72 ? 341  ALA   A O     1 
ATOM   2443  C  CB    . ALA   A 1  343  ? -45.724 47.920  87.524  1.00 21.04 ? 341  ALA   A CB    1 
ATOM   2444  N  N     . TYR   A 1  344  ? -43.104 49.701  88.808  1.00 17.46 ? 342  TYR   A N     1 
ATOM   2445  C  CA    . TYR   A 1  344  ? -42.045 49.723  89.811  1.00 18.15 ? 342  TYR   A CA    1 
ATOM   2446  C  C     . TYR   A 1  344  ? -42.325 50.704  90.933  1.00 19.75 ? 342  TYR   A C     1 
ATOM   2447  O  O     . TYR   A 1  344  ? -41.589 50.711  91.919  1.00 19.42 ? 342  TYR   A O     1 
ATOM   2448  C  CB    . TYR   A 1  344  ? -40.654 49.921  89.187  1.00 16.69 ? 342  TYR   A CB    1 
ATOM   2449  C  CG    . TYR   A 1  344  ? -40.226 51.297  88.684  1.00 15.52 ? 342  TYR   A CG    1 
ATOM   2450  C  CD1   . TYR   A 1  344  ? -41.080 52.397  88.644  1.00 16.52 ? 342  TYR   A CD1   1 
ATOM   2451  C  CD2   . TYR   A 1  344  ? -38.916 51.465  88.227  1.00 15.85 ? 342  TYR   A CD2   1 
ATOM   2452  C  CE1   . TYR   A 1  344  ? -40.632 53.623  88.154  1.00 16.36 ? 342  TYR   A CE1   1 
ATOM   2453  C  CE2   . TYR   A 1  344  ? -38.465 52.660  87.753  1.00 17.82 ? 342  TYR   A CE2   1 
ATOM   2454  C  CZ    . TYR   A 1  344  ? -39.308 53.744  87.716  1.00 17.87 ? 342  TYR   A CZ    1 
ATOM   2455  O  OH    . TYR   A 1  344  ? -38.811 54.930  87.233  1.00 15.91 ? 342  TYR   A OH    1 
ATOM   2456  N  N     . GLY   A 1  345  ? -43.370 51.516  90.811  1.00 16.72 ? 343  GLY   A N     1 
ATOM   2457  C  CA    . GLY   A 1  345  ? -43.680 52.498  91.821  1.00 18.20 ? 343  GLY   A CA    1 
ATOM   2458  C  C     . GLY   A 1  345  ? -44.675 51.961  92.836  1.00 17.83 ? 343  GLY   A C     1 
ATOM   2459  O  O     . GLY   A 1  345  ? -45.623 51.254  92.492  1.00 18.74 ? 343  GLY   A O     1 
ATOM   2460  N  N     . LYS   A 1  346  ? -44.451 52.338  94.091  1.00 18.00 ? 344  LYS   A N     1 
ATOM   2461  C  CA    . LYS   A 1  346  ? -45.282 51.855  95.184  1.00 19.23 ? 344  LYS   A CA    1 
ATOM   2462  C  C     . LYS   A 1  346  ? -46.706 52.387  95.116  1.00 20.00 ? 344  LYS   A C     1 
ATOM   2463  O  O     . LYS   A 1  346  ? -47.610 51.788  95.709  1.00 20.92 ? 344  LYS   A O     1 
ATOM   2464  C  CB    . LYS   A 1  346  ? -44.658 52.243  96.514  1.00 19.45 ? 344  LYS   A CB    1 
ATOM   2465  C  CG    . LYS   A 1  346  ? -43.310 51.610  96.704  1.00 17.92 ? 344  LYS   A CG    1 
ATOM   2466  C  CD    . LYS   A 1  346  ? -42.663 52.090  97.971  1.00 19.79 ? 344  LYS   A CD    1 
ATOM   2467  C  CE    . LYS   A 1  346  ? -41.433 51.248  98.263  1.00 20.00 ? 344  LYS   A CE    1 
ATOM   2468  N  NZ    . LYS   A 1  346  ? -40.657 51.813  99.392  1.00 21.82 ? 344  LYS   A NZ    1 
ATOM   2469  N  N     . ARG   A 1  347  ? -46.921 53.502  94.426  1.00 17.97 ? 345  ARG   A N     1 
ATOM   2470  C  CA    . ARG   A 1  347  ? -48.255 54.072  94.302  1.00 17.93 ? 345  ARG   A CA    1 
ATOM   2471  C  C     . ARG   A 1  347  ? -49.059 53.468  93.162  1.00 19.24 ? 345  ARG   A C     1 
ATOM   2472  O  O     . ARG   A 1  347  ? -50.261 53.734  93.080  1.00 18.66 ? 345  ARG   A O     1 
ATOM   2473  C  CB    . ARG   A 1  347  ? -48.156 55.591  94.129  1.00 18.30 ? 345  ARG   A CB    1 
ATOM   2474  C  CG    . ARG   A 1  347  ? -47.597 56.277  95.371  1.00 17.82 ? 345  ARG   A CG    1 
ATOM   2475  C  CD    . ARG   A 1  347  ? -47.196 57.701  95.084  1.00 16.94 ? 345  ARG   A CD    1 
ATOM   2476  N  NE    . ARG   A 1  347  ? -45.982 57.740  94.280  1.00 18.62 ? 345  ARG   A NE    1 
ATOM   2477  C  CZ    . ARG   A 1  347  ? -45.500 58.834  93.706  1.00 16.81 ? 345  ARG   A CZ    1 
ATOM   2478  N  NH1   . ARG   A 1  347  ? -46.098 60.006  93.841  1.00 17.52 ? 345  ARG   A NH1   1 
ATOM   2479  N  NH2   . ARG   A 1  347  ? -44.391 58.746  92.973  1.00 16.13 ? 345  ARG   A NH2   1 
ATOM   2480  N  N     . CYS   A 1  348  ? -48.446 52.649  92.311  1.00 17.82 ? 346  CYS   A N     1 
ATOM   2481  C  CA    . CYS   A 1  348  ? -49.090 52.184  91.082  1.00 18.45 ? 346  CYS   A CA    1 
ATOM   2482  C  C     . CYS   A 1  348  ? -50.523 51.696  91.248  1.00 17.54 ? 346  CYS   A C     1 
ATOM   2483  O  O     . CYS   A 1  348  ? -51.399 52.174  90.513  1.00 18.87 ? 346  CYS   A O     1 
ATOM   2484  C  CB    . CYS   A 1  348  ? -48.222 51.115  90.403  1.00 20.12 ? 346  CYS   A CB    1 
ATOM   2485  S  SG    . CYS   A 1  348  ? -48.727 50.816  88.691  1.00 23.20 ? 346  CYS   A SG    1 
ATOM   2486  N  N     . PRO   A 1  349  ? -50.832 50.751  92.136  1.00 18.93 ? 347  PRO   A N     1 
ATOM   2487  C  CA    . PRO   A 1  349  ? -52.225 50.290  92.218  1.00 20.10 ? 347  PRO   A CA    1 
ATOM   2488  C  C     . PRO   A 1  349  ? -53.187 51.389  92.631  1.00 18.58 ? 347  PRO   A C     1 
ATOM   2489  O  O     . PRO   A 1  349  ? -54.327 51.415  92.154  1.00 21.01 ? 347  PRO   A O     1 
ATOM   2490  C  CB    . PRO   A 1  349  ? -52.170 49.140  93.237  1.00 20.51 ? 347  PRO   A CB    1 
ATOM   2491  C  CG    . PRO   A 1  349  ? -50.925 49.349  93.998  1.00 22.28 ? 347  PRO   A CG    1 
ATOM   2492  C  CD    . PRO   A 1  349  ? -49.964 50.093  93.131  1.00 19.98 ? 347  PRO   A CD    1 
ATOM   2493  N  N     . PHE   A 1  350  ? -52.738 52.315  93.474  1.00 19.43 ? 348  PHE   A N     1 
ATOM   2494  C  CA    . PHE   A 1  350  ? -53.590 53.416  93.907  1.00 20.26 ? 348  PHE   A CA    1 
ATOM   2495  C  C     . PHE   A 1  350  ? -53.760 54.446  92.813  1.00 18.88 ? 348  PHE   A C     1 
ATOM   2496  O  O     . PHE   A 1  350  ? -54.835 55.038  92.681  1.00 17.99 ? 348  PHE   A O     1 
ATOM   2497  C  CB    . PHE   A 1  350  ? -52.996 54.029  95.165  1.00 20.07 ? 348  PHE   A CB    1 
ATOM   2498  C  CG    . PHE   A 1  350  ? -52.661 53.006  96.191  1.00 21.15 ? 348  PHE   A CG    1 
ATOM   2499  C  CD1   . PHE   A 1  350  ? -53.666 52.450  96.970  1.00 22.75 ? 348  PHE   A CD1   1 
ATOM   2500  C  CD2   . PHE   A 1  350  ? -51.371 52.541  96.329  1.00 20.20 ? 348  PHE   A CD2   1 
ATOM   2501  C  CE1   . PHE   A 1  350  ? -53.370 51.478  97.896  1.00 26.24 ? 348  PHE   A CE1   1 
ATOM   2502  C  CE2   . PHE   A 1  350  ? -51.070 51.561  97.253  1.00 23.36 ? 348  PHE   A CE2   1 
ATOM   2503  C  CZ    . PHE   A 1  350  ? -52.068 51.035  98.037  1.00 25.79 ? 348  PHE   A CZ    1 
ATOM   2504  N  N     . VAL   A 1  351  ? -52.717 54.650  92.013  1.00 18.03 ? 349  VAL   A N     1 
ATOM   2505  C  CA    . VAL   A 1  351  ? -52.846 55.489  90.834  1.00 18.06 ? 349  VAL   A CA    1 
ATOM   2506  C  C     . VAL   A 1  351  ? -53.860 54.887  89.877  1.00 18.84 ? 349  VAL   A C     1 
ATOM   2507  O  O     . VAL   A 1  351  ? -54.717 55.590  89.333  1.00 17.60 ? 349  VAL   A O     1 
ATOM   2508  C  CB    . VAL   A 1  351  ? -51.467 55.670  90.179  1.00 15.78 ? 349  VAL   A CB    1 
ATOM   2509  C  CG1   . VAL   A 1  351  ? -51.627 56.433  88.878  1.00 16.53 ? 349  VAL   A CG1   1 
ATOM   2510  C  CG2   . VAL   A 1  351  ? -50.532 56.421  91.115  1.00 19.17 ? 349  VAL   A CG2   1 
ATOM   2511  N  N     . LEU   A 1  352  ? -53.791 53.570  89.671  1.00 19.74 ? 350  LEU   A N     1 
ATOM   2512  C  CA    . LEU   A 1  352  ? -54.762 52.916  88.806  1.00 18.47 ? 350  LEU   A CA    1 
ATOM   2513  C  C     . LEU   A 1  352  ? -56.177 53.063  89.343  1.00 19.11 ? 350  LEU   A C     1 
ATOM   2514  O  O     . LEU   A 1  352  ? -57.106 53.308  88.570  1.00 19.62 ? 350  LEU   A O     1 
ATOM   2515  C  CB    . LEU   A 1  352  ? -54.408 51.445  88.626  1.00 19.83 ? 350  LEU   A CB    1 
ATOM   2516  C  CG    . LEU   A 1  352  ? -53.165 51.227  87.778  1.00 19.05 ? 350  LEU   A CG    1 
ATOM   2517  C  CD1   . LEU   A 1  352  ? -52.793 49.765  87.806  1.00 21.20 ? 350  LEU   A CD1   1 
ATOM   2518  C  CD2   . LEU   A 1  352  ? -53.414 51.694  86.358  1.00 20.47 ? 350  LEU   A CD2   1 
ATOM   2519  N  N     . ASP   A 1  353  ? -56.366 52.910  90.662  1.00 19.58 ? 351  ASP   A N     1 
ATOM   2520  C  CA    . ASP   A 1  353  ? -57.697 53.133  91.227  1.00 19.64 ? 351  ASP   A CA    1 
ATOM   2521  C  C     . ASP   A 1  353  ? -58.186 54.534  90.904  1.00 16.74 ? 351  ASP   A C     1 
ATOM   2522  O  O     . ASP   A 1  353  ? -59.357 54.733  90.555  1.00 19.57 ? 351  ASP   A O     1 
ATOM   2523  C  CB    . ASP   A 1  353  ? -57.672 52.962  92.743  1.00 20.48 ? 351  ASP   A CB    1 
ATOM   2524  C  CG    . ASP   A 1  353  ? -57.462 51.524  93.174  1.00 24.01 ? 351  ASP   A CG    1 
ATOM   2525  O  OD1   . ASP   A 1  353  ? -57.788 50.604  92.395  1.00 26.35 ? 351  ASP   A OD1   1 
ATOM   2526  O  OD2   . ASP   A 1  353  ? -56.977 51.325  94.309  1.00 28.16 ? 351  ASP   A OD2   1 
ATOM   2527  N  N     . PHE   A 1  354  ? -57.303 55.523  91.039  1.00 17.77 ? 352  PHE   A N     1 
ATOM   2528  C  CA    . PHE   A 1  354  ? -57.672 56.892  90.726  1.00 16.84 ? 352  PHE   A CA    1 
ATOM   2529  C  C     . PHE   A 1  354  ? -58.040 57.027  89.258  1.00 17.05 ? 352  PHE   A C     1 
ATOM   2530  O  O     . PHE   A 1  354  ? -59.022 57.687  88.919  1.00 17.98 ? 352  PHE   A O     1 
ATOM   2531  C  CB    . PHE   A 1  354  ? -56.516 57.835  91.075  1.00 17.68 ? 352  PHE   A CB    1 
ATOM   2532  C  CG    . PHE   A 1  354  ? -56.697 59.216  90.525  1.00 19.02 ? 352  PHE   A CG    1 
ATOM   2533  C  CD1   . PHE   A 1  354  ? -57.453 60.150  91.211  1.00 19.48 ? 352  PHE   A CD1   1 
ATOM   2534  C  CD2   . PHE   A 1  354  ? -56.132 59.572  89.306  1.00 20.07 ? 352  PHE   A CD2   1 
ATOM   2535  C  CE1   . PHE   A 1  354  ? -57.650 61.422  90.692  1.00 21.29 ? 352  PHE   A CE1   1 
ATOM   2536  C  CE2   . PHE   A 1  354  ? -56.322 60.825  88.786  1.00 20.12 ? 352  PHE   A CE2   1 
ATOM   2537  C  CZ    . PHE   A 1  354  ? -57.083 61.757  89.477  1.00 19.16 ? 352  PHE   A CZ    1 
ATOM   2538  N  N     . ILE   A 1  355  ? -57.236 56.436  88.368  1.00 15.75 ? 353  ILE   A N     1 
ATOM   2539  C  CA    . ILE   A 1  355  ? -57.468 56.586  86.934  1.00 15.97 ? 353  ILE   A CA    1 
ATOM   2540  C  C     . ILE   A 1  355  ? -58.745 55.886  86.513  1.00 18.03 ? 353  ILE   A C     1 
ATOM   2541  O  O     . ILE   A 1  355  ? -59.520 56.413  85.711  1.00 18.29 ? 353  ILE   A O     1 
ATOM   2542  C  CB    . ILE   A 1  355  ? -56.262 56.065  86.144  1.00 17.58 ? 353  ILE   A CB    1 
ATOM   2543  C  CG1   . ILE   A 1  355  ? -55.061 56.982  86.359  1.00 17.77 ? 353  ILE   A CG1   1 
ATOM   2544  C  CG2   . ILE   A 1  355  ? -56.612 55.940  84.669  1.00 19.14 ? 353  ILE   A CG2   1 
ATOM   2545  C  CD1   . ILE   A 1  355  ? -53.804 56.427  85.774  1.00 19.61 ? 353  ILE   A CD1   1 
ATOM   2546  N  N     . ILE   A 1  356  ? -58.965 54.671  87.013  1.00 18.78 ? 354  ILE   A N     1 
ATOM   2547  C  CA    . ILE   A 1  356  ? -60.199 53.960  86.701  1.00 18.09 ? 354  ILE   A CA    1 
ATOM   2548  C  C     . ILE   A 1  356  ? -61.405 54.760  87.167  1.00 19.37 ? 354  ILE   A C     1 
ATOM   2549  O  O     . ILE   A 1  356  ? -62.391 54.913  86.436  1.00 18.79 ? 354  ILE   A O     1 
ATOM   2550  C  CB    . ILE   A 1  356  ? -60.152 52.546  87.302  1.00 20.44 ? 354  ILE   A CB    1 
ATOM   2551  C  CG1   . ILE   A 1  356  ? -59.058 51.743  86.597  1.00 20.41 ? 354  ILE   A CG1   1 
ATOM   2552  C  CG2   . ILE   A 1  356  ? -61.512 51.863  87.192  1.00 22.64 ? 354  ILE   A CG2   1 
ATOM   2553  C  CD1   . ILE   A 1  356  ? -58.683 50.460  87.316  1.00 20.78 ? 354  ILE   A CD1   1 
ATOM   2554  N  N     . ASP   A 1  357  ? -61.324 55.337  88.364  1.00 18.34 ? 355  ASP   A N     1 
ATOM   2555  C  CA    . ASP   A 1  357  ? -62.431 56.163  88.825  1.00 18.42 ? 355  ASP   A CA    1 
ATOM   2556  C  C     . ASP   A 1  357  ? -62.601 57.406  87.955  1.00 16.93 ? 355  ASP   A C     1 
ATOM   2557  O  O     . ASP   A 1  357  ? -63.733 57.796  87.626  1.00 19.63 ? 355  ASP   A O     1 
ATOM   2558  C  CB    . ASP   A 1  357  ? -62.222 56.560  90.277  1.00 21.10 ? 355  ASP   A CB    1 
ATOM   2559  C  CG    . ASP   A 1  357  ? -63.278 57.513  90.754  1.00 21.49 ? 355  ASP   A CG    1 
ATOM   2560  O  OD1   . ASP   A 1  357  ? -64.395 57.045  91.046  1.00 25.44 ? 355  ASP   A OD1   1 
ATOM   2561  O  OD2   . ASP   A 1  357  ? -63.010 58.727  90.810  1.00 21.94 ? 355  ASP   A OD2   1 
ATOM   2562  N  N     . LEU   A 1  358  ? -61.492 58.037  87.562  1.00 18.15 ? 356  LEU   A N     1 
ATOM   2563  C  CA    . LEU   A 1  358  ? -61.589 59.194  86.684  1.00 17.58 ? 356  LEU   A CA    1 
ATOM   2564  C  C     . LEU   A 1  358  ? -62.216 58.812  85.352  1.00 16.21 ? 356  LEU   A C     1 
ATOM   2565  O  O     . LEU   A 1  358  ? -63.038 59.558  84.807  1.00 18.02 ? 356  LEU   A O     1 
ATOM   2566  C  CB    . LEU   A 1  358  ? -60.201 59.805  86.478  1.00 16.11 ? 356  LEU   A CB    1 
ATOM   2567  C  CG    . LEU   A 1  358  ? -60.107 60.910  85.433  1.00 15.67 ? 356  LEU   A CG    1 
ATOM   2568  C  CD1   . LEU   A 1  358  ? -60.944 62.119  85.832  1.00 19.33 ? 356  LEU   A CD1   1 
ATOM   2569  C  CD2   . LEU   A 1  358  ? -58.626 61.308  85.235  1.00 16.59 ? 356  LEU   A CD2   1 
ATOM   2570  N  N     . ALA   A 1  359  ? -61.846 57.646  84.819  1.00 17.78 ? 357  ALA   A N     1 
ATOM   2571  C  CA    . ALA   A 1  359  ? -62.453 57.168  83.585  1.00 19.64 ? 357  ALA   A CA    1 
ATOM   2572  C  C     . ALA   A 1  359  ? -63.952 56.991  83.758  1.00 18.19 ? 357  ALA   A C     1 
ATOM   2573  O  O     . ALA   A 1  359  ? -64.731 57.351  82.873  1.00 18.70 ? 357  ALA   A O     1 
ATOM   2574  C  CB    . ALA   A 1  359  ? -61.805 55.849  83.158  1.00 19.97 ? 357  ALA   A CB    1 
ATOM   2575  N  N     . ARG   A 1  360  ? -64.371 56.460  84.907  1.00 17.88 ? 358  ARG   A N     1 
ATOM   2576  C  CA    . ARG   A 1  360  ? -65.799 56.319  85.178  1.00 18.99 ? 358  ARG   A CA    1 
ATOM   2577  C  C     . ARG   A 1  360  ? -66.490 57.678  85.256  1.00 21.43 ? 358  ARG   A C     1 
ATOM   2578  O  O     . ARG   A 1  360  ? -67.540 57.890  84.637  1.00 23.53 ? 358  ARG   A O     1 
ATOM   2579  C  CB    . ARG   A 1  360  ? -66.018 55.534  86.471  1.00 22.14 ? 358  ARG   A CB    1 
ATOM   2580  C  CG    . ARG   A 1  360  ? -65.626 54.071  86.402  1.00 25.54 ? 358  ARG   A CG    1 
ATOM   2581  C  CD    . ARG   A 1  360  ? -66.187 53.283  87.592  1.00 32.09 ? 358  ARG   A CD    1 
ATOM   2582  N  NE    . ARG   A 1  360  ? -65.477 52.022  87.777  1.00 34.93 ? 358  ARG   A NE    1 
ATOM   2583  C  CZ    . ARG   A 1  360  ? -65.783 50.895  87.150  1.00 41.85 ? 358  ARG   A CZ    1 
ATOM   2584  N  NH1   . ARG   A 1  360  ? -66.820 50.819  86.331  1.00 42.05 ? 358  ARG   A NH1   1 
ATOM   2585  N  NH2   . ARG   A 1  360  ? -65.025 49.819  87.344  1.00 41.33 ? 358  ARG   A NH2   1 
ATOM   2586  N  N     . ARG   A 1  361  ? -65.919 58.612  86.024  1.00 20.62 ? 359  ARG   A N     1 
ATOM   2587  C  CA    . ARG   A 1  361  ? -66.539 59.927  86.192  1.00 20.42 ? 359  ARG   A CA    1 
ATOM   2588  C  C     . ARG   A 1  361  ? -66.622 60.681  84.873  1.00 20.08 ? 359  ARG   A C     1 
ATOM   2589  O  O     . ARG   A 1  361  ? -67.636 61.325  84.571  1.00 22.13 ? 359  ARG   A O     1 
ATOM   2590  C  CB    . ARG   A 1  361  ? -65.726 60.761  87.183  1.00 22.98 ? 359  ARG   A CB    1 
ATOM   2591  C  CG    . ARG   A 1  361  ? -65.794 60.294  88.613  1.00 25.46 ? 359  ARG   A CG    1 
ATOM   2592  C  CD    . ARG   A 1  361  ? -65.082 61.279  89.513  1.00 26.23 ? 359  ARG   A CD    1 
ATOM   2593  N  NE    . ARG   A 1  361  ? -63.630 61.159  89.457  1.00 24.86 ? 359  ARG   A NE    1 
ATOM   2594  C  CZ    . ARG   A 1  361  ? -62.797 62.163  89.214  1.00 22.12 ? 359  ARG   A CZ    1 
ATOM   2595  N  NH1   . ARG   A 1  361  ? -63.235 63.357  88.850  1.00 22.05 ? 359  ARG   A NH1   1 
ATOM   2596  N  NH2   . ARG   A 1  361  ? -61.490 61.969  89.350  1.00 21.01 ? 359  ARG   A NH2   1 
ATOM   2597  N  N     . SER   A 1  362  ? -65.551 60.642  84.090  1.00 18.75 ? 360  SER   A N     1 
ATOM   2598  C  CA    . SER   A 1  362  ? -65.491 61.419  82.865  1.00 18.14 ? 360  SER   A CA    1 
ATOM   2599  C  C     . SER   A 1  362  ? -66.171 60.710  81.710  1.00 18.85 ? 360  SER   A C     1 
ATOM   2600  O  O     . SER   A 1  362  ? -66.521 61.359  80.719  1.00 20.97 ? 360  SER   A O     1 
ATOM   2601  C  CB    . SER   A 1  362  ? -64.024 61.647  82.499  1.00 19.73 ? 360  SER   A CB    1 
ATOM   2602  O  OG    . SER   A 1  362  ? -63.381 60.416  82.184  1.00 18.43 ? 360  SER   A OG    1 
ATOM   2603  N  N     . GLY   A 1  363  ? -66.350 59.397  81.811  1.00 18.47 ? 361  GLY   A N     1 
ATOM   2604  C  CA    . GLY   A 1  363  ? -66.819 58.637  80.676  1.00 20.91 ? 361  GLY   A CA    1 
ATOM   2605  C  C     . GLY   A 1  363  ? -65.802 58.456  79.574  1.00 20.86 ? 361  GLY   A C     1 
ATOM   2606  O  O     . GLY   A 1  363  ? -66.175 58.014  78.481  1.00 23.66 ? 361  GLY   A O     1 
ATOM   2607  N  N     . ARG   A 1  364  ? -64.538 58.801  79.821  1.00 19.81 ? 362  ARG   A N     1 
ATOM   2608  C  CA    . ARG   A 1  364  ? -63.467 58.622  78.849  1.00 19.73 ? 362  ARG   A CA    1 
ATOM   2609  C  C     . ARG   A 1  364  ? -62.822 57.277  79.119  1.00 19.30 ? 362  ARG   A C     1 
ATOM   2610  O  O     . ARG   A 1  364  ? -62.443 56.986  80.255  1.00 18.98 ? 362  ARG   A O     1 
ATOM   2611  C  CB    . ARG   A 1  364  ? -62.386 59.691  79.021  1.00 21.47 ? 362  ARG   A CB    1 
ATOM   2612  C  CG    . ARG   A 1  364  ? -62.865 61.127  79.074  1.00 26.09 ? 362  ARG   A CG    1 
ATOM   2613  C  CD    . ARG   A 1  364  ? -62.905 61.793  77.715  1.00 18.76 ? 362  ARG   A CD    1 
ATOM   2614  N  NE    . ARG   A 1  364  ? -63.719 63.002  77.797  1.00 18.06 ? 362  ARG   A NE    1 
ATOM   2615  C  CZ    . ARG   A 1  364  ? -63.243 64.231  77.930  1.00 18.65 ? 362  ARG   A CZ    1 
ATOM   2616  N  NH1   . ARG   A 1  364  ? -61.945 64.481  77.888  1.00 17.45 ? 362  ARG   A NH1   1 
ATOM   2617  N  NH2   . ARG   A 1  364  ? -64.093 65.237  78.106  1.00 18.04 ? 362  ARG   A NH2   1 
ATOM   2618  N  N     . ARG   A 1  365  ? -62.688 56.461  78.080  1.00 17.55 ? 363  ARG   A N     1 
ATOM   2619  C  CA    . ARG   A 1  365  ? -62.055 55.158  78.230  1.00 16.00 ? 363  ARG   A CA    1 
ATOM   2620  C  C     . ARG   A 1  365  ? -60.549 55.385  78.140  1.00 18.71 ? 363  ARG   A C     1 
ATOM   2621  O  O     . ARG   A 1  365  ? -59.922 55.254  77.084  1.00 19.84 ? 363  ARG   A O     1 
ATOM   2622  C  CB    . ARG   A 1  365  ? -62.544 54.203  77.159  1.00 18.61 ? 363  ARG   A CB    1 
ATOM   2623  C  CG    . ARG   A 1  365  ? -61.999 52.814  77.356  1.00 19.29 ? 363  ARG   A CG    1 
ATOM   2624  C  CD    . ARG   A 1  365  ? -62.877 51.783  76.714  1.00 24.19 ? 363  ARG   A CD    1 
ATOM   2625  N  NE    . ARG   A 1  365  ? -62.351 50.463  77.022  1.00 22.75 ? 363  ARG   A NE    1 
ATOM   2626  C  CZ    . ARG   A 1  365  ? -61.649 49.730  76.173  1.00 19.99 ? 363  ARG   A CZ    1 
ATOM   2627  N  NH1   . ARG   A 1  365  ? -61.473 50.109  74.916  1.00 23.75 ? 363  ARG   A NH1   1 
ATOM   2628  N  NH2   . ARG   A 1  365  ? -61.121 48.589  76.593  1.00 20.34 ? 363  ARG   A NH2   1 
ATOM   2629  N  N     . ILE   A 1  366  ? -59.966 55.741  79.284  1.00 16.82 ? 364  ILE   A N     1 
ATOM   2630  C  CA    . ILE   A 1  366  ? -58.570 56.150  79.305  1.00 17.25 ? 364  ILE   A CA    1 
ATOM   2631  C  C     . ILE   A 1  366  ? -57.697 54.986  78.880  1.00 18.45 ? 364  ILE   A C     1 
ATOM   2632  O  O     . ILE   A 1  366  ? -57.865 53.855  79.351  1.00 17.40 ? 364  ILE   A O     1 
ATOM   2633  C  CB    . ILE   A 1  366  ? -58.195 56.667  80.698  1.00 16.86 ? 364  ILE   A CB    1 
ATOM   2634  C  CG1   . ILE   A 1  366  ? -59.044 57.894  81.039  1.00 19.00 ? 364  ILE   A CG1   1 
ATOM   2635  C  CG2   . ILE   A 1  366  ? -56.695 56.993  80.777  1.00 19.12 ? 364  ILE   A CG2   1 
ATOM   2636  C  CD1   . ILE   A 1  366  ? -58.853 58.374  82.485  1.00 19.44 ? 364  ILE   A CD1   1 
ATOM   2637  N  N     . MET   A 1  367  ? -56.759 55.260  77.980  1.00 16.68 ? 365  MET   A N     1 
ATOM   2638  C  CA    . MET   A 1  367  ? -55.792 54.252  77.564  1.00 16.81 ? 365  MET   A CA    1 
ATOM   2639  C  C     . MET   A 1  367  ? -54.677 54.234  78.595  1.00 16.77 ? 365  MET   A C     1 
ATOM   2640  O  O     . MET   A 1  367  ? -54.000 55.243  78.796  1.00 19.92 ? 365  MET   A O     1 
ATOM   2641  C  CB    . MET   A 1  367  ? -55.250 54.584  76.175  1.00 16.37 ? 365  MET   A CB    1 
ATOM   2642  C  CG    . MET   A 1  367  ? -56.365 54.858  75.160  1.00 17.95 ? 365  MET   A CG    1 
ATOM   2643  S  SD    . MET   A 1  367  ? -55.756 55.261  73.509  1.00 19.62 ? 365  MET   A SD    1 
ATOM   2644  C  CE    . MET   A 1  367  ? -55.579 53.646  72.732  1.00 23.17 ? 365  MET   A CE    1 
ATOM   2645  N  N     . VAL   A 1  368  ? -54.505 53.118  79.280  1.00 15.30 ? 366  VAL   A N     1 
ATOM   2646  C  CA    . VAL   A 1  368  ? -53.578 53.063  80.394  1.00 15.81 ? 366  VAL   A CA    1 
ATOM   2647  C  C     . VAL   A 1  368  ? -52.447 52.153  79.975  1.00 15.88 ? 366  VAL   A C     1 
ATOM   2648  O  O     . VAL   A 1  368  ? -52.646 50.948  79.790  1.00 17.14 ? 366  VAL   A O     1 
ATOM   2649  C  CB    . VAL   A 1  368  ? -54.244 52.553  81.675  1.00 17.99 ? 366  VAL   A CB    1 
ATOM   2650  C  CG1   . VAL   A 1  368  ? -53.201 52.427  82.784  1.00 19.77 ? 366  VAL   A CG1   1 
ATOM   2651  C  CG2   . VAL   A 1  368  ? -55.386 53.472  82.079  1.00 19.45 ? 366  VAL   A CG2   1 
ATOM   2652  N  N     . ARG   A 1  369  ? -51.260 52.724  79.815  1.00 15.55 ? 367  ARG   A N     1 
ATOM   2653  C  CA    . ARG   A 1  369  ? -50.092 51.920  79.517  1.00 15.72 ? 367  ARG   A CA    1 
ATOM   2654  C  C     . ARG   A 1  369  ? -49.424 51.543  80.826  1.00 16.49 ? 367  ARG   A C     1 
ATOM   2655  O  O     . ARG   A 1  369  ? -48.939 52.411  81.558  1.00 17.60 ? 367  ARG   A O     1 
ATOM   2656  C  CB    . ARG   A 1  369  ? -49.126 52.681  78.623  1.00 16.05 ? 367  ARG   A CB    1 
ATOM   2657  C  CG    . ARG   A 1  369  ? -47.934 51.818  78.250  1.00 17.69 ? 367  ARG   A CG    1 
ATOM   2658  C  CD    . ARG   A 1  369  ? -46.764 52.641  77.801  1.00 18.46 ? 367  ARG   A CD    1 
ATOM   2659  N  NE    . ARG   A 1  369  ? -47.061 53.307  76.545  1.00 17.45 ? 367  ARG   A NE    1 
ATOM   2660  C  CZ    . ARG   A 1  369  ? -46.485 54.432  76.146  1.00 19.95 ? 367  ARG   A CZ    1 
ATOM   2661  N  NH1   . ARG   A 1  369  ? -45.537 55.021  76.864  1.00 18.67 ? 367  ARG   A NH1   1 
ATOM   2662  N  NH2   . ARG   A 1  369  ? -46.880 54.989  75.007  1.00 18.05 ? 367  ARG   A NH2   1 
ATOM   2663  N  N     . LEU   A 1  370  ? -49.401 50.250  81.110  1.00 16.56 ? 368  LEU   A N     1 
ATOM   2664  C  CA    . LEU   A 1  370  ? -48.717 49.738  82.278  1.00 16.05 ? 368  LEU   A CA    1 
ATOM   2665  C  C     . LEU   A 1  370  ? -47.297 49.398  81.856  1.00 16.36 ? 368  LEU   A C     1 
ATOM   2666  O  O     . LEU   A 1  370  ? -47.090 48.605  80.933  1.00 16.32 ? 368  LEU   A O     1 
ATOM   2667  C  CB    . LEU   A 1  370  ? -49.440 48.497  82.795  1.00 16.58 ? 368  LEU   A CB    1 
ATOM   2668  C  CG    . LEU   A 1  370  ? -48.909 47.949  84.108  1.00 18.04 ? 368  LEU   A CG    1 
ATOM   2669  C  CD1   . LEU   A 1  370  ? -49.129 48.943  85.241  1.00 21.22 ? 368  LEU   A CD1   1 
ATOM   2670  C  CD2   . LEU   A 1  370  ? -49.588 46.619  84.415  1.00 20.71 ? 368  LEU   A CD2   1 
ATOM   2671  N  N     . VAL   A 1  371  ? -46.324 50.015  82.515  1.00 15.72 ? 369  VAL   A N     1 
ATOM   2672  C  CA    . VAL   A 1  371  ? -44.920 49.739  82.271  1.00 15.93 ? 369  VAL   A CA    1 
ATOM   2673  C  C     . VAL   A 1  371  ? -44.312 49.363  83.601  1.00 16.75 ? 369  VAL   A C     1 
ATOM   2674  O  O     . VAL   A 1  371  ? -44.932 49.513  84.652  1.00 17.78 ? 369  VAL   A O     1 
ATOM   2675  C  CB    . VAL   A 1  371  ? -44.182 50.954  81.693  1.00 15.41 ? 369  VAL   A CB    1 
ATOM   2676  C  CG1   . VAL   A 1  371  ? -44.880 51.443  80.451  1.00 17.59 ? 369  VAL   A CG1   1 
ATOM   2677  C  CG2   . VAL   A 1  371  ? -44.065 52.057  82.748  1.00 16.84 ? 369  VAL   A CG2   1 
ATOM   2678  N  N     . LYS   A 1  372  ? -43.067 48.895  83.561  1.00 17.45 ? 370  LYS   A N     1 
ATOM   2679  C  CA    . LYS   A 1  372  ? -42.368 48.711  84.828  1.00 18.55 ? 370  LYS   A CA    1 
ATOM   2680  C  C     . LYS   A 1  372  ? -41.765 50.020  85.329  1.00 17.95 ? 370  LYS   A C     1 
ATOM   2681  O  O     . LYS   A 1  372  ? -42.164 50.530  86.381  1.00 21.34 ? 370  LYS   A O     1 
ATOM   2682  C  CB    . LYS   A 1  372  ? -41.411 47.520  84.755  1.00 18.89 ? 370  LYS   A CB    1 
ATOM   2683  C  CG    . LYS   A 1  372  ? -42.240 46.238  84.654  1.00 20.61 ? 370  LYS   A CG    1 
ATOM   2684  C  CD    . LYS   A 1  372  ? -41.432 44.953  84.564  1.00 20.77 ? 370  LYS   A CD    1 
ATOM   2685  C  CE    . LYS   A 1  372  ? -42.379 43.793  84.210  1.00 20.90 ? 370  LYS   A CE    1 
ATOM   2686  N  NZ    . LYS   A 1  372  ? -41.608 42.539  83.934  1.00 20.62 ? 370  LYS   A NZ    1 
ATOM   2687  N  N     . GLY   A 1  373  ? -40.877 50.625  84.563  1.00 16.85 ? 371  GLY   A N     1 
ATOM   2688  C  CA    . GLY   A 1  373  ? -40.423 51.976  84.864  1.00 16.96 ? 371  GLY   A CA    1 
ATOM   2689  C  C     . GLY   A 1  373  ? -38.984 52.145  84.404  1.00 16.65 ? 371  GLY   A C     1 
ATOM   2690  O  O     . GLY   A 1  373  ? -38.165 51.244  84.468  1.00 17.22 ? 371  GLY   A O     1 
ATOM   2691  N  N     . ALA   A 1  374  ? -38.666 53.354  83.944  1.00 16.77 ? 372  ALA   A N     1 
ATOM   2692  C  CA    . ALA   A 1  374  ? -37.412 53.595  83.228  1.00 15.45 ? 372  ALA   A CA    1 
ATOM   2693  C  C     . ALA   A 1  374  ? -36.345 54.322  84.037  1.00 18.13 ? 372  ALA   A C     1 
ATOM   2694  O  O     . ALA   A 1  374  ? -35.224 54.485  83.543  1.00 19.34 ? 372  ALA   A O     1 
ATOM   2695  C  CB    . ALA   A 1  374  ? -37.668 54.386  81.947  1.00 17.58 ? 372  ALA   A CB    1 
ATOM   2696  N  N     . TYR   A 1  375  ? -36.645 54.761  85.257  1.00 16.88 ? 373  TYR   A N     1 
ATOM   2697  C  CA    . TYR   A 1  375  ? -35.770 55.669  85.989  1.00 16.72 ? 373  TYR   A CA    1 
ATOM   2698  C  C     . TYR   A 1  375  ? -35.283 55.062  87.294  1.00 15.80 ? 373  TYR   A C     1 
ATOM   2699  O  O     . TYR   A 1  375  ? -34.987 55.797  88.231  1.00 17.22 ? 373  TYR   A O     1 
ATOM   2700  C  CB    . TYR   A 1  375  ? -36.495 56.977  86.309  1.00 17.60 ? 373  TYR   A CB    1 
ATOM   2701  C  CG    . TYR   A 1  375  ? -37.061 57.682  85.116  1.00 16.15 ? 373  TYR   A CG    1 
ATOM   2702  C  CD1   . TYR   A 1  375  ? -38.264 57.276  84.550  1.00 15.92 ? 373  TYR   A CD1   1 
ATOM   2703  C  CD2   . TYR   A 1  375  ? -36.406 58.771  84.561  1.00 20.00 ? 373  TYR   A CD2   1 
ATOM   2704  C  CE1   . TYR   A 1  375  ? -38.783 57.929  83.449  1.00 17.45 ? 373  TYR   A CE1   1 
ATOM   2705  C  CE2   . TYR   A 1  375  ? -36.924 59.434  83.469  1.00 20.41 ? 373  TYR   A CE2   1 
ATOM   2706  C  CZ    . TYR   A 1  375  ? -38.112 59.001  82.921  1.00 21.36 ? 373  TYR   A CZ    1 
ATOM   2707  O  OH    . TYR   A 1  375  ? -38.641 59.654  81.830  1.00 24.03 ? 373  TYR   A OH    1 
ATOM   2708  N  N     . TRP   A 1  376  ? -35.164 53.739  87.355  1.00 15.39 ? 374  TRP   A N     1 
ATOM   2709  C  CA    . TRP   A 1  376  ? -34.949 53.079  88.643  1.00 16.74 ? 374  TRP   A CA    1 
ATOM   2710  C  C     . TRP   A 1  376  ? -33.682 53.572  89.341  1.00 17.46 ? 374  TRP   A C     1 
ATOM   2711  O  O     . TRP   A 1  376  ? -33.732 53.982  90.509  1.00 18.60 ? 374  TRP   A O     1 
ATOM   2712  C  CB    . TRP   A 1  376  ? -34.929 51.564  88.478  1.00 18.44 ? 374  TRP   A CB    1 
ATOM   2713  C  CG    . TRP   A 1  376  ? -34.785 50.863  89.789  1.00 19.16 ? 374  TRP   A CG    1 
ATOM   2714  C  CD1   . TRP   A 1  376  ? -35.767 50.636  90.699  1.00 18.16 ? 374  TRP   A CD1   1 
ATOM   2715  C  CD2   . TRP   A 1  376  ? -33.583 50.319  90.348  1.00 18.58 ? 374  TRP   A CD2   1 
ATOM   2716  N  NE1   . TRP   A 1  376  ? -35.258 49.981  91.792  1.00 19.33 ? 374  TRP   A NE1   1 
ATOM   2717  C  CE2   . TRP   A 1  376  ? -33.917 49.776  91.602  1.00 18.87 ? 374  TRP   A CE2   1 
ATOM   2718  C  CE3   . TRP   A 1  376  ? -32.258 50.250  89.914  1.00 20.33 ? 374  TRP   A CE3   1 
ATOM   2719  C  CZ2   . TRP   A 1  376  ? -32.977 49.155  92.425  1.00 21.72 ? 374  TRP   A CZ2   1 
ATOM   2720  C  CZ3   . TRP   A 1  376  ? -31.326 49.629  90.730  1.00 23.16 ? 374  TRP   A CZ3   1 
ATOM   2721  C  CH2   . TRP   A 1  376  ? -31.689 49.097  91.972  1.00 22.85 ? 374  TRP   A CH2   1 
ATOM   2722  N  N     . ASP   A 1  377  ? -32.531 53.519  88.647  1.00 18.46 ? 375  ASP   A N     1 
ATOM   2723  C  CA    . ASP   A 1  377  ? -31.260 53.943  89.245  1.00 20.15 ? 375  ASP   A CA    1 
ATOM   2724  C  C     . ASP   A 1  377  ? -31.357 55.348  89.787  1.00 18.72 ? 375  ASP   A C     1 
ATOM   2725  O  O     . ASP   A 1  377  ? -30.850 55.645  90.874  1.00 17.95 ? 375  ASP   A O     1 
ATOM   2726  C  CB    . ASP   A 1  377  ? -30.159 54.007  88.186  1.00 27.46 ? 375  ASP   A CB    1 
ATOM   2727  C  CG    . ASP   A 1  377  ? -29.749 52.670  87.665  1.00 38.94 ? 375  ASP   A CG    1 
ATOM   2728  O  OD1   . ASP   A 1  377  ? -29.834 51.680  88.412  1.00 40.91 ? 375  ASP   A OD1   1 
ATOM   2729  O  OD2   . ASP   A 1  377  ? -29.306 52.631  86.493  1.00 42.47 ? 375  ASP   A OD2   1 
ATOM   2730  N  N     . ALA   A 1  378  ? -31.979 56.237  89.016  1.00 16.71 ? 376  ALA   A N     1 
ATOM   2731  C  CA    . ALA   A 1  378  ? -32.043 57.631  89.399  1.00 17.45 ? 376  ALA   A CA    1 
ATOM   2732  C  C     . ALA   A 1  378  ? -32.938 57.820  90.605  1.00 16.01 ? 376  ALA   A C     1 
ATOM   2733  O  O     . ALA   A 1  378  ? -32.676 58.701  91.430  1.00 16.38 ? 376  ALA   A O     1 
ATOM   2734  C  CB    . ALA   A 1  378  ? -32.547 58.464  88.218  1.00 16.92 ? 376  ALA   A CB    1 
ATOM   2735  N  N     . GLU   A 1  379  ? -34.006 57.024  90.713  1.00 16.04 ? 377  GLU   A N     1 
ATOM   2736  C  CA    . GLU   A 1  379  ? -34.876 57.145  91.877  1.00 16.60 ? 377  GLU   A CA    1 
ATOM   2737  C  C     . GLU   A 1  379  ? -34.157 56.706  93.141  1.00 16.33 ? 377  GLU   A C     1 
ATOM   2738  O  O     . GLU   A 1  379  ? -34.365 57.292  94.211  1.00 18.15 ? 377  GLU   A O     1 
ATOM   2739  C  CB    . GLU   A 1  379  ? -36.141 56.316  91.694  1.00 16.70 ? 377  GLU   A CB    1 
ATOM   2740  C  CG    . GLU   A 1  379  ? -36.986 56.708  90.480  1.00 18.29 ? 377  GLU   A CG    1 
ATOM   2741  C  CD    . GLU   A 1  379  ? -37.610 58.092  90.580  1.00 18.09 ? 377  GLU   A CD    1 
ATOM   2742  O  OE1   . GLU   A 1  379  ? -37.495 58.763  91.631  1.00 18.49 ? 377  GLU   A OE1   1 
ATOM   2743  O  OE2   . GLU   A 1  379  ? -38.232 58.506  89.577  1.00 18.53 ? 377  GLU   A OE2   1 
ATOM   2744  N  N     . ILE   A 1  380  ? -33.299 55.686  93.035  1.00 16.40 ? 378  ILE   A N     1 
ATOM   2745  C  CA    . ILE   A 1  380  ? -32.551 55.245  94.209  1.00 17.20 ? 378  ILE   A CA    1 
ATOM   2746  C  C     . ILE   A 1  380  ? -31.596 56.340  94.652  1.00 17.58 ? 378  ILE   A C     1 
ATOM   2747  O  O     . ILE   A 1  380  ? -31.523 56.691  95.835  1.00 17.87 ? 378  ILE   A O     1 
ATOM   2748  C  CB    . ILE   A 1  380  ? -31.797 53.937  93.911  1.00 17.64 ? 378  ILE   A CB    1 
ATOM   2749  C  CG1   . ILE   A 1  380  ? -32.742 52.834  93.443  1.00 18.29 ? 378  ILE   A CG1   1 
ATOM   2750  C  CG2   . ILE   A 1  380  ? -30.996 53.480  95.131  1.00 19.98 ? 378  ILE   A CG2   1 
ATOM   2751  C  CD1   . ILE   A 1  380  ? -33.844 52.485  94.439  1.00 19.38 ? 378  ILE   A CD1   1 
ATOM   2752  N  N     . LYS   A 1  381  ? -30.856 56.909  93.700  1.00 15.72 ? 379  LYS   A N     1 
ATOM   2753  C  CA    . LYS   A 1  381  ? -29.899 57.953  94.034  1.00 15.86 ? 379  LYS   A CA    1 
ATOM   2754  C  C     . LYS   A 1  381  ? -30.591 59.163  94.637  1.00 16.74 ? 379  LYS   A C     1 
ATOM   2755  O  O     . LYS   A 1  381  ? -30.144 59.706  95.650  1.00 16.35 ? 379  LYS   A O     1 
ATOM   2756  C  CB    . LYS   A 1  381  ? -29.102 58.359  92.795  1.00 16.11 ? 379  LYS   A CB    1 
ATOM   2757  C  CG    . LYS   A 1  381  ? -28.130 59.486  93.071  1.00 16.88 ? 379  LYS   A CG    1 
ATOM   2758  C  CD    . LYS   A 1  381  ? -27.248 59.763  91.855  1.00 17.86 ? 379  LYS   A CD    1 
ATOM   2759  C  CE    . LYS   A 1  381  ? -26.244 60.852  92.163  1.00 20.39 ? 379  LYS   A CE    1 
ATOM   2760  N  NZ    . LYS   A 1  381  ? -25.352 61.112  90.979  1.00 17.25 ? 379  LYS   A NZ    1 
ATOM   2761  N  N     . ARG   A 1  382  ? -31.698 59.594  94.029  1.00 16.58 ? 380  ARG   A N     1 
ATOM   2762  C  CA    . ARG   A 1  382  ? -32.355 60.809  94.489  1.00 15.90 ? 380  ARG   A CA    1 
ATOM   2763  C  C     . ARG   A 1  382  ? -32.873 60.656  95.906  1.00 17.20 ? 380  ARG   A C     1 
ATOM   2764  O  O     . ARG   A 1  382  ? -32.722 61.566  96.721  1.00 18.43 ? 380  ARG   A O     1 
ATOM   2765  C  CB    . ARG   A 1  382  ? -33.500 61.183  93.548  1.00 17.61 ? 380  ARG   A CB    1 
ATOM   2766  C  CG    . ARG   A 1  382  ? -34.176 62.476  93.919  1.00 23.08 ? 380  ARG   A CG    1 
ATOM   2767  C  CD    . ARG   A 1  382  ? -33.214 63.645  93.762  1.00 31.21 ? 380  ARG   A CD    1 
ATOM   2768  N  NE    . ARG   A 1  382  ? -33.827 64.864  94.270  1.00 42.09 ? 380  ARG   A NE    1 
ATOM   2769  C  CZ    . ARG   A 1  382  ? -34.693 65.601  93.591  1.00 49.89 ? 380  ARG   A CZ    1 
ATOM   2770  N  NH1   . ARG   A 1  382  ? -35.004 65.321  92.334  1.00 47.62 ? 380  ARG   A NH1   1 
ATOM   2771  N  NH2   . ARG   A 1  382  ? -35.270 66.639  94.191  1.00 48.55 ? 380  ARG   A NH2   1 
ATOM   2772  N  N     . ALA   A 1  383  ? -33.478 59.510  96.223  1.00 16.08 ? 381  ALA   A N     1 
ATOM   2773  C  CA    . ALA   A 1  383  ? -33.999 59.325  97.572  1.00 17.23 ? 381  ALA   A CA    1 
ATOM   2774  C  C     . ALA   A 1  383  ? -32.862 59.317  98.580  1.00 17.77 ? 381  ALA   A C     1 
ATOM   2775  O  O     . ALA   A 1  383  ? -32.987 59.874  99.675  1.00 18.70 ? 381  ALA   A O     1 
ATOM   2776  C  CB    . ALA   A 1  383  ? -34.817 58.035  97.654  1.00 19.39 ? 381  ALA   A CB    1 
ATOM   2777  N  N     . GLN   A 1  384  ? -31.733 58.710  98.215  1.00 17.08 ? 382  GLN   A N     1 
ATOM   2778  C  CA    . GLN   A 1  384  ? -30.581 58.719  99.114  1.00 17.62 ? 382  GLN   A CA    1 
ATOM   2779  C  C     . GLN   A 1  384  ? -30.050 60.135  99.305  1.00 19.23 ? 382  GLN   A C     1 
ATOM   2780  O  O     . GLN   A 1  384  ? -29.790 60.560  100.437 1.00 20.21 ? 382  GLN   A O     1 
ATOM   2781  C  CB    . GLN   A 1  384  ? -29.497 57.785  98.576  1.00 16.47 ? 382  GLN   A CB    1 
ATOM   2782  C  CG    . GLN   A 1  384  ? -29.862 56.318  98.674  1.00 18.18 ? 382  GLN   A CG    1 
ATOM   2783  C  CD    . GLN   A 1  384  ? -28.706 55.428  98.289  1.00 20.97 ? 382  GLN   A CD    1 
ATOM   2784  O  OE1   . GLN   A 1  384  ? -27.756 55.878  97.666  1.00 21.54 ? 382  GLN   A OE1   1 
ATOM   2785  N  NE2   . GLN   A 1  384  ? -28.777 54.165  98.667  1.00 19.78 ? 382  GLN   A NE2   1 
ATOM   2786  N  N     . LEU   A 1  385  ? -29.878 60.885  98.210  1.00 17.57 ? 383  LEU   A N     1 
ATOM   2787  C  CA    . LEU   A 1  385  ? -29.377 62.253  98.322  1.00 18.10 ? 383  LEU   A CA    1 
ATOM   2788  C  C     . LEU   A 1  385  ? -30.290 63.101  99.192  1.00 19.88 ? 383  LEU   A C     1 
ATOM   2789  O  O     . LEU   A 1  385  ? -29.819 63.935  99.973  1.00 20.87 ? 383  LEU   A O     1 
ATOM   2790  C  CB    . LEU   A 1  385  ? -29.271 62.897  96.937  1.00 17.23 ? 383  LEU   A CB    1 
ATOM   2791  C  CG    . LEU   A 1  385  ? -28.137 62.453  96.013  1.00 20.92 ? 383  LEU   A CG    1 
ATOM   2792  C  CD1   . LEU   A 1  385  ? -28.310 63.130  94.668  1.00 22.16 ? 383  LEU   A CD1   1 
ATOM   2793  C  CD2   . LEU   A 1  385  ? -26.802 62.828  96.599  1.00 23.75 ? 383  LEU   A CD2   1 
ATOM   2794  N  N     . ASP   A 1  386  ? -31.600 62.905  99.071  1.00 18.76 ? 384  ASP   A N     1 
ATOM   2795  C  CA    . ASP   A 1  386  ? -32.560 63.746  99.761  1.00 19.43 ? 384  ASP   A CA    1 
ATOM   2796  C  C     . ASP   A 1  386  ? -32.837 63.271  101.179 1.00 20.16 ? 384  ASP   A C     1 
ATOM   2797  O  O     . ASP   A 1  386  ? -33.589 63.929  101.906 1.00 19.95 ? 384  ASP   A O     1 
ATOM   2798  C  CB    . ASP   A 1  386  ? -33.847 63.860  98.933  1.00 21.00 ? 384  ASP   A CB    1 
ATOM   2799  C  CG    . ASP   A 1  386  ? -33.663 64.706  97.680  1.00 28.74 ? 384  ASP   A CG    1 
ATOM   2800  O  OD1   . ASP   A 1  386  ? -32.602 65.361  97.533  1.00 27.79 ? 384  ASP   A OD1   1 
ATOM   2801  O  OD2   . ASP   A 1  386  ? -34.578 64.709  96.829  1.00 28.95 ? 384  ASP   A OD2   1 
ATOM   2802  N  N     . GLY   A 1  387  ? -32.237 62.159  101.593 1.00 18.94 ? 385  GLY   A N     1 
ATOM   2803  C  CA    . GLY   A 1  387  ? -32.406 61.688  102.958 1.00 19.01 ? 385  GLY   A CA    1 
ATOM   2804  C  C     . GLY   A 1  387  ? -33.841 61.344  103.282 1.00 19.97 ? 385  GLY   A C     1 
ATOM   2805  O  O     . GLY   A 1  387  ? -34.306 61.609  104.397 1.00 20.80 ? 385  GLY   A O     1 
ATOM   2806  N  N     . LEU   A 1  388  ? -34.554 60.750  102.342 1.00 20.42 ? 386  LEU   A N     1 
ATOM   2807  C  CA    . LEU   A 1  388  ? -35.971 60.511  102.566 1.00 22.34 ? 386  LEU   A CA    1 
ATOM   2808  C  C     . LEU   A 1  388  ? -36.200 59.160  103.238 1.00 23.04 ? 386  LEU   A C     1 
ATOM   2809  O  O     . LEU   A 1  388  ? -35.293 58.336  103.389 1.00 22.72 ? 386  LEU   A O     1 
ATOM   2810  C  CB    . LEU   A 1  388  ? -36.748 60.674  101.260 1.00 19.33 ? 386  LEU   A CB    1 
ATOM   2811  C  CG    . LEU   A 1  388  ? -36.573 62.074  100.661 1.00 21.90 ? 386  LEU   A CG    1 
ATOM   2812  C  CD1   . LEU   A 1  388  ? -37.301 62.241  99.325  1.00 22.55 ? 386  LEU   A CD1   1 
ATOM   2813  C  CD2   . LEU   A 1  388  ? -37.004 63.164  101.639 1.00 21.74 ? 386  LEU   A CD2   1 
ATOM   2814  N  N     . ALA   A 1  389  ? -37.438 58.951  103.693 1.00 23.99 ? 387  ALA   A N     1 
ATOM   2815  C  CA    . ALA   A 1  389  ? -37.712 57.806  104.552 1.00 25.55 ? 387  ALA   A CA    1 
ATOM   2816  C  C     . ALA   A 1  389  ? -37.496 56.486  103.827 1.00 25.98 ? 387  ALA   A C     1 
ATOM   2817  O  O     . ALA   A 1  389  ? -37.085 55.498  104.443 1.00 26.11 ? 387  ALA   A O     1 
ATOM   2818  C  CB    . ALA   A 1  389  ? -39.138 57.894  105.098 1.00 27.02 ? 387  ALA   A CB    1 
ATOM   2819  N  N     . ASP   A 1  390  ? -37.767 56.443  102.531 1.00 20.97 ? 388  ASP   A N     1 
ATOM   2820  C  CA    . ASP   A 1  390  ? -37.727 55.192  101.787 1.00 22.18 ? 388  ASP   A CA    1 
ATOM   2821  C  C     . ASP   A 1  390  ? -37.761 55.573  100.316 1.00 19.61 ? 388  ASP   A C     1 
ATOM   2822  O  O     . ASP   A 1  390  ? -37.794 56.756  99.967  1.00 20.41 ? 388  ASP   A O     1 
ATOM   2823  C  CB    . ASP   A 1  390  ? -38.912 54.301  102.183 1.00 22.36 ? 388  ASP   A CB    1 
ATOM   2824  C  CG    . ASP   A 1  390  ? -38.643 52.818  101.975 1.00 25.15 ? 388  ASP   A CG    1 
ATOM   2825  O  OD1   . ASP   A 1  390  ? -38.006 52.443  100.975 1.00 25.38 ? 388  ASP   A OD1   1 
ATOM   2826  O  OD2   . ASP   A 1  390  ? -39.083 52.012  102.819 1.00 28.93 ? 388  ASP   A OD2   1 
ATOM   2827  N  N     . PHE   A 1  391  ? -37.732 54.580  99.474  1.00 19.13 ? 389  PHE   A N     1 
ATOM   2828  C  CA    . PHE   A 1  391  ? -37.743 54.814  98.045  1.00 17.86 ? 389  PHE   A CA    1 
ATOM   2829  C  C     . PHE   A 1  391  ? -39.176 54.837  97.540  1.00 20.66 ? 389  PHE   A C     1 
ATOM   2830  O  O     . PHE   A 1  391  ? -40.066 54.228  98.144  1.00 19.92 ? 389  PHE   A O     1 
ATOM   2831  C  CB    . PHE   A 1  391  ? -36.974 53.701  97.349  1.00 18.95 ? 389  PHE   A CB    1 
ATOM   2832  C  CG    . PHE   A 1  391  ? -35.568 53.591  97.827  1.00 18.84 ? 389  PHE   A CG    1 
ATOM   2833  C  CD1   . PHE   A 1  391  ? -34.640 54.526  97.431  1.00 19.78 ? 389  PHE   A CD1   1 
ATOM   2834  C  CD2   . PHE   A 1  391  ? -35.194 52.613  98.730  1.00 20.00 ? 389  PHE   A CD2   1 
ATOM   2835  C  CE1   . PHE   A 1  391  ? -33.341 54.473  97.880  1.00 20.91 ? 389  PHE   A CE1   1 
ATOM   2836  C  CE2   . PHE   A 1  391  ? -33.885 52.559  99.194  1.00 20.55 ? 389  PHE   A CE2   1 
ATOM   2837  C  CZ    . PHE   A 1  391  ? -32.968 53.487  98.768  1.00 19.70 ? 389  PHE   A CZ    1 
ATOM   2838  N  N     . PRO   A 1  392  ? -39.424 55.560  96.450  1.00 17.80 ? 390  PRO   A N     1 
ATOM   2839  C  CA    . PRO   A 1  392  ? -40.753 55.545  95.826  1.00 17.82 ? 390  PRO   A CA    1 
ATOM   2840  C  C     . PRO   A 1  392  ? -40.922 54.426  94.810  1.00 16.57 ? 390  PRO   A C     1 
ATOM   2841  O  O     . PRO   A 1  392  ? -41.953 54.357  94.127  1.00 20.36 ? 390  PRO   A O     1 
ATOM   2842  C  CB    . PRO   A 1  392  ? -40.788 56.911  95.138  1.00 16.70 ? 390  PRO   A CB    1 
ATOM   2843  C  CG    . PRO   A 1  392  ? -39.350 57.114  94.684  1.00 16.11 ? 390  PRO   A CG    1 
ATOM   2844  C  CD    . PRO   A 1  392  ? -38.489 56.466  95.762  1.00 17.82 ? 390  PRO   A CD    1 
ATOM   2845  N  N     . VAL   A 1  393  ? -39.913 53.567  94.688  1.00 17.49 ? 391  VAL   A N     1 
ATOM   2846  C  CA    . VAL   A 1  393  ? -39.925 52.424  93.795  1.00 16.75 ? 391  VAL   A CA    1 
ATOM   2847  C  C     . VAL   A 1  393  ? -39.494 51.212  94.599  1.00 19.03 ? 391  VAL   A C     1 
ATOM   2848  O  O     . VAL   A 1  393  ? -38.884 51.329  95.664  1.00 20.31 ? 391  VAL   A O     1 
ATOM   2849  C  CB    . VAL   A 1  393  ? -38.979 52.608  92.588  1.00 17.12 ? 391  VAL   A CB    1 
ATOM   2850  C  CG1   . VAL   A 1  393  ? -39.457 53.765  91.705  1.00 18.39 ? 391  VAL   A CG1   1 
ATOM   2851  C  CG2   . VAL   A 1  393  ? -37.563 52.870  93.053  1.00 18.46 ? 391  VAL   A CG2   1 
ATOM   2852  N  N     . PHE   A 1  394  ? -39.823 50.037  94.076  1.00 18.90 ? 392  PHE   A N     1 
ATOM   2853  C  CA    . PHE   A 1  394  ? -39.322 48.813  94.681  1.00 18.60 ? 392  PHE   A CA    1 
ATOM   2854  C  C     . PHE   A 1  394  ? -37.814 48.715  94.491  1.00 18.10 ? 392  PHE   A C     1 
ATOM   2855  O  O     . PHE   A 1  394  ? -37.222 49.392  93.652  1.00 20.55 ? 392  PHE   A O     1 
ATOM   2856  C  CB    . PHE   A 1  394  ? -40.046 47.607  94.102  1.00 19.86 ? 392  PHE   A CB    1 
ATOM   2857  C  CG    . PHE   A 1  394  ? -41.512 47.658  94.341  1.00 19.53 ? 392  PHE   A CG    1 
ATOM   2858  C  CD1   . PHE   A 1  394  ? -41.999 47.593  95.633  1.00 22.53 ? 392  PHE   A CD1   1 
ATOM   2859  C  CD2   . PHE   A 1  394  ? -42.395 47.829  93.296  1.00 18.80 ? 392  PHE   A CD2   1 
ATOM   2860  C  CE1   . PHE   A 1  394  ? -43.354 47.672  95.884  1.00 20.82 ? 392  PHE   A CE1   1 
ATOM   2861  C  CE2   . PHE   A 1  394  ? -43.764 47.902  93.538  1.00 19.65 ? 392  PHE   A CE2   1 
ATOM   2862  C  CZ    . PHE   A 1  394  ? -44.241 47.821  94.840  1.00 20.55 ? 392  PHE   A CZ    1 
ATOM   2863  N  N     . THR   A 1  395  ? -37.182 47.892  95.324  1.00 19.60 ? 393  THR   A N     1 
ATOM   2864  C  CA    . THR   A 1  395  ? -35.742 47.703  95.247  1.00 22.33 ? 393  THR   A CA    1 
ATOM   2865  C  C     . THR   A 1  395  ? -35.343 46.306  94.811  1.00 21.62 ? 393  THR   A C     1 
ATOM   2866  O  O     . THR   A 1  395  ? -34.161 46.084  94.523  1.00 21.70 ? 393  THR   A O     1 
ATOM   2867  C  CB    . THR   A 1  395  ? -35.055 48.018  96.581  1.00 20.97 ? 393  THR   A CB    1 
ATOM   2868  O  OG1   . THR   A 1  395  ? -35.588 47.168  97.606  1.00 22.67 ? 393  THR   A OG1   1 
ATOM   2869  C  CG2   . THR   A 1  395  ? -35.245 49.482  96.947  1.00 22.37 ? 393  THR   A CG2   1 
ATOM   2870  N  N     . ARG   A 1  396  ? -36.278 45.370  94.749  1.00 21.64 ? 394  ARG   A N     1 
ATOM   2871  C  CA    . ARG   A 1  396  ? -36.030 44.067  94.157  1.00 22.73 ? 394  ARG   A CA    1 
ATOM   2872  C  C     . ARG   A 1  396  ? -36.812 43.977  92.861  1.00 21.74 ? 394  ARG   A C     1 
ATOM   2873  O  O     . ARG   A 1  396  ? -38.004 44.312  92.818  1.00 22.19 ? 394  ARG   A O     1 
ATOM   2874  C  CB    . ARG   A 1  396  ? -36.435 42.930  95.089  1.00 24.17 ? 394  ARG   A CB    1 
ATOM   2875  C  CG    . ARG   A 1  396  ? -35.640 42.884  96.358  1.00 26.15 ? 394  ARG   A CG    1 
ATOM   2876  C  CD    . ARG   A 1  396  ? -35.951 41.615  97.142  1.00 30.95 ? 394  ARG   A CD    1 
ATOM   2877  N  NE    . ARG   A 1  396  ? -35.360 41.685  98.469  1.00 30.58 ? 394  ARG   A NE    1 
ATOM   2878  C  CZ    . ARG   A 1  396  ? -34.557 40.767  98.987  1.00 37.73 ? 394  ARG   A CZ    1 
ATOM   2879  N  NH1   . ARG   A 1  396  ? -34.293 39.639  98.346  1.00 36.70 ? 394  ARG   A NH1   1 
ATOM   2880  N  NH2   . ARG   A 1  396  ? -34.011 40.985  100.181 1.00 31.34 ? 394  ARG   A NH2   1 
ATOM   2881  N  N     . LYS   A 1  397  ? -36.125 43.561  91.801  1.00 23.13 ? 395  LYS   A N     1 
ATOM   2882  C  CA    . LYS   A 1  397  ? -36.759 43.489  90.494  1.00 22.92 ? 395  LYS   A CA    1 
ATOM   2883  C  C     . LYS   A 1  397  ? -38.002 42.609  90.534  1.00 23.61 ? 395  LYS   A C     1 
ATOM   2884  O  O     . LYS   A 1  397  ? -39.017 42.918  89.897  1.00 21.10 ? 395  LYS   A O     1 
ATOM   2885  C  CB    . LYS   A 1  397  ? -35.740 43.000  89.464  1.00 23.18 ? 395  LYS   A CB    1 
ATOM   2886  C  CG    . LYS   A 1  397  ? -36.129 43.289  88.036  1.00 26.51 ? 395  LYS   A CG    1 
ATOM   2887  C  CD    . LYS   A 1  397  ? -36.836 42.118  87.419  1.00 23.06 ? 395  LYS   A CD    1 
ATOM   2888  C  CE    . LYS   A 1  397  ? -37.303 42.451  86.018  1.00 23.93 ? 395  LYS   A CE    1 
ATOM   2889  N  NZ    . LYS   A 1  397  ? -37.919 41.267  85.366  1.00 26.72 ? 395  LYS   A NZ    1 
ATOM   2890  N  N     . ILE   A 1  398  ? -37.957 41.518  91.304  1.00 21.02 ? 396  ILE   A N     1 
ATOM   2891  C  CA    . ILE   A 1  398  ? -39.095 40.608  91.346  1.00 23.17 ? 396  ILE   A CA    1 
ATOM   2892  C  C     . ILE   A 1  398  ? -40.319 41.289  91.948  1.00 20.59 ? 396  ILE   A C     1 
ATOM   2893  O  O     . ILE   A 1  398  ? -41.462 40.943  91.620  1.00 23.89 ? 396  ILE   A O     1 
ATOM   2894  C  CB    . ILE   A 1  398  ? -38.698 39.310  92.080  1.00 26.31 ? 396  ILE   A CB    1 
ATOM   2895  C  CG1   . ILE   A 1  398  ? -39.728 38.222  91.804  1.00 27.98 ? 396  ILE   A CG1   1 
ATOM   2896  C  CG2   . ILE   A 1  398  ? -38.540 39.562  93.573  1.00 25.34 ? 396  ILE   A CG2   1 
ATOM   2897  C  CD1   . ILE   A 1  398  ? -39.235 36.823  92.132  1.00 32.88 ? 396  ILE   A CD1   1 
ATOM   2898  N  N     . HIS   A 1  399  ? -40.106 42.274  92.818  1.00 22.94 ? 397  HIS   A N     1 
ATOM   2899  C  CA    . HIS   A 1  399  ? -41.232 43.025  93.362  1.00 22.68 ? 397  HIS   A CA    1 
ATOM   2900  C  C     . HIS   A 1  399  ? -41.941 43.806  92.269  1.00 19.32 ? 397  HIS   A C     1 
ATOM   2901  O  O     . HIS   A 1  399  ? -43.175 43.825  92.208  1.00 22.01 ? 397  HIS   A O     1 
ATOM   2902  C  CB    . HIS   A 1  399  ? -40.752 43.963  94.462  1.00 23.25 ? 397  HIS   A CB    1 
ATOM   2903  C  CG    . HIS   A 1  399  ? -40.246 43.250  95.677  1.00 21.49 ? 397  HIS   A CG    1 
ATOM   2904  N  ND1   . HIS   A 1  399  ? -39.591 43.897  96.702  1.00 23.11 ? 397  HIS   A ND1   1 
ATOM   2905  C  CD2   . HIS   A 1  399  ? -40.289 41.941  96.022  1.00 29.06 ? 397  HIS   A CD2   1 
ATOM   2906  C  CE1   . HIS   A 1  399  ? -39.255 43.017  97.629  1.00 25.15 ? 397  HIS   A CE1   1 
ATOM   2907  N  NE2   . HIS   A 1  399  ? -39.664 41.823  97.238  1.00 25.92 ? 397  HIS   A NE2   1 
ATOM   2908  N  N     . THR   A 1  400  ? -41.172 44.448  91.393  1.00 21.37 ? 398  THR   A N     1 
ATOM   2909  C  CA    . THR   A 1  400  ? -41.776 45.155  90.272  1.00 19.61 ? 398  THR   A CA    1 
ATOM   2910  C  C     . THR   A 1  400  ? -42.565 44.201  89.382  1.00 20.48 ? 398  THR   A C     1 
ATOM   2911  O  O     . THR   A 1  400  ? -43.650 44.543  88.895  1.00 20.15 ? 398  THR   A O     1 
ATOM   2912  C  CB    . THR   A 1  400  ? -40.668 45.864  89.498  1.00 19.34 ? 398  THR   A CB    1 
ATOM   2913  O  OG1   . THR   A 1  400  ? -40.145 46.916  90.313  1.00 19.24 ? 398  THR   A OG1   1 
ATOM   2914  C  CG2   . THR   A 1  400  ? -41.193 46.446  88.170  1.00 18.87 ? 398  THR   A CG2   1 
ATOM   2915  N  N     . ASP   A 1  401  ? -42.056 42.985  89.188  1.00 20.16 ? 399  ASP   A N     1 
ATOM   2916  C  CA    . ASP   A 1  401  ? -42.772 42.019  88.365  1.00 21.17 ? 399  ASP   A CA    1 
ATOM   2917  C  C     . ASP   A 1  401  ? -44.108 41.654  88.996  1.00 20.36 ? 399  ASP   A C     1 
ATOM   2918  O  O     . ASP   A 1  401  ? -45.128 41.579  88.305  1.00 21.81 ? 399  ASP   A O     1 
ATOM   2919  C  CB    . ASP   A 1  401  ? -41.921 40.765  88.144  1.00 23.93 ? 399  ASP   A CB    1 
ATOM   2920  C  CG    . ASP   A 1  401  ? -40.733 41.016  87.229  1.00 26.71 ? 399  ASP   A CG    1 
ATOM   2921  O  OD1   . ASP   A 1  401  ? -40.784 41.964  86.416  1.00 25.89 ? 399  ASP   A OD1   1 
ATOM   2922  O  OD2   . ASP   A 1  401  ? -39.745 40.263  87.331  1.00 27.23 ? 399  ASP   A OD2   1 
ATOM   2923  N  N     . VAL   A 1  402  ? -44.113 41.395  90.309  1.00 21.37 ? 400  VAL   A N     1 
ATOM   2924  C  CA    . VAL   A 1  402  ? -45.366 41.080  90.989  1.00 22.24 ? 400  VAL   A CA    1 
ATOM   2925  C  C     . VAL   A 1  402  ? -46.304 42.274  90.940  1.00 21.17 ? 400  VAL   A C     1 
ATOM   2926  O  O     . VAL   A 1  402  ? -47.505 42.129  90.675  1.00 21.71 ? 400  VAL   A O     1 
ATOM   2927  C  CB    . VAL   A 1  402  ? -45.101 40.624  92.431  1.00 22.79 ? 400  VAL   A CB    1 
ATOM   2928  C  CG1   . VAL   A 1  402  ? -46.423 40.467  93.199  1.00 22.15 ? 400  VAL   A CG1   1 
ATOM   2929  C  CG2   . VAL   A 1  402  ? -44.317 39.326  92.424  1.00 26.41 ? 400  VAL   A CG2   1 
ATOM   2930  N  N     . SER   A 1  403  ? -45.769 43.472  91.189  1.00 21.17 ? 401  SER   A N     1 
ATOM   2931  C  CA    . SER   A 1  403  ? -46.578 44.679  91.079  1.00 19.31 ? 401  SER   A CA    1 
ATOM   2932  C  C     . SER   A 1  403  ? -47.214 44.771  89.699  1.00 22.25 ? 401  SER   A C     1 
ATOM   2933  O  O     . SER   A 1  403  ? -48.412 45.041  89.566  1.00 20.38 ? 401  SER   A O     1 
ATOM   2934  C  CB    . SER   A 1  403  ? -45.703 45.904  91.344  1.00 20.74 ? 401  SER   A CB    1 
ATOM   2935  O  OG    . SER   A 1  403  ? -46.434 47.099  91.144  1.00 20.71 ? 401  SER   A OG    1 
ATOM   2936  N  N     . TYR   A 1  404  ? -46.426 44.519  88.656  1.00 20.79 ? 402  TYR   A N     1 
ATOM   2937  C  CA    . TYR   A 1  404  ? -46.952 44.604  87.302  1.00 20.46 ? 402  TYR   A CA    1 
ATOM   2938  C  C     . TYR   A 1  404  ? -48.120 43.644  87.107  1.00 19.21 ? 402  TYR   A C     1 
ATOM   2939  O  O     . TYR   A 1  404  ? -49.180 44.031  86.606  1.00 19.69 ? 402  TYR   A O     1 
ATOM   2940  C  CB    . TYR   A 1  404  ? -45.826 44.330  86.305  1.00 19.02 ? 402  TYR   A CB    1 
ATOM   2941  C  CG    . TYR   A 1  404  ? -46.156 44.674  84.873  1.00 19.81 ? 402  TYR   A CG    1 
ATOM   2942  C  CD1   . TYR   A 1  404  ? -46.932 43.821  84.095  1.00 18.68 ? 402  TYR   A CD1   1 
ATOM   2943  C  CD2   . TYR   A 1  404  ? -45.681 45.839  84.292  1.00 18.39 ? 402  TYR   A CD2   1 
ATOM   2944  C  CE1   . TYR   A 1  404  ? -47.236 44.122  82.784  1.00 19.03 ? 402  TYR   A CE1   1 
ATOM   2945  C  CE2   . TYR   A 1  404  ? -45.979 46.142  82.973  1.00 18.28 ? 402  TYR   A CE2   1 
ATOM   2946  C  CZ    . TYR   A 1  404  ? -46.748 45.283  82.228  1.00 18.03 ? 402  TYR   A CZ    1 
ATOM   2947  O  OH    . TYR   A 1  404  ? -47.052 45.580  80.922  1.00 20.24 ? 402  TYR   A OH    1 
ATOM   2948  N  N     . ILE   A 1  405  ? -47.952 42.389  87.527  1.00 21.26 ? 403  ILE   A N     1 
ATOM   2949  C  CA    . ILE   A 1  405  ? -49.003 41.400  87.322  1.00 21.34 ? 403  ILE   A CA    1 
ATOM   2950  C  C     . ILE   A 1  405  ? -50.234 41.732  88.156  1.00 20.02 ? 403  ILE   A C     1 
ATOM   2951  O  O     . ILE   A 1  405  ? -51.366 41.601  87.685  1.00 22.81 ? 403  ILE   A O     1 
ATOM   2952  C  CB    . ILE   A 1  405  ? -48.455 39.990  87.590  1.00 23.04 ? 403  ILE   A CB    1 
ATOM   2953  C  CG1   . ILE   A 1  405  ? -47.313 39.715  86.609  1.00 26.53 ? 403  ILE   A CG1   1 
ATOM   2954  C  CG2   . ILE   A 1  405  ? -49.559 38.965  87.446  1.00 25.35 ? 403  ILE   A CG2   1 
ATOM   2955  C  CD1   . ILE   A 1  405  ? -46.439 38.527  86.981  1.00 28.32 ? 403  ILE   A CD1   1 
ATOM   2956  N  N     . ALA   A 1  406  ? -50.033 42.194  89.392  1.00 21.94 ? 404  ALA   A N     1 
ATOM   2957  C  CA    . ALA   A 1  406  ? -51.167 42.594  90.220  1.00 22.30 ? 404  ALA   A CA    1 
ATOM   2958  C  C     . ALA   A 1  406  ? -51.908 43.761  89.592  1.00 20.85 ? 404  ALA   A C     1 
ATOM   2959  O  O     . ALA   A 1  406  ? -53.146 43.803  89.592  1.00 22.76 ? 404  ALA   A O     1 
ATOM   2960  C  CB    . ALA   A 1  406  ? -50.677 43.001  91.603  1.00 23.88 ? 404  ALA   A CB    1 
ATOM   2961  N  N     . CYS   A 1  407  ? -51.167 44.732  89.060  1.00 20.31 ? 405  CYS   A N     1 
ATOM   2962  C  CA    . CYS   A 1  407  ? -51.817 45.880  88.449  1.00 18.54 ? 405  CYS   A CA    1 
ATOM   2963  C  C     . CYS   A 1  407  ? -52.511 45.499  87.150  1.00 20.18 ? 405  CYS   A C     1 
ATOM   2964  O  O     . CYS   A 1  407  ? -53.544 46.086  86.802  1.00 21.77 ? 405  CYS   A O     1 
ATOM   2965  C  CB    . CYS   A 1  407  ? -50.788 46.987  88.243  1.00 21.79 ? 405  CYS   A CB    1 
ATOM   2966  S  SG    . CYS   A 1  407  ? -50.299 47.754  89.802  1.00 26.08 ? 405  CYS   A SG    1 
ATOM   2967  N  N     . ALA   A 1  408  ? -51.965 44.519  86.428  1.00 21.04 ? 406  ALA   A N     1 
ATOM   2968  C  CA    . ALA   A 1  408  ? -52.639 44.012  85.243  1.00 21.25 ? 406  ALA   A CA    1 
ATOM   2969  C  C     . ALA   A 1  408  ? -53.962 43.357  85.607  1.00 19.43 ? 406  ALA   A C     1 
ATOM   2970  O  O     . ALA   A 1  408  ? -54.941 43.468  84.863  1.00 21.75 ? 406  ALA   A O     1 
ATOM   2971  C  CB    . ALA   A 1  408  ? -51.731 43.021  84.516  1.00 22.52 ? 406  ALA   A CB    1 
ATOM   2972  N  N     . ALA   A 1  409  ? -54.007 42.662  86.742  1.00 22.71 ? 407  ALA   A N     1 
ATOM   2973  C  CA    . ALA   A 1  409  ? -55.264 42.073  87.192  1.00 21.94 ? 407  ALA   A CA    1 
ATOM   2974  C  C     . ALA   A 1  409  ? -56.306 43.148  87.462  1.00 22.39 ? 407  ALA   A C     1 
ATOM   2975  O  O     . ALA   A 1  409  ? -57.485 42.985  87.121  1.00 24.40 ? 407  ALA   A O     1 
ATOM   2976  C  CB    . ALA   A 1  409  ? -55.016 41.232  88.446  1.00 27.17 ? 407  ALA   A CB    1 
ATOM   2977  N  N     . LYS   A 1  410  ? -55.881 44.263  88.062  1.00 20.83 ? 408  LYS   A N     1 
ATOM   2978  C  CA    . LYS   A 1  410  ? -56.796 45.373  88.300  1.00 20.87 ? 408  LYS   A CA    1 
ATOM   2979  C  C     . LYS   A 1  410  ? -57.292 45.960  86.985  1.00 20.24 ? 408  LYS   A C     1 
ATOM   2980  O  O     . LYS   A 1  410  ? -58.486 46.245  86.827  1.00 21.59 ? 408  LYS   A O     1 
ATOM   2981  C  CB    . LYS   A 1  410  ? -56.083 46.443  89.128  1.00 21.06 ? 408  LYS   A CB    1 
ATOM   2982  C  CG    . LYS   A 1  410  ? -56.928 47.661  89.466  1.00 23.52 ? 408  LYS   A CG    1 
ATOM   2983  C  CD    . LYS   A 1  410  ? -56.119 48.656  90.267  1.00 23.76 ? 408  LYS   A CD    1 
ATOM   2984  C  CE    . LYS   A 1  410  ? -55.687 48.082  91.599  1.00 27.96 ? 408  LYS   A CE    1 
ATOM   2985  N  NZ    . LYS   A 1  410  ? -56.823 48.092  92.538  1.00 27.48 ? 408  LYS   A NZ    1 
ATOM   2986  N  N     . LEU   A 1  411  ? -56.384 46.153  86.023  1.00 19.31 ? 409  LEU   A N     1 
ATOM   2987  C  CA    . LEU   A 1  411  ? -56.778 46.718  84.740  1.00 18.52 ? 409  LEU   A CA    1 
ATOM   2988  C  C     . LEU   A 1  411  ? -57.693 45.774  83.972  1.00 19.30 ? 409  LEU   A C     1 
ATOM   2989  O  O     . LEU   A 1  411  ? -58.644 46.222  83.325  1.00 19.79 ? 409  LEU   A O     1 
ATOM   2990  C  CB    . LEU   A 1  411  ? -55.536 47.058  83.911  1.00 17.79 ? 409  LEU   A CB    1 
ATOM   2991  C  CG    . LEU   A 1  411  ? -54.818 48.318  84.365  1.00 18.71 ? 409  LEU   A CG    1 
ATOM   2992  C  CD1   . LEU   A 1  411  ? -53.419 48.394  83.762  1.00 19.16 ? 409  LEU   A CD1   1 
ATOM   2993  C  CD2   . LEU   A 1  411  ? -55.621 49.534  83.976  1.00 18.96 ? 409  LEU   A CD2   1 
ATOM   2994  N  N     . LEU   A 1  412  ? -57.423 44.466  84.028  1.00 21.39 ? 410  LEU   A N     1 
ATOM   2995  C  CA    . LEU   A 1  412  ? -58.234 43.531  83.259  1.00 20.56 ? 410  LEU   A CA    1 
ATOM   2996  C  C     . LEU   A 1  412  ? -59.639 43.395  83.815  1.00 23.41 ? 410  LEU   A C     1 
ATOM   2997  O  O     . LEU   A 1  412  ? -60.538 42.977  83.083  1.00 25.24 ? 410  LEU   A O     1 
ATOM   2998  C  CB    . LEU   A 1  412  ? -57.537 42.174  83.149  1.00 23.30 ? 410  LEU   A CB    1 
ATOM   2999  C  CG    . LEU   A 1  412  ? -56.349 42.165  82.178  1.00 20.85 ? 410  LEU   A CG    1 
ATOM   3000  C  CD1   . LEU   A 1  412  ? -55.606 40.854  82.281  1.00 25.74 ? 410  LEU   A CD1   1 
ATOM   3001  C  CD2   . LEU   A 1  412  ? -56.832 42.381  80.764  1.00 23.69 ? 410  LEU   A CD2   1 
ATOM   3002  N  N     . ALA   A 1  413  ? -59.856 43.770  85.070  1.00 21.04 ? 411  ALA   A N     1 
ATOM   3003  C  CA    . ALA   A 1  413  ? -61.205 43.810  85.623  1.00 22.64 ? 411  ALA   A CA    1 
ATOM   3004  C  C     . ALA   A 1  413  ? -61.953 45.078  85.239  1.00 23.83 ? 411  ALA   A C     1 
ATOM   3005  O  O     . ALA   A 1  413  ? -63.135 45.213  85.564  1.00 26.03 ? 411  ALA   A O     1 
ATOM   3006  C  CB    . ALA   A 1  413  ? -61.152 43.696  87.146  1.00 22.88 ? 411  ALA   A CB    1 
ATOM   3007  N  N     . ALA   A 1  414  ? -61.294 46.012  84.556  1.00 22.01 ? 412  ALA   A N     1 
ATOM   3008  C  CA    . ALA   A 1  414  ? -61.875 47.312  84.253  1.00 25.33 ? 412  ALA   A CA    1 
ATOM   3009  C  C     . ALA   A 1  414  ? -61.828 47.637  82.764  1.00 22.18 ? 412  ALA   A C     1 
ATOM   3010  O  O     . ALA   A 1  414  ? -61.871 48.810  82.397  1.00 19.65 ? 412  ALA   A O     1 
ATOM   3011  C  CB    . ALA   A 1  414  ? -61.184 48.412  85.068  1.00 24.45 ? 412  ALA   A CB    1 
ATOM   3012  N  N     . THR   A 1  415  ? -61.768 46.621  81.893  1.00 23.25 ? 413  THR   A N     1 
ATOM   3013  C  CA    . THR   A 1  415  ? -61.675 46.888  80.460  1.00 22.11 ? 413  THR   A CA    1 
ATOM   3014  C  C     . THR   A 1  415  ? -62.902 47.599  79.907  1.00 21.40 ? 413  THR   A C     1 
ATOM   3015  O  O     . THR   A 1  415  ? -62.829 48.178  78.816  1.00 24.25 ? 413  THR   A O     1 
ATOM   3016  C  CB    . THR   A 1  415  ? -61.388 45.611  79.652  1.00 23.63 ? 413  THR   A CB    1 
ATOM   3017  O  OG1   . THR   A 1  415  ? -62.450 44.667  79.834  1.00 26.98 ? 413  THR   A OG1   1 
ATOM   3018  C  CG2   . THR   A 1  415  ? -60.069 44.979  80.076  1.00 24.05 ? 413  THR   A CG2   1 
ATOM   3019  N  N     . ASP   A 1  416  ? -64.032 47.576  80.617  1.00 23.34 ? 414  ASP   A N     1 
ATOM   3020  C  CA    . ASP   A 1  416  ? -65.159 48.359  80.133  1.00 22.81 ? 414  ASP   A CA    1 
ATOM   3021  C  C     . ASP   A 1  416  ? -64.925 49.856  80.285  1.00 24.97 ? 414  ASP   A C     1 
ATOM   3022  O  O     . ASP   A 1  416  ? -65.523 50.638  79.542  1.00 29.53 ? 414  ASP   A O     1 
ATOM   3023  C  CB    . ASP   A 1  416  ? -66.461 47.928  80.814  1.00 25.78 ? 414  ASP   A CB    1 
ATOM   3024  C  CG    . ASP   A 1  416  ? -66.418 48.104  82.313  1.00 35.89 ? 414  ASP   A CG    1 
ATOM   3025  O  OD1   . ASP   A 1  416  ? -65.365 47.809  82.922  1.00 34.71 ? 414  ASP   A OD1   1 
ATOM   3026  O  OD2   . ASP   A 1  416  ? -67.440 48.546  82.884  1.00 50.09 ? 414  ASP   A OD2   1 
ATOM   3027  N  N     . VAL   A 1  417  ? -64.049 50.279  81.197  1.00 23.17 ? 415  VAL   A N     1 
ATOM   3028  C  CA    . VAL   A 1  417  ? -63.874 51.702  81.451  1.00 24.55 ? 415  VAL   A CA    1 
ATOM   3029  C  C     . VAL   A 1  417  ? -62.484 52.224  81.121  1.00 20.03 ? 415  VAL   A C     1 
ATOM   3030  O  O     . VAL   A 1  417  ? -62.336 53.441  80.947  1.00 21.30 ? 415  VAL   A O     1 
ATOM   3031  C  CB    . VAL   A 1  417  ? -64.276 52.107  82.882  1.00 29.09 ? 415  VAL   A CB    1 
ATOM   3032  C  CG1   . VAL   A 1  417  ? -65.713 51.695  83.160  1.00 32.63 ? 415  VAL   A CG1   1 
ATOM   3033  C  CG2   . VAL   A 1  417  ? -63.346 51.494  83.877  1.00 25.93 ? 415  VAL   A CG2   1 
ATOM   3034  N  N     . VAL   A 1  418  ? -61.457 51.374  81.057  1.00 19.79 ? 416  VAL   A N     1 
ATOM   3035  C  CA    . VAL   A 1  418  ? -60.143 51.773  80.569  1.00 18.37 ? 416  VAL   A CA    1 
ATOM   3036  C  C     . VAL   A 1  418  ? -59.701 50.785  79.505  1.00 18.07 ? 416  VAL   A C     1 
ATOM   3037  O  O     . VAL   A 1  418  ? -60.207 49.668  79.406  1.00 19.07 ? 416  VAL   A O     1 
ATOM   3038  C  CB    . VAL   A 1  418  ? -59.074 51.863  81.682  1.00 19.22 ? 416  VAL   A CB    1 
ATOM   3039  C  CG1   . VAL   A 1  418  ? -59.421 52.967  82.674  1.00 19.67 ? 416  VAL   A CG1   1 
ATOM   3040  C  CG2   . VAL   A 1  418  ? -58.901 50.532  82.375  1.00 20.11 ? 416  VAL   A CG2   1 
ATOM   3041  N  N     . PHE   A 1  419  ? -58.699 51.193  78.737  1.00 16.61 ? 417  PHE   A N     1 
ATOM   3042  C  CA    . PHE   A 1  419  ? -58.089 50.332  77.731  1.00 18.57 ? 417  PHE   A CA    1 
ATOM   3043  C  C     . PHE   A 1  419  ? -56.685 49.996  78.195  1.00 15.86 ? 417  PHE   A C     1 
ATOM   3044  O  O     . PHE   A 1  419  ? -55.773 50.830  78.059  1.00 17.02 ? 417  PHE   A O     1 
ATOM   3045  C  CB    . PHE   A 1  419  ? -58.042 51.063  76.388  1.00 16.26 ? 417  PHE   A CB    1 
ATOM   3046  C  CG    . PHE   A 1  419  ? -57.330 50.304  75.300  1.00 18.06 ? 417  PHE   A CG    1 
ATOM   3047  C  CD1   . PHE   A 1  419  ? -57.808 49.083  74.856  1.00 20.01 ? 417  PHE   A CD1   1 
ATOM   3048  C  CD2   . PHE   A 1  419  ? -56.210 50.840  74.696  1.00 17.50 ? 417  PHE   A CD2   1 
ATOM   3049  C  CE1   . PHE   A 1  419  ? -57.167 48.404  73.844  1.00 17.95 ? 417  PHE   A CE1   1 
ATOM   3050  C  CE2   . PHE   A 1  419  ? -55.563 50.166  73.696  1.00 18.07 ? 417  PHE   A CE2   1 
ATOM   3051  C  CZ    . PHE   A 1  419  ? -56.042 48.957  73.254  1.00 17.22 ? 417  PHE   A CZ    1 
ATOM   3052  N  N     . PRO   A 1  420  ? -56.457 48.808  78.744  1.00 16.12 ? 418  PRO   A N     1 
ATOM   3053  C  CA    . PRO   A 1  420  ? -55.119 48.470  79.244  1.00 16.37 ? 418  PRO   A CA    1 
ATOM   3054  C  C     . PRO   A 1  420  ? -54.155 48.201  78.109  1.00 18.32 ? 418  PRO   A C     1 
ATOM   3055  O  O     . PRO   A 1  420  ? -54.489 47.557  77.115  1.00 18.14 ? 418  PRO   A O     1 
ATOM   3056  C  CB    . PRO   A 1  420  ? -55.349 47.190  80.058  1.00 16.21 ? 418  PRO   A CB    1 
ATOM   3057  C  CG    . PRO   A 1  420  ? -56.840 47.160  80.316  1.00 16.83 ? 418  PRO   A CG    1 
ATOM   3058  C  CD    . PRO   A 1  420  ? -57.451 47.787  79.098  1.00 18.21 ? 418  PRO   A CD    1 
ATOM   3059  N  N     . GLN   A 1  421  ? -52.936 48.691  78.285  1.00 16.59 ? 419  GLN   A N     1 
ATOM   3060  C  CA    . GLN   A 1  421  ? -51.871 48.517  77.309  1.00 15.79 ? 419  GLN   A CA    1 
ATOM   3061  C  C     . GLN   A 1  421  ? -50.671 47.980  78.066  1.00 16.59 ? 419  GLN   A C     1 
ATOM   3062  O  O     . GLN   A 1  421  ? -50.057 48.703  78.857  1.00 17.79 ? 419  GLN   A O     1 
ATOM   3063  C  CB    . GLN   A 1  421  ? -51.555 49.848  76.648  1.00 15.08 ? 419  GLN   A CB    1 
ATOM   3064  C  CG    . GLN   A 1  421  ? -52.770 50.452  75.973  1.00 17.41 ? 419  GLN   A CG    1 
ATOM   3065  C  CD    . GLN   A 1  421  ? -52.571 51.895  75.625  1.00 16.05 ? 419  GLN   A CD    1 
ATOM   3066  O  OE1   . GLN   A 1  421  ? -52.351 52.729  76.501  1.00 17.94 ? 419  GLN   A OE1   1 
ATOM   3067  N  NE2   . GLN   A 1  421  ? -52.671 52.208  74.341  1.00 17.80 ? 419  GLN   A NE2   1 
ATOM   3068  N  N     . PHE   A 1  422  ? -50.344 46.717  77.838  1.00 16.45 ? 420  PHE   A N     1 
ATOM   3069  C  CA    . PHE   A 1  422  ? -49.328 46.039  78.634  1.00 16.29 ? 420  PHE   A CA    1 
ATOM   3070  C  C     . PHE   A 1  422  ? -47.995 46.113  77.909  1.00 16.21 ? 420  PHE   A C     1 
ATOM   3071  O  O     . PHE   A 1  422  ? -47.707 45.303  77.023  1.00 18.50 ? 420  PHE   A O     1 
ATOM   3072  C  CB    . PHE   A 1  422  ? -49.751 44.613  78.934  1.00 19.00 ? 420  PHE   A CB    1 
ATOM   3073  C  CG    . PHE   A 1  422  ? -51.031 44.545  79.688  1.00 18.59 ? 420  PHE   A CG    1 
ATOM   3074  C  CD1   . PHE   A 1  422  ? -51.106 45.030  80.981  1.00 20.31 ? 420  PHE   A CD1   1 
ATOM   3075  C  CD2   . PHE   A 1  422  ? -52.164 44.023  79.095  1.00 18.60 ? 420  PHE   A CD2   1 
ATOM   3076  C  CE1   . PHE   A 1  422  ? -52.293 44.984  81.679  1.00 21.77 ? 420  PHE   A CE1   1 
ATOM   3077  C  CE2   . PHE   A 1  422  ? -53.351 43.970  79.787  1.00 20.80 ? 420  PHE   A CE2   1 
ATOM   3078  C  CZ    . PHE   A 1  422  ? -53.412 44.455  81.078  1.00 20.32 ? 420  PHE   A CZ    1 
ATOM   3079  N  N     . ALA   A 1  423  ? -47.181 47.084  78.305  1.00 16.88 ? 421  ALA   A N     1 
ATOM   3080  C  CA    . ALA   A 1  423  ? -45.883 47.308  77.685  1.00 15.46 ? 421  ALA   A CA    1 
ATOM   3081  C  C     . ALA   A 1  423  ? -44.868 46.452  78.427  1.00 18.24 ? 421  ALA   A C     1 
ATOM   3082  O  O     . ALA   A 1  423  ? -44.593 46.686  79.611  1.00 20.05 ? 421  ALA   A O     1 
ATOM   3083  C  CB    . ALA   A 1  423  ? -45.524 48.787  77.772  1.00 16.48 ? 421  ALA   A CB    1 
ATOM   3084  N  N     . THR   A 1  424  ? -44.316 45.461  77.738  1.00 18.09 ? 422  THR   A N     1 
ATOM   3085  C  CA    . THR   A 1  424  ? -43.284 44.641  78.355  1.00 18.42 ? 422  THR   A CA    1 
ATOM   3086  C  C     . THR   A 1  424  ? -42.584 43.825  77.281  1.00 18.86 ? 422  THR   A C     1 
ATOM   3087  O  O     . THR   A 1  424  ? -43.191 43.439  76.279  1.00 20.62 ? 422  THR   A O     1 
ATOM   3088  C  CB    . THR   A 1  424  ? -43.846 43.706  79.436  1.00 21.27 ? 422  THR   A CB    1 
ATOM   3089  O  OG1   . THR   A 1  424  ? -42.750 43.015  80.062  1.00 21.01 ? 422  THR   A OG1   1 
ATOM   3090  C  CG2   . THR   A 1  424  ? -44.814 42.703  78.838  1.00 22.31 ? 422  THR   A CG2   1 
ATOM   3091  N  N     . HIS   A 1  425  ? -41.294 43.575  77.506  1.00 18.62 ? 423  HIS   A N     1 
ATOM   3092  C  CA    . HIS   A 1  425  ? -40.534 42.652  76.682  1.00 19.77 ? 423  HIS   A CA    1 
ATOM   3093  C  C     . HIS   A 1  425  ? -40.299 41.327  77.373  1.00 21.71 ? 423  HIS   A C     1 
ATOM   3094  O  O     . HIS   A 1  425  ? -39.600 40.470  76.826  1.00 23.85 ? 423  HIS   A O     1 
ATOM   3095  C  CB    . HIS   A 1  425  ? -39.194 43.281  76.313  1.00 19.40 ? 423  HIS   A CB    1 
ATOM   3096  C  CG    . HIS   A 1  425  ? -39.334 44.537  75.525  1.00 19.25 ? 423  HIS   A CG    1 
ATOM   3097  N  ND1   . HIS   A 1  425  ? -38.600 45.671  75.795  1.00 21.43 ? 423  HIS   A ND1   1 
ATOM   3098  C  CD2   . HIS   A 1  425  ? -40.151 44.851  74.492  1.00 21.42 ? 423  HIS   A CD2   1 
ATOM   3099  C  CE1   . HIS   A 1  425  ? -38.950 46.626  74.950  1.00 22.76 ? 423  HIS   A CE1   1 
ATOM   3100  N  NE2   . HIS   A 1  425  ? -39.896 46.156  74.156  1.00 20.21 ? 423  HIS   A NE2   1 
ATOM   3101  N  N     . ASN   A 1  426  ? -40.869 41.139  78.554  1.00 21.12 ? 424  ASN   A N     1 
ATOM   3102  C  CA    . ASN   A 1  426  ? -40.624 39.947  79.361  1.00 22.39 ? 424  ASN   A CA    1 
ATOM   3103  C  C     . ASN   A 1  426  ? -41.676 38.901  78.997  1.00 23.38 ? 424  ASN   A C     1 
ATOM   3104  O  O     . ASN   A 1  426  ? -42.873 39.096  79.233  1.00 23.19 ? 424  ASN   A O     1 
ATOM   3105  C  CB    . ASN   A 1  426  ? -40.673 40.351  80.833  1.00 20.79 ? 424  ASN   A CB    1 
ATOM   3106  C  CG    . ASN   A 1  426  ? -40.336 39.216  81.778  1.00 23.29 ? 424  ASN   A CG    1 
ATOM   3107  O  OD1   . ASN   A 1  426  ? -40.753 38.082  81.582  1.00 25.91 ? 424  ASN   A OD1   1 
ATOM   3108  N  ND2   . ASN   A 1  426  ? -39.598 39.538  82.838  1.00 23.65 ? 424  ASN   A ND2   1 
ATOM   3109  N  N     . ALA   A 1  427  ? -41.230 37.784  78.414  1.00 21.63 ? 425  ALA   A N     1 
ATOM   3110  C  CA    . ALA   A 1  427  ? -42.158 36.756  77.955  1.00 22.73 ? 425  ALA   A CA    1 
ATOM   3111  C  C     . ALA   A 1  427  ? -42.929 36.120  79.105  1.00 20.30 ? 425  ALA   A C     1 
ATOM   3112  O  O     . ALA   A 1  427  ? -44.059 35.658  78.909  1.00 23.71 ? 425  ALA   A O     1 
ATOM   3113  C  CB    . ALA   A 1  427  ? -41.395 35.679  77.180  1.00 26.10 ? 425  ALA   A CB    1 
ATOM   3114  N  N     . GLN   A 1  428  ? -42.336 36.067  80.297  1.00 22.79 ? 426  GLN   A N     1 
ATOM   3115  C  CA    . GLN   A 1  428  ? -43.064 35.544  81.449  1.00 25.59 ? 426  GLN   A CA    1 
ATOM   3116  C  C     . GLN   A 1  428  ? -44.199 36.481  81.822  1.00 25.11 ? 426  GLN   A C     1 
ATOM   3117  O  O     . GLN   A 1  428  ? -45.339 36.044  82.029  1.00 24.35 ? 426  GLN   A O     1 
ATOM   3118  C  CB    . GLN   A 1  428  ? -42.113 35.371  82.633  1.00 22.63 ? 426  GLN   A CB    1 
ATOM   3119  C  CG    . GLN   A 1  428  ? -42.645 34.440  83.718  1.00 27.55 ? 426  GLN   A CG    1 
ATOM   3120  C  CD    . GLN   A 1  428  ? -43.739 35.066  84.569  1.00 29.99 ? 426  GLN   A CD    1 
ATOM   3121  O  OE1   . GLN   A 1  428  ? -43.710 36.263  84.861  1.00 30.58 ? 426  GLN   A OE1   1 
ATOM   3122  N  NE2   . GLN   A 1  428  ? -44.707 34.253  84.975  1.00 28.61 ? 426  GLN   A NE2   1 
ATOM   3123  N  N     . THR   A 1  429  ? -43.894 37.777  81.922  1.00 23.66 ? 427  THR   A N     1 
ATOM   3124  C  CA    . THR   A 1  429  ? -44.924 38.773  82.190  1.00 21.90 ? 427  THR   A CA    1 
ATOM   3125  C  C     . THR   A 1  429  ? -46.036 38.685  81.157  1.00 21.81 ? 427  THR   A C     1 
ATOM   3126  O  O     . THR   A 1  429  ? -47.225 38.653  81.500  1.00 23.38 ? 427  THR   A O     1 
ATOM   3127  C  CB    . THR   A 1  429  ? -44.300 40.168  82.147  1.00 21.52 ? 427  THR   A CB    1 
ATOM   3128  O  OG1   . THR   A 1  429  ? -43.133 40.200  82.973  1.00 22.62 ? 427  THR   A OG1   1 
ATOM   3129  C  CG2   . THR   A 1  429  ? -45.299 41.196  82.651  1.00 23.66 ? 427  THR   A CG2   1 
ATOM   3130  N  N     . LEU   A 1  430  ? -45.655 38.637  79.879  1.00 21.52 ? 428  LEU   A N     1 
ATOM   3131  C  CA    . LEU   A 1  430  ? -46.623 38.590  78.793  1.00 21.56 ? 428  LEU   A CA    1 
ATOM   3132  C  C     . LEU   A 1  430  ? -47.528 37.377  78.930  1.00 22.87 ? 428  LEU   A C     1 
ATOM   3133  O  O     . LEU   A 1  430  ? -48.756 37.493  78.878  1.00 22.71 ? 428  LEU   A O     1 
ATOM   3134  C  CB    . LEU   A 1  430  ? -45.872 38.548  77.460  1.00 19.45 ? 428  LEU   A CB    1 
ATOM   3135  C  CG    . LEU   A 1  430  ? -46.571 38.792  76.117  1.00 24.70 ? 428  LEU   A CG    1 
ATOM   3136  C  CD1   . LEU   A 1  430  ? -45.487 38.947  75.073  1.00 29.55 ? 428  LEU   A CD1   1 
ATOM   3137  C  CD2   . LEU   A 1  430  ? -47.513 37.666  75.706  1.00 26.94 ? 428  LEU   A CD2   1 
ATOM   3138  N  N     . ALA   A 1  431  ? -46.931 36.197  79.101  1.00 25.34 ? 429  ALA   A N     1 
ATOM   3139  C  CA    . ALA   A 1  431  ? -47.711 34.966  79.171  1.00 24.65 ? 429  ALA   A CA    1 
ATOM   3140  C  C     . ALA   A 1  431  ? -48.675 34.984  80.351  1.00 24.56 ? 429  ALA   A C     1 
ATOM   3141  O  O     . ALA   A 1  431  ? -49.820 34.526  80.237  1.00 23.56 ? 429  ALA   A O     1 
ATOM   3142  C  CB    . ALA   A 1  431  ? -46.760 33.779  79.290  1.00 24.60 ? 429  ALA   A CB    1 
ATOM   3143  N  N     . ALA   A 1  432  ? -48.223 35.507  81.492  1.00 25.55 ? 430  ALA   A N     1 
ATOM   3144  C  CA    . ALA   A 1  432  ? -49.083 35.591  82.667  1.00 25.88 ? 430  ALA   A CA    1 
ATOM   3145  C  C     . ALA   A 1  432  ? -50.321 36.426  82.379  1.00 26.87 ? 430  ALA   A C     1 
ATOM   3146  O  O     . ALA   A 1  432  ? -51.434 36.063  82.779  1.00 26.39 ? 430  ALA   A O     1 
ATOM   3147  C  CB    . ALA   A 1  432  ? -48.298 36.184  83.838  1.00 24.52 ? 430  ALA   A CB    1 
ATOM   3148  N  N     . ILE   A 1  433  ? -50.154 37.529  81.656  1.00 25.46 ? 431  ILE   A N     1 
ATOM   3149  C  CA    . ILE   A 1  433  ? -51.275 38.417  81.378  1.00 20.85 ? 431  ILE   A CA    1 
ATOM   3150  C  C     . ILE   A 1  433  ? -52.152 37.850  80.279  1.00 23.20 ? 431  ILE   A C     1 
ATOM   3151  O  O     . ILE   A 1  433  ? -53.381 37.930  80.349  1.00 24.47 ? 431  ILE   A O     1 
ATOM   3152  C  CB    . ILE   A 1  433  ? -50.726 39.810  81.030  1.00 22.19 ? 431  ILE   A CB    1 
ATOM   3153  C  CG1   . ILE   A 1  433  ? -50.102 40.423  82.284  1.00 27.50 ? 431  ILE   A CG1   1 
ATOM   3154  C  CG2   . ILE   A 1  433  ? -51.808 40.682  80.413  1.00 23.00 ? 431  ILE   A CG2   1 
ATOM   3155  C  CD1   . ILE   A 1  433  ? -49.392 41.696  82.026  1.00 27.27 ? 431  ILE   A CD1   1 
ATOM   3156  N  N     . TYR   A 1  434  ? -51.533 37.256  79.258  1.00 22.25 ? 432  TYR   A N     1 
ATOM   3157  C  CA    . TYR   A 1  434  ? -52.286 36.629  78.182  1.00 23.46 ? 432  TYR   A CA    1 
ATOM   3158  C  C     . TYR   A 1  434  ? -53.279 35.615  78.732  1.00 24.51 ? 432  TYR   A C     1 
ATOM   3159  O  O     . TYR   A 1  434  ? -54.443 35.574  78.313  1.00 28.01 ? 432  TYR   A O     1 
ATOM   3160  C  CB    . TYR   A 1  434  ? -51.305 35.959  77.222  1.00 25.88 ? 432  TYR   A CB    1 
ATOM   3161  C  CG    . TYR   A 1  434  ? -51.943 35.045  76.216  1.00 27.99 ? 432  TYR   A CG    1 
ATOM   3162  C  CD1   . TYR   A 1  434  ? -52.775 35.545  75.223  1.00 27.99 ? 432  TYR   A CD1   1 
ATOM   3163  C  CD2   . TYR   A 1  434  ? -51.711 33.674  76.258  1.00 29.36 ? 432  TYR   A CD2   1 
ATOM   3164  C  CE1   . TYR   A 1  434  ? -53.359 34.707  74.301  1.00 25.97 ? 432  TYR   A CE1   1 
ATOM   3165  C  CE2   . TYR   A 1  434  ? -52.283 32.829  75.338  1.00 31.47 ? 432  TYR   A CE2   1 
ATOM   3166  C  CZ    . TYR   A 1  434  ? -53.108 33.350  74.363  1.00 32.25 ? 432  TYR   A CZ    1 
ATOM   3167  O  OH    . TYR   A 1  434  ? -53.680 32.508  73.443  1.00 35.33 ? 432  TYR   A OH    1 
ATOM   3168  N  N     . HIS   A 1  435  ? -52.837 34.790  79.681  1.00 25.84 ? 433  HIS   A N     1 
ATOM   3169  C  CA    . HIS   A 1  435  ? -53.733 33.804  80.273  1.00 29.81 ? 433  HIS   A CA    1 
ATOM   3170  C  C     . HIS   A 1  435  ? -54.671 34.422  81.298  1.00 29.57 ? 433  HIS   A C     1 
ATOM   3171  O  O     . HIS   A 1  435  ? -55.821 33.981  81.424  1.00 28.27 ? 433  HIS   A O     1 
ATOM   3172  C  CB    . HIS   A 1  435  ? -52.931 32.657  80.872  1.00 29.75 ? 433  HIS   A CB    1 
ATOM   3173  C  CG    . HIS   A 1  435  ? -52.319 31.770  79.838  1.00 33.63 ? 433  HIS   A CG    1 
ATOM   3174  N  ND1   . HIS   A 1  435  ? -53.026 30.770  79.209  1.00 32.72 ? 433  HIS   A ND1   1 
ATOM   3175  C  CD2   . HIS   A 1  435  ? -51.084 31.766  79.282  1.00 28.09 ? 433  HIS   A CD2   1 
ATOM   3176  C  CE1   . HIS   A 1  435  ? -52.244 30.167  78.330  1.00 32.41 ? 433  HIS   A CE1   1 
ATOM   3177  N  NE2   . HIS   A 1  435  ? -51.060 30.752  78.356  1.00 30.13 ? 433  HIS   A NE2   1 
ATOM   3178  N  N     . MET   A 1  436  ? -54.210 35.445  82.022  1.00 26.38 ? 434  MET   A N     1 
ATOM   3179  C  CA    . MET   A 1  436  ? -55.092 36.146  82.951  1.00 26.22 ? 434  MET   A CA    1 
ATOM   3180  C  C     . MET   A 1  436  ? -56.277 36.764  82.222  1.00 26.85 ? 434  MET   A C     1 
ATOM   3181  O  O     . MET   A 1  436  ? -57.407 36.737  82.722  1.00 29.54 ? 434  MET   A O     1 
ATOM   3182  C  CB    . MET   A 1  436  ? -54.305 37.224  83.688  1.00 27.46 ? 434  MET   A CB    1 
ATOM   3183  C  CG    . MET   A 1  436  ? -55.102 37.945  84.738  1.00 27.56 ? 434  MET   A CG    1 
ATOM   3184  S  SD    . MET   A 1  436  ? -54.207 39.362  85.369  1.00 29.03 ? 434  MET   A SD    1 
ATOM   3185  C  CE    . MET   A 1  436  ? -52.946 38.569  86.362  1.00 28.51 ? 434  MET   A CE    1 
ATOM   3186  N  N     . ALA   A 1  437  ? -56.042 37.302  81.025  1.00 24.96 ? 435  ALA   A N     1 
ATOM   3187  C  CA    . ALA   A 1  437  ? -57.091 37.974  80.274  1.00 26.70 ? 435  ALA   A CA    1 
ATOM   3188  C  C     . ALA   A 1  437  ? -58.120 37.004  79.716  1.00 30.04 ? 435  ALA   A C     1 
ATOM   3189  O  O     . ALA   A 1  437  ? -59.250 37.414  79.442  1.00 29.18 ? 435  ALA   A O     1 
ATOM   3190  C  CB    . ALA   A 1  437  ? -56.470 38.791  79.144  1.00 27.49 ? 435  ALA   A CB    1 
ATOM   3191  N  N     . GLY   A 1  438  ? -57.759 35.744  79.529  1.00 35.46 ? 436  GLY   A N     1 
ATOM   3192  C  CA    . GLY   A 1  438  ? -58.733 34.749  79.134  1.00 38.25 ? 436  GLY   A CA    1 
ATOM   3193  C  C     . GLY   A 1  438  ? -58.961 34.690  77.639  1.00 34.30 ? 436  GLY   A C     1 
ATOM   3194  O  O     . GLY   A 1  438  ? -58.317 35.370  76.836  1.00 34.13 ? 436  GLY   A O     1 
ATOM   3195  N  N     . LYS   A 1  439  ? -59.948 33.864  77.271  1.00 41.81 ? 437  LYS   A N     1 
ATOM   3196  C  CA    . LYS   A 1  439  ? -60.171 33.510  75.873  1.00 40.92 ? 437  LYS   A CA    1 
ATOM   3197  C  C     . LYS   A 1  439  ? -60.972 34.560  75.114  1.00 37.48 ? 437  LYS   A C     1 
ATOM   3198  O  O     . LYS   A 1  439  ? -60.811 34.686  73.895  1.00 43.66 ? 437  LYS   A O     1 
ATOM   3199  C  CB    . LYS   A 1  439  ? -60.876 32.154  75.783  1.00 46.74 ? 437  LYS   A CB    1 
ATOM   3200  N  N     . ASP   A 1  440  ? -61.835 35.312  75.795  1.00 34.16 ? 438  ASP   A N     1 
ATOM   3201  C  CA    . ASP   A 1  440  ? -62.633 36.329  75.120  1.00 36.80 ? 438  ASP   A CA    1 
ATOM   3202  C  C     . ASP   A 1  440  ? -61.750 37.518  74.780  1.00 37.96 ? 438  ASP   A C     1 
ATOM   3203  O  O     . ASP   A 1  440  ? -61.197 38.162  75.678  1.00 37.73 ? 438  ASP   A O     1 
ATOM   3204  C  CB    . ASP   A 1  440  ? -63.784 36.778  76.016  1.00 36.37 ? 438  ASP   A CB    1 
ATOM   3205  C  CG    . ASP   A 1  440  ? -64.873 35.732  76.132  1.00 45.00 ? 438  ASP   A CG    1 
ATOM   3206  O  OD1   . ASP   A 1  440  ? -64.747 34.667  75.490  1.00 46.27 ? 438  ASP   A OD1   1 
ATOM   3207  O  OD2   . ASP   A 1  440  ? -65.854 35.977  76.865  1.00 45.71 ? 438  ASP   A OD2   1 
ATOM   3208  N  N     . PHE   A 1  441  ? -61.619 37.817  73.490  1.00 30.78 ? 439  PHE   A N     1 
ATOM   3209  C  CA    . PHE   A 1  441  ? -60.834 38.963  73.071  1.00 27.06 ? 439  PHE   A CA    1 
ATOM   3210  C  C     . PHE   A 1  441  ? -61.470 39.620  71.857  1.00 30.62 ? 439  PHE   A C     1 
ATOM   3211  O  O     . PHE   A 1  441  ? -62.060 38.960  71.000  1.00 29.72 ? 439  PHE   A O     1 
ATOM   3212  C  CB    . PHE   A 1  441  ? -59.369 38.618  72.744  1.00 25.88 ? 439  PHE   A CB    1 
ATOM   3213  C  CG    . PHE   A 1  441  ? -58.554 39.824  72.392  1.00 24.86 ? 439  PHE   A CG    1 
ATOM   3214  C  CD1   . PHE   A 1  441  ? -58.051 40.639  73.392  1.00 25.06 ? 439  PHE   A CD1   1 
ATOM   3215  C  CD2   . PHE   A 1  441  ? -58.354 40.189  71.068  1.00 27.10 ? 439  PHE   A CD2   1 
ATOM   3216  C  CE1   . PHE   A 1  441  ? -57.340 41.773  73.088  1.00 23.92 ? 439  PHE   A CE1   1 
ATOM   3217  C  CE2   . PHE   A 1  441  ? -57.636 41.330  70.760  1.00 24.97 ? 439  PHE   A CE2   1 
ATOM   3218  C  CZ    . PHE   A 1  441  ? -57.140 42.123  71.779  1.00 25.07 ? 439  PHE   A CZ    1 
ATOM   3219  N  N     . HIS   A 1  442  ? -61.336 40.938  71.800  1.00 23.72 ? 440  HIS   A N     1 
ATOM   3220  C  CA    . HIS   A 1  442  ? -61.670 41.702  70.615  1.00 27.35 ? 440  HIS   A CA    1 
ATOM   3221  C  C     . HIS   A 1  442  ? -60.721 42.884  70.589  1.00 30.85 ? 440  HIS   A C     1 
ATOM   3222  O  O     . HIS   A 1  442  ? -60.237 43.323  71.638  1.00 24.90 ? 440  HIS   A O     1 
ATOM   3223  C  CB    . HIS   A 1  442  ? -63.119 42.191  70.659  1.00 27.59 ? 440  HIS   A CB    1 
ATOM   3224  C  CG    . HIS   A 1  442  ? -63.415 43.092  71.815  1.00 24.45 ? 440  HIS   A CG    1 
ATOM   3225  N  ND1   . HIS   A 1  442  ? -63.779 42.617  73.057  1.00 29.27 ? 440  HIS   A ND1   1 
ATOM   3226  C  CD2   . HIS   A 1  442  ? -63.395 44.442  71.917  1.00 26.81 ? 440  HIS   A CD2   1 
ATOM   3227  C  CE1   . HIS   A 1  442  ? -63.973 43.639  73.874  1.00 27.24 ? 440  HIS   A CE1   1 
ATOM   3228  N  NE2   . HIS   A 1  442  ? -63.746 44.756  73.207  1.00 27.06 ? 440  HIS   A NE2   1 
ATOM   3229  N  N     . VAL   A 1  443  ? -60.438 43.382  69.385  1.00 27.98 ? 441  VAL   A N     1 
ATOM   3230  C  CA    . VAL   A 1  443  ? -59.577 44.550  69.274  1.00 32.11 ? 441  VAL   A CA    1 
ATOM   3231  C  C     . VAL   A 1  443  ? -60.250 45.710  69.984  1.00 29.14 ? 441  VAL   A C     1 
ATOM   3232  O  O     . VAL   A 1  443  ? -61.438 45.990  69.769  1.00 27.94 ? 441  VAL   A O     1 
ATOM   3233  C  CB    . VAL   A 1  443  ? -59.251 44.860  67.805  1.00 31.52 ? 441  VAL   A CB    1 
ATOM   3234  C  CG1   . VAL   A 1  443  ? -58.622 46.239  67.687  1.00 31.93 ? 441  VAL   A CG1   1 
ATOM   3235  C  CG2   . VAL   A 1  443  ? -58.306 43.805  67.245  1.00 37.30 ? 441  VAL   A CG2   1 
ATOM   3236  N  N     . GLY   A 1  444  ? -59.501 46.371  70.862  1.00 25.04 ? 442  GLY   A N     1 
ATOM   3237  C  CA    . GLY   A 1  444  ? -60.051 47.376  71.736  1.00 22.43 ? 442  GLY   A CA    1 
ATOM   3238  C  C     . GLY   A 1  444  ? -60.239 46.922  73.166  1.00 21.74 ? 442  GLY   A C     1 
ATOM   3239  O  O     . GLY   A 1  444  ? -60.479 47.764  74.036  1.00 21.68 ? 442  GLY   A O     1 
ATOM   3240  N  N     . LYS   A 1  445  ? -60.140 45.623  73.441  1.00 21.18 ? 443  LYS   A N     1 
ATOM   3241  C  CA    . LYS   A 1  445  ? -60.285 45.183  74.820  1.00 20.44 ? 443  LYS   A CA    1 
ATOM   3242  C  C     . LYS   A 1  445  ? -59.044 45.537  75.620  1.00 23.57 ? 443  LYS   A C     1 
ATOM   3243  O  O     . LYS   A 1  445  ? -59.134 46.154  76.688  1.00 21.06 ? 443  LYS   A O     1 
ATOM   3244  C  CB    . LYS   A 1  445  ? -60.557 43.687  74.886  1.00 23.06 ? 443  LYS   A CB    1 
ATOM   3245  C  CG    . LYS   A 1  445  ? -60.968 43.277  76.281  1.00 27.32 ? 443  LYS   A CG    1 
ATOM   3246  C  CD    . LYS   A 1  445  ? -61.351 41.826  76.379  1.00 31.44 ? 443  LYS   A CD    1 
ATOM   3247  C  CE    . LYS   A 1  445  ? -62.136 41.591  77.663  1.00 35.66 ? 443  LYS   A CE    1 
ATOM   3248  N  NZ    . LYS   A 1  445  ? -62.468 40.151  77.859  1.00 40.40 ? 443  LYS   A NZ    1 
ATOM   3249  N  N     . TYR   A 1  446  ? -57.883 45.127  75.114  1.00 21.73 ? 444  TYR   A N     1 
ATOM   3250  C  CA    A TYR   A 1  446  ? -56.582 45.501  75.649  0.53 20.38 ? 444  TYR   A CA    1 
ATOM   3251  C  CA    B TYR   A 1  446  ? -56.586 45.531  75.637  0.47 20.38 ? 444  TYR   A CA    1 
ATOM   3252  C  C     . TYR   A 1  446  ? -55.568 45.256  74.544  1.00 19.52 ? 444  TYR   A C     1 
ATOM   3253  O  O     . TYR   A 1  446  ? -55.890 44.690  73.496  1.00 20.27 ? 444  TYR   A O     1 
ATOM   3254  C  CB    A TYR   A 1  446  ? -56.230 44.703  76.910  0.53 19.60 ? 444  TYR   A CB    1 
ATOM   3255  C  CB    B TYR   A 1  446  ? -56.226 44.763  76.909  0.47 19.58 ? 444  TYR   A CB    1 
ATOM   3256  C  CG    A TYR   A 1  446  ? -55.732 43.287  76.664  0.53 20.57 ? 444  TYR   A CG    1 
ATOM   3257  C  CG    B TYR   A 1  446  ? -56.173 43.273  76.692  0.47 21.50 ? 444  TYR   A CG    1 
ATOM   3258  C  CD1   A TYR   A 1  446  ? -56.621 42.223  76.545  0.53 24.23 ? 444  TYR   A CD1   1 
ATOM   3259  C  CD1   B TYR   A 1  446  ? -57.310 42.492  76.844  0.47 20.82 ? 444  TYR   A CD1   1 
ATOM   3260  C  CD2   A TYR   A 1  446  ? -54.371 43.014  76.576  0.53 21.15 ? 444  TYR   A CD2   1 
ATOM   3261  C  CD2   B TYR   A 1  446  ? -54.991 42.648  76.320  0.47 19.24 ? 444  TYR   A CD2   1 
ATOM   3262  C  CE1   A TYR   A 1  446  ? -56.167 40.935  76.330  0.53 20.04 ? 444  TYR   A CE1   1 
ATOM   3263  C  CE1   B TYR   A 1  446  ? -57.269 41.137  76.639  0.47 21.79 ? 444  TYR   A CE1   1 
ATOM   3264  C  CE2   A TYR   A 1  446  ? -53.908 41.728  76.361  0.53 20.81 ? 444  TYR   A CE2   1 
ATOM   3265  C  CE2   B TYR   A 1  446  ? -54.941 41.285  76.109  0.47 22.28 ? 444  TYR   A CE2   1 
ATOM   3266  C  CZ    A TYR   A 1  446  ? -54.810 40.694  76.240  0.53 21.92 ? 444  TYR   A CZ    1 
ATOM   3267  C  CZ    B TYR   A 1  446  ? -56.082 40.537  76.270  0.47 20.85 ? 444  TYR   A CZ    1 
ATOM   3268  O  OH    A TYR   A 1  446  ? -54.346 39.415  76.030  0.53 24.60 ? 444  TYR   A OH    1 
ATOM   3269  O  OH    B TYR   A 1  446  ? -56.042 39.179  76.065  0.47 25.00 ? 444  TYR   A OH    1 
ATOM   3270  N  N     . GLU   A 1  447  ? -54.328 45.668  74.790  1.00 17.44 ? 445  GLU   A N     1 
ATOM   3271  C  CA    . GLU   A 1  447  ? -53.270 45.362  73.840  1.00 18.56 ? 445  GLU   A CA    1 
ATOM   3272  C  C     . GLU   A 1  447  ? -51.978 45.206  74.616  1.00 19.75 ? 445  GLU   A C     1 
ATOM   3273  O  O     . GLU   A 1  447  ? -51.882 45.584  75.782  1.00 19.33 ? 445  GLU   A O     1 
ATOM   3274  C  CB    . GLU   A 1  447  ? -53.115 46.449  72.772  1.00 18.04 ? 445  GLU   A CB    1 
ATOM   3275  C  CG    . GLU   A 1  447  ? -52.588 47.759  73.338  1.00 18.49 ? 445  GLU   A CG    1 
ATOM   3276  C  CD    . GLU   A 1  447  ? -52.550 48.883  72.327  1.00 18.94 ? 445  GLU   A CD    1 
ATOM   3277  O  OE1   . GLU   A 1  447  ? -53.133 48.750  71.232  1.00 21.16 ? 445  GLU   A OE1   1 
ATOM   3278  O  OE2   . GLU   A 1  447  ? -51.931 49.922  72.643  1.00 18.16 ? 445  GLU   A OE2   1 
ATOM   3279  N  N     . PHE   A 1  448  ? -50.976 44.649  73.948  1.00 18.03 ? 446  PHE   A N     1 
ATOM   3280  C  CA    . PHE   A 1  448  ? -49.613 44.689  74.444  1.00 19.29 ? 446  PHE   A CA    1 
ATOM   3281  C  C     . PHE   A 1  448  ? -48.882 45.833  73.767  1.00 15.76 ? 446  PHE   A C     1 
ATOM   3282  O  O     . PHE   A 1  448  ? -49.364 46.421  72.801  1.00 17.60 ? 446  PHE   A O     1 
ATOM   3283  C  CB    . PHE   A 1  448  ? -48.906 43.374  74.144  1.00 20.22 ? 446  PHE   A CB    1 
ATOM   3284  C  CG    . PHE   A 1  448  ? -49.468 42.219  74.890  1.00 20.35 ? 446  PHE   A CG    1 
ATOM   3285  C  CD1   . PHE   A 1  448  ? -49.153 42.027  76.223  1.00 20.16 ? 446  PHE   A CD1   1 
ATOM   3286  C  CD2   . PHE   A 1  448  ? -50.332 41.333  74.263  1.00 20.93 ? 446  PHE   A CD2   1 
ATOM   3287  C  CE1   . PHE   A 1  448  ? -49.689 40.958  76.928  1.00 24.31 ? 446  PHE   A CE1   1 
ATOM   3288  C  CE2   . PHE   A 1  448  ? -50.864 40.254  74.956  1.00 24.80 ? 446  PHE   A CE2   1 
ATOM   3289  C  CZ    . PHE   A 1  448  ? -50.547 40.074  76.292  1.00 22.90 ? 446  PHE   A CZ    1 
ATOM   3290  N  N     . GLN   A 1  449  ? -47.713 46.164  74.300  1.00 16.54 ? 447  GLN   A N     1 
ATOM   3291  C  CA    . GLN   A 1  449  ? -46.877 47.183  73.684  1.00 16.70 ? 447  GLN   A CA    1 
ATOM   3292  C  C     . GLN   A 1  449  ? -45.427 46.779  73.810  1.00 18.01 ? 447  GLN   A C     1 
ATOM   3293  O  O     . GLN   A 1  449  ? -45.038 46.059  74.733  1.00 18.75 ? 447  GLN   A O     1 
ATOM   3294  C  CB    . GLN   A 1  449  ? -47.048 48.562  74.309  1.00 16.62 ? 447  GLN   A CB    1 
ATOM   3295  C  CG    . GLN   A 1  449  ? -48.450 49.083  74.169  1.00 16.37 ? 447  GLN   A CG    1 
ATOM   3296  C  CD    . GLN   A 1  449  ? -48.538 50.573  74.375  1.00 17.81 ? 447  GLN   A CD    1 
ATOM   3297  O  OE1   . GLN   A 1  449  ? -47.592 51.207  74.872  1.00 18.71 ? 447  GLN   A OE1   1 
ATOM   3298  N  NE2   . GLN   A 1  449  ? -49.674 51.154  74.002  1.00 18.20 ? 447  GLN   A NE2   1 
ATOM   3299  N  N     . CYS   A 1  450  ? -44.633 47.248  72.864  1.00 16.95 ? 448  CYS   A N     1 
ATOM   3300  C  CA    . CYS   A 1  450  ? -43.215 46.963  72.905  1.00 17.06 ? 448  CYS   A CA    1 
ATOM   3301  C  C     . CYS   A 1  450  ? -42.472 48.127  72.281  1.00 17.61 ? 448  CYS   A C     1 
ATOM   3302  O  O     . CYS   A 1  450  ? -43.062 49.022  71.672  1.00 19.45 ? 448  CYS   A O     1 
ATOM   3303  C  CB    . CYS   A 1  450  ? -42.886 45.658  72.181  1.00 19.48 ? 448  CYS   A CB    1 
ATOM   3304  S  SG    . CYS   A 1  450  ? -43.002 45.757  70.388  1.00 21.77 ? 448  CYS   A SG    1 
ATOM   3305  N  N     . LEU   A 1  451  ? -41.156 48.088  72.427  1.00 16.54 ? 449  LEU   A N     1 
ATOM   3306  C  CA    . LEU   A 1  451  ? -40.301 49.117  71.865  1.00 18.54 ? 449  LEU   A CA    1 
ATOM   3307  C  C     . LEU   A 1  451  ? -39.822 48.697  70.481  1.00 18.67 ? 449  LEU   A C     1 
ATOM   3308  O  O     . LEU   A 1  451  ? -39.482 47.532  70.250  1.00 20.45 ? 449  LEU   A O     1 
ATOM   3309  C  CB    . LEU   A 1  451  ? -39.104 49.352  72.784  1.00 20.43 ? 449  LEU   A CB    1 
ATOM   3310  C  CG    . LEU   A 1  451  ? -38.057 50.360  72.326  1.00 24.08 ? 449  LEU   A CG    1 
ATOM   3311  C  CD1   . LEU   A 1  451  ? -38.619 51.781  72.261  1.00 23.38 ? 449  LEU   A CD1   1 
ATOM   3312  C  CD2   . LEU   A 1  451  ? -36.869 50.282  73.283  1.00 25.21 ? 449  LEU   A CD2   1 
ATOM   3313  N  N     . HIS   A 1  452  ? -39.824 49.655  69.559  1.00 18.50 ? 450  HIS   A N     1 
ATOM   3314  C  CA    . HIS   A 1  452  ? -39.246 49.434  68.242  1.00 19.67 ? 450  HIS   A CA    1 
ATOM   3315  C  C     . HIS   A 1  452  ? -37.814 48.924  68.350  1.00 20.50 ? 450  HIS   A C     1 
ATOM   3316  O  O     . HIS   A 1  452  ? -37.029 49.392  69.179  1.00 22.85 ? 450  HIS   A O     1 
ATOM   3317  C  CB    . HIS   A 1  452  ? -39.228 50.756  67.476  1.00 18.90 ? 450  HIS   A CB    1 
ATOM   3318  C  CG    . HIS   A 1  452  ? -38.464 50.683  66.193  1.00 18.16 ? 450  HIS   A CG    1 
ATOM   3319  N  ND1   . HIS   A 1  452  ? -39.034 50.271  65.006  1.00 19.93 ? 450  HIS   A ND1   1 
ATOM   3320  C  CD2   . HIS   A 1  452  ? -37.162 50.940  65.919  1.00 20.89 ? 450  HIS   A CD2   1 
ATOM   3321  C  CE1   . HIS   A 1  452  ? -38.118 50.287  64.054  1.00 21.55 ? 450  HIS   A CE1   1 
ATOM   3322  N  NE2   . HIS   A 1  452  ? -36.975 50.687  64.582  1.00 20.97 ? 450  HIS   A NE2   1 
ATOM   3323  N  N     . GLY   A 1  453  ? -37.474 47.977  67.483  1.00 25.96 ? 451  GLY   A N     1 
ATOM   3324  C  CA    . GLY   A 1  453  ? -36.102 47.503  67.423  1.00 25.72 ? 451  GLY   A CA    1 
ATOM   3325  C  C     . GLY   A 1  453  ? -35.655 46.789  68.674  1.00 37.46 ? 451  GLY   A C     1 
ATOM   3326  O  O     . GLY   A 1  453  ? -34.454 46.730  68.962  1.00 36.12 ? 451  GLY   A O     1 
ATOM   3327  N  N     . MET   A 1  454  ? -36.598 46.255  69.437  1.00 25.11 ? 452  MET   A N     1 
ATOM   3328  C  CA    . MET   A 1  454  ? -36.291 45.506  70.643  1.00 24.85 ? 452  MET   A CA    1 
ATOM   3329  C  C     . MET   A 1  454  ? -37.355 44.444  70.860  1.00 25.85 ? 452  MET   A C     1 
ATOM   3330  O  O     . MET   A 1  454  ? -37.041 43.265  71.052  1.00 26.81 ? 452  MET   A O     1 
ATOM   3331  C  CB    . MET   A 1  454  ? -36.221 46.444  71.845  1.00 25.43 ? 452  MET   A CB    1 
ATOM   3332  C  CG    . MET   A 1  454  ? -36.106 45.732  73.166  1.00 26.55 ? 452  MET   A CG    1 
ATOM   3333  S  SD    . MET   A 1  454  ? -34.596 44.761  73.224  1.00 33.92 ? 452  MET   A SD    1 
ATOM   3334  C  CE    . MET   A 1  454  ? -33.366 46.066  73.222  1.00 35.61 ? 452  MET   A CE    1 
ATOM   3335  N  N     . GLY   A 1  455  ? -38.619 44.845  70.799  1.00 23.76 ? 453  GLY   A N     1 
ATOM   3336  C  CA    . GLY   A 1  455  ? -39.694 43.932  71.129  1.00 22.71 ? 453  GLY   A CA    1 
ATOM   3337  C  C     . GLY   A 1  455  ? -40.256 43.106  69.995  1.00 24.71 ? 453  GLY   A C     1 
ATOM   3338  O  O     . GLY   A 1  455  ? -41.031 42.181  70.252  1.00 25.21 ? 453  GLY   A O     1 
ATOM   3339  N  N     . GLU   A 1  456  ? -39.899 43.409  68.746  1.00 24.93 ? 454  GLU   A N     1 
ATOM   3340  C  CA    . GLU   A 1  456  ? -40.515 42.712  67.618  1.00 26.16 ? 454  GLU   A CA    1 
ATOM   3341  C  C     . GLU   A 1  456  ? -40.249 41.213  67.588  1.00 27.04 ? 454  GLU   A C     1 
ATOM   3342  O  O     . GLU   A 1  456  ? -41.176 40.464  67.234  1.00 27.84 ? 454  GLU   A O     1 
ATOM   3343  C  CB    . GLU   A 1  456  ? -40.128 43.361  66.283  1.00 28.26 ? 454  GLU   A CB    1 
ATOM   3344  C  CG    . GLU   A 1  456  ? -40.577 44.798  66.135  1.00 33.90 ? 454  GLU   A CG    1 
ATOM   3345  C  CD    . GLU   A 1  456  ? -39.455 45.760  66.403  1.00 33.79 ? 454  GLU   A CD    1 
ATOM   3346  O  OE1   . GLU   A 1  456  ? -38.558 45.400  67.196  1.00 31.70 ? 454  GLU   A OE1   1 
ATOM   3347  O  OE2   . GLU   A 1  456  ? -39.458 46.866  65.817  1.00 31.62 ? 454  GLU   A OE2   1 
ATOM   3348  N  N     . PRO   A 1  457  ? -39.049 40.711  67.898  1.00 26.61 ? 455  PRO   A N     1 
ATOM   3349  C  CA    . PRO   A 1  457  ? -38.876 39.251  67.928  1.00 28.54 ? 455  PRO   A CA    1 
ATOM   3350  C  C     . PRO   A 1  457  ? -39.870 38.549  68.836  1.00 28.85 ? 455  PRO   A C     1 
ATOM   3351  O  O     . PRO   A 1  457  ? -40.428 37.513  68.455  1.00 29.48 ? 455  PRO   A O     1 
ATOM   3352  C  CB    . PRO   A 1  457  ? -37.427 39.077  68.404  1.00 30.16 ? 455  PRO   A CB    1 
ATOM   3353  C  CG    . PRO   A 1  457  ? -36.742 40.316  67.955  1.00 28.92 ? 455  PRO   A CG    1 
ATOM   3354  C  CD    . PRO   A 1  457  ? -37.768 41.410  68.133  1.00 28.26 ? 455  PRO   A CD    1 
ATOM   3355  N  N     . LEU   A 1  458  ? -40.113 39.101  70.027  1.00 26.03 ? 456  LEU   A N     1 
ATOM   3356  C  CA    . LEU   A 1  458  ? -41.098 38.513  70.929  1.00 25.39 ? 456  LEU   A CA    1 
ATOM   3357  C  C     . LEU   A 1  458  ? -42.503 38.634  70.359  1.00 24.47 ? 456  LEU   A C     1 
ATOM   3358  O  O     . LEU   A 1  458  ? -43.259 37.657  70.324  1.00 24.86 ? 456  LEU   A O     1 
ATOM   3359  C  CB    . LEU   A 1  458  ? -41.020 39.192  72.296  1.00 24.84 ? 456  LEU   A CB    1 
ATOM   3360  C  CG    . LEU   A 1  458  ? -42.099 38.766  73.293  1.00 24.56 ? 456  LEU   A CG    1 
ATOM   3361  C  CD1   . LEU   A 1  458  ? -42.075 37.244  73.490  1.00 22.69 ? 456  LEU   A CD1   1 
ATOM   3362  C  CD2   . LEU   A 1  458  ? -41.882 39.504  74.606  1.00 26.53 ? 456  LEU   A CD2   1 
ATOM   3363  N  N     . TYR   A 1  459  ? -42.872 39.826  69.900  1.00 23.96 ? 457  TYR   A N     1 
ATOM   3364  C  CA    . TYR   A 1  459  ? -44.257 40.055  69.530  1.00 24.88 ? 457  TYR   A CA    1 
ATOM   3365  C  C     . TYR   A 1  459  ? -44.615 39.502  68.160  1.00 24.63 ? 457  TYR   A C     1 
ATOM   3366  O  O     . TYR   A 1  459  ? -45.806 39.335  67.870  1.00 26.55 ? 457  TYR   A O     1 
ATOM   3367  C  CB    . TYR   A 1  459  ? -44.633 41.522  69.734  1.00 21.85 ? 457  TYR   A CB    1 
ATOM   3368  C  CG    . TYR   A 1  459  ? -44.850 41.789  71.196  1.00 20.89 ? 457  TYR   A CG    1 
ATOM   3369  C  CD1   . TYR   A 1  459  ? -46.054 41.447  71.796  1.00 23.03 ? 457  TYR   A CD1   1 
ATOM   3370  C  CD2   . TYR   A 1  459  ? -43.846 42.326  71.986  1.00 23.34 ? 457  TYR   A CD2   1 
ATOM   3371  C  CE1   . TYR   A 1  459  ? -46.263 41.656  73.122  1.00 22.49 ? 457  TYR   A CE1   1 
ATOM   3372  C  CE2   . TYR   A 1  459  ? -44.048 42.544  73.338  1.00 19.79 ? 457  TYR   A CE2   1 
ATOM   3373  C  CZ    . TYR   A 1  459  ? -45.265 42.210  73.893  1.00 22.84 ? 457  TYR   A CZ    1 
ATOM   3374  O  OH    . TYR   A 1  459  ? -45.485 42.419  75.234  1.00 23.54 ? 457  TYR   A OH    1 
ATOM   3375  N  N     . GLU   A 1  460  ? -43.625 39.177  67.327  1.00 24.58 ? 458  GLU   A N     1 
ATOM   3376  C  CA    . GLU   A 1  460  ? -43.936 38.380  66.147  1.00 29.29 ? 458  GLU   A CA    1 
ATOM   3377  C  C     . GLU   A 1  460  ? -44.343 36.955  66.495  1.00 29.21 ? 458  GLU   A C     1 
ATOM   3378  O  O     . GLU   A 1  460  ? -44.848 36.242  65.622  1.00 31.32 ? 458  GLU   A O     1 
ATOM   3379  C  CB    . GLU   A 1  460  ? -42.787 38.419  65.140  1.00 33.17 ? 458  GLU   A CB    1 
ATOM   3380  C  CG    . GLU   A 1  460  ? -42.864 39.640  64.231  1.00 38.39 ? 458  GLU   A CG    1 
ATOM   3381  C  CD    . GLU   A 1  460  ? -41.688 39.754  63.286  1.00 52.23 ? 458  GLU   A CD    1 
ATOM   3382  O  OE1   . GLU   A 1  460  ? -40.706 38.999  63.460  1.00 53.52 ? 458  GLU   A OE1   1 
ATOM   3383  O  OE2   . GLU   A 1  460  ? -41.748 40.602  62.370  1.00 54.47 ? 458  GLU   A OE2   1 
ATOM   3384  N  N     . GLU   A 1  461  ? -44.158 36.541  67.748  1.00 27.35 ? 459  GLU   A N     1 
ATOM   3385  C  CA    . GLU   A 1  461  ? -44.703 35.295  68.267  1.00 29.82 ? 459  GLU   A CA    1 
ATOM   3386  C  C     . GLU   A 1  461  ? -46.052 35.487  68.950  1.00 27.94 ? 459  GLU   A C     1 
ATOM   3387  O  O     . GLU   A 1  461  ? -46.625 34.514  69.455  1.00 30.95 ? 459  GLU   A O     1 
ATOM   3388  C  CB    . GLU   A 1  461  ? -43.715 34.668  69.256  1.00 27.19 ? 459  GLU   A CB    1 
ATOM   3389  C  CG    . GLU   A 1  461  ? -42.321 34.487  68.691  1.00 31.72 ? 459  GLU   A CG    1 
ATOM   3390  C  CD    . GLU   A 1  461  ? -42.301 33.566  67.480  1.00 37.85 ? 459  GLU   A CD    1 
ATOM   3391  O  OE1   . GLU   A 1  461  ? -43.167 32.665  67.396  1.00 35.06 ? 459  GLU   A OE1   1 
ATOM   3392  O  OE2   . GLU   A 1  461  ? -41.420 33.743  66.611  1.00 37.08 ? 459  GLU   A OE2   1 
ATOM   3393  N  N     . VAL   A 1  462  ? -46.571 36.715  68.974  1.00 26.20 ? 460  VAL   A N     1 
ATOM   3394  C  CA    . VAL   A 1  462  ? -47.804 37.056  69.673  1.00 24.02 ? 460  VAL   A CA    1 
ATOM   3395  C  C     . VAL   A 1  462  ? -48.878 37.537  68.703  1.00 26.58 ? 460  VAL   A C     1 
ATOM   3396  O  O     . VAL   A 1  462  ? -50.003 37.020  68.689  1.00 28.60 ? 460  VAL   A O     1 
ATOM   3397  C  CB    . VAL   A 1  462  ? -47.547 38.112  70.776  1.00 25.83 ? 460  VAL   A CB    1 
ATOM   3398  C  CG1   . VAL   A 1  462  ? -48.859 38.570  71.393  1.00 23.60 ? 460  VAL   A CG1   1 
ATOM   3399  C  CG2   . VAL   A 1  462  ? -46.604 37.564  71.838  1.00 25.60 ? 460  VAL   A CG2   1 
ATOM   3400  N  N     . VAL   A 1  463  ? -48.542 38.524  67.871  1.00 24.88 ? 461  VAL   A N     1 
ATOM   3401  C  CA    . VAL   A 1  463  ? -49.502 39.125  66.957  1.00 26.62 ? 461  VAL   A CA    1 
ATOM   3402  C  C     . VAL   A 1  463  ? -49.855 38.144  65.849  1.00 32.31 ? 461  VAL   A C     1 
ATOM   3403  O  O     . VAL   A 1  463  ? -48.991 37.427  65.328  1.00 33.38 ? 461  VAL   A O     1 
ATOM   3404  C  CB    . VAL   A 1  463  ? -48.897 40.408  66.368  1.00 27.13 ? 461  VAL   A CB    1 
ATOM   3405  C  CG1   . VAL   A 1  463  ? -49.858 41.046  65.367  1.00 29.28 ? 461  VAL   A CG1   1 
ATOM   3406  C  CG2   . VAL   A 1  463  ? -48.546 41.379  67.481  1.00 25.51 ? 461  VAL   A CG2   1 
ATOM   3407  N  N     . GLY   A 1  464  ? -51.121 38.119  65.473  1.00 32.30 ? 462  GLY   A N     1 
ATOM   3408  C  CA    . GLY   A 1  464  ? -51.501 37.349  64.310  1.00 34.93 ? 462  GLY   A CA    1 
ATOM   3409  C  C     . GLY   A 1  464  ? -52.279 36.102  64.683  1.00 34.75 ? 462  GLY   A C     1 
ATOM   3410  O  O     . GLY   A 1  464  ? -52.062 35.489  65.737  1.00 32.48 ? 462  GLY   A O     1 
ATOM   3411  N  N     . ARG   A 1  465  ? -53.194 35.709  63.789  1.00 34.44 ? 463  ARG   A N     1 
ATOM   3412  C  CA    . ARG   A 1  465  ? -54.043 34.549  64.038  1.00 36.68 ? 463  ARG   A CA    1 
ATOM   3413  C  C     . ARG   A 1  465  ? -53.225 33.271  64.183  1.00 41.29 ? 463  ARG   A C     1 
ATOM   3414  O  O     . ARG   A 1  465  ? -53.638 32.345  64.892  1.00 44.60 ? 463  ARG   A O     1 
ATOM   3415  C  CB    . ARG   A 1  465  ? -55.070 34.403  62.913  1.00 39.99 ? 463  ARG   A CB    1 
ATOM   3416  N  N     . GLY   A 1  466  ? -52.070 33.199  63.533  1.00 34.70 ? 464  GLY   A N     1 
ATOM   3417  C  CA    . GLY   A 1  466  ? -51.221 32.036  63.676  1.00 34.77 ? 464  GLY   A CA    1 
ATOM   3418  C  C     . GLY   A 1  466  ? -50.391 32.000  64.935  1.00 39.30 ? 464  GLY   A C     1 
ATOM   3419  O  O     . GLY   A 1  466  ? -49.660 31.031  65.168  1.00 37.27 ? 464  GLY   A O     1 
ATOM   3420  N  N     . LYS   A 1  467  ? -50.489 33.039  65.771  1.00 35.52 ? 465  LYS   A N     1 
ATOM   3421  C  CA    . LYS   A 1  467  ? -49.742 33.101  67.022  1.00 31.28 ? 465  LYS   A CA    1 
ATOM   3422  C  C     . LYS   A 1  467  ? -50.755 33.179  68.158  1.00 33.92 ? 465  LYS   A C     1 
ATOM   3423  O  O     . LYS   A 1  467  ? -51.643 32.336  68.225  1.00 37.03 ? 465  LYS   A O     1 
ATOM   3424  C  CB    . LYS   A 1  467  ? -48.705 34.210  66.987  1.00 32.73 ? 465  LYS   A CB    1 
ATOM   3425  C  CG    . LYS   A 1  467  ? -47.707 34.082  65.854  1.00 31.79 ? 465  LYS   A CG    1 
ATOM   3426  C  CD    . LYS   A 1  467  ? -46.776 32.901  66.076  1.00 34.15 ? 465  LYS   A CD    1 
ATOM   3427  C  CE    . LYS   A 1  467  ? -45.705 32.878  65.016  1.00 38.76 ? 465  LYS   A CE    1 
ATOM   3428  N  NZ    . LYS   A 1  467  ? -44.751 31.771  65.245  1.00 36.34 ? 465  LYS   A NZ    1 
ATOM   3429  N  N     . LEU   A 1  468  ? -50.653 34.174  69.044  1.00 31.81 ? 466  LEU   A N     1 
ATOM   3430  C  CA    . LEU   A 1  468  ? -51.601 34.361  70.134  1.00 29.45 ? 466  LEU   A CA    1 
ATOM   3431  C  C     . LEU   A 1  468  ? -52.770 35.254  69.750  1.00 31.35 ? 466  LEU   A C     1 
ATOM   3432  O  O     . LEU   A 1  468  ? -53.710 35.386  70.541  1.00 30.13 ? 466  LEU   A O     1 
ATOM   3433  C  CB    . LEU   A 1  468  ? -50.893 34.936  71.362  1.00 29.51 ? 466  LEU   A CB    1 
ATOM   3434  C  CG    . LEU   A 1  468  ? -49.735 34.089  71.912  1.00 30.86 ? 466  LEU   A CG    1 
ATOM   3435  C  CD1   . LEU   A 1  468  ? -49.270 34.586  73.269  1.00 31.12 ? 466  LEU   A CD1   1 
ATOM   3436  C  CD2   . LEU   A 1  468  ? -50.128 32.617  71.983  1.00 37.20 ? 466  LEU   A CD2   1 
ATOM   3437  N  N     . ASP   A 1  469  ? -52.730 35.859  68.561  1.00 31.00 ? 467  ASP   A N     1 
ATOM   3438  C  CA    . ASP   A 1  469  ? -53.803 36.710  68.056  1.00 27.95 ? 467  ASP   A CA    1 
ATOM   3439  C  C     . ASP   A 1  469  ? -54.136 37.818  69.046  1.00 27.14 ? 467  ASP   A C     1 
ATOM   3440  O  O     . ASP   A 1  469  ? -55.300 38.086  69.353  1.00 25.82 ? 467  ASP   A O     1 
ATOM   3441  C  CB    . ASP   A 1  469  ? -55.044 35.897  67.686  1.00 30.78 ? 467  ASP   A CB    1 
ATOM   3442  C  CG    . ASP   A 1  469  ? -55.959 36.639  66.737  1.00 35.25 ? 467  ASP   A CG    1 
ATOM   3443  O  OD1   . ASP   A 1  469  ? -55.474 37.517  65.993  1.00 36.91 ? 467  ASP   A OD1   1 
ATOM   3444  O  OD2   . ASP   A 1  469  ? -57.173 36.348  66.740  1.00 43.48 ? 467  ASP   A OD2   1 
ATOM   3445  N  N     . ARG   A 1  470  ? -53.085 38.457  69.560  1.00 27.79 ? 468  ARG   A N     1 
ATOM   3446  C  CA    . ARG   A 1  470  ? -53.217 39.642  70.381  1.00 24.08 ? 468  ARG   A CA    1 
ATOM   3447  C  C     . ARG   A 1  470  ? -52.412 40.778  69.767  1.00 24.60 ? 468  ARG   A C     1 
ATOM   3448  O  O     . ARG   A 1  470  ? -51.299 40.556  69.280  1.00 24.35 ? 468  ARG   A O     1 
ATOM   3449  C  CB    . ARG   A 1  470  ? -52.729 39.393  71.817  1.00 23.42 ? 468  ARG   A CB    1 
ATOM   3450  C  CG    . ARG   A 1  470  ? -53.524 38.326  72.561  1.00 21.65 ? 468  ARG   A CG    1 
ATOM   3451  C  CD    . ARG   A 1  470  ? -54.962 38.756  72.801  1.00 25.05 ? 468  ARG   A CD    1 
ATOM   3452  N  NE    . ARG   A 1  470  ? -55.724 37.685  73.433  1.00 28.34 ? 468  ARG   A NE    1 
ATOM   3453  C  CZ    . ARG   A 1  470  ? -56.437 36.786  72.770  1.00 28.11 ? 468  ARG   A CZ    1 
ATOM   3454  N  NH1   . ARG   A 1  470  ? -56.530 36.814  71.450  1.00 29.39 ? 468  ARG   A NH1   1 
ATOM   3455  N  NH2   . ARG   A 1  470  ? -57.084 35.842  73.450  1.00 32.07 ? 468  ARG   A NH2   1 
ATOM   3456  N  N     . PRO   A 1  471  ? -52.956 41.989  69.750  1.00 22.77 ? 469  PRO   A N     1 
ATOM   3457  C  CA    . PRO   A 1  471  ? -52.269 43.111  69.109  1.00 21.31 ? 469  PRO   A CA    1 
ATOM   3458  C  C     . PRO   A 1  471  ? -51.157 43.659  69.982  1.00 22.70 ? 469  PRO   A C     1 
ATOM   3459  O  O     . PRO   A 1  471  ? -51.157 43.534  71.211  1.00 20.28 ? 469  PRO   A O     1 
ATOM   3460  C  CB    . PRO   A 1  471  ? -53.381 44.156  68.958  1.00 22.41 ? 469  PRO   A CB    1 
ATOM   3461  C  CG    . PRO   A 1  471  ? -54.303 43.857  70.100  1.00 24.49 ? 469  PRO   A CG    1 
ATOM   3462  C  CD    . PRO   A 1  471  ? -54.279 42.367  70.262  1.00 21.65 ? 469  PRO   A CD    1 
ATOM   3463  N  N     . CYS   A 1  472  ? -50.193 44.276  69.317  1.00 20.75 ? 470  CYS   A N     1 
ATOM   3464  C  CA    . CYS   A 1  472  ? -49.100 44.939  69.996  1.00 19.05 ? 470  CYS   A CA    1 
ATOM   3465  C  C     . CYS   A 1  472  ? -48.889 46.286  69.337  1.00 19.73 ? 470  CYS   A C     1 
ATOM   3466  O  O     . CYS   A 1  472  ? -48.828 46.371  68.106  1.00 21.07 ? 470  CYS   A O     1 
ATOM   3467  C  CB    . CYS   A 1  472  ? -47.820 44.117  69.866  1.00 21.08 ? 470  CYS   A CB    1 
ATOM   3468  S  SG    . CYS   A 1  472  ? -46.436 44.840  70.735  1.00 22.15 ? 470  CYS   A SG    1 
ATOM   3469  N  N     . ARG   A 1  473  ? -48.754 47.321  70.153  1.00 17.87 ? 471  ARG   A N     1 
ATOM   3470  C  CA    . ARG   A 1  473  ? -48.433 48.660  69.687  1.00 16.86 ? 471  ARG   A CA    1 
ATOM   3471  C  C     . ARG   A 1  473  ? -46.948 48.901  69.898  1.00 19.34 ? 471  ARG   A C     1 
ATOM   3472  O  O     . ARG   A 1  473  ? -46.440 48.749  71.010  1.00 18.91 ? 471  ARG   A O     1 
ATOM   3473  C  CB    . ARG   A 1  473  ? -49.235 49.717  70.447  1.00 18.66 ? 471  ARG   A CB    1 
ATOM   3474  C  CG    . ARG   A 1  473  ? -49.054 51.120  69.874  1.00 18.77 ? 471  ARG   A CG    1 
ATOM   3475  C  CD    . ARG   A 1  473  ? -49.970 52.112  70.560  1.00 17.23 ? 471  ARG   A CD    1 
ATOM   3476  N  NE    . ARG   A 1  473  ? -51.346 51.627  70.531  1.00 17.70 ? 471  ARG   A NE    1 
ATOM   3477  C  CZ    . ARG   A 1  473  ? -52.177 51.780  69.513  1.00 21.23 ? 471  ARG   A CZ    1 
ATOM   3478  N  NH1   . ARG   A 1  473  ? -51.858 52.516  68.459  1.00 19.76 ? 471  ARG   A NH1   1 
ATOM   3479  N  NH2   . ARG   A 1  473  ? -53.356 51.168  69.548  1.00 19.39 ? 471  ARG   A NH2   1 
ATOM   3480  N  N     . ILE   A 1  474  ? -46.271 49.308  68.834  1.00 17.20 ? 472  ILE   A N     1 
ATOM   3481  C  CA    . ILE   A 1  474  ? -44.830 49.508  68.853  1.00 16.76 ? 472  ILE   A CA    1 
ATOM   3482  C  C     . ILE   A 1  474  ? -44.565 50.961  69.199  1.00 17.23 ? 472  ILE   A C     1 
ATOM   3483  O  O     . ILE   A 1  474  ? -45.040 51.869  68.510  1.00 18.03 ? 472  ILE   A O     1 
ATOM   3484  C  CB    . ILE   A 1  474  ? -44.224 49.152  67.494  1.00 17.61 ? 472  ILE   A CB    1 
ATOM   3485  C  CG1   . ILE   A 1  474  ? -44.417 47.669  67.201  1.00 22.28 ? 472  ILE   A CG1   1 
ATOM   3486  C  CG2   . ILE   A 1  474  ? -42.739 49.499  67.476  1.00 19.63 ? 472  ILE   A CG2   1 
ATOM   3487  C  CD1   . ILE   A 1  474  ? -44.094 47.313  65.775  1.00 23.28 ? 472  ILE   A CD1   1 
ATOM   3488  N  N     . TYR   A 1  475  ? -43.816 51.184  70.272  1.00 17.51 ? 473  TYR   A N     1 
ATOM   3489  C  CA    . TYR   A 1  475  ? -43.400 52.522  70.657  1.00 18.97 ? 473  TYR   A CA    1 
ATOM   3490  C  C     . TYR   A 1  475  ? -42.194 52.867  69.803  1.00 18.74 ? 473  TYR   A C     1 
ATOM   3491  O  O     . TYR   A 1  475  ? -41.156 52.196  69.870  1.00 17.95 ? 473  TYR   A O     1 
ATOM   3492  C  CB    . TYR   A 1  475  ? -43.049 52.525  72.142  1.00 19.71 ? 473  TYR   A CB    1 
ATOM   3493  C  CG    . TYR   A 1  475  ? -42.728 53.866  72.775  1.00 18.72 ? 473  TYR   A CG    1 
ATOM   3494  C  CD1   . TYR   A 1  475  ? -43.722 54.639  73.362  1.00 20.31 ? 473  TYR   A CD1   1 
ATOM   3495  C  CD2   . TYR   A 1  475  ? -41.422 54.344  72.807  1.00 24.85 ? 473  TYR   A CD2   1 
ATOM   3496  C  CE1   . TYR   A 1  475  ? -43.425 55.858  73.956  1.00 19.00 ? 473  TYR   A CE1   1 
ATOM   3497  C  CE2   . TYR   A 1  475  ? -41.119 55.562  73.393  1.00 26.05 ? 473  TYR   A CE2   1 
ATOM   3498  C  CZ    . TYR   A 1  475  ? -42.126 56.314  73.967  1.00 25.56 ? 473  TYR   A CZ    1 
ATOM   3499  O  OH    . TYR   A 1  475  ? -41.820 57.530  74.542  1.00 29.28 ? 473  TYR   A OH    1 
ATOM   3500  N  N     . ALA   A 1  476  ? -42.359 53.877  68.964  1.00 18.58 ? 474  ALA   A N     1 
ATOM   3501  C  CA    . ALA   A 1  476  ? -41.477 54.102  67.822  1.00 17.56 ? 474  ALA   A CA    1 
ATOM   3502  C  C     . ALA   A 1  476  ? -40.763 55.423  68.005  1.00 16.86 ? 474  ALA   A C     1 
ATOM   3503  O  O     . ALA   A 1  476  ? -41.346 56.488  67.751  1.00 16.92 ? 474  ALA   A O     1 
ATOM   3504  C  CB    . ALA   A 1  476  ? -42.301 54.115  66.539  1.00 20.68 ? 474  ALA   A CB    1 
ATOM   3505  N  N     . PRO   A 1  477  ? -39.501 55.416  68.424  1.00 18.04 ? 475  PRO   A N     1 
ATOM   3506  C  CA    . PRO   A 1  477  ? -38.771 56.678  68.536  1.00 17.65 ? 475  PRO   A CA    1 
ATOM   3507  C  C     . PRO   A 1  477  ? -38.542 57.266  67.156  1.00 16.23 ? 475  PRO   A C     1 
ATOM   3508  O  O     . PRO   A 1  477  ? -38.327 56.545  66.180  1.00 17.67 ? 475  PRO   A O     1 
ATOM   3509  C  CB    . PRO   A 1  477  ? -37.442 56.264  69.182  1.00 18.35 ? 475  PRO   A CB    1 
ATOM   3510  C  CG    . PRO   A 1  477  ? -37.699 54.887  69.755  1.00 21.04 ? 475  PRO   A CG    1 
ATOM   3511  C  CD    . PRO   A 1  477  ? -38.683 54.260  68.824  1.00 17.97 ? 475  PRO   A CD    1 
ATOM   3512  N  N     . VAL   A 1  478  ? -38.605 58.587  67.085  1.00 15.49 ? 476  VAL   A N     1 
ATOM   3513  C  CA    . VAL   A 1  478  ? -38.434 59.313  65.838  1.00 17.91 ? 476  VAL   A CA    1 
ATOM   3514  C  C     . VAL   A 1  478  ? -37.476 60.457  66.111  1.00 19.35 ? 476  VAL   A C     1 
ATOM   3515  O  O     . VAL   A 1  478  ? -37.727 61.281  66.995  1.00 21.39 ? 476  VAL   A O     1 
ATOM   3516  C  CB    . VAL   A 1  478  ? -39.776 59.865  65.338  1.00 17.10 ? 476  VAL   A CB    1 
ATOM   3517  C  CG1   . VAL   A 1  478  ? -39.580 60.636  64.036  1.00 18.14 ? 476  VAL   A CG1   1 
ATOM   3518  C  CG2   . VAL   A 1  478  ? -40.771 58.734  65.133  1.00 19.88 ? 476  VAL   A CG2   1 
ATOM   3519  N  N     . GLY   A 1  479  ? -36.385 60.518  65.365  1.00 19.23 ? 477  GLY   A N     1 
ATOM   3520  C  CA    . GLY   A 1  479  ? -35.497 61.642  65.571  1.00 22.12 ? 477  GLY   A CA    1 
ATOM   3521  C  C     . GLY   A 1  479  ? -34.169 61.436  64.890  1.00 21.94 ? 477  GLY   A C     1 
ATOM   3522  O  O     . GLY   A 1  479  ? -33.842 60.351  64.401  1.00 21.92 ? 477  GLY   A O     1 
ATOM   3523  N  N     . THR   A 1  480  ? -33.400 62.514  64.888  1.00 25.03 ? 478  THR   A N     1 
ATOM   3524  C  CA    . THR   A 1  480  ? -32.073 62.542  64.303  1.00 26.48 ? 478  THR   A CA    1 
ATOM   3525  C  C     . THR   A 1  480  ? -31.084 61.837  65.219  1.00 29.65 ? 478  THR   A C     1 
ATOM   3526  O  O     . THR   A 1  480  ? -31.401 61.458  66.349  1.00 30.07 ? 478  THR   A O     1 
ATOM   3527  C  CB    . THR   A 1  480  ? -31.622 63.989  64.131  1.00 28.05 ? 478  THR   A CB    1 
ATOM   3528  O  OG1   . THR   A 1  480  ? -31.649 64.638  65.412  1.00 32.35 ? 478  THR   A OG1   1 
ATOM   3529  C  CG2   . THR   A 1  480  ? -32.539 64.720  63.181  1.00 29.86 ? 478  THR   A CG2   1 
ATOM   3530  N  N     . HIS   A 1  481  ? -29.857 61.687  64.717  1.00 31.45 ? 479  HIS   A N     1 
ATOM   3531  C  CA    . HIS   A 1  481  ? -28.796 61.078  65.514  1.00 35.44 ? 479  HIS   A CA    1 
ATOM   3532  C  C     . HIS   A 1  481  ? -28.558 61.846  66.808  1.00 35.50 ? 479  HIS   A C     1 
ATOM   3533  O  O     . HIS   A 1  481  ? -28.380 61.240  67.872  1.00 33.26 ? 479  HIS   A O     1 
ATOM   3534  C  CB    . HIS   A 1  481  ? -27.500 61.022  64.709  1.00 29.96 ? 479  HIS   A CB    1 
ATOM   3535  C  CG    . HIS   A 1  481  ? -27.585 60.186  63.470  1.00 33.59 ? 479  HIS   A CG    1 
ATOM   3536  N  ND1   . HIS   A 1  481  ? -26.529 60.061  62.592  1.00 32.96 ? 479  HIS   A ND1   1 
ATOM   3537  C  CD2   . HIS   A 1  481  ? -28.588 59.429  62.963  1.00 33.24 ? 479  HIS   A CD2   1 
ATOM   3538  C  CE1   . HIS   A 1  481  ? -26.879 59.269  61.594  1.00 35.62 ? 479  HIS   A CE1   1 
ATOM   3539  N  NE2   . HIS   A 1  481  ? -28.122 58.869  61.797  1.00 35.94 ? 479  HIS   A NE2   1 
ATOM   3540  N  N     . GLU   A 1  482  ? -28.533 63.180  66.739  1.00 36.76 ? 480  GLU   A N     1 
ATOM   3541  C  CA    . GLU   A 1  482  ? -28.301 63.972  67.944  1.00 37.49 ? 480  GLU   A CA    1 
ATOM   3542  C  C     . GLU   A 1  482  ? -29.402 63.746  68.971  1.00 39.39 ? 480  GLU   A C     1 
ATOM   3543  O  O     . GLU   A 1  482  ? -29.130 63.616  70.171  1.00 37.97 ? 480  GLU   A O     1 
ATOM   3544  C  CB    . GLU   A 1  482  ? -28.202 65.455  67.588  1.00 40.89 ? 480  GLU   A CB    1 
ATOM   3545  N  N     . THR   A 1  483  ? -30.654 63.687  68.515  1.00 33.27 ? 481  THR   A N     1 
ATOM   3546  C  CA    . THR   A 1  483  ? -31.769 63.543  69.441  1.00 33.58 ? 481  THR   A CA    1 
ATOM   3547  C  C     . THR   A 1  483  ? -31.779 62.165  70.092  1.00 36.91 ? 481  THR   A C     1 
ATOM   3548  O  O     . THR   A 1  483  ? -32.071 62.041  71.287  1.00 34.28 ? 481  THR   A O     1 
ATOM   3549  C  CB    . THR   A 1  483  ? -33.086 63.797  68.712  1.00 33.07 ? 481  THR   A CB    1 
ATOM   3550  O  OG1   . THR   A 1  483  ? -33.033 65.064  68.049  1.00 40.89 ? 481  THR   A OG1   1 
ATOM   3551  C  CG2   . THR   A 1  483  ? -34.238 63.816  69.701  1.00 42.41 ? 481  THR   A CG2   1 
ATOM   3552  N  N     . LEU   A 1  484  ? -31.469 61.117  69.324  1.00 31.66 ? 482  LEU   A N     1 
ATOM   3553  C  CA    . LEU   A 1  484  ? -31.569 59.768  69.874  1.00 31.69 ? 482  LEU   A CA    1 
ATOM   3554  C  C     . LEU   A 1  484  ? -30.426 59.467  70.836  1.00 32.09 ? 482  LEU   A C     1 
ATOM   3555  O  O     . LEU   A 1  484  ? -30.609 58.727  71.808  1.00 33.61 ? 482  LEU   A O     1 
ATOM   3556  C  CB    . LEU   A 1  484  ? -31.641 58.732  68.750  1.00 32.49 ? 482  LEU   A CB    1 
ATOM   3557  C  CG    . LEU   A 1  484  ? -30.423 58.552  67.841  1.00 34.78 ? 482  LEU   A CG    1 
ATOM   3558  C  CD1   . LEU   A 1  484  ? -29.464 57.502  68.392  1.00 36.76 ? 482  LEU   A CD1   1 
ATOM   3559  C  CD2   . LEU   A 1  484  ? -30.860 58.186  66.432  1.00 34.58 ? 482  LEU   A CD2   1 
ATOM   3560  N  N     . LEU   A 1  485  ? -29.242 60.025  70.584  1.00 34.69 ? 483  LEU   A N     1 
ATOM   3561  C  CA    . LEU   A 1  485  ? -28.104 59.738  71.449  1.00 32.38 ? 483  LEU   A CA    1 
ATOM   3562  C  C     . LEU   A 1  485  ? -28.247 60.369  72.825  1.00 34.79 ? 483  LEU   A C     1 
ATOM   3563  O  O     . LEU   A 1  485  ? -27.584 59.920  73.766  1.00 36.90 ? 483  LEU   A O     1 
ATOM   3564  C  CB    . LEU   A 1  485  ? -26.804 60.202  70.790  1.00 33.42 ? 483  LEU   A CB    1 
ATOM   3565  C  CG    . LEU   A 1  485  ? -26.325 59.374  69.595  1.00 33.86 ? 483  LEU   A CG    1 
ATOM   3566  C  CD1   . LEU   A 1  485  ? -25.159 60.064  68.919  1.00 34.24 ? 483  LEU   A CD1   1 
ATOM   3567  C  CD2   . LEU   A 1  485  ? -25.946 57.958  70.011  1.00 31.98 ? 483  LEU   A CD2   1 
ATOM   3568  N  N     . ALA   A 1  486  ? -29.119 61.375  72.958  1.00 36.56 ? 484  ALA   A N     1 
ATOM   3569  C  CA    . ALA   A 1  486  ? -29.205 62.155  74.188  1.00 36.18 ? 484  ALA   A CA    1 
ATOM   3570  C  C     . ALA   A 1  486  ? -29.544 61.280  75.391  1.00 36.92 ? 484  ALA   A C     1 
ATOM   3571  O  O     . ALA   A 1  486  ? -28.934 61.414  76.459  1.00 38.48 ? 484  ALA   A O     1 
ATOM   3572  C  CB    . ALA   A 1  486  ? -30.239 63.269  74.021  1.00 36.63 ? 484  ALA   A CB    1 
ATOM   3573  N  N     . TYR   A 1  487  ? -30.522 60.382  75.243  1.00 37.98 ? 485  TYR   A N     1 
ATOM   3574  C  CA    . TYR   A 1  487  ? -30.935 59.516  76.344  1.00 40.07 ? 485  TYR   A CA    1 
ATOM   3575  C  C     . TYR   A 1  487  ? -30.975 58.050  75.926  1.00 37.42 ? 485  TYR   A C     1 
ATOM   3576  O  O     . TYR   A 1  487  ? -31.747 57.260  76.475  1.00 31.78 ? 485  TYR   A O     1 
ATOM   3577  C  CB    . TYR   A 1  487  ? -32.266 59.967  76.951  1.00 44.49 ? 485  TYR   A CB    1 
ATOM   3578  C  CG    . TYR   A 1  487  ? -32.235 61.399  77.440  1.00 46.29 ? 485  TYR   A CG    1 
ATOM   3579  C  CD1   . TYR   A 1  487  ? -31.658 61.726  78.663  1.00 48.06 ? 485  TYR   A CD1   1 
ATOM   3580  C  CD2   . TYR   A 1  487  ? -32.766 62.428  76.669  1.00 43.40 ? 485  TYR   A CD2   1 
ATOM   3581  C  CE1   . TYR   A 1  487  ? -31.616 63.038  79.109  1.00 51.89 ? 485  TYR   A CE1   1 
ATOM   3582  C  CE2   . TYR   A 1  487  ? -32.730 63.742  77.104  1.00 47.34 ? 485  TYR   A CE2   1 
ATOM   3583  C  CZ    . TYR   A 1  487  ? -32.155 64.042  78.324  1.00 55.11 ? 485  TYR   A CZ    1 
ATOM   3584  O  OH    . TYR   A 1  487  ? -32.118 65.350  78.759  1.00 53.52 ? 485  TYR   A OH    1 
ATOM   3585  N  N     . LEU   A 1  488  ? -30.136 57.664  74.962  1.00 37.04 ? 486  LEU   A N     1 
ATOM   3586  C  CA    . LEU   A 1  488  ? -30.079 56.261  74.566  1.00 31.08 ? 486  LEU   A CA    1 
ATOM   3587  C  C     . LEU   A 1  488  ? -29.560 55.382  75.698  1.00 29.17 ? 486  LEU   A C     1 
ATOM   3588  O  O     . LEU   A 1  488  ? -29.923 54.203  75.787  1.00 27.56 ? 486  LEU   A O     1 
ATOM   3589  C  CB    . LEU   A 1  488  ? -29.204 56.101  73.326  1.00 32.21 ? 486  LEU   A CB    1 
ATOM   3590  C  CG    . LEU   A 1  488  ? -29.183 54.701  72.713  1.00 38.31 ? 486  LEU   A CG    1 
ATOM   3591  C  CD1   . LEU   A 1  488  ? -30.604 54.218  72.488  1.00 35.68 ? 486  LEU   A CD1   1 
ATOM   3592  C  CD2   . LEU   A 1  488  ? -28.421 54.715  71.409  1.00 28.34 ? 486  LEU   A CD2   1 
ATOM   3593  N  N     . VAL   A 1  489  ? -28.711 55.934  76.567  1.00 34.91 ? 487  VAL   A N     1 
ATOM   3594  C  CA    . VAL   A 1  489  ? -28.179 55.154  77.681  1.00 30.22 ? 487  VAL   A CA    1 
ATOM   3595  C  C     . VAL   A 1  489  ? -29.310 54.642  78.565  1.00 31.23 ? 487  VAL   A C     1 
ATOM   3596  O  O     . VAL   A 1  489  ? -29.360 53.456  78.912  1.00 29.30 ? 487  VAL   A O     1 
ATOM   3597  C  CB    . VAL   A 1  489  ? -27.147 55.975  78.473  1.00 35.52 ? 487  VAL   A CB    1 
ATOM   3598  C  CG1   . VAL   A 1  489  ? -26.831 55.286  79.796  1.00 35.80 ? 487  VAL   A CG1   1 
ATOM   3599  C  CG2   . VAL   A 1  489  ? -25.882 56.165  77.645  1.00 34.45 ? 487  VAL   A CG2   1 
ATOM   3600  N  N     . ARG   A 1  490  ? -30.239 55.527  78.940  1.00 33.09 ? 488  ARG   A N     1 
ATOM   3601  C  CA    . ARG   A 1  490  ? -31.357 55.096  79.775  1.00 36.62 ? 488  ARG   A CA    1 
ATOM   3602  C  C     . ARG   A 1  490  ? -32.203 54.047  79.062  1.00 34.36 ? 488  ARG   A C     1 
ATOM   3603  O  O     . ARG   A 1  490  ? -32.639 53.067  79.678  1.00 35.28 ? 488  ARG   A O     1 
ATOM   3604  C  CB    . ARG   A 1  490  ? -32.214 56.296  80.196  1.00 39.25 ? 488  ARG   A CB    1 
ATOM   3605  C  CG    . ARG   A 1  490  ? -33.333 55.943  81.181  1.00 35.51 ? 488  ARG   A CG    1 
ATOM   3606  C  CD    . ARG   A 1  490  ? -34.249 57.135  81.497  1.00 35.87 ? 488  ARG   A CD    1 
ATOM   3607  N  NE    . ARG   A 1  490  ? -35.101 57.485  80.366  1.00 41.51 ? 488  ARG   A NE    1 
ATOM   3608  C  CZ    . ARG   A 1  490  ? -35.215 58.702  79.848  1.00 37.17 ? 488  ARG   A CZ    1 
ATOM   3609  N  NH1   . ARG   A 1  490  ? -34.575 59.739  80.365  1.00 34.59 ? 488  ARG   A NH1   1 
ATOM   3610  N  NH2   . ARG   A 1  490  ? -35.997 58.885  78.787  1.00 37.60 ? 488  ARG   A NH2   1 
ATOM   3611  N  N     . ARG   A 1  491  ? -32.422 54.224  77.755  1.00 34.67 ? 489  ARG   A N     1 
ATOM   3612  C  CA    . ARG   A 1  491  ? -33.254 53.287  77.010  1.00 35.21 ? 489  ARG   A CA    1 
ATOM   3613  C  C     . ARG   A 1  491  ? -32.584 51.928  76.874  1.00 44.05 ? 489  ARG   A C     1 
ATOM   3614  O  O     . ARG   A 1  491  ? -33.272 50.901  76.859  1.00 37.72 ? 489  ARG   A O     1 
ATOM   3615  C  CB    . ARG   A 1  491  ? -33.590 53.860  75.632  1.00 42.98 ? 489  ARG   A CB    1 
ATOM   3616  N  N     . LEU   A 1  492  ? -31.249 51.899  76.787  1.00 36.57 ? 490  LEU   A N     1 
ATOM   3617  C  CA    . LEU   A 1  492  ? -30.551 50.624  76.654  1.00 39.13 ? 490  LEU   A CA    1 
ATOM   3618  C  C     . LEU   A 1  492  ? -30.560 49.845  77.966  1.00 43.40 ? 490  LEU   A C     1 
ATOM   3619  O  O     . LEU   A 1  492  ? -30.710 48.615  77.966  1.00 36.53 ? 490  LEU   A O     1 
ATOM   3620  C  CB    . LEU   A 1  492  ? -29.121 50.851  76.156  1.00 37.52 ? 490  LEU   A CB    1 
ATOM   3621  C  CG    . LEU   A 1  492  ? -28.957 51.336  74.712  1.00 37.79 ? 490  LEU   A CG    1 
ATOM   3622  C  CD1   . LEU   A 1  492  ? -27.509 51.746  74.429  1.00 38.05 ? 490  LEU   A CD1   1 
ATOM   3623  C  CD2   . LEU   A 1  492  ? -29.420 50.267  73.729  1.00 41.62 ? 490  LEU   A CD2   1 
ATOM   3624  N  N     . LEU   A 1  493  ? -30.407 50.542  79.096  1.00 36.23 ? 491  LEU   A N     1 
ATOM   3625  C  CA    . LEU   A 1  493  ? -30.399 49.861  80.385  1.00 30.73 ? 491  LEU   A CA    1 
ATOM   3626  C  C     . LEU   A 1  493  ? -31.739 49.217  80.710  1.00 39.94 ? 491  LEU   A C     1 
ATOM   3627  O  O     . LEU   A 1  493  ? -31.782 48.289  81.526  1.00 41.00 ? 491  LEU   A O     1 
ATOM   3628  C  CB    . LEU   A 1  493  ? -30.016 50.835  81.499  1.00 38.05 ? 491  LEU   A CB    1 
ATOM   3629  C  CG    . LEU   A 1  493  ? -28.572 51.325  81.504  1.00 40.25 ? 491  LEU   A CG    1 
ATOM   3630  C  CD1   . LEU   A 1  493  ? -28.338 52.219  82.720  1.00 42.81 ? 491  LEU   A CD1   1 
ATOM   3631  C  CD2   . LEU   A 1  493  ? -27.613 50.136  81.491  1.00 41.11 ? 491  LEU   A CD2   1 
ATOM   3632  N  N     . GLU   A 1  494  ? -32.830 49.696  80.102  1.00 42.76 ? 492  GLU   A N     1 
ATOM   3633  C  CA    . GLU   A 1  494  ? -34.144 49.111  80.362  1.00 45.51 ? 492  GLU   A CA    1 
ATOM   3634  C  C     . GLU   A 1  494  ? -34.148 47.623  80.055  1.00 43.67 ? 492  GLU   A C     1 
ATOM   3635  O  O     . GLU   A 1  494  ? -34.738 46.828  80.796  1.00 37.92 ? 492  GLU   A O     1 
ATOM   3636  C  CB    . GLU   A 1  494  ? -35.207 49.803  79.511  1.00 36.94 ? 492  GLU   A CB    1 
ATOM   3637  C  CG    . GLU   A 1  494  ? -35.420 51.274  79.817  1.00 36.19 ? 492  GLU   A CG    1 
ATOM   3638  C  CD    . GLU   A 1  494  ? -36.244 51.958  78.751  1.00 37.86 ? 492  GLU   A CD    1 
ATOM   3639  O  OE1   . GLU   A 1  494  ? -36.797 51.258  77.869  1.00 41.10 ? 492  GLU   A OE1   1 
ATOM   3640  O  OE2   . GLU   A 1  494  ? -36.361 53.198  78.798  1.00 47.51 ? 492  GLU   A OE2   1 
ATOM   3641  N  N     . ASN   A 1  495  ? -33.494 47.231  78.964  1.00 41.59 ? 493  ASN   A N     1 
ATOM   3642  C  CA    . ASN   A 1  495  ? -33.449 45.840  78.534  1.00 41.00 ? 493  ASN   A CA    1 
ATOM   3643  C  C     . ASN   A 1  495  ? -32.030 45.279  78.502  1.00 40.84 ? 493  ASN   A C     1 
ATOM   3644  O  O     . ASN   A 1  495  ? -31.826 44.188  77.959  1.00 42.00 ? 493  ASN   A O     1 
ATOM   3645  C  CB    . ASN   A 1  495  ? -34.124 45.677  77.165  1.00 37.57 ? 493  ASN   A CB    1 
ATOM   3646  C  CG    . ASN   A 1  495  ? -35.530 46.274  77.122  1.00 35.77 ? 493  ASN   A CG    1 
ATOM   3647  O  OD1   . ASN   A 1  495  ? -36.478 45.727  77.713  1.00 33.48 ? 493  ASN   A OD1   1 
ATOM   3648  N  ND2   . ASN   A 1  495  ? -35.675 47.392  76.401  1.00 31.40 ? 493  ASN   A ND2   1 
ATOM   3649  N  N     . GLY   A 1  496  ? -31.050 45.982  79.079  1.00 46.99 ? 494  GLY   A N     1 
ATOM   3650  C  CA    . GLY   A 1  496  ? -29.664 45.549  79.004  1.00 42.98 ? 494  GLY   A CA    1 
ATOM   3651  C  C     . GLY   A 1  496  ? -28.964 45.315  80.332  1.00 48.14 ? 494  GLY   A C     1 
ATOM   3652  O  O     . GLY   A 1  496  ? -27.813 44.865  80.354  1.00 46.97 ? 494  GLY   A O     1 
ATOM   3653  N  N     . ALA   A 1  497  ? -29.632 45.621  81.443  1.00 43.52 ? 495  ALA   A N     1 
ATOM   3654  C  CA    . ALA   A 1  497  ? -29.068 45.346  82.758  1.00 43.81 ? 495  ALA   A CA    1 
ATOM   3655  C  C     . ALA   A 1  497  ? -29.132 43.850  83.060  1.00 39.72 ? 495  ALA   A C     1 
ATOM   3656  O  O     . ALA   A 1  497  ? -29.935 43.108  82.487  1.00 39.91 ? 495  ALA   A O     1 
ATOM   3657  C  CB    . ALA   A 1  497  ? -29.822 46.125  83.837  1.00 38.58 ? 495  ALA   A CB    1 
ATOM   3658  N  N     . ASN   A 1  498  ? -28.276 43.406  83.987  1.00 41.44 ? 496  ASN   A N     1 
ATOM   3659  C  CA    . ASN   A 1  498  ? -28.181 41.974  84.281  1.00 41.04 ? 496  ASN   A CA    1 
ATOM   3660  C  C     . ASN   A 1  498  ? -29.519 41.383  84.715  1.00 36.17 ? 496  ASN   A C     1 
ATOM   3661  O  O     . ASN   A 1  498  ? -29.777 40.195  84.483  1.00 37.49 ? 496  ASN   A O     1 
ATOM   3662  C  CB    . ASN   A 1  498  ? -27.107 41.716  85.340  1.00 43.89 ? 496  ASN   A CB    1 
ATOM   3663  N  N     . SER   A 1  499  ? -30.379 42.185  85.344  1.00 37.40 ? 497  SER   A N     1 
ATOM   3664  C  CA    . SER   A 1  499  ? -31.702 41.730  85.751  1.00 37.96 ? 497  SER   A CA    1 
ATOM   3665  C  C     . SER   A 1  499  ? -32.731 41.805  84.630  1.00 29.40 ? 497  SER   A C     1 
ATOM   3666  O  O     . SER   A 1  499  ? -33.830 41.258  84.785  1.00 32.65 ? 497  SER   A O     1 
ATOM   3667  C  CB    . SER   A 1  499  ? -32.190 42.556  86.945  1.00 36.21 ? 497  SER   A CB    1 
ATOM   3668  O  OG    . SER   A 1  499  ? -31.948 43.936  86.727  1.00 42.77 ? 497  SER   A OG    1 
ATOM   3669  N  N     . SER   A 1  500  ? -32.402 42.454  83.516  1.00 29.62 ? 498  SER   A N     1 
ATOM   3670  C  CA    . SER   A 1  500  ? -33.367 42.658  82.446  1.00 27.03 ? 498  SER   A CA    1 
ATOM   3671  C  C     . SER   A 1  500  ? -33.617 41.368  81.681  1.00 31.82 ? 498  SER   A C     1 
ATOM   3672  O  O     . SER   A 1  500  ? -32.688 40.612  81.388  1.00 31.28 ? 498  SER   A O     1 
ATOM   3673  C  CB    . SER   A 1  500  ? -32.867 43.724  81.477  1.00 32.91 ? 498  SER   A CB    1 
ATOM   3674  O  OG    . SER   A 1  500  ? -32.832 44.987  82.101  1.00 36.31 ? 498  SER   A OG    1 
ATOM   3675  N  N     . PHE   A 1  501  ? -34.888 41.134  81.342  1.00 26.41 ? 499  PHE   A N     1 
ATOM   3676  C  CA    . PHE   A 1  501  ? -35.257 39.946  80.583  1.00 26.63 ? 499  PHE   A CA    1 
ATOM   3677  C  C     . PHE   A 1  501  ? -34.467 39.843  79.289  1.00 32.69 ? 499  PHE   A C     1 
ATOM   3678  O  O     . PHE   A 1  501  ? -34.012 38.759  78.913  1.00 30.47 ? 499  PHE   A O     1 
ATOM   3679  C  CB    . PHE   A 1  501  ? -36.750 39.969  80.254  1.00 26.13 ? 499  PHE   A CB    1 
ATOM   3680  C  CG    . PHE   A 1  501  ? -37.184 38.827  79.383  1.00 26.11 ? 499  PHE   A CG    1 
ATOM   3681  C  CD1   . PHE   A 1  501  ? -37.556 37.625  79.946  1.00 26.94 ? 499  PHE   A CD1   1 
ATOM   3682  C  CD2   . PHE   A 1  501  ? -37.213 38.951  78.003  1.00 27.96 ? 499  PHE   A CD2   1 
ATOM   3683  C  CE1   . PHE   A 1  501  ? -37.957 36.565  79.153  1.00 27.30 ? 499  PHE   A CE1   1 
ATOM   3684  C  CE2   . PHE   A 1  501  ? -37.607 37.890  77.204  1.00 27.80 ? 499  PHE   A CE2   1 
ATOM   3685  C  CZ    . PHE   A 1  501  ? -37.979 36.700  77.782  1.00 30.24 ? 499  PHE   A CZ    1 
ATOM   3686  N  N     . VAL   A 1  502  ? -34.332 40.958  78.571  1.00 31.28 ? 500  VAL   A N     1 
ATOM   3687  C  CA    . VAL   A 1  502  ? -33.697 40.909  77.260  1.00 33.46 ? 500  VAL   A CA    1 
ATOM   3688  C  C     . VAL   A 1  502  ? -32.226 40.550  77.394  1.00 31.74 ? 500  VAL   A C     1 
ATOM   3689  O  O     . VAL   A 1  502  ? -31.672 39.820  76.563  1.00 40.94 ? 500  VAL   A O     1 
ATOM   3690  C  CB    . VAL   A 1  502  ? -33.916 42.227  76.503  1.00 32.44 ? 500  VAL   A CB    1 
ATOM   3691  C  CG1   . VAL   A 1  502  ? -33.037 42.282  75.263  1.00 47.06 ? 500  VAL   A CG1   1 
ATOM   3692  C  CG2   . VAL   A 1  502  ? -35.390 42.381  76.129  1.00 32.16 ? 500  VAL   A CG2   1 
ATOM   3693  N  N     . HIS   A 1  503  ? -31.572 41.041  78.444  1.00 29.23 ? 501  HIS   A N     1 
ATOM   3694  C  CA    . HIS   A 1  503  ? -30.212 40.591  78.718  1.00 30.58 ? 501  HIS   A CA    1 
ATOM   3695  C  C     . HIS   A 1  503  ? -30.196 39.101  79.030  1.00 35.43 ? 501  HIS   A C     1 
ATOM   3696  O  O     . HIS   A 1  503  ? -29.376 38.348  78.493  1.00 34.19 ? 501  HIS   A O     1 
ATOM   3697  C  CB    . HIS   A 1  503  ? -29.624 41.396  79.877  1.00 34.35 ? 501  HIS   A CB    1 
ATOM   3698  C  CG    . HIS   A 1  503  ? -28.244 40.968  80.273  1.00 42.42 ? 501  HIS   A CG    1 
ATOM   3699  N  ND1   . HIS   A 1  503  ? -28.008 40.031  81.258  1.00 39.81 ? 501  HIS   A ND1   1 
ATOM   3700  C  CD2   . HIS   A 1  503  ? -27.026 41.348  79.816  1.00 42.01 ? 501  HIS   A CD2   1 
ATOM   3701  C  CE1   . HIS   A 1  503  ? -26.705 39.854  81.391  1.00 40.19 ? 501  HIS   A CE1   1 
ATOM   3702  N  NE2   . HIS   A 1  503  ? -26.087 40.640  80.527  1.00 39.80 ? 501  HIS   A NE2   1 
ATOM   3703  N  N     . ARG   A 1  504  ? -31.130 38.651  79.869  1.00 29.62 ? 502  ARG   A N     1 
ATOM   3704  C  CA    . ARG   A 1  504  ? -31.109 37.269  80.332  1.00 33.22 ? 502  ARG   A CA    1 
ATOM   3705  C  C     . ARG   A 1  504  ? -31.450 36.287  79.216  1.00 34.74 ? 502  ARG   A C     1 
ATOM   3706  O  O     . ARG   A 1  504  ? -30.886 35.188  79.160  1.00 33.67 ? 502  ARG   A O     1 
ATOM   3707  C  CB    . ARG   A 1  504  ? -32.033 37.112  81.538  1.00 32.64 ? 502  ARG   A CB    1 
ATOM   3708  C  CG    . ARG   A 1  504  ? -31.507 37.839  82.766  1.00 35.47 ? 502  ARG   A CG    1 
ATOM   3709  C  CD    . ARG   A 1  504  ? -32.604 38.134  83.773  1.00 35.63 ? 502  ARG   A CD    1 
ATOM   3710  N  NE    . ARG   A 1  504  ? -33.416 36.958  84.059  1.00 37.73 ? 502  ARG   A NE    1 
ATOM   3711  C  CZ    . ARG   A 1  504  ? -33.049 35.966  84.859  1.00 40.05 ? 502  ARG   A CZ    1 
ATOM   3712  N  NH1   . ARG   A 1  504  ? -31.862 35.951  85.442  1.00 41.68 ? 502  ARG   A NH1   1 
ATOM   3713  N  NH2   . ARG   A 1  504  ? -33.894 34.961  85.075  1.00 40.40 ? 502  ARG   A NH2   1 
ATOM   3714  N  N     . ILE   A 1  505  ? -32.362 36.659  78.312  1.00 34.88 ? 503  ILE   A N     1 
ATOM   3715  C  CA    . ILE   A 1  505  ? -32.693 35.769  77.199  1.00 32.95 ? 503  ILE   A CA    1 
ATOM   3716  C  C     . ILE   A 1  505  ? -31.463 35.497  76.342  1.00 39.09 ? 503  ILE   A C     1 
ATOM   3717  O  O     . ILE   A 1  505  ? -31.303 34.395  75.801  1.00 40.27 ? 503  ILE   A O     1 
ATOM   3718  C  CB    . ILE   A 1  505  ? -33.879 36.310  76.370  1.00 40.69 ? 503  ILE   A CB    1 
ATOM   3719  C  CG1   . ILE   A 1  505  ? -34.278 35.310  75.289  1.00 45.11 ? 503  ILE   A CG1   1 
ATOM   3720  C  CG2   . ILE   A 1  505  ? -33.520 37.595  75.690  1.00 38.71 ? 503  ILE   A CG2   1 
ATOM   3721  C  CD1   . ILE   A 1  505  ? -35.559 34.619  75.565  1.00 34.64 ? 503  ILE   A CD1   1 
ATOM   3722  N  N     . ASN   A 1  506  ? -30.568 36.476  76.223  1.00 36.70 ? 504  ASN   A N     1 
ATOM   3723  C  CA    . ASN   A 1  506  ? -29.338 36.326  75.460  1.00 36.87 ? 504  ASN   A CA    1 
ATOM   3724  C  C     . ASN   A 1  506  ? -28.202 35.714  76.268  1.00 40.05 ? 504  ASN   A C     1 
ATOM   3725  O  O     . ASN   A 1  506  ? -27.103 35.549  75.731  1.00 46.25 ? 504  ASN   A O     1 
ATOM   3726  C  CB    . ASN   A 1  506  ? -28.888 37.678  74.904  1.00 41.04 ? 504  ASN   A CB    1 
ATOM   3727  C  CG    . ASN   A 1  506  ? -29.845 38.229  73.876  1.00 41.21 ? 504  ASN   A CG    1 
ATOM   3728  O  OD1   . ASN   A 1  506  ? -30.428 37.483  73.091  1.00 49.38 ? 504  ASN   A OD1   1 
ATOM   3729  N  ND2   . ASN   A 1  506  ? -30.018 39.544  73.876  1.00 49.51 ? 504  ASN   A ND2   1 
ATOM   3730  N  N     . ASP   A 1  507  ? -28.425 35.391  77.543  1.00 37.08 ? 505  ASP   A N     1 
ATOM   3731  C  CA    . ASP   A 1  507  ? -27.378 34.805  78.367  1.00 39.09 ? 505  ASP   A CA    1 
ATOM   3732  C  C     . ASP   A 1  507  ? -27.526 33.292  78.325  1.00 42.62 ? 505  ASP   A C     1 
ATOM   3733  O  O     . ASP   A 1  507  ? -28.501 32.761  78.878  1.00 38.69 ? 505  ASP   A O     1 
ATOM   3734  C  CB    . ASP   A 1  507  ? -27.477 35.302  79.801  1.00 37.41 ? 505  ASP   A CB    1 
ATOM   3735  C  CG    . ASP   A 1  507  ? -26.294 34.862  80.663  1.00 45.86 ? 505  ASP   A CG    1 
ATOM   3736  O  OD1   . ASP   A 1  507  ? -25.606 33.879  80.303  1.00 46.50 ? 505  ASP   A OD1   1 
ATOM   3737  O  OD2   . ASP   A 1  507  ? -26.055 35.497  81.711  1.00 41.81 ? 505  ASP   A OD2   1 
ATOM   3738  N  N     . PRO   A 1  508  ? -26.588 32.561  77.720  1.00 46.06 ? 506  PRO   A N     1 
ATOM   3739  C  CA    . PRO   A 1  508  ? -26.725 31.097  77.658  1.00 46.60 ? 506  PRO   A CA    1 
ATOM   3740  C  C     . PRO   A 1  508  ? -26.700 30.433  79.019  1.00 42.24 ? 506  PRO   A C     1 
ATOM   3741  O  O     . PRO   A 1  508  ? -27.194 29.307  79.154  1.00 49.47 ? 506  PRO   A O     1 
ATOM   3742  C  CB    . PRO   A 1  508  ? -25.528 30.661  76.799  1.00 48.30 ? 506  PRO   A CB    1 
ATOM   3743  C  CG    . PRO   A 1  508  ? -25.004 31.926  76.160  1.00 51.93 ? 506  PRO   A CG    1 
ATOM   3744  C  CD    . PRO   A 1  508  ? -25.338 33.033  77.106  1.00 43.41 ? 506  PRO   A CD    1 
ATOM   3745  N  N     . LYS   A 1  509  ? -26.137 31.093  80.032  1.00 39.83 ? 507  LYS   A N     1 
ATOM   3746  C  CA    . LYS   A 1  509  ? -26.110 30.536  81.379  1.00 42.35 ? 507  LYS   A CA    1 
ATOM   3747  C  C     . LYS   A 1  509  ? -27.467 30.587  82.070  1.00 43.11 ? 507  LYS   A C     1 
ATOM   3748  O  O     . LYS   A 1  509  ? -27.626 29.966  83.125  1.00 44.63 ? 507  LYS   A O     1 
ATOM   3749  C  CB    . LYS   A 1  509  ? -25.069 31.270  82.224  1.00 48.10 ? 507  LYS   A CB    1 
ATOM   3750  N  N     . VAL   A 1  510  ? -28.440 31.305  81.515  1.00 40.37 ? 508  VAL   A N     1 
ATOM   3751  C  CA    . VAL   A 1  510  ? -29.770 31.420  82.106  1.00 37.63 ? 508  VAL   A CA    1 
ATOM   3752  C  C     . VAL   A 1  510  ? -30.695 30.448  81.385  1.00 31.99 ? 508  VAL   A C     1 
ATOM   3753  O  O     . VAL   A 1  510  ? -30.894 30.552  80.170  1.00 36.83 ? 508  VAL   A O     1 
ATOM   3754  C  CB    . VAL   A 1  510  ? -30.298 32.862  82.025  1.00 38.33 ? 508  VAL   A CB    1 
ATOM   3755  C  CG1   . VAL   A 1  510  ? -31.680 32.958  82.664  1.00 35.50 ? 508  VAL   A CG1   1 
ATOM   3756  C  CG2   . VAL   A 1  510  ? -29.325 33.833  82.688  1.00 35.99 ? 508  VAL   A CG2   1 
ATOM   3757  N  N     . SER   A 1  511  ? -31.260 29.501  82.128  1.00 32.55 ? 509  SER   A N     1 
ATOM   3758  C  CA    . SER   A 1  511  ? -32.108 28.485  81.529  1.00 32.48 ? 509  SER   A CA    1 
ATOM   3759  C  C     . SER   A 1  511  ? -33.510 29.035  81.291  1.00 32.80 ? 509  SER   A C     1 
ATOM   3760  O  O     . SER   A 1  511  ? -33.908 30.063  81.848  1.00 35.73 ? 509  SER   A O     1 
ATOM   3761  C  CB    . SER   A 1  511  ? -32.207 27.261  82.439  1.00 39.79 ? 509  SER   A CB    1 
ATOM   3762  O  OG    . SER   A 1  511  ? -32.915 27.573  83.628  1.00 38.47 ? 509  SER   A OG    1 
ATOM   3763  N  N     . ILE   A 1  512  ? -34.262 28.329  80.446  1.00 34.06 ? 510  ILE   A N     1 
ATOM   3764  C  CA    . ILE   A 1  512  ? -35.653 28.705  80.215  1.00 32.95 ? 510  ILE   A CA    1 
ATOM   3765  C  C     . ILE   A 1  512  ? -36.459 28.563  81.496  1.00 37.51 ? 510  ILE   A C     1 
ATOM   3766  O  O     . ILE   A 1  512  ? -37.325 29.392  81.797  1.00 36.16 ? 510  ILE   A O     1 
ATOM   3767  C  CB    . ILE   A 1  512  ? -36.247 27.897  79.047  1.00 34.41 ? 510  ILE   A CB    1 
ATOM   3768  C  CG1   . ILE   A 1  512  ? -35.497 28.232  77.758  1.00 34.86 ? 510  ILE   A CG1   1 
ATOM   3769  C  CG2   . ILE   A 1  512  ? -37.734 28.181  78.892  1.00 36.45 ? 510  ILE   A CG2   1 
ATOM   3770  C  CD1   . ILE   A 1  512  ? -35.938 27.430  76.575  1.00 42.91 ? 510  ILE   A CD1   1 
ATOM   3771  N  N     . ASP   A 1  513  ? -36.168 27.526  82.286  1.00 37.84 ? 511  ASP   A N     1 
ATOM   3772  C  CA    . ASP   A 1  513  ? -36.845 27.362  83.567  1.00 36.63 ? 511  ASP   A CA    1 
ATOM   3773  C  C     . ASP   A 1  513  ? -36.636 28.574  84.463  1.00 36.23 ? 511  ASP   A C     1 
ATOM   3774  O  O     . ASP   A 1  513  ? -37.561 29.004  85.161  1.00 36.44 ? 511  ASP   A O     1 
ATOM   3775  C  CB    . ASP   A 1  513  ? -36.364 26.086  84.255  1.00 43.26 ? 511  ASP   A CB    1 
ATOM   3776  C  CG    . ASP   A 1  513  ? -36.806 24.840  83.527  1.00 46.25 ? 511  ASP   A CG    1 
ATOM   3777  O  OD1   . ASP   A 1  513  ? -37.942 24.833  83.005  1.00 49.62 ? 511  ASP   A OD1   1 
ATOM   3778  O  OD2   . ASP   A 1  513  ? -36.017 23.873  83.467  1.00 57.23 ? 511  ASP   A OD2   1 
ATOM   3779  N  N     . GLU   A 1  514  ? -35.432 29.146  84.449  1.00 33.20 ? 512  GLU   A N     1 
ATOM   3780  C  CA    . GLU   A 1  514  ? -35.195 30.368  85.209  1.00 36.26 ? 512  GLU   A CA    1 
ATOM   3781  C  C     . GLU   A 1  514  ? -36.003 31.532  84.647  1.00 34.48 ? 512  GLU   A C     1 
ATOM   3782  O  O     . GLU   A 1  514  ? -36.507 32.368  85.406  1.00 35.06 ? 512  GLU   A O     1 
ATOM   3783  C  CB    . GLU   A 1  514  ? -33.700 30.697  85.222  1.00 38.48 ? 512  GLU   A CB    1 
ATOM   3784  C  CG    . GLU   A 1  514  ? -32.869 29.766  86.099  1.00 45.34 ? 512  GLU   A CG    1 
ATOM   3785  C  CD    . GLU   A 1  514  ? -31.379 29.852  85.805  1.00 49.33 ? 512  GLU   A CD    1 
ATOM   3786  O  OE1   . GLU   A 1  514  ? -31.008 29.835  84.614  1.00 47.82 ? 512  GLU   A OE1   1 
ATOM   3787  O  OE2   . GLU   A 1  514  ? -30.580 29.939  86.761  1.00 57.61 ? 512  GLU   A OE2   1 
ATOM   3788  N  N     . LEU   A 1  515  ? -36.148 31.593  83.321  1.00 34.80 ? 513  LEU   A N     1 
ATOM   3789  C  CA    . LEU   A 1  515  ? -36.851 32.712  82.699  1.00 29.96 ? 513  LEU   A CA    1 
ATOM   3790  C  C     . LEU   A 1  515  ? -38.358 32.606  82.875  1.00 30.85 ? 513  LEU   A C     1 
ATOM   3791  O  O     . LEU   A 1  515  ? -39.051 33.629  82.883  1.00 30.39 ? 513  LEU   A O     1 
ATOM   3792  C  CB    . LEU   A 1  515  ? -36.502 32.800  81.215  1.00 32.24 ? 513  LEU   A CB    1 
ATOM   3793  C  CG    . LEU   A 1  515  ? -35.070 33.223  80.897  1.00 33.21 ? 513  LEU   A CG    1 
ATOM   3794  C  CD1   . LEU   A 1  515  ? -34.791 33.047  79.413  1.00 36.43 ? 513  LEU   A CD1   1 
ATOM   3795  C  CD2   . LEU   A 1  515  ? -34.834 34.666  81.330  1.00 34.07 ? 513  LEU   A CD2   1 
ATOM   3796  N  N     . ILE   A 1  516  ? -38.890 31.390  82.986  1.00 32.65 ? 514  ILE   A N     1 
ATOM   3797  C  CA    . ILE   A 1  516  ? -40.322 31.196  83.162  1.00 29.50 ? 514  ILE   A CA    1 
ATOM   3798  C  C     . ILE   A 1  516  ? -40.711 31.097  84.630  1.00 32.05 ? 514  ILE   A C     1 
ATOM   3799  O  O     . ILE   A 1  516  ? -41.880 30.829  84.937  1.00 32.71 ? 514  ILE   A O     1 
ATOM   3800  C  CB    . ILE   A 1  516  ? -40.861 30.011  82.346  1.00 31.71 ? 514  ILE   A CB    1 
ATOM   3801  C  CG1   . ILE   A 1  516  ? -40.310 28.690  82.895  1.00 37.15 ? 514  ILE   A CG1   1 
ATOM   3802  C  CG2   . ILE   A 1  516  ? -40.525 30.190  80.874  1.00 31.68 ? 514  ILE   A CG2   1 
ATOM   3803  C  CD1   . ILE   A 1  516  ? -40.911 27.454  82.257  1.00 36.56 ? 514  ILE   A CD1   1 
ATOM   3804  N  N     . ALA   A 1  517  ? -39.759 31.294  85.542  1.00 29.27 ? 515  ALA   A N     1 
ATOM   3805  C  CA    . ALA   A 1  517  ? -40.087 31.325  86.959  1.00 33.24 ? 515  ALA   A CA    1 
ATOM   3806  C  C     . ALA   A 1  517  ? -41.186 32.347  87.217  1.00 32.73 ? 515  ALA   A C     1 
ATOM   3807  O  O     . ALA   A 1  517  ? -41.162 33.458  86.685  1.00 32.15 ? 515  ALA   A O     1 
ATOM   3808  C  CB    . ALA   A 1  517  ? -38.852 31.684  87.789  1.00 33.46 ? 515  ALA   A CB    1 
ATOM   3809  N  N     . ASP   A 1  518  ? -42.151 31.961  88.043  1.00 29.99 ? 516  ASP   A N     1 
ATOM   3810  C  CA    . ASP   A 1  518  ? -43.300 32.798  88.361  1.00 30.64 ? 516  ASP   A CA    1 
ATOM   3811  C  C     . ASP   A 1  518  ? -42.944 33.740  89.504  1.00 28.49 ? 516  ASP   A C     1 
ATOM   3812  O  O     . ASP   A 1  518  ? -42.784 33.294  90.646  1.00 30.11 ? 516  ASP   A O     1 
ATOM   3813  C  CB    . ASP   A 1  518  ? -44.468 31.905  88.765  1.00 32.64 ? 516  ASP   A CB    1 
ATOM   3814  C  CG    . ASP   A 1  518  ? -45.715 32.688  89.101  1.00 33.37 ? 516  ASP   A CG    1 
ATOM   3815  O  OD1   . ASP   A 1  518  ? -45.749 33.916  88.875  1.00 32.53 ? 516  ASP   A OD1   1 
ATOM   3816  O  OD2   . ASP   A 1  518  ? -46.663 32.053  89.597  1.00 40.06 ? 516  ASP   A OD2   1 
ATOM   3817  N  N     . PRO   A 1  519  ? -42.822 35.045  89.252  1.00 29.51 ? 517  PRO   A N     1 
ATOM   3818  C  CA    . PRO   A 1  519  ? -42.438 35.953  90.340  1.00 29.03 ? 517  PRO   A CA    1 
ATOM   3819  C  C     . PRO   A 1  519  ? -43.440 35.978  91.480  1.00 25.13 ? 517  PRO   A C     1 
ATOM   3820  O  O     . PRO   A 1  519  ? -43.048 36.205  92.632  1.00 29.04 ? 517  PRO   A O     1 
ATOM   3821  C  CB    . PRO   A 1  519  ? -42.325 37.318  89.641  1.00 28.11 ? 517  PRO   A CB    1 
ATOM   3822  C  CG    . PRO   A 1  519  ? -43.165 37.192  88.421  1.00 32.22 ? 517  PRO   A CG    1 
ATOM   3823  C  CD    . PRO   A 1  519  ? -43.087 35.757  87.992  1.00 27.50 ? 517  PRO   A CD    1 
ATOM   3824  N  N     . VAL   A 1  520  ? -44.721 35.755  91.186  1.00 27.78 ? 518  VAL   A N     1 
ATOM   3825  C  CA    . VAL   A 1  520  ? -45.743 35.776  92.229  1.00 26.53 ? 518  VAL   A CA    1 
ATOM   3826  C  C     . VAL   A 1  520  ? -45.479 34.679  93.248  1.00 33.59 ? 518  VAL   A C     1 
ATOM   3827  O  O     . VAL   A 1  520  ? -45.430 34.928  94.457  1.00 31.13 ? 518  VAL   A O     1 
ATOM   3828  C  CB    . VAL   A 1  520  ? -47.145 35.654  91.608  1.00 29.88 ? 518  VAL   A CB    1 
ATOM   3829  C  CG1   . VAL   A 1  520  ? -48.209 35.694  92.696  1.00 32.06 ? 518  VAL   A CG1   1 
ATOM   3830  C  CG2   . VAL   A 1  520  ? -47.368 36.762  90.591  1.00 27.77 ? 518  VAL   A CG2   1 
ATOM   3831  N  N     . GLU   A 1  521  ? -45.286 33.450  92.771  1.00 33.01 ? 519  GLU   A N     1 
ATOM   3832  C  CA    . GLU   A 1  521  ? -45.061 32.343  93.693  1.00 33.55 ? 519  GLU   A CA    1 
ATOM   3833  C  C     . GLU   A 1  521  ? -43.699 32.429  94.362  1.00 33.96 ? 519  GLU   A C     1 
ATOM   3834  O  O     . GLU   A 1  521  ? -43.548 31.988  95.507  1.00 35.67 ? 519  GLU   A O     1 
ATOM   3835  C  CB    . GLU   A 1  521  ? -45.254 31.005  92.984  1.00 36.33 ? 519  GLU   A CB    1 
ATOM   3836  C  CG    . GLU   A 1  521  ? -46.700 30.741  92.599  1.00 40.70 ? 519  GLU   A CG    1 
ATOM   3837  C  CD    . GLU   A 1  521  ? -47.664 30.989  93.748  1.00 44.90 ? 519  GLU   A CD    1 
ATOM   3838  O  OE1   . GLU   A 1  521  ? -47.334 30.631  94.900  1.00 47.96 ? 519  GLU   A OE1   1 
ATOM   3839  O  OE2   . GLU   A 1  521  ? -48.754 31.546  93.501  1.00 47.42 ? 519  GLU   A OE2   1 
ATOM   3840  N  N     . VAL   A 1  522  ? -42.700 32.996  93.680  1.00 31.91 ? 520  VAL   A N     1 
ATOM   3841  C  CA    . VAL   A 1  522  ? -41.382 33.136  94.291  1.00 31.18 ? 520  VAL   A CA    1 
ATOM   3842  C  C     . VAL   A 1  522  ? -41.428 34.137  95.440  1.00 37.87 ? 520  VAL   A C     1 
ATOM   3843  O  O     . VAL   A 1  522  ? -40.897 33.883  96.529  1.00 38.26 ? 520  VAL   A O     1 
ATOM   3844  C  CB    . VAL   A 1  522  ? -40.313 33.498  93.243  1.00 34.39 ? 520  VAL   A CB    1 
ATOM   3845  C  CG1   . VAL   A 1  522  ? -38.980 33.760  93.927  1.00 36.79 ? 520  VAL   A CG1   1 
ATOM   3846  C  CG2   . VAL   A 1  522  ? -40.174 32.385  92.203  1.00 36.34 ? 520  VAL   A CG2   1 
ATOM   3847  N  N     . VAL   A 1  523  ? -42.071 35.289  95.219  1.00 31.23 ? 521  VAL   A N     1 
ATOM   3848  C  CA    . VAL   A 1  523  ? -42.195 36.275  96.288  1.00 31.93 ? 521  VAL   A CA    1 
ATOM   3849  C  C     . VAL   A 1  523  ? -43.023 35.716  97.437  1.00 32.56 ? 521  VAL   A C     1 
ATOM   3850  O  O     . VAL   A 1  523  ? -42.710 35.940  98.613  1.00 35.45 ? 521  VAL   A O     1 
ATOM   3851  C  CB    . VAL   A 1  523  ? -42.777 37.595  95.746  1.00 28.17 ? 521  VAL   A CB    1 
ATOM   3852  C  CG1   . VAL   A 1  523  ? -43.104 38.537  96.892  1.00 32.91 ? 521  VAL   A CG1   1 
ATOM   3853  C  CG2   . VAL   A 1  523  ? -41.791 38.243  94.797  1.00 30.29 ? 521  VAL   A CG2   1 
ATOM   3854  N  N     . ARG   A 1  524  ? -44.091 34.980  97.115  1.00 32.64 ? 522  ARG   A N     1 
ATOM   3855  C  CA    . ARG   A 1  524  ? -44.969 34.451  98.154  1.00 35.33 ? 522  ARG   A CA    1 
ATOM   3856  C  C     . ARG   A 1  524  ? -44.230 33.508  99.093  1.00 39.24 ? 522  ARG   A C     1 
ATOM   3857  O  O     . ARG   A 1  524  ? -44.537 33.460  100.291 1.00 41.43 ? 522  ARG   A O     1 
ATOM   3858  C  CB    . ARG   A 1  524  ? -46.169 33.742  97.525  1.00 40.21 ? 522  ARG   A CB    1 
ATOM   3859  C  CG    . ARG   A 1  524  ? -46.536 32.435  98.219  1.00 45.71 ? 522  ARG   A CG    1 
ATOM   3860  C  CD    . ARG   A 1  524  ? -48.013 32.124  98.154  1.00 44.42 ? 522  ARG   A CD    1 
ATOM   3861  N  NE    . ARG   A 1  524  ? -48.584 32.393  96.842  1.00 42.23 ? 522  ARG   A NE    1 
ATOM   3862  C  CZ    . ARG   A 1  524  ? -49.585 33.234  96.630  1.00 38.20 ? 522  ARG   A CZ    1 
ATOM   3863  N  NH1   . ARG   A 1  524  ? -50.149 33.900  97.626  1.00 39.77 ? 522  ARG   A NH1   1 
ATOM   3864  N  NH2   . ARG   A 1  524  ? -50.038 33.406  95.391  1.00 41.51 ? 522  ARG   A NH2   1 
ATOM   3865  N  N     . ALA   A 1  525  ? -43.252 32.768  98.578  1.00 38.71 ? 523  ALA   A N     1 
ATOM   3866  C  CA    . ALA   A 1  525  ? -42.525 31.775  99.354  1.00 38.90 ? 523  ALA   A CA    1 
ATOM   3867  C  C     . ALA   A 1  525  ? -41.317 32.348  100.083 1.00 38.47 ? 523  ALA   A C     1 
ATOM   3868  O  O     . ALA   A 1  525  ? -40.661 31.614  100.829 1.00 45.39 ? 523  ALA   A O     1 
ATOM   3869  C  CB    . ALA   A 1  525  ? -42.082 30.624  98.448  1.00 39.98 ? 523  ALA   A CB    1 
ATOM   3870  N  N     . MET   A 1  526  ? -41.004 33.626  99.889  1.00 38.72 ? 524  MET   A N     1 
ATOM   3871  C  CA    A MET   A 1  526  ? -39.855 34.226  100.548 0.49 39.22 ? 524  MET   A CA    1 
ATOM   3872  C  CA    B MET   A 1  526  ? -39.850 34.210  100.549 0.51 39.22 ? 524  MET   A CA    1 
ATOM   3873  C  C     . MET   A 1  526  ? -40.069 34.258  102.061 1.00 42.53 ? 524  MET   A C     1 
ATOM   3874  O  O     . MET   A 1  526  ? -41.202 34.386  102.532 1.00 41.55 ? 524  MET   A O     1 
ATOM   3875  C  CB    A MET   A 1  526  ? -39.649 35.651  100.043 0.49 42.70 ? 524  MET   A CB    1 
ATOM   3876  C  CB    B MET   A 1  526  ? -39.584 35.613  100.007 0.51 42.69 ? 524  MET   A CB    1 
ATOM   3877  C  CG    A MET   A 1  526  ? -39.206 35.736  98.595  0.49 41.62 ? 524  MET   A CG    1 
ATOM   3878  C  CG    B MET   A 1  526  ? -38.463 35.666  98.976  0.51 41.47 ? 524  MET   A CG    1 
ATOM   3879  S  SD    A MET   A 1  526  ? -37.587 34.989  98.340  0.49 45.10 ? 524  MET   A SD    1 
ATOM   3880  S  SD    B MET   A 1  526  ? -38.509 37.129  97.920  0.51 42.65 ? 524  MET   A SD    1 
ATOM   3881  C  CE    A MET   A 1  526  ? -36.589 35.969  99.462  0.49 41.40 ? 524  MET   A CE    1 
ATOM   3882  C  CE    B MET   A 1  526  ? -36.861 37.095  97.216  0.51 38.40 ? 524  MET   A CE    1 
ATOM   3883  N  N     . PRO   A 1  527  ? -38.991 34.142  102.847 1.00 45.90 ? 525  PRO   A N     1 
ATOM   3884  C  CA    . PRO   A 1  527  ? -39.157 34.166  104.313 1.00 48.21 ? 525  PRO   A CA    1 
ATOM   3885  C  C     . PRO   A 1  527  ? -39.811 35.437  104.820 1.00 46.10 ? 525  PRO   A C     1 
ATOM   3886  O  O     . PRO   A 1  527  ? -40.710 35.381  105.670 1.00 36.87 ? 525  PRO   A O     1 
ATOM   3887  C  CB    . PRO   A 1  527  ? -37.721 33.991  104.836 1.00 44.20 ? 525  PRO   A CB    1 
ATOM   3888  C  CG    . PRO   A 1  527  ? -36.843 34.373  103.693 1.00 46.19 ? 525  PRO   A CG    1 
ATOM   3889  C  CD    . PRO   A 1  527  ? -37.582 33.964  102.458 1.00 43.46 ? 525  PRO   A CD    1 
ATOM   3890  N  N     . VAL   A 1  528  ? -39.389 36.588  104.310 1.00 45.04 ? 526  VAL   A N     1 
ATOM   3891  C  CA    . VAL   A 1  528  ? -40.036 37.863  104.580 1.00 38.14 ? 526  VAL   A CA    1 
ATOM   3892  C  C     . VAL   A 1  528  ? -40.539 38.382  103.243 1.00 34.50 ? 526  VAL   A C     1 
ATOM   3893  O  O     . VAL   A 1  528  ? -39.738 38.719  102.362 1.00 40.51 ? 526  VAL   A O     1 
ATOM   3894  C  CB    . VAL   A 1  528  ? -39.077 38.864  105.233 1.00 39.14 ? 526  VAL   A CB    1 
ATOM   3895  C  CG1   . VAL   A 1  528  ? -39.770 40.200  105.439 1.00 42.70 ? 526  VAL   A CG1   1 
ATOM   3896  C  CG2   . VAL   A 1  528  ? -38.566 38.310  106.552 1.00 44.00 ? 526  VAL   A CG2   1 
ATOM   3897  N  N     . VAL   A 1  529  ? -41.860 38.437  103.079 1.00 34.40 ? 527  VAL   A N     1 
ATOM   3898  C  CA    . VAL   A 1  529  ? -42.425 38.924  101.829 1.00 33.56 ? 527  VAL   A CA    1 
ATOM   3899  C  C     . VAL   A 1  529  ? -42.141 40.413  101.689 1.00 38.24 ? 527  VAL   A C     1 
ATOM   3900  O  O     . VAL   A 1  529  ? -42.441 41.210  102.589 1.00 34.96 ? 527  VAL   A O     1 
ATOM   3901  C  CB    . VAL   A 1  529  ? -43.928 38.628  101.759 1.00 33.42 ? 527  VAL   A CB    1 
ATOM   3902  C  CG1   . VAL   A 1  529  ? -44.536 39.305  100.536 1.00 31.24 ? 527  VAL   A CG1   1 
ATOM   3903  C  CG2   . VAL   A 1  529  ? -44.168 37.126  101.711 1.00 40.09 ? 527  VAL   A CG2   1 
ATOM   3904  N  N     . GLY   A 1  530  ? -41.540 40.793  100.563 1.00 30.39 ? 528  GLY   A N     1 
ATOM   3905  C  CA    . GLY   A 1  530  ? -41.322 42.192  100.262 1.00 29.85 ? 528  GLY   A CA    1 
ATOM   3906  C  C     . GLY   A 1  530  ? -40.143 42.852  100.937 1.00 26.18 ? 528  GLY   A C     1 
ATOM   3907  O  O     . GLY   A 1  530  ? -40.108 44.080  101.011 1.00 30.93 ? 528  GLY   A O     1 
ATOM   3908  N  N     . ALA   A 1  531  ? -39.168 42.089  101.436 1.00 29.97 ? 529  ALA   A N     1 
ATOM   3909  C  CA    . ALA   A 1  531  ? -38.012 42.714  102.071 1.00 27.77 ? 529  ALA   A CA    1 
ATOM   3910  C  C     . ALA   A 1  531  ? -37.226 43.563  101.076 1.00 26.70 ? 529  ALA   A C     1 
ATOM   3911  O  O     . ALA   A 1  531  ? -37.111 43.217  99.896  1.00 29.30 ? 529  ALA   A O     1 
ATOM   3912  C  CB    . ALA   A 1  531  ? -37.092 41.652  102.681 1.00 30.13 ? 529  ALA   A CB    1 
ATOM   3913  N  N     . LYS   A 1  532  ? -36.697 44.687  101.564 1.00 26.87 ? 530  LYS   A N     1 
ATOM   3914  C  CA    . LYS   A 1  532  ? -35.826 45.551  100.775 1.00 26.92 ? 530  LYS   A CA    1 
ATOM   3915  C  C     . LYS   A 1  532  ? -34.632 44.758  100.255 1.00 28.13 ? 530  LYS   A C     1 
ATOM   3916  O  O     . LYS   A 1  532  ? -34.202 43.771  100.858 1.00 25.77 ? 530  LYS   A O     1 
ATOM   3917  C  CB    . LYS   A 1  532  ? -35.318 46.703  101.655 1.00 28.88 ? 530  LYS   A CB    1 
ATOM   3918  C  CG    . LYS   A 1  532  ? -34.311 47.650  100.988 1.00 32.18 ? 530  LYS   A CG    1 
ATOM   3919  C  CD    . LYS   A 1  532  ? -33.789 48.707  101.950 1.00 28.28 ? 530  LYS   A CD    1 
ATOM   3920  C  CE    . LYS   A 1  532  ? -32.978 48.084  103.084 1.00 30.30 ? 530  LYS   A CE    1 
ATOM   3921  N  NZ    . LYS   A 1  532  ? -31.700 47.477  102.599 1.00 27.91 ? 530  LYS   A NZ    1 
ATOM   3922  N  N     . HIS   A 1  533  ? -34.108 45.182  99.108  1.00 26.59 ? 531  HIS   A N     1 
ATOM   3923  C  CA    . HIS   A 1  533  ? -32.874 44.598  98.608  1.00 25.80 ? 531  HIS   A CA    1 
ATOM   3924  C  C     . HIS   A 1  533  ? -31.771 44.739  99.653  1.00 27.96 ? 531  HIS   A C     1 
ATOM   3925  O  O     . HIS   A 1  533  ? -31.599 45.798  100.262 1.00 27.51 ? 531  HIS   A O     1 
ATOM   3926  C  CB    . HIS   A 1  533  ? -32.455 45.287  97.313  1.00 25.19 ? 531  HIS   A CB    1 
ATOM   3927  C  CG    . HIS   A 1  533  ? -31.435 44.521  96.534  1.00 28.82 ? 531  HIS   A CG    1 
ATOM   3928  N  ND1   . HIS   A 1  533  ? -30.132 44.369  96.962  1.00 27.74 ? 531  HIS   A ND1   1 
ATOM   3929  C  CD2   . HIS   A 1  533  ? -31.528 43.852  95.361  1.00 33.44 ? 531  HIS   A CD2   1 
ATOM   3930  C  CE1   . HIS   A 1  533  ? -29.464 43.646  96.081  1.00 36.44 ? 531  HIS   A CE1   1 
ATOM   3931  N  NE2   . HIS   A 1  533  ? -30.287 43.318  95.101  1.00 39.12 ? 531  HIS   A NE2   1 
ATOM   3932  N  N     . ASP   A 1  534  ? -31.028 43.648  99.864  1.00 25.61 ? 532  ASP   A N     1 
ATOM   3933  C  CA    . ASP   A 1  534  ? -29.987 43.634  100.888 1.00 29.35 ? 532  ASP   A CA    1 
ATOM   3934  C  C     . ASP   A 1  534  ? -28.862 44.615  100.589 1.00 29.69 ? 532  ASP   A C     1 
ATOM   3935  O  O     . ASP   A 1  534  ? -28.208 45.108  101.516 1.00 35.73 ? 532  ASP   A O     1 
ATOM   3936  C  CB    . ASP   A 1  534  ? -29.411 42.224  100.997 1.00 32.70 ? 532  ASP   A CB    1 
ATOM   3937  C  CG    . ASP   A 1  534  ? -30.457 41.200  101.379 1.00 49.33 ? 532  ASP   A CG    1 
ATOM   3938  O  OD1   . ASP   A 1  534  ? -31.281 41.495  102.270 1.00 53.82 ? 532  ASP   A OD1   1 
ATOM   3939  O  OD2   . ASP   A 1  534  ? -30.461 40.100  100.784 1.00 65.36 ? 532  ASP   A OD2   1 
ATOM   3940  N  N     . ARG   A 1  535  ? -28.604 44.898  99.314  1.00 25.77 ? 533  ARG   A N     1 
ATOM   3941  C  CA    . ARG   A 1  535  ? -27.449 45.685  98.906  1.00 26.98 ? 533  ARG   A CA    1 
ATOM   3942  C  C     . ARG   A 1  535  ? -27.783 47.141  98.599  1.00 25.44 ? 533  ARG   A C     1 
ATOM   3943  O  O     . ARG   A 1  535  ? -26.921 47.871  98.096  1.00 27.71 ? 533  ARG   A O     1 
ATOM   3944  C  CB    . ARG   A 1  535  ? -26.754 45.036  97.706  1.00 31.62 ? 533  ARG   A CB    1 
ATOM   3945  N  N     . ILE   A 1  536  ? -28.997 47.587  98.897  1.00 25.68 ? 534  ILE   A N     1 
ATOM   3946  C  CA    . ILE   A 1  536  ? -29.382 48.978  98.700  1.00 26.69 ? 534  ILE   A CA    1 
ATOM   3947  C  C     . ILE   A 1  536  ? -29.695 49.574  100.062 1.00 26.29 ? 534  ILE   A C     1 
ATOM   3948  O  O     . ILE   A 1  536  ? -30.591 49.094  100.765 1.00 27.37 ? 534  ILE   A O     1 
ATOM   3949  C  CB    . ILE   A 1  536  ? -30.580 49.100  97.754  1.00 24.55 ? 534  ILE   A CB    1 
ATOM   3950  C  CG1   . ILE   A 1  536  ? -30.202 48.526  96.393  1.00 28.70 ? 534  ILE   A CG1   1 
ATOM   3951  C  CG2   . ILE   A 1  536  ? -31.034 50.548  97.657  1.00 26.11 ? 534  ILE   A CG2   1 
ATOM   3952  C  CD1   . ILE   A 1  536  ? -31.326 48.554  95.425  1.00 29.24 ? 534  ILE   A CD1   1 
ATOM   3953  N  N     . ALA   A 1  537  ? -28.968 50.621  100.424 1.00 21.64 ? 535  ALA   A N     1 
ATOM   3954  C  CA    . ALA   A 1  537  ? -29.141 51.240  101.726 1.00 21.51 ? 535  ALA   A CA    1 
ATOM   3955  C  C     . ALA   A 1  537  ? -30.326 52.192  101.689 1.00 25.83 ? 535  ALA   A C     1 
ATOM   3956  O  O     . ALA   A 1  537  ? -30.463 52.988  100.755 1.00 21.52 ? 535  ALA   A O     1 
ATOM   3957  C  CB    . ALA   A 1  537  ? -27.880 52.019  102.092 1.00 24.41 ? 535  ALA   A CB    1 
ATOM   3958  N  N     . LEU   A 1  538  ? -31.185 52.108  102.701 1.00 23.84 ? 536  LEU   A N     1 
ATOM   3959  C  CA    . LEU   A 1  538  ? -32.131 53.187  102.921 1.00 21.63 ? 536  LEU   A CA    1 
ATOM   3960  C  C     . LEU   A 1  538  ? -31.344 54.476  103.149 1.00 24.29 ? 536  LEU   A C     1 
ATOM   3961  O  O     . LEU   A 1  538  ? -30.201 54.438  103.617 1.00 22.18 ? 536  LEU   A O     1 
ATOM   3962  C  CB    . LEU   A 1  538  ? -33.009 52.891  104.139 1.00 22.61 ? 536  LEU   A CB    1 
ATOM   3963  C  CG    . LEU   A 1  538  ? -34.049 51.776  103.996 1.00 24.91 ? 536  LEU   A CG    1 
ATOM   3964  C  CD1   . LEU   A 1  538  ? -34.719 51.518  105.331 1.00 30.60 ? 536  LEU   A CD1   1 
ATOM   3965  C  CD2   . LEU   A 1  538  ? -35.084 52.136  102.938 1.00 25.17 ? 536  LEU   A CD2   1 
ATOM   3966  N  N     . PRO   A 1  539  ? -31.911 55.628  102.799 1.00 19.70 ? 537  PRO   A N     1 
ATOM   3967  C  CA    . PRO   A 1  539  ? -31.158 56.881  102.957 1.00 20.60 ? 537  PRO   A CA    1 
ATOM   3968  C  C     . PRO   A 1  539  ? -30.629 57.109  104.362 1.00 20.56 ? 537  PRO   A C     1 
ATOM   3969  O  O     . PRO   A 1  539  ? -29.495 57.573  104.520 1.00 22.37 ? 537  PRO   A O     1 
ATOM   3970  C  CB    . PRO   A 1  539  ? -32.156 57.945  102.493 1.00 20.69 ? 537  PRO   A CB    1 
ATOM   3971  C  CG    . PRO   A 1  539  ? -32.995 57.205  101.483 1.00 20.90 ? 537  PRO   A CG    1 
ATOM   3972  C  CD    . PRO   A 1  539  ? -33.151 55.821  102.025 1.00 21.91 ? 537  PRO   A CD    1 
ATOM   3973  N  N     . ALA   A 1  540  ? -31.405 56.764  105.387 1.00 20.90 ? 538  ALA   A N     1 
ATOM   3974  C  CA    . ALA   A 1  540  ? -30.935 56.921  106.759 1.00 23.29 ? 538  ALA   A CA    1 
ATOM   3975  C  C     . ALA   A 1  540  ? -29.710 56.067  107.056 1.00 26.52 ? 538  ALA   A C     1 
ATOM   3976  O  O     . ALA   A 1  540  ? -28.994 56.351  108.021 1.00 25.94 ? 538  ALA   A O     1 
ATOM   3977  C  CB    . ALA   A 1  540  ? -32.046 56.566  107.745 1.00 25.72 ? 538  ALA   A CB    1 
ATOM   3978  N  N     . GLU   A 1  541  ? -29.448 55.032  106.261 1.00 23.30 ? 539  GLU   A N     1 
ATOM   3979  C  CA    . GLU   A 1  541  ? -28.400 54.072  106.584 1.00 23.18 ? 539  GLU   A CA    1 
ATOM   3980  C  C     . GLU   A 1  541  ? -27.178 54.197  105.680 1.00 25.21 ? 539  GLU   A C     1 
ATOM   3981  O  O     . GLU   A 1  541  ? -26.343 53.288  105.648 1.00 23.44 ? 539  GLU   A O     1 
ATOM   3982  C  CB    . GLU   A 1  541  ? -28.960 52.648  106.593 1.00 30.42 ? 539  GLU   A CB    1 
ATOM   3983  C  CG    . GLU   A 1  541  ? -30.111 52.480  107.574 1.00 33.77 ? 539  GLU   A CG    1 
ATOM   3984  C  CD    . GLU   A 1  541  ? -30.650 51.067  107.618 1.00 41.32 ? 539  GLU   A CD    1 
ATOM   3985  O  OE1   . GLU   A 1  541  ? -29.838 50.119  107.638 1.00 53.26 ? 539  GLU   A OE1   1 
ATOM   3986  O  OE2   . GLU   A 1  541  ? -31.888 50.905  107.627 1.00 52.66 ? 539  GLU   A OE2   1 
ATOM   3987  N  N     . LEU   A 1  542  ? -27.044 55.321  104.965 1.00 21.75 ? 540  LEU   A N     1 
ATOM   3988  C  CA    . LEU   A 1  542  ? -25.925 55.494  104.040 1.00 23.74 ? 540  LEU   A CA    1 
ATOM   3989  C  C     . LEU   A 1  542  ? -24.575 55.302  104.714 1.00 23.86 ? 540  LEU   A C     1 
ATOM   3990  O  O     . LEU   A 1  542  ? -23.612 54.871  104.072 1.00 26.17 ? 540  LEU   A O     1 
ATOM   3991  C  CB    . LEU   A 1  542  ? -25.944 56.896  103.436 1.00 26.73 ? 540  LEU   A CB    1 
ATOM   3992  C  CG    . LEU   A 1  542  ? -26.878 57.199  102.274 1.00 30.38 ? 540  LEU   A CG    1 
ATOM   3993  C  CD1   . LEU   A 1  542  ? -26.456 58.523  101.656 1.00 26.36 ? 540  LEU   A CD1   1 
ATOM   3994  C  CD2   . LEU   A 1  542  ? -26.863 56.081  101.242 1.00 29.04 ? 540  LEU   A CD2   1 
ATOM   3995  N  N     . PHE   A 1  543  ? -24.466 55.645  105.991 1.00 22.46 ? 541  PHE   A N     1 
ATOM   3996  C  CA    . PHE   A 1  543  ? -23.181 55.564  106.665 1.00 25.08 ? 541  PHE   A CA    1 
ATOM   3997  C  C     . PHE   A 1  543  ? -23.082 54.355  107.576 1.00 24.10 ? 541  PHE   A C     1 
ATOM   3998  O  O     . PHE   A 1  543  ? -22.109 54.232  108.329 1.00 24.15 ? 541  PHE   A O     1 
ATOM   3999  C  CB    . PHE   A 1  543  ? -22.885 56.870  107.398 1.00 23.68 ? 541  PHE   A CB    1 
ATOM   4000  C  CG    . PHE   A 1  543  ? -23.106 58.078  106.546 1.00 23.30 ? 541  PHE   A CG    1 
ATOM   4001  C  CD1   . PHE   A 1  543  ? -22.406 58.233  105.356 1.00 25.41 ? 541  PHE   A CD1   1 
ATOM   4002  C  CD2   . PHE   A 1  543  ? -24.035 59.039  106.904 1.00 21.70 ? 541  PHE   A CD2   1 
ATOM   4003  C  CE1   . PHE   A 1  543  ? -22.613 59.329  104.555 1.00 24.30 ? 541  PHE   A CE1   1 
ATOM   4004  C  CE2   . PHE   A 1  543  ? -24.248 60.141  106.103 1.00 20.20 ? 541  PHE   A CE2   1 
ATOM   4005  C  CZ    . PHE   A 1  543  ? -23.538 60.292  104.925 1.00 23.47 ? 541  PHE   A CZ    1 
ATOM   4006  N  N     . GLY   A 1  544  ? -24.060 53.458  107.515 1.00 24.26 ? 542  GLY   A N     1 
ATOM   4007  C  CA    . GLY   A 1  544  ? -23.972 52.221  108.269 1.00 27.45 ? 542  GLY   A CA    1 
ATOM   4008  C  C     . GLY   A 1  544  ? -23.837 52.480  109.753 1.00 29.19 ? 542  GLY   A C     1 
ATOM   4009  O  O     . GLY   A 1  544  ? -24.508 53.344  110.326 1.00 27.08 ? 542  GLY   A O     1 
ATOM   4010  N  N     . ASP   A 1  545  ? -22.927 51.740  110.384 1.00 28.67 ? 543  ASP   A N     1 
ATOM   4011  C  CA    . ASP   A 1  545  ? -22.765 51.819  111.831 1.00 31.20 ? 543  ASP   A CA    1 
ATOM   4012  C  C     . ASP   A 1  545  ? -22.102 53.110  112.296 1.00 30.65 ? 543  ASP   A C     1 
ATOM   4013  O  O     . ASP   A 1  545  ? -22.116 53.387  113.503 1.00 34.14 ? 543  ASP   A O     1 
ATOM   4014  C  CB    . ASP   A 1  545  ? -21.949 50.623  112.331 1.00 35.14 ? 543  ASP   A CB    1 
ATOM   4015  C  CG    . ASP   A 1  545  ? -22.664 49.301  112.126 1.00 49.41 ? 543  ASP   A CG    1 
ATOM   4016  O  OD1   . ASP   A 1  545  ? -23.870 49.318  111.799 1.00 49.29 ? 543  ASP   A OD1   1 
ATOM   4017  O  OD2   . ASP   A 1  545  ? -22.018 48.243  112.294 1.00 60.49 ? 543  ASP   A OD2   1 
ATOM   4018  N  N     . ALA   A 1  546  ? -21.527 53.899  111.388 1.00 25.25 ? 544  ALA   A N     1 
ATOM   4019  C  CA    . ALA   A 1  546  ? -20.782 55.087  111.802 1.00 28.30 ? 544  ALA   A CA    1 
ATOM   4020  C  C     . ALA   A 1  546  ? -21.702 56.134  112.413 1.00 30.51 ? 544  ALA   A C     1 
ATOM   4021  O  O     . ALA   A 1  546  ? -21.389 56.718  113.456 1.00 29.41 ? 544  ALA   A O     1 
ATOM   4022  C  CB    . ALA   A 1  546  ? -20.012 55.669  110.620 1.00 27.48 ? 544  ALA   A CB    1 
ATOM   4023  N  N     . ARG   A 1  547  ? -22.844 56.386  111.779 1.00 26.12 ? 545  ARG   A N     1 
ATOM   4024  C  CA    . ARG   A 1  547  ? -23.795 57.361  112.288 1.00 27.29 ? 545  ARG   A CA    1 
ATOM   4025  C  C     . ARG   A 1  547  ? -25.041 57.287  111.430 1.00 23.51 ? 545  ARG   A C     1 
ATOM   4026  O  O     . ARG   A 1  547  ? -25.043 56.699  110.343 1.00 23.36 ? 545  ARG   A O     1 
ATOM   4027  C  CB    . ARG   A 1  547  ? -23.256 58.788  112.264 1.00 25.94 ? 545  ARG   A CB    1 
ATOM   4028  C  CG    . ARG   A 1  547  ? -22.902 59.258  110.898 1.00 28.41 ? 545  ARG   A CG    1 
ATOM   4029  C  CD    . ARG   A 1  547  ? -22.279 60.627  110.932 1.00 28.03 ? 545  ARG   A CD    1 
ATOM   4030  N  NE    . ARG   A 1  547  ? -21.455 60.810  109.749 1.00 23.97 ? 545  ARG   A NE    1 
ATOM   4031  C  CZ    . ARG   A 1  547  ? -21.809 61.497  108.670 1.00 23.50 ? 545  ARG   A CZ    1 
ATOM   4032  N  NH1   . ARG   A 1  547  ? -22.957 62.154  108.610 1.00 23.74 ? 545  ARG   A NH1   1 
ATOM   4033  N  NH2   . ARG   A 1  547  ? -20.982 61.535  107.632 1.00 24.61 ? 545  ARG   A NH2   1 
ATOM   4034  N  N     . THR   A 1  548  ? -26.091 57.921  111.930 1.00 22.38 ? 546  THR   A N     1 
ATOM   4035  C  CA    . THR   A 1  548  ? -27.372 57.975  111.251 1.00 21.21 ? 546  THR   A CA    1 
ATOM   4036  C  C     . THR   A 1  548  ? -27.379 59.196  110.345 1.00 20.43 ? 546  THR   A C     1 
ATOM   4037  O  O     . THR   A 1  548  ? -27.080 60.310  110.789 1.00 20.64 ? 546  THR   A O     1 
ATOM   4038  C  CB    . THR   A 1  548  ? -28.495 58.083  112.283 1.00 25.63 ? 546  THR   A CB    1 
ATOM   4039  O  OG1   . THR   A 1  548  ? -28.410 56.982  113.197 1.00 29.60 ? 546  THR   A OG1   1 
ATOM   4040  C  CG2   . THR   A 1  548  ? -29.848 58.073  111.598 1.00 26.15 ? 546  THR   A CG2   1 
ATOM   4041  N  N     . ASN   A 1  549  ? -27.702 58.982  109.073 1.00 19.29 ? 547  ASN   A N     1 
ATOM   4042  C  CA    . ASN   A 1  549  ? -27.825 60.090  108.142 1.00 18.95 ? 547  ASN   A CA    1 
ATOM   4043  C  C     . ASN   A 1  549  ? -28.965 60.998  108.584 1.00 20.70 ? 547  ASN   A C     1 
ATOM   4044  O  O     . ASN   A 1  549  ? -29.972 60.534  109.117 1.00 21.32 ? 547  ASN   A O     1 
ATOM   4045  C  CB    . ASN   A 1  549  ? -28.108 59.529  106.743 1.00 19.28 ? 547  ASN   A CB    1 
ATOM   4046  C  CG    . ASN   A 1  549  ? -27.937 60.562  105.652 1.00 19.04 ? 547  ASN   A CG    1 
ATOM   4047  O  OD1   . ASN   A 1  549  ? -27.383 61.637  105.877 1.00 19.57 ? 547  ASN   A OD1   1 
ATOM   4048  N  ND2   . ASN   A 1  549  ? -28.380 60.227  104.446 1.00 20.99 ? 547  ASN   A ND2   1 
ATOM   4049  N  N     . SER   A 1  550  ? -28.794 62.300  108.391 1.00 20.15 ? 548  SER   A N     1 
ATOM   4050  C  CA    . SER   A 1  550  ? -29.905 63.216  108.607 1.00 19.85 ? 548  SER   A CA    1 
ATOM   4051  C  C     . SER   A 1  550  ? -31.005 62.933  107.596 1.00 20.32 ? 548  SER   A C     1 
ATOM   4052  O  O     . SER   A 1  550  ? -30.763 62.430  106.495 1.00 21.07 ? 548  SER   A O     1 
ATOM   4053  C  CB    . SER   A 1  550  ? -29.440 64.656  108.442 1.00 18.06 ? 548  SER   A CB    1 
ATOM   4054  O  OG    . SER   A 1  550  ? -28.960 64.872  107.125 1.00 20.17 ? 548  SER   A OG    1 
ATOM   4055  N  N     . ALA   A 1  551  ? -32.229 63.260  107.986 1.00 21.28 ? 549  ALA   A N     1 
ATOM   4056  C  CA    . ALA   A 1  551  ? -33.394 63.049  107.145 1.00 21.80 ? 549  ALA   A CA    1 
ATOM   4057  C  C     . ALA   A 1  551  ? -33.875 64.377  106.584 1.00 22.00 ? 549  ALA   A C     1 
ATOM   4058  O  O     . ALA   A 1  551  ? -33.883 65.399  107.281 1.00 21.01 ? 549  ALA   A O     1 
ATOM   4059  C  CB    . ALA   A 1  551  ? -34.525 62.382  107.928 1.00 23.39 ? 549  ALA   A CB    1 
ATOM   4060  N  N     . GLY   A 1  552  ? -34.281 64.353  105.321 1.00 20.46 ? 550  GLY   A N     1 
ATOM   4061  C  CA    . GLY   A 1  552  ? -34.879 65.494  104.686 1.00 21.75 ? 550  GLY   A CA    1 
ATOM   4062  C  C     . GLY   A 1  552  ? -36.387 65.404  104.680 1.00 21.18 ? 550  GLY   A C     1 
ATOM   4063  O  O     . GLY   A 1  552  ? -37.003 64.678  105.470 1.00 22.99 ? 550  GLY   A O     1 
ATOM   4064  N  N     . LEU   A 1  553  ? -36.992 66.169  103.777 1.00 22.03 ? 551  LEU   A N     1 
ATOM   4065  C  CA    . LEU   A 1  553  ? -38.436 66.229  103.639 1.00 21.54 ? 551  LEU   A CA    1 
ATOM   4066  C  C     . LEU   A 1  553  ? -38.737 66.229  102.155 1.00 21.96 ? 551  LEU   A C     1 
ATOM   4067  O  O     . LEU   A 1  553  ? -38.005 66.838  101.374 1.00 22.82 ? 551  LEU   A O     1 
ATOM   4068  C  CB    . LEU   A 1  553  ? -38.974 67.519  104.242 1.00 24.03 ? 551  LEU   A CB    1 
ATOM   4069  C  CG    . LEU   A 1  553  ? -38.896 67.588  105.760 1.00 22.99 ? 551  LEU   A CG    1 
ATOM   4070  C  CD1   . LEU   A 1  553  ? -39.338 68.958  106.239 1.00 30.61 ? 551  LEU   A CD1   1 
ATOM   4071  C  CD2   . LEU   A 1  553  ? -39.748 66.489  106.399 1.00 24.70 ? 551  LEU   A CD2   1 
ATOM   4072  N  N     . ASP   A 1  554  ? -39.813 65.552  101.772 1.00 20.81 ? 552  ASP   A N     1 
ATOM   4073  C  CA    . ASP   A 1  554  ? -40.162 65.411  100.360 1.00 20.89 ? 552  ASP   A CA    1 
ATOM   4074  C  C     . ASP   A 1  554  ? -41.123 66.534  100.006 1.00 20.17 ? 552  ASP   A C     1 
ATOM   4075  O  O     . ASP   A 1  554  ? -42.315 66.466  100.314 1.00 19.87 ? 552  ASP   A O     1 
ATOM   4076  C  CB    . ASP   A 1  554  ? -40.810 64.057  100.110 1.00 20.64 ? 552  ASP   A CB    1 
ATOM   4077  C  CG    . ASP   A 1  554  ? -41.115 63.826  98.647  1.00 20.94 ? 552  ASP   A CG    1 
ATOM   4078  O  OD1   . ASP   A 1  554  ? -40.847 64.733  97.826  1.00 21.80 ? 552  ASP   A OD1   1 
ATOM   4079  O  OD2   . ASP   A 1  554  ? -41.613 62.733  98.321  1.00 23.02 ? 552  ASP   A OD2   1 
ATOM   4080  N  N     . LEU   A 1  555  ? -40.615 67.556  99.322  1.00 19.00 ? 553  LEU   A N     1 
ATOM   4081  C  CA    . LEU   A 1  555  ? -41.458 68.686  98.960  1.00 19.88 ? 553  LEU   A CA    1 
ATOM   4082  C  C     . LEU   A 1  555  ? -42.333 68.397  97.751  1.00 19.26 ? 553  LEU   A C     1 
ATOM   4083  O  O     . LEU   A 1  555  ? -42.994 69.312  97.257  1.00 22.59 ? 553  LEU   A O     1 
ATOM   4084  C  CB    . LEU   A 1  555  ? -40.613 69.938  98.745  1.00 20.58 ? 553  LEU   A CB    1 
ATOM   4085  C  CG    . LEU   A 1  555  ? -39.806 70.349  99.982  1.00 21.42 ? 553  LEU   A CG    1 
ATOM   4086  C  CD1   . LEU   A 1  555  ? -39.047 71.635  99.706  1.00 26.30 ? 553  LEU   A CD1   1 
ATOM   4087  C  CD2   . LEU   A 1  555  ? -40.732 70.500  101.179 1.00 25.19 ? 553  LEU   A CD2   1 
ATOM   4088  N  N     . SER   A 1  556  ? -42.354 67.160  97.267  1.00 18.86 ? 554  SER   A N     1 
ATOM   4089  C  CA    . SER   A 1  556  ? -43.355 66.759  96.289  1.00 19.38 ? 554  SER   A CA    1 
ATOM   4090  C  C     . SER   A 1  556  ? -44.494 65.974  96.917  1.00 20.66 ? 554  SER   A C     1 
ATOM   4091  O  O     . SER   A 1  556  ? -45.433 65.598  96.214  1.00 20.90 ? 554  SER   A O     1 
ATOM   4092  C  CB    . SER   A 1  556  ? -42.714 65.928  95.174  1.00 21.73 ? 554  SER   A CB    1 
ATOM   4093  O  OG    . SER   A 1  556  ? -42.421 64.618  95.637  1.00 23.34 ? 554  SER   A OG    1 
ATOM   4094  N  N     . ASN   A 1  557  ? -44.440 65.724  98.218  1.00 18.33 ? 555  ASN   A N     1 
ATOM   4095  C  CA    . ASN   A 1  557  ? -45.448 64.940  98.912  1.00 18.44 ? 555  ASN   A CA    1 
ATOM   4096  C  C     . ASN   A 1  557  ? -46.480 65.898  99.498  1.00 21.00 ? 555  ASN   A C     1 
ATOM   4097  O  O     . ASN   A 1  557  ? -46.137 66.744  100.330 1.00 20.02 ? 555  ASN   A O     1 
ATOM   4098  C  CB    . ASN   A 1  557  ? -44.752 64.132  100.010 1.00 21.00 ? 555  ASN   A CB    1 
ATOM   4099  C  CG    . ASN   A 1  557  ? -45.706 63.250  100.790 1.00 19.90 ? 555  ASN   A CG    1 
ATOM   4100  O  OD1   . ASN   A 1  557  ? -46.725 63.711  101.294 1.00 22.81 ? 555  ASN   A OD1   1 
ATOM   4101  N  ND2   . ASN   A 1  557  ? -45.372 61.967  100.890 1.00 22.02 ? 555  ASN   A ND2   1 
ATOM   4102  N  N     . GLU   A 1  558  ? -47.747 65.760  99.074  1.00 20.07 ? 556  GLU   A N     1 
ATOM   4103  C  CA    . GLU   A 1  558  ? -48.774 66.699  99.530  1.00 22.28 ? 556  GLU   A CA    1 
ATOM   4104  C  C     . GLU   A 1  558  ? -48.989 66.633  101.034 1.00 20.81 ? 556  GLU   A C     1 
ATOM   4105  O  O     . GLU   A 1  558  ? -49.317 67.652  101.657 1.00 22.25 ? 556  GLU   A O     1 
ATOM   4106  C  CB    . GLU   A 1  558  ? -50.110 66.472  98.823  1.00 24.66 ? 556  GLU   A CB    1 
ATOM   4107  C  CG    . GLU   A 1  558  ? -50.113 66.780  97.358  1.00 23.07 ? 556  GLU   A CG    1 
ATOM   4108  C  CD    . GLU   A 1  558  ? -49.868 68.246  97.002  1.00 21.96 ? 556  GLU   A CD    1 
ATOM   4109  O  OE1   . GLU   A 1  558  ? -49.909 69.162  97.852  1.00 20.97 ? 556  GLU   A OE1   1 
ATOM   4110  O  OE2   . GLU   A 1  558  ? -49.644 68.478  95.802  1.00 21.94 ? 556  GLU   A OE2   1 
ATOM   4111  N  N     . GLU   A 1  559  ? -48.881 65.442  101.630 1.00 19.65 ? 557  GLU   A N     1 
ATOM   4112  C  CA    . GLU   A 1  559  ? -48.994 65.365  103.084 1.00 20.50 ? 557  GLU   A CA    1 
ATOM   4113  C  C     . GLU   A 1  559  ? -47.884 66.167  103.736 1.00 22.00 ? 557  GLU   A C     1 
ATOM   4114  O  O     . GLU   A 1  559  ? -48.124 66.940  104.666 1.00 23.68 ? 557  GLU   A O     1 
ATOM   4115  C  CB    . GLU   A 1  559  ? -48.929 63.916  103.566 1.00 26.38 ? 557  GLU   A CB    1 
ATOM   4116  C  CG    . GLU   A 1  559  ? -50.059 63.010  103.128 1.00 28.64 ? 557  GLU   A CG    1 
ATOM   4117  C  CD    . GLU   A 1  559  ? -49.846 61.575  103.595 1.00 37.42 ? 557  GLU   A CD    1 
ATOM   4118  O  OE1   . GLU   A 1  559  ? -48.881 61.333  104.353 1.00 44.57 ? 557  GLU   A OE1   1 
ATOM   4119  O  OE2   . GLU   A 1  559  ? -50.630 60.687  103.198 1.00 39.30 ? 557  GLU   A OE2   1 
ATOM   4120  N  N     . THR   A 1  560  ? -46.658 66.021  103.229 1.00 19.89 ? 558  THR   A N     1 
ATOM   4121  C  CA    . THR   A 1  560  ? -45.548 66.794  103.769 1.00 22.40 ? 558  THR   A CA    1 
ATOM   4122  C  C     . THR   A 1  560  ? -45.764 68.282  103.558 1.00 20.97 ? 558  THR   A C     1 
ATOM   4123  O  O     . THR   A 1  560  ? -45.534 69.081  104.465 1.00 22.35 ? 558  THR   A O     1 
ATOM   4124  C  CB    . THR   A 1  560  ? -44.252 66.347  103.101 1.00 21.24 ? 558  THR   A CB    1 
ATOM   4125  O  OG1   . THR   A 1  560  ? -44.099 64.942  103.296 1.00 23.44 ? 558  THR   A OG1   1 
ATOM   4126  C  CG2   . THR   A 1  560  ? -43.052 67.087  103.683 1.00 22.94 ? 558  THR   A CG2   1 
ATOM   4127  N  N     . LEU   A 1  561  ? -46.212 68.681  102.365 1.00 19.26 ? 559  LEU   A N     1 
ATOM   4128  C  CA    . LEU   A 1  561  ? -46.433 70.101  102.131 1.00 19.10 ? 559  LEU   A CA    1 
ATOM   4129  C  C     . LEU   A 1  561  ? -47.516 70.643  103.051 1.00 21.73 ? 559  LEU   A C     1 
ATOM   4130  O  O     . LEU   A 1  561  ? -47.411 71.772  103.544 1.00 22.05 ? 559  LEU   A O     1 
ATOM   4131  C  CB    . LEU   A 1  561  ? -46.795 70.344  100.669 1.00 18.28 ? 559  LEU   A CB    1 
ATOM   4132  C  CG    . LEU   A 1  561  ? -45.643 70.080  99.701  1.00 18.22 ? 559  LEU   A CG    1 
ATOM   4133  C  CD1   . LEU   A 1  561  ? -46.158 70.256  98.286  1.00 18.56 ? 559  LEU   A CD1   1 
ATOM   4134  C  CD2   . LEU   A 1  561  ? -44.475 71.027  99.968  1.00 20.40 ? 559  LEU   A CD2   1 
ATOM   4135  N  N     . ALA   A 1  562  ? -48.560 69.851  103.305 1.00 21.11 ? 560  ALA   A N     1 
ATOM   4136  C  CA    . ALA   A 1  562  ? -49.635 70.342  104.159 1.00 20.59 ? 560  ALA   A CA    1 
ATOM   4137  C  C     . ALA   A 1  562  ? -49.169 70.462  105.599 1.00 21.09 ? 560  ALA   A C     1 
ATOM   4138  O  O     . ALA   A 1  562  ? -49.447 71.465  106.268 1.00 22.85 ? 560  ALA   A O     1 
ATOM   4139  C  CB    . ALA   A 1  562  ? -50.862 69.434  104.058 1.00 24.42 ? 560  ALA   A CB    1 
ATOM   4140  N  N     . SER   A 1  563  ? -48.450 69.453  106.092 1.00 21.97 ? 561  SER   A N     1 
ATOM   4141  C  CA    A SER   A 1  563  ? -47.932 69.518  107.453 0.43 24.00 ? 561  SER   A CA    1 
ATOM   4142  C  CA    B SER   A 1  563  ? -47.947 69.533  107.457 0.57 23.99 ? 561  SER   A CA    1 
ATOM   4143  C  C     . SER   A 1  563  ? -46.886 70.618  107.588 1.00 22.78 ? 561  SER   A C     1 
ATOM   4144  O  O     . SER   A 1  563  ? -46.868 71.354  108.582 1.00 26.22 ? 561  SER   A O     1 
ATOM   4145  C  CB    A SER   A 1  563  ? -47.349 68.161  107.843 0.43 24.44 ? 561  SER   A CB    1 
ATOM   4146  C  CB    B SER   A 1  563  ? -47.426 68.172  107.923 0.57 24.45 ? 561  SER   A CB    1 
ATOM   4147  O  OG    A SER   A 1  563  ? -46.793 68.207  109.140 0.43 25.04 ? 561  SER   A OG    1 
ATOM   4148  O  OG    B SER   A 1  563  ? -46.225 67.823  107.269 0.57 27.99 ? 561  SER   A OG    1 
ATOM   4149  N  N     . LEU   A 1  564  ? -46.015 70.750  106.587 1.00 23.60 ? 562  LEU   A N     1 
ATOM   4150  C  CA    . LEU   A 1  564  ? -44.990 71.787  106.633 1.00 22.58 ? 562  LEU   A CA    1 
ATOM   4151  C  C     . LEU   A 1  564  ? -45.610 73.177  106.597 1.00 24.12 ? 562  LEU   A C     1 
ATOM   4152  O  O     . LEU   A 1  564  ? -45.167 74.079  107.317 1.00 24.52 ? 562  LEU   A O     1 
ATOM   4153  C  CB    . LEU   A 1  564  ? -44.022 71.605  105.468 1.00 22.51 ? 562  LEU   A CB    1 
ATOM   4154  C  CG    . LEU   A 1  564  ? -42.652 72.255  105.579 1.00 31.18 ? 562  LEU   A CG    1 
ATOM   4155  C  CD1   . LEU   A 1  564  ? -41.959 71.707  106.803 1.00 28.97 ? 562  LEU   A CD1   1 
ATOM   4156  C  CD2   . LEU   A 1  564  ? -41.843 71.966  104.331 1.00 27.44 ? 562  LEU   A CD2   1 
ATOM   4157  N  N     . THR   A 1  565  ? -46.651 73.368  105.779 1.00 23.34 ? 563  THR   A N     1 
ATOM   4158  C  CA    . THR   A 1  565  ? -47.332 74.657  105.752 1.00 23.67 ? 563  THR   A CA    1 
ATOM   4159  C  C     . THR   A 1  565  ? -47.761 75.073  107.153 1.00 21.93 ? 563  THR   A C     1 
ATOM   4160  O  O     . THR   A 1  565  ? -47.521 76.207  107.582 1.00 25.14 ? 563  THR   A O     1 
ATOM   4161  C  CB    . THR   A 1  565  ? -48.551 74.599  104.834 1.00 22.93 ? 563  THR   A CB    1 
ATOM   4162  O  OG1   . THR   A 1  565  ? -48.127 74.387  103.483 1.00 23.04 ? 563  THR   A OG1   1 
ATOM   4163  C  CG2   . THR   A 1  565  ? -49.324 75.910  104.902 1.00 27.37 ? 563  THR   A CG2   1 
ATOM   4164  N  N     . GLU   A 1  566  ? -48.383 74.154  107.892 1.00 23.15 ? 564  GLU   A N     1 
ATOM   4165  C  CA    . GLU   A 1  566  ? -48.849 74.511  109.226 1.00 25.17 ? 564  GLU   A CA    1 
ATOM   4166  C  C     . GLU   A 1  566  ? -47.681 74.772  110.164 1.00 25.20 ? 564  GLU   A C     1 
ATOM   4167  O  O     . GLU   A 1  566  ? -47.698 75.742  110.931 1.00 25.50 ? 564  GLU   A O     1 
ATOM   4168  C  CB    . GLU   A 1  566  ? -49.782 73.431  109.771 1.00 28.41 ? 564  GLU   A CB    1 
ATOM   4169  C  CG    . GLU   A 1  566  ? -51.064 73.284  108.957 1.00 37.62 ? 564  GLU   A CG    1 
ATOM   4170  C  CD    . GLU   A 1  566  ? -51.766 74.617  108.709 1.00 40.93 ? 564  GLU   A CD    1 
ATOM   4171  O  OE1   . GLU   A 1  566  ? -51.922 75.406  109.668 1.00 43.98 ? 564  GLU   A OE1   1 
ATOM   4172  O  OE2   . GLU   A 1  566  ? -52.156 74.878  107.546 1.00 38.28 ? 564  GLU   A OE2   1 
ATOM   4173  N  N     . ALA   A 1  567  ? -46.647 73.933  110.098 1.00 24.49 ? 565  ALA   A N     1 
ATOM   4174  C  CA    . ALA   A 1  567  ? -45.490 74.128  110.965 1.00 24.98 ? 565  ALA   A CA    1 
ATOM   4175  C  C     . ALA   A 1  567  ? -44.775 75.433  110.641 1.00 22.57 ? 565  ALA   A C     1 
ATOM   4176  O  O     . ALA   A 1  567  ? -44.293 76.128  111.545 1.00 25.44 ? 565  ALA   A O     1 
ATOM   4177  C  CB    . ALA   A 1  567  ? -44.542 72.939  110.832 1.00 27.95 ? 565  ALA   A CB    1 
ATOM   4178  N  N     . LEU   A 1  568  ? -44.691 75.781  109.356 1.00 22.46 ? 566  LEU   A N     1 
ATOM   4179  C  CA    . LEU   A 1  568  ? -44.036 77.027  108.974 1.00 20.94 ? 566  LEU   A CA    1 
ATOM   4180  C  C     . LEU   A 1  568  ? -44.833 78.231  109.442 1.00 22.96 ? 566  LEU   A C     1 
ATOM   4181  O  O     . LEU   A 1  568  ? -44.264 79.181  109.991 1.00 25.20 ? 566  LEU   A O     1 
ATOM   4182  C  CB    . LEU   A 1  568  ? -43.839 77.078  107.458 1.00 22.05 ? 566  LEU   A CB    1 
ATOM   4183  C  CG    . LEU   A 1  568  ? -42.897 76.040  106.858 1.00 21.64 ? 566  LEU   A CG    1 
ATOM   4184  C  CD1   . LEU   A 1  568  ? -42.943 76.138  105.342 1.00 21.66 ? 566  LEU   A CD1   1 
ATOM   4185  C  CD2   . LEU   A 1  568  ? -41.479 76.240  107.355 1.00 22.54 ? 566  LEU   A CD2   1 
ATOM   4186  N  N     . ARG   A 1  569  ? -46.150 78.208  109.237 1.00 24.01 ? 567  ARG   A N     1 
ATOM   4187  C  CA    . ARG   A 1  569  ? -47.000 79.272  109.759 1.00 23.84 ? 567  ARG   A CA    1 
ATOM   4188  C  C     . ARG   A 1  569  ? -46.828 79.415  111.265 1.00 26.31 ? 567  ARG   A C     1 
ATOM   4189  O  O     . ARG   A 1  569  ? -46.693 80.529  111.785 1.00 30.07 ? 567  ARG   A O     1 
ATOM   4190  C  CB    . ARG   A 1  569  ? -48.457 78.979  109.409 1.00 25.94 ? 567  ARG   A CB    1 
ATOM   4191  C  CG    . ARG   A 1  569  ? -48.771 79.138  107.932 1.00 27.19 ? 567  ARG   A CG    1 
ATOM   4192  C  CD    . ARG   A 1  569  ? -50.224 78.765  107.628 1.00 34.86 ? 567  ARG   A CD    1 
ATOM   4193  N  NE    . ARG   A 1  569  ? -50.514 78.841  106.200 1.00 37.90 ? 567  ARG   A NE    1 
ATOM   4194  C  CZ    . ARG   A 1  569  ? -51.648 78.431  105.648 1.00 44.19 ? 567  ARG   A CZ    1 
ATOM   4195  N  NH1   . ARG   A 1  569  ? -52.614 77.893  106.375 1.00 50.41 ? 567  ARG   A NH1   1 
ATOM   4196  N  NH2   . ARG   A 1  569  ? -51.817 78.566  104.335 1.00 47.35 ? 567  ARG   A NH2   1 
ATOM   4197  N  N     . GLU   A 1  570  ? -46.823 78.287  111.983 1.00 25.24 ? 568  GLU   A N     1 
ATOM   4198  C  CA    . GLU   A 1  570  ? -46.659 78.329  113.432 1.00 27.46 ? 568  GLU   A CA    1 
ATOM   4199  C  C     . GLU   A 1  570  ? -45.302 78.899  113.820 1.00 30.00 ? 568  GLU   A C     1 
ATOM   4200  O  O     . GLU   A 1  570  ? -45.180 79.594  114.835 1.00 32.17 ? 568  GLU   A O     1 
ATOM   4201  C  CB    . GLU   A 1  570  ? -46.862 76.932  114.019 1.00 29.29 ? 568  GLU   A CB    1 
ATOM   4202  C  CG    . GLU   A 1  570  ? -48.321 76.472  113.999 1.00 32.95 ? 568  GLU   A CG    1 
ATOM   4203  C  CD    . GLU   A 1  570  ? -48.476 74.976  114.216 1.00 43.59 ? 568  GLU   A CD    1 
ATOM   4204  O  OE1   . GLU   A 1  570  ? -47.455 74.258  114.175 1.00 53.30 ? 568  GLU   A OE1   1 
ATOM   4205  O  OE2   . GLU   A 1  570  ? -49.623 74.518  114.424 1.00 55.22 ? 568  GLU   A OE2   1 
ATOM   4206  N  N     . SER   A 1  571  ? -44.269 78.621  113.025 1.00 27.53 ? 569  SER   A N     1 
ATOM   4207  C  CA    . SER   A 1  571  ? -42.959 79.184  113.328 1.00 28.45 ? 569  SER   A CA    1 
ATOM   4208  C  C     . SER   A 1  571  ? -42.959 80.701  113.192 1.00 27.93 ? 569  SER   A C     1 
ATOM   4209  O  O     . SER   A 1  571  ? -42.237 81.385  113.924 1.00 28.72 ? 569  SER   A O     1 
ATOM   4210  C  CB    . SER   A 1  571  ? -41.899 78.568  112.416 1.00 25.54 ? 569  SER   A CB    1 
ATOM   4211  O  OG    . SER   A 1  571  ? -41.917 79.170  111.132 1.00 27.33 ? 569  SER   A OG    1 
ATOM   4212  N  N     . ALA   A 1  572  ? -43.763 81.245  112.279 1.00 29.21 ? 570  ALA   A N     1 
ATOM   4213  C  CA    . ALA   A 1  572  ? -43.815 82.690  112.093 1.00 29.01 ? 570  ALA   A CA    1 
ATOM   4214  C  C     . ALA   A 1  572  ? -44.592 83.396  113.193 1.00 32.94 ? 570  ALA   A C     1 
ATOM   4215  O  O     . ALA   A 1  572  ? -44.510 84.622  113.295 1.00 39.41 ? 570  ALA   A O     1 
ATOM   4216  C  CB    . ALA   A 1  572  ? -44.407 83.030  110.727 1.00 33.11 ? 570  ALA   A CB    1 
ATOM   4217  N  N     . ALA   A 1  573  ? -45.332 82.654  114.010 1.00 29.65 ? 571  ALA   A N     1 
ATOM   4218  C  CA    . ALA   A 1  573  ? -46.043 83.206  115.154 1.00 36.25 ? 571  ALA   A CA    1 
ATOM   4219  C  C     . ALA   A 1  573  ? -45.219 83.157  116.434 1.00 42.35 ? 571  ALA   A C     1 
ATOM   4220  O  O     . ALA   A 1  573  ? -45.690 83.620  117.478 1.00 41.86 ? 571  ALA   A O     1 
ATOM   4221  C  CB    . ALA   A 1  573  ? -47.370 82.465  115.359 1.00 34.67 ? 571  ALA   A CB    1 
ATOM   4222  N  N     . MET   A 1  574  ? -44.007 82.611  116.382 1.00 32.85 ? 572  MET   A N     1 
ATOM   4223  C  CA    . MET   A 1  574  ? -43.164 82.509  117.563 1.00 36.83 ? 572  MET   A CA    1 
ATOM   4224  C  C     . MET   A 1  574  ? -42.390 83.805  117.780 1.00 34.79 ? 572  MET   A C     1 
ATOM   4225  O  O     . MET   A 1  574  ? -42.085 84.540  116.836 1.00 34.11 ? 572  MET   A O     1 
ATOM   4226  C  CB    . MET   A 1  574  ? -42.206 81.324  117.434 1.00 37.25 ? 572  MET   A CB    1 
ATOM   4227  C  CG    . MET   A 1  574  ? -42.900 79.963  117.512 1.00 34.89 ? 572  MET   A CG    1 
ATOM   4228  S  SD    . MET   A 1  574  ? -41.827 78.582  117.085 1.00 38.16 ? 572  MET   A SD    1 
ATOM   4229  C  CE    . MET   A 1  574  ? -42.923 77.181  117.322 1.00 47.29 ? 572  MET   A CE    1 
ATOM   4230  N  N     . LYS   A 1  575  ? -42.098 84.092  119.050 1.00 37.87 ? 573  LYS   A N     1 
ATOM   4231  C  CA    . LYS   A 1  575  ? -41.392 85.314  119.439 1.00 39.09 ? 573  LYS   A CA    1 
ATOM   4232  C  C     . LYS   A 1  575  ? -39.903 85.000  119.547 1.00 35.95 ? 573  LYS   A C     1 
ATOM   4233  O  O     . LYS   A 1  575  ? -39.325 84.897  120.631 1.00 37.57 ? 573  LYS   A O     1 
ATOM   4234  C  CB    . LYS   A 1  575  ? -41.952 85.867  120.746 1.00 41.15 ? 573  LYS   A CB    1 
ATOM   4235  N  N     . TRP   A 1  576  ? -39.279 84.852  118.382 1.00 32.22 ? 574  TRP   A N     1 
ATOM   4236  C  CA    . TRP   A 1  576  ? -37.870 84.499  118.305 1.00 28.44 ? 574  TRP   A CA    1 
ATOM   4237  C  C     . TRP   A 1  576  ? -37.014 85.626  118.861 1.00 25.47 ? 574  TRP   A C     1 
ATOM   4238  O  O     . TRP   A 1  576  ? -37.176 86.790  118.482 1.00 28.94 ? 574  TRP   A O     1 
ATOM   4239  C  CB    . TRP   A 1  576  ? -37.487 84.265  116.847 1.00 26.93 ? 574  TRP   A CB    1 
ATOM   4240  C  CG    . TRP   A 1  576  ? -38.186 83.117  116.194 1.00 25.34 ? 574  TRP   A CG    1 
ATOM   4241  C  CD1   . TRP   A 1  576  ? -39.168 83.180  115.235 1.00 26.57 ? 574  TRP   A CD1   1 
ATOM   4242  C  CD2   . TRP   A 1  576  ? -37.965 81.728  116.449 1.00 26.32 ? 574  TRP   A CD2   1 
ATOM   4243  N  NE1   . TRP   A 1  576  ? -39.557 81.917  114.881 1.00 27.53 ? 574  TRP   A NE1   1 
ATOM   4244  C  CE2   . TRP   A 1  576  ? -38.834 81.005  115.606 1.00 26.56 ? 574  TRP   A CE2   1 
ATOM   4245  C  CE3   . TRP   A 1  576  ? -37.113 81.023  117.308 1.00 24.66 ? 574  TRP   A CE3   1 
ATOM   4246  C  CZ2   . TRP   A 1  576  ? -38.875 79.611  115.591 1.00 28.21 ? 574  TRP   A CZ2   1 
ATOM   4247  C  CZ3   . TRP   A 1  576  ? -37.148 79.640  117.290 1.00 25.34 ? 574  TRP   A CZ3   1 
ATOM   4248  C  CH2   . TRP   A 1  576  ? -38.027 78.947  116.438 1.00 29.36 ? 574  TRP   A CH2   1 
ATOM   4249  N  N     . THR   A 1  577  ? -36.099 85.283  119.761 1.00 26.68 ? 575  THR   A N     1 
ATOM   4250  C  CA    . THR   A 1  577  ? -35.145 86.252  120.273 1.00 24.84 ? 575  THR   A CA    1 
ATOM   4251  C  C     . THR   A 1  577  ? -33.759 85.632  120.300 1.00 30.24 ? 575  THR   A C     1 
ATOM   4252  O  O     . THR   A 1  577  ? -33.598 84.409  120.285 1.00 27.88 ? 575  THR   A O     1 
ATOM   4253  C  CB    . THR   A 1  577  ? -35.479 86.726  121.695 1.00 29.32 ? 575  THR   A CB    1 
ATOM   4254  O  OG1   . THR   A 1  577  ? -35.344 85.625  122.602 1.00 32.20 ? 575  THR   A OG1   1 
ATOM   4255  C  CG2   . THR   A 1  577  ? -36.887 87.277  121.758 1.00 32.63 ? 575  THR   A CG2   1 
ATOM   4256  N  N     . ALA   A 1  578  ? -32.759 86.505  120.351 1.00 27.45 ? 576  ALA   A N     1 
ATOM   4257  C  CA    . ALA   A 1  578  ? -31.373 86.127  120.569 1.00 26.94 ? 576  ALA   A CA    1 
ATOM   4258  C  C     . ALA   A 1  578  ? -30.815 87.087  121.601 1.00 29.97 ? 576  ALA   A C     1 
ATOM   4259  O  O     . ALA   A 1  578  ? -30.925 88.306  121.434 1.00 30.01 ? 576  ALA   A O     1 
ATOM   4260  C  CB    . ALA   A 1  578  ? -30.556 86.234  119.277 1.00 26.69 ? 576  ALA   A CB    1 
ATOM   4261  N  N     . LEU   A 1  579  ? -30.244 86.545  122.666 1.00 28.03 ? 577  LEU   A N     1 
ATOM   4262  C  CA    . LEU   A 1  579  ? -29.746 87.333  123.781 1.00 31.12 ? 577  LEU   A CA    1 
ATOM   4263  C  C     . LEU   A 1  579  ? -28.301 86.959  124.039 1.00 29.78 ? 577  LEU   A C     1 
ATOM   4264  O  O     . LEU   A 1  579  ? -27.864 85.860  123.684 1.00 27.44 ? 577  LEU   A O     1 
ATOM   4265  C  CB    . LEU   A 1  579  ? -30.551 87.052  125.061 1.00 29.18 ? 577  LEU   A CB    1 
ATOM   4266  C  CG    . LEU   A 1  579  ? -32.062 87.234  124.973 1.00 35.08 ? 577  LEU   A CG    1 
ATOM   4267  C  CD1   . LEU   A 1  579  ? -32.691 86.949  126.326 1.00 35.26 ? 577  LEU   A CD1   1 
ATOM   4268  C  CD2   . LEU   A 1  579  ? -32.402 88.636  124.502 1.00 39.68 ? 577  LEU   A CD2   1 
ATOM   4269  N  N     . PRO   A 1  580  ? -27.528 87.853  124.672 1.00 28.28 ? 578  PRO   A N     1 
ATOM   4270  C  CA    . PRO   A 1  580  ? -26.210 87.456  125.169 1.00 29.68 ? 578  PRO   A CA    1 
ATOM   4271  C  C     . PRO   A 1  580  ? -26.376 86.468  126.308 1.00 33.63 ? 578  PRO   A C     1 
ATOM   4272  O  O     . PRO   A 1  580  ? -26.711 86.849  127.434 1.00 36.65 ? 578  PRO   A O     1 
ATOM   4273  C  CB    . PRO   A 1  580  ? -25.591 88.778  125.644 1.00 31.82 ? 578  PRO   A CB    1 
ATOM   4274  C  CG    . PRO   A 1  580  ? -26.505 89.873  125.127 1.00 33.72 ? 578  PRO   A CG    1 
ATOM   4275  C  CD    . PRO   A 1  580  ? -27.851 89.245  125.024 1.00 30.59 ? 578  PRO   A CD    1 
ATOM   4276  N  N     . GLN   A 1  581  ? -26.194 85.189  126.008 1.00 30.24 ? 579  GLN   A N     1 
ATOM   4277  C  CA    . GLN   A 1  581  ? -26.410 84.112  126.967 1.00 31.41 ? 579  GLN   A CA    1 
ATOM   4278  C  C     . GLN   A 1  581  ? -25.071 83.804  127.610 1.00 30.35 ? 579  GLN   A C     1 
ATOM   4279  O  O     . GLN   A 1  581  ? -24.330 82.928  127.169 1.00 31.00 ? 579  GLN   A O     1 
ATOM   4280  C  CB    . GLN   A 1  581  ? -26.988 82.887  126.272 1.00 29.56 ? 579  GLN   A CB    1 
ATOM   4281  C  CG    . GLN   A 1  581  ? -28.352 83.112  125.654 1.00 31.81 ? 579  GLN   A CG    1 
ATOM   4282  C  CD    . GLN   A 1  581  ? -29.438 83.265  126.701 1.00 33.70 ? 579  GLN   A CD    1 
ATOM   4283  O  OE1   . GLN   A 1  581  ? -29.193 83.081  127.896 1.00 31.90 ? 579  GLN   A OE1   1 
ATOM   4284  N  NE2   . GLN   A 1  581  ? -30.644 83.599  126.262 1.00 32.81 ? 579  GLN   A NE2   1 
ATOM   4285  N  N     . LEU   A 1  582  ? -24.753 84.548  128.663 1.00 33.07 ? 580  LEU   A N     1 
ATOM   4286  C  CA    . LEU   A 1  582  ? -23.533 84.314  129.410 1.00 32.54 ? 580  LEU   A CA    1 
ATOM   4287  C  C     . LEU   A 1  582  ? -23.713 83.121  130.349 1.00 34.05 ? 580  LEU   A C     1 
ATOM   4288  O  O     . LEU   A 1  582  ? -24.824 82.624  130.564 1.00 36.18 ? 580  LEU   A O     1 
ATOM   4289  C  CB    . LEU   A 1  582  ? -23.132 85.575  130.173 1.00 34.43 ? 580  LEU   A CB    1 
ATOM   4290  C  CG    . LEU   A 1  582  ? -22.233 86.563  129.413 1.00 42.99 ? 580  LEU   A CG    1 
ATOM   4291  C  CD1   . LEU   A 1  582  ? -22.922 87.124  128.182 1.00 39.39 ? 580  LEU   A CD1   1 
ATOM   4292  C  CD2   . LEU   A 1  582  ? -21.787 87.699  130.314 1.00 44.24 ? 580  LEU   A CD2   1 
ATOM   4293  N  N     . ALA   A 1  583  ? -22.595 82.645  130.902 1.00 32.95 ? 581  ALA   A N     1 
ATOM   4294  C  CA    . ALA   A 1  583  ? -22.667 81.525  131.831 1.00 33.15 ? 581  ALA   A CA    1 
ATOM   4295  C  C     . ALA   A 1  583  ? -23.536 81.867  133.029 1.00 35.71 ? 581  ALA   A C     1 
ATOM   4296  O  O     . ALA   A 1  583  ? -24.145 80.977  133.630 1.00 43.79 ? 581  ALA   A O     1 
ATOM   4297  C  CB    . ALA   A 1  583  ? -21.266 81.131  132.296 1.00 35.19 ? 581  ALA   A CB    1 
ATOM   4298  N  N     . THR   A 1  584  ? -23.613 83.150  133.374 1.00 36.38 ? 582  THR   A N     1 
ATOM   4299  C  CA    . THR   A 1  584  ? -24.376 83.622  134.520 1.00 37.93 ? 582  THR   A CA    1 
ATOM   4300  C  C     . THR   A 1  584  ? -25.848 83.825  134.202 1.00 40.85 ? 582  THR   A C     1 
ATOM   4301  O  O     . THR   A 1  584  ? -26.643 84.022  135.128 1.00 44.01 ? 582  THR   A O     1 
ATOM   4302  C  CB    . THR   A 1  584  ? -23.788 84.950  135.013 1.00 40.90 ? 582  THR   A CB    1 
ATOM   4303  O  OG1   . THR   A 1  584  ? -23.704 85.871  133.917 1.00 45.26 ? 582  THR   A OG1   1 
ATOM   4304  C  CG2   . THR   A 1  584  ? -22.401 84.743  135.602 1.00 45.20 ? 582  THR   A CG2   1 
ATOM   4305  N  N     . GLY   A 1  585  ? -26.226 83.790  132.927 1.00 38.97 ? 583  GLY   A N     1 
ATOM   4306  C  CA    . GLY   A 1  585  ? -27.583 84.063  132.521 1.00 39.32 ? 583  GLY   A CA    1 
ATOM   4307  C  C     . GLY   A 1  585  ? -27.643 85.098  131.415 1.00 41.93 ? 583  GLY   A C     1 
ATOM   4308  O  O     . GLY   A 1  585  ? -26.622 85.658  131.002 1.00 40.63 ? 583  GLY   A O     1 
ATOM   4309  N  N     . PRO   A 1  586  ? -28.848 85.374  130.917 1.00 39.19 ? 584  PRO   A N     1 
ATOM   4310  C  CA    . PRO   A 1  586  ? -28.994 86.382  129.860 1.00 37.12 ? 584  PRO   A CA    1 
ATOM   4311  C  C     . PRO   A 1  586  ? -28.514 87.741  130.340 1.00 43.88 ? 584  PRO   A C     1 
ATOM   4312  O  O     . PRO   A 1  586  ? -28.757 88.137  131.482 1.00 39.68 ? 584  PRO   A O     1 
ATOM   4313  C  CB    . PRO   A 1  586  ? -30.503 86.400  129.591 1.00 45.62 ? 584  PRO   A CB    1 
ATOM   4314  C  CG    . PRO   A 1  586  ? -31.057 85.184  130.283 1.00 46.50 ? 584  PRO   A CG    1 
ATOM   4315  C  CD    . PRO   A 1  586  ? -30.149 84.903  131.418 1.00 43.33 ? 584  PRO   A CD    1 
ATOM   4316  N  N     . ALA   A 1  587  ? -27.827 88.457  129.456 1.00 38.46 ? 585  ALA   A N     1 
ATOM   4317  C  CA    . ALA   A 1  587  ? -27.296 89.778  129.754 1.00 38.96 ? 585  ALA   A CA    1 
ATOM   4318  C  C     . ALA   A 1  587  ? -28.096 90.844  129.018 1.00 41.38 ? 585  ALA   A C     1 
ATOM   4319  O  O     . ALA   A 1  587  ? -28.720 90.579  127.987 1.00 38.19 ? 585  ALA   A O     1 
ATOM   4320  C  CB    . ALA   A 1  587  ? -25.819 89.880  129.359 1.00 42.77 ? 585  ALA   A CB    1 
ATOM   4321  N  N     . ALA   A 1  588  ? -28.093 92.053  129.572 1.00 39.90 ? 586  ALA   A N     1 
ATOM   4322  C  CA    . ALA   A 1  588  ? -28.743 93.177  128.924 1.00 37.31 ? 586  ALA   A CA    1 
ATOM   4323  C  C     . ALA   A 1  588  ? -27.849 93.741  127.824 1.00 39.00 ? 586  ALA   A C     1 
ATOM   4324  O  O     . ALA   A 1  588  ? -26.640 93.498  127.781 1.00 41.49 ? 586  ALA   A O     1 
ATOM   4325  C  CB    . ALA   A 1  588  ? -29.046 94.273  129.947 1.00 36.87 ? 586  ALA   A CB    1 
ATOM   4326  N  N     . GLY   A 1  589  ? -28.461 94.506  126.930 1.00 38.61 ? 587  GLY   A N     1 
ATOM   4327  C  CA    . GLY   A 1  589  ? -27.704 95.129  125.862 1.00 37.77 ? 587  GLY   A CA    1 
ATOM   4328  C  C     . GLY   A 1  589  ? -28.622 95.875  124.919 1.00 39.75 ? 587  GLY   A C     1 
ATOM   4329  O  O     . GLY   A 1  589  ? -29.821 96.022  125.172 1.00 41.61 ? 587  GLY   A O     1 
ATOM   4330  N  N     . GLU   A 1  590  ? -28.037 96.350  123.822 1.00 41.13 ? 588  GLU   A N     1 
ATOM   4331  C  CA    . GLU   A 1  590  ? -28.804 97.065  122.812 1.00 37.66 ? 588  GLU   A CA    1 
ATOM   4332  C  C     . GLU   A 1  590  ? -29.660 96.084  122.020 1.00 35.73 ? 588  GLU   A C     1 
ATOM   4333  O  O     . GLU   A 1  590  ? -29.154 95.099  121.471 1.00 34.22 ? 588  GLU   A O     1 
ATOM   4334  C  CB    . GLU   A 1  590  ? -27.865 97.818  121.872 1.00 42.95 ? 588  GLU   A CB    1 
ATOM   4335  N  N     . THR   A 1  591  ? -30.957 96.365  121.949 1.00 35.52 ? 589  THR   A N     1 
ATOM   4336  C  CA    . THR   A 1  591  ? -31.928 95.469  121.339 1.00 34.58 ? 589  THR   A CA    1 
ATOM   4337  C  C     . THR   A 1  591  ? -32.473 96.082  120.055 1.00 36.41 ? 589  THR   A C     1 
ATOM   4338  O  O     . THR   A 1  591  ? -32.743 97.285  119.995 1.00 36.61 ? 589  THR   A O     1 
ATOM   4339  C  CB    . THR   A 1  591  ? -33.071 95.197  122.324 1.00 39.13 ? 589  THR   A CB    1 
ATOM   4340  O  OG1   . THR   A 1  591  ? -32.554 94.531  123.486 1.00 38.77 ? 589  THR   A OG1   1 
ATOM   4341  C  CG2   . THR   A 1  591  ? -34.136 94.332  121.692 1.00 37.42 ? 589  THR   A CG2   1 
ATOM   4342  N  N     . ARG   A 1  592  ? -32.623 95.252  119.022 1.00 29.80 ? 590  ARG   A N     1 
ATOM   4343  C  CA    . ARG   A 1  592  ? -33.210 95.704  117.771 1.00 35.65 ? 590  ARG   A CA    1 
ATOM   4344  C  C     . ARG   A 1  592  ? -33.959 94.542  117.139 1.00 34.09 ? 590  ARG   A C     1 
ATOM   4345  O  O     . ARG   A 1  592  ? -33.741 93.376  117.479 1.00 31.54 ? 590  ARG   A O     1 
ATOM   4346  C  CB    . ARG   A 1  592  ? -32.153 96.236  116.798 1.00 34.99 ? 590  ARG   A CB    1 
ATOM   4347  C  CG    . ARG   A 1  592  ? -31.190 95.176  116.309 1.00 36.84 ? 590  ARG   A CG    1 
ATOM   4348  C  CD    . ARG   A 1  592  ? -30.428 95.633  115.076 1.00 40.96 ? 590  ARG   A CD    1 
ATOM   4349  N  NE    . ARG   A 1  592  ? -29.368 94.693  114.736 1.00 40.75 ? 590  ARG   A NE    1 
ATOM   4350  C  CZ    . ARG   A 1  592  ? -29.556 93.566  114.064 1.00 37.39 ? 590  ARG   A CZ    1 
ATOM   4351  N  NH1   . ARG   A 1  592  ? -30.754 93.216  113.623 1.00 38.95 ? 590  ARG   A NH1   1 
ATOM   4352  N  NH2   . ARG   A 1  592  ? -28.517 92.768  113.833 1.00 39.24 ? 590  ARG   A NH2   1 
ATOM   4353  N  N     . THR   A 1  593  ? -34.858 94.876  116.220 1.00 33.24 ? 591  THR   A N     1 
ATOM   4354  C  CA    . THR   A 1  593  ? -35.577 93.835  115.509 1.00 29.71 ? 591  THR   A CA    1 
ATOM   4355  C  C     . THR   A 1  593  ? -34.699 93.208  114.430 1.00 30.96 ? 591  THR   A C     1 
ATOM   4356  O  O     . THR   A 1  593  ? -33.721 93.794  113.952 1.00 32.43 ? 591  THR   A O     1 
ATOM   4357  C  CB    . THR   A 1  593  ? -36.823 94.404  114.850 1.00 35.19 ? 591  THR   A CB    1 
ATOM   4358  O  OG1   . THR   A 1  593  ? -36.433 95.461  113.968 1.00 36.56 ? 591  THR   A OG1   1 
ATOM   4359  C  CG2   . THR   A 1  593  ? -37.787 94.934  115.908 1.00 38.59 ? 591  THR   A CG2   1 
ATOM   4360  N  N     . VAL   A 1  594  ? -35.067 91.989  114.059 1.00 29.16 ? 592  VAL   A N     1 
ATOM   4361  C  CA    . VAL   A 1  594  ? -34.476 91.277  112.935 1.00 27.96 ? 592  VAL   A CA    1 
ATOM   4362  C  C     . VAL   A 1  594  ? -35.558 91.198  111.871 1.00 30.37 ? 592  VAL   A C     1 
ATOM   4363  O  O     . VAL   A 1  594  ? -36.644 90.664  112.127 1.00 27.97 ? 592  VAL   A O     1 
ATOM   4364  C  CB    . VAL   A 1  594  ? -34.006 89.875  113.348 1.00 26.78 ? 592  VAL   A CB    1 
ATOM   4365  C  CG1   . VAL   A 1  594  ? -33.432 89.123  112.151 1.00 27.15 ? 592  VAL   A CG1   1 
ATOM   4366  C  CG2   . VAL   A 1  594  ? -32.966 89.966  114.472 1.00 29.87 ? 592  VAL   A CG2   1 
ATOM   4367  N  N     . LEU   A 1  595  ? -35.273 91.733  110.686 1.00 28.22 ? 593  LEU   A N     1 
ATOM   4368  C  CA    . LEU   A 1  595  ? -36.258 91.857  109.620 1.00 28.68 ? 593  LEU   A CA    1 
ATOM   4369  C  C     . LEU   A 1  595  ? -35.973 90.845  108.519 1.00 27.59 ? 593  LEU   A C     1 
ATOM   4370  O  O     . LEU   A 1  595  ? -34.812 90.549  108.220 1.00 28.69 ? 593  LEU   A O     1 
ATOM   4371  C  CB    . LEU   A 1  595  ? -36.245 93.273  109.027 1.00 29.09 ? 593  LEU   A CB    1 
ATOM   4372  C  CG    . LEU   A 1  595  ? -36.471 94.444  109.989 1.00 31.15 ? 593  LEU   A CG    1 
ATOM   4373  C  CD1   . LEU   A 1  595  ? -36.558 95.768  109.239 1.00 33.99 ? 593  LEU   A CD1   1 
ATOM   4374  C  CD2   . LEU   A 1  595  ? -37.720 94.214  110.820 1.00 31.91 ? 593  LEU   A CD2   1 
ATOM   4375  N  N     . ASN   A 1  596  ? -37.038 90.318  107.927 1.00 25.39 ? 594  ASN   A N     1 
ATOM   4376  C  CA    . ASN   A 1  596  ? -36.928 89.392  106.806 1.00 25.14 ? 594  ASN   A CA    1 
ATOM   4377  C  C     . ASN   A 1  596  ? -36.261 90.106  105.635 1.00 23.97 ? 594  ASN   A C     1 
ATOM   4378  O  O     . ASN   A 1  596  ? -36.773 91.137  105.180 1.00 24.50 ? 594  ASN   A O     1 
ATOM   4379  C  CB    . ASN   A 1  596  ? -38.349 88.981  106.424 1.00 24.48 ? 594  ASN   A CB    1 
ATOM   4380  C  CG    . ASN   A 1  596  ? -38.397 87.888  105.371 1.00 25.58 ? 594  ASN   A CG    1 
ATOM   4381  O  OD1   . ASN   A 1  596  ? -37.540 87.803  104.492 1.00 25.16 ? 594  ASN   A OD1   1 
ATOM   4382  N  ND2   . ASN   A 1  596  ? -39.419 87.045  105.456 1.00 26.73 ? 594  ASN   A ND2   1 
ATOM   4383  N  N     . PRO   A 1  597  ? -35.135 89.609  105.118 1.00 23.12 ? 595  PRO   A N     1 
ATOM   4384  C  CA    . PRO   A 1  597  ? -34.468 90.320  104.016 1.00 23.02 ? 595  PRO   A CA    1 
ATOM   4385  C  C     . PRO   A 1  597  ? -35.300 90.394  102.756 1.00 23.22 ? 595  PRO   A C     1 
ATOM   4386  O  O     . PRO   A 1  597  ? -35.068 91.278  101.922 1.00 24.71 ? 595  PRO   A O     1 
ATOM   4387  C  CB    . PRO   A 1  597  ? -33.173 89.519  103.799 1.00 23.06 ? 595  PRO   A CB    1 
ATOM   4388  C  CG    . PRO   A 1  597  ? -33.449 88.167  104.374 1.00 23.51 ? 595  PRO   A CG    1 
ATOM   4389  C  CD    . PRO   A 1  597  ? -34.393 88.406  105.535 1.00 22.65 ? 595  PRO   A CD    1 
ATOM   4390  N  N     . GLY   A 1  598  ? -36.281 89.514  102.600 1.00 21.86 ? 596  GLY   A N     1 
ATOM   4391  C  CA    . GLY   A 1  598  ? -37.147 89.560  101.443 1.00 22.54 ? 596  GLY   A CA    1 
ATOM   4392  C  C     . GLY   A 1  598  ? -38.329 90.479  101.580 1.00 26.33 ? 596  GLY   A C     1 
ATOM   4393  O  O     . GLY   A 1  598  ? -39.055 90.689  100.602 1.00 24.92 ? 596  GLY   A O     1 
ATOM   4394  N  N     . ASP   A 1  599  ? -38.532 91.040  102.770 1.00 24.83 ? 597  ASP   A N     1 
ATOM   4395  C  CA    . ASP   A 1  599  ? -39.657 91.927  103.035 1.00 24.55 ? 597  ASP   A CA    1 
ATOM   4396  C  C     . ASP   A 1  599  ? -39.461 92.507  104.422 1.00 24.46 ? 597  ASP   A C     1 
ATOM   4397  O  O     . ASP   A 1  599  ? -39.796 91.861  105.422 1.00 24.78 ? 597  ASP   A O     1 
ATOM   4398  C  CB    . ASP   A 1  599  ? -40.969 91.150  102.989 1.00 25.93 ? 597  ASP   A CB    1 
ATOM   4399  C  CG    . ASP   A 1  599  ? -42.187 92.042  103.113 1.00 28.46 ? 597  ASP   A CG    1 
ATOM   4400  O  OD1   . ASP   A 1  599  ? -42.059 93.189  103.588 1.00 28.43 ? 597  ASP   A OD1   1 
ATOM   4401  O  OD2   . ASP   A 1  599  ? -43.278 91.580  102.728 1.00 30.07 ? 597  ASP   A OD2   1 
ATOM   4402  N  N     . HIS   A 1  600  ? -38.908 93.718  104.485 1.00 23.94 ? 598  HIS   A N     1 
ATOM   4403  C  CA    . HIS   A 1  600  ? -38.555 94.323  105.763 1.00 27.76 ? 598  HIS   A CA    1 
ATOM   4404  C  C     . HIS   A 1  600  ? -39.761 94.580  106.659 1.00 27.86 ? 598  HIS   A C     1 
ATOM   4405  O  O     . HIS   A 1  600  ? -39.568 94.852  107.850 1.00 32.06 ? 598  HIS   A O     1 
ATOM   4406  C  CB    . HIS   A 1  600  ? -37.747 95.603  105.535 1.00 30.16 ? 598  HIS   A CB    1 
ATOM   4407  C  CG    . HIS   A 1  600  ? -36.369 95.355  105.005 1.00 33.71 ? 598  HIS   A CG    1 
ATOM   4408  N  ND1   . HIS   A 1  600  ? -35.510 96.373  104.647 1.00 35.61 ? 598  HIS   A ND1   1 
ATOM   4409  C  CD2   . HIS   A 1  600  ? -35.697 94.200  104.777 1.00 31.37 ? 598  HIS   A CD2   1 
ATOM   4410  C  CE1   . HIS   A 1  600  ? -34.372 95.856  104.218 1.00 40.16 ? 598  HIS   A CE1   1 
ATOM   4411  N  NE2   . HIS   A 1  600  ? -34.458 94.540  104.289 1.00 34.54 ? 598  HIS   A NE2   1 
ATOM   4412  N  N     . ARG   A 1  601  ? -40.984 94.488  106.126 1.00 28.23 ? 599  ARG   A N     1 
ATOM   4413  C  CA    . ARG   A 1  601  ? -42.186 94.612  106.944 1.00 29.41 ? 599  ARG   A CA    1 
ATOM   4414  C  C     . ARG   A 1  601  ? -42.415 93.389  107.821 1.00 33.55 ? 599  ARG   A C     1 
ATOM   4415  O  O     . ARG   A 1  601  ? -43.165 93.477  108.800 1.00 33.53 ? 599  ARG   A O     1 
ATOM   4416  C  CB    . ARG   A 1  601  ? -43.408 94.805  106.047 1.00 28.91 ? 599  ARG   A CB    1 
ATOM   4417  C  CG    . ARG   A 1  601  ? -43.301 95.988  105.109 1.00 30.63 ? 599  ARG   A CG    1 
ATOM   4418  C  CD    . ARG   A 1  601  ? -44.407 95.971  104.071 1.00 33.65 ? 599  ARG   A CD    1 
ATOM   4419  N  NE    . ARG   A 1  601  ? -44.368 94.775  103.236 1.00 31.71 ? 599  ARG   A NE    1 
ATOM   4420  C  CZ    . ARG   A 1  601  ? -45.264 94.491  102.301 1.00 34.67 ? 599  ARG   A CZ    1 
ATOM   4421  N  NH1   . ARG   A 1  601  ? -46.280 95.305  102.044 1.00 34.72 ? 599  ARG   A NH1   1 
ATOM   4422  N  NH2   . ARG   A 1  601  ? -45.143 93.362  101.608 1.00 32.18 ? 599  ARG   A NH2   1 
ATOM   4423  N  N     . ASP   A 1  602  ? -41.795 92.259  107.487 1.00 28.30 ? 600  ASP   A N     1 
ATOM   4424  C  CA    . ASP   A 1  602  ? -41.956 91.013  108.233 1.00 30.35 ? 600  ASP   A CA    1 
ATOM   4425  C  C     . ASP   A 1  602  ? -40.891 90.968  109.318 1.00 31.14 ? 600  ASP   A C     1 
ATOM   4426  O  O     . ASP   A 1  602  ? -39.737 90.623  109.059 1.00 30.09 ? 600  ASP   A O     1 
ATOM   4427  C  CB    . ASP   A 1  602  ? -41.829 89.813  107.300 1.00 31.34 ? 600  ASP   A CB    1 
ATOM   4428  C  CG    . ASP   A 1  602  ? -41.999 88.489  108.027 1.00 32.72 ? 600  ASP   A CG    1 
ATOM   4429  O  OD1   . ASP   A 1  602  ? -42.616 88.483  109.111 1.00 32.88 ? 600  ASP   A OD1   1 
ATOM   4430  O  OD2   . ASP   A 1  602  ? -41.503 87.457  107.521 1.00 30.79 ? 600  ASP   A OD2   1 
ATOM   4431  N  N     . VAL   A 1  603  ? -41.280 91.309  110.541 1.00 28.86 ? 601  VAL   A N     1 
ATOM   4432  C  CA    . VAL   A 1  603  ? -40.370 91.265  111.678 1.00 28.46 ? 601  VAL   A CA    1 
ATOM   4433  C  C     . VAL   A 1  603  ? -40.256 89.816  112.131 1.00 29.66 ? 601  VAL   A C     1 
ATOM   4434  O  O     . VAL   A 1  603  ? -41.256 89.183  112.486 1.00 31.37 ? 601  VAL   A O     1 
ATOM   4435  C  CB    . VAL   A 1  603  ? -40.874 92.168  112.812 1.00 31.26 ? 601  VAL   A CB    1 
ATOM   4436  C  CG1   . VAL   A 1  603  ? -39.963 92.061  114.019 1.00 34.31 ? 601  VAL   A CG1   1 
ATOM   4437  C  CG2   . VAL   A 1  603  ? -40.952 93.608  112.340 1.00 31.31 ? 601  VAL   A CG2   1 
ATOM   4438  N  N     . VAL   A 1  604  ? -39.042 89.280  112.099 1.00 29.22 ? 602  VAL   A N     1 
ATOM   4439  C  CA    . VAL   A 1  604  ? -38.831 87.879  112.446 1.00 27.91 ? 602  VAL   A CA    1 
ATOM   4440  C  C     . VAL   A 1  604  ? -38.587 87.713  113.934 1.00 26.91 ? 602  VAL   A C     1 
ATOM   4441  O  O     . VAL   A 1  604  ? -39.041 86.745  114.547 1.00 29.98 ? 602  VAL   A O     1 
ATOM   4442  C  CB    . VAL   A 1  604  ? -37.675 87.294  111.614 1.00 25.09 ? 602  VAL   A CB    1 
ATOM   4443  C  CG1   . VAL   A 1  604  ? -37.524 85.818  111.915 1.00 26.40 ? 602  VAL   A CG1   1 
ATOM   4444  C  CG2   . VAL   A 1  604  ? -37.925 87.530  110.126 1.00 25.95 ? 602  VAL   A CG2   1 
ATOM   4445  N  N     . GLY   A 1  605  ? -37.888 88.657  114.539 1.00 27.38 ? 603  GLY   A N     1 
ATOM   4446  C  CA    . GLY   A 1  605  ? -37.625 88.560  115.953 1.00 28.51 ? 603  GLY   A CA    1 
ATOM   4447  C  C     . GLY   A 1  605  ? -36.822 89.739  116.426 1.00 28.47 ? 603  GLY   A C     1 
ATOM   4448  O  O     . GLY   A 1  605  ? -36.760 90.780  115.771 1.00 30.15 ? 603  GLY   A O     1 
ATOM   4449  N  N     . SER   A 1  606  ? -36.190 89.552  117.576 1.00 27.48 ? 604  SER   A N     1 
ATOM   4450  C  CA    A SER   A 1  606  ? -35.444 90.621  118.209 0.51 26.96 ? 604  SER   A CA    1 
ATOM   4451  C  CA    B SER   A 1  606  ? -35.458 90.617  118.234 0.49 26.99 ? 604  SER   A CA    1 
ATOM   4452  C  C     . SER   A 1  606  ? -34.134 90.062  118.728 1.00 30.54 ? 604  SER   A C     1 
ATOM   4453  O  O     . SER   A 1  606  ? -34.080 88.941  119.242 1.00 30.29 ? 604  SER   A O     1 
ATOM   4454  C  CB    A SER   A 1  606  ? -36.239 91.245  119.358 0.51 30.76 ? 604  SER   A CB    1 
ATOM   4455  C  CB    B SER   A 1  606  ? -36.265 91.152  119.419 0.49 30.74 ? 604  SER   A CB    1 
ATOM   4456  O  OG    A SER   A 1  606  ? -37.396 91.891  118.863 0.51 30.85 ? 604  SER   A OG    1 
ATOM   4457  O  OG    B SER   A 1  606  ? -35.492 92.034  120.203 0.49 29.06 ? 604  SER   A OG    1 
ATOM   4458  N  N     . VAL   A 1  607  ? -33.073 90.839  118.564 1.00 26.90 ? 605  VAL   A N     1 
ATOM   4459  C  CA    . VAL   A 1  607  ? -31.755 90.449  119.037 1.00 26.07 ? 605  VAL   A CA    1 
ATOM   4460  C  C     . VAL   A 1  607  ? -31.280 91.506  120.018 1.00 28.44 ? 605  VAL   A C     1 
ATOM   4461  O  O     . VAL   A 1  607  ? -31.424 92.707  119.765 1.00 29.49 ? 605  VAL   A O     1 
ATOM   4462  C  CB    . VAL   A 1  607  ? -30.747 90.244  117.888 1.00 26.69 ? 605  VAL   A CB    1 
ATOM   4463  C  CG1   . VAL   A 1  607  ? -30.616 91.502  117.033 1.00 30.93 ? 605  VAL   A CG1   1 
ATOM   4464  C  CG2   . VAL   A 1  607  ? -29.384 89.824  118.448 1.00 26.94 ? 605  VAL   A CG2   1 
ATOM   4465  N  N     . THR   A 1  608  ? -30.749 91.053  121.145 1.00 29.09 ? 606  THR   A N     1 
ATOM   4466  C  CA    . THR   A 1  608  ? -30.033 91.904  122.079 1.00 31.28 ? 606  THR   A CA    1 
ATOM   4467  C  C     . THR   A 1  608  ? -28.551 91.630  121.880 1.00 30.84 ? 606  THR   A C     1 
ATOM   4468  O  O     . THR   A 1  608  ? -28.102 90.489  122.032 1.00 29.29 ? 606  THR   A O     1 
ATOM   4469  C  CB    . THR   A 1  608  ? -30.449 91.569  123.507 1.00 31.88 ? 606  THR   A CB    1 
ATOM   4470  O  OG1   . THR   A 1  608  ? -31.850 91.841  123.665 1.00 31.72 ? 606  THR   A OG1   1 
ATOM   4471  C  CG2   . THR   A 1  608  ? -29.655 92.402  124.492 1.00 34.40 ? 606  THR   A CG2   1 
ATOM   4472  N  N     . GLU   A 1  609  ? -27.800 92.663  121.521 1.00 30.25 ? 607  GLU   A N     1 
ATOM   4473  C  CA    . GLU   A 1  609  ? -26.401 92.477  121.171 1.00 32.24 ? 607  GLU   A CA    1 
ATOM   4474  C  C     . GLU   A 1  609  ? -25.484 92.645  122.381 1.00 29.67 ? 607  GLU   A C     1 
ATOM   4475  O  O     . GLU   A 1  609  ? -25.825 93.303  123.368 1.00 30.90 ? 607  GLU   A O     1 
ATOM   4476  C  CB    . GLU   A 1  609  ? -26.019 93.379  119.994 1.00 33.66 ? 607  GLU   A CB    1 
ATOM   4477  C  CG    . GLU   A 1  609  ? -26.738 92.927  118.712 1.00 37.31 ? 607  GLU   A CG    1 
ATOM   4478  C  CD    . GLU   A 1  609  ? -26.386 93.736  117.478 1.00 43.72 ? 607  GLU   A CD    1 
ATOM   4479  O  OE1   . GLU   A 1  609  ? -26.154 94.957  117.605 1.00 50.35 ? 607  GLU   A OE1   1 
ATOM   4480  O  OE2   . GLU   A 1  609  ? -26.347 93.141  116.374 1.00 41.01 ? 607  GLU   A OE2   1 
ATOM   4481  N  N     . THR   A 1  610  ? -24.324 92.009  122.305 1.00 29.74 ? 608  THR   A N     1 
ATOM   4482  C  CA    . THR   A 1  610  ? -23.420 91.883  123.439 1.00 30.29 ? 608  THR   A CA    1 
ATOM   4483  C  C     . THR   A 1  610  ? -22.511 93.099  123.505 1.00 33.47 ? 608  THR   A C     1 
ATOM   4484  O  O     . THR   A 1  610  ? -21.925 93.498  122.494 1.00 37.15 ? 608  THR   A O     1 
ATOM   4485  C  CB    . THR   A 1  610  ? -22.563 90.629  123.253 1.00 33.00 ? 608  THR   A CB    1 
ATOM   4486  O  OG1   . THR   A 1  610  ? -23.411 89.502  123.007 1.00 30.33 ? 608  THR   A OG1   1 
ATOM   4487  C  CG2   . THR   A 1  610  ? -21.700 90.363  124.478 1.00 31.48 ? 608  THR   A CG2   1 
ATOM   4488  N  N     . SER   A 1  611  ? -22.382 93.678  124.693 1.00 33.52 ? 609  SER   A N     1 
ATOM   4489  C  CA    . SER   A 1  611  ? -21.393 94.724  124.878 1.00 35.17 ? 609  SER   A CA    1 
ATOM   4490  C  C     . SER   A 1  611  ? -19.999 94.117  124.845 1.00 39.01 ? 609  SER   A C     1 
ATOM   4491  O  O     . SER   A 1  611  ? -19.799 92.946  125.178 1.00 35.44 ? 609  SER   A O     1 
ATOM   4492  C  CB    . SER   A 1  611  ? -21.601 95.418  126.221 1.00 37.59 ? 609  SER   A CB    1 
ATOM   4493  O  OG    . SER   A 1  611  ? -21.155 94.597  127.284 1.00 38.26 ? 609  SER   A OG    1 
ATOM   4494  N  N     . GLU   A 1  612  ? -19.025 94.922  124.422 1.00 39.73 ? 610  GLU   A N     1 
ATOM   4495  C  CA    . GLU   A 1  612  ? -17.651 94.436  124.413 1.00 40.20 ? 610  GLU   A CA    1 
ATOM   4496  C  C     . GLU   A 1  612  ? -17.188 94.061  125.815 1.00 39.44 ? 610  GLU   A C     1 
ATOM   4497  O  O     . GLU   A 1  612  ? -16.400 93.122  125.979 1.00 39.69 ? 610  GLU   A O     1 
ATOM   4498  C  CB    . GLU   A 1  612  ? -16.729 95.461  123.754 1.00 45.83 ? 610  GLU   A CB    1 
ATOM   4499  C  CG    . GLU   A 1  612  ? -16.692 95.337  122.235 1.00 46.54 ? 610  GLU   A CG    1 
ATOM   4500  C  CD    . GLU   A 1  612  ? -16.626 96.676  121.530 1.00 51.67 ? 610  GLU   A CD    1 
ATOM   4501  O  OE1   . GLU   A 1  612  ? -17.671 97.355  121.446 1.00 57.93 ? 610  GLU   A OE1   1 
ATOM   4502  O  OE2   . GLU   A 1  612  ? -15.529 97.050  121.061 1.00 56.47 ? 610  GLU   A OE2   1 
ATOM   4503  N  N     . GLU   A 1  613  ? -17.700 94.749  126.836 1.00 37.06 ? 611  GLU   A N     1 
ATOM   4504  C  CA    . GLU   A 1  613  ? -17.388 94.378  128.212 1.00 44.61 ? 611  GLU   A CA    1 
ATOM   4505  C  C     . GLU   A 1  613  ? -17.934 92.996  128.553 1.00 37.38 ? 611  GLU   A C     1 
ATOM   4506  O  O     . GLU   A 1  613  ? -17.246 92.189  129.188 1.00 34.25 ? 611  GLU   A O     1 
ATOM   4507  C  CB    . GLU   A 1  613  ? -17.938 95.430  129.176 1.00 43.96 ? 611  GLU   A CB    1 
ATOM   4508  N  N     . ASP   A 1  614  ? -19.175 92.706  128.152 1.00 35.73 ? 612  ASP   A N     1 
ATOM   4509  C  CA    . ASP   A 1  614  ? -19.749 91.396  128.442 1.00 32.00 ? 612  ASP   A CA    1 
ATOM   4510  C  C     . ASP   A 1  614  ? -19.087 90.298  127.620 1.00 32.80 ? 612  ASP   A C     1 
ATOM   4511  O  O     . ASP   A 1  614  ? -19.015 89.147  128.067 1.00 31.71 ? 612  ASP   A O     1 
ATOM   4512  C  CB    . ASP   A 1  614  ? -21.253 91.402  128.191 1.00 34.70 ? 612  ASP   A CB    1 
ATOM   4513  C  CG    . ASP   A 1  614  ? -22.017 92.154  129.264 1.00 37.45 ? 612  ASP   A CG    1 
ATOM   4514  O  OD1   . ASP   A 1  614  ? -21.521 92.227  130.409 1.00 40.92 ? 612  ASP   A OD1   1 
ATOM   4515  O  OD2   . ASP   A 1  614  ? -23.113 92.667  128.957 1.00 41.20 ? 612  ASP   A OD2   1 
ATOM   4516  N  N     . ALA   A 1  615  ? -18.610 90.625  126.420 1.00 29.63 ? 613  ALA   A N     1 
ATOM   4517  C  CA    . ALA   A 1  615  ? -17.864 89.642  125.642 1.00 29.58 ? 613  ALA   A CA    1 
ATOM   4518  C  C     . ALA   A 1  615  ? -16.594 89.228  126.376 1.00 31.36 ? 613  ALA   A C     1 
ATOM   4519  O  O     . ALA   A 1  615  ? -16.278 88.036  126.479 1.00 29.71 ? 613  ALA   A O     1 
ATOM   4520  C  CB    . ALA   A 1  615  ? -17.537 90.205  124.261 1.00 30.79 ? 613  ALA   A CB    1 
ATOM   4521  N  N     . ARG   A 1  616  ? -15.856 90.205  126.905 1.00 34.36 ? 614  ARG   A N     1 
ATOM   4522  C  CA    . ARG   A 1  616  ? -14.671 89.883  127.694 1.00 34.20 ? 614  ARG   A CA    1 
ATOM   4523  C  C     . ARG   A 1  616  ? -15.039 89.098  128.945 1.00 32.70 ? 614  ARG   A C     1 
ATOM   4524  O  O     . ARG   A 1  616  ? -14.346 88.144  129.314 1.00 33.31 ? 614  ARG   A O     1 
ATOM   4525  C  CB    . ARG   A 1  616  ? -13.910 91.160  128.048 1.00 36.80 ? 614  ARG   A CB    1 
ATOM   4526  C  CG    . ARG   A 1  616  ? -13.206 91.787  126.855 1.00 44.42 ? 614  ARG   A CG    1 
ATOM   4527  C  CD    . ARG   A 1  616  ? -12.456 93.056  127.234 1.00 52.27 ? 614  ARG   A CD    1 
ATOM   4528  N  NE    . ARG   A 1  616  ? -13.011 94.231  126.573 1.00 55.09 ? 614  ARG   A NE    1 
ATOM   4529  C  CZ    . ARG   A 1  616  ? -13.707 95.181  127.183 1.00 51.35 ? 614  ARG   A CZ    1 
ATOM   4530  N  NH1   . ARG   A 1  616  ? -13.938 95.144  128.487 1.00 57.44 ? 614  ARG   A NH1   1 
ATOM   4531  N  NH2   . ARG   A 1  616  ? -14.176 96.200  126.468 1.00 51.63 ? 614  ARG   A NH2   1 
ATOM   4532  N  N     . ARG   A 1  617  ? -16.146 89.462  129.594 1.00 30.66 ? 615  ARG   A N     1 
ATOM   4533  C  CA    . ARG   A 1  617  ? -16.581 88.703  130.761 1.00 34.36 ? 615  ARG   A CA    1 
ATOM   4534  C  C     . ARG   A 1  617  ? -16.903 87.261  130.387 1.00 33.78 ? 615  ARG   A C     1 
ATOM   4535  O  O     . ARG   A 1  617  ? -16.554 86.329  131.121 1.00 31.75 ? 615  ARG   A O     1 
ATOM   4536  C  CB    . ARG   A 1  617  ? -17.782 89.379  131.420 1.00 36.96 ? 615  ARG   A CB    1 
ATOM   4537  C  CG    . ARG   A 1  617  ? -18.197 88.729  132.723 1.00 42.82 ? 615  ARG   A CG    1 
ATOM   4538  C  CD    . ARG   A 1  617  ? -18.935 89.711  133.615 1.00 48.64 ? 615  ARG   A CD    1 
ATOM   4539  N  NE    . ARG   A 1  617  ? -20.192 90.152  133.027 1.00 46.64 ? 615  ARG   A NE    1 
ATOM   4540  C  CZ    . ARG   A 1  617  ? -21.358 89.553  133.226 1.00 54.06 ? 615  ARG   A CZ    1 
ATOM   4541  N  NH1   . ARG   A 1  617  ? -21.458 88.469  133.981 1.00 50.15 ? 615  ARG   A NH1   1 
ATOM   4542  N  NH2   . ARG   A 1  617  ? -22.452 90.055  132.657 1.00 48.24 ? 615  ARG   A NH2   1 
ATOM   4543  N  N     . ALA   A 1  618  ? -17.552 87.056  129.235 1.00 31.04 ? 616  ALA   A N     1 
ATOM   4544  C  CA    . ALA   A 1  618  ? -17.900 85.703  128.815 1.00 30.88 ? 616  ALA   A CA    1 
ATOM   4545  C  C     . ALA   A 1  618  ? -16.653 84.844  128.636 1.00 28.21 ? 616  ALA   A C     1 
ATOM   4546  O  O     . ALA   A 1  618  ? -16.644 83.664  129.007 1.00 29.57 ? 616  ALA   A O     1 
ATOM   4547  C  CB    . ALA   A 1  618  ? -18.724 85.747  127.526 1.00 30.77 ? 616  ALA   A CB    1 
ATOM   4548  N  N     . VAL   A 1  619  ? -15.583 85.422  128.088 1.00 27.78 ? 617  VAL   A N     1 
ATOM   4549  C  CA    . VAL   A 1  619  ? -14.350 84.656  127.923 1.00 28.15 ? 617  VAL   A CA    1 
ATOM   4550  C  C     . VAL   A 1  619  ? -13.791 84.243  129.278 1.00 29.51 ? 617  VAL   A C     1 
ATOM   4551  O  O     . VAL   A 1  619  ? -13.364 83.098  129.464 1.00 29.68 ? 617  VAL   A O     1 
ATOM   4552  C  CB    . VAL   A 1  619  ? -13.320 85.429  127.079 1.00 29.04 ? 617  VAL   A CB    1 
ATOM   4553  C  CG1   . VAL   A 1  619  ? -12.019 84.644  126.988 1.00 30.37 ? 617  VAL   A CG1   1 
ATOM   4554  C  CG2   . VAL   A 1  619  ? -13.868 85.694  125.685 1.00 28.73 ? 617  VAL   A CG2   1 
ATOM   4555  N  N     . ARG   A 1  620  ? -13.800 85.161  130.250 1.00 29.80 ? 618  ARG   A N     1 
ATOM   4556  C  CA    . ARG   A 1  620  ? -13.301 84.814  131.577 1.00 31.28 ? 618  ARG   A CA    1 
ATOM   4557  C  C     . ARG   A 1  620  ? -14.148 83.720  132.206 1.00 32.60 ? 618  ARG   A C     1 
ATOM   4558  O  O     . ARG   A 1  620  ? -13.612 82.784  132.811 1.00 35.77 ? 618  ARG   A O     1 
ATOM   4559  C  CB    . ARG   A 1  620  ? -13.244 86.055  132.470 1.00 35.52 ? 618  ARG   A CB    1 
ATOM   4560  C  CG    . ARG   A 1  620  ? -12.170 87.047  132.055 1.00 41.84 ? 618  ARG   A CG    1 
ATOM   4561  C  CD    . ARG   A 1  620  ? -12.089 88.234  133.014 1.00 49.21 ? 618  ARG   A CD    1 
ATOM   4562  N  NE    . ARG   A 1  620  ? -12.541 89.468  132.381 1.00 56.84 ? 618  ARG   A NE    1 
ATOM   4563  C  CZ    . ARG   A 1  620  ? -13.616 90.155  132.743 1.00 48.26 ? 618  ARG   A CZ    1 
ATOM   4564  N  NH1   . ARG   A 1  620  ? -14.357 89.788  133.778 1.00 52.70 ? 618  ARG   A NH1   1 
ATOM   4565  N  NH2   . ARG   A 1  620  ? -13.953 91.242  132.055 1.00 51.10 ? 618  ARG   A NH2   1 
ATOM   4566  N  N     . LEU   A 1  621  ? -15.474 83.802  132.047 1.00 28.84 ? 619  LEU   A N     1 
ATOM   4567  C  CA    . LEU   A 1  621  ? -16.339 82.740  132.555 1.00 34.88 ? 619  LEU   A CA    1 
ATOM   4568  C  C     . LEU   A 1  621  ? -16.050 81.419  131.855 1.00 30.94 ? 619  LEU   A C     1 
ATOM   4569  O  O     . LEU   A 1  621  ? -16.059 80.357  132.491 1.00 32.79 ? 619  LEU   A O     1 
ATOM   4570  C  CB    . LEU   A 1  621  ? -17.804 83.126  132.377 1.00 32.62 ? 619  LEU   A CB    1 
ATOM   4571  C  CG    . LEU   A 1  621  ? -18.298 84.356  133.140 1.00 32.86 ? 619  LEU   A CG    1 
ATOM   4572  C  CD1   . LEU   A 1  621  ? -19.697 84.750  132.695 1.00 31.44 ? 619  LEU   A CD1   1 
ATOM   4573  C  CD2   . LEU   A 1  621  ? -18.280 84.095  134.638 1.00 37.74 ? 619  LEU   A CD2   1 
ATOM   4574  N  N     . ALA   A 1  622  ? -15.799 81.466  130.542 1.00 29.28 ? 620  ALA   A N     1 
ATOM   4575  C  CA    . ALA   A 1  622  ? -15.426 80.261  129.808 1.00 30.71 ? 620  ALA   A CA    1 
ATOM   4576  C  C     . ALA   A 1  622  ? -14.124 79.680  130.337 1.00 28.09 ? 620  ALA   A C     1 
ATOM   4577  O  O     . ALA   A 1  622  ? -14.007 78.462  130.515 1.00 31.60 ? 620  ALA   A O     1 
ATOM   4578  C  CB    . ALA   A 1  622  ? -15.290 80.574  128.319 1.00 27.88 ? 620  ALA   A CB    1 
ATOM   4579  N  N     . ALA   A 1  623  ? -13.134 80.540  130.595 1.00 28.95 ? 621  ALA   A N     1 
ATOM   4580  C  CA    . ALA   A 1  623  ? -11.876 80.070  131.162 1.00 29.83 ? 621  ALA   A CA    1 
ATOM   4581  C  C     . ALA   A 1  623  ? -12.094 79.425  132.523 1.00 29.29 ? 621  ALA   A C     1 
ATOM   4582  O  O     . ALA   A 1  623  ? -11.513 78.374  132.816 1.00 31.95 ? 621  ALA   A O     1 
ATOM   4583  C  CB    . ALA   A 1  623  ? -10.879 81.224  131.259 1.00 32.93 ? 621  ALA   A CB    1 
ATOM   4584  N  N     . ASP   A 1  624  ? -12.944 80.034  133.360 1.00 28.99 ? 622  ASP   A N     1 
ATOM   4585  C  CA    . ASP   A 1  624  ? -13.204 79.488  134.691 1.00 35.89 ? 622  ASP   A CA    1 
ATOM   4586  C  C     . ASP   A 1  624  ? -13.856 78.117  134.597 1.00 35.35 ? 622  ASP   A C     1 
ATOM   4587  O  O     . ASP   A 1  624  ? -13.550 77.216  135.387 1.00 40.58 ? 622  ASP   A O     1 
ATOM   4588  C  CB    . ASP   A 1  624  ? -14.129 80.426  135.474 1.00 39.58 ? 622  ASP   A CB    1 
ATOM   4589  C  CG    . ASP   A 1  624  ? -13.484 81.760  135.801 1.00 47.97 ? 622  ASP   A CG    1 
ATOM   4590  O  OD1   . ASP   A 1  624  ? -12.236 81.850  135.785 1.00 52.75 ? 622  ASP   A OD1   1 
ATOM   4591  O  OD2   . ASP   A 1  624  ? -14.236 82.717  136.087 1.00 51.51 ? 622  ASP   A OD2   1 
ATOM   4592  N  N     . ALA   A 1  625  ? -14.751 77.946  133.631 1.00 38.52 ? 623  ALA   A N     1 
ATOM   4593  C  CA    . ALA   A 1  625  ? -15.509 76.721  133.439 1.00 40.36 ? 623  ALA   A CA    1 
ATOM   4594  C  C     . ALA   A 1  625  ? -14.794 75.693  132.582 1.00 37.59 ? 623  ALA   A C     1 
ATOM   4595  O  O     . ALA   A 1  625  ? -15.309 74.580  132.426 1.00 42.36 ? 623  ALA   A O     1 
ATOM   4596  C  CB    . ALA   A 1  625  ? -16.830 77.049  132.753 1.00 43.24 ? 623  ALA   A CB    1 
ATOM   4597  N  N     . ALA   A 1  626  ? -13.649 76.036  132.000 1.00 34.76 ? 624  ALA   A N     1 
ATOM   4598  C  CA    . ALA   A 1  626  ? -12.952 75.095  131.125 1.00 32.61 ? 624  ALA   A CA    1 
ATOM   4599  C  C     . ALA   A 1  626  ? -12.651 73.755  131.790 1.00 33.56 ? 624  ALA   A C     1 
ATOM   4600  O  O     . ALA   A 1  626  ? -12.924 72.714  131.172 1.00 33.59 ? 624  ALA   A O     1 
ATOM   4601  C  CB    . ALA   A 1  626  ? -11.708 75.759  130.519 1.00 33.19 ? 624  ALA   A CB    1 
ATOM   4602  N  N     . PRO   A 1  627  ? -12.109 73.694  133.016 1.00 33.04 ? 625  PRO   A N     1 
ATOM   4603  C  CA    . PRO   A 1  627  ? -11.820 72.373  133.603 1.00 34.69 ? 625  PRO   A CA    1 
ATOM   4604  C  C     . PRO   A 1  627  ? -13.049 71.493  133.755 1.00 32.76 ? 625  PRO   A C     1 
ATOM   4605  O  O     . PRO   A 1  627  ? -12.974 70.281  133.506 1.00 35.42 ? 625  PRO   A O     1 
ATOM   4606  C  CB    . PRO   A 1  627  ? -11.197 72.726  134.963 1.00 33.71 ? 625  PRO   A CB    1 
ATOM   4607  C  CG    . PRO   A 1  627  ? -10.617 74.091  134.754 1.00 34.24 ? 625  PRO   A CG    1 
ATOM   4608  C  CD    . PRO   A 1  627  ? -11.630 74.783  133.887 1.00 36.36 ? 625  PRO   A CD    1 
ATOM   4609  N  N     . ASP   A 1  628  ? -14.182 72.067  134.155 1.00 33.46 ? 626  ASP   A N     1 
ATOM   4610  C  CA    . ASP   A 1  628  ? -15.368 71.250  134.369 1.00 33.88 ? 626  ASP   A CA    1 
ATOM   4611  C  C     . ASP   A 1  628  ? -15.863 70.648  133.066 1.00 37.34 ? 626  ASP   A C     1 
ATOM   4612  O  O     . ASP   A 1  628  ? -16.370 69.521  133.058 1.00 35.94 ? 626  ASP   A O     1 
ATOM   4613  C  CB    . ASP   A 1  628  ? -16.480 72.076  135.021 1.00 35.51 ? 626  ASP   A CB    1 
ATOM   4614  C  CG    . ASP   A 1  628  ? -16.143 72.495  136.442 1.00 40.27 ? 626  ASP   A CG    1 
ATOM   4615  O  OD1   . ASP   A 1  628  ? -15.254 71.863  137.050 1.00 47.08 ? 626  ASP   A OD1   1 
ATOM   4616  O  OD2   . ASP   A 1  628  ? -16.768 73.450  136.945 1.00 49.80 ? 626  ASP   A OD2   1 
ATOM   4617  N  N     . TRP   A 1  629  ? -15.714 71.374  131.961 1.00 31.93 ? 627  TRP   A N     1 
ATOM   4618  C  CA    . TRP   A 1  629  ? -16.184 70.845  130.691 1.00 31.62 ? 627  TRP   A CA    1 
ATOM   4619  C  C     . TRP   A 1  629  ? -15.196 69.839  130.123 1.00 29.37 ? 627  TRP   A C     1 
ATOM   4620  O  O     . TRP   A 1  629  ? -15.604 68.813  129.569 1.00 30.76 ? 627  TRP   A O     1 
ATOM   4621  C  CB    . TRP   A 1  629  ? -16.446 71.978  129.701 1.00 30.03 ? 627  TRP   A CB    1 
ATOM   4622  C  CG    . TRP   A 1  629  ? -16.916 71.473  128.381 1.00 27.75 ? 627  TRP   A CG    1 
ATOM   4623  C  CD1   . TRP   A 1  629  ? -16.314 71.650  127.167 1.00 24.58 ? 627  TRP   A CD1   1 
ATOM   4624  C  CD2   . TRP   A 1  629  ? -18.073 70.666  128.141 1.00 25.93 ? 627  TRP   A CD2   1 
ATOM   4625  N  NE1   . TRP   A 1  629  ? -17.035 71.019  126.191 1.00 26.39 ? 627  TRP   A NE1   1 
ATOM   4626  C  CE2   . TRP   A 1  629  ? -18.122 70.409  126.758 1.00 25.51 ? 627  TRP   A CE2   1 
ATOM   4627  C  CE3   . TRP   A 1  629  ? -19.079 70.147  128.959 1.00 28.57 ? 627  TRP   A CE3   1 
ATOM   4628  C  CZ2   . TRP   A 1  629  ? -19.131 69.650  126.175 1.00 26.63 ? 627  TRP   A CZ2   1 
ATOM   4629  C  CZ3   . TRP   A 1  629  ? -20.079 69.393  128.376 1.00 27.60 ? 627  TRP   A CZ3   1 
ATOM   4630  C  CH2   . TRP   A 1  629  ? -20.098 69.151  126.999 1.00 29.58 ? 627  TRP   A CH2   1 
ATOM   4631  N  N     . ALA   A 1  630  ? -13.895 70.110  130.271 1.00 29.06 ? 628  ALA   A N     1 
ATOM   4632  C  CA    . ALA   A 1  630  ? -12.885 69.158  129.824 1.00 32.15 ? 628  ALA   A CA    1 
ATOM   4633  C  C     . ALA   A 1  630  ? -13.016 67.830  130.551 1.00 31.89 ? 628  ALA   A C     1 
ATOM   4634  O  O     . ALA   A 1  630  ? -12.663 66.781  129.996 1.00 33.20 ? 628  ALA   A O     1 
ATOM   4635  C  CB    . ALA   A 1  630  ? -11.488 69.740  130.035 1.00 30.91 ? 628  ALA   A CB    1 
ATOM   4636  N  N     . ALA   A 1  631  ? -13.522 67.856  131.787 1.00 31.54 ? 629  ALA   A N     1 
ATOM   4637  C  CA    . ALA   A 1  631  ? -13.677 66.653  132.594 1.00 34.66 ? 629  ALA   A CA    1 
ATOM   4638  C  C     . ALA   A 1  631  ? -14.879 65.807  132.194 1.00 34.57 ? 629  ALA   A C     1 
ATOM   4639  O  O     . ALA   A 1  631  ? -14.984 64.661  132.645 1.00 32.86 ? 629  ALA   A O     1 
ATOM   4640  C  CB    . ALA   A 1  631  ? -13.780 67.019  134.076 1.00 34.00 ? 629  ALA   A CB    1 
ATOM   4641  N  N     . VAL   A 1  632  ? -15.791 66.331  131.383 1.00 30.09 ? 630  VAL   A N     1 
ATOM   4642  C  CA    . VAL   A 1  632  ? -16.880 65.507  130.870 1.00 29.73 ? 630  VAL   A CA    1 
ATOM   4643  C  C     . VAL   A 1  632  ? -16.236 64.573  129.856 1.00 30.39 ? 630  VAL   A C     1 
ATOM   4644  O  O     . VAL   A 1  632  ? -15.585 65.056  128.924 1.00 30.92 ? 630  VAL   A O     1 
ATOM   4645  C  CB    . VAL   A 1  632  ? -17.990 66.369  130.251 1.00 30.72 ? 630  VAL   A CB    1 
ATOM   4646  C  CG1   . VAL   A 1  632  ? -19.100 65.493  129.670 1.00 29.82 ? 630  VAL   A CG1   1 
ATOM   4647  C  CG2   . VAL   A 1  632  ? -18.554 67.315  131.310 1.00 32.01 ? 630  VAL   A CG2   1 
ATOM   4648  N  N     . PRO   A 1  633  ? -16.351 63.253  130.011 1.00 28.25 ? 631  PRO   A N     1 
ATOM   4649  C  CA    . PRO   A 1  633  ? -15.618 62.353  129.125 1.00 26.62 ? 631  PRO   A CA    1 
ATOM   4650  C  C     . PRO   A 1  633  ? -16.030 62.574  127.682 1.00 29.19 ? 631  PRO   A C     1 
ATOM   4651  O  O     . PRO   A 1  633  ? -17.177 62.963  127.398 1.00 28.42 ? 631  PRO   A O     1 
ATOM   4652  C  CB    . PRO   A 1  633  ? -16.033 60.959  129.617 1.00 31.23 ? 631  PRO   A CB    1 
ATOM   4653  C  CG    . PRO   A 1  633  ? -16.488 61.170  131.026 1.00 33.80 ? 631  PRO   A CG    1 
ATOM   4654  C  CD    . PRO   A 1  633  ? -17.108 62.528  131.043 1.00 32.22 ? 631  PRO   A CD    1 
ATOM   4655  N  N     . PRO   A 1  634  ? -15.114 62.360  126.738 1.00 25.28 ? 632  PRO   A N     1 
ATOM   4656  C  CA    . PRO   A 1  634  ? -15.462 62.570  125.321 1.00 24.23 ? 632  PRO   A CA    1 
ATOM   4657  C  C     . PRO   A 1  634  ? -16.721 61.838  124.891 1.00 24.89 ? 632  PRO   A C     1 
ATOM   4658  O  O     . PRO   A 1  634  ? -17.513 62.395  124.128 1.00 23.85 ? 632  PRO   A O     1 
ATOM   4659  C  CB    . PRO   A 1  634  ? -14.215 62.073  124.572 1.00 26.09 ? 632  PRO   A CB    1 
ATOM   4660  C  CG    . PRO   A 1  634  ? -13.100 62.200  125.564 1.00 25.70 ? 632  PRO   A CG    1 
ATOM   4661  C  CD    . PRO   A 1  634  ? -13.697 62.003  126.932 1.00 26.80 ? 632  PRO   A CD    1 
ATOM   4662  N  N     . SER   A 1  635  ? -16.939 60.613  125.379 1.00 27.01 ? 633  SER   A N     1 
ATOM   4663  C  CA    . SER   A 1  635  ? -18.133 59.872  124.982 1.00 26.75 ? 633  SER   A CA    1 
ATOM   4664  C  C     . SER   A 1  635  ? -19.398 60.603  125.412 1.00 26.30 ? 633  SER   A C     1 
ATOM   4665  O  O     . SER   A 1  635  ? -20.390 60.627  124.674 1.00 27.10 ? 633  SER   A O     1 
ATOM   4666  C  CB    . SER   A 1  635  ? -18.098 58.469  125.586 1.00 34.45 ? 633  SER   A CB    1 
ATOM   4667  N  N     . GLU   A 1  636  ? -19.378 61.215  126.600 1.00 26.55 ? 634  GLU   A N     1 
ATOM   4668  C  CA    . GLU   A 1  636  ? -20.556 61.945  127.059 1.00 27.33 ? 634  GLU   A CA    1 
ATOM   4669  C  C     . GLU   A 1  636  ? -20.707 63.275  126.327 1.00 26.73 ? 634  GLU   A C     1 
ATOM   4670  O  O     . GLU   A 1  636  ? -21.830 63.697  126.027 1.00 27.99 ? 634  GLU   A O     1 
ATOM   4671  C  CB    . GLU   A 1  636  ? -20.522 62.131  128.574 1.00 29.25 ? 634  GLU   A CB    1 
ATOM   4672  C  CG    . GLU   A 1  636  ? -21.703 62.925  129.117 1.00 34.27 ? 634  GLU   A CG    1 
ATOM   4673  C  CD    . GLU   A 1  636  ? -23.054 62.390  128.648 1.00 44.48 ? 634  GLU   A CD    1 
ATOM   4674  O  OE1   . GLU   A 1  636  ? -23.253 61.156  128.678 1.00 46.12 ? 634  GLU   A OE1   1 
ATOM   4675  O  OE2   . GLU   A 1  636  ? -23.915 63.202  128.236 1.00 39.04 ? 634  GLU   A OE2   1 
ATOM   4676  N  N     . ARG   A 1  637  ? -19.596 63.945  126.006 1.00 25.53 ? 635  ARG   A N     1 
ATOM   4677  C  CA    . ARG   A 1  637  ? -19.692 65.141  125.175 1.00 23.59 ? 635  ARG   A CA    1 
ATOM   4678  C  C     . ARG   A 1  637  ? -20.294 64.802  123.820 1.00 23.37 ? 635  ARG   A C     1 
ATOM   4679  O  O     . ARG   A 1  637  ? -21.162 65.524  123.317 1.00 24.00 ? 635  ARG   A O     1 
ATOM   4680  C  CB    . ARG   A 1  637  ? -18.318 65.791  125.009 1.00 24.33 ? 635  ARG   A CB    1 
ATOM   4681  C  CG    . ARG   A 1  637  ? -17.675 66.127  126.344 1.00 25.14 ? 635  ARG   A CG    1 
ATOM   4682  C  CD    . ARG   A 1  637  ? -16.529 67.111  126.212 1.00 25.81 ? 635  ARG   A CD    1 
ATOM   4683  N  NE    . ARG   A 1  637  ? -15.465 66.624  125.348 1.00 26.63 ? 635  ARG   A NE    1 
ATOM   4684  C  CZ    . ARG   A 1  637  ? -14.275 66.203  125.758 1.00 25.65 ? 635  ARG   A CZ    1 
ATOM   4685  N  NH1   . ARG   A 1  637  ? -13.971 66.115  127.044 1.00 28.14 ? 635  ARG   A NH1   1 
ATOM   4686  N  NH2   . ARG   A 1  637  ? -13.361 65.877  124.853 1.00 25.69 ? 635  ARG   A NH2   1 
ATOM   4687  N  N     . ALA   A 1  638  ? -19.850 63.694  123.224 1.00 23.23 ? 636  ALA   A N     1 
ATOM   4688  C  CA    . ALA   A 1  638  ? -20.402 63.259  121.947 1.00 22.27 ? 636  ALA   A CA    1 
ATOM   4689  C  C     . ALA   A 1  638  ? -21.878 62.908  122.079 1.00 23.10 ? 636  ALA   A C     1 
ATOM   4690  O  O     . ALA   A 1  638  ? -22.666 63.143  121.157 1.00 22.33 ? 636  ALA   A O     1 
ATOM   4691  C  CB    . ALA   A 1  638  ? -19.617 62.052  121.434 1.00 22.88 ? 636  ALA   A CB    1 
ATOM   4692  N  N     . ALA   A 1  639  ? -22.268 62.340  123.221 1.00 22.98 ? 637  ALA   A N     1 
ATOM   4693  C  CA    . ALA   A 1  639  ? -23.678 62.039  123.445 1.00 23.30 ? 637  ALA   A CA    1 
ATOM   4694  C  C     . ALA   A 1  639  ? -24.522 63.310  123.442 1.00 24.62 ? 637  ALA   A C     1 
ATOM   4695  O  O     . ALA   A 1  639  ? -25.668 63.304  122.972 1.00 24.94 ? 637  ALA   A O     1 
ATOM   4696  C  CB    . ALA   A 1  639  ? -23.855 61.247  124.740 1.00 26.05 ? 637  ALA   A CB    1 
ATOM   4697  N  N     . CYS   A 1  640  ? -23.976 64.413  123.966 1.00 23.44 ? 638  CYS   A N     1 
ATOM   4698  C  CA    . CYS   A 1  640  ? -24.679 65.693  123.882 1.00 24.19 ? 638  CYS   A CA    1 
ATOM   4699  C  C     . CYS   A 1  640  ? -24.887 66.102  122.435 1.00 24.13 ? 638  CYS   A C     1 
ATOM   4700  O  O     . CYS   A 1  640  ? -25.973 66.558  122.060 1.00 23.54 ? 638  CYS   A O     1 
ATOM   4701  C  CB    . CYS   A 1  640  ? -23.887 66.792  124.584 1.00 24.74 ? 638  CYS   A CB    1 
ATOM   4702  S  SG    . CYS   A 1  640  ? -23.764 66.656  126.360 1.00 27.51 ? 638  CYS   A SG    1 
ATOM   4703  N  N     . LEU   A 1  641  ? -23.852 65.952  121.608 1.00 22.20 ? 639  LEU   A N     1 
ATOM   4704  C  CA    . LEU   A 1  641  ? -23.998 66.294  120.201 1.00 22.03 ? 639  LEU   A CA    1 
ATOM   4705  C  C     . LEU   A 1  641  ? -25.064 65.433  119.546 1.00 21.86 ? 639  LEU   A C     1 
ATOM   4706  O  O     . LEU   A 1  641  ? -25.891 65.934  118.774 1.00 21.44 ? 639  LEU   A O     1 
ATOM   4707  C  CB    . LEU   A 1  641  ? -22.661 66.130  119.482 1.00 22.16 ? 639  LEU   A CB    1 
ATOM   4708  C  CG    . LEU   A 1  641  ? -21.733 67.346  119.450 1.00 23.27 ? 639  LEU   A CG    1 
ATOM   4709  C  CD1   . LEU   A 1  641  ? -21.325 67.813  120.837 1.00 25.93 ? 639  LEU   A CD1   1 
ATOM   4710  C  CD2   . LEU   A 1  641  ? -20.503 67.023  118.611 1.00 20.85 ? 639  LEU   A CD2   1 
ATOM   4711  N  N     . ASP   A 1  642  ? -25.058 64.131  119.834 1.00 21.37 ? 640  ASP   A N     1 
ATOM   4712  C  CA    . ASP   A 1  642  ? -26.054 63.251  119.236 1.00 23.12 ? 640  ASP   A CA    1 
ATOM   4713  C  C     . ASP   A 1  642  ? -27.462 63.615  119.694 1.00 22.94 ? 640  ASP   A C     1 
ATOM   4714  O  O     . ASP   A 1  642  ? -28.409 63.590  118.897 1.00 23.02 ? 640  ASP   A O     1 
ATOM   4715  C  CB    . ASP   A 1  642  ? -25.737 61.789  119.548 1.00 23.19 ? 640  ASP   A CB    1 
ATOM   4716  C  CG    . ASP   A 1  642  ? -24.645 61.220  118.650 1.00 24.11 ? 640  ASP   A CG    1 
ATOM   4717  O  OD1   . ASP   A 1  642  ? -24.410 61.775  117.555 1.00 25.62 ? 640  ASP   A OD1   1 
ATOM   4718  O  OD2   . ASP   A 1  642  ? -24.049 60.201  119.040 1.00 25.70 ? 640  ASP   A OD2   1 
ATOM   4719  N  N     . ARG   A 1  643  ? -27.625 63.955  120.977 1.00 23.09 ? 641  ARG   A N     1 
ATOM   4720  C  CA    . ARG   A 1  643  ? -28.937 64.399  121.445 1.00 21.92 ? 641  ARG   A CA    1 
ATOM   4721  C  C     . ARG   A 1  643  ? -29.352 65.690  120.753 1.00 25.22 ? 641  ARG   A C     1 
ATOM   4722  O  O     . ARG   A 1  643  ? -30.523 65.863  120.399 1.00 25.67 ? 641  ARG   A O     1 
ATOM   4723  C  CB    . ARG   A 1  643  ? -28.947 64.584  122.963 1.00 25.72 ? 641  ARG   A CB    1 
ATOM   4724  C  CG    . ARG   A 1  643  ? -29.066 63.283  123.726 1.00 25.56 ? 641  ARG   A CG    1 
ATOM   4725  C  CD    . ARG   A 1  643  ? -29.250 63.520  125.220 1.00 26.44 ? 641  ARG   A CD    1 
ATOM   4726  N  NE    . ARG   A 1  643  ? -28.137 64.246  125.814 1.00 27.86 ? 641  ARG   A NE    1 
ATOM   4727  C  CZ    . ARG   A 1  643  ? -27.103 63.662  126.405 1.00 27.86 ? 641  ARG   A CZ    1 
ATOM   4728  N  NH1   . ARG   A 1  643  ? -26.984 62.346  126.437 1.00 30.82 ? 641  ARG   A NH1   1 
ATOM   4729  N  NH2   . ARG   A 1  643  ? -26.173 64.417  126.986 1.00 31.11 ? 641  ARG   A NH2   1 
ATOM   4730  N  N     . ALA   A 1  644  ? -28.408 66.613  120.555 1.00 20.88 ? 642  ALA   A N     1 
ATOM   4731  C  CA    . ALA   A 1  644  ? -28.741 67.842  119.847 1.00 21.89 ? 642  ALA   A CA    1 
ATOM   4732  C  C     . ALA   A 1  644  ? -29.165 67.551  118.414 1.00 20.56 ? 642  ALA   A C     1 
ATOM   4733  O  O     . ALA   A 1  644  ? -30.076 68.200  117.888 1.00 23.05 ? 642  ALA   A O     1 
ATOM   4734  C  CB    . ALA   A 1  644  ? -27.576 68.829  119.883 1.00 23.64 ? 642  ALA   A CB    1 
ATOM   4735  N  N     . ALA   A 1  645  ? -28.517 66.579  117.761 1.00 20.71 ? 643  ALA   A N     1 
ATOM   4736  C  CA    . ALA   A 1  645  ? -28.905 66.201  116.406 1.00 21.59 ? 643  ALA   A CA    1 
ATOM   4737  C  C     . ALA   A 1  645  ? -30.334 65.672  116.371 1.00 24.14 ? 643  ALA   A C     1 
ATOM   4738  O  O     . ALA   A 1  645  ? -31.118 66.026  115.483 1.00 23.16 ? 643  ALA   A O     1 
ATOM   4739  C  CB    . ALA   A 1  645  ? -27.919 65.164  115.864 1.00 21.58 ? 643  ALA   A CB    1 
ATOM   4740  N  N     . GLU   A 1  646  ? -30.682 64.802  117.315 1.00 22.73 ? 644  GLU   A N     1 
ATOM   4741  C  CA    . GLU   A 1  646  ? -32.053 64.311  117.391 1.00 24.01 ? 644  GLU   A CA    1 
ATOM   4742  C  C     . GLU   A 1  646  ? -33.031 65.457  117.593 1.00 26.03 ? 644  GLU   A C     1 
ATOM   4743  O  O     . GLU   A 1  646  ? -34.108 65.481  116.983 1.00 24.29 ? 644  GLU   A O     1 
ATOM   4744  C  CB    . GLU   A 1  646  ? -32.193 63.315  118.538 1.00 28.30 ? 644  GLU   A CB    1 
ATOM   4745  C  CG    . GLU   A 1  646  ? -31.477 62.002  118.341 1.00 37.68 ? 644  GLU   A CG    1 
ATOM   4746  C  CD    . GLU   A 1  646  ? -32.039 61.198  117.185 1.00 47.81 ? 644  GLU   A CD    1 
ATOM   4747  O  OE1   . GLU   A 1  646  ? -33.233 61.370  116.862 1.00 49.08 ? 644  GLU   A OE1   1 
ATOM   4748  O  OE2   . GLU   A 1  646  ? -31.280 60.397  116.596 1.00 45.52 ? 644  GLU   A OE2   1 
ATOM   4749  N  N     . LEU   A 1  647  ? -32.674 66.417  118.448 1.00 23.12 ? 645  LEU   A N     1 
ATOM   4750  C  CA    . LEU   A 1  647  ? -33.570 67.542  118.696 1.00 22.07 ? 645  LEU   A CA    1 
ATOM   4751  C  C     . LEU   A 1  647  ? -33.718 68.408  117.453 1.00 27.64 ? 645  LEU   A C     1 
ATOM   4752  O  O     . LEU   A 1  647  ? -34.820 68.863  117.138 1.00 25.64 ? 645  LEU   A O     1 
ATOM   4753  C  CB    . LEU   A 1  647  ? -33.074 68.373  119.877 1.00 25.96 ? 645  LEU   A CB    1 
ATOM   4754  C  CG    . LEU   A 1  647  ? -33.138 67.717  121.251 1.00 24.98 ? 645  LEU   A CG    1 
ATOM   4755  C  CD1   . LEU   A 1  647  ? -32.431 68.582  122.284 1.00 26.37 ? 645  LEU   A CD1   1 
ATOM   4756  C  CD2   . LEU   A 1  647  ? -34.584 67.461  121.670 1.00 31.20 ? 645  LEU   A CD2   1 
ATOM   4757  N  N     . MET   A 1  648  ? -32.623 68.648  116.732 1.00 23.06 ? 646  MET   A N     1 
ATOM   4758  C  CA    . MET   A 1  648  ? -32.735 69.425  115.504 1.00 23.15 ? 646  MET   A CA    1 
ATOM   4759  C  C     . MET   A 1  648  ? -33.555 68.690  114.464 1.00 22.78 ? 646  MET   A C     1 
ATOM   4760  O  O     . MET   A 1  648  ? -34.342 69.309  113.744 1.00 24.57 ? 646  MET   A O     1 
ATOM   4761  C  CB    . MET   A 1  648  ? -31.357 69.761  114.949 1.00 21.78 ? 646  MET   A CB    1 
ATOM   4762  C  CG    . MET   A 1  648  ? -30.694 70.850  115.719 1.00 24.37 ? 646  MET   A CG    1 
ATOM   4763  S  SD    . MET   A 1  648  ? -29.291 71.463  114.802 1.00 26.74 ? 646  MET   A SD    1 
ATOM   4764  C  CE    . MET   A 1  648  ? -28.606 72.574  116.024 1.00 28.66 ? 646  MET   A CE    1 
ATOM   4765  N  N     . GLN   A 1  649  ? -33.379 67.371  114.362 1.00 23.71 ? 647  GLN   A N     1 
ATOM   4766  C  CA    . GLN   A 1  649  ? -34.162 66.605  113.400 1.00 23.26 ? 647  GLN   A CA    1 
ATOM   4767  C  C     . GLN   A 1  649  ? -35.652 66.705  113.705 1.00 23.10 ? 647  GLN   A C     1 
ATOM   4768  O  O     . GLN   A 1  649  ? -36.468 66.893  112.794 1.00 25.64 ? 647  GLN   A O     1 
ATOM   4769  C  CB    . GLN   A 1  649  ? -33.720 65.143  113.401 1.00 25.01 ? 647  GLN   A CB    1 
ATOM   4770  C  CG    . GLN   A 1  649  ? -34.433 64.303  112.366 1.00 24.01 ? 647  GLN   A CG    1 
ATOM   4771  C  CD    . GLN   A 1  649  ? -33.900 64.554  110.975 1.00 22.86 ? 647  GLN   A CD    1 
ATOM   4772  O  OE1   . GLN   A 1  649  ? -32.807 64.118  110.641 1.00 21.60 ? 647  GLN   A OE1   1 
ATOM   4773  N  NE2   . GLN   A 1  649  ? -34.654 65.278  110.169 1.00 25.54 ? 647  GLN   A NE2   1 
ATOM   4774  N  N     . ALA   A 1  650  ? -36.020 66.586  114.983 1.00 23.69 ? 648  ALA   A N     1 
ATOM   4775  C  CA    . ALA   A 1  650  ? -37.426 66.654  115.369 1.00 26.81 ? 648  ALA   A CA    1 
ATOM   4776  C  C     . ALA   A 1  650  ? -37.995 68.044  115.140 1.00 30.12 ? 648  ALA   A C     1 
ATOM   4777  O  O     . ALA   A 1  650  ? -39.179 68.186  114.808 1.00 29.93 ? 648  ALA   A O     1 
ATOM   4778  C  CB    . ALA   A 1  650  ? -37.579 66.265  116.840 1.00 28.65 ? 648  ALA   A CB    1 
ATOM   4779  N  N     . ARG   A 1  651  ? -37.173 69.071  115.314 1.00 24.46 ? 649  ARG   A N     1 
ATOM   4780  C  CA    . ARG   A 1  651  ? -37.595 70.459  115.212 1.00 24.52 ? 649  ARG   A CA    1 
ATOM   4781  C  C     . ARG   A 1  651  ? -37.383 71.029  113.816 1.00 24.55 ? 649  ARG   A C     1 
ATOM   4782  O  O     . ARG   A 1  651  ? -37.611 72.223  113.605 1.00 25.52 ? 649  ARG   A O     1 
ATOM   4783  C  CB    . ARG   A 1  651  ? -36.858 71.302  116.260 1.00 27.90 ? 649  ARG   A CB    1 
ATOM   4784  C  CG    . ARG   A 1  651  ? -37.454 72.685  116.528 1.00 29.74 ? 649  ARG   A CG    1 
ATOM   4785  C  CD    . ARG   A 1  651  ? -37.203 73.157  117.960 1.00 30.71 ? 649  ARG   A CD    1 
ATOM   4786  N  NE    . ARG   A 1  651  ? -37.702 74.509  118.195 1.00 36.74 ? 649  ARG   A NE    1 
ATOM   4787  C  CZ    . ARG   A 1  651  ? -38.974 74.812  118.421 1.00 36.76 ? 649  ARG   A CZ    1 
ATOM   4788  N  NH1   . ARG   A 1  651  ? -39.926 73.893  118.361 1.00 36.53 ? 649  ARG   A NH1   1 
ATOM   4789  N  NH2   . ARG   A 1  651  ? -39.300 76.070  118.707 1.00 39.86 ? 649  ARG   A NH2   1 
ATOM   4790  N  N     . MET   A 1  652  ? -36.951 70.204  112.863 1.00 24.65 ? 650  MET   A N     1 
ATOM   4791  C  CA    . MET   A 1  652  ? -36.631 70.708  111.528 1.00 25.31 ? 650  MET   A CA    1 
ATOM   4792  C  C     . MET   A 1  652  ? -37.702 71.610  110.936 1.00 23.04 ? 650  MET   A C     1 
ATOM   4793  O  O     . MET   A 1  652  ? -37.354 72.696  110.451 1.00 24.40 ? 650  MET   A O     1 
ATOM   4794  C  CB    . MET   A 1  652  ? -36.253 69.568  110.575 1.00 25.02 ? 650  MET   A CB    1 
ATOM   4795  C  CG    . MET   A 1  652  ? -36.072 70.038  109.150 1.00 23.93 ? 650  MET   A CG    1 
ATOM   4796  S  SD    . MET   A 1  652  ? -35.597 68.698  108.032 1.00 26.10 ? 650  MET   A SD    1 
ATOM   4797  C  CE    . MET   A 1  652  ? -33.886 68.473  108.483 1.00 24.34 ? 650  MET   A CE    1 
ATOM   4798  N  N     . PRO   A 1  653  ? -38.990 71.256  110.947 1.00 24.97 ? 651  PRO   A N     1 
ATOM   4799  C  CA    . PRO   A 1  653  ? -39.968 72.143  110.292 1.00 27.33 ? 651  PRO   A CA    1 
ATOM   4800  C  C     . PRO   A 1  653  ? -39.989 73.542  110.873 1.00 25.87 ? 651  PRO   A C     1 
ATOM   4801  O  O     . PRO   A 1  653  ? -40.043 74.525  110.120 1.00 24.48 ? 651  PRO   A O     1 
ATOM   4802  C  CB    . PRO   A 1  653  ? -41.296 71.403  110.488 1.00 23.48 ? 651  PRO   A CB    1 
ATOM   4803  C  CG    . PRO   A 1  653  ? -40.895 69.963  110.554 1.00 27.77 ? 651  PRO   A CG    1 
ATOM   4804  C  CD    . PRO   A 1  653  ? -39.602 69.977  111.347 1.00 26.04 ? 651  PRO   A CD    1 
ATOM   4805  N  N     . THR   A 1  654  ? -39.921 73.656  112.199 1.00 22.78 ? 652  THR   A N     1 
ATOM   4806  C  CA    . THR   A 1  654  ? -39.871 74.971  112.823 1.00 24.19 ? 652  THR   A CA    1 
ATOM   4807  C  C     . THR   A 1  654  ? -38.573 75.686  112.483 1.00 25.05 ? 652  THR   A C     1 
ATOM   4808  O  O     . THR   A 1  654  ? -38.578 76.887  112.185 1.00 25.88 ? 652  THR   A O     1 
ATOM   4809  C  CB    . THR   A 1  654  ? -40.044 74.833  114.336 1.00 26.15 ? 652  THR   A CB    1 
ATOM   4810  O  OG1   . THR   A 1  654  ? -41.307 74.218  114.610 1.00 28.65 ? 652  THR   A OG1   1 
ATOM   4811  C  CG2   . THR   A 1  654  ? -39.984 76.195  115.006 1.00 30.00 ? 652  THR   A CG2   1 
ATOM   4812  N  N     . LEU   A 1  655  ? -37.452 74.958  112.496 1.00 23.41 ? 653  LEU   A N     1 
ATOM   4813  C  CA    . LEU   A 1  655  ? -36.181 75.558  112.109 1.00 21.67 ? 653  LEU   A CA    1 
ATOM   4814  C  C     . LEU   A 1  655  ? -36.205 76.045  110.663 1.00 24.91 ? 653  LEU   A C     1 
ATOM   4815  O  O     . LEU   A 1  655  ? -35.633 77.096  110.353 1.00 24.95 ? 653  LEU   A O     1 
ATOM   4816  C  CB    . LEU   A 1  655  ? -35.047 74.553  112.312 1.00 24.03 ? 653  LEU   A CB    1 
ATOM   4817  C  CG    . LEU   A 1  655  ? -34.862 74.051  113.743 1.00 23.56 ? 653  LEU   A CG    1 
ATOM   4818  C  CD1   . LEU   A 1  655  ? -33.725 73.042  113.821 1.00 24.04 ? 653  LEU   A CD1   1 
ATOM   4819  C  CD2   . LEU   A 1  655  ? -34.596 75.215  114.656 1.00 28.89 ? 653  LEU   A CD2   1 
ATOM   4820  N  N     . LEU   A 1  656  ? -36.848 75.288  109.765 1.00 26.18 ? 654  LEU   A N     1 
ATOM   4821  C  CA    . LEU   A 1  656  ? -36.984 75.728  108.378 1.00 23.53 ? 654  LEU   A CA    1 
ATOM   4822  C  C     . LEU   A 1  656  ? -37.629 77.096  108.304 1.00 24.73 ? 654  LEU   A C     1 
ATOM   4823  O  O     . LEU   A 1  656  ? -37.159 77.982  107.579 1.00 24.84 ? 654  LEU   A O     1 
ATOM   4824  C  CB    . LEU   A 1  656  ? -37.847 74.749  107.577 1.00 24.12 ? 654  LEU   A CB    1 
ATOM   4825  C  CG    . LEU   A 1  656  ? -37.374 73.309  107.448 1.00 25.92 ? 654  LEU   A CG    1 
ATOM   4826  C  CD1   . LEU   A 1  656  ? -38.230 72.554  106.455 1.00 27.96 ? 654  LEU   A CD1   1 
ATOM   4827  C  CD2   . LEU   A 1  656  ? -35.914 73.281  107.052 1.00 25.62 ? 654  LEU   A CD2   1 
ATOM   4828  N  N     . GLY   A 1  657  ? -38.733 77.273  109.028 1.00 23.79 ? 655  GLY   A N     1 
ATOM   4829  C  CA    . GLY   A 1  657  ? -39.454 78.527  108.950 1.00 26.98 ? 655  GLY   A CA    1 
ATOM   4830  C  C     . GLY   A 1  657  ? -38.610 79.696  109.397 1.00 24.55 ? 655  GLY   A C     1 
ATOM   4831  O  O     . GLY   A 1  657  ? -38.679 80.783  108.821 1.00 26.27 ? 655  GLY   A O     1 
ATOM   4832  N  N     . LEU   A 1  658  ? -37.799 79.492  110.435 1.00 23.03 ? 656  LEU   A N     1 
ATOM   4833  C  CA    . LEU   A 1  658  ? -36.953 80.575  110.907 1.00 23.89 ? 656  LEU   A CA    1 
ATOM   4834  C  C     . LEU   A 1  658  ? -35.875 80.894  109.882 1.00 21.72 ? 656  LEU   A C     1 
ATOM   4835  O  O     . LEU   A 1  658  ? -35.647 82.059  109.544 1.00 23.18 ? 656  LEU   A O     1 
ATOM   4836  C  CB    . LEU   A 1  658  ? -36.345 80.210  112.264 1.00 22.62 ? 656  LEU   A CB    1 
ATOM   4837  C  CG    . LEU   A 1  658  ? -35.478 81.288  112.902 1.00 24.27 ? 656  LEU   A CG    1 
ATOM   4838  C  CD1   . LEU   A 1  658  ? -36.261 82.597  113.007 1.00 24.99 ? 656  LEU   A CD1   1 
ATOM   4839  C  CD2   . LEU   A 1  658  ? -35.004 80.831  114.270 1.00 26.04 ? 656  LEU   A CD2   1 
ATOM   4840  N  N     . ILE   A 1  659  ? -35.210 79.862  109.367 1.00 21.96 ? 657  ILE   A N     1 
ATOM   4841  C  CA    . ILE   A 1  659  ? -34.167 80.071  108.373 1.00 23.41 ? 657  ILE   A CA    1 
ATOM   4842  C  C     . ILE   A 1  659  ? -34.729 80.739  107.126 1.00 23.33 ? 657  ILE   A C     1 
ATOM   4843  O  O     . ILE   A 1  659  ? -34.120 81.662  106.571 1.00 22.36 ? 657  ILE   A O     1 
ATOM   4844  C  CB    . ILE   A 1  659  ? -33.481 78.732  108.062 1.00 22.41 ? 657  ILE   A CB    1 
ATOM   4845  C  CG1   . ILE   A 1  659  ? -32.722 78.264  109.301 1.00 22.50 ? 657  ILE   A CG1   1 
ATOM   4846  C  CG2   . ILE   A 1  659  ? -32.557 78.891  106.890 1.00 23.25 ? 657  ILE   A CG2   1 
ATOM   4847  C  CD1   . ILE   A 1  659  ? -32.382 76.806  109.301 1.00 25.14 ? 657  ILE   A CD1   1 
ATOM   4848  N  N     . ILE   A 1  660  ? -35.906 80.296  106.679 1.00 22.26 ? 658  ILE   A N     1 
ATOM   4849  C  CA    . ILE   A 1  660  ? -36.526 80.878  105.492 1.00 23.55 ? 658  ILE   A CA    1 
ATOM   4850  C  C     . ILE   A 1  660  ? -36.709 82.380  105.665 1.00 23.80 ? 658  ILE   A C     1 
ATOM   4851  O  O     . ILE   A 1  660  ? -36.376 83.171  104.775 1.00 25.03 ? 658  ILE   A O     1 
ATOM   4852  C  CB    . ILE   A 1  660  ? -37.854 80.164  105.187 1.00 21.60 ? 658  ILE   A CB    1 
ATOM   4853  C  CG1   . ILE   A 1  660  ? -37.577 78.788  104.575 1.00 22.60 ? 658  ILE   A CG1   1 
ATOM   4854  C  CG2   . ILE   A 1  660  ? -38.718 81.010  104.267 1.00 24.00 ? 658  ILE   A CG2   1 
ATOM   4855  C  CD1   . ILE   A 1  660  ? -38.796 77.889  104.575 1.00 27.58 ? 658  ILE   A CD1   1 
ATOM   4856  N  N     . ARG   A 1  661  ? -37.216 82.798  106.821 1.00 23.65 ? 659  ARG   A N     1 
ATOM   4857  C  CA    . ARG   A 1  661  ? -37.568 84.198  107.011 1.00 26.19 ? 659  ARG   A CA    1 
ATOM   4858  C  C     . ARG   A 1  661  ? -36.393 85.052  107.452 1.00 26.24 ? 659  ARG   A C     1 
ATOM   4859  O  O     . ARG   A 1  661  ? -36.343 86.239  107.110 1.00 25.75 ? 659  ARG   A O     1 
ATOM   4860  C  CB    . ARG   A 1  661  ? -38.720 84.327  108.011 1.00 27.22 ? 659  ARG   A CB    1 
ATOM   4861  C  CG    . ARG   A 1  661  ? -40.048 83.864  107.435 1.00 24.09 ? 659  ARG   A CG    1 
ATOM   4862  C  CD    . ARG   A 1  661  ? -41.154 83.814  108.469 1.00 26.94 ? 659  ARG   A CD    1 
ATOM   4863  N  NE    . ARG   A 1  661  ? -41.424 85.115  109.064 1.00 26.79 ? 659  ARG   A NE    1 
ATOM   4864  C  CZ    . ARG   A 1  661  ? -41.358 85.373  110.364 1.00 28.36 ? 659  ARG   A CZ    1 
ATOM   4865  N  NH1   . ARG   A 1  661  ? -40.995 84.447  111.237 1.00 29.72 ? 659  ARG   A NH1   1 
ATOM   4866  N  NH2   . ARG   A 1  661  ? -41.683 86.586  110.802 1.00 28.59 ? 659  ARG   A NH2   1 
ATOM   4867  N  N     . GLU   A 1  662  ? -35.451 84.481  108.206 1.00 25.12 ? 660  GLU   A N     1 
ATOM   4868  C  CA    . GLU   A 1  662  ? -34.330 85.275  108.695 1.00 25.53 ? 660  GLU   A CA    1 
ATOM   4869  C  C     . GLU   A 1  662  ? -33.229 85.416  107.648 1.00 23.55 ? 660  GLU   A C     1 
ATOM   4870  O  O     . GLU   A 1  662  ? -32.615 86.479  107.530 1.00 25.91 ? 660  GLU   A O     1 
ATOM   4871  C  CB    . GLU   A 1  662  ? -33.773 84.674  109.991 1.00 26.86 ? 660  GLU   A CB    1 
ATOM   4872  C  CG    . GLU   A 1  662  ? -32.658 85.509  110.603 1.00 25.72 ? 660  GLU   A CG    1 
ATOM   4873  C  CD    . GLU   A 1  662  ? -32.108 84.951  111.909 1.00 26.30 ? 660  GLU   A CD    1 
ATOM   4874  O  OE1   . GLU   A 1  662  ? -32.117 83.713  112.110 1.00 27.49 ? 660  GLU   A OE1   1 
ATOM   4875  O  OE2   . GLU   A 1  662  ? -31.664 85.767  112.737 1.00 26.82 ? 660  GLU   A OE2   1 
ATOM   4876  N  N     . ALA   A 1  663  ? -32.974 84.369  106.870 1.00 22.93 ? 661  ALA   A N     1 
ATOM   4877  C  CA    . ALA   A 1  663  ? -31.772 84.320  106.047 1.00 21.86 ? 661  ALA   A CA    1 
ATOM   4878  C  C     . ALA   A 1  663  ? -32.058 84.308  104.550 1.00 23.32 ? 661  ALA   A C     1 
ATOM   4879  O  O     . ALA   A 1  663  ? -31.133 84.093  103.758 1.00 28.34 ? 661  ALA   A O     1 
ATOM   4880  C  CB    . ALA   A 1  663  ? -30.893 83.128  106.451 1.00 23.65 ? 661  ALA   A CB    1 
ATOM   4881  N  N     . GLY   A 1  664  ? -33.307 84.515  104.141 1.00 25.31 ? 662  GLY   A N     1 
ATOM   4882  C  CA    . GLY   A 1  664  ? -33.619 84.540  102.721 1.00 25.40 ? 662  GLY   A CA    1 
ATOM   4883  C  C     . GLY   A 1  664  ? -33.504 83.211  102.015 1.00 25.97 ? 662  GLY   A C     1 
ATOM   4884  O  O     . GLY   A 1  664  ? -33.265 83.177  100.807 1.00 28.69 ? 662  GLY   A O     1 
ATOM   4885  N  N     . LYS   A 1  665  ? -33.663 82.109  102.733 1.00 24.99 ? 663  LYS   A N     1 
ATOM   4886  C  CA    . LYS   A 1  665  ? -33.490 80.791  102.140 1.00 22.35 ? 663  LYS   A CA    1 
ATOM   4887  C  C     . LYS   A 1  665  ? -34.823 80.241  101.651 1.00 21.37 ? 663  LYS   A C     1 
ATOM   4888  O  O     . LYS   A 1  665  ? -35.869 80.465  102.257 1.00 21.52 ? 663  LYS   A O     1 
ATOM   4889  C  CB    . LYS   A 1  665  ? -32.922 79.818  103.169 1.00 22.91 ? 663  LYS   A CB    1 
ATOM   4890  C  CG    . LYS   A 1  665  ? -31.591 80.235  103.767 1.00 23.79 ? 663  LYS   A CG    1 
ATOM   4891  C  CD    . LYS   A 1  665  ? -30.549 80.469  102.695 1.00 26.10 ? 663  LYS   A CD    1 
ATOM   4892  C  CE    . LYS   A 1  665  ? -29.184 80.726  103.324 1.00 29.55 ? 663  LYS   A CE    1 
ATOM   4893  N  NZ    . LYS   A 1  665  ? -28.159 81.174  102.324 1.00 30.41 ? 663  LYS   A NZ    1 
ATOM   4894  N  N     . SER   A 1  666  ? -34.767 79.503  100.546 1.00 21.90 ? 664  SER   A N     1 
ATOM   4895  C  CA    . SER   A 1  666  ? -35.910 78.711  100.127 1.00 22.95 ? 664  SER   A CA    1 
ATOM   4896  C  C     . SER   A 1  666  ? -36.067 77.506  101.049 1.00 24.30 ? 664  SER   A C     1 
ATOM   4897  O  O     . SER   A 1  666  ? -35.168 77.157  101.821 1.00 24.85 ? 664  SER   A O     1 
ATOM   4898  C  CB    . SER   A 1  666  ? -35.673 78.182  98.719  1.00 23.01 ? 664  SER   A CB    1 
ATOM   4899  O  OG    . SER   A 1  666  ? -34.643 77.209  98.749  1.00 25.97 ? 664  SER   A OG    1 
ATOM   4900  N  N     . ALA   A 1  667  ? -37.228 76.854  100.966 1.00 22.84 ? 665  ALA   A N     1 
ATOM   4901  C  CA    . ALA   A 1  667  ? -37.453 75.671  101.792 1.00 21.75 ? 665  ALA   A CA    1 
ATOM   4902  C  C     . ALA   A 1  667  ? -36.425 74.580  101.505 1.00 23.24 ? 665  ALA   A C     1 
ATOM   4903  O  O     . ALA   A 1  667  ? -35.898 73.962  102.437 1.00 22.00 ? 665  ALA   A O     1 
ATOM   4904  C  CB    . ALA   A 1  667  ? -38.878 75.144  101.609 1.00 25.07 ? 665  ALA   A CB    1 
ATOM   4905  N  N     . LEU   A 1  668  ? -36.143 74.315  100.228 1.00 22.65 ? 666  LEU   A N     1 
ATOM   4906  C  CA    . LEU   A 1  668  ? -35.144 73.309  99.879  1.00 20.39 ? 666  LEU   A CA    1 
ATOM   4907  C  C     . LEU   A 1  668  ? -33.810 73.626  100.526 1.00 24.33 ? 666  LEU   A C     1 
ATOM   4908  O  O     . LEU   A 1  668  ? -33.156 72.737  101.082 1.00 23.60 ? 666  LEU   A O     1 
ATOM   4909  C  CB    . LEU   A 1  668  ? -34.957 73.252  98.364  1.00 25.55 ? 666  LEU   A CB    1 
ATOM   4910  C  CG    . LEU   A 1  668  ? -35.886 72.331  97.596  1.00 38.57 ? 666  LEU   A CG    1 
ATOM   4911  C  CD1   . LEU   A 1  668  ? -35.585 72.455  96.109  1.00 27.96 ? 666  LEU   A CD1   1 
ATOM   4912  C  CD2   . LEU   A 1  668  ? -35.690 70.908  98.095  1.00 36.64 ? 666  LEU   A CD2   1 
ATOM   4913  N  N     . ASN   A 1  669  ? -33.392 74.889  100.466 1.00 21.46 ? 667  ASN   A N     1 
ATOM   4914  C  CA    . ASN   A 1  669  ? -32.094 75.243  101.019 1.00 22.34 ? 667  ASN   A CA    1 
ATOM   4915  C  C     . ASN   A 1  669  ? -32.115 75.241  102.541 1.00 21.92 ? 667  ASN   A C     1 
ATOM   4916  O  O     . ASN   A 1  669  ? -31.107 74.894  103.166 1.00 23.68 ? 667  ASN   A O     1 
ATOM   4917  C  CB    . ASN   A 1  669  ? -31.653 76.594  100.467 1.00 26.43 ? 667  ASN   A CB    1 
ATOM   4918  C  CG    . ASN   A 1  669  ? -31.375 76.541  98.976  1.00 29.89 ? 667  ASN   A CG    1 
ATOM   4919  O  OD1   . ASN   A 1  669  ? -30.916 75.520  98.457  1.00 37.54 ? 667  ASN   A OD1   1 
ATOM   4920  N  ND2   . ASN   A 1  669  ? -31.652 77.632  98.283  1.00 35.00 ? 667  ASN   A ND2   1 
ATOM   4921  N  N     . ALA   A 1  670  ? -33.251 75.576  103.154 1.00 21.34 ? 668  ALA   A N     1 
ATOM   4922  C  CA    . ALA   A 1  670  ? -33.353 75.477  104.604 1.00 22.80 ? 668  ALA   A CA    1 
ATOM   4923  C  C     . ALA   A 1  670  ? -33.299 74.027  105.064 1.00 21.13 ? 668  ALA   A C     1 
ATOM   4924  O  O     . ALA   A 1  670  ? -32.696 73.719  106.100 1.00 21.56 ? 668  ALA   A O     1 
ATOM   4925  C  CB    . ALA   A 1  670  ? -34.641 76.143  105.087 1.00 21.06 ? 668  ALA   A CB    1 
ATOM   4926  N  N     . ILE   A 1  671  ? -33.949 73.126  104.332 1.00 22.43 ? 669  ILE   A N     1 
ATOM   4927  C  CA    . ILE   A 1  671  ? -33.846 71.705  104.656 1.00 20.04 ? 669  ILE   A CA    1 
ATOM   4928  C  C     . ILE   A 1  671  ? -32.390 71.267  104.637 1.00 21.49 ? 669  ILE   A C     1 
ATOM   4929  O  O     . ILE   A 1  671  ? -31.912 70.595  105.560 1.00 22.80 ? 669  ILE   A O     1 
ATOM   4930  C  CB    . ILE   A 1  671  ? -34.683 70.870  103.675 1.00 22.75 ? 669  ILE   A CB    1 
ATOM   4931  C  CG1   . ILE   A 1  671  ? -36.169 71.124  103.910 1.00 20.50 ? 669  ILE   A CG1   1 
ATOM   4932  C  CG2   . ILE   A 1  671  ? -34.324 69.401  103.802 1.00 24.40 ? 669  ILE   A CG2   1 
ATOM   4933  C  CD1   . ILE   A 1  671  ? -37.043 70.585  102.801 1.00 23.51 ? 669  ILE   A CD1   1 
ATOM   4934  N  N     . ALA   A 1  672  ? -31.672 71.633  103.574 1.00 19.78 ? 670  ALA   A N     1 
ATOM   4935  C  CA    . ALA   A 1  672  ? -30.269 71.263  103.461 1.00 20.20 ? 670  ALA   A CA    1 
ATOM   4936  C  C     . ALA   A 1  672  ? -29.460 71.872  104.593 1.00 20.31 ? 670  ALA   A C     1 
ATOM   4937  O  O     . ALA   A 1  672  ? -28.557 71.227  105.133 1.00 20.85 ? 670  ALA   A O     1 
ATOM   4938  C  CB    . ALA   A 1  672  ? -29.729 71.716  102.109 1.00 20.91 ? 670  ALA   A CB    1 
ATOM   4939  N  N     . GLU   A 1  673  ? -29.787 73.107  104.970 1.00 19.67 ? 671  GLU   A N     1 
ATOM   4940  C  CA    . GLU   A 1  673  ? -29.091 73.782  106.060 1.00 20.65 ? 671  GLU   A CA    1 
ATOM   4941  C  C     . GLU   A 1  673  ? -29.248 73.016  107.369 1.00 21.98 ? 671  GLU   A C     1 
ATOM   4942  O  O     . GLU   A 1  673  ? -28.271 72.789  108.095 1.00 21.08 ? 671  GLU   A O     1 
ATOM   4943  C  CB    . GLU   A 1  673  ? -29.661 75.193  106.196 1.00 24.15 ? 671  GLU   A CB    1 
ATOM   4944  C  CG    . GLU   A 1  673  ? -29.061 76.018  107.315 1.00 27.53 ? 671  GLU   A CG    1 
ATOM   4945  C  CD    . GLU   A 1  673  ? -27.737 76.625  106.922 1.00 28.20 ? 671  GLU   A CD    1 
ATOM   4946  O  OE1   . GLU   A 1  673  ? -27.415 76.659  105.712 1.00 29.32 ? 671  GLU   A OE1   1 
ATOM   4947  O  OE2   . GLU   A 1  673  ? -27.010 77.067  107.826 1.00 25.31 ? 671  GLU   A OE2   1 
ATOM   4948  N  N     . VAL   A 1  674  ? -30.476 72.603  107.689 1.00 18.64 ? 672  VAL   A N     1 
ATOM   4949  C  CA    . VAL   A 1  674  ? -30.708 71.881  108.935 1.00 19.27 ? 672  VAL   A CA    1 
ATOM   4950  C  C     . VAL   A 1  674  ? -30.090 70.491  108.872 1.00 19.97 ? 672  VAL   A C     1 
ATOM   4951  O  O     . VAL   A 1  674  ? -29.498 70.017  109.849 1.00 18.79 ? 672  VAL   A O     1 
ATOM   4952  C  CB    . VAL   A 1  674  ? -32.209 71.843  109.271 1.00 20.22 ? 672  VAL   A CB    1 
ATOM   4953  C  CG1   . VAL   A 1  674  ? -32.434 71.085  110.567 1.00 21.26 ? 672  VAL   A CG1   1 
ATOM   4954  C  CG2   . VAL   A 1  674  ? -32.773 73.260  109.371 1.00 20.83 ? 672  VAL   A CG2   1 
ATOM   4955  N  N     . ARG   A 1  675  ? -30.201 69.823  107.721 1.00 19.61 ? 673  ARG   A N     1 
ATOM   4956  C  CA    . ARG   A 1  675  ? -29.564 68.523  107.587 1.00 17.94 ? 673  ARG   A CA    1 
ATOM   4957  C  C     . ARG   A 1  675  ? -28.074 68.627  107.827 1.00 18.24 ? 673  ARG   A C     1 
ATOM   4958  O  O     . ARG   A 1  675  ? -27.495 67.767  108.490 1.00 18.51 ? 673  ARG   A O     1 
ATOM   4959  C  CB    . ARG   A 1  675  ? -29.815 67.943  106.202 1.00 18.06 ? 673  ARG   A CB    1 
ATOM   4960  C  CG    . ARG   A 1  675  ? -31.227 67.460  106.011 1.00 18.49 ? 673  ARG   A CG    1 
ATOM   4961  C  CD    . ARG   A 1  675  ? -31.292 66.710  104.699 1.00 20.80 ? 673  ARG   A CD    1 
ATOM   4962  N  NE    . ARG   A 1  675  ? -30.564 65.452  104.791 1.00 19.77 ? 673  ARG   A NE    1 
ATOM   4963  C  CZ    . ARG   A 1  675  ? -30.196 64.719  103.750 1.00 19.38 ? 673  ARG   A CZ    1 
ATOM   4964  N  NH1   . ARG   A 1  675  ? -30.456 65.103  102.509 1.00 19.60 ? 673  ARG   A NH1   1 
ATOM   4965  N  NH2   . ARG   A 1  675  ? -29.561 63.569  103.961 1.00 19.29 ? 673  ARG   A NH2   1 
ATOM   4966  N  N     . GLU   A 1  676  ? -27.439 69.671  107.287 1.00 17.36 ? 674  GLU   A N     1 
ATOM   4967  C  CA    . GLU   A 1  676  ? -25.997 69.802  107.469 1.00 17.72 ? 674  GLU   A CA    1 
ATOM   4968  C  C     . GLU   A 1  676  ? -25.650 69.994  108.937 1.00 18.64 ? 674  GLU   A C     1 
ATOM   4969  O  O     . GLU   A 1  676  ? -24.659 69.443  109.427 1.00 18.80 ? 674  GLU   A O     1 
ATOM   4970  C  CB    . GLU   A 1  676  ? -25.446 70.943  106.620 1.00 19.48 ? 674  GLU   A CB    1 
ATOM   4971  C  CG    . GLU   A 1  676  ? -23.940 71.048  106.726 1.00 22.06 ? 674  GLU   A CG    1 
ATOM   4972  C  CD    . GLU   A 1  676  ? -23.265 71.566  105.478 1.00 37.97 ? 674  GLU   A CD    1 
ATOM   4973  O  OE1   . GLU   A 1  676  ? -23.779 72.523  104.856 1.00 53.36 ? 674  GLU   A OE1   1 
ATOM   4974  O  OE2   . GLU   A 1  676  ? -22.204 71.003  105.124 1.00 37.70 ? 674  GLU   A OE2   1 
ATOM   4975  N  N     . ALA   A 1  677  ? -26.458 70.765  109.661 1.00 18.39 ? 675  ALA   A N     1 
ATOM   4976  C  CA    . ALA   A 1  677  ? -26.204 70.938  111.087 1.00 17.28 ? 675  ALA   A CA    1 
ATOM   4977  C  C     . ALA   A 1  677  ? -26.303 69.605  111.811 1.00 19.71 ? 675  ALA   A C     1 
ATOM   4978  O  O     . ALA   A 1  677  ? -25.444 69.268  112.634 1.00 19.21 ? 675  ALA   A O     1 
ATOM   4979  C  CB    . ALA   A 1  677  ? -27.185 71.957  111.676 1.00 17.99 ? 675  ALA   A CB    1 
ATOM   4980  N  N     . ILE   A 1  678  ? -27.354 68.835  111.517 1.00 18.96 ? 676  ILE   A N     1 
ATOM   4981  C  CA    . ILE   A 1  678  ? -27.511 67.510  112.105 1.00 19.58 ? 676  ILE   A CA    1 
ATOM   4982  C  C     . ILE   A 1  678  ? -26.309 66.642  111.782 1.00 19.85 ? 676  ILE   A C     1 
ATOM   4983  O  O     . ILE   A 1  678  ? -25.778 65.937  112.654 1.00 19.60 ? 676  ILE   A O     1 
ATOM   4984  C  CB    . ILE   A 1  678  ? -28.815 66.881  111.584 1.00 17.86 ? 676  ILE   A CB    1 
ATOM   4985  C  CG1   . ILE   A 1  678  ? -30.023 67.668  112.089 1.00 21.58 ? 676  ILE   A CG1   1 
ATOM   4986  C  CG2   . ILE   A 1  678  ? -28.915 65.412  111.945 1.00 21.24 ? 676  ILE   A CG2   1 
ATOM   4987  C  CD1   . ILE   A 1  678  ? -31.332 67.305  111.384 1.00 20.76 ? 676  ILE   A CD1   1 
ATOM   4988  N  N     . ASP   A 1  679  ? -25.864 66.683  110.523 1.00 17.76 ? 677  ASP   A N     1 
ATOM   4989  C  CA    . ASP   A 1  679  ? -24.740 65.855  110.099 1.00 17.09 ? 677  ASP   A CA    1 
ATOM   4990  C  C     . ASP   A 1  679  ? -23.444 66.263  110.785 1.00 18.81 ? 677  ASP   A C     1 
ATOM   4991  O  O     . ASP   A 1  679  ? -22.664 65.394  111.186 1.00 18.43 ? 677  ASP   A O     1 
ATOM   4992  C  CB    . ASP   A 1  679  ? -24.573 65.935  108.586 1.00 18.27 ? 677  ASP   A CB    1 
ATOM   4993  C  CG    . ASP   A 1  679  ? -25.724 65.301  107.843 1.00 22.61 ? 677  ASP   A CG    1 
ATOM   4994  O  OD1   . ASP   A 1  679  ? -26.351 64.380  108.385 1.00 22.89 ? 677  ASP   A OD1   1 
ATOM   4995  O  OD2   . ASP   A 1  679  ? -25.970 65.693  106.687 1.00 23.82 ? 677  ASP   A OD2   1 
ATOM   4996  N  N     . PHE   A 1  680  ? -23.188 67.569  110.921 1.00 17.91 ? 678  PHE   A N     1 
ATOM   4997  C  CA    . PHE   A 1  680  ? -22.034 68.016  111.704 1.00 19.59 ? 678  PHE   A CA    1 
ATOM   4998  C  C     . PHE   A 1  680  ? -22.065 67.441  113.110 1.00 19.29 ? 678  PHE   A C     1 
ATOM   4999  O  O     . PHE   A 1  680  ? -21.062 66.917  113.608 1.00 18.99 ? 678  PHE   A O     1 
ATOM   5000  C  CB    . PHE   A 1  680  ? -22.003 69.542  111.798 1.00 19.34 ? 678  PHE   A CB    1 
ATOM   5001  C  CG    . PHE   A 1  680  ? -21.358 70.225  110.632 1.00 17.85 ? 678  PHE   A CG    1 
ATOM   5002  C  CD1   . PHE   A 1  680  ? -20.134 69.798  110.147 1.00 17.69 ? 678  PHE   A CD1   1 
ATOM   5003  C  CD2   . PHE   A 1  680  ? -21.978 71.311  110.032 1.00 19.18 ? 678  PHE   A CD2   1 
ATOM   5004  C  CE1   . PHE   A 1  680  ? -19.534 70.442  109.091 1.00 19.18 ? 678  PHE   A CE1   1 
ATOM   5005  C  CE2   . PHE   A 1  680  ? -21.393 71.954  108.970 1.00 18.87 ? 678  PHE   A CE2   1 
ATOM   5006  C  CZ    . PHE   A 1  680  ? -20.168 71.521  108.486 1.00 19.33 ? 678  PHE   A CZ    1 
ATOM   5007  N  N     . LEU   A 1  681  ? -23.205 67.566  113.783 1.00 18.08 ? 679  LEU   A N     1 
ATOM   5008  C  CA    . LEU   A 1  681  ? -23.297 67.079  115.153 1.00 17.46 ? 679  LEU   A CA    1 
ATOM   5009  C  C     . LEU   A 1  681  ? -22.982 65.592  115.213 1.00 20.06 ? 679  LEU   A C     1 
ATOM   5010  O  O     . LEU   A 1  681  ? -22.183 65.143  116.045 1.00 19.35 ? 679  LEU   A O     1 
ATOM   5011  C  CB    . LEU   A 1  681  ? -24.695 67.367  115.709 1.00 20.53 ? 679  LEU   A CB    1 
ATOM   5012  C  CG    . LEU   A 1  681  ? -24.989 68.845  115.946 1.00 22.51 ? 679  LEU   A CG    1 
ATOM   5013  C  CD1   . LEU   A 1  681  ? -26.490 69.102  115.966 1.00 21.04 ? 679  LEU   A CD1   1 
ATOM   5014  C  CD2   . LEU   A 1  681  ? -24.366 69.314  117.255 1.00 21.36 ? 679  LEU   A CD2   1 
ATOM   5015  N  N     . ARG   A 1  682  ? -23.575 64.811  114.316 1.00 18.45 ? 680  ARG   A N     1 
ATOM   5016  C  CA    . ARG   A 1  682  ? -23.380 63.373  114.385 1.00 18.58 ? 680  ARG   A CA    1 
ATOM   5017  C  C     . ARG   A 1  682  ? -21.991 62.978  113.912 1.00 19.51 ? 680  ARG   A C     1 
ATOM   5018  O  O     . ARG   A 1  682  ? -21.410 62.027  114.441 1.00 19.41 ? 680  ARG   A O     1 
ATOM   5019  C  CB    . ARG   A 1  682  ? -24.459 62.671  113.570 1.00 17.31 ? 680  ARG   A CB    1 
ATOM   5020  C  CG    . ARG   A 1  682  ? -25.815 62.810  114.194 1.00 18.88 ? 680  ARG   A CG    1 
ATOM   5021  C  CD    . ARG   A 1  682  ? -26.854 62.147  113.334 1.00 19.86 ? 680  ARG   A CD    1 
ATOM   5022  N  NE    . ARG   A 1  682  ? -28.135 62.142  114.018 1.00 21.83 ? 680  ARG   A NE    1 
ATOM   5023  C  CZ    . ARG   A 1  682  ? -29.293 61.954  113.404 1.00 21.18 ? 680  ARG   A CZ    1 
ATOM   5024  N  NH1   . ARG   A 1  682  ? -29.354 61.741  112.101 1.00 22.35 ? 680  ARG   A NH1   1 
ATOM   5025  N  NH2   . ARG   A 1  682  ? -30.415 61.979  114.120 1.00 24.40 ? 680  ARG   A NH2   1 
ATOM   5026  N  N     . TYR   A 1  683  ? -21.444 63.703  112.936 1.00 18.52 ? 681  TYR   A N     1 
ATOM   5027  C  CA    . TYR   A 1  683  ? -20.112 63.376  112.445 1.00 16.77 ? 681  TYR   A CA    1 
ATOM   5028  C  C     . TYR   A 1  683  ? -19.049 63.683  113.491 1.00 21.19 ? 681  TYR   A C     1 
ATOM   5029  O  O     . TYR   A 1  683  ? -18.186 62.845  113.772 1.00 19.39 ? 681  TYR   A O     1 
ATOM   5030  C  CB    . TYR   A 1  683  ? -19.851 64.142  111.156 1.00 18.99 ? 681  TYR   A CB    1 
ATOM   5031  C  CG    . TYR   A 1  683  ? -18.459 63.935  110.621 1.00 19.74 ? 681  TYR   A CG    1 
ATOM   5032  C  CD1   . TYR   A 1  683  ? -18.133 62.776  109.937 1.00 19.05 ? 681  TYR   A CD1   1 
ATOM   5033  C  CD2   . TYR   A 1  683  ? -17.470 64.895  110.809 1.00 19.01 ? 681  TYR   A CD2   1 
ATOM   5034  C  CE1   . TYR   A 1  683  ? -16.856 62.574  109.442 1.00 18.17 ? 681  TYR   A CE1   1 
ATOM   5035  C  CE2   . TYR   A 1  683  ? -16.186 64.702  110.326 1.00 19.89 ? 681  TYR   A CE2   1 
ATOM   5036  C  CZ    . TYR   A 1  683  ? -15.892 63.541  109.649 1.00 19.58 ? 681  TYR   A CZ    1 
ATOM   5037  O  OH    . TYR   A 1  683  ? -14.624 63.338  109.158 1.00 19.80 ? 681  TYR   A OH    1 
ATOM   5038  N  N     . TYR   A 1  684  ? -19.103 64.873  114.097 1.00 19.04 ? 682  TYR   A N     1 
ATOM   5039  C  CA    . TYR   A 1  684  ? -18.093 65.182  115.106 1.00 20.50 ? 682  TYR   A CA    1 
ATOM   5040  C  C     . TYR   A 1  684  ? -18.253 64.308  116.338 1.00 21.12 ? 682  TYR   A C     1 
ATOM   5041  O  O     . TYR   A 1  684  ? -17.256 63.964  116.973 1.00 19.46 ? 682  TYR   A O     1 
ATOM   5042  C  CB    . TYR   A 1  684  ? -18.100 66.661  115.481 1.00 19.14 ? 682  TYR   A CB    1 
ATOM   5043  C  CG    . TYR   A 1  684  ? -17.726 67.564  114.333 1.00 17.03 ? 682  TYR   A CG    1 
ATOM   5044  C  CD1   . TYR   A 1  684  ? -16.674 67.246  113.475 1.00 18.62 ? 682  TYR   A CD1   1 
ATOM   5045  C  CD2   . TYR   A 1  684  ? -18.440 68.727  114.091 1.00 19.05 ? 682  TYR   A CD2   1 
ATOM   5046  C  CE1   . TYR   A 1  684  ? -16.337 68.076  112.417 1.00 20.61 ? 682  TYR   A CE1   1 
ATOM   5047  C  CE2   . TYR   A 1  684  ? -18.110 69.559  113.051 1.00 17.59 ? 682  TYR   A CE2   1 
ATOM   5048  C  CZ    . TYR   A 1  684  ? -17.066 69.231  112.203 1.00 18.97 ? 682  TYR   A CZ    1 
ATOM   5049  O  OH    . TYR   A 1  684  ? -16.747 70.064  111.154 1.00 19.59 ? 682  TYR   A OH    1 
ATOM   5050  N  N     . ALA   A 1  685  ? -19.485 63.920  116.678 1.00 18.90 ? 683  ALA   A N     1 
ATOM   5051  C  CA    . ALA   A 1  685  ? -19.679 62.960  117.754 1.00 19.58 ? 683  ALA   A CA    1 
ATOM   5052  C  C     . ALA   A 1  685  ? -18.995 61.640  117.428 1.00 20.94 ? 683  ALA   A C     1 
ATOM   5053  O  O     . ALA   A 1  685  ? -18.283 61.076  118.266 1.00 21.02 ? 683  ALA   A O     1 
ATOM   5054  C  CB    . ALA   A 1  685  ? -21.176 62.751  118.010 1.00 21.00 ? 683  ALA   A CB    1 
ATOM   5055  N  N     . GLU   A 1  686  ? -19.201 61.131  116.208 1.00 19.97 ? 684  GLU   A N     1 
ATOM   5056  C  CA    . GLU   A 1  686  ? -18.590 59.857  115.849 1.00 21.86 ? 684  GLU   A CA    1 
ATOM   5057  C  C     . GLU   A 1  686  ? -17.075 59.973  115.774 1.00 21.12 ? 684  GLU   A C     1 
ATOM   5058  O  O     . GLU   A 1  686  ? -16.359 59.092  116.261 1.00 20.67 ? 684  GLU   A O     1 
ATOM   5059  C  CB    . GLU   A 1  686  ? -19.162 59.330  114.538 1.00 23.01 ? 684  GLU   A CB    1 
ATOM   5060  C  CG    . GLU   A 1  686  ? -18.465 58.066  114.022 1.00 27.76 ? 684  GLU   A CG    1 
ATOM   5061  C  CD    . GLU   A 1  686  ? -18.555 56.868  114.979 1.00 32.43 ? 684  GLU   A CD    1 
ATOM   5062  O  OE1   . GLU   A 1  686  ? -19.409 56.856  115.905 1.00 31.41 ? 684  GLU   A OE1   1 
ATOM   5063  O  OE2   . GLU   A 1  686  ? -17.764 55.915  114.796 1.00 36.05 ? 684  GLU   A OE2   1 
ATOM   5064  N  N     . GLN   A 1  687  ? -16.566 61.059  115.193 1.00 18.32 ? 685  GLN   A N     1 
ATOM   5065  C  CA    . GLN   A 1  687  ? -15.118 61.228  115.119 1.00 17.39 ? 685  GLN   A CA    1 
ATOM   5066  C  C     . GLN   A 1  687  ? -14.523 61.297  116.516 1.00 18.92 ? 685  GLN   A C     1 
ATOM   5067  O  O     . GLN   A 1  687  ? -13.416 60.798  116.761 1.00 21.70 ? 685  GLN   A O     1 
ATOM   5068  C  CB    . GLN   A 1  687  ? -14.775 62.489  114.333 1.00 18.21 ? 685  GLN   A CB    1 
ATOM   5069  C  CG    . GLN   A 1  687  ? -15.107 62.386  112.849 1.00 17.90 ? 685  GLN   A CG    1 
ATOM   5070  C  CD    . GLN   A 1  687  ? -14.374 61.233  112.196 1.00 21.70 ? 685  GLN   A CD    1 
ATOM   5071  O  OE1   . GLN   A 1  687  ? -13.155 61.159  112.259 1.00 22.71 ? 685  GLN   A OE1   1 
ATOM   5072  N  NE2   . GLN   A 1  687  ? -15.119 60.316  111.590 1.00 25.92 ? 685  GLN   A NE2   1 
ATOM   5073  N  N     . THR   A 1  688  ? -15.245 61.924  117.442 1.00 17.71 ? 686  THR   A N     1 
ATOM   5074  C  CA    . THR   A 1  688  ? -14.797 61.953  118.827 1.00 18.23 ? 686  THR   A CA    1 
ATOM   5075  C  C     . THR   A 1  688  ? -14.710 60.546  119.399 1.00 20.53 ? 686  THR   A C     1 
ATOM   5076  O  O     . THR   A 1  688  ? -13.714 60.181  120.036 1.00 21.78 ? 686  THR   A O     1 
ATOM   5077  C  CB    . THR   A 1  688  ? -15.755 62.809  119.656 1.00 18.90 ? 686  THR   A CB    1 
ATOM   5078  O  OG1   . THR   A 1  688  ? -15.577 64.180  119.294 1.00 20.92 ? 686  THR   A OG1   1 
ATOM   5079  C  CG2   . THR   A 1  688  ? -15.468 62.638  121.149 1.00 21.78 ? 686  THR   A CG2   1 
ATOM   5080  N  N     . ARG   A 1  689  ? -15.747 59.739  119.179 1.00 20.61 ? 687  ARG   A N     1 
ATOM   5081  C  CA    . ARG   A 1  689  ? -15.751 58.380  119.702 1.00 21.63 ? 687  ARG   A CA    1 
ATOM   5082  C  C     . ARG   A 1  689  ? -14.645 57.543  119.089 1.00 22.73 ? 687  ARG   A C     1 
ATOM   5083  O  O     . ARG   A 1  689  ? -14.191 56.574  119.707 1.00 24.40 ? 687  ARG   A O     1 
ATOM   5084  C  CB    . ARG   A 1  689  ? -17.101 57.720  119.457 1.00 22.16 ? 687  ARG   A CB    1 
ATOM   5085  C  CG    . ARG   A 1  689  ? -18.202 58.243  120.373 1.00 23.27 ? 687  ARG   A CG    1 
ATOM   5086  C  CD    . ARG   A 1  689  ? -19.465 57.433  120.173 1.00 27.19 ? 687  ARG   A CD    1 
ATOM   5087  N  NE    . ARG   A 1  689  ? -20.003 57.618  118.835 1.00 26.98 ? 687  ARG   A NE    1 
ATOM   5088  C  CZ    . ARG   A 1  689  ? -21.009 58.433  118.545 1.00 27.59 ? 687  ARG   A CZ    1 
ATOM   5089  N  NH1   . ARG   A 1  689  ? -21.609 59.151  119.481 1.00 29.77 ? 687  ARG   A NH1   1 
ATOM   5090  N  NH2   . ARG   A 1  689  ? -21.429 58.519  117.288 1.00 27.71 ? 687  ARG   A NH2   1 
ATOM   5091  N  N     . ARG   A 1  690  ? -14.201 57.903  117.888 1.00 20.18 ? 688  ARG   A N     1 
ATOM   5092  C  CA    . ARG   A 1  690  ? -13.102 57.190  117.253 1.00 22.16 ? 688  ARG   A CA    1 
ATOM   5093  C  C     . ARG   A 1  690  ? -11.733 57.630  117.749 1.00 23.12 ? 688  ARG   A C     1 
ATOM   5094  O  O     . ARG   A 1  690  ? -10.766 56.881  117.571 1.00 22.65 ? 688  ARG   A O     1 
ATOM   5095  C  CB    . ARG   A 1  690  ? -13.145 57.396  115.738 1.00 21.38 ? 688  ARG   A CB    1 
ATOM   5096  C  CG    . ARG   A 1  690  ? -14.354 56.771  115.059 1.00 24.50 ? 688  ARG   A CG    1 
ATOM   5097  C  CD    . ARG   A 1  690  ? -14.254 55.255  114.970 1.00 25.59 ? 688  ARG   A CD    1 
ATOM   5098  N  NE    . ARG   A 1  690  ? -13.093 54.834  114.190 1.00 24.95 ? 688  ARG   A NE    1 
ATOM   5099  C  CZ    . ARG   A 1  690  ? -12.065 54.168  114.691 1.00 31.54 ? 688  ARG   A CZ    1 
ATOM   5100  N  NH1   . ARG   A 1  690  ? -12.023 53.817  115.968 1.00 26.59 ? 688  ARG   A NH1   1 
ATOM   5101  N  NH2   . ARG   A 1  690  ? -11.055 53.841  113.890 1.00 27.51 ? 688  ARG   A NH2   1 
ATOM   5102  N  N     . THR   A 1  691  ? -11.609 58.822  118.344 1.00 19.47 ? 689  THR   A N     1 
ATOM   5103  C  CA    . THR   A 1  691  ? -10.269 59.378  118.533 1.00 20.33 ? 689  THR   A CA    1 
ATOM   5104  C  C     . THR   A 1  691  ? -9.921  59.858  119.936 1.00 24.08 ? 689  THR   A C     1 
ATOM   5105  O  O     . THR   A 1  691  ? -8.850  59.521  120.445 1.00 28.32 ? 689  THR   A O     1 
ATOM   5106  C  CB    . THR   A 1  691  ? -10.003 60.531  117.559 1.00 20.45 ? 689  THR   A CB    1 
ATOM   5107  O  OG1   . THR   A 1  691  ? -10.975 61.564  117.763 1.00 23.00 ? 689  THR   A OG1   1 
ATOM   5108  C  CG2   . THR   A 1  691  ? -10.053 60.052  116.110 1.00 21.18 ? 689  THR   A CG2   1 
ATOM   5109  N  N     . LEU   A 1  692  ? -10.783 60.647  120.576 1.00 21.86 ? 690  LEU   A N     1 
ATOM   5110  C  CA    . LEU   A 1  692  ? -10.320 61.486  121.677 1.00 23.70 ? 690  LEU   A CA    1 
ATOM   5111  C  C     . LEU   A 1  692  ? -10.107 60.693  122.963 1.00 25.44 ? 690  LEU   A C     1 
ATOM   5112  O  O     . LEU   A 1  692  ? -10.967 59.911  123.380 1.00 26.67 ? 690  LEU   A O     1 
ATOM   5113  C  CB    . LEU   A 1  692  ? -11.280 62.650  121.906 1.00 22.93 ? 690  LEU   A CB    1 
ATOM   5114  C  CG    . LEU   A 1  692  ? -11.298 63.692  120.783 1.00 26.06 ? 690  LEU   A CG    1 
ATOM   5115  C  CD1   . LEU   A 1  692  ? -12.075 64.908  121.232 1.00 26.12 ? 690  LEU   A CD1   1 
ATOM   5116  C  CD2   . LEU   A 1  692  ? -9.893  64.089  120.359 1.00 27.90 ? 690  LEU   A CD2   1 
ATOM   5117  N  N     . GLY   A 1  693  ? -8.950  60.908  123.585 1.00 23.50 ? 691  GLY   A N     1 
ATOM   5118  C  CA    . GLY   A 1  693  ? -8.580  60.261  124.818 1.00 27.82 ? 691  GLY   A CA    1 
ATOM   5119  C  C     . GLY   A 1  693  ? -7.987  61.257  125.794 1.00 26.77 ? 691  GLY   A C     1 
ATOM   5120  O  O     . GLY   A 1  693  ? -7.912  62.458  125.518 1.00 28.38 ? 691  GLY   A O     1 
ATOM   5121  N  N     . PRO   A 1  694  ? -7.528  60.764  126.946 1.00 28.74 ? 692  PRO   A N     1 
ATOM   5122  C  CA    . PRO   A 1  694  ? -7.057  61.677  128.005 1.00 31.76 ? 692  PRO   A CA    1 
ATOM   5123  C  C     . PRO   A 1  694  ? -5.906  62.576  127.583 1.00 34.17 ? 692  PRO   A C     1 
ATOM   5124  O  O     . PRO   A 1  694  ? -5.795  63.703  128.082 1.00 35.82 ? 692  PRO   A O     1 
ATOM   5125  C  CB    . PRO   A 1  694  ? -6.641  60.723  129.133 1.00 35.75 ? 692  PRO   A CB    1 
ATOM   5126  C  CG    . PRO   A 1  694  ? -7.388  59.457  128.864 1.00 30.26 ? 692  PRO   A CG    1 
ATOM   5127  C  CD    . PRO   A 1  694  ? -7.511  59.354  127.372 1.00 30.63 ? 692  PRO   A CD    1 
ATOM   5128  N  N     . GLY   A 1  695  ? -5.049  62.119  126.677 1.00 27.56 ? 693  GLY   A N     1 
ATOM   5129  C  CA    . GLY   A 1  695  ? -3.913  62.901  126.250 1.00 31.81 ? 693  GLY   A CA    1 
ATOM   5130  C  C     . GLY   A 1  695  ? -4.201  63.960  125.220 1.00 33.54 ? 693  GLY   A C     1 
ATOM   5131  O  O     . GLY   A 1  695  ? -3.303  64.726  124.862 1.00 30.40 ? 693  GLY   A O     1 
ATOM   5132  N  N     . HIS   A 1  696  ? -5.433  64.036  124.716 1.00 28.23 ? 694  HIS   A N     1 
ATOM   5133  C  CA    . HIS   A 1  696  ? -5.794  65.052  123.730 1.00 27.70 ? 694  HIS   A CA    1 
ATOM   5134  C  C     . HIS   A 1  696  ? -6.515  66.161  124.487 1.00 28.90 ? 694  HIS   A C     1 
ATOM   5135  O  O     . HIS   A 1  696  ? -7.741  66.262  124.499 1.00 33.18 ? 694  HIS   A O     1 
ATOM   5136  C  CB    . HIS   A 1  696  ? -6.639  64.441  122.613 1.00 27.59 ? 694  HIS   A CB    1 
ATOM   5137  C  CG    . HIS   A 1  696  ? -6.057  63.176  122.060 1.00 24.28 ? 694  HIS   A CG    1 
ATOM   5138  N  ND1   . HIS   A 1  696  ? -6.673  61.950  122.198 1.00 25.78 ? 694  HIS   A ND1   1 
ATOM   5139  C  CD2   . HIS   A 1  696  ? -4.880  62.938  121.433 1.00 25.64 ? 694  HIS   A CD2   1 
ATOM   5140  C  CE1   . HIS   A 1  696  ? -5.919  61.017  121.644 1.00 23.28 ? 694  HIS   A CE1   1 
ATOM   5141  N  NE2   . HIS   A 1  696  ? -4.824  61.590  121.180 1.00 27.21 ? 694  HIS   A NE2   1 
ATOM   5142  N  N     . GLY   A 1  697  ? -5.722  66.989  125.156 1.00 28.74 ? 695  GLY   A N     1 
ATOM   5143  C  CA    . GLY   A 1  697  ? -6.272  68.013  126.010 1.00 28.24 ? 695  GLY   A CA    1 
ATOM   5144  C  C     . GLY   A 1  697  ? -6.869  69.140  125.197 1.00 26.27 ? 695  GLY   A C     1 
ATOM   5145  O  O     . GLY   A 1  697  ? -6.363  69.498  124.130 1.00 26.60 ? 695  GLY   A O     1 
ATOM   5146  N  N     . PRO   A 1  698  ? -7.962  69.719  125.676 1.00 25.99 ? 696  PRO   A N     1 
ATOM   5147  C  CA    . PRO   A 1  698  ? -8.561  70.845  124.958 1.00 26.45 ? 696  PRO   A CA    1 
ATOM   5148  C  C     . PRO   A 1  698  ? -7.634  72.053  124.951 1.00 25.44 ? 696  PRO   A C     1 
ATOM   5149  O  O     . PRO   A 1  698  ? -6.758  72.210  125.804 1.00 27.57 ? 696  PRO   A O     1 
ATOM   5150  C  CB    . PRO   A 1  698  ? -9.845  71.128  125.744 1.00 28.39 ? 696  PRO   A CB    1 
ATOM   5151  C  CG    . PRO   A 1  698  ? -9.609  70.559  127.078 1.00 35.80 ? 696  PRO   A CG    1 
ATOM   5152  C  CD    . PRO   A 1  698  ? -8.726  69.360  126.878 1.00 33.64 ? 696  PRO   A CD    1 
ATOM   5153  N  N     . LEU   A 1  699  ? -7.822  72.907  123.944 1.00 24.45 ? 697  LEU   A N     1 
ATOM   5154  C  CA    . LEU   A 1  699  ? -7.093  74.171  123.911 1.00 24.80 ? 697  LEU   A CA    1 
ATOM   5155  C  C     . LEU   A 1  699  ? -7.508  75.074  125.059 1.00 26.57 ? 697  LEU   A C     1 
ATOM   5156  O  O     . LEU   A 1  699  ? -6.664  75.720  125.692 1.00 27.65 ? 697  LEU   A O     1 
ATOM   5157  C  CB    . LEU   A 1  699  ? -7.344  74.888  122.590 1.00 23.11 ? 697  LEU   A CB    1 
ATOM   5158  C  CG    . LEU   A 1  699  ? -6.779  74.246  121.334 1.00 26.94 ? 697  LEU   A CG    1 
ATOM   5159  C  CD1   . LEU   A 1  699  ? -7.178  75.094  120.131 1.00 23.52 ? 697  LEU   A CD1   1 
ATOM   5160  C  CD2   . LEU   A 1  699  ? -5.261  74.099  121.441 1.00 27.07 ? 697  LEU   A CD2   1 
ATOM   5161  N  N     . GLY   A 1  700  ? -8.804  75.135  125.340 1.00 25.16 ? 698  GLY   A N     1 
ATOM   5162  C  CA    . GLY   A 1  700  ? -9.348  76.106  126.255 1.00 24.37 ? 698  GLY   A CA    1 
ATOM   5163  C  C     . GLY   A 1  700  ? -10.489 76.816  125.568 1.00 27.71 ? 698  GLY   A C     1 
ATOM   5164  O  O     . GLY   A 1  700  ? -11.072 76.296  124.608 1.00 25.91 ? 698  GLY   A O     1 
ATOM   5165  N  N     . PRO   A 1  701  ? -10.824 78.018  126.024 1.00 25.03 ? 699  PRO   A N     1 
ATOM   5166  C  CA    . PRO   A 1  701  ? -11.959 78.735  125.430 1.00 24.85 ? 699  PRO   A CA    1 
ATOM   5167  C  C     . PRO   A 1  701  ? -11.709 78.993  123.954 1.00 23.79 ? 699  PRO   A C     1 
ATOM   5168  O  O     . PRO   A 1  701  ? -10.665 79.520  123.563 1.00 24.42 ? 699  PRO   A O     1 
ATOM   5169  C  CB    . PRO   A 1  701  ? -12.007 80.040  126.230 1.00 27.01 ? 699  PRO   A CB    1 
ATOM   5170  C  CG    . PRO   A 1  701  ? -11.416 79.669  127.562 1.00 29.34 ? 699  PRO   A CG    1 
ATOM   5171  C  CD    . PRO   A 1  701  ? -10.311 78.702  127.224 1.00 27.10 ? 699  PRO   A CD    1 
ATOM   5172  N  N     . ILE   A 1  702  ? -12.664 78.580  123.131 1.00 24.08 ? 700  ILE   A N     1 
ATOM   5173  C  CA    A ILE   A 1  702  ? -12.588 78.773  121.692 0.56 22.35 ? 700  ILE   A CA    1 
ATOM   5174  C  CA    B ILE   A 1  702  ? -12.601 78.754  121.684 0.44 22.37 ? 700  ILE   A CA    1 
ATOM   5175  C  C     . ILE   A 1  702  ? -13.656 79.772  121.282 1.00 22.51 ? 700  ILE   A C     1 
ATOM   5176  O  O     . ILE   A 1  702  ? -14.822 79.650  121.678 1.00 23.07 ? 700  ILE   A O     1 
ATOM   5177  C  CB    A ILE   A 1  702  ? -12.719 77.443  120.933 0.56 21.41 ? 700  ILE   A CB    1 
ATOM   5178  C  CB    B ILE   A 1  702  ? -12.837 77.425  120.947 0.44 21.43 ? 700  ILE   A CB    1 
ATOM   5179  C  CG1   A ILE   A 1  702  ? -11.454 76.611  121.133 0.56 23.01 ? 700  ILE   A CG1   1 
ATOM   5180  C  CG1   B ILE   A 1  702  ? -11.824 76.375  121.389 0.44 22.92 ? 700  ILE   A CG1   1 
ATOM   5181  C  CG2   A ILE   A 1  702  ? -12.970 77.685  119.441 0.56 21.28 ? 700  ILE   A CG2   1 
ATOM   5182  C  CG2   B ILE   A 1  702  ? -12.759 77.624  119.429 0.44 21.30 ? 700  ILE   A CG2   1 
ATOM   5183  C  CD1   A ILE   A 1  702  ? -11.484 75.294  120.431 0.56 21.31 ? 700  ILE   A CD1   1 
ATOM   5184  C  CD1   B ILE   A 1  702  ? -10.409 76.708  121.035 0.44 24.02 ? 700  ILE   A CD1   1 
ATOM   5185  N  N     . VAL   A 1  703  ? -13.252 80.760  120.498 1.00 22.30 ? 701  VAL   A N     1 
ATOM   5186  C  CA    . VAL   A 1  703  ? -14.166 81.749  119.952 1.00 21.95 ? 701  VAL   A CA    1 
ATOM   5187  C  C     . VAL   A 1  703  ? -14.594 81.252  118.583 1.00 20.52 ? 701  VAL   A C     1 
ATOM   5188  O  O     . VAL   A 1  703  ? -13.753 81.024  117.713 1.00 22.49 ? 701  VAL   A O     1 
ATOM   5189  C  CB    . VAL   A 1  703  ? -13.480 83.119  119.868 1.00 23.95 ? 701  VAL   A CB    1 
ATOM   5190  C  CG1   . VAL   A 1  703  ? -14.311 84.092  119.073 1.00 25.22 ? 701  VAL   A CG1   1 
ATOM   5191  C  CG2   . VAL   A 1  703  ? -13.245 83.644  121.283 1.00 24.84 ? 701  VAL   A CG2   1 
ATOM   5192  N  N     . CYS   A 1  704  ? -15.895 81.036  118.408 1.00 20.29 ? 702  CYS   A N     1 
ATOM   5193  C  CA    . CYS   A 1  704  ? -16.451 80.557  117.148 1.00 21.12 ? 702  CYS   A CA    1 
ATOM   5194  C  C     . CYS   A 1  704  ? -17.200 81.708  116.504 1.00 21.52 ? 702  CYS   A C     1 
ATOM   5195  O  O     . CYS   A 1  704  ? -18.207 82.175  117.037 1.00 21.28 ? 702  CYS   A O     1 
ATOM   5196  C  CB    . CYS   A 1  704  ? -17.387 79.368  117.358 1.00 22.34 ? 702  CYS   A CB    1 
ATOM   5197  S  SG    . CYS   A 1  704  ? -16.576 77.938  118.088 1.00 22.46 ? 702  CYS   A SG    1 
ATOM   5198  N  N     . ILE   A 1  705  ? -16.701 82.160  115.363 1.00 19.84 ? 703  ILE   A N     1 
ATOM   5199  C  CA    . ILE   A 1  705  ? -17.268 83.282  114.635 1.00 22.14 ? 703  ILE   A CA    1 
ATOM   5200  C  C     . ILE   A 1  705  ? -17.751 82.743  113.301 1.00 20.46 ? 703  ILE   A C     1 
ATOM   5201  O  O     . ILE   A 1  705  ? -16.988 82.096  112.569 1.00 20.53 ? 703  ILE   A O     1 
ATOM   5202  C  CB    . ILE   A 1  705  ? -16.224 84.397  114.456 1.00 21.31 ? 703  ILE   A CB    1 
ATOM   5203  C  CG1   . ILE   A 1  705  ? -15.861 85.017  115.806 1.00 22.48 ? 703  ILE   A CG1   1 
ATOM   5204  C  CG2   . ILE   A 1  705  ? -16.729 85.462  113.517 1.00 22.20 ? 703  ILE   A CG2   1 
ATOM   5205  C  CD1   . ILE   A 1  705  ? -14.589 85.829  115.736 1.00 24.05 ? 703  ILE   A CD1   1 
ATOM   5206  N  N     . SER   A 1  706  ? -19.017 82.979  113.000 1.00 21.66 ? 704  SER   A N     1 
ATOM   5207  C  CA    . SER   A 1  706  ? -19.668 82.304  111.890 1.00 20.57 ? 704  SER   A CA    1 
ATOM   5208  C  C     . SER   A 1  706  ? -20.287 83.307  110.932 1.00 19.65 ? 704  SER   A C     1 
ATOM   5209  O  O     . SER   A 1  706  ? -20.586 84.445  111.313 1.00 21.75 ? 704  SER   A O     1 
ATOM   5210  C  CB    . SER   A 1  706  ? -20.733 81.324  112.404 1.00 22.42 ? 704  SER   A CB    1 
ATOM   5211  O  OG    . SER   A 1  706  ? -21.613 81.963  113.311 1.00 22.53 ? 704  SER   A OG    1 
ATOM   5212  N  N     . PRO   A 1  707  ? -20.514 82.903  109.687 1.00 19.66 ? 705  PRO   A N     1 
ATOM   5213  C  CA    . PRO   A 1  707  ? -21.067 83.808  108.680 1.00 20.94 ? 705  PRO   A CA    1 
ATOM   5214  C  C     . PRO   A 1  707  ? -22.591 83.751  108.674 1.00 19.78 ? 705  PRO   A C     1 
ATOM   5215  O  O     . PRO   A 1  707  ? -23.212 82.847  109.236 1.00 20.45 ? 705  PRO   A O     1 
ATOM   5216  C  CB    . PRO   A 1  707  ? -20.527 83.195  107.384 1.00 20.17 ? 705  PRO   A CB    1 
ATOM   5217  C  CG    . PRO   A 1  707  ? -20.536 81.747  107.664 1.00 18.56 ? 705  PRO   A CG    1 
ATOM   5218  C  CD    . PRO   A 1  707  ? -20.101 81.619  109.097 1.00 20.47 ? 705  PRO   A CD    1 
ATOM   5219  N  N     . TRP   A 1  708  ? -23.187 84.735  108.010 1.00 20.57 ? 706  TRP   A N     1 
ATOM   5220  C  CA    . TRP   A 1  708  ? -24.644 84.774  107.989 1.00 19.41 ? 706  TRP   A CA    1 
ATOM   5221  C  C     . TRP   A 1  708  ? -25.240 83.736  107.047 1.00 20.65 ? 706  TRP   A C     1 
ATOM   5222  O  O     . TRP   A 1  708  ? -26.386 83.327  107.246 1.00 22.25 ? 706  TRP   A O     1 
ATOM   5223  C  CB    . TRP   A 1  708  ? -25.154 86.179  107.607 1.00 20.50 ? 706  TRP   A CB    1 
ATOM   5224  C  CG    . TRP   A 1  708  ? -25.002 86.443  106.144 1.00 19.94 ? 706  TRP   A CG    1 
ATOM   5225  C  CD1   . TRP   A 1  708  ? -23.970 87.091  105.536 1.00 22.41 ? 706  TRP   A CD1   1 
ATOM   5226  C  CD2   . TRP   A 1  708  ? -25.891 86.027  105.095 1.00 21.58 ? 706  TRP   A CD2   1 
ATOM   5227  N  NE1   . TRP   A 1  708  ? -24.152 87.097  104.174 1.00 22.35 ? 706  TRP   A NE1   1 
ATOM   5228  C  CE2   . TRP   A 1  708  ? -25.322 86.446  103.878 1.00 20.60 ? 706  TRP   A CE2   1 
ATOM   5229  C  CE3   . TRP   A 1  708  ? -27.111 85.339  105.071 1.00 22.38 ? 706  TRP   A CE3   1 
ATOM   5230  C  CZ2   . TRP   A 1  708  ? -25.932 86.210  102.647 1.00 19.98 ? 706  TRP   A CZ2   1 
ATOM   5231  C  CZ3   . TRP   A 1  708  ? -27.708 85.090  103.849 1.00 22.68 ? 706  TRP   A CZ3   1 
ATOM   5232  C  CH2   . TRP   A 1  708  ? -27.120 85.531  102.651 1.00 22.14 ? 706  TRP   A CH2   1 
ATOM   5233  N  N     . ASN   A 1  709  ? -24.487 83.275  106.047 1.00 20.51 ? 707  ASN   A N     1 
ATOM   5234  C  CA    . ASN   A 1  709  ? -25.134 82.660  104.892 1.00 22.09 ? 707  ASN   A CA    1 
ATOM   5235  C  C     . ASN   A 1  709  ? -25.468 81.193  105.095 1.00 22.96 ? 707  ASN   A C     1 
ATOM   5236  O  O     . ASN   A 1  709  ? -26.336 80.669  104.393 1.00 22.75 ? 707  ASN   A O     1 
ATOM   5237  C  CB    . ASN   A 1  709  ? -24.271 82.834  103.653 1.00 20.56 ? 707  ASN   A CB    1 
ATOM   5238  C  CG    . ASN   A 1  709  ? -23.043 81.980  103.700 1.00 23.40 ? 707  ASN   A CG    1 
ATOM   5239  O  OD1   . ASN   A 1  709  ? -22.161 82.200  104.527 1.00 23.89 ? 707  ASN   A OD1   1 
ATOM   5240  N  ND2   . ASN   A 1  709  ? -22.976 80.988  102.822 1.00 23.21 ? 707  ASN   A ND2   1 
ATOM   5241  N  N     . PHE   A 1  710  ? -24.779 80.512  106.002 1.00 22.13 ? 708  PHE   A N     1 
ATOM   5242  C  CA    . PHE   A 1  710  ? -25.164 79.184  106.463 1.00 22.78 ? 708  PHE   A CA    1 
ATOM   5243  C  C     . PHE   A 1  710  ? -25.366 79.344  107.962 1.00 22.36 ? 708  PHE   A C     1 
ATOM   5244  O  O     . PHE   A 1  710  ? -24.546 78.886  108.769 1.00 21.89 ? 708  PHE   A O     1 
ATOM   5245  C  CB    . PHE   A 1  710  ? -24.081 78.150  106.164 1.00 21.68 ? 708  PHE   A CB    1 
ATOM   5246  C  CG    . PHE   A 1  710  ? -23.811 77.944  104.692 1.00 26.76 ? 708  PHE   A CG    1 
ATOM   5247  C  CD1   . PHE   A 1  710  ? -24.846 77.927  103.774 1.00 26.14 ? 708  PHE   A CD1   1 
ATOM   5248  C  CD2   . PHE   A 1  710  ? -22.512 77.763  104.228 1.00 23.65 ? 708  PHE   A CD2   1 
ATOM   5249  C  CE1   . PHE   A 1  710  ? -24.601 77.731  102.427 1.00 26.86 ? 708  PHE   A CE1   1 
ATOM   5250  C  CE2   . PHE   A 1  710  ? -22.256 77.567  102.875 1.00 24.79 ? 708  PHE   A CE2   1 
ATOM   5251  C  CZ    . PHE   A 1  710  ? -23.303 77.551  101.977 1.00 28.28 ? 708  PHE   A CZ    1 
ATOM   5252  N  N     . PRO   A 1  711  ? -26.453 80.008  108.365 1.00 22.12 ? 709  PRO   A N     1 
ATOM   5253  C  CA    . PRO   A 1  711  ? -26.544 80.550  109.726 1.00 22.01 ? 709  PRO   A CA    1 
ATOM   5254  C  C     . PRO   A 1  711  ? -26.791 79.517  110.800 1.00 21.51 ? 709  PRO   A C     1 
ATOM   5255  O  O     . PRO   A 1  711  ? -26.677 79.845  111.989 1.00 22.61 ? 709  PRO   A O     1 
ATOM   5256  C  CB    . PRO   A 1  711  ? -27.751 81.487  109.626 1.00 23.36 ? 709  PRO   A CB    1 
ATOM   5257  C  CG    . PRO   A 1  711  ? -28.620 80.821  108.613 1.00 21.64 ? 709  PRO   A CG    1 
ATOM   5258  C  CD    . PRO   A 1  711  ? -27.657 80.305  107.570 1.00 22.21 ? 709  PRO   A CD    1 
ATOM   5259  N  N     . LEU   A 1  712  ? -27.181 78.307  110.434 1.00 22.13 ? 710  LEU   A N     1 
ATOM   5260  C  CA    . LEU   A 1  712  ? -27.279 77.227  111.395 1.00 20.05 ? 710  LEU   A CA    1 
ATOM   5261  C  C     . LEU   A 1  712  ? -26.205 76.176  111.198 1.00 21.48 ? 710  LEU   A C     1 
ATOM   5262  O  O     . LEU   A 1  712  ? -25.614 75.726  112.174 1.00 20.72 ? 710  LEU   A O     1 
ATOM   5263  C  CB    . LEU   A 1  712  ? -28.655 76.563  111.325 1.00 22.23 ? 710  LEU   A CB    1 
ATOM   5264  C  CG    . LEU   A 1  712  ? -28.818 75.453  112.360 1.00 21.77 ? 710  LEU   A CG    1 
ATOM   5265  C  CD1   . LEU   A 1  712  ? -28.744 76.018  113.776 1.00 21.04 ? 710  LEU   A CD1   1 
ATOM   5266  C  CD2   . LEU   A 1  712  ? -30.113 74.678  112.138 1.00 23.63 ? 710  LEU   A CD2   1 
ATOM   5267  N  N     . ALA   A 1  713  ? -25.909 75.807  109.953 1.00 21.07 ? 711  ALA   A N     1 
ATOM   5268  C  CA    . ALA   A 1  713  ? -25.022 74.675  109.711 1.00 18.71 ? 711  ALA   A CA    1 
ATOM   5269  C  C     . ALA   A 1  713  ? -23.590 74.984  110.125 1.00 21.06 ? 711  ALA   A C     1 
ATOM   5270  O  O     . ALA   A 1  713  ? -22.990 74.238  110.904 1.00 20.50 ? 711  ALA   A O     1 
ATOM   5271  C  CB    . ALA   A 1  713  ? -25.087 74.260  108.243 1.00 18.41 ? 711  ALA   A CB    1 
ATOM   5272  N  N     . ILE   A 1  714  ? -23.013 76.058  109.587 1.00 18.89 ? 712  ILE   A N     1 
ATOM   5273  C  CA    . ILE   A 1  714  ? -21.627 76.377  109.926 1.00 18.74 ? 712  ILE   A CA    1 
ATOM   5274  C  C     . ILE   A 1  714  ? -21.529 76.801  111.378 1.00 20.81 ? 712  ILE   A C     1 
ATOM   5275  O  O     . ILE   A 1  714  ? -20.580 76.443  112.086 1.00 21.30 ? 712  ILE   A O     1 
ATOM   5276  C  CB    . ILE   A 1  714  ? -21.065 77.441  108.972 1.00 20.52 ? 712  ILE   A CB    1 
ATOM   5277  C  CG1   . ILE   A 1  714  ? -20.925 76.803  107.585 1.00 22.16 ? 712  ILE   A CG1   1 
ATOM   5278  C  CG2   . ILE   A 1  714  ? -19.734 78.031  109.513 1.00 20.27 ? 712  ILE   A CG2   1 
ATOM   5279  C  CD1   . ILE   A 1  714  ? -19.917 77.454  106.703 1.00 28.68 ? 712  ILE   A CD1   1 
ATOM   5280  N  N     . PHE   A 1  715  ? -22.503 77.586  111.834 1.00 20.63 ? 713  PHE   A N     1 
ATOM   5281  C  CA    . PHE   A 1  715  ? -22.583 77.947  113.240 1.00 20.24 ? 713  PHE   A CA    1 
ATOM   5282  C  C     . PHE   A 1  715  ? -22.509 76.705  114.118 1.00 22.74 ? 713  PHE   A C     1 
ATOM   5283  O  O     . PHE   A 1  715  ? -21.661 76.606  115.015 1.00 20.18 ? 713  PHE   A O     1 
ATOM   5284  C  CB    . PHE   A 1  715  ? -23.905 78.677  113.464 1.00 21.66 ? 713  PHE   A CB    1 
ATOM   5285  C  CG    . PHE   A 1  715  ? -24.137 79.056  114.873 1.00 20.52 ? 713  PHE   A CG    1 
ATOM   5286  C  CD1   . PHE   A 1  715  ? -23.517 80.169  115.394 1.00 22.65 ? 713  PHE   A CD1   1 
ATOM   5287  C  CD2   . PHE   A 1  715  ? -24.980 78.305  115.683 1.00 21.83 ? 713  PHE   A CD2   1 
ATOM   5288  C  CE1   . PHE   A 1  715  ? -23.718 80.530  116.709 1.00 26.00 ? 713  PHE   A CE1   1 
ATOM   5289  C  CE2   . PHE   A 1  715  ? -25.180 78.655  116.995 1.00 23.35 ? 713  PHE   A CE2   1 
ATOM   5290  C  CZ    . PHE   A 1  715  ? -24.562 79.778  117.509 1.00 26.14 ? 713  PHE   A CZ    1 
ATOM   5291  N  N     . THR   A 1  716  ? -23.370 75.725  113.843 1.00 19.86 ? 714  THR   A N     1 
ATOM   5292  C  CA    . THR   A 1  716  ? -23.409 74.513  114.656 1.00 20.90 ? 714  THR   A CA    1 
ATOM   5293  C  C     . THR   A 1  716  ? -22.137 73.698  114.498 1.00 21.85 ? 714  THR   A C     1 
ATOM   5294  O  O     . THR   A 1  716  ? -21.605 73.174  115.486 1.00 20.63 ? 714  THR   A O     1 
ATOM   5295  C  CB    . THR   A 1  716  ? -24.625 73.674  114.261 1.00 21.70 ? 714  THR   A CB    1 
ATOM   5296  O  OG1   . THR   A 1  716  ? -25.820 74.419  114.540 1.00 21.65 ? 714  THR   A OG1   1 
ATOM   5297  C  CG2   . THR   A 1  716  ? -24.651 72.369  115.033 1.00 24.13 ? 714  THR   A CG2   1 
ATOM   5298  N  N     . GLY   A 1  717  ? -21.637 73.585  113.265 1.00 18.38 ? 715  GLY   A N     1 
ATOM   5299  C  CA    . GLY   A 1  717  ? -20.458 72.770  113.027 1.00 20.02 ? 715  GLY   A CA    1 
ATOM   5300  C  C     . GLY   A 1  717  ? -19.269 73.227  113.849 1.00 20.60 ? 715  GLY   A C     1 
ATOM   5301  O  O     . GLY   A 1  717  ? -18.631 72.427  114.532 1.00 21.14 ? 715  GLY   A O     1 
ATOM   5302  N  N     . GLN   A 1  718  ? -18.962 74.524  113.805 1.00 19.24 ? 716  GLN   A N     1 
ATOM   5303  C  CA    . GLN   A 1  718  ? -17.786 75.007  114.529 1.00 20.45 ? 716  GLN   A CA    1 
ATOM   5304  C  C     . GLN   A 1  718  ? -17.945 74.787  116.021 1.00 21.18 ? 716  GLN   A C     1 
ATOM   5305  O  O     . GLN   A 1  718  ? -17.033 74.297  116.697 1.00 20.88 ? 716  GLN   A O     1 
ATOM   5306  C  CB    . GLN   A 1  718  ? -17.554 76.490  114.252 1.00 18.96 ? 716  GLN   A CB    1 
ATOM   5307  C  CG    . GLN   A 1  718  ? -17.268 76.786  112.804 1.00 20.34 ? 716  GLN   A CG    1 
ATOM   5308  C  CD    . GLN   A 1  718  ? -16.820 78.212  112.568 1.00 20.76 ? 716  GLN   A CD    1 
ATOM   5309  O  OE1   . GLN   A 1  718  ? -15.865 78.448  111.825 1.00 20.20 ? 716  GLN   A OE1   1 
ATOM   5310  N  NE2   . GLN   A 1  718  ? -17.496 79.170  113.197 1.00 21.43 ? 716  GLN   A NE2   1 
ATOM   5311  N  N     . ILE   A 1  719  ? -19.103 75.162  116.556 1.00 21.00 ? 717  ILE   A N     1 
ATOM   5312  C  CA    . ILE   A 1  719  ? -19.327 75.060  117.988 1.00 20.98 ? 717  ILE   A CA    1 
ATOM   5313  C  C     . ILE   A 1  719  ? -19.308 73.611  118.433 1.00 21.77 ? 717  ILE   A C     1 
ATOM   5314  O  O     . ILE   A 1  719  ? -18.715 73.273  119.467 1.00 21.44 ? 717  ILE   A O     1 
ATOM   5315  C  CB    . ILE   A 1  719  ? -20.654 75.741  118.339 1.00 23.98 ? 717  ILE   A CB    1 
ATOM   5316  C  CG1   . ILE   A 1  719  ? -20.534 77.240  118.132 1.00 23.08 ? 717  ILE   A CG1   1 
ATOM   5317  C  CG2   . ILE   A 1  719  ? -21.068 75.391  119.748 1.00 29.70 ? 717  ILE   A CG2   1 
ATOM   5318  C  CD1   . ILE   A 1  719  ? -21.875 77.880  118.042 1.00 27.45 ? 717  ILE   A CD1   1 
ATOM   5319  N  N     . ALA   A 1  720  ? -19.965 72.736  117.672 1.00 22.09 ? 718  ALA   A N     1 
ATOM   5320  C  CA    . ALA   A 1  720  ? -20.038 71.333  118.058 1.00 21.94 ? 718  ALA   A CA    1 
ATOM   5321  C  C     . ALA   A 1  720  ? -18.653 70.719  118.093 1.00 19.60 ? 718  ALA   A C     1 
ATOM   5322  O  O     . ALA   A 1  720  ? -18.318 69.975  119.016 1.00 20.73 ? 718  ALA   A O     1 
ATOM   5323  C  CB    . ALA   A 1  720  ? -20.928 70.569  117.072 1.00 22.09 ? 718  ALA   A CB    1 
ATOM   5324  N  N     . ALA   A 1  721  ? -17.839 71.028  117.089 1.00 19.18 ? 719  ALA   A N     1 
ATOM   5325  C  CA    . ALA   A 1  721  ? -16.480 70.510  117.055 1.00 18.11 ? 719  ALA   A CA    1 
ATOM   5326  C  C     . ALA   A 1  721  ? -15.694 70.980  118.271 1.00 21.77 ? 719  ALA   A C     1 
ATOM   5327  O  O     . ALA   A 1  721  ? -15.047 70.179  118.956 1.00 19.51 ? 719  ALA   A O     1 
ATOM   5328  C  CB    . ALA   A 1  721  ? -15.805 70.988  115.777 1.00 19.59 ? 719  ALA   A CB    1 
ATOM   5329  N  N     . ALA   A 1  722  ? -15.729 72.283  118.543 1.00 19.38 ? 720  ALA   A N     1 
ATOM   5330  C  CA    . ALA   A 1  722  ? -14.983 72.817  119.677 1.00 19.28 ? 720  ALA   A CA    1 
ATOM   5331  C  C     . ALA   A 1  722  ? -15.453 72.196  120.989 1.00 22.76 ? 720  ALA   A C     1 
ATOM   5332  O  O     . ALA   A 1  722  ? -14.637 71.766  121.813 1.00 22.23 ? 720  ALA   A O     1 
ATOM   5333  C  CB    . ALA   A 1  722  ? -15.093 74.341  119.707 1.00 22.70 ? 720  ALA   A CB    1 
ATOM   5334  N  N     . LEU   A 1  723  ? -16.771 72.127  121.188 1.00 20.91 ? 721  LEU   A N     1 
ATOM   5335  C  CA    . LEU   A 1  723  ? -17.329 71.573  122.415 1.00 20.47 ? 721  LEU   A CA    1 
ATOM   5336  C  C     . LEU   A 1  723  ? -16.943 70.114  122.588 1.00 21.54 ? 721  LEU   A C     1 
ATOM   5337  O  O     . LEU   A 1  723  ? -16.558 69.684  123.677 1.00 21.31 ? 721  LEU   A O     1 
ATOM   5338  C  CB    . LEU   A 1  723  ? -18.849 71.686  122.383 1.00 23.88 ? 721  LEU   A CB    1 
ATOM   5339  C  CG    . LEU   A 1  723  ? -19.467 73.059  122.594 1.00 21.49 ? 721  LEU   A CG    1 
ATOM   5340  C  CD1   . LEU   A 1  723  ? -20.957 72.952  122.339 1.00 22.40 ? 721  LEU   A CD1   1 
ATOM   5341  C  CD2   . LEU   A 1  723  ? -19.188 73.533  124.003 1.00 23.24 ? 721  LEU   A CD2   1 
ATOM   5342  N  N     . VAL   A 1  724  ? -17.073 69.320  121.527 1.00 22.60 ? 722  VAL   A N     1 
ATOM   5343  C  CA    . VAL   A 1  724  ? -16.868 67.895  121.712 1.00 22.61 ? 722  VAL   A CA    1 
ATOM   5344  C  C     . VAL   A 1  724  ? -15.395 67.598  121.943 1.00 22.16 ? 722  VAL   A C     1 
ATOM   5345  O  O     . VAL   A 1  724  ? -15.051 66.603  122.590 1.00 23.20 ? 722  VAL   A O     1 
ATOM   5346  C  CB    . VAL   A 1  724  ? -17.474 67.101  120.543 1.00 19.75 ? 722  VAL   A CB    1 
ATOM   5347  C  CG1   . VAL   A 1  724  ? -16.538 67.120  119.322 1.00 20.81 ? 722  VAL   A CG1   1 
ATOM   5348  C  CG2   . VAL   A 1  724  ? -17.845 65.693  120.994 1.00 22.79 ? 722  VAL   A CG2   1 
ATOM   5349  N  N     . ALA   A 1  725  ? -14.512 68.464  121.444 1.00 21.48 ? 723  ALA   A N     1 
ATOM   5350  C  CA    . ALA   A 1  725  ? -13.085 68.377  121.731 1.00 21.87 ? 723  ALA   A CA    1 
ATOM   5351  C  C     . ALA   A 1  725  ? -12.749 68.804  123.151 1.00 26.05 ? 723  ALA   A C     1 
ATOM   5352  O  O     . ALA   A 1  725  ? -11.566 68.797  123.518 1.00 25.27 ? 723  ALA   A O     1 
ATOM   5353  C  CB    . ALA   A 1  725  ? -12.303 69.222  120.729 1.00 21.00 ? 723  ALA   A CB    1 
ATOM   5354  N  N     . GLY   A 1  726  ? -13.744 69.186  123.944 1.00 23.07 ? 724  GLY   A N     1 
ATOM   5355  C  CA    . GLY   A 1  726  ? -13.530 69.534  125.328 1.00 23.15 ? 724  GLY   A CA    1 
ATOM   5356  C  C     . GLY   A 1  726  ? -13.335 71.002  125.624 1.00 25.16 ? 724  GLY   A C     1 
ATOM   5357  O  O     . GLY   A 1  726  ? -12.962 71.343  126.759 1.00 26.94 ? 724  GLY   A O     1 
ATOM   5358  N  N     . ASN   A 1  727  ? -13.586 71.877  124.664 1.00 24.19 ? 725  ASN   A N     1 
ATOM   5359  C  CA    . ASN   A 1  727  ? -13.369 73.301  124.849 1.00 23.33 ? 725  ASN   A CA    1 
ATOM   5360  C  C     . ASN   A 1  727  ? -14.683 74.007  125.131 1.00 22.73 ? 725  ASN   A C     1 
ATOM   5361  O  O     . ASN   A 1  727  ? -15.682 73.757  124.450 1.00 23.13 ? 725  ASN   A O     1 
ATOM   5362  C  CB    . ASN   A 1  727  ? -12.810 73.908  123.566 1.00 23.77 ? 725  ASN   A CB    1 
ATOM   5363  C  CG    . ASN   A 1  727  ? -11.580 73.211  123.084 1.00 24.16 ? 725  ASN   A CG    1 
ATOM   5364  O  OD1   . ASN   A 1  727  ? -10.497 73.403  123.631 1.00 25.85 ? 725  ASN   A OD1   1 
ATOM   5365  N  ND2   . ASN   A 1  727  ? -11.726 72.407  122.043 1.00 22.59 ? 725  ASN   A ND2   1 
ATOM   5366  N  N     . PRO   A 1  728  ? -14.711 74.929  126.079 1.00 23.62 ? 726  PRO   A N     1 
ATOM   5367  C  CA    . PRO   A 1  728  ? -15.866 75.815  126.186 1.00 24.79 ? 726  PRO   A CA    1 
ATOM   5368  C  C     . PRO   A 1  728  ? -15.837 76.816  125.047 1.00 24.61 ? 726  PRO   A C     1 
ATOM   5369  O  O     . PRO   A 1  728  ? -14.771 77.193  124.550 1.00 25.66 ? 726  PRO   A O     1 
ATOM   5370  C  CB    . PRO   A 1  728  ? -15.658 76.504  127.535 1.00 25.37 ? 726  PRO   A CB    1 
ATOM   5371  C  CG    . PRO   A 1  728  ? -14.200 76.519  127.713 1.00 24.91 ? 726  PRO   A CG    1 
ATOM   5372  C  CD    . PRO   A 1  728  ? -13.635 75.307  127.009 1.00 24.87 ? 726  PRO   A CD    1 
ATOM   5373  N  N     . VAL   A 1  729  ? -17.026 77.251  124.641 1.00 25.24 ? 727  VAL   A N     1 
ATOM   5374  C  CA    . VAL   A 1  729  ? -17.213 77.984  123.396 1.00 23.75 ? 727  VAL   A CA    1 
ATOM   5375  C  C     . VAL   A 1  729  ? -17.856 79.336  123.663 1.00 24.97 ? 727  VAL   A C     1 
ATOM   5376  O  O     . VAL   A 1  729  ? -18.813 79.443  124.433 1.00 25.32 ? 727  VAL   A O     1 
ATOM   5377  C  CB    . VAL   A 1  729  ? -18.048 77.167  122.388 1.00 20.93 ? 727  VAL   A CB    1 
ATOM   5378  C  CG1   . VAL   A 1  729  ? -18.509 78.047  121.219 1.00 24.29 ? 727  VAL   A CG1   1 
ATOM   5379  C  CG2   . VAL   A 1  729  ? -17.210 76.014  121.883 1.00 23.62 ? 727  VAL   A CG2   1 
ATOM   5380  N  N     . LEU   A 1  730  ? -17.322 80.360  123.011 1.00 23.67 ? 728  LEU   A N     1 
ATOM   5381  C  CA    . LEU   A 1  730  ? -17.957 81.661  122.884 1.00 23.58 ? 728  LEU   A CA    1 
ATOM   5382  C  C     . LEU   A 1  730  ? -18.461 81.716  121.454 1.00 23.02 ? 728  LEU   A C     1 
ATOM   5383  O  O     . LEU   A 1  730  ? -17.659 81.751  120.515 1.00 23.64 ? 728  LEU   A O     1 
ATOM   5384  C  CB    . LEU   A 1  730  ? -16.955 82.784  123.138 1.00 26.41 ? 728  LEU   A CB    1 
ATOM   5385  C  CG    . LEU   A 1  730  ? -16.324 82.893  124.535 1.00 23.68 ? 728  LEU   A CG    1 
ATOM   5386  C  CD1   . LEU   A 1  730  ? -17.366 82.687  125.628 1.00 26.21 ? 728  LEU   A CD1   1 
ATOM   5387  C  CD2   . LEU   A 1  730  ? -15.183 81.922  124.695 1.00 25.78 ? 728  LEU   A CD2   1 
ATOM   5388  N  N     . ALA   A 1  731  ? -19.778 81.699  121.287 1.00 24.82 ? 729  ALA   A N     1 
ATOM   5389  C  CA    . ALA   A 1  731  ? -20.396 81.600  119.969 1.00 23.85 ? 729  ALA   A CA    1 
ATOM   5390  C  C     . ALA   A 1  731  ? -20.839 82.990  119.543 1.00 26.62 ? 729  ALA   A C     1 
ATOM   5391  O  O     . ALA   A 1  731  ? -21.743 83.571  120.148 1.00 25.74 ? 729  ALA   A O     1 
ATOM   5392  C  CB    . ALA   A 1  731  ? -21.584 80.644  120.001 1.00 25.11 ? 729  ALA   A CB    1 
ATOM   5393  N  N     . LYS   A 1  732  ? -20.215 83.514  118.488 1.00 22.81 ? 730  LYS   A N     1 
ATOM   5394  C  CA    . LYS   A 1  732  ? -20.515 84.849  117.984 1.00 23.65 ? 730  LYS   A CA    1 
ATOM   5395  C  C     . LYS   A 1  732  ? -21.118 84.678  116.598 1.00 22.87 ? 730  LYS   A C     1 
ATOM   5396  O  O     . LYS   A 1  732  ? -20.386 84.594  115.605 1.00 22.75 ? 730  LYS   A O     1 
ATOM   5397  C  CB    . LYS   A 1  732  ? -19.237 85.689  117.921 1.00 25.56 ? 730  LYS   A CB    1 
ATOM   5398  C  CG    . LYS   A 1  732  ? -19.440 87.167  118.236 1.00 24.89 ? 730  LYS   A CG    1 
ATOM   5399  C  CD    . LYS   A 1  732  ? -20.424 87.831  117.268 1.00 24.56 ? 730  LYS   A CD    1 
ATOM   5400  C  CE    . LYS   A 1  732  ? -19.791 87.996  115.890 1.00 25.86 ? 730  LYS   A CE    1 
ATOM   5401  N  NZ    . LYS   A 1  732  ? -20.791 88.540  114.918 1.00 25.11 ? 730  LYS   A NZ    1 
ATOM   5402  N  N     . PRO   A 1  733  ? -22.438 84.627  116.473 1.00 20.89 ? 731  PRO   A N     1 
ATOM   5403  C  CA    . PRO   A 1  733  ? -23.044 84.478  115.152 1.00 22.06 ? 731  PRO   A CA    1 
ATOM   5404  C  C     . PRO   A 1  733  ? -23.018 85.797  114.399 1.00 20.99 ? 731  PRO   A C     1 
ATOM   5405  O  O     . PRO   A 1  733  ? -22.886 86.878  114.976 1.00 23.73 ? 731  PRO   A O     1 
ATOM   5406  C  CB    . PRO   A 1  733  ? -24.484 84.086  115.480 1.00 21.90 ? 731  PRO   A CB    1 
ATOM   5407  C  CG    . PRO   A 1  733  ? -24.753 84.789  116.781 1.00 24.16 ? 731  PRO   A CG    1 
ATOM   5408  C  CD    . PRO   A 1  733  ? -23.449 84.698  117.543 1.00 22.51 ? 731  PRO   A CD    1 
ATOM   5409  N  N     . ALA   A 1  734  ? -23.130 85.685  113.078 1.00 21.28 ? 732  ALA   A N     1 
ATOM   5410  C  CA    . ALA   A 1  734  ? -23.182 86.870  112.239 1.00 23.32 ? 732  ALA   A CA    1 
ATOM   5411  C  C     . ALA   A 1  734  ? -24.312 87.785  112.690 1.00 23.15 ? 732  ALA   A C     1 
ATOM   5412  O  O     . ALA   A 1  734  ? -25.380 87.326  113.111 1.00 23.96 ? 732  ALA   A O     1 
ATOM   5413  C  CB    . ALA   A 1  734  ? -23.436 86.454  110.798 1.00 21.68 ? 732  ALA   A CB    1 
ATOM   5414  N  N     . GLU   A 1  735  ? -24.081 89.091  112.581 1.00 22.80 ? 733  GLU   A N     1 
ATOM   5415  C  CA    . GLU   A 1  735  ? -25.082 90.046  113.036 1.00 25.68 ? 733  GLU   A CA    1 
ATOM   5416  C  C     . GLU   A 1  735  ? -26.382 89.953  112.249 1.00 26.62 ? 733  GLU   A C     1 
ATOM   5417  O  O     . GLU   A 1  735  ? -27.426 90.382  112.752 1.00 27.33 ? 733  GLU   A O     1 
ATOM   5418  C  CB    . GLU   A 1  735  ? -24.526 91.469  112.986 1.00 27.22 ? 733  GLU   A CB    1 
ATOM   5419  C  CG    . GLU   A 1  735  ? -24.020 91.912  111.619 1.00 26.40 ? 733  GLU   A CG    1 
ATOM   5420  C  CD    . GLU   A 1  735  ? -22.533 91.627  111.422 1.00 31.19 ? 733  GLU   A CD    1 
ATOM   5421  O  OE1   . GLU   A 1  735  ? -22.011 90.682  112.059 1.00 29.43 ? 733  GLU   A OE1   1 
ATOM   5422  O  OE2   . GLU   A 1  735  ? -21.893 92.347  110.628 1.00 30.39 ? 733  GLU   A OE2   1 
ATOM   5423  N  N     . GLU   A 1  736  ? -26.352 89.393  111.040 1.00 25.66 ? 734  GLU   A N     1 
ATOM   5424  C  CA    . GLU   A 1  736  ? -27.561 89.336  110.234 1.00 23.84 ? 734  GLU   A CA    1 
ATOM   5425  C  C     . GLU   A 1  736  ? -28.490 88.219  110.676 1.00 24.77 ? 734  GLU   A C     1 
ATOM   5426  O  O     . GLU   A 1  736  ? -29.707 88.330  110.495 1.00 26.99 ? 734  GLU   A O     1 
ATOM   5427  C  CB    . GLU   A 1  736  ? -27.204 89.131  108.763 1.00 23.18 ? 734  GLU   A CB    1 
ATOM   5428  C  CG    . GLU   A 1  736  ? -26.390 90.255  108.144 1.00 27.28 ? 734  GLU   A CG    1 
ATOM   5429  C  CD    . GLU   A 1  736  ? -24.892 90.014  108.213 1.00 33.08 ? 734  GLU   A CD    1 
ATOM   5430  O  OE1   . GLU   A 1  736  ? -24.437 89.197  109.052 1.00 25.26 ? 734  GLU   A OE1   1 
ATOM   5431  O  OE2   . GLU   A 1  736  ? -24.163 90.646  107.417 1.00 27.69 ? 734  GLU   A OE2   1 
ATOM   5432  N  N     . THR   A 1  737  ? -27.955 87.149  111.259 1.00 23.69 ? 735  THR   A N     1 
ATOM   5433  C  CA    . THR   A 1  737  ? -28.724 85.926  111.505 1.00 23.51 ? 735  THR   A CA    1 
ATOM   5434  C  C     . THR   A 1  737  ? -28.552 85.415  112.935 1.00 23.17 ? 735  THR   A C     1 
ATOM   5435  O  O     . THR   A 1  737  ? -28.197 84.252  113.150 1.00 24.49 ? 735  THR   A O     1 
ATOM   5436  C  CB    . THR   A 1  737  ? -28.348 84.853  110.484 1.00 23.92 ? 735  THR   A CB    1 
ATOM   5437  O  OG1   . THR   A 1  737  ? -26.921 84.678  110.483 1.00 22.57 ? 735  THR   A OG1   1 
ATOM   5438  C  CG2   . THR   A 1  737  ? -28.809 85.261  109.093 1.00 23.16 ? 735  THR   A CG2   1 
ATOM   5439  N  N     . PRO   A 1  738  ? -28.836 86.247  113.947 1.00 23.54 ? 736  PRO   A N     1 
ATOM   5440  C  CA    . PRO   A 1  738  ? -28.691 85.777  115.332 1.00 23.07 ? 736  PRO   A CA    1 
ATOM   5441  C  C     . PRO   A 1  738  ? -29.788 84.840  115.799 1.00 25.74 ? 736  PRO   A C     1 
ATOM   5442  O  O     . PRO   A 1  738  ? -29.553 84.078  116.746 1.00 24.19 ? 736  PRO   A O     1 
ATOM   5443  C  CB    . PRO   A 1  738  ? -28.732 87.078  116.143 1.00 27.02 ? 736  PRO   A CB    1 
ATOM   5444  C  CG    . PRO   A 1  738  ? -29.676 87.922  115.366 1.00 25.49 ? 736  PRO   A CG    1 
ATOM   5445  C  CD    . PRO   A 1  738  ? -29.360 87.625  113.909 1.00 25.93 ? 736  PRO   A CD    1 
ATOM   5446  N  N     . LEU   A 1  739  ? -30.984 84.887  115.203 1.00 23.34 ? 737  LEU   A N     1 
ATOM   5447  C  CA    . LEU   A 1  739  ? -32.106 84.152  115.781 1.00 23.20 ? 737  LEU   A CA    1 
ATOM   5448  C  C     . LEU   A 1  739  ? -31.921 82.645  115.657 1.00 21.41 ? 737  LEU   A C     1 
ATOM   5449  O  O     . LEU   A 1  739  ? -32.108 81.906  116.629 1.00 23.93 ? 737  LEU   A O     1 
ATOM   5450  C  CB    . LEU   A 1  739  ? -33.420 84.590  115.144 1.00 21.54 ? 737  LEU   A CB    1 
ATOM   5451  C  CG    . LEU   A 1  739  ? -33.761 86.063  115.305 1.00 25.21 ? 737  LEU   A CG    1 
ATOM   5452  C  CD1   . LEU   A 1  739  ? -35.043 86.359  114.527 1.00 25.30 ? 737  LEU   A CD1   1 
ATOM   5453  C  CD2   . LEU   A 1  739  ? -33.922 86.421  116.785 1.00 24.78 ? 737  LEU   A CD2   1 
ATOM   5454  N  N     . ILE   A 1  740  ? -31.594 82.164  114.459 1.00 22.49 ? 738  ILE   A N     1 
ATOM   5455  C  CA    . ILE   A 1  740  ? -31.398 80.726  114.293 1.00 21.90 ? 738  ILE   A CA    1 
ATOM   5456  C  C     . ILE   A 1  740  ? -30.202 80.252  115.110 1.00 20.81 ? 738  ILE   A C     1 
ATOM   5457  O  O     . ILE   A 1  740  ? -30.193 79.126  115.623 1.00 23.45 ? 738  ILE   A O     1 
ATOM   5458  C  CB    . ILE   A 1  740  ? -31.308 80.348  112.799 1.00 22.33 ? 738  ILE   A CB    1 
ATOM   5459  C  CG1   . ILE   A 1  740  ? -31.299 78.830  112.619 1.00 23.93 ? 738  ILE   A CG1   1 
ATOM   5460  C  CG2   . ILE   A 1  740  ? -30.053 80.923  112.182 1.00 24.55 ? 738  ILE   A CG2   1 
ATOM   5461  C  CD1   . ILE   A 1  740  ? -32.529 78.129  113.126 1.00 24.66 ? 738  ILE   A CD1   1 
ATOM   5462  N  N     . ALA   A 1  741  ? -29.199 81.111  115.276 1.00 23.19 ? 739  ALA   A N     1 
ATOM   5463  C  CA    . ALA   A 1  741  ? -28.065 80.767  116.122 1.00 24.92 ? 739  ALA   A CA    1 
ATOM   5464  C  C     . ALA   A 1  741  ? -28.497 80.622  117.572 1.00 23.21 ? 739  ALA   A C     1 
ATOM   5465  O  O     . ALA   A 1  741  ? -28.099 79.669  118.251 1.00 24.97 ? 739  ALA   A O     1 
ATOM   5466  C  CB    . ALA   A 1  741  ? -26.985 81.837  115.992 1.00 26.16 ? 739  ALA   A CB    1 
ATOM   5467  N  N     . ALA   A 1  742  ? -29.321 81.550  118.058 1.00 23.77 ? 740  ALA   A N     1 
ATOM   5468  C  CA    . ALA   A 1  742  ? -29.824 81.437  119.420 1.00 23.35 ? 740  ALA   A CA    1 
ATOM   5469  C  C     . ALA   A 1  742  ? -30.614 80.151  119.598 1.00 25.95 ? 740  ALA   A C     1 
ATOM   5470  O  O     . ALA   A 1  742  ? -30.525 79.497  120.641 1.00 26.83 ? 740  ALA   A O     1 
ATOM   5471  C  CB    . ALA   A 1  742  ? -30.684 82.655  119.771 1.00 24.59 ? 740  ALA   A CB    1 
ATOM   5472  N  N     . GLU   A 1  743  ? -31.381 79.763  118.580 1.00 23.83 ? 741  GLU   A N     1 
ATOM   5473  C  CA    . GLU   A 1  743  ? -32.144 78.527  118.682 1.00 26.53 ? 741  GLU   A CA    1 
ATOM   5474  C  C     . GLU   A 1  743  ? -31.220 77.311  118.678 1.00 23.31 ? 741  GLU   A C     1 
ATOM   5475  O  O     . GLU   A 1  743  ? -31.452 76.344  119.418 1.00 24.85 ? 741  GLU   A O     1 
ATOM   5476  C  CB    . GLU   A 1  743  ? -33.171 78.477  117.552 1.00 25.11 ? 741  GLU   A CB    1 
ATOM   5477  C  CG    . GLU   A 1  743  ? -33.953 77.190  117.442 1.00 30.04 ? 741  GLU   A CG    1 
ATOM   5478  C  CD    . GLU   A 1  743  ? -34.907 76.942  118.593 1.00 26.79 ? 741  GLU   A CD    1 
ATOM   5479  O  OE1   . GLU   A 1  743  ? -35.095 77.829  119.464 1.00 27.51 ? 741  GLU   A OE1   1 
ATOM   5480  O  OE2   . GLU   A 1  743  ? -35.464 75.827  118.625 1.00 30.75 ? 741  GLU   A OE2   1 
ATOM   5481  N  N     . GLY   A 1  744  ? -30.158 77.349  117.870 1.00 24.83 ? 742  GLY   A N     1 
ATOM   5482  C  CA    . GLY   A 1  744  ? -29.187 76.267  117.894 1.00 24.04 ? 742  GLY   A CA    1 
ATOM   5483  C  C     . GLY   A 1  744  ? -28.507 76.137  119.244 1.00 23.30 ? 742  GLY   A C     1 
ATOM   5484  O  O     . GLY   A 1  744  ? -28.286 75.026  119.733 1.00 24.62 ? 742  GLY   A O     1 
ATOM   5485  N  N     . VAL   A 1  745  ? -28.166 77.270  119.863 1.00 24.64 ? 743  VAL   A N     1 
ATOM   5486  C  CA    . VAL   A 1  745  ? -27.599 77.233  121.208 1.00 24.37 ? 743  VAL   A CA    1 
ATOM   5487  C  C     . VAL   A 1  745  ? -28.611 76.679  122.205 1.00 26.87 ? 743  VAL   A C     1 
ATOM   5488  O  O     . VAL   A 1  745  ? -28.270 75.868  123.076 1.00 27.38 ? 743  VAL   A O     1 
ATOM   5489  C  CB    . VAL   A 1  745  ? -27.075 78.623  121.617 1.00 26.28 ? 743  VAL   A CB    1 
ATOM   5490  C  CG1   . VAL   A 1  745  ? -26.776 78.672  123.121 1.00 28.51 ? 743  VAL   A CG1   1 
ATOM   5491  C  CG2   . VAL   A 1  745  ? -25.818 78.961  120.821 1.00 27.04 ? 743  VAL   A CG2   1 
ATOM   5492  N  N     . ARG   A 1  746  ? -29.876 77.093  122.085 1.00 26.06 ? 744  ARG   A N     1 
ATOM   5493  C  CA    . ARG   A 1  746  ? -30.898 76.561  122.978 1.00 27.37 ? 744  ARG   A CA    1 
ATOM   5494  C  C     . ARG   A 1  746  ? -30.993 75.046  122.850 1.00 25.76 ? 744  ARG   A C     1 
ATOM   5495  O  O     . ARG   A 1  746  ? -31.099 74.330  123.850 1.00 27.95 ? 744  ARG   A O     1 
ATOM   5496  C  CB    . ARG   A 1  746  ? -32.248 77.206  122.662 1.00 28.09 ? 744  ARG   A CB    1 
ATOM   5497  C  CG    . ARG   A 1  746  ? -33.328 76.848  123.660 1.00 29.43 ? 744  ARG   A CG    1 
ATOM   5498  C  CD    . ARG   A 1  746  ? -34.725 77.148  123.133 1.00 28.66 ? 744  ARG   A CD    1 
ATOM   5499  N  NE    . ARG   A 1  746  ? -35.053 76.299  121.994 1.00 30.90 ? 744  ARG   A NE    1 
ATOM   5500  C  CZ    . ARG   A 1  746  ? -35.371 75.014  122.082 1.00 33.07 ? 744  ARG   A CZ    1 
ATOM   5501  N  NH1   . ARG   A 1  746  ? -35.415 74.389  123.250 1.00 34.09 ? 744  ARG   A NH1   1 
ATOM   5502  N  NH2   . ARG   A 1  746  ? -35.647 74.337  120.970 1.00 30.29 ? 744  ARG   A NH2   1 
ATOM   5503  N  N     . ILE   A 1  747  ? -30.946 74.540  121.618 1.00 24.70 ? 745  ILE   A N     1 
ATOM   5504  C  CA    . ILE   A 1  747  ? -31.006 73.099  121.401 1.00 25.74 ? 745  ILE   A CA    1 
ATOM   5505  C  C     . ILE   A 1  747  ? -29.787 72.402  121.995 1.00 26.67 ? 745  ILE   A C     1 
ATOM   5506  O  O     . ILE   A 1  747  ? -29.907 71.349  122.632 1.00 25.25 ? 745  ILE   A O     1 
ATOM   5507  C  CB    . ILE   A 1  747  ? -31.178 72.815  119.901 1.00 23.69 ? 745  ILE   A CB    1 
ATOM   5508  C  CG1   . ILE   A 1  747  ? -32.594 73.212  119.467 1.00 25.77 ? 745  ILE   A CG1   1 
ATOM   5509  C  CG2   . ILE   A 1  747  ? -30.834 71.348  119.588 1.00 26.29 ? 745  ILE   A CG2   1 
ATOM   5510  C  CD1   . ILE   A 1  747  ? -32.782 73.321  117.960 1.00 25.95 ? 745  ILE   A CD1   1 
ATOM   5511  N  N     . LEU   A 1  748  ? -28.593 72.961  121.786 1.00 25.11 ? 746  LEU   A N     1 
ATOM   5512  C  CA    . LEU   A 1  748  ? -27.392 72.350  122.342 1.00 24.32 ? 746  LEU   A CA    1 
ATOM   5513  C  C     . LEU   A 1  748  ? -27.441 72.354  123.860 1.00 25.30 ? 746  LEU   A C     1 
ATOM   5514  O  O     . LEU   A 1  748  ? -27.076 71.367  124.509 1.00 24.76 ? 746  LEU   A O     1 
ATOM   5515  C  CB    . LEU   A 1  748  ? -26.160 73.100  121.848 1.00 23.42 ? 746  LEU   A CB    1 
ATOM   5516  C  CG    . LEU   A 1  748  ? -25.656 72.658  120.482 1.00 26.65 ? 746  LEU   A CG    1 
ATOM   5517  C  CD1   . LEU   A 1  748  ? -24.792 73.747  119.859 1.00 29.25 ? 746  LEU   A CD1   1 
ATOM   5518  C  CD2   . LEU   A 1  748  ? -24.859 71.381  120.634 1.00 27.24 ? 746  LEU   A CD2   1 
ATOM   5519  N  N     . ARG   A 1  749  ? -27.911 73.453  124.444 1.00 22.49 ? 747  ARG   A N     1 
ATOM   5520  C  CA    . ARG   A 1  749  ? -28.055 73.491  125.892 1.00 25.42 ? 747  ARG   A CA    1 
ATOM   5521  C  C     . ARG   A 1  749  ? -29.098 72.487  126.372 1.00 26.57 ? 747  ARG   A C     1 
ATOM   5522  O  O     . ARG   A 1  749  ? -28.892 71.806  127.385 1.00 29.10 ? 747  ARG   A O     1 
ATOM   5523  C  CB    . ARG   A 1  749  ? -28.385 74.911  126.343 1.00 28.10 ? 747  ARG   A CB    1 
ATOM   5524  C  CG    . ARG   A 1  749  ? -27.183 75.843  126.306 1.00 32.67 ? 747  ARG   A CG    1 
ATOM   5525  C  CD    . ARG   A 1  749  ? -27.542 77.212  126.842 1.00 40.00 ? 747  ARG   A CD    1 
ATOM   5526  N  NE    . ARG   A 1  749  ? -26.382 78.082  127.009 1.00 33.16 ? 747  ARG   A NE    1 
ATOM   5527  C  CZ    . ARG   A 1  749  ? -26.401 79.191  127.736 1.00 36.65 ? 747  ARG   A CZ    1 
ATOM   5528  N  NH1   . ARG   A 1  749  ? -27.499 79.586  128.362 1.00 34.58 ? 747  ARG   A NH1   1 
ATOM   5529  N  NH2   . ARG   A 1  749  ? -25.291 79.917  127.848 1.00 38.24 ? 747  ARG   A NH2   1 
ATOM   5530  N  N     . GLU   A 1  750  ? -30.219 72.366  125.648 1.00 25.39 ? 748  GLU   A N     1 
ATOM   5531  C  CA    . GLU   A 1  750  ? -31.205 71.347  125.999 1.00 28.44 ? 748  GLU   A CA    1 
ATOM   5532  C  C     . GLU   A 1  750  ? -30.607 69.945  125.929 1.00 29.29 ? 748  GLU   A C     1 
ATOM   5533  O  O     . GLU   A 1  750  ? -30.921 69.077  126.756 1.00 28.26 ? 748  GLU   A O     1 
ATOM   5534  C  CB    . GLU   A 1  750  ? -32.426 71.457  125.091 1.00 27.14 ? 748  GLU   A CB    1 
ATOM   5535  C  CG    . GLU   A 1  750  ? -33.509 70.466  125.451 1.00 30.52 ? 748  GLU   A CG    1 
ATOM   5536  C  CD    . GLU   A 1  750  ? -34.691 70.510  124.504 1.00 33.13 ? 748  GLU   A CD    1 
ATOM   5537  O  OE1   . GLU   A 1  750  ? -34.870 71.522  123.791 1.00 42.37 ? 748  GLU   A OE1   1 
ATOM   5538  O  OE2   . GLU   A 1  750  ? -35.434 69.511  124.467 1.00 34.01 ? 748  GLU   A OE2   1 
ATOM   5539  N  N     . ALA   A 1  751  ? -29.716 69.716  124.966 1.00 26.45 ? 749  ALA   A N     1 
ATOM   5540  C  CA    . ALA   A 1  751  ? -29.085 68.414  124.784 1.00 26.43 ? 749  ALA   A CA    1 
ATOM   5541  C  C     . ALA   A 1  751  ? -28.082 68.092  125.875 1.00 28.43 ? 749  ALA   A C     1 
ATOM   5542  O  O     . ALA   A 1  751  ? -27.562 66.970  125.909 1.00 30.63 ? 749  ALA   A O     1 
ATOM   5543  C  CB    . ALA   A 1  751  ? -28.378 68.362  123.430 1.00 23.51 ? 749  ALA   A CB    1 
ATOM   5544  N  N     . GLY   A 1  752  ? -27.775 69.049  126.742 1.00 26.74 ? 750  GLY   A N     1 
ATOM   5545  C  CA    . GLY   A 1  752  ? -26.902 68.804  127.873 1.00 29.48 ? 750  GLY   A CA    1 
ATOM   5546  C  C     . GLY   A 1  752  ? -25.633 69.627  127.888 1.00 29.33 ? 750  GLY   A C     1 
ATOM   5547  O  O     . GLY   A 1  752  ? -24.837 69.468  128.821 1.00 29.54 ? 750  GLY   A O     1 
ATOM   5548  N  N     . ILE   A 1  753  ? -25.385 70.495  126.912 1.00 27.19 ? 751  ILE   A N     1 
ATOM   5549  C  CA    . ILE   A 1  753  ? -24.195 71.342  126.976 1.00 27.61 ? 751  ILE   A CA    1 
ATOM   5550  C  C     . ILE   A 1  753  ? -24.424 72.369  128.077 1.00 27.30 ? 751  ILE   A C     1 
ATOM   5551  O  O     . ILE   A 1  753  ? -25.387 73.143  127.999 1.00 27.97 ? 751  ILE   A O     1 
ATOM   5552  C  CB    . ILE   A 1  753  ? -23.920 72.053  125.643 1.00 23.84 ? 751  ILE   A CB    1 
ATOM   5553  C  CG1   . ILE   A 1  753  ? -23.737 71.056  124.496 1.00 23.27 ? 751  ILE   A CG1   1 
ATOM   5554  C  CG2   . ILE   A 1  753  ? -22.684 72.923  125.767 1.00 28.03 ? 751  ILE   A CG2   1 
ATOM   5555  C  CD1   . ILE   A 1  753  ? -22.509 70.185  124.616 1.00 23.48 ? 751  ILE   A CD1   1 
ATOM   5556  N  N     . PRO   A 1  754  ? -23.571 72.431  129.098 1.00 29.51 ? 752  PRO   A N     1 
ATOM   5557  C  CA    . PRO   A 1  754  ? -23.782 73.405  130.173 1.00 30.58 ? 752  PRO   A CA    1 
ATOM   5558  C  C     . PRO   A 1  754  ? -23.673 74.835  129.665 1.00 27.86 ? 752  PRO   A C     1 
ATOM   5559  O  O     . PRO   A 1  754  ? -22.942 75.129  128.717 1.00 27.62 ? 752  PRO   A O     1 
ATOM   5560  C  CB    . PRO   A 1  754  ? -22.657 73.092  131.167 1.00 36.00 ? 752  PRO   A CB    1 
ATOM   5561  C  CG    . PRO   A 1  754  ? -22.150 71.749  130.793 1.00 29.87 ? 752  PRO   A CG    1 
ATOM   5562  C  CD    . PRO   A 1  754  ? -22.366 71.622  129.316 1.00 26.49 ? 752  PRO   A CD    1 
ATOM   5563  N  N     . ALA   A 1  755  ? -24.409 75.732  130.334 1.00 29.38 ? 753  ALA   A N     1 
ATOM   5564  C  CA    . ALA   A 1  755  ? -24.364 77.149  129.986 1.00 29.70 ? 753  ALA   A CA    1 
ATOM   5565  C  C     . ALA   A 1  755  ? -22.949 77.706  130.059 1.00 28.09 ? 753  ALA   A C     1 
ATOM   5566  O  O     . ALA   A 1  755  ? -22.584 78.582  129.269 1.00 31.39 ? 753  ALA   A O     1 
ATOM   5567  C  CB    . ALA   A 1  755  ? -25.277 77.938  130.929 1.00 34.20 ? 753  ALA   A CB    1 
ATOM   5568  N  N     . SER   A 1  756  ? -22.147 77.233  131.012 1.00 28.85 ? 754  SER   A N     1 
ATOM   5569  C  CA    . SER   A 1  756  ? -20.782 77.716  131.116 1.00 29.85 ? 754  SER   A CA    1 
ATOM   5570  C  C     . SER   A 1  756  ? -19.918 77.257  129.951 1.00 28.91 ? 754  SER   A C     1 
ATOM   5571  O  O     . SER   A 1  756  ? -18.932 77.926  129.632 1.00 30.94 ? 754  SER   A O     1 
ATOM   5572  C  CB    . SER   A 1  756  ? -20.181 77.249  132.436 1.00 31.98 ? 754  SER   A CB    1 
ATOM   5573  O  OG    . SER   A 1  756  ? -20.102 75.837  132.492 1.00 32.88 ? 754  SER   A OG    1 
ATOM   5574  N  N     . ALA   A 1  757  ? -20.277 76.145  129.301 1.00 28.66 ? 755  ALA   A N     1 
ATOM   5575  C  CA    . ALA   A 1  757  ? -19.512 75.625  128.177 1.00 24.99 ? 755  ALA   A CA    1 
ATOM   5576  C  C     . ALA   A 1  757  ? -19.933 76.220  126.843 1.00 29.04 ? 755  ALA   A C     1 
ATOM   5577  O  O     . ALA   A 1  757  ? -19.177 76.121  125.876 1.00 27.33 ? 755  ALA   A O     1 
ATOM   5578  C  CB    . ALA   A 1  757  ? -19.647 74.103  128.093 1.00 28.18 ? 755  ALA   A CB    1 
ATOM   5579  N  N     . LEU   A 1  758  ? -21.111 76.832  126.759 1.00 25.52 ? 756  LEU   A N     1 
ATOM   5580  C  CA    . LEU   A 1  758  ? -21.600 77.362  125.489 1.00 25.33 ? 756  LEU   A CA    1 
ATOM   5581  C  C     . LEU   A 1  758  ? -22.327 78.666  125.776 1.00 27.75 ? 756  LEU   A C     1 
ATOM   5582  O  O     . LEU   A 1  758  ? -23.448 78.661  126.291 1.00 29.68 ? 756  LEU   A O     1 
ATOM   5583  C  CB    . LEU   A 1  758  ? -22.512 76.374  124.785 1.00 24.87 ? 756  LEU   A CB    1 
ATOM   5584  C  CG    . LEU   A 1  758  ? -23.108 76.882  123.472 1.00 25.80 ? 756  LEU   A CG    1 
ATOM   5585  C  CD1   . LEU   A 1  758  ? -22.000 77.372  122.534 1.00 25.56 ? 756  LEU   A CD1   1 
ATOM   5586  C  CD2   . LEU   A 1  758  ? -23.924 75.787  122.826 1.00 27.09 ? 756  LEU   A CD2   1 
ATOM   5587  N  N     . GLN   A 1  759  ? -21.679 79.772  125.445 1.00 25.25 ? 757  GLN   A N     1 
ATOM   5588  C  CA    . GLN   A 1  759  ? -22.227 81.100  125.645 1.00 27.59 ? 757  GLN   A CA    1 
ATOM   5589  C  C     . GLN   A 1  759  ? -22.465 81.737  124.287 1.00 28.58 ? 757  GLN   A C     1 
ATOM   5590  O  O     . GLN   A 1  759  ? -21.580 81.730  123.426 1.00 30.14 ? 757  GLN   A O     1 
ATOM   5591  C  CB    . GLN   A 1  759  ? -21.266 81.952  126.472 1.00 26.32 ? 757  GLN   A CB    1 
ATOM   5592  C  CG    . GLN   A 1  759  ? -21.108 81.471  127.893 1.00 27.13 ? 757  GLN   A CG    1 
ATOM   5593  C  CD    . GLN   A 1  759  ? -20.090 82.291  128.651 1.00 27.94 ? 757  GLN   A CD    1 
ATOM   5594  O  OE1   . GLN   A 1  759  ? -20.436 83.274  129.308 1.00 28.51 ? 757  GLN   A OE1   1 
ATOM   5595  N  NE2   . GLN   A 1  759  ? -18.821 81.901  128.552 1.00 28.45 ? 757  GLN   A NE2   1 
ATOM   5596  N  N     . LEU   A 1  760  ? -23.665 82.258  124.091 1.00 27.57 ? 758  LEU   A N     1 
ATOM   5597  C  CA    . LEU   A 1  760  ? -24.043 82.924  122.853 1.00 26.51 ? 758  LEU   A CA    1 
ATOM   5598  C  C     . LEU   A 1  760  ? -23.833 84.418  123.019 1.00 26.18 ? 758  LEU   A C     1 
ATOM   5599  O  O     . LEU   A 1  760  ? -24.342 85.014  123.971 1.00 27.19 ? 758  LEU   A O     1 
ATOM   5600  C  CB    . LEU   A 1  760  ? -25.515 82.668  122.536 1.00 25.56 ? 758  LEU   A CB    1 
ATOM   5601  C  CG    . LEU   A 1  760  ? -25.994 83.352  121.254 1.00 26.46 ? 758  LEU   A CG    1 
ATOM   5602  C  CD1   . LEU   A 1  760  ? -25.519 82.611  120.002 1.00 26.14 ? 758  LEU   A CD1   1 
ATOM   5603  C  CD2   . LEU   A 1  760  ? -27.495 83.497  121.255 1.00 28.70 ? 758  LEU   A CD2   1 
ATOM   5604  N  N     . LEU   A 1  761  ? -23.101 85.024  122.092 1.00 26.03 ? 759  LEU   A N     1 
ATOM   5605  C  CA    A LEU   A 1  761  ? -22.773 86.446  122.149 0.51 27.59 ? 759  LEU   A CA    1 
ATOM   5606  C  CA    B LEU   A 1  761  ? -22.767 86.447  122.148 0.49 27.59 ? 759  LEU   A CA    1 
ATOM   5607  C  C     . LEU   A 1  761  ? -23.172 87.098  120.833 1.00 26.30 ? 759  LEU   A C     1 
ATOM   5608  O  O     . LEU   A 1  761  ? -22.342 87.287  119.938 1.00 26.65 ? 759  LEU   A O     1 
ATOM   5609  C  CB    A LEU   A 1  761  ? -21.292 86.647  122.471 0.51 27.53 ? 759  LEU   A CB    1 
ATOM   5610  C  CB    B LEU   A 1  761  ? -21.277 86.668  122.424 0.49 27.53 ? 759  LEU   A CB    1 
ATOM   5611  C  CG    A LEU   A 1  761  ? -20.874 85.931  123.758 0.51 27.20 ? 759  LEU   A CG    1 
ATOM   5612  C  CG    B LEU   A 1  761  ? -20.623 86.128  123.703 0.49 26.72 ? 759  LEU   A CG    1 
ATOM   5613  C  CD1   A LEU   A 1  761  ? -19.377 85.841  123.880 0.51 25.38 ? 759  LEU   A CD1   1 
ATOM   5614  C  CD1   B LEU   A 1  761  ? -21.488 86.382  124.930 0.49 27.38 ? 759  LEU   A CD1   1 
ATOM   5615  C  CD2   A LEU   A 1  761  ? -21.466 86.627  124.971 0.51 27.48 ? 759  LEU   A CD2   1 
ATOM   5616  C  CD2   B LEU   A 1  761  ? -20.280 84.651  123.572 0.49 27.50 ? 759  LEU   A CD2   1 
ATOM   5617  N  N     . PRO   A 1  762  ? -24.442 87.458  120.679 1.00 25.05 ? 760  PRO   A N     1 
ATOM   5618  C  CA    . PRO   A 1  762  ? -24.862 88.137  119.450 1.00 27.17 ? 760  PRO   A CA    1 
ATOM   5619  C  C     . PRO   A 1  762  ? -24.195 89.499  119.334 1.00 29.77 ? 760  PRO   A C     1 
ATOM   5620  O  O     . PRO   A 1  762  ? -23.798 90.116  120.324 1.00 30.37 ? 760  PRO   A O     1 
ATOM   5621  C  CB    . PRO   A 1  762  ? -26.379 88.288  119.625 1.00 26.85 ? 760  PRO   A CB    1 
ATOM   5622  C  CG    . PRO   A 1  762  ? -26.744 87.334  120.722 1.00 28.09 ? 760  PRO   A CG    1 
ATOM   5623  C  CD    . PRO   A 1  762  ? -25.556 87.257  121.615 1.00 24.67 ? 760  PRO   A CD    1 
ATOM   5624  N  N     . GLY   A 1  763  ? -24.082 89.973  118.107 1.00 26.86 ? 761  GLY   A N     1 
ATOM   5625  C  CA    . GLY   A 1  763  ? -23.530 91.281  117.846 1.00 29.35 ? 761  GLY   A CA    1 
ATOM   5626  C  C     . GLY   A 1  763  ? -22.736 91.273  116.560 1.00 28.25 ? 761  GLY   A C     1 
ATOM   5627  O  O     . GLY   A 1  763  ? -22.693 90.279  115.835 1.00 27.32 ? 761  GLY   A O     1 
ATOM   5628  N  N     . ASP   A 1  764  ? -22.088 92.397  116.279 1.00 30.49 ? 762  ASP   A N     1 
ATOM   5629  C  CA    . ASP   A 1  764  ? -21.406 92.583  115.006 1.00 30.28 ? 762  ASP   A CA    1 
ATOM   5630  C  C     . ASP   A 1  764  ? -19.925 92.214  115.130 1.00 28.60 ? 762  ASP   A C     1 
ATOM   5631  O  O     . ASP   A 1  764  ? -19.521 91.509  116.063 1.00 27.08 ? 762  ASP   A O     1 
ATOM   5632  C  CB    . ASP   A 1  764  ? -21.663 94.003  114.464 1.00 34.36 ? 762  ASP   A CB    1 
ATOM   5633  C  CG    . ASP   A 1  764  ? -21.163 95.102  115.396 1.00 34.92 ? 762  ASP   A CG    1 
ATOM   5634  O  OD1   . ASP   A 1  764  ? -20.240 94.852  116.198 1.00 37.32 ? 762  ASP   A OD1   1 
ATOM   5635  O  OD2   . ASP   A 1  764  ? -21.707 96.227  115.334 1.00 46.72 ? 762  ASP   A OD2   1 
ATOM   5636  N  N     . GLY   A 1  765  ? -19.111 92.682  114.185 1.00 26.26 ? 763  GLY   A N     1 
ATOM   5637  C  CA    . GLY   A 1  765  ? -17.695 92.358  114.185 1.00 27.36 ? 763  GLY   A CA    1 
ATOM   5638  C  C     . GLY   A 1  765  ? -16.960 92.842  115.414 1.00 29.36 ? 763  GLY   A C     1 
ATOM   5639  O  O     . GLY   A 1  765  ? -15.943 92.247  115.790 1.00 30.58 ? 763  GLY   A O     1 
ATOM   5640  N  N     . ARG   A 1  766  ? -17.458 93.901  116.061 1.00 29.19 ? 764  ARG   A N     1 
ATOM   5641  C  CA    . ARG   A 1  766  ? -16.844 94.379  117.296 1.00 32.27 ? 764  ARG   A CA    1 
ATOM   5642  C  C     . ARG   A 1  766  ? -16.878 93.311  118.374 1.00 31.07 ? 764  ARG   A C     1 
ATOM   5643  O  O     . ARG   A 1  766  ? -15.941 93.194  119.169 1.00 30.21 ? 764  ARG   A O     1 
ATOM   5644  C  CB    . ARG   A 1  766  ? -17.588 95.607  117.816 1.00 38.92 ? 764  ARG   A CB    1 
ATOM   5645  C  CG    . ARG   A 1  766  ? -17.375 96.878  117.047 1.00 45.21 ? 764  ARG   A CG    1 
ATOM   5646  C  CD    . ARG   A 1  766  ? -18.258 97.953  117.649 1.00 39.17 ? 764  ARG   A CD    1 
ATOM   5647  N  NE    . ARG   A 1  766  ? -19.668 97.655  117.433 1.00 40.96 ? 764  ARG   A NE    1 
ATOM   5648  C  CZ    . ARG   A 1  766  ? -20.636 97.936  118.292 1.00 42.98 ? 764  ARG   A CZ    1 
ATOM   5649  N  NH1   . ARG   A 1  766  ? -20.377 98.462  119.478 1.00 48.96 ? 764  ARG   A NH1   1 
ATOM   5650  N  NH2   . ARG   A 1  766  ? -21.897 97.683  117.953 1.00 45.29 ? 764  ARG   A NH2   1 
ATOM   5651  N  N     . VAL   A 1  767  ? -17.979 92.562  118.454 1.00 28.50 ? 765  VAL   A N     1 
ATOM   5652  C  CA    . VAL   A 1  767  ? -18.067 91.497  119.443 1.00 29.03 ? 765  VAL   A CA    1 
ATOM   5653  C  C     . VAL   A 1  767  ? -17.108 90.379  119.088 1.00 27.43 ? 765  VAL   A C     1 
ATOM   5654  O  O     . VAL   A 1  767  ? -16.416 89.833  119.957 1.00 28.33 ? 765  VAL   A O     1 
ATOM   5655  C  CB    . VAL   A 1  767  ? -19.521 91.004  119.574 1.00 28.32 ? 765  VAL   A CB    1 
ATOM   5656  C  CG1   . VAL   A 1  767  ? -19.634 89.928  120.648 1.00 29.78 ? 765  VAL   A CG1   1 
ATOM   5657  C  CG2   . VAL   A 1  767  ? -20.437 92.169  119.880 1.00 30.64 ? 765  VAL   A CG2   1 
ATOM   5658  N  N     . GLY   A 1  768  ? -17.048 90.023  117.801 1.00 26.23 ? 766  GLY   A N     1 
ATOM   5659  C  CA    . GLY   A 1  768  ? -16.080 89.031  117.370 1.00 24.61 ? 766  GLY   A CA    1 
ATOM   5660  C  C     . GLY   A 1  768  ? -14.661 89.444  117.702 1.00 26.11 ? 766  GLY   A C     1 
ATOM   5661  O  O     . GLY   A 1  768  ? -13.875 88.653  118.227 1.00 26.23 ? 766  GLY   A O     1 
ATOM   5662  N  N     . ALA   A 1  769  ? -14.321 90.702  117.419 1.00 27.60 ? 767  ALA   A N     1 
ATOM   5663  C  CA    . ALA   A 1  769  ? -12.957 91.169  117.644 1.00 27.00 ? 767  ALA   A CA    1 
ATOM   5664  C  C     . ALA   A 1  769  ? -12.628 91.205  119.130 1.00 26.89 ? 767  ALA   A C     1 
ATOM   5665  O  O     . ALA   A 1  769  ? -11.511 90.855  119.531 1.00 29.29 ? 767  ALA   A O     1 
ATOM   5666  C  CB    . ALA   A 1  769  ? -12.768 92.551  117.020 1.00 26.72 ? 767  ALA   A CB    1 
ATOM   5667  N  N     . ALA   A 1  770  ? -13.591 91.620  119.957 1.00 29.10 ? 768  ALA   A N     1 
ATOM   5668  C  CA    . ALA   A 1  770  ? -13.365 91.656  121.398 1.00 30.02 ? 768  ALA   A CA    1 
ATOM   5669  C  C     . ALA   A 1  770  ? -13.112 90.256  121.933 1.00 30.30 ? 768  ALA   A C     1 
ATOM   5670  O  O     . ALA   A 1  770  ? -12.280 90.061  122.828 1.00 29.39 ? 768  ALA   A O     1 
ATOM   5671  C  CB    . ALA   A 1  770  ? -14.571 92.289  122.090 1.00 29.82 ? 768  ALA   A CB    1 
ATOM   5672  N  N     . LEU   A 1  771  ? -13.818 89.266  121.383 1.00 28.21 ? 769  LEU   A N     1 
ATOM   5673  C  CA    . LEU   A 1  771  ? -13.605 87.880  121.783 1.00 30.61 ? 769  LEU   A CA    1 
ATOM   5674  C  C     . LEU   A 1  771  ? -12.230 87.388  121.351 1.00 28.45 ? 769  LEU   A C     1 
ATOM   5675  O  O     . LEU   A 1  771  ? -11.518 86.741  122.129 1.00 29.04 ? 769  LEU   A O     1 
ATOM   5676  C  CB    . LEU   A 1  771  ? -14.706 87.006  121.184 1.00 26.46 ? 769  LEU   A CB    1 
ATOM   5677  C  CG    . LEU   A 1  771  ? -16.100 87.254  121.753 1.00 26.16 ? 769  LEU   A CG    1 
ATOM   5678  C  CD1   . LEU   A 1  771  ? -17.134 86.435  120.986 1.00 27.65 ? 769  LEU   A CD1   1 
ATOM   5679  C  CD2   . LEU   A 1  771  ? -16.125 86.929  123.237 1.00 27.99 ? 769  LEU   A CD2   1 
ATOM   5680  N  N     . VAL   A 1  772  ? -11.848 87.674  120.104 1.00 24.84 ? 770  VAL   A N     1 
ATOM   5681  C  CA    . VAL   A 1  772  ? -10.547 87.247  119.596 1.00 24.78 ? 770  VAL   A CA    1 
ATOM   5682  C  C     . VAL   A 1  772  ? -9.421  87.829  120.443 1.00 26.82 ? 770  VAL   A C     1 
ATOM   5683  O  O     . VAL   A 1  772  ? -8.414  87.162  120.707 1.00 31.50 ? 770  VAL   A O     1 
ATOM   5684  C  CB    . VAL   A 1  772  ? -10.404 87.621  118.108 1.00 26.22 ? 770  VAL   A CB    1 
ATOM   5685  C  CG1   . VAL   A 1  772  ? -8.975  87.406  117.637 1.00 27.09 ? 770  VAL   A CG1   1 
ATOM   5686  C  CG2   . VAL   A 1  772  ? -11.352 86.787  117.260 1.00 25.99 ? 770  VAL   A CG2   1 
ATOM   5687  N  N     . ALA   A 1  773  ? -9.572  89.078  120.873 1.00 28.92 ? 771  ALA   A N     1 
ATOM   5688  C  CA    . ALA   A 1  773  ? -8.516  89.782  121.590 1.00 28.44 ? 771  ALA   A CA    1 
ATOM   5689  C  C     . ALA   A 1  773  ? -8.435  89.402  123.063 1.00 34.74 ? 771  ALA   A C     1 
ATOM   5690  O  O     . ALA   A 1  773  ? -7.446  89.752  123.720 1.00 35.72 ? 771  ALA   A O     1 
ATOM   5691  C  CB    . ALA   A 1  773  ? -8.722  91.290  121.457 1.00 30.68 ? 771  ALA   A CB    1 
ATOM   5692  N  N     . ALA   A 1  774  ? -9.431  88.695  123.592 1.00 31.42 ? 772  ALA   A N     1 
ATOM   5693  C  CA    . ALA   A 1  774  ? -9.465  88.394  125.019 1.00 33.06 ? 772  ALA   A CA    1 
ATOM   5694  C  C     . ALA   A 1  774  ? -8.332  87.448  125.406 1.00 30.69 ? 772  ALA   A C     1 
ATOM   5695  O  O     . ALA   A 1  774  ? -8.050  86.470  124.715 1.00 33.31 ? 772  ALA   A O     1 
ATOM   5696  C  CB    . ALA   A 1  774  ? -10.815 87.790  125.397 1.00 32.51 ? 772  ALA   A CB    1 
ATOM   5697  N  N     . ALA   A 1  775  ? -7.683  87.741  126.539 1.00 37.52 ? 773  ALA   A N     1 
ATOM   5698  C  CA    . ALA   A 1  775  ? -6.449  87.041  126.884 1.00 39.76 ? 773  ALA   A CA    1 
ATOM   5699  C  C     . ALA   A 1  775  ? -6.664  85.547  127.085 1.00 31.52 ? 773  ALA   A C     1 
ATOM   5700  O  O     . ALA   A 1  775  ? -5.761  84.753  126.808 1.00 34.12 ? 773  ALA   A O     1 
ATOM   5701  C  CB    . ALA   A 1  775  ? -5.811  87.667  128.124 1.00 36.67 ? 773  ALA   A CB    1 
ATOM   5702  N  N     . GLU   A 1  776  ? -7.841  85.138  127.553 1.00 31.16 ? 774  GLU   A N     1 
ATOM   5703  C  CA    . GLU   A 1  776  ? -8.083  83.721  127.805 1.00 27.95 ? 774  GLU   A CA    1 
ATOM   5704  C  C     . GLU   A 1  776  ? -8.518  82.953  126.558 1.00 28.89 ? 774  GLU   A C     1 
ATOM   5705  O  O     . GLU   A 1  776  ? -8.675  81.728  126.621 1.00 31.27 ? 774  GLU   A O     1 
ATOM   5706  C  CB    . GLU   A 1  776  ? -9.107  83.544  128.927 1.00 32.48 ? 774  GLU   A CB    1 
ATOM   5707  C  CG    . GLU   A 1  776  ? -8.722  84.239  130.233 1.00 36.44 ? 774  GLU   A CG    1 
ATOM   5708  C  CD    . GLU   A 1  776  ? -9.189  85.691  130.311 1.00 44.11 ? 774  GLU   A CD    1 
ATOM   5709  O  OE1   . GLU   A 1  776  ? -9.665  86.244  129.294 1.00 36.80 ? 774  GLU   A OE1   1 
ATOM   5710  O  OE2   . GLU   A 1  776  ? -9.074  86.286  131.404 1.00 49.04 ? 774  GLU   A OE2   1 
ATOM   5711  N  N     . THR   A 1  777  ? -8.701  83.627  125.431 1.00 27.24 ? 775  THR   A N     1 
ATOM   5712  C  CA    . THR   A 1  777  ? -9.088  82.937  124.206 1.00 26.61 ? 775  THR   A CA    1 
ATOM   5713  C  C     . THR   A 1  777  ? -7.946  82.054  123.727 1.00 27.33 ? 775  THR   A C     1 
ATOM   5714  O  O     . THR   A 1  777  ? -6.828  82.533  123.496 1.00 29.53 ? 775  THR   A O     1 
ATOM   5715  C  CB    . THR   A 1  777  ? -9.465  83.964  123.153 1.00 25.24 ? 775  THR   A CB    1 
ATOM   5716  O  OG1   . THR   A 1  777  ? -10.711 84.557  123.534 1.00 26.77 ? 775  THR   A OG1   1 
ATOM   5717  C  CG2   . THR   A 1  777  ? -9.599  83.292  121.786 1.00 25.82 ? 775  THR   A CG2   1 
ATOM   5718  N  N     . ALA   A 1  778  ? -8.221  80.759  123.608 1.00 24.95 ? 776  ALA   A N     1 
ATOM   5719  C  CA    . ALA   A 1  778  ? -7.194  79.769  123.327 1.00 23.13 ? 776  ALA   A CA    1 
ATOM   5720  C  C     . ALA   A 1  778  ? -7.219  79.284  121.887 1.00 24.84 ? 776  ALA   A C     1 
ATOM   5721  O  O     . ALA   A 1  778  ? -6.295  78.583  121.465 1.00 24.94 ? 776  ALA   A O     1 
ATOM   5722  C  CB    . ALA   A 1  778  ? -7.343  78.571  124.275 1.00 25.34 ? 776  ALA   A CB    1 
ATOM   5723  N  N     . GLY   A 1  779  ? -8.253  79.632  121.135 1.00 22.75 ? 777  GLY   A N     1 
ATOM   5724  C  CA    . GLY   A 1  779  ? -8.354  79.222  119.756 1.00 20.75 ? 777  GLY   A CA    1 
ATOM   5725  C  C     . GLY   A 1  779  ? -9.499  79.961  119.116 1.00 20.89 ? 777  GLY   A C     1 
ATOM   5726  O  O     . GLY   A 1  779  ? -10.428 80.399  119.800 1.00 22.00 ? 777  GLY   A O     1 
ATOM   5727  N  N     . VAL   A 1  780  ? -9.429  80.130  117.805 1.00 20.77 ? 778  VAL   A N     1 
ATOM   5728  C  CA    . VAL   A 1  780  ? -10.430 80.876  117.063 1.00 20.55 ? 778  VAL   A CA    1 
ATOM   5729  C  C     . VAL   A 1  780  ? -10.838 80.038  115.865 1.00 18.87 ? 778  VAL   A C     1 
ATOM   5730  O  O     . VAL   A 1  780  ? -9.980  79.562  115.112 1.00 19.67 ? 778  VAL   A O     1 
ATOM   5731  C  CB    . VAL   A 1  780  ? -9.905  82.257  116.623 1.00 21.52 ? 778  VAL   A CB    1 
ATOM   5732  C  CG1   . VAL   A 1  780  ? -10.962 82.990  115.826 1.00 22.00 ? 778  VAL   A CG1   1 
ATOM   5733  C  CG2   . VAL   A 1  780  ? -9.530  83.089  117.846 1.00 22.21 ? 778  VAL   A CG2   1 
ATOM   5734  N  N     . MET   A 1  781  ? -12.136 79.825  115.711 1.00 19.28 ? 779  MET   A N     1 
ATOM   5735  C  CA    . MET   A 1  781  ? -12.683 79.170  114.531 1.00 17.66 ? 779  MET   A CA    1 
ATOM   5736  C  C     . MET   A 1  781  ? -13.490 80.231  113.808 1.00 20.42 ? 779  MET   A C     1 
ATOM   5737  O  O     . MET   A 1  781  ? -14.499 80.714  114.333 1.00 19.59 ? 779  MET   A O     1 
ATOM   5738  C  CB    . MET   A 1  781  ? -13.555 77.987  114.933 1.00 21.33 ? 779  MET   A CB    1 
ATOM   5739  C  CG    . MET   A 1  781  ? -12.812 76.957  115.755 1.00 19.92 ? 779  MET   A CG    1 
ATOM   5740  S  SD    . MET   A 1  781  ? -13.892 75.678  116.383 1.00 21.82 ? 779  MET   A SD    1 
ATOM   5741  C  CE    . MET   A 1  781  ? -14.123 74.712  114.900 1.00 21.06 ? 779  MET   A CE    1 
ATOM   5742  N  N     . PHE   A 1  782  ? -13.030 80.609  112.621 1.00 21.14 ? 780  PHE   A N     1 
ATOM   5743  C  CA    . PHE   A 1  782  ? -13.643 81.664  111.835 1.00 20.92 ? 780  PHE   A CA    1 
ATOM   5744  C  C     . PHE   A 1  782  ? -14.087 81.099  110.499 1.00 20.42 ? 780  PHE   A C     1 
ATOM   5745  O  O     . PHE   A 1  782  ? -13.294 80.469  109.791 1.00 18.77 ? 780  PHE   A O     1 
ATOM   5746  C  CB    . PHE   A 1  782  ? -12.639 82.784  111.553 1.00 20.87 ? 780  PHE   A CB    1 
ATOM   5747  C  CG    . PHE   A 1  782  ? -13.183 83.853  110.662 1.00 21.02 ? 780  PHE   A CG    1 
ATOM   5748  C  CD1   . PHE   A 1  782  ? -14.054 84.800  111.161 1.00 19.85 ? 780  PHE   A CD1   1 
ATOM   5749  C  CD2   . PHE   A 1  782  ? -12.863 83.889  109.317 1.00 20.48 ? 780  PHE   A CD2   1 
ATOM   5750  C  CE1   . PHE   A 1  782  ? -14.578 85.784  110.352 1.00 21.54 ? 780  PHE   A CE1   1 
ATOM   5751  C  CE2   . PHE   A 1  782  ? -13.381 84.868  108.506 1.00 21.25 ? 780  PHE   A CE2   1 
ATOM   5752  C  CZ    . PHE   A 1  782  ? -14.240 85.817  109.022 1.00 19.47 ? 780  PHE   A CZ    1 
ATOM   5753  N  N     . THR   A 1  783  ? -15.333 81.371  110.138 1.00 17.52 ? 781  THR   A N     1 
ATOM   5754  C  CA    . THR   A 1  783  ? -15.774 81.190  108.765 1.00 18.55 ? 781  THR   A CA    1 
ATOM   5755  C  C     . THR   A 1  783  ? -16.405 82.501  108.335 1.00 19.42 ? 781  THR   A C     1 
ATOM   5756  O  O     . THR   A 1  783  ? -17.244 83.053  109.051 1.00 19.76 ? 781  THR   A O     1 
ATOM   5757  C  CB    . THR   A 1  783  ? -16.739 80.013  108.641 1.00 20.83 ? 781  THR   A CB    1 
ATOM   5758  O  OG1   . THR   A 1  783  ? -16.089 78.831  109.123 1.00 20.00 ? 781  THR   A OG1   1 
ATOM   5759  C  CG2   . THR   A 1  783  ? -17.109 79.789  107.183 1.00 19.73 ? 781  THR   A CG2   1 
ATOM   5760  N  N     . GLY   A 1  784  ? -15.961 83.023  107.198 1.00 19.28 ? 782  GLY   A N     1 
ATOM   5761  C  CA    . GLY   A 1  784  ? -16.384 84.348  106.793 1.00 19.53 ? 782  GLY   A CA    1 
ATOM   5762  C  C     . GLY   A 1  784  ? -15.522 84.833  105.651 1.00 17.69 ? 782  GLY   A C     1 
ATOM   5763  O  O     . GLY   A 1  784  ? -14.864 84.041  104.977 1.00 19.44 ? 782  GLY   A O     1 
ATOM   5764  N  N     . SER   A 1  785  ? -15.525 86.145  105.454 1.00 19.58 ? 783  SER   A N     1 
ATOM   5765  C  CA    . SER   A 1  785  ? -14.785 86.704  104.330 1.00 20.75 ? 783  SER   A CA    1 
ATOM   5766  C  C     . SER   A 1  785  ? -13.279 86.664  104.573 1.00 21.50 ? 783  SER   A C     1 
ATOM   5767  O  O     . SER   A 1  785  ? -12.800 86.704  105.711 1.00 21.27 ? 783  SER   A O     1 
ATOM   5768  C  CB    . SER   A 1  785  ? -15.228 88.142  104.072 1.00 24.84 ? 783  SER   A CB    1 
ATOM   5769  O  OG    . SER   A 1  785  ? -14.890 88.978  105.166 1.00 23.96 ? 783  SER   A OG    1 
ATOM   5770  N  N     . THR   A 1  786  ? -12.527 86.583  103.474 1.00 21.01 ? 784  THR   A N     1 
ATOM   5771  C  CA    . THR   A 1  786  ? -11.074 86.595  103.568 1.00 22.29 ? 784  THR   A CA    1 
ATOM   5772  C  C     . THR   A 1  786  ? -10.570 87.881  104.210 1.00 20.95 ? 784  THR   A C     1 
ATOM   5773  O  O     . THR   A 1  786  ? -9.625  87.855  105.010 1.00 20.89 ? 784  THR   A O     1 
ATOM   5774  C  CB    . THR   A 1  786  ? -10.483 86.409  102.172 1.00 21.58 ? 784  THR   A CB    1 
ATOM   5775  O  OG1   . THR   A 1  786  ? -10.954 85.167  101.634 1.00 22.47 ? 784  THR   A OG1   1 
ATOM   5776  C  CG2   . THR   A 1  786  ? -8.972  86.386  102.246 1.00 23.74 ? 784  THR   A CG2   1 
ATOM   5777  N  N     . GLU   A 1  787  ? -11.202 89.013  103.888 1.00 24.88 ? 785  GLU   A N     1 
ATOM   5778  C  CA    . GLU   A 1  787  ? -10.756 90.294  104.425 1.00 22.38 ? 785  GLU   A CA    1 
ATOM   5779  C  C     . GLU   A 1  787  ? -10.917 90.343  105.937 1.00 23.05 ? 785  GLU   A C     1 
ATOM   5780  O  O     . GLU   A 1  787  ? -10.054 90.874  106.641 1.00 23.36 ? 785  GLU   A O     1 
ATOM   5781  C  CB    . GLU   A 1  787  ? -11.525 91.444  103.770 1.00 28.03 ? 785  GLU   A CB    1 
ATOM   5782  N  N     . VAL   A 1  788  ? -12.016 89.797  106.456 1.00 21.74 ? 786  VAL   A N     1 
ATOM   5783  C  CA    . VAL   A 1  788  ? -12.178 89.775  107.908 1.00 21.18 ? 786  VAL   A CA    1 
ATOM   5784  C  C     . VAL   A 1  788  ? -11.197 88.800  108.545 1.00 22.53 ? 786  VAL   A C     1 
ATOM   5785  O  O     . VAL   A 1  788  ? -10.594 89.095  109.583 1.00 21.30 ? 786  VAL   A O     1 
ATOM   5786  C  CB    . VAL   A 1  788  ? -13.637 89.477  108.284 1.00 20.57 ? 786  VAL   A CB    1 
ATOM   5787  C  CG1   . VAL   A 1  788  ? -13.749 89.213  109.775 1.00 22.94 ? 786  VAL   A CG1   1 
ATOM   5788  C  CG2   . VAL   A 1  788  ? -14.497 90.661  107.913 1.00 23.17 ? 786  VAL   A CG2   1 
ATOM   5789  N  N     . ALA   A 1  789  ? -11.004 87.632  107.934 1.00 20.93 ? 787  ALA   A N     1 
ATOM   5790  C  CA    . ALA   A 1  789  ? -10.028 86.685  108.462 1.00 19.23 ? 787  ALA   A CA    1 
ATOM   5791  C  C     . ALA   A 1  789  ? -8.661  87.336  108.582 1.00 20.34 ? 787  ALA   A C     1 
ATOM   5792  O  O     . ALA   A 1  789  ? -7.929  87.087  109.545 1.00 20.75 ? 787  ALA   A O     1 
ATOM   5793  C  CB    . ALA   A 1  789  ? -9.948  85.459  107.554 1.00 19.17 ? 787  ALA   A CB    1 
ATOM   5794  N  N     . ARG   A 1  790  ? -8.310  88.187  107.617 1.00 21.06 ? 788  ARG   A N     1 
ATOM   5795  C  CA    . ARG   A 1  790  ? -7.021  88.865  107.654 1.00 21.48 ? 788  ARG   A CA    1 
ATOM   5796  C  C     . ARG   A 1  790  ? -6.928  89.806  108.851 1.00 21.51 ? 788  ARG   A C     1 
ATOM   5797  O  O     . ARG   A 1  790  ? -5.868  89.920  109.477 1.00 22.20 ? 788  ARG   A O     1 
ATOM   5798  C  CB    . ARG   A 1  790  ? -6.801  89.602  106.332 1.00 23.47 ? 788  ARG   A CB    1 
ATOM   5799  C  CG    . ARG   A 1  790  ? -5.451  90.299  106.221 1.00 25.06 ? 788  ARG   A CG    1 
ATOM   5800  C  CD    . ARG   A 1  790  ? -5.194  90.791  104.794 1.00 24.36 ? 788  ARG   A CD    1 
ATOM   5801  N  NE    . ARG   A 1  790  ? -5.153  89.694  103.830 1.00 23.25 ? 788  ARG   A NE    1 
ATOM   5802  C  CZ    . ARG   A 1  790  ? -5.976  89.549  102.798 1.00 23.29 ? 788  ARG   A CZ    1 
ATOM   5803  N  NH1   . ARG   A 1  790  ? -6.927  90.432  102.534 1.00 26.87 ? 788  ARG   A NH1   1 
ATOM   5804  N  NH2   . ARG   A 1  790  ? -5.841  88.488  102.008 1.00 24.39 ? 788  ARG   A NH2   1 
ATOM   5805  N  N     . LEU   A 1  791  ? -8.038  90.466  109.205 1.00 23.39 ? 789  LEU   A N     1 
ATOM   5806  C  CA    . LEU   A 1  791  ? -8.054  91.287  110.408 1.00 23.16 ? 789  LEU   A CA    1 
ATOM   5807  C  C     . LEU   A 1  791  ? -7.877  90.430  111.655 1.00 23.00 ? 789  LEU   A C     1 
ATOM   5808  O  O     . LEU   A 1  791  ? -7.122  90.788  112.566 1.00 24.13 ? 789  LEU   A O     1 
ATOM   5809  C  CB    . LEU   A 1  791  ? -9.360  92.065  110.482 1.00 23.67 ? 789  LEU   A CB    1 
ATOM   5810  C  CG    . LEU   A 1  791  ? -9.611  93.092  109.373 1.00 27.80 ? 789  LEU   A CG    1 
ATOM   5811  C  CD1   . LEU   A 1  791  ? -11.013 93.656  109.480 1.00 28.18 ? 789  LEU   A CD1   1 
ATOM   5812  C  CD2   . LEU   A 1  791  ? -8.582  94.195  109.433 1.00 29.94 ? 789  LEU   A CD2   1 
ATOM   5813  N  N     . ILE   A 1  792  ? -8.558  89.285  111.707 1.00 22.36 ? 790  ILE   A N     1 
ATOM   5814  C  CA    . ILE   A 1  792  ? -8.385  88.376  112.838 1.00 23.59 ? 790  ILE   A CA    1 
ATOM   5815  C  C     . ILE   A 1  792  ? -6.953  87.859  112.904 1.00 24.26 ? 790  ILE   A C     1 
ATOM   5816  O  O     . ILE   A 1  792  ? -6.352  87.783  113.985 1.00 25.43 ? 790  ILE   A O     1 
ATOM   5817  C  CB    . ILE   A 1  792  ? -9.418  87.238  112.764 1.00 23.23 ? 790  ILE   A CB    1 
ATOM   5818  C  CG1   . ILE   A 1  792  ? -10.805 87.813  113.002 1.00 22.67 ? 790  ILE   A CG1   1 
ATOM   5819  C  CG2   . ILE   A 1  792  ? -9.074  86.126  113.762 1.00 23.89 ? 790  ILE   A CG2   1 
ATOM   5820  C  CD1   . ILE   A 1  792  ? -11.905 86.867  112.671 1.00 22.21 ? 790  ILE   A CD1   1 
ATOM   5821  N  N     . GLN   A 1  793  ? -6.384  87.504  111.752 1.00 21.79 ? 791  GLN   A N     1 
ATOM   5822  C  CA    . GLN   A 1  793  ? -4.999  87.063  111.705 1.00 22.06 ? 791  GLN   A CA    1 
ATOM   5823  C  C     . GLN   A 1  793  ? -4.081  88.116  112.309 1.00 21.91 ? 791  GLN   A C     1 
ATOM   5824  O  O     . GLN   A 1  793  ? -3.169  87.793  113.075 1.00 24.51 ? 791  GLN   A O     1 
ATOM   5825  C  CB    . GLN   A 1  793  ? -4.619  86.774  110.251 1.00 24.35 ? 791  GLN   A CB    1 
ATOM   5826  C  CG    . GLN   A 1  793  ? -3.165  86.390  110.039 1.00 23.32 ? 791  GLN   A CG    1 
ATOM   5827  C  CD    . GLN   A 1  793  ? -2.769  86.473  108.576 1.00 23.88 ? 791  GLN   A CD    1 
ATOM   5828  O  OE1   . GLN   A 1  793  ? -3.223  87.359  107.847 1.00 27.68 ? 791  GLN   A OE1   1 
ATOM   5829  N  NE2   . GLN   A 1  793  ? -1.939  85.538  108.134 1.00 26.05 ? 791  GLN   A NE2   1 
ATOM   5830  N  N     . ALA   A 1  794  ? -4.335  89.389  112.001 1.00 23.16 ? 792  ALA   A N     1 
ATOM   5831  C  CA    . ALA   A 1  794  ? -3.502  90.454  112.548 1.00 26.73 ? 792  ALA   A CA    1 
ATOM   5832  C  C     . ALA   A 1  794  ? -3.674  90.570  114.058 1.00 26.97 ? 792  ALA   A C     1 
ATOM   5833  O  O     . ALA   A 1  794  ? -2.688  90.741  114.784 1.00 29.98 ? 792  ALA   A O     1 
ATOM   5834  C  CB    . ALA   A 1  794  ? -3.829  91.773  111.853 1.00 26.82 ? 792  ALA   A CB    1 
ATOM   5835  N  N     . GLN   A 1  795  ? -4.917  90.470  114.546 1.00 24.93 ? 793  GLN   A N     1 
ATOM   5836  C  CA    . GLN   A 1  795  ? -5.164  90.503  115.989 1.00 25.70 ? 793  GLN   A CA    1 
ATOM   5837  C  C     . GLN   A 1  795  ? -4.393  89.405  116.705 1.00 27.11 ? 793  GLN   A C     1 
ATOM   5838  O  O     . GLN   A 1  795  ? -3.781  89.641  117.754 1.00 29.28 ? 793  GLN   A O     1 
ATOM   5839  C  CB    . GLN   A 1  795  ? -6.648  90.286  116.263 1.00 29.03 ? 793  GLN   A CB    1 
ATOM   5840  C  CG    . GLN   A 1  795  ? -7.561  91.477  116.138 1.00 32.29 ? 793  GLN   A CG    1 
ATOM   5841  C  CD    . GLN   A 1  795  ? -8.951  91.146  116.668 1.00 35.59 ? 793  GLN   A CD    1 
ATOM   5842  O  OE1   . GLN   A 1  795  ? -9.740  90.473  115.998 1.00 35.89 ? 793  GLN   A OE1   1 
ATOM   5843  N  NE2   . GLN   A 1  795  ? -9.243  91.585  117.883 1.00 30.58 ? 793  GLN   A NE2   1 
ATOM   5844  N  N     . LEU   A 1  796  ? -4.447  88.180  116.173 1.00 24.11 ? 794  LEU   A N     1 
ATOM   5845  C  CA    . LEU   A 1  796  ? -3.826  87.050  116.848 1.00 26.57 ? 794  LEU   A CA    1 
ATOM   5846  C  C     . LEU   A 1  796  ? -2.309  87.063  116.752 1.00 27.47 ? 794  LEU   A C     1 
ATOM   5847  O  O     . LEU   A 1  796  ? -1.643  86.412  117.565 1.00 31.80 ? 794  LEU   A O     1 
ATOM   5848  C  CB    . LEU   A 1  796  ? -4.366  85.732  116.296 1.00 24.72 ? 794  LEU   A CB    1 
ATOM   5849  C  CG    . LEU   A 1  796  ? -5.823  85.394  116.615 1.00 22.53 ? 794  LEU   A CG    1 
ATOM   5850  C  CD1   . LEU   A 1  796  ? -6.234  84.069  115.973 1.00 24.65 ? 794  LEU   A CD1   1 
ATOM   5851  C  CD2   . LEU   A 1  796  ? -6.009  85.336  118.125 1.00 23.56 ? 794  LEU   A CD2   1 
ATOM   5852  N  N     . ALA   A 1  797  ? -1.746  87.779  115.784 1.00 25.99 ? 795  ALA   A N     1 
ATOM   5853  C  CA    . ALA   A 1  797  ? -0.296  87.806  115.672 1.00 28.30 ? 795  ALA   A CA    1 
ATOM   5854  C  C     . ALA   A 1  797  ? 0.340   88.507  116.865 1.00 29.73 ? 795  ALA   A C     1 
ATOM   5855  O  O     . ALA   A 1  797  ? 1.515   88.268  117.158 1.00 38.50 ? 795  ALA   A O     1 
ATOM   5856  C  CB    . ALA   A 1  797  ? 0.122   88.444  114.347 1.00 28.28 ? 795  ALA   A CB    1 
ATOM   5857  N  N     . ASP   A 1  798  ? -0.423  89.343  117.572 1.00 32.40 ? 796  ASP   A N     1 
ATOM   5858  C  CA    . ASP   A 1  798  ? 0.036   89.957  118.812 1.00 35.61 ? 796  ASP   A CA    1 
ATOM   5859  C  C     . ASP   A 1  798  ? 0.067   88.984  119.976 1.00 38.92 ? 796  ASP   A C     1 
ATOM   5860  O  O     . ASP   A 1  798  ? 0.688   89.296  120.997 1.00 34.73 ? 796  ASP   A O     1 
ATOM   5861  C  CB    . ASP   A 1  798  ? -0.934  91.063  119.232 1.00 30.27 ? 796  ASP   A CB    1 
ATOM   5862  C  CG    . ASP   A 1  798  ? -0.880  92.265  118.326 1.00 46.91 ? 796  ASP   A CG    1 
ATOM   5863  O  OD1   . ASP   A 1  798  ? 0.120   92.401  117.591 1.00 47.90 ? 796  ASP   A OD1   1 
ATOM   5864  O  OD2   . ASP   A 1  798  ? -1.833  93.078  118.359 1.00 45.35 ? 796  ASP   A OD2   1 
ATOM   5865  N  N     . ARG   A 1  799  ? -0.572  87.826  119.855 1.00 28.99 ? 797  ARG   A N     1 
ATOM   5866  C  CA    A ARG   A 1  799  ? -0.908  86.993  120.997 0.46 30.25 ? 797  ARG   A CA    1 
ATOM   5867  C  CA    B ARG   A 1  799  ? -0.889  87.004  121.010 0.54 30.23 ? 797  ARG   A CA    1 
ATOM   5868  C  C     . ARG   A 1  799  ? -0.136  85.679  120.990 1.00 27.36 ? 797  ARG   A C     1 
ATOM   5869  O  O     . ARG   A 1  799  ? 0.151   85.110  119.933 1.00 28.81 ? 797  ARG   A O     1 
ATOM   5870  C  CB    A ARG   A 1  799  ? -2.403  86.687  120.966 0.46 35.12 ? 797  ARG   A CB    1 
ATOM   5871  C  CB    B ARG   A 1  799  ? -2.399  86.747  121.101 0.54 35.24 ? 797  ARG   A CB    1 
ATOM   5872  C  CG    A ARG   A 1  799  ? -3.253  87.926  120.767 0.46 34.04 ? 797  ARG   A CG    1 
ATOM   5873  C  CG    B ARG   A 1  799  ? -3.236  88.015  121.283 0.54 33.62 ? 797  ARG   A CG    1 
ATOM   5874  C  CD    A ARG   A 1  799  ? -3.667  88.496  122.104 0.46 33.29 ? 797  ARG   A CD    1 
ATOM   5875  C  CD    B ARG   A 1  799  ? -4.687  87.691  121.629 0.54 36.39 ? 797  ARG   A CD    1 
ATOM   5876  N  NE    A ARG   A 1  799  ? -4.291  87.466  122.924 0.46 36.94 ? 797  ARG   A NE    1 
ATOM   5877  N  NE    B ARG   A 1  799  ? -4.755  86.723  122.715 0.54 37.94 ? 797  ARG   A NE    1 
ATOM   5878  C  CZ    A ARG   A 1  799  ? -5.487  86.944  122.688 0.46 34.55 ? 797  ARG   A CZ    1 
ATOM   5879  C  CZ    B ARG   A 1  799  ? -5.468  85.605  122.691 0.54 31.95 ? 797  ARG   A CZ    1 
ATOM   5880  N  NH1   A ARG   A 1  799  ? -6.228  87.343  121.667 0.46 36.62 ? 797  ARG   A NH1   1 
ATOM   5881  N  NH1   B ARG   A 1  799  ? -6.309  85.338  121.704 0.54 27.09 ? 797  ARG   A NH1   1 
ATOM   5882  N  NH2   A ARG   A 1  799  ? -5.947  85.989  123.491 0.46 37.67 ? 797  ARG   A NH2   1 
ATOM   5883  N  NH2   B ARG   A 1  799  ? -5.346  84.738  123.694 0.54 33.10 ? 797  ARG   A NH2   1 
ATOM   5884  N  N     . LEU   A 1  800  ? 0.181   85.201  122.192 1.00 28.14 ? 798  LEU   A N     1 
ATOM   5885  C  CA    . LEU   A 1  800  ? 0.726   83.871  122.407 1.00 31.07 ? 798  LEU   A CA    1 
ATOM   5886  C  C     . LEU   A 1  800  ? -0.049  83.225  123.545 1.00 25.19 ? 798  LEU   A C     1 
ATOM   5887  O  O     . LEU   A 1  800  ? -0.564  83.910  124.430 1.00 30.24 ? 798  LEU   A O     1 
ATOM   5888  C  CB    . LEU   A 1  800  ? 2.202   83.914  122.801 1.00 30.05 ? 798  LEU   A CB    1 
ATOM   5889  C  CG    . LEU   A 1  800  ? 3.196   84.400  121.751 1.00 29.42 ? 798  LEU   A CG    1 
ATOM   5890  C  CD1   . LEU   A 1  800  ? 4.577   84.540  122.368 1.00 31.01 ? 798  LEU   A CD1   1 
ATOM   5891  C  CD2   . LEU   A 1  800  ? 3.217   83.438  120.572 1.00 31.28 ? 798  LEU   A CD2   1 
ATOM   5892  N  N     . SER   A 1  801  ? -0.138  81.898  123.501 1.00 28.95 ? 799  SER   A N     1 
ATOM   5893  C  CA    . SER   A 1  801  ? -0.737  81.136  124.583 1.00 28.74 ? 799  SER   A CA    1 
ATOM   5894  C  C     . SER   A 1  801  ? 0.132   81.262  125.831 1.00 36.23 ? 799  SER   A C     1 
ATOM   5895  O  O     . SER   A 1  801  ? 1.266   81.743  125.765 1.00 33.59 ? 799  SER   A O     1 
ATOM   5896  C  CB    . SER   A 1  801  ? -0.816  79.667  124.183 1.00 32.06 ? 799  SER   A CB    1 
ATOM   5897  O  OG    . SER   A 1  801  ? 0.476   79.088  124.201 1.00 32.78 ? 799  SER   A OG    1 
ATOM   5898  N  N     . PRO   A 1  802  ? -0.376  80.841  126.994 1.00 32.49 ? 800  PRO   A N     1 
ATOM   5899  C  CA    . PRO   A 1  802  ? 0.477   80.840  128.196 1.00 36.24 ? 800  PRO   A CA    1 
ATOM   5900  C  C     . PRO   A 1  802  ? 1.743   80.022  128.037 1.00 36.69 ? 800  PRO   A C     1 
ATOM   5901  O  O     . PRO   A 1  802  ? 2.739   80.298  128.719 1.00 42.07 ? 800  PRO   A O     1 
ATOM   5902  C  CB    . PRO   A 1  802  ? -0.444  80.260  129.276 1.00 39.84 ? 800  PRO   A CB    1 
ATOM   5903  C  CG    . PRO   A 1  802  ? -1.811  80.616  128.821 1.00 40.12 ? 800  PRO   A CG    1 
ATOM   5904  C  CD    . PRO   A 1  802  ? -1.778  80.522  127.320 1.00 33.70 ? 800  PRO   A CD    1 
ATOM   5905  N  N     . ALA   A 1  803  ? 1.735   79.020  127.163 1.00 36.69 ? 801  ALA   A N     1 
ATOM   5906  C  CA    . ALA   A 1  803  ? 2.932   78.255  126.846 1.00 38.87 ? 801  ALA   A CA    1 
ATOM   5907  C  C     . ALA   A 1  803  ? 3.825   78.944  125.824 1.00 41.20 ? 801  ALA   A C     1 
ATOM   5908  O  O     . ALA   A 1  803  ? 4.853   78.375  125.448 1.00 39.88 ? 801  ALA   A O     1 
ATOM   5909  C  CB    . ALA   A 1  803  ? 2.551   76.864  126.331 1.00 41.09 ? 801  ALA   A CB    1 
ATOM   5910  N  N     . GLY   A 1  804  ? 3.454   80.131  125.350 1.00 39.08 ? 802  GLY   A N     1 
ATOM   5911  C  CA    . GLY   A 1  804  ? 4.275   80.836  124.385 1.00 31.30 ? 802  GLY   A CA    1 
ATOM   5912  C  C     . GLY   A 1  804  ? 4.156   80.366  122.954 1.00 34.77 ? 802  GLY   A C     1 
ATOM   5913  O  O     . GLY   A 1  804  ? 5.131   80.440  122.202 1.00 33.05 ? 802  GLY   A O     1 
ATOM   5914  N  N     . ARG   A 1  805  ? 2.987   79.899  122.537 1.00 32.68 ? 803  ARG   A N     1 
ATOM   5915  C  CA    . ARG   A 1  805  ? 2.801   79.392  121.188 1.00 33.10 ? 803  ARG   A CA    1 
ATOM   5916  C  C     . ARG   A 1  805  ? 1.636   80.112  120.527 1.00 24.06 ? 803  ARG   A C     1 
ATOM   5917  O  O     . ARG   A 1  805  ? 0.795   80.699  121.215 1.00 27.62 ? 803  ARG   A O     1 
ATOM   5918  C  CB    . ARG   A 1  805  ? 2.555   77.876  121.215 1.00 34.23 ? 803  ARG   A CB    1 
ATOM   5919  C  CG    . ARG   A 1  805  ? 3.735   77.087  121.784 1.00 35.78 ? 803  ARG   A CG    1 
ATOM   5920  C  CD    . ARG   A 1  805  ? 5.045   77.426  121.059 1.00 34.58 ? 803  ARG   A CD    1 
ATOM   5921  N  NE    . ARG   A 1  805  ? 6.189   76.715  121.631 1.00 33.84 ? 803  ARG   A NE    1 
ATOM   5922  C  CZ    . ARG   A 1  805  ? 7.067   77.240  122.475 1.00 38.11 ? 803  ARG   A CZ    1 
ATOM   5923  N  NH1   . ARG   A 1  805  ? 6.989   78.503  122.864 1.00 35.14 ? 803  ARG   A NH1   1 
ATOM   5924  N  NH2   . ARG   A 1  805  ? 8.049   76.476  122.946 1.00 47.21 ? 803  ARG   A NH2   1 
ATOM   5925  N  N     . PRO   A 1  806  ? 1.581   80.129  119.193 1.00 26.76 ? 804  PRO   A N     1 
ATOM   5926  C  CA    . PRO   A 1  806  ? 0.501   80.862  118.519 1.00 26.78 ? 804  PRO   A CA    1 
ATOM   5927  C  C     . PRO   A 1  806  ? -0.867  80.294  118.867 1.00 26.21 ? 804  PRO   A C     1 
ATOM   5928  O  O     . PRO   A 1  806  ? -1.030  79.090  119.068 1.00 24.90 ? 804  PRO   A O     1 
ATOM   5929  C  CB    . PRO   A 1  806  ? 0.808   80.659  117.032 1.00 27.88 ? 804  PRO   A CB    1 
ATOM   5930  C  CG    . PRO   A 1  806  ? 2.273   80.384  116.984 1.00 29.88 ? 804  PRO   A CG    1 
ATOM   5931  C  CD    . PRO   A 1  806  ? 2.573   79.613  118.236 1.00 29.69 ? 804  PRO   A CD    1 
ATOM   5932  N  N     . ILE   A 1  807  ? -1.854  81.185  118.929 1.00 23.74 ? 805  ILE   A N     1 
ATOM   5933  C  CA    . ILE   A 1  807  ? -3.249  80.797  119.135 1.00 23.60 ? 805  ILE   A CA    1 
ATOM   5934  C  C     . ILE   A 1  807  ? -3.784  80.174  117.853 1.00 21.56 ? 805  ILE   A C     1 
ATOM   5935  O  O     . ILE   A 1  807  ? -3.815  80.844  116.808 1.00 24.73 ? 805  ILE   A O     1 
ATOM   5936  C  CB    . ILE   A 1  807  ? -4.096  82.012  119.529 1.00 24.16 ? 805  ILE   A CB    1 
ATOM   5937  C  CG1   . ILE   A 1  807  ? -3.496  82.684  120.762 1.00 27.80 ? 805  ILE   A CG1   1 
ATOM   5938  C  CG2   . ILE   A 1  807  ? -5.555  81.601  119.753 1.00 25.82 ? 805  ILE   A CG2   1 
ATOM   5939  C  CD1   . ILE   A 1  807  ? -3.402  81.783  121.969 1.00 30.65 ? 805  ILE   A CD1   1 
ATOM   5940  N  N     . PRO   A 1  808  ? -4.215  78.910  117.874 1.00 22.62 ? 806  PRO   A N     1 
ATOM   5941  C  CA    . PRO   A 1  808  ? -4.701  78.279  116.638 1.00 22.61 ? 806  PRO   A CA    1 
ATOM   5942  C  C     . PRO   A 1  808  ? -5.884  79.024  116.034 1.00 20.92 ? 806  PRO   A C     1 
ATOM   5943  O  O     . PRO   A 1  808  ? -6.818  79.431  116.731 1.00 22.38 ? 806  PRO   A O     1 
ATOM   5944  C  CB    . PRO   A 1  808  ? -5.110  76.877  117.098 1.00 22.72 ? 806  PRO   A CB    1 
ATOM   5945  C  CG    . PRO   A 1  808  ? -4.253  76.619  118.301 1.00 27.09 ? 806  PRO   A CG    1 
ATOM   5946  C  CD    . PRO   A 1  808  ? -4.157  77.953  118.991 1.00 24.75 ? 806  PRO   A CD    1 
ATOM   5947  N  N     . LEU   A 1  809  ? -5.836  79.178  114.715 1.00 21.06 ? 807  LEU   A N     1 
ATOM   5948  C  CA    . LEU   A 1  809  ? -6.891  79.837  113.961 1.00 22.12 ? 807  LEU   A CA    1 
ATOM   5949  C  C     . LEU   A 1  809  ? -7.272  78.926  112.809 1.00 22.35 ? 807  LEU   A C     1 
ATOM   5950  O  O     . LEU   A 1  809  ? -6.419  78.568  111.988 1.00 21.75 ? 807  LEU   A O     1 
ATOM   5951  C  CB    . LEU   A 1  809  ? -6.407  81.178  113.407 1.00 22.14 ? 807  LEU   A CB    1 
ATOM   5952  C  CG    . LEU   A 1  809  ? -7.367  81.839  112.418 1.00 22.63 ? 807  LEU   A CG    1 
ATOM   5953  C  CD1   . LEU   A 1  809  ? -8.667  82.196  113.118 1.00 22.25 ? 807  LEU   A CD1   1 
ATOM   5954  C  CD2   . LEU   A 1  809  ? -6.727  83.068  111.804 1.00 25.06 ? 807  LEU   A CD2   1 
ATOM   5955  N  N     . ILE   A 1  810  ? -8.542  78.531  112.760 1.00 18.30 ? 808  ILE   A N     1 
ATOM   5956  C  CA    . ILE   A 1  810  ? -9.119  77.950  111.560 1.00 20.10 ? 808  ILE   A CA    1 
ATOM   5957  C  C     . ILE   A 1  810  ? -9.875  79.075  110.890 1.00 20.10 ? 808  ILE   A C     1 
ATOM   5958  O  O     . ILE   A 1  810  ? -10.785 79.657  111.490 1.00 21.42 ? 808  ILE   A O     1 
ATOM   5959  C  CB    . ILE   A 1  810  ? -10.060 76.783  111.881 1.00 17.64 ? 808  ILE   A CB    1 
ATOM   5960  C  CG1   . ILE   A 1  810  ? -9.341  75.703  112.681 1.00 20.60 ? 808  ILE   A CG1   1 
ATOM   5961  C  CG2   . ILE   A 1  810  ? -10.562 76.181  110.570 1.00 20.83 ? 808  ILE   A CG2   1 
ATOM   5962  C  CD1   . ILE   A 1  810  ? -10.225 74.489  112.979 1.00 22.62 ? 808  ILE   A CD1   1 
ATOM   5963  N  N     . ALA   A 1  811  ? -9.495  79.403  109.660 1.00 18.72 ? 809  ALA   A N     1 
ATOM   5964  C  CA    . ALA   A 1  811  ? -10.091 80.533  108.956 1.00 19.31 ? 809  ALA   A CA    1 
ATOM   5965  C  C     . ALA   A 1  811  ? -10.509 80.013  107.594 1.00 19.68 ? 809  ALA   A C     1 
ATOM   5966  O  O     . ALA   A 1  811  ? -9.672  79.783  106.716 1.00 20.45 ? 809  ALA   A O     1 
ATOM   5967  C  CB    . ALA   A 1  811  ? -9.129  81.703  108.835 1.00 21.70 ? 809  ALA   A CB    1 
ATOM   5968  N  N     . GLU   A 1  812  ? -11.803 79.786  107.444 1.00 16.39 ? 810  GLU   A N     1 
ATOM   5969  C  CA    . GLU   A 1  812  ? -12.383 79.227  106.235 1.00 18.53 ? 810  GLU   A CA    1 
ATOM   5970  C  C     . GLU   A 1  812  ? -13.087 80.368  105.527 1.00 17.99 ? 810  GLU   A C     1 
ATOM   5971  O  O     . GLU   A 1  812  ? -14.027 80.950  106.076 1.00 18.66 ? 810  GLU   A O     1 
ATOM   5972  C  CB    . GLU   A 1  812  ? -13.336 78.104  106.622 1.00 21.72 ? 810  GLU   A CB    1 
ATOM   5973  C  CG    . GLU   A 1  812  ? -12.586 76.968  107.323 1.00 20.16 ? 810  GLU   A CG    1 
ATOM   5974  C  CD    . GLU   A 1  812  ? -11.432 76.437  106.474 1.00 25.01 ? 810  GLU   A CD    1 
ATOM   5975  O  OE1   . GLU   A 1  812  ? -11.689 75.647  105.544 1.00 23.04 ? 810  GLU   A OE1   1 
ATOM   5976  O  OE2   . GLU   A 1  812  ? -10.265 76.815  106.721 1.00 22.85 ? 810  GLU   A OE2   1 
ATOM   5977  N  N     . THR   A 1  813  ? -12.595 80.723  104.338 1.00 18.56 ? 811  THR   A N     1 
ATOM   5978  C  CA    . THR   A 1  813  ? -12.903 82.023  103.762 1.00 19.07 ? 811  THR   A CA    1 
ATOM   5979  C  C     . THR   A 1  813  ? -13.495 81.920  102.358 1.00 18.62 ? 811  THR   A C     1 
ATOM   5980  O  O     . THR   A 1  813  ? -14.102 80.902  102.019 1.00 19.87 ? 811  THR   A O     1 
ATOM   5981  C  CB    . THR   A 1  813  ? -11.679 82.942  103.854 1.00 17.78 ? 811  THR   A CB    1 
ATOM   5982  O  OG1   . THR   A 1  813  ? -10.513 82.266  103.359 1.00 21.42 ? 811  THR   A OG1   1 
ATOM   5983  C  CG2   . THR   A 1  813  ? -11.441 83.299  105.318 1.00 20.46 ? 811  THR   A CG2   1 
ATOM   5984  N  N     . GLY   A 1  814  ? -13.346 82.965  101.549 1.00 20.80 ? 812  GLY   A N     1 
ATOM   5985  C  CA    . GLY   A 1  814  ? -14.120 83.091  100.328 1.00 20.07 ? 812  GLY   A CA    1 
ATOM   5986  C  C     . GLY   A 1  814  ? -13.605 82.247  99.175  1.00 19.35 ? 812  GLY   A C     1 
ATOM   5987  O  O     . GLY   A 1  814  ? -12.562 81.605  99.234  1.00 20.10 ? 812  GLY   A O     1 
ATOM   5988  N  N     . GLY   A 1  815  ? -14.370 82.264  98.085  1.00 18.74 ? 813  GLY   A N     1 
ATOM   5989  C  CA    . GLY   A 1  815  ? -14.017 81.515  96.904  1.00 19.88 ? 813  GLY   A CA    1 
ATOM   5990  C  C     . GLY   A 1  815  ? -14.164 82.380  95.668  1.00 20.49 ? 813  GLY   A C     1 
ATOM   5991  O  O     . GLY   A 1  815  ? -14.824 83.414  95.681  1.00 23.15 ? 813  GLY   A O     1 
ATOM   5992  N  N     . GLN   A 1  816  ? -13.501 81.951  94.601  1.00 18.88 ? 814  GLN   A N     1 
ATOM   5993  C  CA    . GLN   A 1  816  ? -13.707 82.506  93.265  1.00 18.89 ? 814  GLN   A CA    1 
ATOM   5994  C  C     . GLN   A 1  816  ? -13.868 81.310  92.335  1.00 18.21 ? 814  GLN   A C     1 
ATOM   5995  O  O     . GLN   A 1  816  ? -13.010 80.991  91.511  1.00 20.77 ? 814  GLN   A O     1 
ATOM   5996  C  CB    . GLN   A 1  816  ? -12.557 83.411  92.839  1.00 20.37 ? 814  GLN   A CB    1 
ATOM   5997  C  CG    . GLN   A 1  816  ? -12.859 84.213  91.591  1.00 22.72 ? 814  GLN   A CG    1 
ATOM   5998  C  CD    . GLN   A 1  816  ? -13.911 85.279  91.835  1.00 24.28 ? 814  GLN   A CD    1 
ATOM   5999  O  OE1   . GLN   A 1  816  ? -15.105 84.995  91.848  1.00 22.42 ? 814  GLN   A OE1   1 
ATOM   6000  N  NE2   . GLN   A 1  816  ? -13.465 86.514  92.046  1.00 26.23 ? 814  GLN   A NE2   1 
ATOM   6001  N  N     . ASN   A 1  817  ? -14.983 80.627  92.504  1.00 16.59 ? 815  ASN   A N     1 
ATOM   6002  C  CA    . ASN   A 1  817  ? -15.098 79.244  92.081  1.00 17.02 ? 815  ASN   A CA    1 
ATOM   6003  C  C     . ASN   A 1  817  ? -15.439 79.160  90.606  1.00 16.15 ? 815  ASN   A C     1 
ATOM   6004  O  O     . ASN   A 1  817  ? -16.373 79.815  90.134  1.00 17.38 ? 815  ASN   A O     1 
ATOM   6005  C  CB    . ASN   A 1  817  ? -16.165 78.555  92.921  1.00 15.67 ? 815  ASN   A CB    1 
ATOM   6006  C  CG    . ASN   A 1  817  ? -15.941 78.777  94.397  1.00 16.18 ? 815  ASN   A CG    1 
ATOM   6007  O  OD1   . ASN   A 1  817  ? -14.853 78.512  94.914  1.00 16.77 ? 815  ASN   A OD1   1 
ATOM   6008  N  ND2   . ASN   A 1  817  ? -16.955 79.274  95.081  1.00 16.65 ? 815  ASN   A ND2   1 
ATOM   6009  N  N     . ALA   A 1  818  ? -14.683 78.333  89.890  1.00 15.70 ? 816  ALA   A N     1 
ATOM   6010  C  CA    . ALA   A 1  818  ? -14.849 78.141  88.461  1.00 16.73 ? 816  ALA   A CA    1 
ATOM   6011  C  C     . ALA   A 1  818  ? -15.440 76.771  88.168  1.00 14.54 ? 816  ALA   A C     1 
ATOM   6012  O  O     . ALA   A 1  818  ? -15.302 75.815  88.939  1.00 15.88 ? 816  ALA   A O     1 
ATOM   6013  C  CB    . ALA   A 1  818  ? -13.496 78.256  87.759  1.00 17.55 ? 816  ALA   A CB    1 
ATOM   6014  N  N     . MET   A 1  819  ? -16.099 76.690  87.013  1.00 15.61 ? 817  MET   A N     1 
ATOM   6015  C  CA    . MET   A 1  819  ? -16.488 75.427  86.413  1.00 16.78 ? 817  MET   A CA    1 
ATOM   6016  C  C     . MET   A 1  819  ? -16.026 75.448  84.970  1.00 16.47 ? 817  MET   A C     1 
ATOM   6017  O  O     . MET   A 1  819  ? -16.291 76.413  84.247  1.00 17.68 ? 817  MET   A O     1 
ATOM   6018  C  CB    . MET   A 1  819  ? -17.999 75.233  86.446  1.00 16.20 ? 817  MET   A CB    1 
ATOM   6019  C  CG    . MET   A 1  819  ? -18.420 73.975  85.723  1.00 17.39 ? 817  MET   A CG    1 
ATOM   6020  S  SD    . MET   A 1  819  ? -20.212 73.836  85.588  1.00 19.41 ? 817  MET   A SD    1 
ATOM   6021  C  CE    . MET   A 1  819  ? -20.655 73.581  87.300  1.00 21.59 ? 817  MET   A CE    1 
ATOM   6022  N  N     . ILE   A 1  820  ? -15.318 74.402  84.562  1.00 15.62 ? 818  ILE   A N     1 
ATOM   6023  C  CA    . ILE   A 1  820  ? -14.847 74.274  83.190  1.00 16.74 ? 818  ILE   A CA    1 
ATOM   6024  C  C     . ILE   A 1  820  ? -15.741 73.271  82.485  1.00 14.66 ? 818  ILE   A C     1 
ATOM   6025  O  O     . ILE   A 1  820  ? -16.010 72.181  83.004  1.00 15.99 ? 818  ILE   A O     1 
ATOM   6026  C  CB    . ILE   A 1  820  ? -13.376 73.838  83.143  1.00 16.12 ? 818  ILE   A CB    1 
ATOM   6027  C  CG1   . ILE   A 1  820  ? -12.499 74.915  83.770  1.00 18.02 ? 818  ILE   A CG1   1 
ATOM   6028  C  CG2   . ILE   A 1  820  ? -12.966 73.572  81.696  1.00 16.65 ? 818  ILE   A CG2   1 
ATOM   6029  C  CD1   . ILE   A 1  820  ? -11.012 74.571  83.786  1.00 17.56 ? 818  ILE   A CD1   1 
ATOM   6030  N  N     . VAL   A 1  821  ? -16.216 73.648  81.304  1.00 15.67 ? 819  VAL   A N     1 
ATOM   6031  C  CA    . VAL   A 1  821  ? -17.124 72.825  80.520  1.00 16.23 ? 819  VAL   A CA    1 
ATOM   6032  C  C     . VAL   A 1  821  ? -16.506 72.664  79.143  1.00 16.95 ? 819  VAL   A C     1 
ATOM   6033  O  O     . VAL   A 1  821  ? -16.195 73.662  78.479  1.00 20.22 ? 819  VAL   A O     1 
ATOM   6034  C  CB    . VAL   A 1  821  ? -18.501 73.501  80.396  1.00 16.78 ? 819  VAL   A CB    1 
ATOM   6035  C  CG1   . VAL   A 1  821  ? -19.430 72.648  79.554  1.00 18.55 ? 819  VAL   A CG1   1 
ATOM   6036  C  CG2   . VAL   A 1  821  ? -19.086 73.752  81.777  1.00 17.68 ? 819  VAL   A CG2   1 
ATOM   6037  N  N     . ASP   A 1  822  ? -16.314 71.423  78.715  1.00 17.87 ? 820  ASP   A N     1 
ATOM   6038  C  CA    . ASP   A 1  822  ? -15.771 71.204  77.383  1.00 18.09 ? 820  ASP   A CA    1 
ATOM   6039  C  C     . ASP   A 1  822  ? -16.878 70.784  76.427  1.00 19.74 ? 820  ASP   A C     1 
ATOM   6040  O  O     . ASP   A 1  822  ? -18.045 70.661  76.797  1.00 19.63 ? 820  ASP   A O     1 
ATOM   6041  C  CB    . ASP   A 1  822  ? -14.556 70.267  77.390  1.00 20.32 ? 820  ASP   A CB    1 
ATOM   6042  C  CG    . ASP   A 1  822  ? -14.913 68.803  77.616  1.00 19.01 ? 820  ASP   A CG    1 
ATOM   6043  O  OD1   . ASP   A 1  822  ? -16.094 68.407  77.558  1.00 20.31 ? 820  ASP   A OD1   1 
ATOM   6044  O  OD2   . ASP   A 1  822  ? -13.953 68.026  77.844  1.00 20.42 ? 820  ASP   A OD2   1 
ATOM   6045  N  N     . SER   A 1  823  ? -16.498 70.563  75.167  1.00 19.46 ? 821  SER   A N     1 
ATOM   6046  C  CA    . SER   A 1  823  ? -17.485 70.260  74.143  1.00 22.16 ? 821  SER   A CA    1 
ATOM   6047  C  C     . SER   A 1  823  ? -18.078 68.856  74.262  1.00 23.17 ? 821  SER   A C     1 
ATOM   6048  O  O     . SER   A 1  823  ? -18.975 68.525  73.484  1.00 25.88 ? 821  SER   A O     1 
ATOM   6049  C  CB    . SER   A 1  823  ? -16.867 70.460  72.758  1.00 23.05 ? 821  SER   A CB    1 
ATOM   6050  O  OG    . SER   A 1  823  ? -15.791 69.560  72.569  1.00 25.64 ? 821  SER   A OG    1 
ATOM   6051  N  N     . SER   A 1  824  ? -17.610 68.016  75.189  1.00 19.36 ? 822  SER   A N     1 
ATOM   6052  C  CA    . SER   A 1  824  ? -18.199 66.699  75.388  1.00 20.14 ? 822  SER   A CA    1 
ATOM   6053  C  C     . SER   A 1  824  ? -19.313 66.707  76.423  1.00 19.99 ? 822  SER   A C     1 
ATOM   6054  O  O     . SER   A 1  824  ? -19.996 65.692  76.588  1.00 20.69 ? 822  SER   A O     1 
ATOM   6055  C  CB    . SER   A 1  824  ? -17.131 65.695  75.836  1.00 20.18 ? 822  SER   A CB    1 
ATOM   6056  O  OG    . SER   A 1  824  ? -16.712 65.963  77.168  1.00 19.19 ? 822  SER   A OG    1 
ATOM   6057  N  N     . ALA   A 1  825  ? -19.482 67.812  77.146  1.00 20.98 ? 823  ALA   A N     1 
ATOM   6058  C  CA    . ALA   A 1  825  ? -20.477 67.869  78.201  1.00 20.61 ? 823  ALA   A CA    1 
ATOM   6059  C  C     . ALA   A 1  825  ? -21.873 67.972  77.600  1.00 18.74 ? 823  ALA   A C     1 
ATOM   6060  O  O     . ALA   A 1  825  ? -22.058 68.444  76.476  1.00 22.53 ? 823  ALA   A O     1 
ATOM   6061  C  CB    . ALA   A 1  825  ? -20.217 69.093  79.080  1.00 19.45 ? 823  ALA   A CB    1 
ATOM   6062  N  N     . LEU   A 1  826  ? -22.860 67.512  78.353  1.00 20.66 ? 824  LEU   A N     1 
ATOM   6063  C  CA    . LEU   A 1  826  ? -24.250 67.591  77.925  1.00 22.56 ? 824  LEU   A CA    1 
ATOM   6064  C  C     . LEU   A 1  826  ? -24.810 68.933  78.382  1.00 22.13 ? 824  LEU   A C     1 
ATOM   6065  O  O     . LEU   A 1  826  ? -24.862 69.215  79.586  1.00 21.98 ? 824  LEU   A O     1 
ATOM   6066  C  CB    . LEU   A 1  826  ? -25.065 66.439  78.511  1.00 25.57 ? 824  LEU   A CB    1 
ATOM   6067  N  N     . ALA   A 1  827  ? -25.225 69.757  77.420  1.00 20.63 ? 825  ALA   A N     1 
ATOM   6068  C  CA    . ALA   A 1  827  ? -25.585 71.138  77.725  1.00 20.31 ? 825  ALA   A CA    1 
ATOM   6069  C  C     . ALA   A 1  827  ? -26.692 71.222  78.769  1.00 19.65 ? 825  ALA   A C     1 
ATOM   6070  O  O     . ALA   A 1  827  ? -26.602 72.031  79.702  1.00 19.64 ? 825  ALA   A O     1 
ATOM   6071  C  CB    . ALA   A 1  827  ? -25.976 71.876  76.444  1.00 23.93 ? 825  ALA   A CB    1 
ATOM   6072  N  N     . GLU   A 1  828  ? -27.737 70.399  78.640  1.00 21.64 ? 826  GLU   A N     1 
ATOM   6073  C  CA    . GLU   A 1  828  ? -28.835 70.441  79.602  1.00 21.95 ? 826  GLU   A CA    1 
ATOM   6074  C  C     . GLU   A 1  828  ? -28.345 70.165  81.017  1.00 22.29 ? 826  GLU   A C     1 
ATOM   6075  O  O     . GLU   A 1  828  ? -28.782 70.822  81.972  1.00 21.04 ? 826  GLU   A O     1 
ATOM   6076  C  CB    . GLU   A 1  828  ? -29.932 69.443  79.216  1.00 24.61 ? 826  GLU   A CB    1 
ATOM   6077  C  CG    . GLU   A 1  828  ? -30.792 69.864  78.028  1.00 28.20 ? 826  GLU   A CG    1 
ATOM   6078  C  CD    . GLU   A 1  828  ? -30.120 69.638  76.679  1.00 34.17 ? 826  GLU   A CD    1 
ATOM   6079  O  OE1   . GLU   A 1  828  ? -28.990 69.102  76.638  1.00 32.80 ? 826  GLU   A OE1   1 
ATOM   6080  O  OE2   . GLU   A 1  828  ? -30.735 70.000  75.650  1.00 41.10 ? 826  GLU   A OE2   1 
ATOM   6081  N  N     . GLN   A 1  829  ? -27.445 69.191  81.171  1.00 22.58 ? 827  GLN   A N     1 
ATOM   6082  C  CA    . GLN   A 1  829  ? -26.867 68.888  82.478  1.00 21.94 ? 827  GLN   A CA    1 
ATOM   6083  C  C     . GLN   A 1  829  ? -26.042 70.055  82.987  1.00 19.33 ? 827  GLN   A C     1 
ATOM   6084  O  O     . GLN   A 1  829  ? -26.124 70.432  84.163  1.00 19.70 ? 827  GLN   A O     1 
ATOM   6085  C  CB    . GLN   A 1  829  ? -25.975 67.652  82.361  1.00 24.60 ? 827  GLN   A CB    1 
ATOM   6086  C  CG    . GLN   A 1  829  ? -26.507 66.409  83.013  1.00 42.24 ? 827  GLN   A CG    1 
ATOM   6087  C  CD    . GLN   A 1  829  ? -25.582 65.229  82.792  1.00 41.45 ? 827  GLN   A CD    1 
ATOM   6088  O  OE1   . GLN   A 1  829  ? -24.438 65.395  82.351  1.00 36.15 ? 827  GLN   A OE1   1 
ATOM   6089  N  NE2   . GLN   A 1  829  ? -26.073 64.028  83.082  1.00 42.25 ? 827  GLN   A NE2   1 
ATOM   6090  N  N     . VAL   A 1  830  ? -25.198 70.612  82.122  1.00 18.61 ? 828  VAL   A N     1 
ATOM   6091  C  CA    . VAL   A 1  830  ? -24.386 71.761  82.497  1.00 19.84 ? 828  VAL   A CA    1 
ATOM   6092  C  C     . VAL   A 1  830  ? -25.272 72.891  82.987  1.00 17.96 ? 828  VAL   A C     1 
ATOM   6093  O  O     . VAL   A 1  830  ? -25.036 73.480  84.049  1.00 17.79 ? 828  VAL   A O     1 
ATOM   6094  C  CB    . VAL   A 1  830  ? -23.537 72.215  81.302  1.00 17.94 ? 828  VAL   A CB    1 
ATOM   6095  C  CG1   . VAL   A 1  830  ? -22.891 73.536  81.605  1.00 19.23 ? 828  VAL   A CG1   1 
ATOM   6096  C  CG2   . VAL   A 1  830  ? -22.484 71.160  80.966  1.00 19.28 ? 828  VAL   A CG2   1 
ATOM   6097  N  N     . VAL   A 1  831  ? -26.301 73.222  82.208  1.00 18.93 ? 829  VAL   A N     1 
ATOM   6098  C  CA    . VAL   A 1  831  ? -27.112 74.384  82.538  1.00 16.87 ? 829  VAL   A CA    1 
ATOM   6099  C  C     . VAL   A 1  831  ? -27.806 74.197  83.872  1.00 16.86 ? 829  VAL   A C     1 
ATOM   6100  O  O     . VAL   A 1  831  ? -27.831 75.116  84.698  1.00 16.71 ? 829  VAL   A O     1 
ATOM   6101  C  CB    . VAL   A 1  831  ? -28.083 74.710  81.392  1.00 16.75 ? 829  VAL   A CB    1 
ATOM   6102  C  CG1   . VAL   A 1  831  ? -29.106 75.738  81.839  1.00 17.34 ? 829  VAL   A CG1   1 
ATOM   6103  C  CG2   . VAL   A 1  831  ? -27.294 75.233  80.199  1.00 21.08 ? 829  VAL   A CG2   1 
ATOM   6104  N  N     . GLY   A 1  832  ? -28.356 73.007  84.117  1.00 17.70 ? 830  GLY   A N     1 
ATOM   6105  C  CA    . GLY   A 1  832  ? -28.961 72.754  85.413  1.00 17.43 ? 830  GLY   A CA    1 
ATOM   6106  C  C     . GLY   A 1  832  ? -27.974 72.921  86.550  1.00 16.91 ? 830  GLY   A C     1 
ATOM   6107  O  O     . GLY   A 1  832  ? -28.289 73.533  87.574  1.00 17.57 ? 830  GLY   A O     1 
ATOM   6108  N  N     . ASP   A 1  833  ? -26.760 72.396  86.382  1.00 17.64 ? 831  ASP   A N     1 
ATOM   6109  C  CA    . ASP   A 1  833  ? -25.779 72.498  87.457  1.00 16.39 ? 831  ASP   A CA    1 
ATOM   6110  C  C     . ASP   A 1  833  ? -25.267 73.918  87.618  1.00 16.08 ? 831  ASP   A C     1 
ATOM   6111  O  O     . ASP   A 1  833  ? -24.909 74.323  88.727  1.00 17.89 ? 831  ASP   A O     1 
ATOM   6112  C  CB    . ASP   A 1  833  ? -24.607 71.558  87.197  1.00 17.83 ? 831  ASP   A CB    1 
ATOM   6113  C  CG    . ASP   A 1  833  ? -24.998 70.118  87.319  1.00 18.91 ? 831  ASP   A CG    1 
ATOM   6114  O  OD1   . ASP   A 1  833  ? -26.054 69.833  87.925  1.00 23.01 ? 831  ASP   A OD1   1 
ATOM   6115  O  OD2   . ASP   A 1  833  ? -24.253 69.255  86.814  1.00 19.65 ? 831  ASP   A OD2   1 
ATOM   6116  N  N     . VAL   A 1  834  ? -25.216 74.676  86.524  1.00 16.42 ? 832  VAL   A N     1 
ATOM   6117  C  CA    . VAL   A 1  834  ? -24.792 76.068  86.584  1.00 16.14 ? 832  VAL   A CA    1 
ATOM   6118  C  C     . VAL   A 1  834  ? -25.851 76.920  87.274  1.00 18.98 ? 832  VAL   A C     1 
ATOM   6119  O  O     . VAL   A 1  834  ? -25.547 77.717  88.174  1.00 17.12 ? 832  VAL   A O     1 
ATOM   6120  C  CB    . VAL   A 1  834  ? -24.489 76.581  85.167  1.00 16.76 ? 832  VAL   A CB    1 
ATOM   6121  C  CG1   . VAL   A 1  834  ? -24.335 78.069  85.179  1.00 17.27 ? 832  VAL   A CG1   1 
ATOM   6122  C  CG2   . VAL   A 1  834  ? -23.227 75.913  84.631  1.00 18.49 ? 832  VAL   A CG2   1 
ATOM   6123  N  N     . ILE   A 1  835  ? -27.113 76.770  86.856  1.00 18.30 ? 833  ILE   A N     1 
ATOM   6124  C  CA    . ILE   A 1  835  ? -28.204 77.519  87.474  1.00 17.77 ? 833  ILE   A CA    1 
ATOM   6125  C  C     . ILE   A 1  835  ? -28.241 77.258  88.969  1.00 18.50 ? 833  ILE   A C     1 
ATOM   6126  O  O     . ILE   A 1  835  ? -28.356 78.188  89.778  1.00 20.55 ? 833  ILE   A O     1 
ATOM   6127  C  CB    . ILE   A 1  835  ? -29.542 77.164  86.802  1.00 18.86 ? 833  ILE   A CB    1 
ATOM   6128  C  CG1   . ILE   A 1  835  ? -29.616 77.723  85.377  1.00 22.85 ? 833  ILE   A CG1   1 
ATOM   6129  C  CG2   . ILE   A 1  835  ? -30.728 77.648  87.652  1.00 23.33 ? 833  ILE   A CG2   1 
ATOM   6130  C  CD1   . ILE   A 1  835  ? -29.803 79.228  85.306  1.00 24.72 ? 833  ILE   A CD1   1 
ATOM   6131  N  N     . THR   A 1  836  ? -28.111 75.996  89.362  1.00 18.63 ? 834  THR   A N     1 
ATOM   6132  C  CA    . THR   A 1  836  ? -28.087 75.663  90.779  1.00 19.34 ? 834  THR   A CA    1 
ATOM   6133  C  C     . THR   A 1  836  ? -26.852 76.248  91.453  1.00 18.57 ? 834  THR   A C     1 
ATOM   6134  O  O     . THR   A 1  836  ? -26.955 76.926  92.477  1.00 20.90 ? 834  THR   A O     1 
ATOM   6135  C  CB    . THR   A 1  836  ? -28.131 74.143  90.933  1.00 22.91 ? 834  THR   A CB    1 
ATOM   6136  O  OG1   . THR   A 1  836  ? -29.410 73.676  90.498  1.00 28.46 ? 834  THR   A OG1   1 
ATOM   6137  C  CG2   . THR   A 1  836  ? -27.899 73.739  92.372  1.00 26.00 ? 834  THR   A CG2   1 
ATOM   6138  N  N     . SER   A 1  837  ? -25.674 76.025  90.878  1.00 19.52 ? 835  SER   A N     1 
ATOM   6139  C  CA    . SER   A 1  837  ? -24.450 76.415  91.572  1.00 17.58 ? 835  SER   A CA    1 
ATOM   6140  C  C     . SER   A 1  837  ? -24.305 77.926  91.658  1.00 17.12 ? 835  SER   A C     1 
ATOM   6141  O  O     . SER   A 1  837  ? -23.761 78.444  92.635  1.00 18.23 ? 835  SER   A O     1 
ATOM   6142  C  CB    . SER   A 1  837  ? -23.229 75.819  90.869  1.00 17.07 ? 835  SER   A CB    1 
ATOM   6143  O  OG    . SER   A 1  837  ? -23.285 74.409  90.849  1.00 17.44 ? 835  SER   A OG    1 
ATOM   6144  N  N     . ALA   A 1  838  ? -24.752 78.649  90.637  1.00 16.81 ? 836  ALA   A N     1 
ATOM   6145  C  CA    . ALA   A 1  838  ? -24.517 80.082  90.610  1.00 17.67 ? 836  ALA   A CA    1 
ATOM   6146  C  C     . ALA   A 1  838  ? -25.592 80.854  91.352  1.00 18.34 ? 836  ALA   A C     1 
ATOM   6147  O  O     . ALA   A 1  838  ? -25.302 81.885  91.969  1.00 19.46 ? 836  ALA   A O     1 
ATOM   6148  C  CB    . ALA   A 1  838  ? -24.445 80.589  89.168  1.00 17.79 ? 836  ALA   A CB    1 
ATOM   6149  N  N     . PHE   A 1  839  ? -26.836 80.392  91.285  1.00 17.90 ? 837  PHE   A N     1 
ATOM   6150  C  CA    . PHE   A 1  839  ? -27.954 81.219  91.705  1.00 19.48 ? 837  PHE   A CA    1 
ATOM   6151  C  C     . PHE   A 1  839  ? -28.769 80.682  92.865  1.00 19.48 ? 837  PHE   A C     1 
ATOM   6152  O  O     . PHE   A 1  839  ? -29.540 81.458  93.447  1.00 21.04 ? 837  PHE   A O     1 
ATOM   6153  C  CB    . PHE   A 1  839  ? -28.872 81.528  90.516  1.00 19.96 ? 837  PHE   A CB    1 
ATOM   6154  C  CG    . PHE   A 1  839  ? -28.150 82.138  89.373  1.00 17.96 ? 837  PHE   A CG    1 
ATOM   6155  C  CD1   . PHE   A 1  839  ? -27.453 83.314  89.536  1.00 20.79 ? 837  PHE   A CD1   1 
ATOM   6156  C  CD2   . PHE   A 1  839  ? -28.136 81.522  88.141  1.00 21.05 ? 837  PHE   A CD2   1 
ATOM   6157  C  CE1   . PHE   A 1  839  ? -26.771 83.882  88.495  1.00 20.41 ? 837  PHE   A CE1   1 
ATOM   6158  C  CE2   . PHE   A 1  839  ? -27.446 82.079  87.089  1.00 23.43 ? 837  PHE   A CE2   1 
ATOM   6159  C  CZ    . PHE   A 1  839  ? -26.765 83.267  87.262  1.00 21.37 ? 837  PHE   A CZ    1 
ATOM   6160  N  N     . ASP   A 1  840  ? -28.632 79.404  93.224  1.00 20.49 ? 838  ASP   A N     1 
ATOM   6161  C  CA    . ASP   A 1  840  ? -29.208 78.925  94.473  1.00 22.12 ? 838  ASP   A CA    1 
ATOM   6162  C  C     . ASP   A 1  840  ? -28.781 79.851  95.602  1.00 23.51 ? 838  ASP   A C     1 
ATOM   6163  O  O     . ASP   A 1  840  ? -27.631 80.302  95.657  1.00 21.06 ? 838  ASP   A O     1 
ATOM   6164  C  CB    . ASP   A 1  840  ? -28.710 77.502  94.739  1.00 24.52 ? 838  ASP   A CB    1 
ATOM   6165  C  CG    . ASP   A 1  840  ? -29.310 76.880  95.976  1.00 32.99 ? 838  ASP   A CG    1 
ATOM   6166  O  OD1   . ASP   A 1  840  ? -28.800 77.144  97.085  1.00 33.58 ? 838  ASP   A OD1   1 
ATOM   6167  O  OD2   . ASP   A 1  840  ? -30.277 76.102  95.830  1.00 37.39 ? 838  ASP   A OD2   1 
ATOM   6168  N  N     . SER   A 1  841  ? -29.731 80.181  96.474  1.00 21.28 ? 839  SER   A N     1 
ATOM   6169  C  CA    . SER   A 1  841  ? -29.476 81.091  97.593  1.00 21.20 ? 839  SER   A CA    1 
ATOM   6170  C  C     . SER   A 1  841  ? -28.972 82.450  97.123  1.00 19.80 ? 839  SER   A C     1 
ATOM   6171  O  O     . SER   A 1  841  ? -28.240 83.137  97.842  1.00 19.51 ? 839  SER   A O     1 
ATOM   6172  C  CB    . SER   A 1  841  ? -28.519 80.469  98.616  1.00 26.78 ? 839  SER   A CB    1 
ATOM   6173  O  OG    . SER   A 1  841  ? -28.928 79.151  98.943  1.00 29.12 ? 839  SER   A OG    1 
ATOM   6174  N  N     . ALA   A 1  842  ? -29.347 82.848  95.904  1.00 21.29 ? 840  ALA   A N     1 
ATOM   6175  C  CA    . ALA   A 1  842  ? -28.890 84.104  95.313  1.00 18.07 ? 840  ALA   A CA    1 
ATOM   6176  C  C     . ALA   A 1  842  ? -27.365 84.190  95.288  1.00 17.99 ? 840  ALA   A C     1 
ATOM   6177  O  O     . ALA   A 1  842  ? -26.780 85.252  95.497  1.00 20.48 ? 840  ALA   A O     1 
ATOM   6178  C  CB    . ALA   A 1  842  ? -29.525 85.331  95.978  1.00 19.89 ? 840  ALA   A CB    1 
ATOM   6179  N  N     . GLY   A 1  843  ? -26.721 83.056  95.020  1.00 18.31 ? 841  GLY   A N     1 
ATOM   6180  C  CA    . GLY   A 1  843  ? -25.276 83.017  94.977  1.00 18.86 ? 841  GLY   A CA    1 
ATOM   6181  C  C     . GLY   A 1  843  ? -24.615 83.242  96.311  1.00 18.13 ? 841  GLY   A C     1 
ATOM   6182  O  O     . GLY   A 1  843  ? -23.397 83.418  96.360  1.00 18.26 ? 841  GLY   A O     1 
ATOM   6183  N  N     . GLN   A 1  844  ? -25.373 83.218  97.399  1.00 18.52 ? 842  GLN   A N     1 
ATOM   6184  C  CA    . GLN   A 1  844  ? -24.816 83.472  98.723  1.00 18.03 ? 842  GLN   A CA    1 
ATOM   6185  C  C     . GLN   A 1  844  ? -24.398 82.175  99.403  1.00 20.62 ? 842  GLN   A C     1 
ATOM   6186  O  O     . GLN   A 1  844  ? -24.785 81.837  100.522 1.00 20.77 ? 842  GLN   A O     1 
ATOM   6187  C  CB    . GLN   A 1  844  ? -25.799 84.295  99.543  1.00 18.30 ? 842  GLN   A CB    1 
ATOM   6188  C  CG    . GLN   A 1  844  ? -25.977 85.667  98.933  1.00 18.50 ? 842  GLN   A CG    1 
ATOM   6189  C  CD    . GLN   A 1  844  ? -27.194 86.403  99.461  1.00 19.60 ? 842  GLN   A CD    1 
ATOM   6190  O  OE1   . GLN   A 1  844  ? -27.076 87.514  99.964  1.00 21.03 ? 842  GLN   A OE1   1 
ATOM   6191  N  NE2   . GLN   A 1  844  ? -28.368 85.798  99.320  1.00 20.51 ? 842  GLN   A NE2   1 
ATOM   6192  N  N     . ARG   A 1  845  ? -23.581 81.429  98.668  1.00 18.86 ? 843  ARG   A N     1 
ATOM   6193  C  CA    . ARG   A 1  845  ? -22.866 80.272  99.175  1.00 17.82 ? 843  ARG   A CA    1 
ATOM   6194  C  C     . ARG   A 1  845  ? -21.393 80.501  98.897  1.00 17.73 ? 843  ARG   A C     1 
ATOM   6195  O  O     . ARG   A 1  845  ? -21.023 80.999  97.830  1.00 19.32 ? 843  ARG   A O     1 
ATOM   6196  C  CB    . ARG   A 1  845  ? -23.275 78.992  98.443  1.00 21.95 ? 843  ARG   A CB    1 
ATOM   6197  C  CG    . ARG   A 1  845  ? -24.705 78.515  98.707  1.00 20.25 ? 843  ARG   A CG    1 
ATOM   6198  C  CD    . ARG   A 1  845  ? -24.976 77.227  97.943  1.00 28.21 ? 843  ARG   A CD    1 
ATOM   6199  N  NE    . ARG   A 1  845  ? -26.320 76.714  98.172  1.00 31.79 ? 843  ARG   A NE    1 
ATOM   6200  C  CZ    . ARG   A 1  845  ? -26.629 75.800  99.082  1.00 39.19 ? 843  ARG   A CZ    1 
ATOM   6201  N  NH1   . ARG   A 1  845  ? -25.706 75.259  99.864  1.00 32.74 ? 843  ARG   A NH1   1 
ATOM   6202  N  NH2   . ARG   A 1  845  ? -27.898 75.418  99.212  1.00 38.65 ? 843  ARG   A NH2   1 
ATOM   6203  N  N     . CYS   A 1  846  ? -20.546 80.148  99.854  1.00 17.60 ? 844  CYS   A N     1 
ATOM   6204  C  CA    . CYS   A 1  846  ? -19.124 80.292  99.599  1.00 18.38 ? 844  CYS   A CA    1 
ATOM   6205  C  C     . CYS   A 1  846  ? -18.694 79.417  98.435  1.00 17.99 ? 844  CYS   A C     1 
ATOM   6206  O  O     . CYS   A 1  846  ? -17.745 79.755  97.728  1.00 16.54 ? 844  CYS   A O     1 
ATOM   6207  C  CB    . CYS   A 1  846  ? -18.330 79.947  100.851 1.00 18.27 ? 844  CYS   A CB    1 
ATOM   6208  S  SG    . CYS   A 1  846  ? -18.746 78.361  101.559 1.00 20.47 ? 844  CYS   A SG    1 
ATOM   6209  N  N     . SER   A 1  847  ? -19.390 78.306  98.224  1.00 16.80 ? 845  SER   A N     1 
ATOM   6210  C  CA    . SER   A 1  847  ? -19.117 77.356  97.152  1.00 15.89 ? 845  SER   A CA    1 
ATOM   6211  C  C     . SER   A 1  847  ? -19.711 77.771  95.817  1.00 16.59 ? 845  SER   A C     1 
ATOM   6212  O  O     . SER   A 1  847  ? -19.510 77.057  94.827  1.00 16.88 ? 845  SER   A O     1 
ATOM   6213  C  CB    . SER   A 1  847  ? -19.738 76.022  97.542  1.00 16.35 ? 845  SER   A CB    1 
ATOM   6214  O  OG    . SER   A 1  847  ? -21.090 76.263  97.911  1.00 18.85 ? 845  SER   A OG    1 
ATOM   6215  N  N     . ALA   A 1  848  ? -20.438 78.885  95.764  1.00 17.15 ? 846  ALA   A N     1 
ATOM   6216  C  CA    . ALA   A 1  848  ? -21.211 79.211  94.572  1.00 16.55 ? 846  ALA   A CA    1 
ATOM   6217  C  C     . ALA   A 1  848  ? -20.323 79.375  93.348  1.00 16.48 ? 846  ALA   A C     1 
ATOM   6218  O  O     . ALA   A 1  848  ? -19.182 79.829  93.418  1.00 17.23 ? 846  ALA   A O     1 
ATOM   6219  C  CB    . ALA   A 1  848  ? -22.033 80.485  94.787  1.00 18.13 ? 846  ALA   A CB    1 
ATOM   6220  N  N     . LEU   A 1  849  ? -20.876 79.004  92.204  1.00 17.04 ? 847  LEU   A N     1 
ATOM   6221  C  CA    . LEU   A 1  849  ? -20.154 79.141  90.950  1.00 17.31 ? 847  LEU   A CA    1 
ATOM   6222  C  C     . LEU   A 1  849  ? -20.072 80.612  90.565  1.00 17.94 ? 847  LEU   A C     1 
ATOM   6223  O  O     . LEU   A 1  849  ? -21.101 81.283  90.424  1.00 17.84 ? 847  LEU   A O     1 
ATOM   6224  C  CB    . LEU   A 1  849  ? -20.886 78.357  89.870  1.00 17.50 ? 847  LEU   A CB    1 
ATOM   6225  C  CG    . LEU   A 1  849  ? -20.295 78.545  88.478  1.00 16.30 ? 847  LEU   A CG    1 
ATOM   6226  C  CD1   . LEU   A 1  849  ? -18.880 78.012  88.400  1.00 18.64 ? 847  LEU   A CD1   1 
ATOM   6227  C  CD2   . LEU   A 1  849  ? -21.186 77.856  87.456  1.00 17.98 ? 847  LEU   A CD2   1 
ATOM   6228  N  N     . ARG   A 1  850  ? -18.850 81.116  90.403  1.00 16.70 ? 848  ARG   A N     1 
ATOM   6229  C  CA    . ARG   A 1  850  ? -18.623 82.507  90.051  1.00 18.42 ? 848  ARG   A CA    1 
ATOM   6230  C  C     . ARG   A 1  850  ? -18.155 82.690  88.622  1.00 18.39 ? 848  ARG   A C     1 
ATOM   6231  O  O     . ARG   A 1  850  ? -18.409 83.738  88.031  1.00 20.09 ? 848  ARG   A O     1 
ATOM   6232  C  CB    . ARG   A 1  850  ? -17.566 83.133  90.969  1.00 19.93 ? 848  ARG   A CB    1 
ATOM   6233  C  CG    . ARG   A 1  850  ? -17.832 82.933  92.441  1.00 19.77 ? 848  ARG   A CG    1 
ATOM   6234  C  CD    . ARG   A 1  850  ? -19.168 83.513  92.834  1.00 20.79 ? 848  ARG   A CD    1 
ATOM   6235  N  NE    . ARG   A 1  850  ? -19.359 83.409  94.272  1.00 20.44 ? 848  ARG   A NE    1 
ATOM   6236  C  CZ    . ARG   A 1  850  ? -20.513 83.626  94.884  1.00 20.72 ? 848  ARG   A CZ    1 
ATOM   6237  N  NH1   . ARG   A 1  850  ? -21.605 83.947  94.207  1.00 20.46 ? 848  ARG   A NH1   1 
ATOM   6238  N  NH2   . ARG   A 1  850  ? -20.569 83.522  96.207  1.00 19.65 ? 848  ARG   A NH2   1 
ATOM   6239  N  N     . VAL   A 1  851  ? -17.438 81.713  88.071  1.00 18.67 ? 849  VAL   A N     1 
ATOM   6240  C  CA    . VAL   A 1  851  ? -16.861 81.836  86.737  1.00 18.21 ? 849  VAL   A CA    1 
ATOM   6241  C  C     . VAL   A 1  851  ? -17.135 80.542  85.991  1.00 17.79 ? 849  VAL   A C     1 
ATOM   6242  O  O     . VAL   A 1  851  ? -16.568 79.495  86.328  1.00 18.79 ? 849  VAL   A O     1 
ATOM   6243  C  CB    . VAL   A 1  851  ? -15.353 82.111  86.751  1.00 23.22 ? 849  VAL   A CB    1 
ATOM   6244  C  CG1   . VAL   A 1  851  ? -14.877 82.374  85.323  1.00 26.55 ? 849  VAL   A CG1   1 
ATOM   6245  C  CG2   . VAL   A 1  851  ? -15.009 83.272  87.653  1.00 26.69 ? 849  VAL   A CG2   1 
ATOM   6246  N  N     . LEU   A 1  852  ? -17.987 80.612  84.976  1.00 17.79 ? 850  LEU   A N     1 
ATOM   6247  C  CA    . LEU   A 1  852  ? -18.235 79.489  84.087  1.00 18.46 ? 850  LEU   A CA    1 
ATOM   6248  C  C     . LEU   A 1  852  ? -17.334 79.643  82.870  1.00 16.93 ? 850  LEU   A C     1 
ATOM   6249  O  O     . LEU   A 1  852  ? -17.328 80.695  82.226  1.00 17.74 ? 850  LEU   A O     1 
ATOM   6250  C  CB    . LEU   A 1  852  ? -19.692 79.519  83.642  1.00 16.97 ? 850  LEU   A CB    1 
ATOM   6251  C  CG    . LEU   A 1  852  ? -20.110 78.462  82.626  1.00 18.29 ? 850  LEU   A CG    1 
ATOM   6252  C  CD1   . LEU   A 1  852  ? -19.949 77.061  83.209  1.00 16.66 ? 850  LEU   A CD1   1 
ATOM   6253  C  CD2   . LEU   A 1  852  ? -21.569 78.709  82.201  1.00 17.05 ? 850  LEU   A CD2   1 
ATOM   6254  N  N     . CYS   A 1  853  ? -16.558 78.607  82.580  1.00 16.92 ? 851  CYS   A N     1 
ATOM   6255  C  CA    . CYS   A 1  853  ? -15.604 78.628  81.483  1.00 18.17 ? 851  CYS   A CA    1 
ATOM   6256  C  C     . CYS   A 1  853  ? -16.064 77.633  80.435  1.00 16.01 ? 851  CYS   A C     1 
ATOM   6257  O  O     . CYS   A 1  853  ? -16.113 76.432  80.695  1.00 17.54 ? 851  CYS   A O     1 
ATOM   6258  C  CB    . CYS   A 1  853  ? -14.209 78.250  81.974  1.00 17.69 ? 851  CYS   A CB    1 
ATOM   6259  S  SG    . CYS   A 1  853  ? -13.689 79.165  83.424  1.00 20.41 ? 851  CYS   A SG    1 
ATOM   6260  N  N     . LEU   A 1  854  ? -16.407 78.141  79.261  1.00 16.18 ? 852  LEU   A N     1 
ATOM   6261  C  CA    . LEU   A 1  854  ? -17.038 77.355  78.215  1.00 17.96 ? 852  LEU   A CA    1 
ATOM   6262  C  C     . LEU   A 1  854  ? -16.087 77.197  77.044  1.00 18.08 ? 852  LEU   A C     1 
ATOM   6263  O  O     . LEU   A 1  854  ? -15.551 78.186  76.530  1.00 19.23 ? 852  LEU   A O     1 
ATOM   6264  C  CB    . LEU   A 1  854  ? -18.303 78.050  77.724  1.00 17.93 ? 852  LEU   A CB    1 
ATOM   6265  C  CG    . LEU   A 1  854  ? -19.392 78.244  78.781  1.00 18.49 ? 852  LEU   A CG    1 
ATOM   6266  C  CD1   . LEU   A 1  854  ? -20.573 79.019  78.179  1.00 19.53 ? 852  LEU   A CD1   1 
ATOM   6267  C  CD2   . LEU   A 1  854  ? -19.856 76.902  79.334  1.00 20.16 ? 852  LEU   A CD2   1 
ATOM   6268  N  N     . GLN   A 1  855  ? -15.906 75.959  76.605  1.00 17.39 ? 853  GLN   A N     1 
ATOM   6269  C  CA    . GLN   A 1  855  ? -15.091 75.752  75.419  1.00 16.82 ? 853  GLN   A CA    1 
ATOM   6270  C  C     . GLN   A 1  855  ? -15.753 76.457  74.235  1.00 20.19 ? 853  GLN   A C     1 
ATOM   6271  O  O     . GLN   A 1  855  ? -16.975 76.413  74.070  1.00 19.67 ? 853  GLN   A O     1 
ATOM   6272  C  CB    . GLN   A 1  855  ? -14.923 74.263  75.149  1.00 17.68 ? 853  GLN   A CB    1 
ATOM   6273  C  CG    . GLN   A 1  855  ? -13.879 74.024  74.078  1.00 19.76 ? 853  GLN   A CG    1 
ATOM   6274  C  CD    . GLN   A 1  855  ? -13.779 72.574  73.669  1.00 22.05 ? 853  GLN   A CD    1 
ATOM   6275  O  OE1   . GLN   A 1  855  ? -13.808 71.674  74.499  1.00 25.02 ? 853  GLN   A OE1   1 
ATOM   6276  N  NE2   . GLN   A 1  855  ? -13.651 72.344  72.363  1.00 24.73 ? 853  GLN   A NE2   1 
ATOM   6277  N  N     . GLU   A 1  856  ? -14.927 77.132  73.428  1.00 21.35 ? 854  GLU   A N     1 
ATOM   6278  C  CA    . GLU   A 1  856  ? -15.434 78.079  72.438  1.00 23.08 ? 854  GLU   A CA    1 
ATOM   6279  C  C     . GLU   A 1  856  ? -16.478 77.457  71.518  1.00 21.85 ? 854  GLU   A C     1 
ATOM   6280  O  O     . GLU   A 1  856  ? -17.492 78.092  71.204  1.00 23.22 ? 854  GLU   A O     1 
ATOM   6281  C  CB    . GLU   A 1  856  ? -14.264 78.643  71.627  1.00 24.01 ? 854  GLU   A CB    1 
ATOM   6282  C  CG    . GLU   A 1  856  ? -14.695 79.545  70.484  1.00 24.86 ? 854  GLU   A CG    1 
ATOM   6283  C  CD    . GLU   A 1  856  ? -15.480 80.748  70.961  1.00 37.14 ? 854  GLU   A CD    1 
ATOM   6284  O  OE1   . GLU   A 1  856  ? -15.116 81.315  72.015  1.00 34.56 ? 854  GLU   A OE1   1 
ATOM   6285  O  OE2   . GLU   A 1  856  ? -16.465 81.123  70.285  1.00 37.14 ? 854  GLU   A OE2   1 
ATOM   6286  N  N     . ASP   A 1  857  ? -16.267 76.205  71.105  1.00 22.68 ? 855  ASP   A N     1 
ATOM   6287  C  CA    . ASP   A 1  857  ? -17.138 75.564  70.121  1.00 25.66 ? 855  ASP   A CA    1 
ATOM   6288  C  C     . ASP   A 1  857  ? -18.555 75.326  70.631  1.00 26.14 ? 855  ASP   A C     1 
ATOM   6289  O  O     . ASP   A 1  857  ? -19.474 75.153  69.821  1.00 28.52 ? 855  ASP   A O     1 
ATOM   6290  C  CB    . ASP   A 1  857  ? -16.529 74.242  69.653  1.00 31.20 ? 855  ASP   A CB    1 
ATOM   6291  N  N     . VAL   A 1  858  ? -18.764 75.303  71.944  1.00 20.70 ? 856  VAL   A N     1 
ATOM   6292  C  CA    . VAL   A 1  858  ? -20.085 75.067  72.507  1.00 22.56 ? 856  VAL   A CA    1 
ATOM   6293  C  C     . VAL   A 1  858  ? -20.599 76.251  73.296  1.00 19.09 ? 856  VAL   A C     1 
ATOM   6294  O  O     . VAL   A 1  858  ? -21.722 76.192  73.821  1.00 20.61 ? 856  VAL   A O     1 
ATOM   6295  C  CB    . VAL   A 1  858  ? -20.135 73.783  73.358  1.00 19.45 ? 856  VAL   A CB    1 
ATOM   6296  C  CG1   . VAL   A 1  858  ? -19.901 72.568  72.469  1.00 23.41 ? 856  VAL   A CG1   1 
ATOM   6297  C  CG2   . VAL   A 1  858  ? -19.101 73.845  74.492  1.00 20.30 ? 856  VAL   A CG2   1 
ATOM   6298  N  N     . ALA   A 1  859  ? -19.822 77.332  73.383  1.00 19.47 ? 857  ALA   A N     1 
ATOM   6299  C  CA    . ALA   A 1  859  ? -20.143 78.409  74.307  1.00 19.17 ? 857  ALA   A CA    1 
ATOM   6300  C  C     . ALA   A 1  859  ? -21.451 79.090  73.935  1.00 20.52 ? 857  ALA   A C     1 
ATOM   6301  O  O     . ALA   A 1  859  ? -22.272 79.377  74.810  1.00 19.10 ? 857  ALA   A O     1 
ATOM   6302  C  CB    . ALA   A 1  859  ? -19.001 79.416  74.360  1.00 20.96 ? 857  ALA   A CB    1 
ATOM   6303  N  N     . ASP   A 1  860  ? -21.671 79.348  72.644  1.00 21.64 ? 858  ASP   A N     1 
ATOM   6304  C  CA    . ASP   A 1  860  ? -22.886 80.054  72.254  1.00 22.56 ? 858  ASP   A CA    1 
ATOM   6305  C  C     . ASP   A 1  860  ? -24.127 79.234  72.559  1.00 20.47 ? 858  ASP   A C     1 
ATOM   6306  O  O     . ASP   A 1  860  ? -25.113 79.763  73.086  1.00 22.76 ? 858  ASP   A O     1 
ATOM   6307  C  CB    . ASP   A 1  860  ? -22.834 80.417  70.770  1.00 22.72 ? 858  ASP   A CB    1 
ATOM   6308  C  CG    . ASP   A 1  860  ? -21.853 81.533  70.479  1.00 31.05 ? 858  ASP   A CG    1 
ATOM   6309  O  OD1   . ASP   A 1  860  ? -21.643 82.390  71.362  1.00 35.30 ? 858  ASP   A OD1   1 
ATOM   6310  O  OD2   . ASP   A 1  860  ? -21.291 81.551  69.364  1.00 48.90 ? 858  ASP   A OD2   1 
ATOM   6311  N  N     . ARG   A 1  861  ? -24.102 77.943  72.237  1.00 20.20 ? 859  ARG   A N     1 
ATOM   6312  C  CA    . ARG   A 1  861  ? -25.262 77.103  72.491  1.00 22.08 ? 859  ARG   A CA    1 
ATOM   6313  C  C     . ARG   A 1  861  ? -25.554 77.020  73.985  1.00 20.37 ? 859  ARG   A C     1 
ATOM   6314  O  O     . ARG   A 1  861  ? -26.703 77.161  74.415  1.00 20.43 ? 859  ARG   A O     1 
ATOM   6315  C  CB    . ARG   A 1  861  ? -25.042 75.715  71.899  1.00 26.93 ? 859  ARG   A CB    1 
ATOM   6316  C  CG    . ARG   A 1  861  ? -26.179 74.766  72.171  1.00 36.15 ? 859  ARG   A CG    1 
ATOM   6317  C  CD    . ARG   A 1  861  ? -26.082 73.511  71.328  1.00 45.37 ? 859  ARG   A CD    1 
ATOM   6318  N  NE    . ARG   A 1  861  ? -27.172 72.604  71.662  1.00 55.20 ? 859  ARG   A NE    1 
ATOM   6319  C  CZ    . ARG   A 1  861  ? -27.088 71.641  72.569  1.00 52.96 ? 859  ARG   A CZ    1 
ATOM   6320  N  NH1   . ARG   A 1  861  ? -25.954 71.389  73.203  1.00 51.34 ? 859  ARG   A NH1   1 
ATOM   6321  N  NH2   . ARG   A 1  861  ? -28.166 70.914  72.845  1.00 45.58 ? 859  ARG   A NH2   1 
ATOM   6322  N  N     . ILE   A 1  862  ? -24.516 76.816  74.797  1.00 18.80 ? 860  ILE   A N     1 
ATOM   6323  C  CA    . ILE   A 1  862  ? -24.731 76.709  76.237  1.00 20.59 ? 860  ILE   A CA    1 
ATOM   6324  C  C     . ILE   A 1  862  ? -25.199 78.036  76.816  1.00 20.87 ? 860  ILE   A C     1 
ATOM   6325  O  O     . ILE   A 1  862  ? -26.105 78.077  77.661  1.00 17.80 ? 860  ILE   A O     1 
ATOM   6326  C  CB    . ILE   A 1  862  ? -23.464 76.184  76.931  1.00 19.13 ? 860  ILE   A CB    1 
ATOM   6327  C  CG1   . ILE   A 1  862  ? -23.248 74.720  76.532  1.00 21.89 ? 860  ILE   A CG1   1 
ATOM   6328  C  CG2   . ILE   A 1  862  ? -23.594 76.357  78.450  1.00 20.14 ? 860  ILE   A CG2   1 
ATOM   6329  C  CD1   . ILE   A 1  862  ? -21.925 74.135  77.016  1.00 21.98 ? 860  ILE   A CD1   1 
ATOM   6330  N  N     . LEU   A 1  863  ? -24.606 79.140  76.364  1.00 18.09 ? 861  LEU   A N     1 
ATOM   6331  C  CA    A LEU   A 1  863  ? -25.003 80.450  76.873  0.49 17.74 ? 861  LEU   A CA    1 
ATOM   6332  C  CA    B LEU   A 1  863  ? -24.998 80.451  76.867  0.51 17.74 ? 861  LEU   A CA    1 
ATOM   6333  C  C     . LEU   A 1  863  ? -26.453 80.758  76.533  1.00 19.20 ? 861  LEU   A C     1 
ATOM   6334  O  O     . LEU   A 1  863  ? -27.193 81.278  77.373  1.00 18.18 ? 861  LEU   A O     1 
ATOM   6335  C  CB    A LEU   A 1  863  ? -24.086 81.545  76.326  0.49 20.62 ? 861  LEU   A CB    1 
ATOM   6336  C  CB    B LEU   A 1  863  ? -24.074 81.508  76.271  0.51 20.65 ? 861  LEU   A CB    1 
ATOM   6337  C  CG    A LEU   A 1  863  ? -22.807 81.795  77.119  0.49 21.74 ? 861  LEU   A CG    1 
ATOM   6338  C  CG    B LEU   A 1  863  ? -24.090 82.900  76.871  0.51 21.91 ? 861  LEU   A CG    1 
ATOM   6339  C  CD1   A LEU   A 1  863  ? -21.945 82.828  76.420  0.49 21.27 ? 861  LEU   A CD1   1 
ATOM   6340  C  CD1   B LEU   A 1  863  ? -23.998 82.823  78.387  0.51 20.74 ? 861  LEU   A CD1   1 
ATOM   6341  C  CD2   A LEU   A 1  863  ? -23.151 82.252  78.524  0.49 24.53 ? 861  LEU   A CD2   1 
ATOM   6342  C  CD2   B LEU   A 1  863  ? -22.923 83.673  76.290  0.51 24.90 ? 861  LEU   A CD2   1 
ATOM   6343  N  N     . THR   A 1  864  ? -26.872 80.452  75.306  1.00 19.04 ? 862  THR   A N     1 
ATOM   6344  C  CA    . THR   A 1  864  ? -28.273 80.632  74.950  1.00 19.61 ? 862  THR   A CA    1 
ATOM   6345  C  C     . THR   A 1  864  ? -29.162 79.831  75.883  1.00 18.04 ? 862  THR   A C     1 
ATOM   6346  O  O     . THR   A 1  864  ? -30.168 80.338  76.391  1.00 16.86 ? 862  THR   A O     1 
ATOM   6347  C  CB    . THR   A 1  864  ? -28.493 80.201  73.505  1.00 20.61 ? 862  THR   A CB    1 
ATOM   6348  O  OG1   . THR   A 1  864  ? -27.791 81.108  72.658  1.00 23.43 ? 862  THR   A OG1   1 
ATOM   6349  C  CG2   . THR   A 1  864  ? -29.992 80.212  73.150  1.00 21.30 ? 862  THR   A CG2   1 
ATOM   6350  N  N     . MET   A 1  865  ? -28.804 78.567  76.116  1.00 16.98 ? 863  MET   A N     1 
ATOM   6351  C  CA    . MET   A 1  865  ? -29.613 77.723  76.986  1.00 17.11 ? 863  MET   A CA    1 
ATOM   6352  C  C     . MET   A 1  865  ? -29.593 78.249  78.409  1.00 16.73 ? 863  MET   A C     1 
ATOM   6353  O  O     . MET   A 1  865  ? -30.625 78.280  79.082  1.00 16.09 ? 863  MET   A O     1 
ATOM   6354  C  CB    . MET   A 1  865  ? -29.095 76.286  76.939  1.00 17.81 ? 863  MET   A CB    1 
ATOM   6355  C  CG    . MET   A 1  865  ? -29.979 75.288  77.662  1.00 21.21 ? 863  MET   A CG    1 
ATOM   6356  S  SD    . MET   A 1  865  ? -29.292 73.630  77.524  1.00 24.29 ? 863  MET   A SD    1 
ATOM   6357  C  CE    . MET   A 1  865  ? -29.010 73.620  75.748  1.00 25.97 ? 863  MET   A CE    1 
ATOM   6358  N  N     . LEU   A 1  866  ? -28.424 78.692  78.865  1.00 16.22 ? 864  LEU   A N     1 
ATOM   6359  C  CA    . LEU   A 1  866  ? -28.302 79.227  80.211  1.00 15.82 ? 864  LEU   A CA    1 
ATOM   6360  C  C     . LEU   A 1  866  ? -29.175 80.460  80.385  1.00 15.41 ? 864  LEU   A C     1 
ATOM   6361  O  O     . LEU   A 1  866  ? -29.860 80.607  81.401  1.00 16.57 ? 864  LEU   A O     1 
ATOM   6362  C  CB    . LEU   A 1  866  ? -26.840 79.576  80.464  1.00 16.84 ? 864  LEU   A CB    1 
ATOM   6363  C  CG    . LEU   A 1  866  ? -26.569 80.143  81.850  1.00 21.31 ? 864  LEU   A CG    1 
ATOM   6364  C  CD1   . LEU   A 1  866  ? -27.022 79.166  82.933  1.00 22.19 ? 864  LEU   A CD1   1 
ATOM   6365  C  CD2   . LEU   A 1  866  ? -25.087 80.483  82.004  1.00 21.84 ? 864  LEU   A CD2   1 
ATOM   6366  N  N     . LYS   A 1  867  ? -29.142 81.374  79.415  1.00 17.01 ? 865  LYS   A N     1 
ATOM   6367  C  CA    . LYS   A 1  867  ? -29.961 82.572  79.535  1.00 17.73 ? 865  LYS   A CA    1 
ATOM   6368  C  C     . LYS   A 1  867  ? -31.441 82.225  79.523  1.00 18.69 ? 865  LYS   A C     1 
ATOM   6369  O  O     . LYS   A 1  867  ? -32.229 82.817  80.268  1.00 18.34 ? 865  LYS   A O     1 
ATOM   6370  C  CB    . LYS   A 1  867  ? -29.612 83.572  78.435  1.00 21.04 ? 865  LYS   A CB    1 
ATOM   6371  C  CG    . LYS   A 1  867  ? -28.221 84.173  78.614  1.00 21.26 ? 865  LYS   A CG    1 
ATOM   6372  C  CD    . LYS   A 1  867  ? -27.826 85.000  77.394  1.00 24.77 ? 865  LYS   A CD    1 
ATOM   6373  C  CE    . LYS   A 1  867  ? -26.392 85.493  77.514  1.00 30.26 ? 865  LYS   A CE    1 
ATOM   6374  N  NZ    . LYS   A 1  867  ? -25.927 86.164  76.263  1.00 31.79 ? 865  LYS   A NZ    1 
ATOM   6375  N  N     . GLY   A 1  868  ? -31.835 81.251  78.704  1.00 17.85 ? 866  GLY   A N     1 
ATOM   6376  C  CA    . GLY   A 1  868  ? -33.223 80.830  78.701  1.00 17.31 ? 866  GLY   A CA    1 
ATOM   6377  C  C     . GLY   A 1  868  ? -33.636 80.246  80.036  1.00 17.41 ? 866  GLY   A C     1 
ATOM   6378  O  O     . GLY   A 1  868  ? -34.734 80.516  80.532  1.00 19.04 ? 866  GLY   A O     1 
ATOM   6379  N  N     . ALA   A 1  869  ? -32.756 79.449  80.641  1.00 16.32 ? 867  ALA   A N     1 
ATOM   6380  C  CA    . ALA   A 1  869  ? -33.062 78.867  81.943  1.00 15.63 ? 867  ALA   A CA    1 
ATOM   6381  C  C     . ALA   A 1  869  ? -33.122 79.943  83.018  1.00 15.14 ? 867  ALA   A C     1 
ATOM   6382  O  O     . ALA   A 1  869  ? -33.970 79.881  83.920  1.00 17.84 ? 867  ALA   A O     1 
ATOM   6383  C  CB    . ALA   A 1  869  ? -32.012 77.817  82.296  1.00 17.05 ? 867  ALA   A CB    1 
ATOM   6384  N  N     . LEU   A 1  870  ? -32.224 80.933  82.934  1.00 17.23 ? 868  LEU   A N     1 
ATOM   6385  C  CA    . LEU   A 1  870  ? -32.215 82.045  83.879  1.00 17.96 ? 868  LEU   A CA    1 
ATOM   6386  C  C     . LEU   A 1  870  ? -33.580 82.707  83.941  1.00 19.64 ? 868  LEU   A C     1 
ATOM   6387  O  O     . LEU   A 1  870  ? -34.067 83.059  85.022  1.00 20.48 ? 868  LEU   A O     1 
ATOM   6388  C  CB    . LEU   A 1  870  ? -31.177 83.077  83.423  1.00 20.30 ? 868  LEU   A CB    1 
ATOM   6389  C  CG    . LEU   A 1  870  ? -30.840 84.245  84.355  1.00 23.86 ? 868  LEU   A CG    1 
ATOM   6390  C  CD1   . LEU   A 1  870  ? -29.854 83.803  85.421  1.00 26.42 ? 868  LEU   A CD1   1 
ATOM   6391  C  CD2   . LEU   A 1  870  ? -30.290 85.445  83.583  1.00 27.13 ? 868  LEU   A CD2   1 
ATOM   6392  N  N     . HIS   A 1  871  ? -34.212 82.889  82.788  1.00 16.94 ? 869  HIS   A N     1 
ATOM   6393  C  CA    . HIS   A 1  871  ? -35.473 83.618  82.766  1.00 20.16 ? 869  HIS   A CA    1 
ATOM   6394  C  C     . HIS   A 1  871  ? -36.650 82.819  83.298  1.00 22.69 ? 869  HIS   A C     1 
ATOM   6395  O  O     . HIS   A 1  871  ? -37.736 83.385  83.450  1.00 22.17 ? 869  HIS   A O     1 
ATOM   6396  C  CB    . HIS   A 1  871  ? -35.728 84.190  81.380  1.00 23.32 ? 869  HIS   A CB    1 
ATOM   6397  C  CG    . HIS   A 1  871  ? -34.817 85.332  81.058  1.00 26.64 ? 869  HIS   A CG    1 
ATOM   6398  N  ND1   . HIS   A 1  871  ? -34.961 86.578  81.631  1.00 29.33 ? 869  HIS   A ND1   1 
ATOM   6399  C  CD2   . HIS   A 1  871  ? -33.717 85.405  80.272  1.00 25.53 ? 869  HIS   A CD2   1 
ATOM   6400  C  CE1   . HIS   A 1  871  ? -34.005 87.376  81.192  1.00 30.70 ? 869  HIS   A CE1   1 
ATOM   6401  N  NE2   . HIS   A 1  871  ? -33.236 86.689  80.366  1.00 30.06 ? 869  HIS   A NE2   1 
ATOM   6402  N  N     . GLU   A 1  872  ? -36.457 81.550  83.619  1.00 17.23 ? 870  GLU   A N     1 
ATOM   6403  C  CA    . GLU   A 1  872  ? -37.507 80.747  84.224  1.00 18.55 ? 870  GLU   A CA    1 
ATOM   6404  C  C     . GLU   A 1  872  ? -37.445 80.756  85.740  1.00 18.58 ? 870  GLU   A C     1 
ATOM   6405  O  O     . GLU   A 1  872  ? -38.266 80.096  86.377  1.00 19.68 ? 870  GLU   A O     1 
ATOM   6406  C  CB    . GLU   A 1  872  ? -37.417 79.299  83.733  1.00 18.30 ? 870  GLU   A CB    1 
ATOM   6407  C  CG    . GLU   A 1  872  ? -37.596 79.154  82.228  1.00 19.94 ? 870  GLU   A CG    1 
ATOM   6408  C  CD    . GLU   A 1  872  ? -38.957 79.615  81.755  1.00 22.81 ? 870  GLU   A CD    1 
ATOM   6409  O  OE1   . GLU   A 1  872  ? -39.917 79.559  82.556  1.00 24.05 ? 870  GLU   A OE1   1 
ATOM   6410  O  OE2   . GLU   A 1  872  ? -39.070 80.042  80.580  1.00 23.30 ? 870  GLU   A OE2   1 
ATOM   6411  N  N     . LEU   A 1  873  ? -36.496 81.472  86.333  1.00 18.77 ? 871  LEU   A N     1 
ATOM   6412  C  CA    . LEU   A 1  873  ? -36.381 81.492  87.782  1.00 17.77 ? 871  LEU   A CA    1 
ATOM   6413  C  C     . LEU   A 1  873  ? -37.353 82.497  88.382  1.00 19.68 ? 871  LEU   A C     1 
ATOM   6414  O  O     . LEU   A 1  873  ? -37.572 83.582  87.832  1.00 21.65 ? 871  LEU   A O     1 
ATOM   6415  C  CB    . LEU   A 1  873  ? -34.962 81.872  88.198  1.00 19.44 ? 871  LEU   A CB    1 
ATOM   6416  C  CG    . LEU   A 1  873  ? -33.862 80.922  87.745  1.00 20.60 ? 871  LEU   A CG    1 
ATOM   6417  C  CD1   . LEU   A 1  873  ? -32.490 81.501  88.118  1.00 20.37 ? 871  LEU   A CD1   1 
ATOM   6418  C  CD2   . LEU   A 1  873  ? -34.075 79.564  88.380  1.00 23.74 ? 871  LEU   A CD2   1 
ATOM   6419  N  N     . HIS   A 1  874  ? -37.925 82.134  89.525  1.00 19.91 ? 872  HIS   A N     1 
ATOM   6420  C  CA    . HIS   A 1  874  ? -38.836 82.998  90.257  1.00 20.34 ? 872  HIS   A CA    1 
ATOM   6421  C  C     . HIS   A 1  874  ? -38.072 83.578  91.442  1.00 17.42 ? 872  HIS   A C     1 
ATOM   6422  O  O     . HIS   A 1  874  ? -37.595 82.832  92.306  1.00 19.31 ? 872  HIS   A O     1 
ATOM   6423  C  CB    . HIS   A 1  874  ? -40.043 82.186  90.728  1.00 21.87 ? 872  HIS   A CB    1 
ATOM   6424  C  CG    . HIS   A 1  874  ? -41.058 82.974  91.497  1.00 21.96 ? 872  HIS   A CG    1 
ATOM   6425  N  ND1   . HIS   A 1  874  ? -42.219 82.406  91.975  1.00 31.52 ? 872  HIS   A ND1   1 
ATOM   6426  C  CD2   . HIS   A 1  874  ? -41.100 84.278  91.859  1.00 27.83 ? 872  HIS   A CD2   1 
ATOM   6427  C  CE1   . HIS   A 1  874  ? -42.927 83.323  92.610  1.00 29.66 ? 872  HIS   A CE1   1 
ATOM   6428  N  NE2   . HIS   A 1  874  ? -42.272 84.468  92.554  1.00 25.25 ? 872  HIS   A NE2   1 
ATOM   6429  N  N     . ILE   A 1  875  ? -37.952 84.901  91.469  1.00 19.78 ? 873  ILE   A N     1 
ATOM   6430  C  CA    . ILE   A 1  875  ? -37.256 85.622  92.528  1.00 20.01 ? 873  ILE   A CA    1 
ATOM   6431  C  C     . ILE   A 1  875  ? -38.305 86.271  93.416  1.00 22.19 ? 873  ILE   A C     1 
ATOM   6432  O  O     . ILE   A 1  875  ? -39.213 86.950  92.922  1.00 23.52 ? 873  ILE   A O     1 
ATOM   6433  C  CB    . ILE   A 1  875  ? -36.301 86.682  91.955  1.00 21.51 ? 873  ILE   A CB    1 
ATOM   6434  C  CG1   . ILE   A 1  875  ? -35.082 86.038  91.291  1.00 29.04 ? 873  ILE   A CG1   1 
ATOM   6435  C  CG2   . ILE   A 1  875  ? -35.789 87.579  93.056  1.00 24.59 ? 873  ILE   A CG2   1 
ATOM   6436  C  CD1   . ILE   A 1  875  ? -35.336 85.392  89.960  1.00 34.35 ? 873  ILE   A CD1   1 
ATOM   6437  N  N     . GLY   A 1  876  ? -38.179 86.079  94.721  1.00 21.61 ? 874  GLY   A N     1 
ATOM   6438  C  CA    . GLY   A 1  876  ? -39.136 86.704  95.610  1.00 20.86 ? 874  GLY   A CA    1 
ATOM   6439  C  C     . GLY   A 1  876  ? -38.923 86.297  97.050  1.00 23.49 ? 874  GLY   A C     1 
ATOM   6440  O  O     . GLY   A 1  876  ? -37.943 85.634  97.397  1.00 21.41 ? 874  GLY   A O     1 
ATOM   6441  N  N     . ARG   A 1  877  ? -39.860 86.733  97.894  1.00 23.19 ? 875  ARG   A N     1 
ATOM   6442  C  CA    . ARG   A 1  877  ? -39.835 86.351  99.297  1.00 21.76 ? 875  ARG   A CA    1 
ATOM   6443  C  C     . ARG   A 1  877  ? -40.000 84.839  99.392  1.00 20.63 ? 875  ARG   A C     1 
ATOM   6444  O  O     . ARG   A 1  877  ? -40.829 84.248  98.695  1.00 21.73 ? 875  ARG   A O     1 
ATOM   6445  C  CB    . ARG   A 1  877  ? -40.965 87.067  100.032 1.00 27.65 ? 875  ARG   A CB    1 
ATOM   6446  C  CG    . ARG   A 1  877  ? -40.745 87.178  101.520 1.00 28.53 ? 875  ARG   A CG    1 
ATOM   6447  C  CD    . ARG   A 1  877  ? -41.885 87.951  102.163 1.00 27.71 ? 875  ARG   A CD    1 
ATOM   6448  N  NE    . ARG   A 1  877  ? -43.052 87.119  102.412 1.00 26.91 ? 875  ARG   A NE    1 
ATOM   6449  C  CZ    . ARG   A 1  877  ? -44.123 87.533  103.076 1.00 35.43 ? 875  ARG   A CZ    1 
ATOM   6450  N  NH1   . ARG   A 1  877  ? -44.202 88.763  103.554 1.00 36.00 ? 875  ARG   A NH1   1 
ATOM   6451  N  NH2   . ARG   A 1  877  ? -45.140 86.693  103.259 1.00 31.93 ? 875  ARG   A NH2   1 
ATOM   6452  N  N     . THR   A 1  878  ? -39.190 84.207  100.237 1.00 21.84 ? 876  THR   A N     1 
ATOM   6453  C  CA    . THR   A 1  878  ? -38.958 82.773  100.132 1.00 18.81 ? 876  THR   A CA    1 
ATOM   6454  C  C     . THR   A 1  878  ? -39.966 81.920  100.877 1.00 22.84 ? 876  THR   A C     1 
ATOM   6455  O  O     . THR   A 1  878  ? -39.775 80.701  100.959 1.00 21.88 ? 876  THR   A O     1 
ATOM   6456  C  CB    . THR   A 1  878  ? -37.538 82.429  100.584 1.00 21.12 ? 876  THR   A CB    1 
ATOM   6457  O  OG1   . THR   A 1  878  ? -37.286 83.036  101.853 1.00 24.16 ? 876  THR   A OG1   1 
ATOM   6458  C  CG2   . THR   A 1  878  ? -36.539 82.930  99.581  1.00 24.31 ? 876  THR   A CG2   1 
ATOM   6459  N  N     . ASP   A 1  879  ? -41.030 82.512  101.410 1.00 20.79 ? 877  ASP   A N     1 
ATOM   6460  C  CA    . ASP   A 1  879  ? -42.069 81.728  102.063 1.00 24.11 ? 877  ASP   A CA    1 
ATOM   6461  C  C     . ASP   A 1  879  ? -43.109 81.190  101.084 1.00 24.54 ? 877  ASP   A C     1 
ATOM   6462  O  O     . ASP   A 1  879  ? -44.257 80.937  101.475 1.00 23.05 ? 877  ASP   A O     1 
ATOM   6463  C  CB    . ASP   A 1  879  ? -42.717 82.528  103.195 1.00 19.39 ? 877  ASP   A CB    1 
ATOM   6464  C  CG    . ASP   A 1  879  ? -43.410 83.785  102.705 1.00 28.97 ? 877  ASP   A CG    1 
ATOM   6465  O  OD1   . ASP   A 1  879  ? -42.978 84.357  101.677 1.00 31.44 ? 877  ASP   A OD1   1 
ATOM   6466  O  OD2   . ASP   A 1  879  ? -44.398 84.196  103.347 1.00 30.35 ? 877  ASP   A OD2   1 
ATOM   6467  N  N     . ARG   A 1  880  ? -42.711 81.016  99.826  1.00 22.13 ? 878  ARG   A N     1 
ATOM   6468  C  CA    . ARG   A 1  880  ? -43.506 80.343  98.810  1.00 22.33 ? 878  ARG   A CA    1 
ATOM   6469  C  C     . ARG   A 1  880  ? -42.635 79.276  98.178  1.00 20.23 ? 878  ARG   A C     1 
ATOM   6470  O  O     . ARG   A 1  880  ? -41.499 79.557  97.788  1.00 21.39 ? 878  ARG   A O     1 
ATOM   6471  C  CB    . ARG   A 1  880  ? -43.963 81.304  97.712  1.00 25.17 ? 878  ARG   A CB    1 
ATOM   6472  C  CG    . ARG   A 1  880  ? -45.021 82.295  98.148  1.00 30.20 ? 878  ARG   A CG    1 
ATOM   6473  C  CD    . ARG   A 1  880  ? -45.365 83.217  96.982  1.00 33.47 ? 878  ARG   A CD    1 
ATOM   6474  N  NE    . ARG   A 1  880  ? -46.295 84.266  97.378  1.00 51.44 ? 878  ARG   A NE    1 
ATOM   6475  C  CZ    . ARG   A 1  880  ? -47.563 84.318  96.998  1.00 50.29 ? 878  ARG   A CZ    1 
ATOM   6476  N  NH1   . ARG   A 1  880  ? -48.080 83.403  96.194  1.00 53.81 ? 878  ARG   A NH1   1 
ATOM   6477  N  NH2   . ARG   A 1  880  ? -48.330 85.315  97.431  1.00 54.26 ? 878  ARG   A NH2   1 
ATOM   6478  N  N     . LEU   A 1  881  ? -43.167 78.055  98.085  1.00 19.25 ? 879  LEU   A N     1 
ATOM   6479  C  CA    . LEU   A 1  881  ? -42.437 76.962  97.450  1.00 18.56 ? 879  LEU   A CA    1 
ATOM   6480  C  C     . LEU   A 1  881  ? -42.028 77.299  96.020  1.00 19.51 ? 879  LEU   A C     1 
ATOM   6481  O  O     . LEU   A 1  881  ? -40.993 76.816  95.542  1.00 19.32 ? 879  LEU   A O     1 
ATOM   6482  C  CB    . LEU   A 1  881  ? -43.297 75.699  97.473  1.00 19.44 ? 879  LEU   A CB    1 
ATOM   6483  C  CG    . LEU   A 1  881  ? -42.663 74.423  96.936  1.00 21.84 ? 879  LEU   A CG    1 
ATOM   6484  C  CD1   . LEU   A 1  881  ? -41.535 73.955  97.861  1.00 23.16 ? 879  LEU   A CD1   1 
ATOM   6485  C  CD2   . LEU   A 1  881  ? -43.727 73.344  96.788  1.00 24.47 ? 879  LEU   A CD2   1 
ATOM   6486  N  N     . SER   A 1  882  ? -42.801 78.139  95.332  1.00 17.85 ? 880  SER   A N     1 
ATOM   6487  C  CA    . SER   A 1  882  ? -42.505 78.469  93.945  1.00 16.99 ? 880  SER   A CA    1 
ATOM   6488  C  C     . SER   A 1  882  ? -41.314 79.403  93.787  1.00 21.09 ? 880  SER   A C     1 
ATOM   6489  O  O     . SER   A 1  882  ? -40.888 79.641  92.655  1.00 20.97 ? 880  SER   A O     1 
ATOM   6490  C  CB    . SER   A 1  882  ? -43.726 79.103  93.282  1.00 21.09 ? 880  SER   A CB    1 
ATOM   6491  O  OG    . SER   A 1  882  ? -44.019 80.331  93.916  1.00 24.67 ? 880  SER   A OG    1 
ATOM   6492  N  N     . VAL   A 1  883  ? -40.757 79.928  94.872  1.00 19.65 ? 881  VAL   A N     1 
ATOM   6493  C  CA    . VAL   A 1  883  ? -39.627 80.846  94.764  1.00 19.93 ? 881  VAL   A CA    1 
ATOM   6494  C  C     . VAL   A 1  883  ? -38.329 80.064  94.630  1.00 20.90 ? 881  VAL   A C     1 
ATOM   6495  O  O     . VAL   A 1  883  ? -38.018 79.186  95.443  1.00 22.76 ? 881  VAL   A O     1 
ATOM   6496  C  CB    . VAL   A 1  883  ? -39.579 81.811  95.958  1.00 20.83 ? 881  VAL   A CB    1 
ATOM   6497  C  CG1   . VAL   A 1  883  ? -38.259 82.568  95.967  1.00 20.54 ? 881  VAL   A CG1   1 
ATOM   6498  C  CG2   . VAL   A 1  883  ? -40.722 82.782  95.855  1.00 20.61 ? 881  VAL   A CG2   1 
ATOM   6499  N  N     . ASP   A 1  884  ? -37.560 80.399  93.605  1.00 17.81 ? 882  ASP   A N     1 
ATOM   6500  C  CA    . ASP   A 1  884  ? -36.277 79.764  93.361  1.00 18.81 ? 882  ASP   A CA    1 
ATOM   6501  C  C     . ASP   A 1  884  ? -35.125 80.524  93.988  1.00 22.10 ? 882  ASP   A C     1 
ATOM   6502  O  O     . ASP   A 1  884  ? -34.176 79.910  94.492  1.00 24.91 ? 882  ASP   A O     1 
ATOM   6503  C  CB    . ASP   A 1  884  ? -36.047 79.690  91.856  1.00 20.29 ? 882  ASP   A CB    1 
ATOM   6504  C  CG    . ASP   A 1  884  ? -37.138 78.928  91.166  1.00 18.46 ? 882  ASP   A CG    1 
ATOM   6505  O  OD1   . ASP   A 1  884  ? -37.356 77.770  91.566  1.00 22.31 ? 882  ASP   A OD1   1 
ATOM   6506  O  OD2   . ASP   A 1  884  ? -37.780 79.492  90.262  1.00 20.44 ? 882  ASP   A OD2   1 
ATOM   6507  N  N     . VAL   A 1  885  ? -35.179 81.847  93.921  1.00 20.35 ? 883  VAL   A N     1 
ATOM   6508  C  CA    . VAL   A 1  885  ? -34.071 82.698  94.321  1.00 21.82 ? 883  VAL   A CA    1 
ATOM   6509  C  C     . VAL   A 1  885  ? -34.623 83.722  95.293  1.00 20.56 ? 883  VAL   A C     1 
ATOM   6510  O  O     . VAL   A 1  885  ? -35.556 84.460  94.958  1.00 19.89 ? 883  VAL   A O     1 
ATOM   6511  C  CB    . VAL   A 1  885  ? -33.430 83.390  93.110  1.00 22.03 ? 883  VAL   A CB    1 
ATOM   6512  C  CG1   . VAL   A 1  885  ? -32.312 84.336  93.560  1.00 22.73 ? 883  VAL   A CG1   1 
ATOM   6513  C  CG2   . VAL   A 1  885  ? -32.893 82.340  92.128  1.00 22.28 ? 883  VAL   A CG2   1 
ATOM   6514  N  N     . GLY   A 1  886  ? -34.065 83.755  96.497  1.00 20.68 ? 884  GLY   A N     1 
ATOM   6515  C  CA    . GLY   A 1  886  ? -34.489 84.704  97.490  1.00 19.52 ? 884  GLY   A CA    1 
ATOM   6516  C  C     . GLY   A 1  886  ? -33.689 85.983  97.453  1.00 19.83 ? 884  GLY   A C     1 
ATOM   6517  O  O     . GLY   A 1  886  ? -32.986 86.287  96.482  1.00 20.12 ? 884  GLY   A O     1 
ATOM   6518  N  N     . PRO   A 1  887  ? -33.775 86.755  98.524  1.00 20.67 ? 885  PRO   A N     1 
ATOM   6519  C  CA    . PRO   A 1  887  ? -33.132 88.068  98.553  1.00 19.80 ? 885  PRO   A CA    1 
ATOM   6520  C  C     . PRO   A 1  887  ? -31.659 87.952  98.908  1.00 20.75 ? 885  PRO   A C     1 
ATOM   6521  O  O     . PRO   A 1  887  ? -31.173 86.917  99.358  1.00 20.60 ? 885  PRO   A O     1 
ATOM   6522  C  CB    . PRO   A 1  887  ? -33.883 88.769  99.686  1.00 21.37 ? 885  PRO   A CB    1 
ATOM   6523  C  CG    . PRO   A 1  887  ? -34.188 87.657  100.639 1.00 22.69 ? 885  PRO   A CG    1 
ATOM   6524  C  CD    . PRO   A 1  887  ? -34.544 86.490  99.752  1.00 22.27 ? 885  PRO   A CD    1 
ATOM   6525  N  N     . VAL   A 1  888  ? -30.960 89.061  98.706  1.00 20.69 ? 886  VAL   A N     1 
ATOM   6526  C  CA    . VAL   A 1  888  ? -29.668 89.234  99.342  1.00 20.89 ? 886  VAL   A CA    1 
ATOM   6527  C  C     . VAL   A 1  888  ? -29.868 89.738  100.770 1.00 22.17 ? 886  VAL   A C     1 
ATOM   6528  O  O     . VAL   A 1  888  ? -30.900 90.316  101.121 1.00 21.95 ? 886  VAL   A O     1 
ATOM   6529  C  CB    . VAL   A 1  888  ? -28.727 90.129  98.514  1.00 23.87 ? 886  VAL   A CB    1 
ATOM   6530  C  CG1   . VAL   A 1  888  ? -28.504 89.498  97.139  1.00 22.93 ? 886  VAL   A CG1   1 
ATOM   6531  C  CG2   . VAL   A 1  888  ? -29.287 91.503  98.354  1.00 25.86 ? 886  VAL   A CG2   1 
ATOM   6532  N  N     . ILE   A 1  889  ? -28.876 89.478  101.618 1.00 20.90 ? 887  ILE   A N     1 
ATOM   6533  C  CA    . ILE   A 1  889  ? -29.117 89.535  103.059 1.00 22.40 ? 887  ILE   A CA    1 
ATOM   6534  C  C     . ILE   A 1  889  ? -29.369 90.961  103.536 1.00 22.31 ? 887  ILE   A C     1 
ATOM   6535  O  O     . ILE   A 1  889  ? -30.158 91.183  104.463 1.00 24.78 ? 887  ILE   A O     1 
ATOM   6536  C  CB    . ILE   A 1  889  ? -27.982 88.835  103.830 1.00 22.43 ? 887  ILE   A CB    1 
ATOM   6537  C  CG1   . ILE   A 1  889  ? -28.339 88.717  105.315 1.00 24.22 ? 887  ILE   A CG1   1 
ATOM   6538  C  CG2   . ILE   A 1  889  ? -26.647 89.572  103.647 1.00 22.61 ? 887  ILE   A CG2   1 
ATOM   6539  C  CD1   . ILE   A 1  889  ? -29.614 87.935  105.566 1.00 24.03 ? 887  ILE   A CD1   1 
ATOM   6540  N  N     . THR   A 1  890  ? -28.709 91.949  102.938 1.00 22.11 ? 888  THR   A N     1 
ATOM   6541  C  CA    . THR   A 1  890  ? -28.841 93.324  103.408 1.00 22.29 ? 888  THR   A CA    1 
ATOM   6542  C  C     . THR   A 1  890  ? -28.783 94.282  102.233 1.00 25.27 ? 888  THR   A C     1 
ATOM   6543  O  O     . THR   A 1  890  ? -28.336 93.934  101.137 1.00 23.45 ? 888  THR   A O     1 
ATOM   6544  C  CB    . THR   A 1  890  ? -27.707 93.731  104.363 1.00 26.57 ? 888  THR   A CB    1 
ATOM   6545  O  OG1   . THR   A 1  890  ? -26.448 93.607  103.688 1.00 27.48 ? 888  THR   A OG1   1 
ATOM   6546  C  CG2   . THR   A 1  890  ? -27.708 92.879  105.633 1.00 26.74 ? 888  THR   A CG2   1 
ATOM   6547  N  N     . SER   A 1  891  ? -29.192 95.526  102.493 1.00 26.99 ? 889  SER   A N     1 
ATOM   6548  C  CA    . SER   A 1  891  ? -29.070 96.556  101.466 1.00 25.36 ? 889  SER   A CA    1 
ATOM   6549  C  C     . SER   A 1  891  ? -27.612 96.863  101.160 1.00 27.04 ? 889  SER   A C     1 
ATOM   6550  O  O     . SER   A 1  891  ? -27.284 97.229  100.027 1.00 28.30 ? 889  SER   A O     1 
ATOM   6551  C  CB    . SER   A 1  891  ? -29.808 97.824  101.890 1.00 29.54 ? 889  SER   A CB    1 
ATOM   6552  O  OG    . SER   A 1  891  ? -29.258 98.321  103.089 1.00 37.54 ? 889  SER   A OG    1 
ATOM   6553  N  N     . GLU   A 1  892  ? -26.723 96.712  102.143 1.00 26.22 ? 890  GLU   A N     1 
ATOM   6554  C  CA    . GLU   A 1  892  ? -25.305 96.929  101.878 1.00 28.83 ? 890  GLU   A CA    1 
ATOM   6555  C  C     . GLU   A 1  892  ? -24.747 95.835  100.983 1.00 28.54 ? 890  GLU   A C     1 
ATOM   6556  O  O     . GLU   A 1  892  ? -23.936 96.106  100.090 1.00 28.10 ? 890  GLU   A O     1 
ATOM   6557  C  CB    . GLU   A 1  892  ? -24.517 96.989  103.184 1.00 30.66 ? 890  GLU   A CB    1 
ATOM   6558  C  CG    . GLU   A 1  892  ? -25.065 97.970  104.204 1.00 34.22 ? 890  GLU   A CG    1 
ATOM   6559  C  CD    . GLU   A 1  892  ? -25.989 97.302  105.210 1.00 39.13 ? 890  GLU   A CD    1 
ATOM   6560  O  OE1   . GLU   A 1  892  ? -27.175 97.098  104.893 1.00 37.37 ? 890  GLU   A OE1   1 
ATOM   6561  O  OE2   . GLU   A 1  892  ? -25.518 96.971  106.319 1.00 57.69 ? 890  GLU   A OE2   1 
ATOM   6562  N  N     . ALA   A 1  893  ? -25.148 94.588  101.226 1.00 25.74 ? 891  ALA   A N     1 
ATOM   6563  C  CA    . ALA   A 1  893  ? -24.759 93.521  100.315 1.00 25.38 ? 891  ALA   A CA    1 
ATOM   6564  C  C     . ALA   A 1  893  ? -25.290 93.796  98.917  1.00 29.06 ? 891  ALA   A C     1 
ATOM   6565  O  O     . ALA   A 1  893  ? -24.556 93.667  97.932  1.00 26.05 ? 891  ALA   A O     1 
ATOM   6566  C  CB    . ALA   A 1  893  ? -25.247 92.174  100.842 1.00 22.93 ? 891  ALA   A CB    1 
ATOM   6567  N  N     . LYS   A 1  894  ? -26.554 94.219  98.819  1.00 25.70 ? 892  LYS   A N     1 
ATOM   6568  C  CA    . LYS   A 1  894  ? -27.138 94.562  97.527  1.00 26.26 ? 892  LYS   A CA    1 
ATOM   6569  C  C     . LYS   A 1  894  ? -26.352 95.672  96.841  1.00 26.73 ? 892  LYS   A C     1 
ATOM   6570  O  O     . LYS   A 1  894  ? -26.038 95.581  95.650  1.00 29.16 ? 892  LYS   A O     1 
ATOM   6571  C  CB    . LYS   A 1  894  ? -28.599 94.974  97.713  1.00 25.17 ? 892  LYS   A CB    1 
ATOM   6572  C  CG    . LYS   A 1  894  ? -29.280 95.459  96.447  1.00 27.47 ? 892  LYS   A CG    1 
ATOM   6573  C  CD    . LYS   A 1  894  ? -30.739 95.815  96.713  1.00 28.52 ? 892  LYS   A CD    1 
ATOM   6574  C  CE    . LYS   A 1  894  ? -31.444 96.286  95.450  1.00 34.66 ? 892  LYS   A CE    1 
ATOM   6575  N  NZ    . LYS   A 1  894  ? -32.818 96.769  95.725  1.00 46.67 ? 892  LYS   A NZ    1 
ATOM   6576  N  N     . ASP   A 1  895  ? -26.025 96.735  97.579  1.00 26.78 ? 893  ASP   A N     1 
ATOM   6577  C  CA    . ASP   A 1  895  ? -25.266 97.833  96.987  1.00 32.20 ? 893  ASP   A CA    1 
ATOM   6578  C  C     . ASP   A 1  895  ? -23.908 97.365  96.481  1.00 28.99 ? 893  ASP   A C     1 
ATOM   6579  O  O     . ASP   A 1  895  ? -23.451 97.798  95.417  1.00 29.59 ? 893  ASP   A O     1 
ATOM   6580  C  CB    . ASP   A 1  895  ? -25.087 98.960  98.005  1.00 32.20 ? 893  ASP   A CB    1 
ATOM   6581  C  CG    . ASP   A 1  895  ? -26.378 99.704  98.290  1.00 36.33 ? 893  ASP   A CG    1 
ATOM   6582  O  OD1   . ASP   A 1  895  ? -27.295 99.664  97.442  1.00 42.83 ? 893  ASP   A OD1   1 
ATOM   6583  O  OD2   . ASP   A 1  895  ? -26.471 100.341 99.364  1.00 39.06 ? 893  ASP   A OD2   1 
ATOM   6584  N  N     . ASN   A 1  896  ? -23.240 96.498  97.239  1.00 25.53 ? 894  ASN   A N     1 
ATOM   6585  C  CA    . ASN   A 1  896  ? -21.923 96.033  96.829  1.00 27.63 ? 894  ASN   A CA    1 
ATOM   6586  C  C     . ASN   A 1  896  ? -22.007 95.186  95.566  1.00 26.56 ? 894  ASN   A C     1 
ATOM   6587  O  O     . ASN   A 1  896  ? -21.173 95.327  94.662  1.00 27.11 ? 894  ASN   A O     1 
ATOM   6588  C  CB    . ASN   A 1  896  ? -21.274 95.257  97.971  1.00 29.31 ? 894  ASN   A CB    1 
ATOM   6589  C  CG    . ASN   A 1  896  ? -19.942 94.665  97.585  1.00 36.00 ? 894  ASN   A CG    1 
ATOM   6590  O  OD1   . ASN   A 1  896  ? -19.858 93.500  97.187  1.00 42.36 ? 894  ASN   A OD1   1 
ATOM   6591  N  ND2   . ASN   A 1  896  ? -18.887 95.462  97.698  1.00 43.87 ? 894  ASN   A ND2   1 
ATOM   6592  N  N     . ILE   A 1  897  ? -23.007 94.306  95.488  1.00 28.14 ? 895  ILE   A N     1 
ATOM   6593  C  CA    . ILE   A 1  897  ? -23.178 93.476  94.300  1.00 24.77 ? 895  ILE   A CA    1 
ATOM   6594  C  C     . ILE   A 1  897  ? -23.528 94.336  93.093  1.00 27.82 ? 895  ILE   A C     1 
ATOM   6595  O  O     . ILE   A 1  897  ? -22.957 94.170  92.009  1.00 29.07 ? 895  ILE   A O     1 
ATOM   6596  C  CB    . ILE   A 1  897  ? -24.240 92.395  94.563  1.00 23.68 ? 895  ILE   A CB    1 
ATOM   6597  C  CG1   . ILE   A 1  897  ? -23.822 91.505  95.734  1.00 26.18 ? 895  ILE   A CG1   1 
ATOM   6598  C  CG2   . ILE   A 1  897  ? -24.485 91.552  93.312  1.00 24.24 ? 895  ILE   A CG2   1 
ATOM   6599  C  CD1   . ILE   A 1  897  ? -24.998 90.765  96.369  1.00 24.46 ? 895  ILE   A CD1   1 
ATOM   6600  N  N     . GLU   A 1  898  ? -24.458 95.278  93.263  1.00 26.68 ? 896  GLU   A N     1 
ATOM   6601  C  CA    . GLU   A 1  898  ? -24.863 96.115  92.140  1.00 28.07 ? 896  GLU   A CA    1 
ATOM   6602  C  C     . GLU   A 1  898  ? -23.732 97.019  91.668  1.00 31.42 ? 896  GLU   A C     1 
ATOM   6603  O  O     . GLU   A 1  898  ? -23.617 97.282  90.465  1.00 32.84 ? 896  GLU   A O     1 
ATOM   6604  C  CB    . GLU   A 1  898  ? -26.111 96.923  92.500  1.00 28.45 ? 896  GLU   A CB    1 
ATOM   6605  C  CG    . GLU   A 1  898  ? -27.344 96.063  92.686  1.00 29.78 ? 896  GLU   A CG    1 
ATOM   6606  C  CD    . GLU   A 1  898  ? -28.569 96.865  93.083  1.00 35.16 ? 896  GLU   A CD    1 
ATOM   6607  O  OE1   . GLU   A 1  898  ? -28.407 97.970  93.647  1.00 39.46 ? 896  GLU   A OE1   1 
ATOM   6608  O  OE2   . GLU   A 1  898  ? -29.691 96.382  92.828  1.00 46.02 ? 896  GLU   A OE2   1 
ATOM   6609  N  N     . LYS   A 1  899  ? -22.899 97.511  92.587  1.00 30.39 ? 897  LYS   A N     1 
ATOM   6610  C  CA    . LYS   A 1  899  ? -21.741 98.290  92.175  1.00 29.52 ? 897  LYS   A CA    1 
ATOM   6611  C  C     . LYS   A 1  899  ? -20.842 97.471  91.263  1.00 35.65 ? 897  LYS   A C     1 
ATOM   6612  O  O     . LYS   A 1  899  ? -20.309 97.989  90.276  1.00 32.49 ? 897  LYS   A O     1 
ATOM   6613  C  CB    . LYS   A 1  899  ? -20.966 98.781  93.399  1.00 32.44 ? 897  LYS   A CB    1 
ATOM   6614  N  N     . HIS   A 1  900  ? -20.675 96.183  91.574  1.00 27.78 ? 898  HIS   A N     1 
ATOM   6615  C  CA    . HIS   A 1  900  ? -19.877 95.310  90.716  1.00 28.82 ? 898  HIS   A CA    1 
ATOM   6616  C  C     . HIS   A 1  900  ? -20.533 95.129  89.356  1.00 29.51 ? 898  HIS   A C     1 
ATOM   6617  O  O     . HIS   A 1  900  ? -19.856 95.190  88.324  1.00 33.52 ? 898  HIS   A O     1 
ATOM   6618  C  CB    . HIS   A 1  900  ? -19.682 93.947  91.377  1.00 24.94 ? 898  HIS   A CB    1 
ATOM   6619  C  CG    . HIS   A 1  900  ? -19.047 92.934  90.475  1.00 26.87 ? 898  HIS   A CG    1 
ATOM   6620  N  ND1   . HIS   A 1  900  ? -17.706 92.958  90.159  1.00 29.90 ? 898  HIS   A ND1   1 
ATOM   6621  C  CD2   . HIS   A 1  900  ? -19.577 91.892  89.793  1.00 27.17 ? 898  HIS   A CD2   1 
ATOM   6622  C  CE1   . HIS   A 1  900  ? -17.433 91.959  89.339  1.00 29.55 ? 898  HIS   A CE1   1 
ATOM   6623  N  NE2   . HIS   A 1  900  ? -18.551 91.300  89.097  1.00 26.95 ? 898  HIS   A NE2   1 
ATOM   6624  N  N     . ILE   A 1  901  ? -21.846 94.896  89.338  1.00 25.55 ? 899  ILE   A N     1 
ATOM   6625  C  CA    . ILE   A 1  901  ? -22.550 94.686  88.076  1.00 27.79 ? 899  ILE   A CA    1 
ATOM   6626  C  C     . ILE   A 1  901  ? -22.434 95.918  87.193  1.00 33.51 ? 899  ILE   A C     1 
ATOM   6627  O  O     . ILE   A 1  901  ? -22.199 95.813  85.984  1.00 34.29 ? 899  ILE   A O     1 
ATOM   6628  C  CB    . ILE   A 1  901  ? -24.019 94.308  88.334  1.00 28.03 ? 899  ILE   A CB    1 
ATOM   6629  C  CG1   . ILE   A 1  901  ? -24.109 92.970  89.066  1.00 25.33 ? 899  ILE   A CG1   1 
ATOM   6630  C  CG2   . ILE   A 1  901  ? -24.806 94.276  87.023  1.00 31.04 ? 899  ILE   A CG2   1 
ATOM   6631  C  CD1   . ILE   A 1  901  ? -25.505 92.659  89.599  1.00 27.59 ? 899  ILE   A CD1   1 
ATOM   6632  N  N     . GLU   A 1  902  ? -22.594 97.105  87.782  1.00 32.46 ? 900  GLU   A N     1 
ATOM   6633  C  CA    . GLU   A 1  902  ? -22.537 98.327  86.984  1.00 37.44 ? 900  GLU   A CA    1 
ATOM   6634  C  C     . GLU   A 1  902  ? -21.124 98.633  86.509  1.00 34.93 ? 900  GLU   A C     1 
ATOM   6635  O  O     . GLU   A 1  902  ? -20.949 99.178  85.413  1.00 41.48 ? 900  GLU   A O     1 
ATOM   6636  C  CB    . GLU   A 1  902  ? -23.144 99.503  87.751  1.00 37.87 ? 900  GLU   A CB    1 
ATOM   6637  C  CG    . GLU   A 1  902  ? -24.644 99.373  87.927  1.00 44.96 ? 900  GLU   A CG    1 
ATOM   6638  C  CD    . GLU   A 1  902  ? -25.336 98.955  86.641  1.00 48.40 ? 900  GLU   A CD    1 
ATOM   6639  O  OE1   . GLU   A 1  902  ? -25.249 99.705  85.644  1.00 48.06 ? 900  GLU   A OE1   1 
ATOM   6640  O  OE2   . GLU   A 1  902  ? -25.952 97.866  86.625  1.00 44.32 ? 900  GLU   A OE2   1 
ATOM   6641  N  N     . ARG   A 1  903  ? -20.112 98.290  87.305  1.00 35.45 ? 901  ARG   A N     1 
ATOM   6642  C  CA    . ARG   A 1  903  ? -18.733 98.414  86.843  1.00 40.40 ? 901  ARG   A CA    1 
ATOM   6643  C  C     . ARG   A 1  903  ? -18.493 97.540  85.614  1.00 43.34 ? 901  ARG   A C     1 
ATOM   6644  O  O     . ARG   A 1  903  ? -17.965 98.008  84.598  1.00 42.13 ? 901  ARG   A O     1 
ATOM   6645  C  CB    . ARG   A 1  903  ? -17.777 98.042  87.974  1.00 38.53 ? 901  ARG   A CB    1 
ATOM   6646  C  CG    . ARG   A 1  903  ? -16.309 98.209  87.640  1.00 49.03 ? 901  ARG   A CG    1 
ATOM   6647  C  CD    . ARG   A 1  903  ? -15.451 97.437  88.622  1.00 51.40 ? 901  ARG   A CD    1 
ATOM   6648  N  NE    . ARG   A 1  903  ? -14.140 97.122  88.068  1.00 66.78 ? 901  ARG   A NE    1 
ATOM   6649  C  CZ    . ARG   A 1  903  ? -13.483 95.993  88.297  1.00 64.98 ? 901  ARG   A CZ    1 
ATOM   6650  N  NH1   . ARG   A 1  903  ? -13.998 95.034  89.052  1.00 58.32 ? 901  ARG   A NH1   1 
ATOM   6651  N  NH2   . ARG   A 1  903  ? -12.284 95.817  87.749  1.00 66.35 ? 901  ARG   A NH2   1 
ATOM   6652  N  N     . MET   A 1  904  ? -18.888 96.266  85.687  1.00 37.40 ? 902  MET   A N     1 
ATOM   6653  C  CA    . MET   A 1  904  ? -18.782 95.383  84.529  1.00 35.57 ? 902  MET   A CA    1 
ATOM   6654  C  C     . MET   A 1  904  ? -19.569 95.933  83.347  1.00 39.37 ? 902  MET   A C     1 
ATOM   6655  O  O     . MET   A 1  904  ? -19.072 95.973  82.216  1.00 40.55 ? 902  MET   A O     1 
ATOM   6656  C  CB    . MET   A 1  904  ? -19.291 93.987  84.891  1.00 31.37 ? 902  MET   A CB    1 
ATOM   6657  C  CG    . MET   A 1  904  ? -18.497 93.300  85.968  1.00 32.82 ? 902  MET   A CG    1 
ATOM   6658  S  SD    . MET   A 1  904  ? -16.821 92.960  85.421  1.00 45.61 ? 902  MET   A SD    1 
ATOM   6659  C  CE    . MET   A 1  904  ? -15.882 94.098  86.436  1.00 41.74 ? 902  MET   A CE    1 
ATOM   6660  N  N     . ARG   A 1  905  ? -20.813 96.350  83.592  1.00 33.69 ? 903  ARG   A N     1 
ATOM   6661  C  CA    . ARG   A 1  905  ? -21.629 96.918  82.526  1.00 38.70 ? 903  ARG   A CA    1 
ATOM   6662  C  C     . ARG   A 1  905  ? -20.974 98.160  81.939  1.00 44.73 ? 903  ARG   A C     1 
ATOM   6663  O  O     . ARG   A 1  905  ? -21.042 98.392  80.727  1.00 39.12 ? 903  ARG   A O     1 
ATOM   6664  C  CB    . ARG   A 1  905  ? -23.016 97.258  83.063  1.00 40.92 ? 903  ARG   A CB    1 
ATOM   6665  C  CG    . ARG   A 1  905  ? -24.064 97.421  81.988  1.00 43.40 ? 903  ARG   A CG    1 
ATOM   6666  C  CD    . ARG   A 1  905  ? -25.324 98.034  82.554  1.00 45.40 ? 903  ARG   A CD    1 
ATOM   6667  N  NE    . ARG   A 1  905  ? -25.861 97.281  83.681  1.00 34.80 ? 903  ARG   A NE    1 
ATOM   6668  C  CZ    . ARG   A 1  905  ? -26.759 96.310  83.577  1.00 39.02 ? 903  ARG   A CZ    1 
ATOM   6669  N  NH1   . ARG   A 1  905  ? -27.171 95.870  82.398  1.00 39.79 ? 903  ARG   A NH1   1 
ATOM   6670  N  NH2   . ARG   A 1  905  ? -27.264 95.774  84.685  1.00 41.40 ? 903  ARG   A NH2   1 
ATOM   6671  N  N     . GLY   A 1  906  ? -20.335 98.969  82.786  1.00 42.59 ? 904  GLY   A N     1 
ATOM   6672  C  CA    . GLY   A 1  906  ? -19.646 100.154 82.310  1.00 48.47 ? 904  GLY   A CA    1 
ATOM   6673  C  C     . GLY   A 1  906  ? -18.415 99.856  81.482  1.00 50.64 ? 904  GLY   A C     1 
ATOM   6674  O  O     . GLY   A 1  906  ? -18.005 100.697 80.675  1.00 55.11 ? 904  GLY   A O     1 
ATOM   6675  N  N     . LEU   A 1  907  ? -17.817 98.681  81.663  1.00 48.43 ? 905  LEU   A N     1 
ATOM   6676  C  CA    . LEU   A 1  907  ? -16.664 98.267  80.874  1.00 46.63 ? 905  LEU   A CA    1 
ATOM   6677  C  C     . LEU   A 1  907  ? -17.048 97.687  79.519  1.00 46.15 ? 905  LEU   A C     1 
ATOM   6678  O  O     . LEU   A 1  907  ? -16.157 97.296  78.759  1.00 46.09 ? 905  LEU   A O     1 
ATOM   6679  C  CB    . LEU   A 1  907  ? -15.820 97.258  81.657  1.00 44.24 ? 905  LEU   A CB    1 
ATOM   6680  C  CG    . LEU   A 1  907  ? -15.154 97.817  82.913  1.00 50.96 ? 905  LEU   A CG    1 
ATOM   6681  C  CD1   . LEU   A 1  907  ? -14.211 96.794  83.536  1.00 53.00 ? 905  LEU   A CD1   1 
ATOM   6682  C  CD2   . LEU   A 1  907  ? -14.421 99.106  82.581  1.00 54.67 ? 905  LEU   A CD2   1 
ATOM   6683  N  N     . GLY   A 1  908  ? -18.341 97.623  79.202  1.00 40.66 ? 906  GLY   A N     1 
ATOM   6684  C  CA    . GLY   A 1  908  ? -18.806 97.084  77.944  1.00 39.58 ? 906  GLY   A CA    1 
ATOM   6685  C  C     . GLY   A 1  908  ? -19.218 95.629  77.977  1.00 37.41 ? 906  GLY   A C     1 
ATOM   6686  O  O     . GLY   A 1  908  ? -19.622 95.096  76.938  1.00 37.47 ? 906  GLY   A O     1 
ATOM   6687  N  N     . ARG   A 1  909  ? -19.150 94.978  79.133  1.00 38.97 ? 907  ARG   A N     1 
ATOM   6688  C  CA    . ARG   A 1  909  ? -19.444 93.555  79.204  1.00 31.34 ? 907  ARG   A CA    1 
ATOM   6689  C  C     . ARG   A 1  909  ? -20.939 93.304  79.050  1.00 35.18 ? 907  ARG   A C     1 
ATOM   6690  O  O     . ARG   A 1  909  ? -21.774 94.072  79.540  1.00 35.74 ? 907  ARG   A O     1 
ATOM   6691  C  CB    . ARG   A 1  909  ? -18.949 92.991  80.534  1.00 32.25 ? 907  ARG   A CB    1 
ATOM   6692  C  CG    . ARG   A 1  909  ? -17.507 93.359  80.870  1.00 33.97 ? 907  ARG   A CG    1 
ATOM   6693  C  CD    . ARG   A 1  909  ? -16.511 92.696  79.928  1.00 39.08 ? 907  ARG   A CD    1 
ATOM   6694  N  NE    . ARG   A 1  909  ? -15.137 92.826  80.410  1.00 40.59 ? 907  ARG   A NE    1 
ATOM   6695  C  CZ    . ARG   A 1  909  ? -14.221 93.632  79.885  1.00 50.79 ? 907  ARG   A CZ    1 
ATOM   6696  N  NH1   . ARG   A 1  909  ? -14.486 94.388  78.832  1.00 46.04 ? 907  ARG   A NH1   1 
ATOM   6697  N  NH2   . ARG   A 1  909  ? -13.007 93.676  80.428  1.00 42.09 ? 907  ARG   A NH2   1 
ATOM   6698  N  N     . LYS   A 1  910  ? -21.271 92.215  78.362  1.00 29.08 ? 908  LYS   A N     1 
ATOM   6699  C  CA    . LYS   A 1  910  ? -22.660 91.845  78.140  1.00 27.10 ? 908  LYS   A CA    1 
ATOM   6700  C  C     . LYS   A 1  910  ? -23.270 91.309  79.434  1.00 29.50 ? 908  LYS   A C     1 
ATOM   6701  O  O     . LYS   A 1  910  ? -22.719 90.399  80.065  1.00 27.35 ? 908  LYS   A O     1 
ATOM   6702  C  CB    . LYS   A 1  910  ? -22.717 90.788  77.038  1.00 31.00 ? 908  LYS   A CB    1 
ATOM   6703  C  CG    . LYS   A 1  910  ? -24.044 90.652  76.332  1.00 40.68 ? 908  LYS   A CG    1 
ATOM   6704  C  CD    . LYS   A 1  910  ? -23.849 89.881  75.038  1.00 39.19 ? 908  LYS   A CD    1 
ATOM   6705  C  CE    . LYS   A 1  910  ? -25.172 89.569  74.380  1.00 46.92 ? 908  LYS   A CE    1 
ATOM   6706  N  NZ    . LYS   A 1  910  ? -24.978 88.871  73.081  1.00 54.44 ? 908  LYS   A NZ    1 
ATOM   6707  N  N     . VAL   A 1  911  ? -24.408 91.877  79.831  1.00 27.73 ? 909  VAL   A N     1 
ATOM   6708  C  CA    . VAL   A 1  911  ? -25.025 91.612  81.130  1.00 28.55 ? 909  VAL   A CA    1 
ATOM   6709  C  C     . VAL   A 1  911  ? -26.463 91.171  80.901  1.00 26.05 ? 909  VAL   A C     1 
ATOM   6710  O  O     . VAL   A 1  911  ? -27.267 91.932  80.349  1.00 31.41 ? 909  VAL   A O     1 
ATOM   6711  C  CB    . VAL   A 1  911  ? -24.995 92.861  82.028  1.00 27.69 ? 909  VAL   A CB    1 
ATOM   6712  C  CG1   . VAL   A 1  911  ? -25.757 92.604  83.323  1.00 32.32 ? 909  VAL   A CG1   1 
ATOM   6713  C  CG2   . VAL   A 1  911  ? -23.560 93.295  82.308  1.00 28.28 ? 909  VAL   A CG2   1 
ATOM   6714  N  N     . GLU   A 1  912  ? -26.785 89.951  81.320  1.00 25.23 ? 910  GLU   A N     1 
ATOM   6715  C  CA    . GLU   A 1  912  ? -28.135 89.410  81.255  1.00 25.08 ? 910  GLU   A CA    1 
ATOM   6716  C  C     . GLU   A 1  912  ? -28.707 89.383  82.665  1.00 30.93 ? 910  GLU   A C     1 
ATOM   6717  O  O     . GLU   A 1  912  ? -28.064 88.871  83.587  1.00 25.74 ? 910  GLU   A O     1 
ATOM   6718  C  CB    . GLU   A 1  912  ? -28.116 87.990  80.680  1.00 24.76 ? 910  GLU   A CB    1 
ATOM   6719  C  CG    . GLU   A 1  912  ? -29.499 87.408  80.415  1.00 28.75 ? 910  GLU   A CG    1 
ATOM   6720  C  CD    . GLU   A 1  912  ? -30.108 87.939  79.130  1.00 33.59 ? 910  GLU   A CD    1 
ATOM   6721  O  OE1   . GLU   A 1  912  ? -29.364 88.539  78.327  1.00 31.78 ? 910  GLU   A OE1   1 
ATOM   6722  O  OE2   . GLU   A 1  912  ? -31.327 87.754  78.920  1.00 33.39 ? 910  GLU   A OE2   1 
ATOM   6723  N  N     . GLN   A 1  913  ? -29.903 89.943  82.838  1.00 28.42 ? 911  GLN   A N     1 
ATOM   6724  C  CA    . GLN   A 1  913  ? -30.525 89.989  84.152  1.00 27.82 ? 911  GLN   A CA    1 
ATOM   6725  C  C     . GLN   A 1  913  ? -31.998 89.635  84.047  1.00 33.75 ? 911  GLN   A C     1 
ATOM   6726  O  O     . GLN   A 1  913  ? -32.678 90.039  83.101  1.00 31.75 ? 911  GLN   A O     1 
ATOM   6727  C  CB    . GLN   A 1  913  ? -30.377 91.379  84.793  1.00 30.02 ? 911  GLN   A CB    1 
ATOM   6728  C  CG    . GLN   A 1  913  ? -28.961 91.747  85.176  1.00 29.67 ? 911  GLN   A CG    1 
ATOM   6729  C  CD    . GLN   A 1  913  ? -28.904 92.978  86.061  1.00 31.73 ? 911  GLN   A CD    1 
ATOM   6730  O  OE1   . GLN   A 1  913  ? -29.371 94.050  85.680  1.00 33.96 ? 911  GLN   A OE1   1 
ATOM   6731  N  NE2   . GLN   A 1  913  ? -28.348 92.824  87.257  1.00 26.69 ? 911  GLN   A NE2   1 
ATOM   6732  N  N     . ILE   A 1  914  ? -32.476 88.867  85.026  1.00 30.76 ? 912  ILE   A N     1 
ATOM   6733  C  CA    . ILE   A 1  914  ? -33.904 88.623  85.189  1.00 27.68 ? 912  ILE   A CA    1 
ATOM   6734  C  C     . ILE   A 1  914  ? -34.594 89.921  85.582  1.00 32.08 ? 912  ILE   A C     1 
ATOM   6735  O  O     . ILE   A 1  914  ? -34.038 90.740  86.327  1.00 28.94 ? 912  ILE   A O     1 
ATOM   6736  C  CB    . ILE   A 1  914  ? -34.087 87.567  86.292  1.00 39.20 ? 912  ILE   A CB    1 
ATOM   6737  C  CG1   . ILE   A 1  914  ? -33.615 86.202  85.812  1.00 35.59 ? 912  ILE   A CG1   1 
ATOM   6738  C  CG2   . ILE   A 1  914  ? -35.526 87.510  86.787  1.00 47.46 ? 912  ILE   A CG2   1 
ATOM   6739  C  CD1   . ILE   A 1  914  ? -33.559 85.212  86.927  1.00 33.75 ? 912  ILE   A CD1   1 
ATOM   6740  N  N     . GLY   A 1  915  ? -35.811 90.122  85.082  1.00 34.71 ? 913  GLY   A N     1 
ATOM   6741  C  CA    . GLY   A 1  915  ? -36.632 91.219  85.568  1.00 32.18 ? 913  GLY   A CA    1 
ATOM   6742  C  C     . GLY   A 1  915  ? -37.256 90.842  86.898  1.00 35.42 ? 913  GLY   A C     1 
ATOM   6743  O  O     . GLY   A 1  915  ? -37.808 89.748  87.049  1.00 41.76 ? 913  GLY   A O     1 
ATOM   6744  N  N     . LEU   A 1  916  ? -37.160 91.745  87.870  1.00 33.53 ? 914  LEU   A N     1 
ATOM   6745  C  CA    . LEU   A 1  916  ? -37.669 91.488  89.210  1.00 35.92 ? 914  LEU   A CA    1 
ATOM   6746  C  C     . LEU   A 1  916  ? -39.102 91.984  89.340  1.00 37.80 ? 914  LEU   A C     1 
ATOM   6747  O  O     . LEU   A 1  916  ? -39.457 93.043  88.817  1.00 39.98 ? 914  LEU   A O     1 
ATOM   6748  C  CB    . LEU   A 1  916  ? -36.804 92.194  90.254  1.00 36.19 ? 914  LEU   A CB    1 
ATOM   6749  C  CG    . LEU   A 1  916  ? -35.348 91.747  90.356  1.00 34.34 ? 914  LEU   A CG    1 
ATOM   6750  C  CD1   . LEU   A 1  916  ? -34.654 92.527  91.456  1.00 36.30 ? 914  LEU   A CD1   1 
ATOM   6751  C  CD2   . LEU   A 1  916  ? -35.281 90.253  90.618  1.00 41.44 ? 914  LEU   A CD2   1 
ATOM   6752  N  N     . ALA   A 1  917  ? -39.916 91.211  90.050  1.00 30.22 ? 915  ALA   A N     1 
ATOM   6753  C  CA    . ALA   A 1  917  ? -41.297 91.594  90.286  1.00 33.89 ? 915  ALA   A CA    1 
ATOM   6754  C  C     . ALA   A 1  917  ? -41.355 92.817  91.196  1.00 35.44 ? 915  ALA   A C     1 
ATOM   6755  O  O     . ALA   A 1  917  ? -40.416 93.117  91.943  1.00 37.51 ? 915  ALA   A O     1 
ATOM   6756  C  CB    . ALA   A 1  917  ? -42.064 90.437  90.923  1.00 35.26 ? 915  ALA   A CB    1 
ATOM   6757  N  N     . SER   A 1  918  ? -42.481 93.534  91.125  1.00 36.19 ? 916  SER   A N     1 
ATOM   6758  C  CA    . SER   A 1  918  ? -42.652 94.712  91.971  1.00 37.91 ? 916  SER   A CA    1 
ATOM   6759  C  C     . SER   A 1  918  ? -42.620 94.348  93.449  1.00 34.55 ? 916  SER   A C     1 
ATOM   6760  O  O     . SER   A 1  918  ? -42.194 95.163  94.274  1.00 33.85 ? 916  SER   A O     1 
ATOM   6761  C  CB    . SER   A 1  918  ? -43.966 95.420  91.633  1.00 38.49 ? 916  SER   A CB    1 
ATOM   6762  O  OG    . SER   A 1  918  ? -45.066 94.542  91.811  1.00 46.32 ? 916  SER   A OG    1 
ATOM   6763  N  N     . GLU   A 1  919  ? -43.066 93.136  93.796  1.00 35.46 ? 917  GLU   A N     1 
ATOM   6764  C  CA    . GLU   A 1  919  ? -43.114 92.713  95.192  1.00 33.66 ? 917  GLU   A CA    1 
ATOM   6765  C  C     . GLU   A 1  919  ? -41.738 92.689  95.838  1.00 34.28 ? 917  GLU   A C     1 
ATOM   6766  O  O     . GLU   A 1  919  ? -41.642 92.743  97.067  1.00 31.91 ? 917  GLU   A O     1 
ATOM   6767  C  CB    . GLU   A 1  919  ? -43.749 91.323  95.312  1.00 37.69 ? 917  GLU   A CB    1 
ATOM   6768  C  CG    . GLU   A 1  919  ? -45.259 91.284  95.101  1.00 42.91 ? 917  GLU   A CG    1 
ATOM   6769  C  CD    . GLU   A 1  919  ? -45.656 91.345  93.638  1.00 49.71 ? 917  GLU   A CD    1 
ATOM   6770  O  OE1   . GLU   A 1  919  ? -44.759 91.293  92.769  1.00 43.85 ? 917  GLU   A OE1   1 
ATOM   6771  O  OE2   . GLU   A 1  919  ? -46.870 91.440  93.358  1.00 54.58 ? 917  GLU   A OE2   1 
ATOM   6772  N  N     . THR   A 1  920  ? -40.671 92.615  95.045  1.00 31.77 ? 918  THR   A N     1 
ATOM   6773  C  CA    . THR   A 1  920  ? -39.335 92.588  95.621  1.00 29.60 ? 918  THR   A CA    1 
ATOM   6774  C  C     . THR   A 1  920  ? -38.945 93.925  96.240  1.00 29.30 ? 918  THR   A C     1 
ATOM   6775  O  O     . THR   A 1  920  ? -37.995 93.973  97.026  1.00 28.41 ? 918  THR   A O     1 
ATOM   6776  C  CB    . THR   A 1  920  ? -38.310 92.167  94.564  1.00 28.78 ? 918  THR   A CB    1 
ATOM   6777  O  OG1   . THR   A 1  920  ? -38.343 93.086  93.464  1.00 29.21 ? 918  THR   A OG1   1 
ATOM   6778  C  CG2   . THR   A 1  920  ? -38.601 90.752  94.061  1.00 27.26 ? 918  THR   A CG2   1 
ATOM   6779  N  N     . GLY   A 1  921  ? -39.667 95.007  95.917  1.00 31.03 ? 919  GLY   A N     1 
ATOM   6780  C  CA    . GLY   A 1  921  ? -39.280 96.324  96.401  1.00 32.84 ? 919  GLY   A CA    1 
ATOM   6781  C  C     . GLY   A 1  921  ? -39.256 96.443  97.914  1.00 29.21 ? 919  GLY   A C     1 
ATOM   6782  O  O     . GLY   A 1  921  ? -38.542 97.285  98.463  1.00 32.76 ? 919  GLY   A O     1 
ATOM   6783  N  N     . VAL   A 1  922  ? -40.025 95.602  98.610  1.00 28.63 ? 920  VAL   A N     1 
ATOM   6784  C  CA    . VAL   A 1  922  ? -40.048 95.648  100.071 1.00 28.36 ? 920  VAL   A CA    1 
ATOM   6785  C  C     . VAL   A 1  922  ? -38.862 94.940  100.707 1.00 27.85 ? 920  VAL   A C     1 
ATOM   6786  O  O     . VAL   A 1  922  ? -38.662 95.060  101.924 1.00 29.19 ? 920  VAL   A O     1 
ATOM   6787  C  CB    . VAL   A 1  922  ? -41.367 95.102  100.645 1.00 27.64 ? 920  VAL   A CB    1 
ATOM   6788  C  CG1   . VAL   A 1  922  ? -42.513 96.035  100.300 1.00 29.62 ? 920  VAL   A CG1   1 
ATOM   6789  C  CG2   . VAL   A 1  922  ? -41.631 93.712  100.106 1.00 28.52 ? 920  VAL   A CG2   1 
ATOM   6790  N  N     . GLY   A 1  923  ? -38.072 94.206  99.926  1.00 26.96 ? 921  GLY   A N     1 
ATOM   6791  C  CA    . GLY   A 1  923  ? -36.872 93.577  100.441 1.00 24.97 ? 921  GLY   A CA    1 
ATOM   6792  C  C     . GLY   A 1  923  ? -35.632 94.022  99.695  1.00 23.56 ? 921  GLY   A C     1 
ATOM   6793  O  O     . GLY   A 1  923  ? -35.661 95.030  98.987  1.00 26.01 ? 921  GLY   A O     1 
ATOM   6794  N  N     . THR   A 1  924  ? -34.535 93.283  99.830  1.00 24.85 ? 922  THR   A N     1 
ATOM   6795  C  CA    . THR   A 1  924  ? -33.282 93.625  99.156  1.00 23.78 ? 922  THR   A CA    1 
ATOM   6796  C  C     . THR   A 1  924  ? -32.948 92.481  98.211  1.00 24.72 ? 922  THR   A C     1 
ATOM   6797  O  O     . THR   A 1  924  ? -32.411 91.457  98.637  1.00 24.62 ? 922  THR   A O     1 
ATOM   6798  C  CB    . THR   A 1  924  ? -32.162 93.865  100.157 1.00 23.86 ? 922  THR   A CB    1 
ATOM   6799  O  OG1   . THR   A 1  924  ? -32.126 92.793  101.104 1.00 24.76 ? 922  THR   A OG1   1 
ATOM   6800  C  CG2   . THR   A 1  924  ? -32.404 95.177  100.895 1.00 26.96 ? 922  THR   A CG2   1 
ATOM   6801  N  N     . PHE   A 1  925  ? -33.267 92.655  96.936  1.00 22.67 ? 923  PHE   A N     1 
ATOM   6802  C  CA    . PHE   A 1  925  ? -33.073 91.615  95.942  1.00 20.82 ? 923  PHE   A CA    1 
ATOM   6803  C  C     . PHE   A 1  925  ? -32.110 92.103  94.872  1.00 22.41 ? 923  PHE   A C     1 
ATOM   6804  O  O     . PHE   A 1  925  ? -32.103 93.286  94.513  1.00 26.31 ? 923  PHE   A O     1 
ATOM   6805  C  CB    . PHE   A 1  925  ? -34.398 91.248  95.271  1.00 20.16 ? 923  PHE   A CB    1 
ATOM   6806  C  CG    . PHE   A 1  925  ? -35.345 90.517  96.160  1.00 22.93 ? 923  PHE   A CG    1 
ATOM   6807  C  CD1   . PHE   A 1  925  ? -36.187 91.209  97.013  1.00 22.14 ? 923  PHE   A CD1   1 
ATOM   6808  C  CD2   . PHE   A 1  925  ? -35.403 89.134  96.140  1.00 20.03 ? 923  PHE   A CD2   1 
ATOM   6809  C  CE1   . PHE   A 1  925  ? -37.084 90.532  97.822  1.00 24.25 ? 923  PHE   A CE1   1 
ATOM   6810  C  CE2   . PHE   A 1  925  ? -36.293 88.457  96.950  1.00 20.45 ? 923  PHE   A CE2   1 
ATOM   6811  C  CZ    . PHE   A 1  925  ? -37.135 89.157  97.790  1.00 21.85 ? 923  PHE   A CZ    1 
ATOM   6812  N  N     . VAL   A 1  926  ? -31.296 91.179  94.377  1.00 23.31 ? 924  VAL   A N     1 
ATOM   6813  C  CA    . VAL   A 1  926  ? -30.475 91.380  93.192  1.00 21.43 ? 924  VAL   A CA    1 
ATOM   6814  C  C     . VAL   A 1  926  ? -30.878 90.300  92.202  1.00 23.84 ? 924  VAL   A C     1 
ATOM   6815  O  O     . VAL   A 1  926  ? -30.898 89.124  92.564  1.00 22.42 ? 924  VAL   A O     1 
ATOM   6816  C  CB    . VAL   A 1  926  ? -28.970 91.282  93.500  1.00 21.88 ? 924  VAL   A CB    1 
ATOM   6817  C  CG1   . VAL   A 1  926  ? -28.166 91.336  92.214  1.00 24.55 ? 924  VAL   A CG1   1 
ATOM   6818  C  CG2   . VAL   A 1  926  ? -28.563 92.414  94.420  1.00 24.17 ? 924  VAL   A CG2   1 
ATOM   6819  N  N     . PRO   A 1  927  ? -31.223 90.636  90.967  1.00 23.51 ? 925  PRO   A N     1 
ATOM   6820  C  CA    . PRO   A 1  927  ? -31.635 89.602  90.025  1.00 22.91 ? 925  PRO   A CA    1 
ATOM   6821  C  C     . PRO   A 1  927  ? -30.453 88.730  89.656  1.00 22.96 ? 925  PRO   A C     1 
ATOM   6822  O  O     . PRO   A 1  927  ? -29.317 89.221  89.556  1.00 22.44 ? 925  PRO   A O     1 
ATOM   6823  C  CB    . PRO   A 1  927  ? -32.120 90.402  88.811  1.00 27.26 ? 925  PRO   A CB    1 
ATOM   6824  C  CG    . PRO   A 1  927  ? -31.377 91.685  88.882  1.00 27.81 ? 925  PRO   A CG    1 
ATOM   6825  C  CD    . PRO   A 1  927  ? -31.192 91.974  90.350  1.00 26.05 ? 925  PRO   A CD    1 
ATOM   6826  N  N     . PRO   A 1  928  ? -30.675 87.430  89.491  1.00 24.09 ? 926  PRO   A N     1 
ATOM   6827  C  CA    . PRO   A 1  928  ? -29.653 86.580  88.886  1.00 23.65 ? 926  PRO   A CA    1 
ATOM   6828  C  C     . PRO   A 1  928  ? -29.120 87.231  87.624  1.00 20.66 ? 926  PRO   A C     1 
ATOM   6829  O  O     . PRO   A 1  928  ? -29.878 87.733  86.782  1.00 23.72 ? 926  PRO   A O     1 
ATOM   6830  C  CB    . PRO   A 1  928  ? -30.421 85.290  88.588  1.00 20.61 ? 926  PRO   A CB    1 
ATOM   6831  C  CG    . PRO   A 1  928  ? -31.380 85.214  89.720  1.00 25.64 ? 926  PRO   A CG    1 
ATOM   6832  C  CD    . PRO   A 1  928  ? -31.840 86.643  89.933  1.00 25.86 ? 926  PRO   A CD    1 
ATOM   6833  N  N     . THR   A 1  929  ? -27.802 87.242  87.516  1.00 21.23 ? 927  THR   A N     1 
ATOM   6834  C  CA    . THR   A 1  929  ? -27.096 88.029  86.532  1.00 20.36 ? 927  THR   A CA    1 
ATOM   6835  C  C     . THR   A 1  929  ? -26.036 87.156  85.896  1.00 20.98 ? 927  THR   A C     1 
ATOM   6836  O  O     . THR   A 1  929  ? -25.359 86.391  86.585  1.00 23.08 ? 927  THR   A O     1 
ATOM   6837  C  CB    . THR   A 1  929  ? -26.449 89.231  87.212  1.00 24.91 ? 927  THR   A CB    1 
ATOM   6838  O  OG1   . THR   A 1  929  ? -27.480 90.019  87.821  1.00 23.74 ? 927  THR   A OG1   1 
ATOM   6839  C  CG2   . THR   A 1  929  ? -25.697 90.089  86.204  1.00 26.11 ? 927  THR   A CG2   1 
ATOM   6840  N  N     . ILE   A 1  930  ? -25.908 87.265  84.578  1.00 22.07 ? 928  ILE   A N     1 
ATOM   6841  C  CA    . ILE   A 1  930  ? -24.838 86.618  83.832  1.00 22.09 ? 928  ILE   A CA    1 
ATOM   6842  C  C     . ILE   A 1  930  ? -24.017 87.719  83.196  1.00 22.68 ? 928  ILE   A C     1 
ATOM   6843  O  O     . ILE   A 1  930  ? -24.569 88.589  82.510  1.00 26.98 ? 928  ILE   A O     1 
ATOM   6844  C  CB    . ILE   A 1  930  ? -25.395 85.685  82.745  1.00 19.82 ? 928  ILE   A CB    1 
ATOM   6845  C  CG1   . ILE   A 1  930  ? -26.138 84.508  83.371  1.00 25.78 ? 928  ILE   A CG1   1 
ATOM   6846  C  CG2   . ILE   A 1  930  ? -24.261 85.211  81.834  1.00 27.61 ? 928  ILE   A CG2   1 
ATOM   6847  C  CD1   . ILE   A 1  930  ? -26.982 83.714  82.368  1.00 25.53 ? 928  ILE   A CD1   1 
ATOM   6848  N  N     . ILE   A 1  931  ? -22.711 87.696  83.433  1.00 22.57 ? 929  ILE   A N     1 
ATOM   6849  C  CA    . ILE   A 1  931  ? -21.787 88.688  82.905  1.00 22.92 ? 929  ILE   A CA    1 
ATOM   6850  C  C     . ILE   A 1  931  ? -20.751 87.956  82.069  1.00 27.65 ? 929  ILE   A C     1 
ATOM   6851  O  O     . ILE   A 1  931  ? -20.052 87.071  82.572  1.00 25.21 ? 929  ILE   A O     1 
ATOM   6852  C  CB    . ILE   A 1  931  ? -21.110 89.493  84.024  1.00 27.43 ? 929  ILE   A CB    1 
ATOM   6853  C  CG1   . ILE   A 1  931  ? -22.161 90.223  84.868  1.00 26.03 ? 929  ILE   A CG1   1 
ATOM   6854  C  CG2   . ILE   A 1  931  ? -20.109 90.480  83.442  1.00 25.82 ? 929  ILE   A CG2   1 
ATOM   6855  C  CD1   . ILE   A 1  931  ? -21.561 91.131  85.921  1.00 26.93 ? 929  ILE   A CD1   1 
ATOM   6856  N  N     . GLU   A 1  932  ? -20.646 88.324  80.800  1.00 26.57 ? 930  GLU   A N     1 
ATOM   6857  C  CA    . GLU   A 1  932  ? -19.688 87.692  79.906  1.00 26.78 ? 930  GLU   A CA    1 
ATOM   6858  C  C     . GLU   A 1  932  ? -18.385 88.473  79.958  1.00 22.53 ? 930  GLU   A C     1 
ATOM   6859  O  O     . GLU   A 1  932  ? -18.351 89.662  79.621  1.00 26.64 ? 930  GLU   A O     1 
ATOM   6860  C  CB    . GLU   A 1  932  ? -20.263 87.638  78.494  1.00 25.56 ? 930  GLU   A CB    1 
ATOM   6861  C  CG    . GLU   A 1  932  ? -21.465 86.716  78.419  1.00 27.04 ? 930  GLU   A CG    1 
ATOM   6862  C  CD    . GLU   A 1  932  ? -22.213 86.849  77.123  1.00 32.55 ? 930  GLU   A CD    1 
ATOM   6863  O  OE1   . GLU   A 1  932  ? -21.560 86.810  76.060  1.00 30.17 ? 930  GLU   A OE1   1 
ATOM   6864  O  OE2   . GLU   A 1  932  ? -23.451 86.998  77.170  1.00 30.52 ? 930  GLU   A OE2   1 
ATOM   6865  N  N     . LEU   A 1  933  ? -17.322 87.815  80.404  1.00 26.56 ? 931  LEU   A N     1 
ATOM   6866  C  CA    . LEU   A 1  933  ? -16.018 88.442  80.552  1.00 24.55 ? 931  LEU   A CA    1 
ATOM   6867  C  C     . LEU   A 1  933  ? -15.098 88.084  79.393  1.00 35.64 ? 931  LEU   A C     1 
ATOM   6868  O  O     . LEU   A 1  933  ? -15.292 87.087  78.696  1.00 31.70 ? 931  LEU   A O     1 
ATOM   6869  C  CB    . LEU   A 1  933  ? -15.345 88.013  81.857  1.00 31.75 ? 931  LEU   A CB    1 
ATOM   6870  C  CG    . LEU   A 1  933  ? -16.054 88.376  83.162  1.00 33.79 ? 931  LEU   A CG    1 
ATOM   6871  C  CD1   . LEU   A 1  933  ? -15.189 87.969  84.334  1.00 38.21 ? 931  LEU   A CD1   1 
ATOM   6872  C  CD2   . LEU   A 1  933  ? -16.376 89.863  83.216  1.00 35.04 ? 931  LEU   A CD2   1 
ATOM   6873  N  N     . GLU   A 1  934  ? -14.068 88.913  79.215  1.00 30.90 ? 932  GLU   A N     1 
ATOM   6874  C  CA    . GLU   A 1  934  ? -13.003 88.637  78.258  1.00 38.11 ? 932  GLU   A CA    1 
ATOM   6875  C  C     . GLU   A 1  934  ? -11.912 87.766  78.871  1.00 39.93 ? 932  GLU   A C     1 
ATOM   6876  O  O     . GLU   A 1  934  ? -11.494 86.773  78.268  1.00 44.84 ? 932  GLU   A O     1 
ATOM   6877  C  CB    . GLU   A 1  934  ? -12.412 89.948  77.728  1.00 41.78 ? 932  GLU   A CB    1 
ATOM   6878  N  N     . LYS   A 1  935  ? -11.457 88.114  80.073  1.00 40.50 ? 933  LYS   A N     1 
ATOM   6879  C  CA    . LYS   A 1  935  ? -10.411 87.377  80.769  1.00 40.31 ? 933  LYS   A CA    1 
ATOM   6880  C  C     . LYS   A 1  935  ? -10.831 87.149  82.212  1.00 43.66 ? 933  LYS   A C     1 
ATOM   6881  O  O     . LYS   A 1  935  ? -11.616 87.919  82.771  1.00 41.26 ? 933  LYS   A O     1 
ATOM   6882  C  CB    . LYS   A 1  935  ? -9.092  88.156  80.765  1.00 38.45 ? 933  LYS   A CB    1 
ATOM   6883  N  N     . LEU   A 1  936  ? -10.300 86.081  82.815  1.00 42.19 ? 934  LEU   A N     1 
ATOM   6884  C  CA    . LEU   A 1  936  ? -10.551 85.834  84.231  1.00 42.65 ? 934  LEU   A CA    1 
ATOM   6885  C  C     . LEU   A 1  936  ? -9.939  86.915  85.108  1.00 43.79 ? 934  LEU   A C     1 
ATOM   6886  O  O     . LEU   A 1  936  ? -10.422 87.142  86.223  1.00 44.21 ? 934  LEU   A O     1 
ATOM   6887  C  CB    . LEU   A 1  936  ? -10.033 84.453  84.640  1.00 39.76 ? 934  LEU   A CB    1 
ATOM   6888  C  CG    . LEU   A 1  936  ? -10.958 83.593  85.512  1.00 44.75 ? 934  LEU   A CG    1 
ATOM   6889  C  CD1   . LEU   A 1  936  ? -10.447 82.162  85.590  1.00 39.09 ? 934  LEU   A CD1   1 
ATOM   6890  C  CD2   . LEU   A 1  936  ? -11.115 84.172  86.912  1.00 42.50 ? 934  LEU   A CD2   1 
ATOM   6891  N  N     . SER   A 1  937  ? -8.898  87.595  84.623  1.00 46.00 ? 935  SER   A N     1 
ATOM   6892  C  CA    . SER   A 1  937  ? -8.309  88.719  85.339  1.00 46.11 ? 935  SER   A CA    1 
ATOM   6893  C  C     . SER   A 1  937  ? -9.268  89.894  85.483  1.00 42.78 ? 935  SER   A C     1 
ATOM   6894  O  O     . SER   A 1  937  ? -8.979  90.815  86.257  1.00 45.39 ? 935  SER   A O     1 
ATOM   6895  C  CB    . SER   A 1  937  ? -7.042  89.180  84.616  1.00 47.63 ? 935  SER   A CB    1 
ATOM   6896  O  OG    . SER   A 1  937  ? -7.350  89.644  83.313  1.00 50.94 ? 935  SER   A OG    1 
ATOM   6897  N  N     . ASP   A 1  938  ? -10.388 89.898  84.753  1.00 45.89 ? 936  ASP   A N     1 
ATOM   6898  C  CA    . ASP   A 1  938  ? -11.390 90.943  84.929  1.00 43.06 ? 936  ASP   A CA    1 
ATOM   6899  C  C     . ASP   A 1  938  ? -11.994 90.932  86.326  1.00 46.18 ? 936  ASP   A C     1 
ATOM   6900  O  O     . ASP   A 1  938  ? -12.533 91.954  86.763  1.00 46.28 ? 936  ASP   A O     1 
ATOM   6901  C  CB    . ASP   A 1  938  ? -12.514 90.791  83.900  1.00 49.17 ? 936  ASP   A CB    1 
ATOM   6902  C  CG    . ASP   A 1  938  ? -12.051 91.047  82.482  1.00 51.32 ? 936  ASP   A CG    1 
ATOM   6903  O  OD1   . ASP   A 1  938  ? -10.896 91.487  82.300  1.00 50.89 ? 936  ASP   A OD1   1 
ATOM   6904  O  OD2   . ASP   A 1  938  ? -12.846 90.802  81.548  1.00 49.00 ? 936  ASP   A OD2   1 
ATOM   6905  N  N     . LEU   A 1  939  ? -11.934 89.804  87.027  1.00 41.79 ? 937  LEU   A N     1 
ATOM   6906  C  CA    . LEU   A 1  939  ? -12.441 89.720  88.388  1.00 42.48 ? 937  LEU   A CA    1 
ATOM   6907  C  C     . LEU   A 1  939  ? -11.338 90.047  89.382  1.00 46.63 ? 937  LEU   A C     1 
ATOM   6908  O  O     . LEU   A 1  939  ? -10.187 89.633  89.213  1.00 44.92 ? 937  LEU   A O     1 
ATOM   6909  C  CB    . LEU   A 1  939  ? -12.982 88.322  88.677  1.00 40.19 ? 937  LEU   A CB    1 
ATOM   6910  C  CG    . LEU   A 1  939  ? -14.192 87.884  87.861  1.00 38.30 ? 937  LEU   A CG    1 
ATOM   6911  C  CD1   . LEU   A 1  939  ? -14.804 86.653  88.483  1.00 38.00 ? 937  LEU   A CD1   1 
ATOM   6912  C  CD2   . LEU   A 1  939  ? -15.210 89.013  87.781  1.00 41.74 ? 937  LEU   A CD2   1 
ATOM   6913  N  N     . GLN   A 1  940  ? -11.702 90.787  90.428  1.00 40.91 ? 938  GLN   A N     1 
ATOM   6914  C  CA    . GLN   A 1  940  ? -10.761 91.178  91.471  1.00 46.71 ? 938  GLN   A CA    1 
ATOM   6915  C  C     . GLN   A 1  940  ? -10.956 90.360  92.744  1.00 46.74 ? 938  GLN   A C     1 
ATOM   6916  O  O     . GLN   A 1  940  ? -10.059 89.616  93.150  1.00 53.56 ? 938  GLN   A O     1 
ATOM   6917  C  CB    . GLN   A 1  940  ? -10.883 92.680  91.759  1.00 44.04 ? 938  GLN   A CB    1 
ATOM   6918  N  N     . ARG   A 1  941  ? -12.117 90.482  93.381  1.00 43.68 ? 939  ARG   A N     1 
ATOM   6919  C  CA    . ARG   A 1  941  ? -12.412 89.761  94.611  1.00 33.62 ? 939  ARG   A CA    1 
ATOM   6920  C  C     . ARG   A 1  941  ? -13.742 89.031  94.468  1.00 29.37 ? 939  ARG   A C     1 
ATOM   6921  O  O     . ARG   A 1  941  ? -14.490 89.231  93.506  1.00 33.50 ? 939  ARG   A O     1 
ATOM   6922  C  CB    . ARG   A 1  941  ? -12.441 90.704  95.824  1.00 38.98 ? 939  ARG   A CB    1 
ATOM   6923  N  N     . GLU   A 1  942  ? -14.009 88.156  95.435  1.00 28.48 ? 940  GLU   A N     1 
ATOM   6924  C  CA    . GLU   A 1  942  ? -15.279 87.446  95.509  1.00 25.43 ? 940  GLU   A CA    1 
ATOM   6925  C  C     . GLU   A 1  942  ? -16.435 88.436  95.526  1.00 23.94 ? 940  GLU   A C     1 
ATOM   6926  O  O     . GLU   A 1  942  ? -16.429 89.398  96.300  1.00 26.26 ? 940  GLU   A O     1 
ATOM   6927  C  CB    . GLU   A 1  942  ? -15.306 86.635  96.803  1.00 23.88 ? 940  GLU   A CB    1 
ATOM   6928  C  CG    . GLU   A 1  942  ? -16.615 85.899  97.068  1.00 22.19 ? 940  GLU   A CG    1 
ATOM   6929  C  CD    . GLU   A 1  942  ? -16.627 85.283  98.448  1.00 21.95 ? 940  GLU   A CD    1 
ATOM   6930  O  OE1   . GLU   A 1  942  ? -16.374 86.034  99.413  1.00 26.75 ? 940  GLU   A OE1   1 
ATOM   6931  O  OE2   . GLU   A 1  942  ? -16.854 84.063  98.573  1.00 20.93 ? 940  GLU   A OE2   1 
ATOM   6932  N  N     . VAL   A 1  943  ? -17.432 88.198  94.675  1.00 24.00 ? 941  VAL   A N     1 
ATOM   6933  C  CA    . VAL   A 1  943  ? -18.677 88.964  94.670  1.00 22.86 ? 941  VAL   A CA    1 
ATOM   6934  C  C     . VAL   A 1  943  ? -19.765 88.022  95.162  1.00 25.39 ? 941  VAL   A C     1 
ATOM   6935  O  O     . VAL   A 1  943  ? -20.179 87.101  94.445  1.00 22.62 ? 941  VAL   A O     1 
ATOM   6936  C  CB    . VAL   A 1  943  ? -19.002 89.529  93.281  1.00 24.74 ? 941  VAL   A CB    1 
ATOM   6937  C  CG1   . VAL   A 1  943  ? -20.336 90.272  93.292  1.00 24.84 ? 941  VAL   A CG1   1 
ATOM   6938  C  CG2   . VAL   A 1  943  ? -17.883 90.445  92.823  1.00 27.33 ? 941  VAL   A CG2   1 
ATOM   6939  N  N     . PHE   A 1  944  ? -20.212 88.241  96.397  1.00 24.52 ? 942  PHE   A N     1 
ATOM   6940  C  CA    . PHE   A 1  944  ? -21.039 87.274  97.114  1.00 20.18 ? 942  PHE   A CA    1 
ATOM   6941  C  C     . PHE   A 1  944  ? -22.509 87.560  96.818  1.00 23.19 ? 942  PHE   A C     1 
ATOM   6942  O  O     . PHE   A 1  944  ? -23.258 88.104  97.629  1.00 23.10 ? 942  PHE   A O     1 
ATOM   6943  C  CB    . PHE   A 1  944  ? -20.737 87.336  98.607  1.00 21.28 ? 942  PHE   A CB    1 
ATOM   6944  C  CG    . PHE   A 1  944  ? -21.117 86.094  99.360  1.00 20.34 ? 942  PHE   A CG    1 
ATOM   6945  C  CD1   . PHE   A 1  944  ? -20.438 84.907  99.158  1.00 19.49 ? 942  PHE   A CD1   1 
ATOM   6946  C  CD2   . PHE   A 1  944  ? -22.132 86.124  100.304 1.00 18.95 ? 942  PHE   A CD2   1 
ATOM   6947  C  CE1   . PHE   A 1  944  ? -20.788 83.768  99.870  1.00 18.54 ? 942  PHE   A CE1   1 
ATOM   6948  C  CE2   . PHE   A 1  944  ? -22.471 84.982  101.016 1.00 20.08 ? 942  PHE   A CE2   1 
ATOM   6949  C  CZ    . PHE   A 1  944  ? -21.805 83.809  100.795 1.00 18.32 ? 942  PHE   A CZ    1 
ATOM   6950  N  N     . GLY   A 1  945  ? -22.911 87.191  95.609  1.00 21.86 ? 943  GLY   A N     1 
ATOM   6951  C  CA    . GLY   A 1  945  ? -24.258 87.441  95.162  1.00 21.97 ? 943  GLY   A CA    1 
ATOM   6952  C  C     . GLY   A 1  945  ? -24.557 86.634  93.923  1.00 21.26 ? 943  GLY   A C     1 
ATOM   6953  O  O     . GLY   A 1  945  ? -23.755 85.800  93.494  1.00 21.02 ? 943  GLY   A O     1 
ATOM   6954  N  N     . PRO   A 1  946  ? -25.716 86.870  93.319  1.00 20.76 ? 944  PRO   A N     1 
ATOM   6955  C  CA    . PRO   A 1  946  ? -26.170 86.032  92.197  1.00 21.00 ? 944  PRO   A CA    1 
ATOM   6956  C  C     . PRO   A 1  946  ? -25.597 86.512  90.867  1.00 19.99 ? 944  PRO   A C     1 
ATOM   6957  O  O     . PRO   A 1  946  ? -26.322 86.911  89.953  1.00 22.02 ? 944  PRO   A O     1 
ATOM   6958  C  CB    . PRO   A 1  946  ? -27.691 86.197  92.269  1.00 21.19 ? 944  PRO   A CB    1 
ATOM   6959  C  CG    . PRO   A 1  946  ? -27.860 87.620  92.736  1.00 23.71 ? 944  PRO   A CG    1 
ATOM   6960  C  CD    . PRO   A 1  946  ? -26.701 87.908  93.678  1.00 21.78 ? 944  PRO   A CD    1 
ATOM   6961  N  N     . VAL   A 1  947  ? -24.274 86.464  90.750  1.00 21.79 ? 945  VAL   A N     1 
ATOM   6962  C  CA    . VAL   A 1  947  ? -23.584 87.042  89.606  1.00 21.30 ? 945  VAL   A CA    1 
ATOM   6963  C  C     . VAL   A 1  947  ? -22.645 85.995  89.037  1.00 21.70 ? 945  VAL   A C     1 
ATOM   6964  O  O     . VAL   A 1  947  ? -21.593 85.710  89.622  1.00 21.97 ? 945  VAL   A O     1 
ATOM   6965  C  CB    . VAL   A 1  947  ? -22.829 88.326  89.959  1.00 25.16 ? 945  VAL   A CB    1 
ATOM   6966  C  CG1   . VAL   A 1  947  ? -22.223 88.905  88.707  1.00 23.25 ? 945  VAL   A CG1   1 
ATOM   6967  C  CG2   . VAL   A 1  947  ? -23.785 89.327  90.620  1.00 22.44 ? 945  VAL   A CG2   1 
ATOM   6968  N  N     . LEU   A 1  948  ? -23.023 85.426  87.901  1.00 19.70 ? 946  LEU   A N     1 
ATOM   6969  C  CA    . LEU   A 1  948  ? -22.218 84.437  87.210  1.00 17.90 ? 946  LEU   A CA    1 
ATOM   6970  C  C     . LEU   A 1  948  ? -21.433 85.132  86.115  1.00 20.39 ? 946  LEU   A C     1 
ATOM   6971  O  O     . LEU   A 1  948  ? -22.002 85.881  85.315  1.00 24.41 ? 946  LEU   A O     1 
ATOM   6972  C  CB    . LEU   A 1  948  ? -23.126 83.392  86.577  1.00 19.96 ? 946  LEU   A CB    1 
ATOM   6973  C  CG    . LEU   A 1  948  ? -22.356 82.359  85.766  1.00 19.38 ? 946  LEU   A CG    1 
ATOM   6974  C  CD1   . LEU   A 1  948  ? -21.378 81.601  86.675  1.00 20.59 ? 946  LEU   A CD1   1 
ATOM   6975  C  CD2   . LEU   A 1  948  ? -23.353 81.447  85.109  1.00 22.41 ? 946  LEU   A CD2   1 
ATOM   6976  N  N     . HIS   A 1  949  ? -20.136 84.880  86.073  1.00 20.24 ? 947  HIS   A N     1 
ATOM   6977  C  CA    . HIS   A 1  949  ? -19.303 85.391  84.998  1.00 21.78 ? 947  HIS   A CA    1 
ATOM   6978  C  C     . HIS   A 1  949  ? -18.991 84.254  84.043  1.00 22.14 ? 947  HIS   A C     1 
ATOM   6979  O  O     . HIS   A 1  949  ? -18.858 83.102  84.459  1.00 21.87 ? 947  HIS   A O     1 
ATOM   6980  C  CB    . HIS   A 1  949  ? -18.030 86.003  85.553  1.00 22.50 ? 947  HIS   A CB    1 
ATOM   6981  C  CG    . HIS   A 1  949  ? -18.293 87.022  86.610  1.00 24.98 ? 947  HIS   A CG    1 
ATOM   6982  N  ND1   . HIS   A 1  949  ? -18.481 86.682  87.932  1.00 22.63 ? 947  HIS   A ND1   1 
ATOM   6983  C  CD2   . HIS   A 1  949  ? -18.447 88.365  86.536  1.00 28.01 ? 947  HIS   A CD2   1 
ATOM   6984  C  CE1   . HIS   A 1  949  ? -18.714 87.780  88.633  1.00 25.10 ? 947  HIS   A CE1   1 
ATOM   6985  N  NE2   . HIS   A 1  949  ? -18.700 88.812  87.809  1.00 25.96 ? 947  HIS   A NE2   1 
ATOM   6986  N  N     . VAL   A 1  950  ? -18.941 84.573  82.756  1.00 20.76 ? 948  VAL   A N     1 
ATOM   6987  C  CA    . VAL   A 1  950  ? -18.757 83.569  81.716  1.00 21.56 ? 948  VAL   A CA    1 
ATOM   6988  C  C     . VAL   A 1  950  ? -17.544 83.951  80.893  1.00 25.29 ? 948  VAL   A C     1 
ATOM   6989  O  O     . VAL   A 1  950  ? -17.460 85.076  80.387  1.00 26.39 ? 948  VAL   A O     1 
ATOM   6990  C  CB    . VAL   A 1  950  ? -20.009 83.430  80.830  1.00 22.73 ? 948  VAL   A CB    1 
ATOM   6991  C  CG1   . VAL   A 1  950  ? -19.759 82.404  79.715  1.00 24.34 ? 948  VAL   A CG1   1 
ATOM   6992  C  CG2   . VAL   A 1  950  ? -21.193 83.008  81.669  1.00 20.81 ? 948  VAL   A CG2   1 
ATOM   6993  N  N     . ILE   A 1  951  ? -16.603 83.023  80.774  1.00 21.67 ? 949  ILE   A N     1 
ATOM   6994  C  CA    . ILE   A 1  951  ? -15.474 83.190  79.873  1.00 23.02 ? 949  ILE   A CA    1 
ATOM   6995  C  C     . ILE   A 1  951  ? -15.446 82.017  78.906  1.00 22.32 ? 949  ILE   A C     1 
ATOM   6996  O  O     . ILE   A 1  951  ? -15.956 80.930  79.195  1.00 21.30 ? 949  ILE   A O     1 
ATOM   6997  C  CB    . ILE   A 1  951  ? -14.131 83.346  80.603  1.00 27.28 ? 949  ILE   A CB    1 
ATOM   6998  C  CG1   . ILE   A 1  951  ? -13.795 82.073  81.359  1.00 27.41 ? 949  ILE   A CG1   1 
ATOM   6999  C  CG2   . ILE   A 1  951  ? -14.187 84.531  81.558  1.00 32.58 ? 949  ILE   A CG2   1 
ATOM   7000  C  CD1   . ILE   A 1  951  ? -12.515 82.185  82.148  1.00 40.65 ? 949  ILE   A CD1   1 
ATOM   7001  N  N     . ARG   A 1  952  ? -14.855 82.255  77.740  1.00 22.30 ? 950  ARG   A N     1 
ATOM   7002  C  CA    . ARG   A 1  952  ? -14.737 81.247  76.701  1.00 21.36 ? 950  ARG   A CA    1 
ATOM   7003  C  C     . ARG   A 1  952  ? -13.271 80.887  76.533  1.00 20.20 ? 950  ARG   A C     1 
ATOM   7004  O  O     . ARG   A 1  952  ? -12.387 81.721  76.738  1.00 24.79 ? 950  ARG   A O     1 
ATOM   7005  C  CB    . ARG   A 1  952  ? -15.266 81.797  75.381  1.00 24.07 ? 950  ARG   A CB    1 
ATOM   7006  C  CG    . ARG   A 1  952  ? -16.643 82.412  75.501  1.00 24.22 ? 950  ARG   A CG    1 
ATOM   7007  C  CD    . ARG   A 1  952  ? -16.901 83.355  74.351  1.00 28.86 ? 950  ARG   A CD    1 
ATOM   7008  N  NE    . ARG   A 1  952  ? -17.272 82.645  73.134  1.00 32.39 ? 950  ARG   A NE    1 
ATOM   7009  C  CZ    . ARG   A 1  952  ? -18.516 82.534  72.690  1.00 30.39 ? 950  ARG   A CZ    1 
ATOM   7010  N  NH1   . ARG   A 1  952  ? -19.532 83.082  73.337  1.00 29.58 ? 950  ARG   A NH1   1 
ATOM   7011  N  NH2   . ARG   A 1  952  ? -18.748 81.854  71.570  1.00 27.88 ? 950  ARG   A NH2   1 
ATOM   7012  N  N     . TYR   A 1  953  ? -13.013 79.641  76.146  1.00 20.16 ? 951  TYR   A N     1 
ATOM   7013  C  CA    . TYR   A 1  953  ? -11.633 79.221  75.948  1.00 20.82 ? 951  TYR   A CA    1 
ATOM   7014  C  C     . TYR   A 1  953  ? -11.541 78.259  74.774  1.00 20.01 ? 951  TYR   A C     1 
ATOM   7015  O  O     . TYR   A 1  953  ? -12.463 77.483  74.512  1.00 20.74 ? 951  TYR   A O     1 
ATOM   7016  C  CB    . TYR   A 1  953  ? -11.037 78.574  77.216  1.00 21.34 ? 951  TYR   A CB    1 
ATOM   7017  C  CG    . TYR   A 1  953  ? -11.588 77.198  77.502  1.00 19.38 ? 951  TYR   A CG    1 
ATOM   7018  C  CD1   . TYR   A 1  953  ? -12.804 77.032  78.157  1.00 18.60 ? 951  TYR   A CD1   1 
ATOM   7019  C  CD2   . TYR   A 1  953  ? -10.893 76.061  77.106  1.00 20.02 ? 951  TYR   A CD2   1 
ATOM   7020  C  CE1   . TYR   A 1  953  ? -13.310 75.779  78.406  1.00 17.86 ? 951  TYR   A CE1   1 
ATOM   7021  C  CE2   . TYR   A 1  953  ? -11.384 74.804  77.351  1.00 17.98 ? 951  TYR   A CE2   1 
ATOM   7022  C  CZ    . TYR   A 1  953  ? -12.597 74.661  78.006  1.00 18.36 ? 951  TYR   A CZ    1 
ATOM   7023  O  OH    . TYR   A 1  953  ? -13.086 73.403  78.242  1.00 20.84 ? 951  TYR   A OH    1 
ATOM   7024  N  N     . ARG   A 1  954  ? -10.405 78.322  74.076  1.00 23.26 ? 952  ARG   A N     1 
ATOM   7025  C  CA    . ARG   A 1  954  ? -10.088 77.355  73.035  1.00 23.38 ? 952  ARG   A CA    1 
ATOM   7026  C  C     . ARG   A 1  954  ? -9.501  76.105  73.675  1.00 20.08 ? 952  ARG   A C     1 
ATOM   7027  O  O     . ARG   A 1  954  ? -8.760  76.189  74.658  1.00 20.49 ? 952  ARG   A O     1 
ATOM   7028  C  CB    . ARG   A 1  954  ? -9.079  77.956  72.056  1.00 27.63 ? 952  ARG   A CB    1 
ATOM   7029  N  N     . ARG   A 1  955  ? -9.840  74.940  73.112  1.00 23.43 ? 953  ARG   A N     1 
ATOM   7030  C  CA    . ARG   A 1  955  ? -9.462  73.669  73.728  1.00 22.64 ? 953  ARG   A CA    1 
ATOM   7031  C  C     . ARG   A 1  955  ? -7.965  73.593  74.021  1.00 21.90 ? 953  ARG   A C     1 
ATOM   7032  O  O     . ARG   A 1  955  ? -7.555  73.115  75.085  1.00 24.41 ? 953  ARG   A O     1 
ATOM   7033  C  CB    . ARG   A 1  955  ? -9.898  72.497  72.840  1.00 29.02 ? 953  ARG   A CB    1 
ATOM   7034  C  CG    . ARG   A 1  955  ? -9.430  71.121  73.337  1.00 35.54 ? 953  ARG   A CG    1 
ATOM   7035  C  CD    . ARG   A 1  955  ? -9.780  70.960  74.803  1.00 41.20 ? 953  ARG   A CD    1 
ATOM   7036  N  NE    . ARG   A 1  955  ? -9.374  69.699  75.416  1.00 46.32 ? 953  ARG   A NE    1 
ATOM   7037  C  CZ    . ARG   A 1  955  ? -8.231  69.504  76.060  1.00 42.22 ? 953  ARG   A CZ    1 
ATOM   7038  N  NH1   . ARG   A 1  955  ? -7.296  70.440  76.114  1.00 33.73 ? 953  ARG   A NH1   1 
ATOM   7039  N  NH2   . ARG   A 1  955  ? -8.020  68.338  76.668  1.00 39.73 ? 953  ARG   A NH2   1 
ATOM   7040  N  N     . ASP   A 1  956  ? -7.130  74.065  73.095  1.00 22.85 ? 954  ASP   A N     1 
ATOM   7041  C  CA    . ASP   A 1  956  ? -5.692  73.968  73.321  1.00 23.00 ? 954  ASP   A CA    1 
ATOM   7042  C  C     . ASP   A 1  956  ? -5.225  74.841  74.472  1.00 26.05 ? 954  ASP   A C     1 
ATOM   7043  O  O     . ASP   A 1  956  ? -4.112  74.638  74.976  1.00 25.42 ? 954  ASP   A O     1 
ATOM   7044  C  CB    . ASP   A 1  956  ? -4.914  74.352  72.066  1.00 24.53 ? 954  ASP   A CB    1 
ATOM   7045  C  CG    . ASP   A 1  956  ? -5.057  73.335  70.953  1.00 31.66 ? 954  ASP   A CG    1 
ATOM   7046  O  OD1   . ASP   A 1  956  ? -5.422  72.177  71.252  1.00 32.21 ? 954  ASP   A OD1   1 
ATOM   7047  O  OD2   . ASP   A 1  956  ? -4.795  73.695  69.785  1.00 36.18 ? 954  ASP   A OD2   1 
ATOM   7048  N  N     . ASP   A 1  957  ? -6.035  75.811  74.888  1.00 22.35 ? 955  ASP   A N     1 
ATOM   7049  C  CA    . ASP   A 1  957  ? -5.684  76.697  75.986  1.00 23.24 ? 955  ASP   A CA    1 
ATOM   7050  C  C     . ASP   A 1  957  ? -6.213  76.213  77.327  1.00 21.64 ? 955  ASP   A C     1 
ATOM   7051  O  O     . ASP   A 1  957  ? -6.211  76.981  78.296  1.00 22.28 ? 955  ASP   A O     1 
ATOM   7052  C  CB    . ASP   A 1  957  ? -6.187  78.113  75.706  1.00 26.83 ? 955  ASP   A CB    1 
ATOM   7053  C  CG    . ASP   A 1  957  ? -5.485  78.757  74.530  1.00 33.76 ? 955  ASP   A CG    1 
ATOM   7054  O  OD1   . ASP   A 1  957  ? -4.310  78.409  74.276  1.00 32.47 ? 955  ASP   A OD1   1 
ATOM   7055  O  OD2   . ASP   A 1  957  ? -6.106  79.612  73.868  1.00 34.59 ? 955  ASP   A OD2   1 
ATOM   7056  N  N     . LEU   A 1  958  ? -6.660  74.958  77.407  1.00 21.61 ? 956  LEU   A N     1 
ATOM   7057  C  CA    . LEU   A 1  958  ? -7.226  74.462  78.658  1.00 21.43 ? 956  LEU   A CA    1 
ATOM   7058  C  C     . LEU   A 1  958  ? -6.222  74.561  79.801  1.00 20.28 ? 956  LEU   A C     1 
ATOM   7059  O  O     . LEU   A 1  958  ? -6.573  74.981  80.911  1.00 19.83 ? 956  LEU   A O     1 
ATOM   7060  C  CB    . LEU   A 1  958  ? -7.713  73.023  78.490  1.00 20.89 ? 956  LEU   A CB    1 
ATOM   7061  C  CG    . LEU   A 1  958  ? -8.230  72.335  79.756  1.00 21.28 ? 956  LEU   A CG    1 
ATOM   7062  C  CD1   . LEU   A 1  958  ? -9.405  73.099  80.359  1.00 22.11 ? 956  LEU   A CD1   1 
ATOM   7063  C  CD2   . LEU   A 1  958  ? -8.621  70.897  79.452  1.00 23.86 ? 956  LEU   A CD2   1 
ATOM   7064  N  N     . ASP   A 1  959  ? -4.964  74.195  79.556  1.00 17.93 ? 957  ASP   A N     1 
ATOM   7065  C  CA    . ASP   A 1  959  ? -3.994  74.236  80.642  1.00 20.49 ? 957  ASP   A CA    1 
ATOM   7066  C  C     . ASP   A 1  959  ? -3.749  75.665  81.097  1.00 20.00 ? 957  ASP   A C     1 
ATOM   7067  O  O     . ASP   A 1  959  ? -3.644  75.927  82.299  1.00 21.02 ? 957  ASP   A O     1 
ATOM   7068  C  CB    . ASP   A 1  959  ? -2.678  73.574  80.232  1.00 22.72 ? 957  ASP   A CB    1 
ATOM   7069  C  CG    . ASP   A 1  959  ? -1.807  73.256  81.426  1.00 25.14 ? 957  ASP   A CG    1 
ATOM   7070  O  OD1   . ASP   A 1  959  ? -2.280  72.528  82.319  1.00 23.71 ? 957  ASP   A OD1   1 
ATOM   7071  O  OD2   . ASP   A 1  959  ? -0.665  73.746  81.490  1.00 31.03 ? 957  ASP   A OD2   1 
ATOM   7072  N  N     . ARG   A 1  960  ? -3.666  76.602  80.151  1.00 20.48 ? 958  ARG   A N     1 
ATOM   7073  C  CA    . ARG   A 1  960  ? -3.541  78.010  80.509  1.00 23.23 ? 958  ARG   A CA    1 
ATOM   7074  C  C     . ARG   A 1  960  ? -4.743  78.465  81.326  1.00 21.81 ? 958  ARG   A C     1 
ATOM   7075  O  O     . ARG   A 1  960  ? -4.594  79.220  82.296  1.00 23.27 ? 958  ARG   A O     1 
ATOM   7076  C  CB    . ARG   A 1  960  ? -3.394  78.854  79.237  1.00 24.02 ? 958  ARG   A CB    1 
ATOM   7077  C  CG    . ARG   A 1  960  ? -3.133  80.348  79.466  1.00 27.13 ? 958  ARG   A CG    1 
ATOM   7078  C  CD    . ARG   A 1  960  ? -4.434  81.150  79.599  1.00 38.16 ? 958  ARG   A CD    1 
ATOM   7079  N  NE    . ARG   A 1  960  ? -5.334  80.956  78.467  1.00 39.29 ? 958  ARG   A NE    1 
ATOM   7080  C  CZ    . ARG   A 1  960  ? -6.655  81.074  78.528  1.00 42.74 ? 958  ARG   A CZ    1 
ATOM   7081  N  NH1   . ARG   A 1  960  ? -7.273  81.365  79.661  1.00 40.71 ? 958  ARG   A NH1   1 
ATOM   7082  N  NH2   . ARG   A 1  960  ? -7.374  80.892  77.424  1.00 45.43 ? 958  ARG   A NH2   1 
ATOM   7083  N  N     . LEU   A 1  961  ? -5.941  78.023  80.936  1.00 20.69 ? 959  LEU   A N     1 
ATOM   7084  C  CA    . LEU   A 1  961  ? -7.151  78.398  81.659  1.00 20.58 ? 959  LEU   A CA    1 
ATOM   7085  C  C     . LEU   A 1  961  ? -7.096  77.923  83.104  1.00 21.76 ? 959  LEU   A C     1 
ATOM   7086  O  O     . LEU   A 1  961  ? -7.425  78.680  84.026  1.00 20.89 ? 959  LEU   A O     1 
ATOM   7087  C  CB    . LEU   A 1  961  ? -8.377  77.820  80.961  1.00 20.41 ? 959  LEU   A CB    1 
ATOM   7088  C  CG    . LEU   A 1  961  ? -9.675  77.954  81.760  1.00 18.87 ? 959  LEU   A CG    1 
ATOM   7089  C  CD1   . LEU   A 1  961  ? -10.055 79.420  81.926  1.00 27.05 ? 959  LEU   A CD1   1 
ATOM   7090  C  CD2   . LEU   A 1  961  ? -10.777 77.159  81.082  1.00 22.52 ? 959  LEU   A CD2   1 
ATOM   7091  N  N     . VAL   A 1  962  ? -6.703  76.662  83.324  1.00 18.58 ? 960  VAL   A N     1 
ATOM   7092  C  CA    . VAL   A 1  962  ? -6.552  76.166  84.693  1.00 19.14 ? 960  VAL   A CA    1 
ATOM   7093  C  C     . VAL   A 1  962  ? -5.560  77.024  85.469  1.00 22.17 ? 960  VAL   A C     1 
ATOM   7094  O  O     . VAL   A 1  962  ? -5.776  77.333  86.647  1.00 20.67 ? 960  VAL   A O     1 
ATOM   7095  C  CB    . VAL   A 1  962  ? -6.175  74.674  84.707  1.00 21.09 ? 960  VAL   A CB    1 
ATOM   7096  C  CG1   . VAL   A 1  962  ? -5.851  74.217  86.141  1.00 22.83 ? 960  VAL   A CG1   1 
ATOM   7097  C  CG2   . VAL   A 1  962  ? -7.304  73.842  84.122  1.00 21.37 ? 960  VAL   A CG2   1 
ATOM   7098  N  N     . ASP   A 1  963  ? -4.464  77.430  84.824  1.00 21.85 ? 961  ASP   A N     1 
ATOM   7099  C  CA    . ASP   A 1  963  ? -3.549  78.376  85.456  1.00 22.65 ? 961  ASP   A CA    1 
ATOM   7100  C  C     . ASP   A 1  963  ? -4.277  79.657  85.842  1.00 22.22 ? 961  ASP   A C     1 
ATOM   7101  O  O     . ASP   A 1  963  ? -4.086  80.183  86.945  1.00 25.29 ? 961  ASP   A O     1 
ATOM   7102  C  CB    . ASP   A 1  963  ? -2.390  78.717  84.517  1.00 24.03 ? 961  ASP   A CB    1 
ATOM   7103  C  CG    . ASP   A 1  963  ? -1.381  77.601  84.388  1.00 32.36 ? 961  ASP   A CG    1 
ATOM   7104  O  OD1   . ASP   A 1  963  ? -1.349  76.703  85.250  1.00 40.38 ? 961  ASP   A OD1   1 
ATOM   7105  O  OD2   . ASP   A 1  963  ? -0.604  77.637  83.407  1.00 42.95 ? 961  ASP   A OD2   1 
ATOM   7106  N  N     . ASP   A 1  964  ? -5.105  80.183  84.932  1.00 21.92 ? 962  ASP   A N     1 
ATOM   7107  C  CA    . ASP   A 1  964  ? -5.850  81.407  85.219  1.00 24.23 ? 962  ASP   A CA    1 
ATOM   7108  C  C     . ASP   A 1  964  ? -6.780  81.227  86.414  1.00 26.87 ? 962  ASP   A C     1 
ATOM   7109  O  O     . ASP   A 1  964  ? -6.922  82.136  87.240  1.00 25.65 ? 962  ASP   A O     1 
ATOM   7110  C  CB    . ASP   A 1  964  ? -6.656  81.834  83.994  1.00 26.53 ? 962  ASP   A CB    1 
ATOM   7111  C  CG    . ASP   A 1  964  ? -5.779  82.349  82.876  1.00 31.11 ? 962  ASP   A CG    1 
ATOM   7112  O  OD1   . ASP   A 1  964  ? -4.577  82.585  83.118  1.00 36.38 ? 962  ASP   A OD1   1 
ATOM   7113  O  OD2   . ASP   A 1  964  ? -6.301  82.508  81.754  1.00 41.54 ? 962  ASP   A OD2   1 
ATOM   7114  N  N     . VAL   A 1  965  ? -7.441  80.075  86.511  1.00 21.05 ? 963  VAL   A N     1 
ATOM   7115  C  CA    . VAL   A 1  965  ? -8.288  79.816  87.673  1.00 22.11 ? 963  VAL   A CA    1 
ATOM   7116  C  C     . VAL   A 1  965  ? -7.452  79.815  88.945  1.00 23.54 ? 963  VAL   A C     1 
ATOM   7117  O  O     . VAL   A 1  965  ? -7.822  80.433  89.951  1.00 23.99 ? 963  VAL   A O     1 
ATOM   7118  C  CB    . VAL   A 1  965  ? -9.062  78.497  87.501  1.00 18.42 ? 963  VAL   A CB    1 
ATOM   7119  C  CG1   . VAL   A 1  965  ? -9.821  78.176  88.781  1.00 22.01 ? 963  VAL   A CG1   1 
ATOM   7120  C  CG2   . VAL   A 1  965  ? -10.026 78.596  86.330  1.00 20.90 ? 963  VAL   A CG2   1 
ATOM   7121  N  N     . ASN   A 1  966  ? -6.314  79.113  88.921  1.00 19.89 ? 964  ASN   A N     1 
ATOM   7122  C  CA    . ASN   A 1  966  ? -5.445  79.056  90.092  1.00 19.25 ? 964  ASN   A CA    1 
ATOM   7123  C  C     . ASN   A 1  966  ? -4.888  80.426  90.426  1.00 22.83 ? 964  ASN   A C     1 
ATOM   7124  O  O     . ASN   A 1  966  ? -4.644  80.730  91.599  1.00 23.35 ? 964  ASN   A O     1 
ATOM   7125  C  CB    . ASN   A 1  966  ? -4.287  78.082  89.848  1.00 21.95 ? 964  ASN   A CB    1 
ATOM   7126  C  CG    . ASN   A 1  966  ? -4.725  76.621  89.839  1.00 22.02 ? 964  ASN   A CG    1 
ATOM   7127  O  OD1   . ASN   A 1  966  ? -5.770  76.268  90.387  1.00 20.39 ? 964  ASN   A OD1   1 
ATOM   7128  N  ND2   . ASN   A 1  966  ? -3.906  75.758  89.231  1.00 22.44 ? 964  ASN   A ND2   1 
ATOM   7129  N  N     . ALA   A 1  967  ? -4.702  81.270  89.411  1.00 23.72 ? 965  ALA   A N     1 
ATOM   7130  C  CA    . ALA   A 1  967  ? -4.025  82.549  89.579  1.00 28.04 ? 965  ALA   A CA    1 
ATOM   7131  C  C     . ALA   A 1  967  ? -4.816  83.547  90.411  1.00 26.60 ? 965  ALA   A C     1 
ATOM   7132  O  O     . ALA   A 1  967  ? -4.234  84.544  90.852  1.00 29.27 ? 965  ALA   A O     1 
ATOM   7133  C  CB    . ALA   A 1  967  ? -3.680  83.154  88.215  1.00 32.28 ? 965  ALA   A CB    1 
ATOM   7134  N  N     . THR   A 1  968  ? -6.110  83.319  90.641  1.00 24.56 ? 966  THR   A N     1 
ATOM   7135  C  CA    . THR   A 1  968  ? -6.848  84.227  91.513  1.00 22.90 ? 966  THR   A CA    1 
ATOM   7136  C  C     . THR   A 1  968  ? -6.343  84.179  92.946  1.00 23.27 ? 966  THR   A C     1 
ATOM   7137  O  O     . THR   A 1  968  ? -6.547  85.142  93.691  1.00 25.91 ? 966  THR   A O     1 
ATOM   7138  C  CB    . THR   A 1  968  ? -8.331  83.877  91.544  1.00 22.03 ? 966  THR   A CB    1 
ATOM   7139  O  OG1   . THR   A 1  968  ? -8.508  82.625  92.218  1.00 22.90 ? 966  THR   A OG1   1 
ATOM   7140  C  CG2   . THR   A 1  968  ? -8.903  83.781  90.130  1.00 22.44 ? 966  THR   A CG2   1 
ATOM   7141  N  N     . GLY   A 1  969  ? -5.720  83.078  93.353  1.00 22.14 ? 967  GLY   A N     1 
ATOM   7142  C  CA    . GLY   A 1  969  ? -5.326  82.882  94.727  1.00 22.02 ? 967  GLY   A CA    1 
ATOM   7143  C  C     . GLY   A 1  969  ? -6.350  82.163  95.574  1.00 22.22 ? 967  GLY   A C     1 
ATOM   7144  O  O     . GLY   A 1  969  ? -6.006  81.672  96.652  1.00 20.77 ? 967  GLY   A O     1 
ATOM   7145  N  N     . TYR   A 1  970  ? -7.595  82.083  95.114  1.00 19.77 ? 968  TYR   A N     1 
ATOM   7146  C  CA    . TYR   A 1  970  ? -8.602  81.312  95.807  1.00 19.26 ? 968  TYR   A CA    1 
ATOM   7147  C  C     . TYR   A 1  970  ? -8.440  79.837  95.468  1.00 18.60 ? 968  TYR   A C     1 
ATOM   7148  O  O     . TYR   A 1  970  ? -7.650  79.452  94.602  1.00 23.30 ? 968  TYR   A O     1 
ATOM   7149  C  CB    . TYR   A 1  970  ? -9.994  81.798  95.419  1.00 20.15 ? 968  TYR   A CB    1 
ATOM   7150  C  CG    . TYR   A 1  970  ? -10.285 83.211  95.864  1.00 19.25 ? 968  TYR   A CG    1 
ATOM   7151  C  CD1   . TYR   A 1  970  ? -10.791 83.467  97.132  1.00 23.30 ? 968  TYR   A CD1   1 
ATOM   7152  C  CD2   . TYR   A 1  970  ? -10.078 84.286  95.009  1.00 24.32 ? 968  TYR   A CD2   1 
ATOM   7153  C  CE1   . TYR   A 1  970  ? -11.080 84.766  97.543  1.00 23.36 ? 968  TYR   A CE1   1 
ATOM   7154  C  CE2   . TYR   A 1  970  ? -10.364 85.585  95.409  1.00 25.82 ? 968  TYR   A CE2   1 
ATOM   7155  C  CZ    . TYR   A 1  970  ? -10.854 85.814  96.677  1.00 26.63 ? 968  TYR   A CZ    1 
ATOM   7156  O  OH    . TYR   A 1  970  ? -11.140 87.099  97.078  1.00 35.65 ? 968  TYR   A OH    1 
ATOM   7157  N  N     . GLY   A 1  971  ? -9.208  79.004  96.152  1.00 16.54 ? 969  GLY   A N     1 
ATOM   7158  C  CA    . GLY   A 1  971  ? -9.085  77.577  95.947  1.00 18.03 ? 969  GLY   A CA    1 
ATOM   7159  C  C     . GLY   A 1  971  ? -10.127 76.808  96.718  1.00 16.43 ? 969  GLY   A C     1 
ATOM   7160  O  O     . GLY   A 1  971  ? -9.794  75.883  97.468  1.00 16.58 ? 969  GLY   A O     1 
ATOM   7161  N  N     . LEU   A 1  972  ? -11.395 77.178  96.530  1.00 16.19 ? 970  LEU   A N     1 
ATOM   7162  C  CA    . LEU   A 1  972  ? -12.453 76.578  97.330  1.00 16.31 ? 970  LEU   A CA    1 
ATOM   7163  C  C     . LEU   A 1  972  ? -13.135 75.460  96.552  1.00 16.34 ? 970  LEU   A C     1 
ATOM   7164  O  O     . LEU   A 1  972  ? -12.737 74.302  96.668  1.00 17.01 ? 970  LEU   A O     1 
ATOM   7165  C  CB    . LEU   A 1  972  ? -13.425 77.640  97.833  1.00 17.06 ? 970  LEU   A CB    1 
ATOM   7166  C  CG    . LEU   A 1  972  ? -14.449 77.152  98.863  1.00 17.89 ? 970  LEU   A CG    1 
ATOM   7167  C  CD1   . LEU   A 1  972  ? -13.767 76.422  100.027 1.00 17.33 ? 970  LEU   A CD1   1 
ATOM   7168  C  CD2   . LEU   A 1  972  ? -15.246 78.341  99.379  1.00 19.02 ? 970  LEU   A CD2   1 
ATOM   7169  N  N     . THR   A 1  973  ? -14.139 75.779  95.743  1.00 15.53 ? 971  THR   A N     1 
ATOM   7170  C  CA    . THR   A 1  973  ? -14.783 74.754  94.939  1.00 16.25 ? 971  THR   A CA    1 
ATOM   7171  C  C     . THR   A 1  973  ? -14.398 74.915  93.478  1.00 16.47 ? 971  THR   A C     1 
ATOM   7172  O  O     . THR   A 1  973  ? -14.030 75.995  93.016  1.00 16.85 ? 971  THR   A O     1 
ATOM   7173  C  CB    . THR   A 1  973  ? -16.308 74.778  95.082  1.00 14.37 ? 971  THR   A CB    1 
ATOM   7174  O  OG1   . THR   A 1  973  ? -16.802 76.056  94.678  1.00 16.86 ? 971  THR   A OG1   1 
ATOM   7175  C  CG2   . THR   A 1  973  ? -16.716 74.469  96.500  1.00 16.56 ? 971  THR   A CG2   1 
ATOM   7176  N  N     . PHE   A 1  974  ? -14.497 73.810  92.751  1.00 15.57 ? 972  PHE   A N     1 
ATOM   7177  C  CA    . PHE   A 1  974  ? -14.181 73.801  91.336  1.00 15.08 ? 972  PHE   A CA    1 
ATOM   7178  C  C     . PHE   A 1  974  ? -14.969 72.684  90.686  1.00 14.20 ? 972  PHE   A C     1 
ATOM   7179  O  O     . PHE   A 1  974  ? -15.034 71.577  91.215  1.00 16.90 ? 972  PHE   A O     1 
ATOM   7180  C  CB    . PHE   A 1  974  ? -12.687 73.528  91.120  1.00 16.01 ? 972  PHE   A CB    1 
ATOM   7181  C  CG    . PHE   A 1  974  ? -12.330 73.335  89.684  1.00 15.01 ? 972  PHE   A CG    1 
ATOM   7182  C  CD1   . PHE   A 1  974  ? -12.163 74.425  88.856  1.00 15.35 ? 972  PHE   A CD1   1 
ATOM   7183  C  CD2   . PHE   A 1  974  ? -12.247 72.059  89.152  1.00 15.61 ? 972  PHE   A CD2   1 
ATOM   7184  C  CE1   . PHE   A 1  974  ? -11.861 74.256  87.517  1.00 17.59 ? 972  PHE   A CE1   1 
ATOM   7185  C  CE2   . PHE   A 1  974  ? -11.941 71.870  87.810  1.00 15.71 ? 972  PHE   A CE2   1 
ATOM   7186  C  CZ    . PHE   A 1  974  ? -11.755 72.967  86.995  1.00 17.02 ? 972  PHE   A CZ    1 
ATOM   7187  N  N     . GLY   A 1  975  ? -15.540 72.968  89.522  1.00 15.12 ? 973  GLY   A N     1 
ATOM   7188  C  CA    . GLY   A 1  975  ? -16.295 71.982  88.784  1.00 14.75 ? 973  GLY   A CA    1 
ATOM   7189  C  C     . GLY   A 1  975  ? -15.728 71.740  87.402  1.00 13.59 ? 973  GLY   A C     1 
ATOM   7190  O  O     . GLY   A 1  975  ? -15.166 72.636  86.771  1.00 15.15 ? 973  GLY   A O     1 
ATOM   7191  N  N     . LEU   A 1  976  ? -15.889 70.513  86.938  1.00 14.97 ? 974  LEU   A N     1 
ATOM   7192  C  CA    . LEU   A 1  976  ? -15.511 70.169  85.580  1.00 14.86 ? 974  LEU   A CA    1 
ATOM   7193  C  C     . LEU   A 1  976  ? -16.612 69.316  84.990  1.00 16.12 ? 974  LEU   A C     1 
ATOM   7194  O  O     . LEU   A 1  976  ? -16.998 68.302  85.578  1.00 16.59 ? 974  LEU   A O     1 
ATOM   7195  C  CB    . LEU   A 1  976  ? -14.214 69.366  85.597  1.00 16.17 ? 974  LEU   A CB    1 
ATOM   7196  C  CG    . LEU   A 1  976  ? -13.766 68.778  84.271  1.00 15.86 ? 974  LEU   A CG    1 
ATOM   7197  C  CD1   . LEU   A 1  976  ? -13.354 69.899  83.323  1.00 18.88 ? 974  LEU   A CD1   1 
ATOM   7198  C  CD2   . LEU   A 1  976  ? -12.603 67.859  84.558  1.00 20.36 ? 974  LEU   A CD2   1 
ATOM   7199  N  N     . HIS   A 1  977  ? -17.105 69.726  83.821  1.00 15.58 ? 975  HIS   A N     1 
ATOM   7200  C  CA    . HIS   A 1  977  ? -18.069 68.945  83.059  1.00 16.03 ? 975  HIS   A CA    1 
ATOM   7201  C  C     . HIS   A 1  977  ? -17.372 68.452  81.801  1.00 14.58 ? 975  HIS   A C     1 
ATOM   7202  O  O     . HIS   A 1  977  ? -17.047 69.246  80.908  1.00 16.53 ? 975  HIS   A O     1 
ATOM   7203  C  CB    . HIS   A 1  977  ? -19.300 69.779  82.708  1.00 17.09 ? 975  HIS   A CB    1 
ATOM   7204  C  CG    . HIS   A 1  977  ? -20.427 69.605  83.668  1.00 19.70 ? 975  HIS   A CG    1 
ATOM   7205  N  ND1   . HIS   A 1  977  ? -21.483 68.755  83.422  1.00 23.79 ? 975  HIS   A ND1   1 
ATOM   7206  C  CD2   . HIS   A 1  977  ? -20.639 70.124  84.900  1.00 25.81 ? 975  HIS   A CD2   1 
ATOM   7207  C  CE1   . HIS   A 1  977  ? -22.315 68.785  84.447  1.00 22.27 ? 975  HIS   A CE1   1 
ATOM   7208  N  NE2   . HIS   A 1  977  ? -21.831 69.615  85.352  1.00 21.83 ? 975  HIS   A NE2   1 
ATOM   7209  N  N     . THR   A 1  978  ? -17.163 67.146  81.742  1.00 14.43 ? 976  THR   A N     1 
ATOM   7210  C  CA    . THR   A 1  978  ? -16.563 66.506  80.583  1.00 16.33 ? 976  THR   A CA    1 
ATOM   7211  C  C     . THR   A 1  978  ? -16.845 65.024  80.678  1.00 16.01 ? 976  THR   A C     1 
ATOM   7212  O  O     . THR   A 1  978  ? -17.010 64.477  81.766  1.00 18.61 ? 976  THR   A O     1 
ATOM   7213  C  CB    . THR   A 1  978  ? -15.041 66.713  80.537  1.00 18.02 ? 976  THR   A CB    1 
ATOM   7214  O  OG1   . THR   A 1  978  ? -14.516 66.040  79.388  1.00 18.17 ? 976  THR   A OG1   1 
ATOM   7215  C  CG2   . THR   A 1  978  ? -14.368 66.118  81.766  1.00 19.33 ? 976  THR   A CG2   1 
ATOM   7216  N  N     . ARG   A 1  979  ? -16.876 64.374  79.526  1.00 16.90 ? 977  ARG   A N     1 
ATOM   7217  C  CA    . ARG   A 1  979  ? -16.950 62.926  79.497  1.00 18.72 ? 977  ARG   A CA    1 
ATOM   7218  C  C     . ARG   A 1  979  ? -15.592 62.268  79.315  1.00 16.77 ? 977  ARG   A C     1 
ATOM   7219  O  O     . ARG   A 1  979  ? -15.514 61.034  79.322  1.00 21.71 ? 977  ARG   A O     1 
ATOM   7220  C  CB    . ARG   A 1  979  ? -17.890 62.480  78.388  1.00 19.56 ? 977  ARG   A CB    1 
ATOM   7221  C  CG    . ARG   A 1  979  ? -19.320 62.875  78.666  1.00 23.72 ? 977  ARG   A CG    1 
ATOM   7222  C  CD    . ARG   A 1  979  ? -20.187 62.561  77.490  1.00 34.79 ? 977  ARG   A CD    1 
ATOM   7223  N  NE    . ARG   A 1  979  ? -21.592 62.770  77.797  1.00 38.11 ? 977  ARG   A NE    1 
ATOM   7224  C  CZ    . ARG   A 1  979  ? -22.576 62.555  76.937  1.00 47.50 ? 977  ARG   A CZ    1 
ATOM   7225  N  NH1   . ARG   A 1  979  ? -22.333 62.140  75.704  1.00 32.66 ? 977  ARG   A NH1   1 
ATOM   7226  N  NH2   . ARG   A 1  979  ? -23.832 62.757  77.325  1.00 42.81 ? 977  ARG   A NH2   1 
ATOM   7227  N  N     . LEU   A 1  980  ? -14.526 63.050  79.184  1.00 15.92 ? 978  LEU   A N     1 
ATOM   7228  C  CA    . LEU   A 1  980  ? -13.257 62.542  78.673  1.00 16.46 ? 978  LEU   A CA    1 
ATOM   7229  C  C     . LEU   A 1  980  ? -12.253 62.357  79.809  1.00 17.81 ? 978  LEU   A C     1 
ATOM   7230  O  O     . LEU   A 1  980  ? -11.866 63.327  80.478  1.00 17.33 ? 978  LEU   A O     1 
ATOM   7231  C  CB    . LEU   A 1  980  ? -12.705 63.497  77.620  1.00 16.65 ? 978  LEU   A CB    1 
ATOM   7232  C  CG    . LEU   A 1  980  ? -13.671 63.856  76.490  1.00 17.44 ? 978  LEU   A CG    1 
ATOM   7233  C  CD1   . LEU   A 1  980  ? -13.056 64.927  75.606  1.00 19.57 ? 978  LEU   A CD1   1 
ATOM   7234  C  CD2   . LEU   A 1  980  ? -14.049 62.614  75.674  1.00 20.33 ? 978  LEU   A CD2   1 
ATOM   7235  N  N     . ASP   A 1  981  ? -11.802 61.113  79.991  1.00 16.82 ? 979  ASP   A N     1 
ATOM   7236  C  CA    . ASP   A 1  981  ? -10.867 60.804  81.072  1.00 17.07 ? 979  ASP   A CA    1 
ATOM   7237  C  C     . ASP   A 1  981  ? -9.578  61.608  80.967  1.00 17.44 ? 979  ASP   A C     1 
ATOM   7238  O  O     . ASP   A 1  981  ? -9.002  61.981  81.997  1.00 17.51 ? 979  ASP   A O     1 
ATOM   7239  C  CB    . ASP   A 1  981  ? -10.529 59.314  81.082  1.00 17.70 ? 979  ASP   A CB    1 
ATOM   7240  C  CG    . ASP   A 1  981  ? -11.664 58.453  81.575  1.00 20.02 ? 979  ASP   A CG    1 
ATOM   7241  O  OD1   . ASP   A 1  981  ? -12.580 58.988  82.215  1.00 23.04 ? 979  ASP   A OD1   1 
ATOM   7242  O  OD2   . ASP   A 1  981  ? -11.629 57.225  81.324  1.00 24.30 ? 979  ASP   A OD2   1 
ATOM   7243  N  N     . GLU   A 1  982  ? -9.070  61.837  79.749  1.00 16.07 ? 980  GLU   A N     1 
ATOM   7244  C  CA    . GLU   A 1  982  ? -7.836  62.606  79.634  1.00 16.63 ? 980  GLU   A CA    1 
ATOM   7245  C  C     . GLU   A 1  982  ? -8.026  64.010  80.191  1.00 16.50 ? 980  GLU   A C     1 
ATOM   7246  O  O     . GLU   A 1  982  ? -7.151  64.542  80.886  1.00 17.40 ? 980  GLU   A O     1 
ATOM   7247  C  CB    . GLU   A 1  982  ? -7.371  62.670  78.181  1.00 18.74 ? 980  GLU   A CB    1 
ATOM   7248  C  CG    . GLU   A 1  982  ? -6.101  63.524  78.006  1.00 19.26 ? 980  GLU   A CG    1 
ATOM   7249  C  CD    . GLU   A 1  982  ? -5.828  63.908  76.564  1.00 26.97 ? 980  GLU   A CD    1 
ATOM   7250  O  OE1   . GLU   A 1  982  ? -6.755  64.387  75.888  1.00 29.23 ? 980  GLU   A OE1   1 
ATOM   7251  O  OE2   . GLU   A 1  982  ? -4.678  63.745  76.102  1.00 24.37 ? 980  GLU   A OE2   1 
ATOM   7252  N  N     . THR   A 1  983  ? -9.186  64.606  79.924  1.00 15.65 ? 981  THR   A N     1 
ATOM   7253  C  CA    . THR   A 1  983  ? -9.445  65.952  80.406  1.00 16.10 ? 981  THR   A CA    1 
ATOM   7254  C  C     . THR   A 1  983  ? -9.633  65.953  81.915  1.00 16.25 ? 981  THR   A C     1 
ATOM   7255  O  O     . THR   A 1  983  ? -9.143  66.857  82.602  1.00 17.17 ? 981  THR   A O     1 
ATOM   7256  C  CB    . THR   A 1  983  ? -10.669 66.518  79.682  1.00 16.86 ? 981  THR   A CB    1 
ATOM   7257  O  OG1   . THR   A 1  983  ? -10.373 66.634  78.281  1.00 19.24 ? 981  THR   A OG1   1 
ATOM   7258  C  CG2   . THR   A 1  983  ? -11.036 67.890  80.239  1.00 18.10 ? 981  THR   A CG2   1 
ATOM   7259  N  N     . ILE   A 1  984  ? -10.329 64.944  82.447  1.00 15.61 ? 982  ILE   A N     1 
ATOM   7260  C  CA    . ILE   A 1  984  ? -10.474 64.831  83.898  1.00 17.02 ? 982  ILE   A CA    1 
ATOM   7261  C  C     . ILE   A 1  984  ? -9.108  64.722  84.551  1.00 17.68 ? 982  ILE   A C     1 
ATOM   7262  O  O     . ILE   A 1  984  ? -8.814  65.413  85.531  1.00 17.45 ? 982  ILE   A O     1 
ATOM   7263  C  CB    . ILE   A 1  984  ? -11.366 63.638  84.275  1.00 16.95 ? 982  ILE   A CB    1 
ATOM   7264  C  CG1   . ILE   A 1  984  ? -12.800 63.884  83.823  1.00 17.56 ? 982  ILE   A CG1   1 
ATOM   7265  C  CG2   . ILE   A 1  984  ? -11.365 63.422  85.783  1.00 18.33 ? 982  ILE   A CG2   1 
ATOM   7266  C  CD1   . ILE   A 1  984  ? -13.707 62.667  83.956  1.00 19.96 ? 982  ILE   A CD1   1 
ATOM   7267  N  N     . ALA   A 1  985  ? -8.254  63.845  84.018  1.00 15.51 ? 983  ALA   A N     1 
ATOM   7268  C  CA    . ALA   A 1  985  ? -6.945  63.644  84.630  1.00 17.79 ? 983  ALA   A CA    1 
ATOM   7269  C  C     . ALA   A 1  985  ? -6.122  64.921  84.562  1.00 17.41 ? 983  ALA   A C     1 
ATOM   7270  O  O     . ALA   A 1  985  ? -5.501  65.326  85.552  1.00 17.97 ? 983  ALA   A O     1 
ATOM   7271  C  CB    . ALA   A 1  985  ? -6.223  62.496  83.925  1.00 18.94 ? 983  ALA   A CB    1 
ATOM   7272  N  N     . HIS   A 1  986  ? -6.119  65.578  83.405  1.00 16.94 ? 984  HIS   A N     1 
ATOM   7273  C  CA    . HIS   A 1  986  ? -5.358  66.811  83.245  1.00 18.64 ? 984  HIS   A CA    1 
ATOM   7274  C  C     . HIS   A 1  986  ? -5.862  67.874  84.206  1.00 17.76 ? 984  HIS   A C     1 
ATOM   7275  O  O     . HIS   A 1  986  ? -5.110  68.412  85.022  1.00 17.80 ? 984  HIS   A O     1 
ATOM   7276  C  CB    . HIS   A 1  986  ? -5.491  67.274  81.792  1.00 18.40 ? 984  HIS   A CB    1 
ATOM   7277  C  CG    . HIS   A 1  986  ? -4.945  68.643  81.510  1.00 21.08 ? 984  HIS   A CG    1 
ATOM   7278  N  ND1   . HIS   A 1  986  ? -5.151  69.281  80.305  1.00 26.85 ? 984  HIS   A ND1   1 
ATOM   7279  C  CD2   . HIS   A 1  986  ? -4.184  69.486  82.250  1.00 19.73 ? 984  HIS   A CD2   1 
ATOM   7280  C  CE1   . HIS   A 1  986  ? -4.555  70.460  80.322  1.00 28.53 ? 984  HIS   A CE1   1 
ATOM   7281  N  NE2   . HIS   A 1  986  ? -3.975  70.616  81.498  1.00 21.13 ? 984  HIS   A NE2   1 
ATOM   7282  N  N     . VAL   A 1  987  ? -7.153  68.176  84.136  1.00 17.06 ? 985  VAL   A N     1 
ATOM   7283  C  CA    . VAL   A 1  987  ? -7.679  69.295  84.907  1.00 18.55 ? 985  VAL   A CA    1 
ATOM   7284  C  C     . VAL   A 1  987  ? -7.547  69.038  86.402  1.00 18.22 ? 985  VAL   A C     1 
ATOM   7285  O  O     . VAL   A 1  987  ? -7.130  69.922  87.159  1.00 18.27 ? 985  VAL   A O     1 
ATOM   7286  C  CB    . VAL   A 1  987  ? -9.125  69.605  84.491  1.00 14.92 ? 985  VAL   A CB    1 
ATOM   7287  C  CG1   . VAL   A 1  987  ? -9.715  70.651  85.422  1.00 18.03 ? 985  VAL   A CG1   1 
ATOM   7288  C  CG2   . VAL   A 1  987  ? -9.142  70.104  83.056  1.00 20.52 ? 985  VAL   A CG2   1 
ATOM   7289  N  N     . THR   A 1  988  ? -7.899  67.830  86.860  1.00 16.48 ? 986  THR   A N     1 
ATOM   7290  C  CA    . THR   A 1  988  ? -7.868  67.612  88.307  1.00 18.00 ? 986  THR   A CA    1 
ATOM   7291  C  C     . THR   A 1  988  ? -6.442  67.545  88.833  1.00 23.95 ? 986  THR   A C     1 
ATOM   7292  O  O     . THR   A 1  988  ? -6.203  67.841  90.009  1.00 21.88 ? 986  THR   A O     1 
ATOM   7293  C  CB    . THR   A 1  988  ? -8.663  66.377  88.737  1.00 20.30 ? 986  THR   A CB    1 
ATOM   7294  O  OG1   . THR   A 1  988  ? -8.078  65.203  88.168  1.00 21.33 ? 986  THR   A OG1   1 
ATOM   7295  C  CG2   . THR   A 1  988  ? -10.105 66.488  88.298  1.00 21.97 ? 986  THR   A CG2   1 
ATOM   7296  N  N     . SER   A 1  989  ? -5.483  67.186  87.989  1.00 19.88 ? 987  SER   A N     1 
ATOM   7297  C  CA    . SER   A 1  989  ? -4.100  67.183  88.434  1.00 23.24 ? 987  SER   A CA    1 
ATOM   7298  C  C     . SER   A 1  989  ? -3.533  68.592  88.539  1.00 23.37 ? 987  SER   A C     1 
ATOM   7299  O  O     . SER   A 1  989  ? -2.609  68.816  89.329  1.00 29.54 ? 987  SER   A O     1 
ATOM   7300  C  CB    . SER   A 1  989  ? -3.238  66.308  87.513  1.00 22.02 ? 987  SER   A CB    1 
ATOM   7301  O  OG    . SER   A 1  989  ? -3.061  66.893  86.238  1.00 29.19 ? 987  SER   A OG    1 
ATOM   7302  N  N     . ARG   A 1  990  ? -4.082  69.550  87.793  1.00 17.75 ? 988  ARG   A N     1 
ATOM   7303  C  CA    . ARG   A 1  990  ? -3.511  70.889  87.718  1.00 20.01 ? 988  ARG   A CA    1 
ATOM   7304  C  C     . ARG   A 1  990  ? -4.266  71.919  88.536  1.00 19.54 ? 988  ARG   A C     1 
ATOM   7305  O  O     . ARG   A 1  990  ? -3.663  72.901  88.974  1.00 20.35 ? 988  ARG   A O     1 
ATOM   7306  C  CB    . ARG   A 1  990  ? -3.437  71.350  86.259  1.00 22.19 ? 988  ARG   A CB    1 
ATOM   7307  C  CG    . ARG   A 1  990  ? -2.686  70.387  85.366  1.00 30.92 ? 988  ARG   A CG    1 
ATOM   7308  C  CD    . ARG   A 1  990  ? -1.189  70.555  85.490  1.00 32.40 ? 988  ARG   A CD    1 
ATOM   7309  N  NE    . ARG   A 1  990  ? -0.693  71.527  84.524  1.00 29.37 ? 988  ARG   A NE    1 
ATOM   7310  C  CZ    . ARG   A 1  990  ? 0.572   71.915  84.439  1.00 27.41 ? 988  ARG   A CZ    1 
ATOM   7311  N  NH1   . ARG   A 1  990  ? 1.488   71.474  85.287  1.00 29.90 ? 988  ARG   A NH1   1 
ATOM   7312  N  NH2   . ARG   A 1  990  ? 0.925   72.757  83.473  1.00 28.99 ? 988  ARG   A NH2   1 
ATOM   7313  N  N     . ILE   A 1  991  ? -5.564  71.717  88.765  1.00 18.61 ? 989  ILE   A N     1 
ATOM   7314  C  CA    . ILE   A 1  991  ? -6.324  72.654  89.575  1.00 17.11 ? 989  ILE   A CA    1 
ATOM   7315  C  C     . ILE   A 1  991  ? -5.868  72.550  91.020  1.00 18.27 ? 989  ILE   A C     1 
ATOM   7316  O  O     . ILE   A 1  991  ? -5.467  71.481  91.494  1.00 20.70 ? 989  ILE   A O     1 
ATOM   7317  C  CB    . ILE   A 1  991  ? -7.827  72.342  89.437  1.00 17.48 ? 989  ILE   A CB    1 
ATOM   7318  C  CG1   . ILE   A 1  991  ? -8.671  73.488  90.002  1.00 19.58 ? 989  ILE   A CG1   1 
ATOM   7319  C  CG2   . ILE   A 1  991  ? -8.167  71.036  90.118  1.00 18.95 ? 989  ILE   A CG2   1 
ATOM   7320  C  CD1   . ILE   A 1  991  ? -8.595  74.741  89.165  1.00 23.47 ? 989  ILE   A CD1   1 
ATOM   7321  N  N     . LYS   A 1  992  ? -5.907  73.682  91.720  1.00 18.12 ? 990  LYS   A N     1 
ATOM   7322  C  CA    . LYS   A 1  992  ? -5.563  73.760  93.136  1.00 18.82 ? 990  LYS   A CA    1 
ATOM   7323  C  C     . LYS   A 1  992  ? -6.776  74.290  93.887  1.00 18.09 ? 990  LYS   A C     1 
ATOM   7324  O  O     . LYS   A 1  992  ? -6.890  75.489  94.145  1.00 20.13 ? 990  LYS   A O     1 
ATOM   7325  C  CB    . LYS   A 1  992  ? -4.360  74.662  93.333  1.00 19.65 ? 990  LYS   A CB    1 
ATOM   7326  C  CG    . LYS   A 1  992  ? -3.089  74.192  92.628  1.00 21.87 ? 990  LYS   A CG    1 
ATOM   7327  C  CD    . LYS   A 1  992  ? -2.017  75.281  92.723  1.00 33.02 ? 990  LYS   A CD    1 
ATOM   7328  C  CE    . LYS   A 1  992  ? -0.690  74.831  92.132  1.00 47.93 ? 990  LYS   A CE    1 
ATOM   7329  N  NZ    . LYS   A 1  992  ? 0.307   75.942  92.129  1.00 57.84 ? 990  LYS   A NZ    1 
ATOM   7330  N  N     . ALA   A 1  993  ? -7.680  73.385  94.230  1.00 18.53 ? 991  ALA   A N     1 
ATOM   7331  C  CA    . ALA   A 1  993  ? -8.861  73.734  95.002  1.00 16.97 ? 991  ALA   A CA    1 
ATOM   7332  C  C     . ALA   A 1  993  ? -9.185  72.599  95.954  1.00 17.37 ? 991  ALA   A C     1 
ATOM   7333  O  O     . ALA   A 1  993  ? -8.862  71.439  95.703  1.00 19.25 ? 991  ALA   A O     1 
ATOM   7334  C  CB    . ALA   A 1  993  ? -10.062 74.005  94.098  1.00 18.37 ? 991  ALA   A CB    1 
ATOM   7335  N  N     . GLY   A 1  994  ? -9.886  72.936  97.038  1.00 15.92 ? 992  GLY   A N     1 
ATOM   7336  C  CA    . GLY   A 1  994  ? -10.120 71.943  98.066  1.00 16.36 ? 992  GLY   A CA    1 
ATOM   7337  C  C     . GLY   A 1  994  ? -11.281 71.017  97.780  1.00 14.66 ? 992  GLY   A C     1 
ATOM   7338  O  O     . GLY   A 1  994  ? -11.317 69.894  98.288  1.00 15.77 ? 992  GLY   A O     1 
ATOM   7339  N  N     . ASN   A 1  995  ? -12.246 71.463  96.981  1.00 14.95 ? 993  ASN   A N     1 
ATOM   7340  C  CA    . ASN   A 1  995  ? -13.432 70.658  96.706  1.00 16.38 ? 993  ASN   A CA    1 
ATOM   7341  C  C     . ASN   A 1  995  ? -13.655 70.650  95.209  1.00 15.38 ? 993  ASN   A C     1 
ATOM   7342  O  O     . ASN   A 1  995  ? -13.951 71.692  94.617  1.00 16.06 ? 993  ASN   A O     1 
ATOM   7343  C  CB    . ASN   A 1  995  ? -14.659 71.174  97.452  1.00 15.94 ? 993  ASN   A CB    1 
ATOM   7344  C  CG    . ASN   A 1  995  ? -14.652 70.754  98.896  1.00 16.35 ? 993  ASN   A CG    1 
ATOM   7345  O  OD1   . ASN   A 1  995  ? -14.012 71.394  99.724  1.00 17.28 ? 993  ASN   A OD1   1 
ATOM   7346  N  ND2   . ASN   A 1  995  ? -15.338 69.664  99.203  1.00 17.12 ? 993  ASN   A ND2   1 
ATOM   7347  N  N     . LEU   A 1  996  ? -13.489 69.479  94.609  1.00 15.20 ? 994  LEU   A N     1 
ATOM   7348  C  CA    . LEU   A 1  996  ? -13.648 69.311  93.177  1.00 14.85 ? 994  LEU   A CA    1 
ATOM   7349  C  C     . LEU   A 1  996  ? -14.926 68.540  92.916  1.00 14.49 ? 994  LEU   A C     1 
ATOM   7350  O  O     . LEU   A 1  996  ? -15.309 67.670  93.697  1.00 14.88 ? 994  LEU   A O     1 
ATOM   7351  C  CB    . LEU   A 1  996  ? -12.486 68.504  92.596  1.00 16.65 ? 994  LEU   A CB    1 
ATOM   7352  C  CG    . LEU   A 1  996  ? -11.104 68.946  93.061  1.00 16.71 ? 994  LEU   A CG    1 
ATOM   7353  C  CD1   . LEU   A 1  996  ? -10.045 68.091  92.373  1.00 19.30 ? 994  LEU   A CD1   1 
ATOM   7354  C  CD2   . LEU   A 1  996  ? -10.885 70.423  92.784  1.00 18.48 ? 994  LEU   A CD2   1 
ATOM   7355  N  N     . TYR   A 1  997  ? -15.571 68.857  91.799  1.00 14.75 ? 995  TYR   A N     1 
ATOM   7356  C  CA    . TYR   A 1  997  ? -16.841 68.232  91.456  1.00 13.87 ? 995  TYR   A CA    1 
ATOM   7357  C  C     . TYR   A 1  997  ? -16.815 67.945  89.972  1.00 15.57 ? 995  TYR   A C     1 
ATOM   7358  O  O     . TYR   A 1  997  ? -16.529 68.841  89.172  1.00 17.25 ? 995  TYR   A O     1 
ATOM   7359  C  CB    . TYR   A 1  997  ? -18.014 69.160  91.776  1.00 15.01 ? 995  TYR   A CB    1 
ATOM   7360  C  CG    . TYR   A 1  997  ? -18.031 69.598  93.213  1.00 15.59 ? 995  TYR   A CG    1 
ATOM   7361  C  CD1   . TYR   A 1  997  ? -17.343 70.725  93.606  1.00 15.96 ? 995  TYR   A CD1   1 
ATOM   7362  C  CD2   . TYR   A 1  997  ? -18.733 68.878  94.167  1.00 17.40 ? 995  TYR   A CD2   1 
ATOM   7363  C  CE1   . TYR   A 1  997  ? -17.351 71.140  94.925  1.00 18.44 ? 995  TYR   A CE1   1 
ATOM   7364  C  CE2   . TYR   A 1  997  ? -18.746 69.287  95.502  1.00 17.33 ? 995  TYR   A CE2   1 
ATOM   7365  C  CZ    . TYR   A 1  997  ? -18.045 70.413  95.854  1.00 18.68 ? 995  TYR   A CZ    1 
ATOM   7366  O  OH    . TYR   A 1  997  ? -18.063 70.834  97.165  1.00 21.93 ? 995  TYR   A OH    1 
ATOM   7367  N  N     . ILE   A 1  998  ? -17.116 66.706  89.612  1.00 14.74 ? 996  ILE   A N     1 
ATOM   7368  C  CA    A ILE   A 1  998  ? -17.042 66.247  88.228  0.57 14.68 ? 996  ILE   A CA    1 
ATOM   7369  C  CA    B ILE   A 1  998  ? -17.047 66.261  88.227  0.43 14.68 ? 996  ILE   A CA    1 
ATOM   7370  C  C     . ILE   A 1  998  ? -18.450 65.889  87.779  1.00 15.02 ? 996  ILE   A C     1 
ATOM   7371  O  O     . ILE   A 1  998  ? -19.072 64.986  88.345  1.00 15.68 ? 996  ILE   A O     1 
ATOM   7372  C  CB    A ILE   A 1  998  ? -16.111 65.031  88.082  0.57 15.86 ? 996  ILE   A CB    1 
ATOM   7373  C  CB    B ILE   A 1  998  ? -16.073 65.086  88.057  0.43 15.88 ? 996  ILE   A CB    1 
ATOM   7374  C  CG1   A ILE   A 1  998  ? -14.725 65.322  88.666  0.57 18.12 ? 996  ILE   A CG1   1 
ATOM   7375  C  CG1   B ILE   A 1  998  ? -14.657 65.530  88.427  0.43 17.65 ? 996  ILE   A CG1   1 
ATOM   7376  C  CG2   A ILE   A 1  998  ? -16.002 64.628  86.610  0.57 16.80 ? 996  ILE   A CG2   1 
ATOM   7377  C  CG2   B ILE   A 1  998  ? -16.123 64.558  86.624  0.43 16.75 ? 996  ILE   A CG2   1 
ATOM   7378  C  CD1   A ILE   A 1  998  ? -14.015 66.471  87.999  0.57 17.69 ? 996  ILE   A CD1   1 
ATOM   7379  C  CD1   B ILE   A 1  998  ? -13.657 64.418  88.450  0.43 19.50 ? 996  ILE   A CD1   1 
ATOM   7380  N  N     . ASN   A 1  999  ? -18.943 66.592  86.757  1.00 15.86 ? 997  ASN   A N     1 
ATOM   7381  C  CA    . ASN   A 1  999  ? -20.236 66.288  86.134  1.00 15.85 ? 997  ASN   A CA    1 
ATOM   7382  C  C     . ASN   A 1  999  ? -21.420 66.441  87.085  1.00 14.73 ? 997  ASN   A C     1 
ATOM   7383  O  O     . ASN   A 1  999  ? -22.392 65.686  87.024  1.00 15.77 ? 997  ASN   A O     1 
ATOM   7384  C  CB    . ASN   A 1  999  ? -20.223 64.928  85.445  1.00 15.65 ? 997  ASN   A CB    1 
ATOM   7385  C  CG    . ASN   A 1  999  ? -19.260 64.908  84.307  1.00 15.78 ? 997  ASN   A CG    1 
ATOM   7386  O  OD1   . ASN   A 1  999  ? -19.072 65.928  83.653  1.00 16.85 ? 997  ASN   A OD1   1 
ATOM   7387  N  ND2   . ASN   A 1  999  ? -18.609 63.778  84.088  1.00 17.07 ? 997  ASN   A ND2   1 
ATOM   7388  N  N     . ARG   A 1  1000 ? -21.345 67.449  87.944  1.00 16.15 ? 998  ARG   A N     1 
ATOM   7389  C  CA    . ARG   A 1  1000 ? -22.409 67.742  88.895  1.00 16.37 ? 998  ARG   A CA    1 
ATOM   7390  C  C     . ARG   A 1  1000 ? -22.229 69.182  89.344  1.00 15.35 ? 998  ARG   A C     1 
ATOM   7391  O  O     . ARG   A 1  1000 ? -21.288 69.864  88.939  1.00 17.65 ? 998  ARG   A O     1 
ATOM   7392  C  CB    . ARG   A 1  1000 ? -22.360 66.777  90.077  1.00 15.35 ? 998  ARG   A CB    1 
ATOM   7393  C  CG    . ARG   A 1  1000 ? -20.961 66.703  90.703  1.00 16.04 ? 998  ARG   A CG    1 
ATOM   7394  C  CD    . ARG   A 1  1000 ? -21.030 66.323  92.168  1.00 16.80 ? 998  ARG   A CD    1 
ATOM   7395  N  NE    . ARG   A 1  1000 ? -21.673 67.374  92.936  1.00 15.04 ? 998  ARG   A NE    1 
ATOM   7396  C  CZ    . ARG   A 1  1000 ? -21.994 67.280  94.214  1.00 18.31 ? 998  ARG   A CZ    1 
ATOM   7397  N  NH1   . ARG   A 1  1000 ? -21.712 66.192  94.921  1.00 18.00 ? 998  ARG   A NH1   1 
ATOM   7398  N  NH2   . ARG   A 1  1000 ? -22.591 68.309  94.802  1.00 18.20 ? 998  ARG   A NH2   1 
ATOM   7399  N  N     . ASN   A 1  1001 ? -23.147 69.651  90.186  1.00 15.24 ? 999  ASN   A N     1 
ATOM   7400  C  CA    . ASN   A 1  1001 ? -23.001 71.005  90.686  1.00 15.76 ? 999  ASN   A CA    1 
ATOM   7401  C  C     . ASN   A 1  1001 ? -21.824 71.067  91.662  1.00 17.03 ? 999  ASN   A C     1 
ATOM   7402  O  O     . ASN   A 1  1001 ? -21.266 70.044  92.066  1.00 16.29 ? 999  ASN   A O     1 
ATOM   7403  C  CB    . ASN   A 1  1001 ? -24.313 71.492  91.312  1.00 18.70 ? 999  ASN   A CB    1 
ATOM   7404  C  CG    . ASN   A 1  1001 ? -24.664 70.771  92.607  1.00 20.12 ? 999  ASN   A CG    1 
ATOM   7405  O  OD1   . ASN   A 1  1001 ? -23.825 70.567  93.473  1.00 20.14 ? 999  ASN   A OD1   1 
ATOM   7406  N  ND2   . ASN   A 1  1001 ? -25.935 70.413  92.748  1.00 27.19 ? 999  ASN   A ND2   1 
ATOM   7407  N  N     A ILE   A 1  1002 ? -21.429 72.286  92.018  0.55 15.37 ? 1000 ILE   A N     1 
ATOM   7408  N  N     B ILE   A 1  1002 ? -21.464 72.280  92.056  0.45 15.37 ? 1000 ILE   A N     1 
ATOM   7409  C  CA    A ILE   A 1  1002 ? -20.218 72.501  92.807  0.55 16.96 ? 1000 ILE   A CA    1 
ATOM   7410  C  CA    B ILE   A 1  1002 ? -20.320 72.476  92.934  0.45 17.09 ? 1000 ILE   A CA    1 
ATOM   7411  C  C     A ILE   A 1  1002 ? -20.533 72.993  94.214  0.55 16.88 ? 1000 ILE   A C     1 
ATOM   7412  C  C     B ILE   A 1  1002 ? -20.746 72.908  94.334  0.45 16.87 ? 1000 ILE   A C     1 
ATOM   7413  O  O     A ILE   A 1  1002 ? -19.678 73.595  94.856  0.55 17.98 ? 1000 ILE   A O     1 
ATOM   7414  O  O     B ILE   A 1  1002 ? -19.933 73.435  95.085  0.45 19.00 ? 1000 ILE   A O     1 
ATOM   7415  C  CB    A ILE   A 1  1002 ? -19.211 73.420  92.100  0.55 14.73 ? 1000 ILE   A CB    1 
ATOM   7416  C  CB    B ILE   A 1  1002 ? -19.276 73.424  92.322  0.45 14.17 ? 1000 ILE   A CB    1 
ATOM   7417  C  CG1   A ILE   A 1  1002 ? -19.717 74.866  92.051  0.55 17.87 ? 1000 ILE   A CG1   1 
ATOM   7418  C  CG1   B ILE   A 1  1002 ? -19.827 74.848  92.205  0.45 17.81 ? 1000 ILE   A CG1   1 
ATOM   7419  C  CG2   A ILE   A 1  1002 ? -18.955 72.917  90.702  0.55 15.51 ? 1000 ILE   A CG2   1 
ATOM   7420  C  CG2   B ILE   A 1  1002 ? -18.855 72.917  90.952  0.45 15.57 ? 1000 ILE   A CG2   1 
ATOM   7421  C  CD1   A ILE   A 1  1002 ? -18.648 75.862  91.640  0.55 17.56 ? 1000 ILE   A CD1   1 
ATOM   7422  C  CD1   B ILE   A 1  1002 ? -18.789 75.853  91.748  0.45 17.53 ? 1000 ILE   A CD1   1 
ATOM   7423  N  N     A ILE   A 1  1003 ? -21.747 72.755  94.703  0.55 17.50 ? 1001 ILE   A N     1 
ATOM   7424  N  N     B ILE   A 1  1003 ? -22.009 72.692  94.705  0.45 16.91 ? 1001 ILE   A N     1 
ATOM   7425  C  CA    A ILE   A 1  1003 ? -22.149 73.259  96.010  0.55 18.30 ? 1001 ILE   A CA    1 
ATOM   7426  C  CA    B ILE   A 1  1003 ? -22.528 73.207  95.965  0.45 18.19 ? 1001 ILE   A CA    1 
ATOM   7427  C  C     A ILE   A 1  1003 ? -22.191 72.160  97.064  0.55 21.23 ? 1001 ILE   A C     1 
ATOM   7428  C  C     B ILE   A 1  1003 ? -23.134 72.077  96.789  0.45 18.65 ? 1001 ILE   A C     1 
ATOM   7429  O  O     A ILE   A 1  1003 ? -22.657 72.397  98.185  0.55 22.33 ? 1001 ILE   A O     1 
ATOM   7430  O  O     B ILE   A 1  1003 ? -23.288 70.946  96.329  0.45 19.82 ? 1001 ILE   A O     1 
ATOM   7431  C  CB    A ILE   A 1  1003 ? -23.457 74.065  95.947  0.55 18.63 ? 1001 ILE   A CB    1 
ATOM   7432  C  CB    B ILE   A 1  1003 ? -23.533 74.358  95.775  0.45 19.14 ? 1001 ILE   A CB    1 
ATOM   7433  C  CG1   A ILE   A 1  1003 ? -24.605 73.219  95.392  0.55 18.49 ? 1001 ILE   A CG1   1 
ATOM   7434  C  CG1   B ILE   A 1  1003 ? -24.774 73.865  95.034  0.45 18.17 ? 1001 ILE   A CG1   1 
ATOM   7435  C  CG2   A ILE   A 1  1003 ? -23.260 75.328  95.109  0.55 19.55 ? 1001 ILE   A CG2   1 
ATOM   7436  C  CG2   B ILE   A 1  1003 ? -22.879 75.521  95.040  0.45 18.33 ? 1001 ILE   A CG2   1 
ATOM   7437  C  CD1   A ILE   A 1  1003 ? -25.951 73.926  95.446  0.55 23.66 ? 1001 ILE   A CD1   1 
ATOM   7438  C  CD1   B ILE   A 1  1003 ? -25.981 74.770  95.208  0.45 21.60 ? 1001 ILE   A CD1   1 
ATOM   7439  N  N     A GLY   A 1  1004 ? -21.670 70.977  96.746  0.55 19.84 ? 1002 GLY   A N     1 
ATOM   7440  N  N     B GLY   A 1  1004 ? -23.466 72.407  98.033  0.45 20.67 ? 1002 GLY   A N     1 
ATOM   7441  C  CA    A GLY   A 1  1004 ? -21.777 69.847  97.655  0.55 17.38 ? 1002 GLY   A CA    1 
ATOM   7442  C  CA    B GLY   A 1  1004 ? -24.081 71.450  98.936  0.45 22.94 ? 1002 GLY   A CA    1 
ATOM   7443  C  C     A GLY   A 1  1004 ? -20.854 70.002  98.849  0.55 19.11 ? 1002 GLY   A C     1 
ATOM   7444  C  C     B GLY   A 1  1004 ? -23.192 70.303  99.373  0.45 21.69 ? 1002 GLY   A C     1 
ATOM   7445  O  O     A GLY   A 1  1004 ? -19.649 70.232  98.703  0.55 19.37 ? 1002 GLY   A O     1 
ATOM   7446  O  O     B GLY   A 1  1004 ? -23.662 69.160  99.444  0.45 20.81 ? 1002 GLY   A O     1 
ATOM   7447  N  N     A ALA   A 1  1005 ? -21.414 69.869  100.041 0.55 17.97 ? 1003 ALA   A N     1 
ATOM   7448  N  N     B ALA   A 1  1005 ? -21.922 70.579  99.675  0.45 20.36 ? 1003 ALA   A N     1 
ATOM   7449  C  CA    A ALA   A 1  1005 ? -20.616 69.923  101.257 0.55 19.58 ? 1003 ALA   A CA    1 
ATOM   7450  C  CA    B ALA   A 1  1005 ? -21.025 69.543  100.169 0.45 19.89 ? 1003 ALA   A CA    1 
ATOM   7451  C  C     A ALA   A 1  1005 ? -21.127 68.898  102.252 0.55 19.64 ? 1003 ALA   A C     1 
ATOM   7452  C  C     B ALA   A 1  1005 ? -21.610 68.881  101.409 0.45 21.08 ? 1003 ALA   A C     1 
ATOM   7453  O  O     A ALA   A 1  1005 ? -21.155 69.140  103.463 0.55 18.75 ? 1003 ALA   A O     1 
ATOM   7454  O  O     B ALA   A 1  1005 ? -22.177 69.548  102.278 0.45 22.26 ? 1003 ALA   A O     1 
ATOM   7455  C  CB    A ALA   A 1  1005 ? -20.591 71.329  101.849 0.55 19.78 ? 1003 ALA   A CB    1 
ATOM   7456  C  CB    B ALA   A 1  1005 ? -19.662 70.145  100.509 0.45 21.94 ? 1003 ALA   A CB    1 
ATOM   7457  N  N     A VAL   A 1  1006 ? -21.544 67.735  101.743 0.55 19.92 ? 1004 VAL   A N     1 
ATOM   7458  N  N     B VAL   A 1  1006 ? -21.467 67.558  101.483 0.45 19.37 ? 1004 VAL   A N     1 
ATOM   7459  C  CA    A VAL   A 1  1006 ? -22.126 66.684  102.567 0.55 18.90 ? 1004 VAL   A CA    1 
ATOM   7460  C  CA    B VAL   A 1  1006 ? -22.068 66.748  102.538 0.45 18.94 ? 1004 VAL   A CA    1 
ATOM   7461  C  C     A VAL   A 1  1006 ? -21.093 66.244  103.588 0.55 17.99 ? 1004 VAL   A C     1 
ATOM   7462  C  C     B VAL   A 1  1006 ? -21.005 66.427  103.578 0.45 18.15 ? 1004 VAL   A C     1 
ATOM   7463  O  O     A VAL   A 1  1006 ? -20.050 65.686  103.234 0.55 17.86 ? 1004 VAL   A O     1 
ATOM   7464  O  O     B VAL   A 1  1006 ? -19.858 66.120  103.237 0.45 18.11 ? 1004 VAL   A O     1 
ATOM   7465  C  CB    A VAL   A 1  1006 ? -22.622 65.497  101.724 0.55 19.41 ? 1004 VAL   A CB    1 
ATOM   7466  C  CB    B VAL   A 1  1006 ? -22.690 65.469  101.944 0.45 19.01 ? 1004 VAL   A CB    1 
ATOM   7467  C  CG1   A VAL   A 1  1006 ? -23.162 64.410  102.630 0.55 20.02 ? 1004 VAL   A CG1   1 
ATOM   7468  C  CG1   B VAL   A 1  1006 ? -23.208 64.556  103.034 0.45 21.23 ? 1004 VAL   A CG1   1 
ATOM   7469  C  CG2   A VAL   A 1  1006 ? -23.693 65.963  100.736 0.55 20.95 ? 1004 VAL   A CG2   1 
ATOM   7470  C  CG2   B VAL   A 1  1006 ? -23.814 65.832  100.968 0.45 20.85 ? 1004 VAL   A CG2   1 
ATOM   7471  N  N     . VAL   A 1  1007 ? -21.380 66.519  104.856 1.00 18.81 ? 1005 VAL   A N     1 
ATOM   7472  C  CA    . VAL   A 1  1007 ? -20.434 66.260  105.929 1.00 18.61 ? 1005 VAL   A CA    1 
ATOM   7473  C  C     . VAL   A 1  1007 ? -19.949 64.822  105.863 1.00 17.14 ? 1005 VAL   A C     1 
ATOM   7474  O  O     . VAL   A 1  1007 ? -20.742 63.886  105.715 1.00 18.57 ? 1005 VAL   A O     1 
ATOM   7475  C  CB    . VAL   A 1  1007 ? -21.123 66.559  107.266 1.00 18.07 ? 1005 VAL   A CB    1 
ATOM   7476  C  CG1   . VAL   A 1  1007 ? -20.238 66.149  108.414 1.00 20.14 ? 1005 VAL   A CG1   1 
ATOM   7477  C  CG2   . VAL   A 1  1007 ? -21.466 68.018  107.343 1.00 20.20 ? 1005 VAL   A CG2   1 
ATOM   7478  N  N     . GLY   A 1  1008 ? -18.630 64.638  105.965 1.00 17.43 ? 1006 GLY   A N     1 
ATOM   7479  C  CA    . GLY   A 1  1008 ? -18.055 63.308  105.943 1.00 18.74 ? 1006 GLY   A CA    1 
ATOM   7480  C  C     . GLY   A 1  1008 ? -18.098 62.619  104.598 1.00 18.18 ? 1006 GLY   A C     1 
ATOM   7481  O  O     . GLY   A 1  1008 ? -17.696 61.457  104.497 1.00 19.89 ? 1006 GLY   A O     1 
ATOM   7482  N  N     . VAL   A 1  1009 ? -18.590 63.293  103.567 1.00 17.32 ? 1007 VAL   A N     1 
ATOM   7483  C  CA    . VAL   A 1  1009 ? -18.680 62.749  102.219 1.00 18.50 ? 1007 VAL   A CA    1 
ATOM   7484  C  C     . VAL   A 1  1009 ? -17.934 63.633  101.238 1.00 19.00 ? 1007 VAL   A C     1 
ATOM   7485  O  O     . VAL   A 1  1009 ? -17.089 63.158  100.472 1.00 19.82 ? 1007 VAL   A O     1 
ATOM   7486  C  CB    . VAL   A 1  1009 ? -20.150 62.556  101.788 1.00 18.08 ? 1007 VAL   A CB    1 
ATOM   7487  C  CG1   . VAL   A 1  1009 ? -20.208 61.977  100.391 1.00 18.65 ? 1007 VAL   A CG1   1 
ATOM   7488  C  CG2   . VAL   A 1  1009 ? -20.869 61.634  102.752 1.00 18.76 ? 1007 VAL   A CG2   1 
ATOM   7489  N  N     . GLN   A 1  1010 ? -18.203 64.939  101.277 1.00 17.36 ? 1008 GLN   A N     1 
ATOM   7490  C  CA    . GLN   A 1  1010 ? -17.324 65.954  100.708 1.00 16.14 ? 1008 GLN   A CA    1 
ATOM   7491  C  C     . GLN   A 1  1010 ? -16.900 66.848  101.867 1.00 17.10 ? 1008 GLN   A C     1 
ATOM   7492  O  O     . GLN   A 1  1010 ? -17.441 67.946  102.032 1.00 20.42 ? 1008 GLN   A O     1 
ATOM   7493  C  CB    . GLN   A 1  1010 ? -18.013 66.792  99.632  1.00 19.27 ? 1008 GLN   A CB    1 
ATOM   7494  C  CG    . GLN   A 1  1010 ? -18.549 65.991  98.455  1.00 20.06 ? 1008 GLN   A CG    1 
ATOM   7495  C  CD    . GLN   A 1  1010 ? -20.038 65.743  98.550  1.00 20.03 ? 1008 GLN   A CD    1 
ATOM   7496  O  OE1   . GLN   A 1  1010 ? -20.793 66.582  99.054  1.00 20.03 ? 1008 GLN   A OE1   1 
ATOM   7497  N  NE2   . GLN   A 1  1010 ? -20.473 64.581  98.072  1.00 19.22 ? 1008 GLN   A NE2   1 
ATOM   7498  N  N     . PRO   A 1  1011 ? -15.945 66.410  102.685 1.00 18.21 ? 1009 PRO   A N     1 
ATOM   7499  C  CA    . PRO   A 1  1011 ? -15.330 67.326  103.654 1.00 18.82 ? 1009 PRO   A CA    1 
ATOM   7500  C  C     . PRO   A 1  1011 ? -14.958 68.603  102.929 1.00 17.34 ? 1009 PRO   A C     1 
ATOM   7501  O  O     . PRO   A 1  1011 ? -14.432 68.578  101.812 1.00 17.04 ? 1009 PRO   A O     1 
ATOM   7502  C  CB    . PRO   A 1  1011 ? -14.081 66.571  104.105 1.00 17.47 ? 1009 PRO   A CB    1 
ATOM   7503  C  CG    . PRO   A 1  1011 ? -14.424 65.140  103.926 1.00 18.83 ? 1009 PRO   A CG    1 
ATOM   7504  C  CD    . PRO   A 1  1011 ? -15.287 65.091  102.683 1.00 17.70 ? 1009 PRO   A CD    1 
ATOM   7505  N  N     . PHE   A 1  1012 ? -15.303 69.726  103.528 1.00 16.84 ? 1010 PHE   A N     1 
ATOM   7506  C  CA    . PHE   A 1  1012 ? -15.407 70.967  102.793 1.00 16.63 ? 1010 PHE   A CA    1 
ATOM   7507  C  C     . PHE   A 1  1012 ? -14.381 71.958  103.300 1.00 17.39 ? 1010 PHE   A C     1 
ATOM   7508  O  O     . PHE   A 1  1012 ? -14.252 72.165  104.511 1.00 18.32 ? 1010 PHE   A O     1 
ATOM   7509  C  CB    . PHE   A 1  1012 ? -16.804 71.579  102.916 1.00 16.95 ? 1010 PHE   A CB    1 
ATOM   7510  C  CG    . PHE   A 1  1012 ? -16.979 72.775  102.048 1.00 17.12 ? 1010 PHE   A CG    1 
ATOM   7511  C  CD1   . PHE   A 1  1012 ? -17.271 72.627  100.700 1.00 17.79 ? 1010 PHE   A CD1   1 
ATOM   7512  C  CD2   . PHE   A 1  1012 ? -16.787 74.055  102.554 1.00 18.68 ? 1010 PHE   A CD2   1 
ATOM   7513  C  CE1   . PHE   A 1  1012 ? -17.400 73.733  99.884  1.00 18.42 ? 1010 PHE   A CE1   1 
ATOM   7514  C  CE2   . PHE   A 1  1012 ? -16.925 75.167  101.739 1.00 20.97 ? 1010 PHE   A CE2   1 
ATOM   7515  C  CZ    . PHE   A 1  1012 ? -17.223 75.004  100.400 1.00 17.68 ? 1010 PHE   A CZ    1 
ATOM   7516  N  N     . GLY   A 1  1013 ? -13.674 72.574  102.383 1.00 16.56 ? 1011 GLY   A N     1 
ATOM   7517  C  CA    . GLY   A 1  1013 ? -12.766 73.638  102.744 1.00 18.25 ? 1011 GLY   A CA    1 
ATOM   7518  C  C     . GLY   A 1  1013 ? -11.687 73.734  101.706 1.00 17.09 ? 1011 GLY   A C     1 
ATOM   7519  O  O     . GLY   A 1  1013 ? -11.272 72.748  101.116 1.00 18.94 ? 1011 GLY   A O     1 
ATOM   7520  N  N     . GLY   A 1  1014 ? -11.210 74.958  101.502 1.00 18.42 ? 1012 GLY   A N     1 
ATOM   7521  C  CA    . GLY   A 1  1014 ? -10.244 75.212  100.467 1.00 20.66 ? 1012 GLY   A CA    1 
ATOM   7522  C  C     . GLY   A 1  1014 ? -8.905  75.695  100.961 1.00 20.37 ? 1012 GLY   A C     1 
ATOM   7523  O  O     . GLY   A 1  1014 ? -8.591  75.629  102.154 1.00 19.55 ? 1012 GLY   A O     1 
ATOM   7524  N  N     . ARG   A 1  1015 ? -8.125  76.217  100.033 1.00 17.85 ? 1013 ARG   A N     1 
ATOM   7525  C  CA    . ARG   A 1  1015 ? -6.745  76.588  100.265 1.00 17.80 ? 1013 ARG   A CA    1 
ATOM   7526  C  C     . ARG   A 1  1015 ? -6.530  78.002  99.761  1.00 18.22 ? 1013 ARG   A C     1 
ATOM   7527  O  O     . ARG   A 1  1015 ? -7.428  78.625  99.202  1.00 18.19 ? 1013 ARG   A O     1 
ATOM   7528  C  CB    . ARG   A 1  1015 ? -5.818  75.631  99.513  1.00 18.85 ? 1013 ARG   A CB    1 
ATOM   7529  C  CG    . ARG   A 1  1015 ? -6.078  75.644  98.006  1.00 18.65 ? 1013 ARG   A CG    1 
ATOM   7530  C  CD    . ARG   A 1  1015 ? -4.962  74.950  97.221  1.00 23.32 ? 1013 ARG   A CD    1 
ATOM   7531  N  NE    . ARG   A 1  1015 ? -3.652  75.155  97.823  1.00 29.97 ? 1013 ARG   A NE    1 
ATOM   7532  C  CZ    . ARG   A 1  1015 ? -2.937  76.263  97.699  1.00 32.50 ? 1013 ARG   A CZ    1 
ATOM   7533  N  NH1   . ARG   A 1  1015 ? -3.360  77.276  96.960  1.00 29.10 ? 1013 ARG   A NH1   1 
ATOM   7534  N  NH2   . ARG   A 1  1015 ? -1.775  76.360  98.343  1.00 26.47 ? 1013 ARG   A NH2   1 
ATOM   7535  N  N     . GLY   A 1  1016 ? -5.311  78.505  99.942  1.00 20.39 ? 1014 GLY   A N     1 
ATOM   7536  C  CA    . GLY   A 1  1016 ? -5.026  79.838  99.452  1.00 20.30 ? 1014 GLY   A CA    1 
ATOM   7537  C  C     . GLY   A 1  1016 ? -5.873  80.859  100.183 1.00 18.35 ? 1014 GLY   A C     1 
ATOM   7538  O  O     . GLY   A 1  1016 ? -6.066  80.788  101.403 1.00 20.37 ? 1014 GLY   A O     1 
ATOM   7539  N  N     . LEU   A 1  1017 ? -6.417  81.808  99.420  1.00 18.86 ? 1015 LEU   A N     1 
ATOM   7540  C  CA    . LEU   A 1  1017 ? -7.313  82.812  99.983  1.00 20.13 ? 1015 LEU   A CA    1 
ATOM   7541  C  C     . LEU   A 1  1017 ? -8.612  82.217  100.495 1.00 18.42 ? 1015 LEU   A C     1 
ATOM   7542  O  O     . LEU   A 1  1017 ? -9.398  82.943  101.111 1.00 19.11 ? 1015 LEU   A O     1 
ATOM   7543  C  CB    . LEU   A 1  1017 ? -7.642  83.866  98.926  1.00 20.63 ? 1015 LEU   A CB    1 
ATOM   7544  C  CG    . LEU   A 1  1017 ? -6.441  84.671  98.424  1.00 21.27 ? 1015 LEU   A CG    1 
ATOM   7545  C  CD1   . LEU   A 1  1017 ? -6.892  85.591  97.289  1.00 21.61 ? 1015 LEU   A CD1   1 
ATOM   7546  C  CD2   . LEU   A 1  1017 ? -5.774  85.473  99.557  1.00 22.20 ? 1015 LEU   A CD2   1 
ATOM   7547  N  N     . SER   A 1  1018 ? -8.850  80.923  100.262 1.00 15.81 ? 1016 SER   A N     1 
ATOM   7548  C  CA    . SER   A 1  1018 ? -10.099 80.285  100.648 1.00 17.99 ? 1016 SER   A CA    1 
ATOM   7549  C  C     . SER   A 1  1018 ? -10.040 79.561  101.980 1.00 16.91 ? 1016 SER   A C     1 
ATOM   7550  O  O     . SER   A 1  1018 ? -11.088 79.152  102.475 1.00 18.90 ? 1016 SER   A O     1 
ATOM   7551  C  CB    . SER   A 1  1018 ? -10.528 79.270  99.594  1.00 18.13 ? 1016 SER   A CB    1 
ATOM   7552  O  OG    . SER   A 1  1018 ? -10.777 79.940  98.380  1.00 17.52 ? 1016 SER   A OG    1 
ATOM   7553  N  N     . GLY   A 1  1019 ? -8.866  79.352  102.559 1.00 16.92 ? 1017 GLY   A N     1 
ATOM   7554  C  CA    . GLY   A 1  1019 ? -8.869  78.656  103.826 1.00 18.29 ? 1017 GLY   A CA    1 
ATOM   7555  C  C     . GLY   A 1  1019 ? -7.501  78.302  104.351 1.00 19.49 ? 1017 GLY   A C     1 
ATOM   7556  O  O     . GLY   A 1  1019 ? -6.534  78.206  103.594 1.00 19.75 ? 1017 GLY   A O     1 
ATOM   7557  N  N     . THR   A 1  1020 ? -7.425  78.130  105.662 1.00 19.55 ? 1018 THR   A N     1 
ATOM   7558  C  CA    . THR   A 1  1020 ? -6.261  77.532  106.292 1.00 19.25 ? 1018 THR   A CA    1 
ATOM   7559  C  C     . THR   A 1  1020 ? -6.410  76.032  106.428 1.00 16.95 ? 1018 THR   A C     1 
ATOM   7560  O  O     . THR   A 1  1020 ? -5.403  75.333  106.576 1.00 19.70 ? 1018 THR   A O     1 
ATOM   7561  C  CB    . THR   A 1  1020 ? -6.092  78.089  107.713 1.00 18.71 ? 1018 THR   A CB    1 
ATOM   7562  O  OG1   . THR   A 1  1020 ? -7.277  77.826  108.488 1.00 19.91 ? 1018 THR   A OG1   1 
ATOM   7563  C  CG2   . THR   A 1  1020 ? -5.828  79.590  107.674 1.00 20.95 ? 1018 THR   A CG2   1 
ATOM   7564  N  N     . GLY   A 1  1021 ? -7.636  75.533  106.448 1.00 19.31 ? 1019 GLY   A N     1 
ATOM   7565  C  CA    . GLY   A 1  1021 ? -7.885  74.188  106.879 1.00 20.84 ? 1019 GLY   A CA    1 
ATOM   7566  C  C     . GLY   A 1  1021 ? -7.656  74.064  108.373 1.00 20.52 ? 1019 GLY   A C     1 
ATOM   7567  O  O     . GLY   A 1  1021 ? -7.335  75.040  109.056 1.00 19.41 ? 1019 GLY   A O     1 
ATOM   7568  N  N     . PRO   A 1  1022 ? -7.860  72.860  108.917 1.00 19.84 ? 1020 PRO   A N     1 
ATOM   7569  C  CA    . PRO   A 1  1022 ? -8.350  71.664  108.227 1.00 19.62 ? 1020 PRO   A CA    1 
ATOM   7570  C  C     . PRO   A 1  1022 ? -9.804  71.814  107.799 1.00 20.09 ? 1020 PRO   A C     1 
ATOM   7571  O  O     . PRO   A 1  1022 ? -10.503 72.734  108.229 1.00 21.50 ? 1020 PRO   A O     1 
ATOM   7572  C  CB    . PRO   A 1  1022 ? -8.192  70.571  109.289 1.00 20.15 ? 1020 PRO   A CB    1 
ATOM   7573  C  CG    . PRO   A 1  1022 ? -8.390  71.298  110.592 1.00 20.62 ? 1020 PRO   A CG    1 
ATOM   7574  C  CD    . PRO   A 1  1022 ? -7.717  72.637  110.367 1.00 19.77 ? 1020 PRO   A CD    1 
ATOM   7575  N  N     . LYS   A 1  1023 ? -10.268 70.906  106.949 1.00 18.67 ? 1021 LYS   A N     1 
ATOM   7576  C  CA    . LYS   A 1  1023 ? -11.633 70.979  106.438 1.00 18.22 ? 1021 LYS   A CA    1 
ATOM   7577  C  C     . LYS   A 1  1023 ? -12.654 70.684  107.528 1.00 19.71 ? 1021 LYS   A C     1 
ATOM   7578  O  O     . LYS   A 1  1023 ? -12.546 69.688  108.245 1.00 19.84 ? 1021 LYS   A O     1 
ATOM   7579  C  CB    . LYS   A 1  1023 ? -11.832 69.931  105.350 1.00 16.92 ? 1021 LYS   A CB    1 
ATOM   7580  C  CG    . LYS   A 1  1023 ? -11.167 70.205  104.027 1.00 16.90 ? 1021 LYS   A CG    1 
ATOM   7581  C  CD    . LYS   A 1  1023 ? -11.380 68.988  103.163 1.00 17.60 ? 1021 LYS   A CD    1 
ATOM   7582  C  CE    . LYS   A 1  1023 ? -10.923 69.204  101.726 1.00 18.00 ? 1021 LYS   A CE    1 
ATOM   7583  N  NZ    . LYS   A 1  1023 ? -11.924 70.005  100.987 1.00 18.19 ? 1021 LYS   A NZ    1 
ATOM   7584  N  N     . ALA   A 1  1024 ? -13.684 71.524  107.605 1.00 19.43 ? 1022 ALA   A N     1 
ATOM   7585  C  CA    . ALA   A 1  1024 ? -14.882 71.165  108.341 1.00 19.70 ? 1022 ALA   A CA    1 
ATOM   7586  C  C     . ALA   A 1  1024 ? -15.515 69.922  107.729 1.00 18.46 ? 1022 ALA   A C     1 
ATOM   7587  O  O     . ALA   A 1  1024 ? -15.449 69.692  106.515 1.00 19.46 ? 1022 ALA   A O     1 
ATOM   7588  C  CB    . ALA   A 1  1024 ? -15.881 72.318  108.287 1.00 20.52 ? 1022 ALA   A CB    1 
ATOM   7589  N  N     . GLY   A 1  1025 ? -16.133 69.112  108.582 1.00 18.95 ? 1023 GLY   A N     1 
ATOM   7590  C  CA    . GLY   A 1  1025 ? -16.776 67.912  108.094 1.00 18.93 ? 1023 GLY   A CA    1 
ATOM   7591  C  C     . GLY   A 1  1025 ? -15.799 66.874  107.616 1.00 20.02 ? 1023 GLY   A C     1 
ATOM   7592  O  O     . GLY   A 1  1025 ? -16.181 65.962  106.876 1.00 18.00 ? 1023 GLY   A O     1 
ATOM   7593  N  N     . GLY   A 1  1026 ? -14.536 66.995  108.027 1.00 17.12 ? 1024 GLY   A N     1 
ATOM   7594  C  CA    . GLY   A 1  1026 ? -13.505 66.047  107.689 1.00 19.50 ? 1024 GLY   A CA    1 
ATOM   7595  C  C     . GLY   A 1  1026 ? -12.761 65.592  108.926 1.00 18.16 ? 1024 GLY   A C     1 
ATOM   7596  O  O     . GLY   A 1  1026 ? -12.958 66.104  110.032 1.00 18.75 ? 1024 GLY   A O     1 
ATOM   7597  N  N     . PRO   A 1  1027 ? -11.872 64.615  108.748 1.00 16.75 ? 1025 PRO   A N     1 
ATOM   7598  C  CA    . PRO   A 1  1027 ? -11.337 63.877  109.896 1.00 19.66 ? 1025 PRO   A CA    1 
ATOM   7599  C  C     . PRO   A 1  1027 ? -10.170 64.557  110.581 1.00 15.68 ? 1025 PRO   A C     1 
ATOM   7600  O  O     . PRO   A 1  1027 ? -9.748  64.089  111.643 1.00 17.79 ? 1025 PRO   A O     1 
ATOM   7601  C  CB    . PRO   A 1  1027 ? -10.909 62.543  109.273 1.00 20.29 ? 1025 PRO   A CB    1 
ATOM   7602  C  CG    . PRO   A 1  1027 ? -10.559 62.911  107.849 1.00 19.83 ? 1025 PRO   A CG    1 
ATOM   7603  C  CD    . PRO   A 1  1027 ? -11.555 63.980  107.458 1.00 17.37 ? 1025 PRO   A CD    1 
ATOM   7604  N  N     . LEU   A 1  1028 ? -9.629  65.623  110.010 1.00 18.05 ? 1026 LEU   A N     1 
ATOM   7605  C  CA    . LEU   A 1  1028 ? -8.544  66.349  110.652 1.00 18.00 ? 1026 LEU   A CA    1 
ATOM   7606  C  C     . LEU   A 1  1028 ? -9.045  67.493  111.510 1.00 17.33 ? 1026 LEU   A C     1 
ATOM   7607  O  O     . LEU   A 1  1028 ? -8.249  68.124  112.202 1.00 19.15 ? 1026 LEU   A O     1 
ATOM   7608  C  CB    . LEU   A 1  1028 ? -7.577  66.909  109.606 1.00 18.20 ? 1026 LEU   A CB    1 
ATOM   7609  C  CG    . LEU   A 1  1028 ? -6.803  65.871  108.799 1.00 22.32 ? 1026 LEU   A CG    1 
ATOM   7610  C  CD1   . LEU   A 1  1028 ? -5.947  66.564  107.768 1.00 22.14 ? 1026 LEU   A CD1   1 
ATOM   7611  C  CD2   . LEU   A 1  1028 ? -5.967  65.036  109.721 1.00 29.68 ? 1026 LEU   A CD2   1 
ATOM   7612  N  N     . TYR   A 1  1029 ? -10.348 67.749  111.498 1.00 18.22 ? 1027 TYR   A N     1 
ATOM   7613  C  CA    . TYR   A 1  1029 ? -10.881 68.968  112.098 1.00 19.07 ? 1027 TYR   A CA    1 
ATOM   7614  C  C     . TYR   A 1  1029 ? -10.723 68.964  113.608 1.00 18.19 ? 1027 TYR   A C     1 
ATOM   7615  O  O     . TYR   A 1  1029 ? -10.197 69.922  114.188 1.00 19.44 ? 1027 TYR   A O     1 
ATOM   7616  C  CB    . TYR   A 1  1029 ? -12.349 69.047  111.743 1.00 18.64 ? 1027 TYR   A CB    1 
ATOM   7617  C  CG    . TYR   A 1  1029 ? -12.995 70.394  111.828 1.00 17.82 ? 1027 TYR   A CG    1 
ATOM   7618  C  CD1   . TYR   A 1  1029 ? -12.595 71.433  111.000 1.00 17.25 ? 1027 TYR   A CD1   1 
ATOM   7619  C  CD2   . TYR   A 1  1029 ? -14.070 70.603  112.684 1.00 19.04 ? 1027 TYR   A CD2   1 
ATOM   7620  C  CE1   . TYR   A 1  1029 ? -13.243 72.660  111.036 1.00 18.16 ? 1027 TYR   A CE1   1 
ATOM   7621  C  CE2   . TYR   A 1  1029 ? -14.710 71.815  112.725 1.00 20.71 ? 1027 TYR   A CE2   1 
ATOM   7622  C  CZ    . TYR   A 1  1029 ? -14.299 72.835  111.901 1.00 19.80 ? 1027 TYR   A CZ    1 
ATOM   7623  O  OH    . TYR   A 1  1029 ? -14.974 74.032  111.942 1.00 20.94 ? 1027 TYR   A OH    1 
ATOM   7624  N  N     . LEU   A 1  1030 ? -11.199 67.907  114.267 1.00 18.25 ? 1028 LEU   A N     1 
ATOM   7625  C  CA    . LEU   A 1  1030 ? -11.181 67.907  115.730 1.00 18.95 ? 1028 LEU   A CA    1 
ATOM   7626  C  C     . LEU   A 1  1030 ? -9.764  68.001  116.260 1.00 20.06 ? 1028 LEU   A C     1 
ATOM   7627  O  O     . LEU   A 1  1030 ? -9.536  68.601  117.317 1.00 20.81 ? 1028 LEU   A O     1 
ATOM   7628  C  CB    . LEU   A 1  1030 ? -11.839 66.648  116.278 1.00 19.41 ? 1028 LEU   A CB    1 
ATOM   7629  C  CG    . LEU   A 1  1030 ? -13.323 66.483  115.984 1.00 20.00 ? 1028 LEU   A CG    1 
ATOM   7630  C  CD1   . LEU   A 1  1030 ? -13.838 65.211  116.655 1.00 24.12 ? 1028 LEU   A CD1   1 
ATOM   7631  C  CD2   . LEU   A 1  1030 ? -14.105 67.713  116.448 1.00 24.06 ? 1028 LEU   A CD2   1 
ATOM   7632  N  N     . GLY   A 1  1031 ? -8.800  67.425  115.542 1.00 18.72 ? 1029 GLY   A N     1 
ATOM   7633  C  CA    . GLY   A 1  1031 ? -7.428  67.420  116.014 1.00 21.45 ? 1029 GLY   A CA    1 
ATOM   7634  C  C     . GLY   A 1  1031 ? -6.806  68.792  116.108 1.00 20.19 ? 1029 GLY   A C     1 
ATOM   7635  O  O     . GLY   A 1  1031 ? -5.803  68.960  116.807 1.00 22.46 ? 1029 GLY   A O     1 
ATOM   7636  N  N     . ARG   A 1  1032 ? -7.369  69.776  115.410 1.00 18.97 ? 1030 ARG   A N     1 
ATOM   7637  C  CA    . ARG   A 1  1032 ? -6.892  71.145  115.520 1.00 17.92 ? 1030 ARG   A CA    1 
ATOM   7638  C  C     . ARG   A 1  1032 ? -7.362  71.812  116.807 1.00 21.22 ? 1030 ARG   A C     1 
ATOM   7639  O  O     . ARG   A 1  1032 ? -6.810  72.845  117.204 1.00 22.17 ? 1030 ARG   A O     1 
ATOM   7640  C  CB    . ARG   A 1  1032 ? -7.375  71.935  114.303 1.00 20.17 ? 1030 ARG   A CB    1 
ATOM   7641  C  CG    . ARG   A 1  1032 ? -6.754  73.309  114.144 1.00 18.64 ? 1030 ARG   A CG    1 
ATOM   7642  C  CD    . ARG   A 1  1032 ? -5.292  73.196  113.731 1.00 20.65 ? 1030 ARG   A CD    1 
ATOM   7643  N  NE    . ARG   A 1  1032 ? -4.766  74.495  113.339 1.00 20.53 ? 1030 ARG   A NE    1 
ATOM   7644  C  CZ    . ARG   A 1  1032 ? -3.696  75.068  113.872 1.00 23.68 ? 1030 ARG   A CZ    1 
ATOM   7645  N  NH1   . ARG   A 1  1032 ? -3.021  74.494  114.857 1.00 26.18 ? 1030 ARG   A NH1   1 
ATOM   7646  N  NH2   . ARG   A 1  1032 ? -3.293  76.245  113.402 1.00 25.83 ? 1030 ARG   A NH2   1 
ATOM   7647  N  N     . LEU   A 1  1033 ? -8.360  71.236  117.473 1.00 19.08 ? 1031 LEU   A N     1 
ATOM   7648  C  CA    . LEU   A 1  1033 ? -9.005  71.852  118.620 1.00 20.28 ? 1031 LEU   A CA    1 
ATOM   7649  C  C     . LEU   A 1  1033 ? -8.542  71.250  119.936 1.00 19.58 ? 1031 LEU   A C     1 
ATOM   7650  O  O     . LEU   A 1  1033 ? -9.165  71.481  120.973 1.00 21.56 ? 1031 LEU   A O     1 
ATOM   7651  C  CB    . LEU   A 1  1033 ? -10.522 71.735  118.472 1.00 20.38 ? 1031 LEU   A CB    1 
ATOM   7652  C  CG    . LEU   A 1  1033 ? -10.998 72.164  117.088 1.00 20.72 ? 1031 LEU   A CG    1 
ATOM   7653  C  CD1   . LEU   A 1  1033 ? -12.499 71.969  116.952 1.00 20.96 ? 1031 LEU   A CD1   1 
ATOM   7654  C  CD2   . LEU   A 1  1033 ? -10.608 73.605  116.830 1.00 23.59 ? 1031 LEU   A CD2   1 
ATOM   7655  N  N     . VAL   A 1  1034 ? -7.461  70.480  119.907 1.00 21.10 ? 1032 VAL   A N     1 
ATOM   7656  C  CA    . VAL   A 1  1034 ? -6.842  69.919  121.094 1.00 22.38 ? 1032 VAL   A CA    1 
ATOM   7657  C  C     . VAL   A 1  1034 ? -5.351  70.212  121.016 1.00 22.87 ? 1032 VAL   A C     1 
ATOM   7658  O  O     . VAL   A 1  1034 ? -4.808  70.493  119.947 1.00 23.48 ? 1032 VAL   A O     1 
ATOM   7659  C  CB    . VAL   A 1  1034 ? -7.096  68.406  121.211 1.00 22.06 ? 1032 VAL   A CB    1 
ATOM   7660  C  CG1   . VAL   A 1  1034 ? -8.575  68.133  121.549 1.00 24.48 ? 1032 VAL   A CG1   1 
ATOM   7661  C  CG2   . VAL   A 1  1034 ? -6.675  67.704  119.912 1.00 21.22 ? 1032 VAL   A CG2   1 
ATOM   7662  N  N     . THR   A 1  1035 ? -4.679  70.131  122.166 1.00 24.46 ? 1033 THR   A N     1 
ATOM   7663  C  CA    . THR   A 1  1035 ? -3.268  70.504  122.193 1.00 24.90 ? 1033 THR   A CA    1 
ATOM   7664  C  C     . THR   A 1  1035 ? -2.380  69.458  121.525 1.00 31.17 ? 1033 THR   A C     1 
ATOM   7665  O  O     . THR   A 1  1035 ? -1.349  69.810  120.943 1.00 34.27 ? 1033 THR   A O     1 
ATOM   7666  C  CB    . THR   A 1  1035 ? -2.827  70.781  123.627 1.00 31.52 ? 1033 THR   A CB    1 
ATOM   7667  O  OG1   . THR   A 1  1035 ? -3.079  69.628  124.434 1.00 39.36 ? 1033 THR   A OG1   1 
ATOM   7668  C  CG2   . THR   A 1  1035 ? -3.599  71.940  124.185 1.00 28.60 ? 1033 THR   A CG2   1 
ATOM   7669  N  N     . THR   A 1  1036 ? -2.757  68.183  121.594 1.00 25.13 ? 1034 THR   A N     1 
ATOM   7670  C  CA    . THR   A 1  1036 ? -2.039  67.095  120.942 1.00 25.99 ? 1034 THR   A CA    1 
ATOM   7671  C  C     . THR   A 1  1036 ? -3.033  66.386  120.039 1.00 27.14 ? 1034 THR   A C     1 
ATOM   7672  O  O     . THR   A 1  1036 ? -4.024  65.828  120.526 1.00 26.21 ? 1034 THR   A O     1 
ATOM   7673  C  CB    . THR   A 1  1036 ? -1.493  66.113  121.982 1.00 33.00 ? 1034 THR   A CB    1 
ATOM   7674  O  OG1   . THR   A 1  1036 ? -0.594  66.800  122.858 1.00 35.57 ? 1034 THR   A OG1   1 
ATOM   7675  C  CG2   . THR   A 1  1036 ? -0.750  64.971  121.294 1.00 35.31 ? 1034 THR   A CG2   1 
ATOM   7676  N  N     . ALA   A 1  1037 ? -2.780  66.416  118.736 1.00 27.32 ? 1035 ALA   A N     1 
ATOM   7677  C  CA    . ALA   A 1  1037 ? -3.759  65.894  117.799 1.00 26.57 ? 1035 ALA   A CA    1 
ATOM   7678  C  C     . ALA   A 1  1037 ? -3.787  64.370  117.858 1.00 24.51 ? 1035 ALA   A C     1 
ATOM   7679  O  O     . ALA   A 1  1037 ? -2.733  63.729  117.911 1.00 26.75 ? 1035 ALA   A O     1 
ATOM   7680  C  CB    . ALA   A 1  1037 ? -3.440  66.354  116.375 1.00 27.43 ? 1035 ALA   A CB    1 
ATOM   7681  N  N     . PRO   A 1  1038 ? -4.971  63.766  117.871 1.00 22.50 ? 1036 PRO   A N     1 
ATOM   7682  C  CA    . PRO   A 1  1038 ? -5.059  62.309  117.756 1.00 20.53 ? 1036 PRO   A CA    1 
ATOM   7683  C  C     . PRO   A 1  1038 ? -4.789  61.884  116.324 1.00 21.62 ? 1036 PRO   A C     1 
ATOM   7684  O  O     . PRO   A 1  1038 ? -4.687  62.697  115.405 1.00 22.20 ? 1036 PRO   A O     1 
ATOM   7685  C  CB    . PRO   A 1  1038 ? -6.517  62.031  118.112 1.00 23.98 ? 1036 PRO   A CB    1 
ATOM   7686  C  CG    . PRO   A 1  1038 ? -7.231  63.241  117.553 1.00 25.23 ? 1036 PRO   A CG    1 
ATOM   7687  C  CD    . PRO   A 1  1038 ? -6.305  64.400  117.859 1.00 24.63 ? 1036 PRO   A CD    1 
ATOM   7688  N  N     . VAL   A 1  1039 ? -4.706  60.571  116.136 1.00 22.33 ? 1037 VAL   A N     1 
ATOM   7689  C  CA    . VAL   A 1  1039 ? -4.587  59.978  114.809 1.00 20.69 ? 1037 VAL   A CA    1 
ATOM   7690  C  C     . VAL   A 1  1039 ? -6.002  59.797  114.266 1.00 21.90 ? 1037 VAL   A C     1 
ATOM   7691  O  O     . VAL   A 1  1039 ? -6.764  58.996  114.828 1.00 21.75 ? 1037 VAL   A O     1 
ATOM   7692  C  CB    . VAL   A 1  1039 ? -3.850  58.637  114.871 1.00 20.57 ? 1037 VAL   A CB    1 
ATOM   7693  C  CG1   . VAL   A 1  1039 ? -3.776  58.009  113.495 1.00 22.52 ? 1037 VAL   A CG1   1 
ATOM   7694  C  CG2   . VAL   A 1  1039 ? -2.458  58.832  115.465 1.00 25.24 ? 1037 VAL   A CG2   1 
ATOM   7695  N  N     . PRO   A 1  1040 ? -6.392  60.499  113.208 1.00 20.33 ? 1038 PRO   A N     1 
ATOM   7696  C  CA    . PRO   A 1  1040 ? -7.757  60.366  112.713 1.00 21.60 ? 1038 PRO   A CA    1 
ATOM   7697  C  C     . PRO   A 1  1040 ? -8.004  58.968  112.179 1.00 20.82 ? 1038 PRO   A C     1 
ATOM   7698  O  O     . PRO   A 1  1040 ? -7.057  58.245  111.829 1.00 20.12 ? 1038 PRO   A O     1 
ATOM   7699  C  CB    . PRO   A 1  1040 ? -7.837  61.414  111.589 1.00 21.10 ? 1038 PRO   A CB    1 
ATOM   7700  C  CG    . PRO   A 1  1040 ? -6.744  62.370  111.886 1.00 23.92 ? 1038 PRO   A CG    1 
ATOM   7701  C  CD    . PRO   A 1  1040 ? -5.647  61.543  112.489 1.00 22.86 ? 1038 PRO   A CD    1 
ATOM   7702  N  N     . PRO   A 1  1041 ? -9.260  58.544  112.118 1.00 18.92 ? 1039 PRO   A N     1 
ATOM   7703  C  CA    . PRO   A 1  1041 ? -9.572  57.277  111.460 1.00 19.26 ? 1039 PRO   A CA    1 
ATOM   7704  C  C     . PRO   A 1  1041 ? -9.030  57.292  110.044 1.00 19.11 ? 1039 PRO   A C     1 
ATOM   7705  O  O     . PRO   A 1  1041 ? -9.075  58.314  109.355 1.00 20.63 ? 1039 PRO   A O     1 
ATOM   7706  C  CB    . PRO   A 1  1041 ? -11.107 57.256  111.441 1.00 21.24 ? 1039 PRO   A CB    1 
ATOM   7707  C  CG    . PRO   A 1  1041 ? -11.508 58.191  112.533 1.00 24.30 ? 1039 PRO   A CG    1 
ATOM   7708  C  CD    . PRO   A 1  1041 ? -10.473 59.261  112.548 1.00 21.83 ? 1039 PRO   A CD    1 
ATOM   7709  N  N     . GLN   A 1  1042 ? -8.487  56.150  109.626 1.00 17.66 ? 1040 GLN   A N     1 
ATOM   7710  C  CA    . GLN   A 1  1042 ? -8.019  55.899  108.265 1.00 18.27 ? 1040 GLN   A CA    1 
ATOM   7711  C  C     . GLN   A 1  1042 ? -6.846  56.774  107.852 1.00 19.12 ? 1040 GLN   A C     1 
ATOM   7712  O  O     . GLN   A 1  1042 ? -6.483  56.793  106.674 1.00 20.87 ? 1040 GLN   A O     1 
ATOM   7713  C  CB    . GLN   A 1  1042 ? -9.143  56.019  107.229 1.00 23.13 ? 1040 GLN   A CB    1 
ATOM   7714  C  CG    . GLN   A 1  1042 ? -10.330 55.138  107.527 1.00 29.83 ? 1040 GLN   A CG    1 
ATOM   7715  C  CD    . GLN   A 1  1042 ? -11.370 55.214  106.426 1.00 34.71 ? 1040 GLN   A CD    1 
ATOM   7716  O  OE1   . GLN   A 1  1042 ? -11.404 54.368  105.536 1.00 44.24 ? 1040 GLN   A OE1   1 
ATOM   7717  N  NE2   . GLN   A 1  1042 ? -12.204 56.245  106.468 1.00 38.48 ? 1040 GLN   A NE2   1 
ATOM   7718  N  N     . HIS   A 1  1043 ? -6.241  57.499  108.783 1.00 17.59 ? 1041 HIS   A N     1 
ATOM   7719  C  CA    . HIS   A 1  1043 ? -5.248  58.514  108.455 1.00 16.84 ? 1041 HIS   A CA    1 
ATOM   7720  C  C     . HIS   A 1  1043 ? -3.865  57.882  108.507 1.00 19.37 ? 1041 HIS   A C     1 
ATOM   7721  O  O     . HIS   A 1  1043 ? -3.268  57.761  109.575 1.00 18.96 ? 1041 HIS   A O     1 
ATOM   7722  C  CB    . HIS   A 1  1043 ? -5.358  59.661  109.445 1.00 17.87 ? 1041 HIS   A CB    1 
ATOM   7723  C  CG    . HIS   A 1  1043 ? -4.402  60.778  109.185 1.00 18.30 ? 1041 HIS   A CG    1 
ATOM   7724  N  ND1   . HIS   A 1  1043 ? -4.687  61.824  108.337 1.00 18.27 ? 1041 HIS   A ND1   1 
ATOM   7725  C  CD2   . HIS   A 1  1043 ? -3.160  61.014  109.672 1.00 18.83 ? 1041 HIS   A CD2   1 
ATOM   7726  C  CE1   . HIS   A 1  1043 ? -3.661  62.658  108.310 1.00 20.15 ? 1041 HIS   A CE1   1 
ATOM   7727  N  NE2   . HIS   A 1  1043 ? -2.723  62.190  109.113 1.00 19.65 ? 1041 HIS   A NE2   1 
ATOM   7728  N  N     . SER   A 1  1044 ? -3.367  57.467  107.350 1.00 17.84 ? 1042 SER   A N     1 
ATOM   7729  C  CA    . SER   A 1  1044 ? -2.017  56.932  107.212 1.00 16.34 ? 1042 SER   A CA    1 
ATOM   7730  C  C     . SER   A 1  1044 ? -1.740  56.863  105.726 1.00 17.41 ? 1042 SER   A C     1 
ATOM   7731  O  O     . SER   A 1  1044 ? -2.644  56.996  104.897 1.00 19.60 ? 1042 SER   A O     1 
ATOM   7732  C  CB    . SER   A 1  1044 ? -1.882  55.538  107.824 1.00 19.31 ? 1042 SER   A CB    1 
ATOM   7733  O  OG    . SER   A 1  1044 ? -2.695  54.615  107.128 1.00 19.48 ? 1042 SER   A OG    1 
ATOM   7734  N  N     . SER   A 1  1045 ? -0.478  56.636  105.396 1.00 16.26 ? 1043 SER   A N     1 
ATOM   7735  C  CA    . SER   A 1  1045 ? -0.111  56.442  104.005 1.00 18.05 ? 1043 SER   A CA    1 
ATOM   7736  C  C     . SER   A 1  1045 ? 1.097   55.533  103.941 1.00 16.68 ? 1043 SER   A C     1 
ATOM   7737  O  O     . SER   A 1  1045 ? 2.046   55.706  104.705 1.00 17.72 ? 1043 SER   A O     1 
ATOM   7738  C  CB    . SER   A 1  1045 ? 0.242   57.773  103.345 1.00 18.25 ? 1043 SER   A CB    1 
ATOM   7739  O  OG    . SER   A 1  1045 ? 0.700   57.547  102.015 1.00 18.14 ? 1043 SER   A OG    1 
ATOM   7740  N  N     . VAL   A 1  1046 ? 1.061   54.573  103.009 1.00 17.77 ? 1044 VAL   A N     1 
ATOM   7741  C  CA    . VAL   A 1  1046 ? 2.217   53.699  102.818 1.00 17.88 ? 1044 VAL   A CA    1 
ATOM   7742  C  C     . VAL   A 1  1046 ? 3.281   54.340  101.958 1.00 17.11 ? 1044 VAL   A C     1 
ATOM   7743  O  O     . VAL   A 1  1046 ? 4.353   53.751  101.784 1.00 20.05 ? 1044 VAL   A O     1 
ATOM   7744  C  CB    . VAL   A 1  1046 ? 1.873   52.314  102.235 1.00 20.31 ? 1044 VAL   A CB    1 
ATOM   7745  C  CG1   . VAL   A 1  1046 ? 0.927   51.576  103.175 1.00 20.93 ? 1044 VAL   A CG1   1 
ATOM   7746  C  CG2   . VAL   A 1  1046 ? 1.273   52.448  100.850 1.00 19.10 ? 1044 VAL   A CG2   1 
ATOM   7747  N  N     . HIS   A 1  1047 ? 3.026   55.529  101.431 1.00 16.35 ? 1045 HIS   A N     1 
ATOM   7748  C  CA    . HIS   A 1  1047 ? 3.951   56.158  100.505 1.00 19.76 ? 1045 HIS   A CA    1 
ATOM   7749  C  C     . HIS   A 1  1047 ? 4.904   57.068  101.253 1.00 19.70 ? 1045 HIS   A C     1 
ATOM   7750  O  O     . HIS   A 1  1047 ? 4.530   57.717  102.234 1.00 20.61 ? 1045 HIS   A O     1 
ATOM   7751  C  CB    . HIS   A 1  1047 ? 3.162   56.916  99.451  1.00 21.37 ? 1045 HIS   A CB    1 
ATOM   7752  C  CG    . HIS   A 1  1047 ? 2.168   56.042  98.761  1.00 25.90 ? 1045 HIS   A CG    1 
ATOM   7753  N  ND1   . HIS   A 1  1047 ? 2.547   55.018  97.917  1.00 29.19 ? 1045 HIS   A ND1   1 
ATOM   7754  C  CD2   . HIS   A 1  1047 ? 0.819   55.986  98.841  1.00 26.67 ? 1045 HIS   A CD2   1 
ATOM   7755  C  CE1   . HIS   A 1  1047 ? 1.468   54.397  97.475  1.00 28.23 ? 1045 HIS   A CE1   1 
ATOM   7756  N  NE2   . HIS   A 1  1047 ? 0.407   54.964  98.022  1.00 29.30 ? 1045 HIS   A NE2   1 
ATOM   7757  N  N     . THR   A 1  1048 ? 6.149   57.082  100.808 1.00 18.56 ? 1046 THR   A N     1 
ATOM   7758  C  CA    . THR   A 1  1048 ? 7.163   57.925  101.415 1.00 18.92 ? 1046 THR   A CA    1 
ATOM   7759  C  C     . THR   A 1  1048 ? 7.647   58.906  100.367 1.00 19.02 ? 1046 THR   A C     1 
ATOM   7760  O  O     . THR   A 1  1048 ? 7.973   58.512  99.243  1.00 19.94 ? 1046 THR   A O     1 
ATOM   7761  C  CB    . THR   A 1  1048 ? 8.322   57.089  101.926 1.00 20.68 ? 1046 THR   A CB    1 
ATOM   7762  O  OG1   . THR   A 1  1048 ? 7.815   56.081  102.809 1.00 22.19 ? 1046 THR   A OG1   1 
ATOM   7763  C  CG2   . THR   A 1  1048 ? 9.280   57.987  102.700 1.00 21.19 ? 1046 THR   A CG2   1 
ATOM   7764  N  N     . ASP   A 1  1049 ? 7.674   60.172  100.730 1.00 18.56 ? 1047 ASP   A N     1 
ATOM   7765  C  CA    . ASP   A 1  1049 ? 8.120   61.179  99.795  1.00 17.13 ? 1047 ASP   A CA    1 
ATOM   7766  C  C     . ASP   A 1  1049 ? 9.577   60.916  99.419  1.00 18.69 ? 1047 ASP   A C     1 
ATOM   7767  O  O     . ASP   A 1  1049 ? 10.421  60.716  100.305 1.00 17.78 ? 1047 ASP   A O     1 
ATOM   7768  C  CB    . ASP   A 1  1049 ? 7.959   62.561  100.420 1.00 16.28 ? 1047 ASP   A CB    1 
ATOM   7769  C  CG    . ASP   A 1  1049 ? 8.365   63.655  99.473  1.00 18.80 ? 1047 ASP   A CG    1 
ATOM   7770  O  OD1   . ASP   A 1  1049 ? 9.587   63.921  99.369  1.00 19.64 ? 1047 ASP   A OD1   1 
ATOM   7771  O  OD2   . ASP   A 1  1049 ? 7.474   64.215  98.792  1.00 19.93 ? 1047 ASP   A OD2   1 
ATOM   7772  N  N     . PRO   A 1  1050 ? 9.904   60.877  98.128  1.00 17.13 ? 1048 PRO   A N     1 
ATOM   7773  C  CA    . PRO   A 1  1050 ? 11.261  60.492  97.732  1.00 17.05 ? 1048 PRO   A CA    1 
ATOM   7774  C  C     . PRO   A 1  1050 ? 12.281  61.579  98.004  1.00 18.69 ? 1048 PRO   A C     1 
ATOM   7775  O  O     . PRO   A 1  1050 ? 13.462  61.270  98.202  1.00 19.13 ? 1048 PRO   A O     1 
ATOM   7776  C  CB    . PRO   A 1  1050 ? 11.119  60.188  96.235  1.00 21.38 ? 1048 PRO   A CB    1 
ATOM   7777  C  CG    . PRO   A 1  1050 ? 9.953   61.046  95.796  1.00 20.94 ? 1048 PRO   A CG    1 
ATOM   7778  C  CD    . PRO   A 1  1050 ? 9.013   61.086  96.976  1.00 18.39 ? 1048 PRO   A CD    1 
ATOM   7779  N  N     . VAL   A 1  1051 ? 11.853  62.840  98.021  1.00 16.95 ? 1049 VAL   A N     1 
ATOM   7780  C  CA    . VAL   A 1  1051 ? 12.765  63.920  98.370  1.00 17.11 ? 1049 VAL   A CA    1 
ATOM   7781  C  C     . VAL   A 1  1051 ? 13.093  63.868  99.851  1.00 18.27 ? 1049 VAL   A C     1 
ATOM   7782  O  O     . VAL   A 1  1051 ? 14.236  64.117  100.254 1.00 18.67 ? 1049 VAL   A O     1 
ATOM   7783  C  CB    . VAL   A 1  1051 ? 12.190  65.278  97.943  1.00 17.38 ? 1049 VAL   A CB    1 
ATOM   7784  C  CG1   . VAL   A 1  1051 ? 13.172  66.377  98.284  1.00 20.28 ? 1049 VAL   A CG1   1 
ATOM   7785  C  CG2   . VAL   A 1  1051 ? 11.930  65.278  96.447  1.00 19.71 ? 1049 VAL   A CG2   1 
ATOM   7786  N  N     . LEU   A 1  1052 ? 12.097  63.558  100.684 1.00 17.20 ? 1050 LEU   A N     1 
ATOM   7787  C  CA    . LEU   A 1  1052 ? 12.364  63.283  102.089 1.00 16.49 ? 1050 LEU   A CA    1 
ATOM   7788  C  C     . LEU   A 1  1052 ? 13.416  62.194  102.224 1.00 18.88 ? 1050 LEU   A C     1 
ATOM   7789  O  O     . LEU   A 1  1052 ? 14.370  62.328  102.995 1.00 16.87 ? 1050 LEU   A O     1 
ATOM   7790  C  CB    . LEU   A 1  1052 ? 11.063  62.867  102.774 1.00 16.49 ? 1050 LEU   A CB    1 
ATOM   7791  C  CG    . LEU   A 1  1052 ? 11.105  62.476  104.256 1.00 16.74 ? 1050 LEU   A CG    1 
ATOM   7792  C  CD1   . LEU   A 1  1052 ? 11.659  61.054  104.499 1.00 16.74 ? 1050 LEU   A CD1   1 
ATOM   7793  C  CD2   . LEU   A 1  1052 ? 11.866  63.510  105.089 1.00 17.40 ? 1050 LEU   A CD2   1 
ATOM   7794  N  N     . LEU   A 1  1053 ? 13.245  61.094  101.486 1.00 17.07 ? 1051 LEU   A N     1 
ATOM   7795  C  CA    . LEU   A 1  1053 ? 14.223  60.014  101.560 1.00 17.06 ? 1051 LEU   A CA    1 
ATOM   7796  C  C     . LEU   A 1  1053 ? 15.609  60.500  101.160 1.00 16.86 ? 1051 LEU   A C     1 
ATOM   7797  O  O     . LEU   A 1  1053 ? 16.604  60.164  101.812 1.00 17.91 ? 1051 LEU   A O     1 
ATOM   7798  C  CB    . LEU   A 1  1053 ? 13.789  58.846  100.674 1.00 18.63 ? 1051 LEU   A CB    1 
ATOM   7799  C  CG    . LEU   A 1  1053 ? 12.587  58.069  101.199 1.00 20.62 ? 1051 LEU   A CG    1 
ATOM   7800  C  CD1   . LEU   A 1  1053 ? 12.119  57.037  100.177 1.00 21.66 ? 1051 LEU   A CD1   1 
ATOM   7801  C  CD2   . LEU   A 1  1053 ? 12.896  57.416  102.533 1.00 22.00 ? 1051 LEU   A CD2   1 
ATOM   7802  N  N     . ASP   A 1  1054 ? 15.690  61.300  100.097 1.00 17.51 ? 1052 ASP   A N     1 
ATOM   7803  C  CA    . ASP   A 1  1054 ? 16.988  61.814  99.669  1.00 17.81 ? 1052 ASP   A CA    1 
ATOM   7804  C  C     . ASP   A 1  1054 ? 17.580  62.726  100.730 1.00 16.97 ? 1052 ASP   A C     1 
ATOM   7805  O  O     . ASP   A 1  1054 ? 18.788  62.705  100.966 1.00 19.32 ? 1052 ASP   A O     1 
ATOM   7806  C  CB    . ASP   A 1  1054 ? 16.843  62.582  98.360  1.00 18.61 ? 1052 ASP   A CB    1 
ATOM   7807  C  CG    . ASP   A 1  1054 ? 16.615  61.676  97.172  1.00 23.20 ? 1052 ASP   A CG    1 
ATOM   7808  O  OD1   . ASP   A 1  1054 ? 16.722  60.443  97.332  1.00 20.52 ? 1052 ASP   A OD1   1 
ATOM   7809  O  OD2   . ASP   A 1  1054 ? 16.325  62.210  96.085  1.00 26.42 ? 1052 ASP   A OD2   1 
ATOM   7810  N  N     . PHE   A 1  1055 ? 16.744  63.539  101.370 1.00 16.46 ? 1053 PHE   A N     1 
ATOM   7811  C  CA    . PHE   A 1  1055 ? 17.231  64.405  102.437 1.00 16.88 ? 1053 PHE   A CA    1 
ATOM   7812  C  C     . PHE   A 1  1055 ? 17.739  63.589  103.616 1.00 18.86 ? 1053 PHE   A C     1 
ATOM   7813  O  O     . PHE   A 1  1055 ? 18.782  63.909  104.200 1.00 18.60 ? 1053 PHE   A O     1 
ATOM   7814  C  CB    . PHE   A 1  1055 ? 16.107  65.346  102.860 1.00 17.54 ? 1053 PHE   A CB    1 
ATOM   7815  C  CG    . PHE   A 1  1055 ? 16.485  66.291  103.949 1.00 17.56 ? 1053 PHE   A CG    1 
ATOM   7816  C  CD1   . PHE   A 1  1055 ? 17.550  67.151  103.792 1.00 20.45 ? 1053 PHE   A CD1   1 
ATOM   7817  C  CD2   . PHE   A 1  1055 ? 15.746  66.342  105.114 1.00 19.24 ? 1053 PHE   A CD2   1 
ATOM   7818  C  CE1   . PHE   A 1  1055 ? 17.890  68.042  104.798 1.00 21.38 ? 1053 PHE   A CE1   1 
ATOM   7819  C  CE2   . PHE   A 1  1055 ? 16.081  67.233  106.126 1.00 20.30 ? 1053 PHE   A CE2   1 
ATOM   7820  C  CZ    . PHE   A 1  1055 ? 17.155  68.075  105.962 1.00 21.13 ? 1053 PHE   A CZ    1 
ATOM   7821  N  N     . ALA   A 1  1056 ? 17.020  62.528  103.984 1.00 18.53 ? 1054 ALA   A N     1 
ATOM   7822  C  CA    . ALA   A 1  1056 ? 17.474  61.679  105.084 1.00 18.49 ? 1054 ALA   A CA    1 
ATOM   7823  C  C     . ALA   A 1  1056 ? 18.839  61.070  104.786 1.00 21.09 ? 1054 ALA   A C     1 
ATOM   7824  O  O     . ALA   A 1  1056 ? 19.703  61.007  105.664 1.00 20.66 ? 1054 ALA   A O     1 
ATOM   7825  C  CB    . ALA   A 1  1056 ? 16.443  60.589  105.377 1.00 20.53 ? 1054 ALA   A CB    1 
ATOM   7826  N  N     . LYS   A 1  1057 ? 19.058  60.621  103.550 1.00 20.22 ? 1055 LYS   A N     1 
ATOM   7827  C  CA    . LYS   A 1  1057 ? 20.376  60.095  103.200 1.00 21.70 ? 1055 LYS   A CA    1 
ATOM   7828  C  C     . LYS   A 1  1057 ? 21.435  61.183  103.251 1.00 20.13 ? 1055 LYS   A C     1 
ATOM   7829  O  O     . LYS   A 1  1057 ? 22.576  60.932  103.665 1.00 21.54 ? 1055 LYS   A O     1 
ATOM   7830  C  CB    . LYS   A 1  1057 ? 20.329  59.479  101.807 1.00 23.37 ? 1055 LYS   A CB    1 
ATOM   7831  C  CG    . LYS   A 1  1057 ? 19.679  58.124  101.792 1.00 24.23 ? 1055 LYS   A CG    1 
ATOM   7832  C  CD    . LYS   A 1  1057 ? 19.890  57.442  100.463 1.00 22.48 ? 1055 LYS   A CD    1 
ATOM   7833  C  CE    . LYS   A 1  1057 ? 19.266  58.243  99.335  1.00 25.34 ? 1055 LYS   A CE    1 
ATOM   7834  N  NZ    . LYS   A 1  1057 ? 19.099  57.372  98.144  1.00 28.41 ? 1055 LYS   A NZ    1 
ATOM   7835  N  N     . TRP   A 1  1058 ? 21.082  62.386  102.801 1.00 19.44 ? 1056 TRP   A N     1 
ATOM   7836  C  CA    . TRP   A 1  1058 ? 22.004  63.512  102.867 1.00 20.84 ? 1056 TRP   A CA    1 
ATOM   7837  C  C     . TRP   A 1  1058 ? 22.367  63.833  104.311 1.00 22.35 ? 1056 TRP   A C     1 
ATOM   7838  O  O     . TRP   A 1  1058 ? 23.539  64.063  104.625 1.00 23.19 ? 1056 TRP   A O     1 
ATOM   7839  C  CB    . TRP   A 1  1058 ? 21.386  64.726  102.167 1.00 21.45 ? 1056 TRP   A CB    1 
ATOM   7840  C  CG    . TRP   A 1  1058 ? 22.222  65.978  102.250 1.00 22.73 ? 1056 TRP   A CG    1 
ATOM   7841  C  CD1   . TRP   A 1  1058 ? 23.235  66.356  101.408 1.00 27.30 ? 1056 TRP   A CD1   1 
ATOM   7842  C  CD2   . TRP   A 1  1058 ? 22.111  67.014  103.233 1.00 22.13 ? 1056 TRP   A CD2   1 
ATOM   7843  N  NE1   . TRP   A 1  1058 ? 23.754  67.566  101.809 1.00 27.59 ? 1056 TRP   A NE1   1 
ATOM   7844  C  CE2   . TRP   A 1  1058 ? 23.085  67.988  102.928 1.00 28.77 ? 1056 TRP   A CE2   1 
ATOM   7845  C  CE3   . TRP   A 1  1058 ? 21.286  67.208  104.344 1.00 22.75 ? 1056 TRP   A CE3   1 
ATOM   7846  C  CZ2   . TRP   A 1  1058 ? 23.251  69.143  103.694 1.00 27.92 ? 1056 TRP   A CZ2   1 
ATOM   7847  C  CZ3   . TRP   A 1  1058 ? 21.452  68.356  105.102 1.00 26.15 ? 1056 TRP   A CZ3   1 
ATOM   7848  C  CH2   . TRP   A 1  1058 ? 22.429  69.305  104.775 1.00 25.78 ? 1056 TRP   A CH2   1 
ATOM   7849  N  N     . LEU   A 1  1059 ? 21.376  63.833  105.206 1.00 19.53 ? 1057 LEU   A N     1 
ATOM   7850  C  CA    . LEU   A 1  1059 ? 21.641  64.069  106.623 1.00 21.58 ? 1057 LEU   A CA    1 
ATOM   7851  C  C     . LEU   A 1  1059 ? 22.614  63.044  107.173 1.00 21.91 ? 1057 LEU   A C     1 
ATOM   7852  O  O     . LEU   A 1  1059 ? 23.557  63.393  107.894 1.00 23.56 ? 1057 LEU   A O     1 
ATOM   7853  C  CB    . LEU   A 1  1059 ? 20.329  64.010  107.409 1.00 19.29 ? 1057 LEU   A CB    1 
ATOM   7854  C  CG    . LEU   A 1  1059 ? 19.446  65.240  107.275 1.00 20.47 ? 1057 LEU   A CG    1 
ATOM   7855  C  CD1   . LEU   A 1  1059 ? 18.062  64.977  107.874 1.00 20.61 ? 1057 LEU   A CD1   1 
ATOM   7856  C  CD2   . LEU   A 1  1059 ? 20.087  66.440  107.964 1.00 21.83 ? 1057 LEU   A CD2   1 
ATOM   7857  N  N     . ASP   A 1  1060 ? 22.388  61.765  106.863 1.00 21.10 ? 1058 ASP   A N     1 
ATOM   7858  C  CA    . ASP   A 1  1060 ? 23.312  60.727  107.307 1.00 25.12 ? 1058 ASP   A CA    1 
ATOM   7859  C  C     . ASP   A 1  1060 ? 24.706  60.960  106.745 1.00 24.53 ? 1058 ASP   A C     1 
ATOM   7860  O  O     . ASP   A 1  1060 ? 25.702  60.811  107.463 1.00 28.67 ? 1058 ASP   A O     1 
ATOM   7861  C  CB    . ASP   A 1  1060 ? 22.792  59.352  106.904 1.00 27.91 ? 1058 ASP   A CB    1 
ATOM   7862  C  CG    . ASP   A 1  1060 ? 21.938  58.720  107.979 1.00 25.04 ? 1058 ASP   A CG    1 
ATOM   7863  O  OD1   . ASP   A 1  1060 ? 22.228  58.946  109.181 1.00 33.80 ? 1058 ASP   A OD1   1 
ATOM   7864  O  OD2   . ASP   A 1  1060 ? 20.995  57.990  107.630 1.00 34.10 ? 1058 ASP   A OD2   1 
ATOM   7865  N  N     . GLY   A 1  1061 ? 24.797  61.352  105.473 1.00 25.88 ? 1059 GLY   A N     1 
ATOM   7866  C  CA    . GLY   A 1  1061 ? 26.100  61.633  104.888 1.00 26.86 ? 1059 GLY   A CA    1 
ATOM   7867  C  C     . GLY   A 1  1061 ? 26.809  62.795  105.553 1.00 29.83 ? 1059 GLY   A C     1 
ATOM   7868  O  O     . GLY   A 1  1061 ? 28.045  62.828  105.607 1.00 27.92 ? 1059 GLY   A O     1 
ATOM   7869  N  N     . LYS   A 1  1062 ? 26.048  63.764  106.061 1.00 26.56 ? 1060 LYS   A N     1 
ATOM   7870  C  CA    . LYS   A 1  1062 ? 26.602  64.885  106.808 1.00 27.04 ? 1060 LYS   A CA    1 
ATOM   7871  C  C     . LYS   A 1  1062 ? 26.902  64.531  108.258 1.00 28.33 ? 1060 LYS   A C     1 
ATOM   7872  O  O     . LYS   A 1  1062 ? 27.462  65.363  108.979 1.00 36.31 ? 1060 LYS   A O     1 
ATOM   7873  C  CB    . LYS   A 1  1062 ? 25.649  66.085  106.757 1.00 29.04 ? 1060 LYS   A CB    1 
ATOM   7874  C  CG    . LYS   A 1  1062 ? 25.506  66.734  105.381 1.00 31.79 ? 1060 LYS   A CG    1 
ATOM   7875  C  CD    . LYS   A 1  1062 ? 26.820  67.364  104.928 1.00 36.99 ? 1060 LYS   A CD    1 
ATOM   7876  C  CE    . LYS   A 1  1062 ? 26.719  67.902  103.512 1.00 43.70 ? 1060 LYS   A CE    1 
ATOM   7877  N  NZ    . LYS   A 1  1062 ? 27.976  68.584  103.093 1.00 45.14 ? 1060 LYS   A NZ    1 
ATOM   7878  N  N     . GLY   A 1  1063 ? 26.563  63.322  108.696 1.00 26.16 ? 1061 GLY   A N     1 
ATOM   7879  C  CA    . GLY   A 1  1063 ? 26.759  62.912  110.071 1.00 28.69 ? 1061 GLY   A CA    1 
ATOM   7880  C  C     . GLY   A 1  1063 ? 25.661  63.312  111.026 1.00 31.39 ? 1061 GLY   A C     1 
ATOM   7881  O  O     . GLY   A 1  1063 ? 25.816  63.108  112.237 1.00 31.00 ? 1061 GLY   A O     1 
ATOM   7882  N  N     . ALA   A 1  1064 ? 24.555  63.870  110.523 1.00 26.45 ? 1062 ALA   A N     1 
ATOM   7883  C  CA    . ALA   A 1  1064 ? 23.423  64.291  111.354 1.00 24.90 ? 1062 ALA   A CA    1 
ATOM   7884  C  C     . ALA   A 1  1064 ? 22.502  63.094  111.584 1.00 26.45 ? 1062 ALA   A C     1 
ATOM   7885  O  O     . ALA   A 1  1064 ? 21.366  63.019  111.099 1.00 22.33 ? 1062 ALA   A O     1 
ATOM   7886  C  CB    . ALA   A 1  1064 ? 22.699  65.466  110.712 1.00 26.17 ? 1062 ALA   A CB    1 
ATOM   7887  N  N     . ARG   A 1  1065 ? 23.032  62.138  112.349 1.00 23.25 ? 1063 ARG   A N     1 
ATOM   7888  C  CA    . ARG   A 1  1065 ? 22.395  60.832  112.471 1.00 23.01 ? 1063 ARG   A CA    1 
ATOM   7889  C  C     . ARG   A 1  1065 ? 21.025  60.938  113.133 1.00 24.74 ? 1063 ARG   A C     1 
ATOM   7890  O  O     . ARG   A 1  1065 ? 20.062  60.299  112.694 1.00 23.85 ? 1063 ARG   A O     1 
ATOM   7891  C  CB    . ARG   A 1  1065 ? 23.304  59.880  113.256 1.00 25.09 ? 1063 ARG   A CB    1 
ATOM   7892  N  N     . ALA   A 1  1066 ? 20.916  61.717  114.211 1.00 24.12 ? 1064 ALA   A N     1 
ATOM   7893  C  CA    . ALA   A 1  1066 ? 19.619  61.841  114.871 1.00 22.81 ? 1064 ALA   A CA    1 
ATOM   7894  C  C     . ALA   A 1  1066 ? 18.591  62.515  113.969 1.00 23.19 ? 1064 ALA   A C     1 
ATOM   7895  O  O     . ALA   A 1  1066 ? 17.424  62.106  113.935 1.00 23.79 ? 1064 ALA   A O     1 
ATOM   7896  C  CB    . ALA   A 1  1066 ? 19.751  62.589  116.196 1.00 24.06 ? 1064 ALA   A CB    1 
ATOM   7897  N  N     . GLU   A 1  1067 ? 19.000  63.557  113.239 1.00 22.56 ? 1065 GLU   A N     1 
ATOM   7898  C  CA    . GLU   A 1  1067 ? 18.064  64.235  112.346 1.00 20.88 ? 1065 GLU   A CA    1 
ATOM   7899  C  C     . GLU   A 1  1067 ? 17.674  63.343  111.177 1.00 21.83 ? 1065 GLU   A C     1 
ATOM   7900  O  O     . GLU   A 1  1067 ? 16.530  63.391  110.715 1.00 21.61 ? 1065 GLU   A O     1 
ATOM   7901  C  CB    . GLU   A 1  1067 ? 18.663  65.546  111.843 1.00 24.01 ? 1065 GLU   A CB    1 
ATOM   7902  C  CG    . GLU   A 1  1067 ? 18.744  66.636  112.900 1.00 22.22 ? 1065 GLU   A CG    1 
ATOM   7903  C  CD    . GLU   A 1  1067 ? 19.939  66.499  113.823 1.00 28.71 ? 1065 GLU   A CD    1 
ATOM   7904  O  OE1   . GLU   A 1  1067 ? 20.817  65.637  113.575 1.00 24.00 ? 1065 GLU   A OE1   1 
ATOM   7905  O  OE2   . GLU   A 1  1067 ? 19.997  67.265  114.809 1.00 31.47 ? 1065 GLU   A OE2   1 
ATOM   7906  N  N     . ALA   A 1  1068 ? 18.613  62.528  110.688 1.00 21.88 ? 1066 ALA   A N     1 
ATOM   7907  C  CA    . ALA   A 1  1068 ? 18.277  61.581  109.628 1.00 22.03 ? 1066 ALA   A CA    1 
ATOM   7908  C  C     . ALA   A 1  1068 ? 17.228  60.592  110.103 1.00 21.51 ? 1066 ALA   A C     1 
ATOM   7909  O  O     . ALA   A 1  1068 ? 16.301  60.250  109.358 1.00 21.09 ? 1066 ALA   A O     1 
ATOM   7910  C  CB    . ALA   A 1  1068 ? 19.530  60.836  109.177 1.00 22.75 ? 1066 ALA   A CB    1 
ATOM   7911  N  N     . GLU   A 1  1069 ? 17.365  60.108  111.338 1.00 20.68 ? 1067 GLU   A N     1 
ATOM   7912  C  CA    . GLU   A 1  1069 ? 16.354  59.218  111.889 1.00 21.17 ? 1067 GLU   A CA    1 
ATOM   7913  C  C     . GLU   A 1  1069 ? 15.018  59.933  112.020 1.00 23.33 ? 1067 GLU   A C     1 
ATOM   7914  O  O     . GLU   A 1  1069 ? 13.966  59.366  111.704 1.00 22.52 ? 1067 GLU   A O     1 
ATOM   7915  C  CB    . GLU   A 1  1069 ? 16.815  58.686  113.245 1.00 25.44 ? 1067 GLU   A CB    1 
ATOM   7916  C  CG    . GLU   A 1  1069 ? 15.755  57.895  113.990 1.00 32.21 ? 1067 GLU   A CG    1 
ATOM   7917  C  CD    . GLU   A 1  1069 ? 15.505  56.521  113.393 1.00 38.51 ? 1067 GLU   A CD    1 
ATOM   7918  O  OE1   . GLU   A 1  1069 ? 16.168  56.161  112.395 1.00 44.24 ? 1067 GLU   A OE1   1 
ATOM   7919  O  OE2   . GLU   A 1  1069 ? 14.642  55.794  113.932 1.00 50.38 ? 1067 GLU   A OE2   1 
ATOM   7920  N  N     . ALA   A 1  1070 ? 15.043  61.184  112.485 1.00 22.74 ? 1068 ALA   A N     1 
ATOM   7921  C  CA    . ALA   A 1  1070 ? 13.809  61.948  112.607 1.00 21.06 ? 1068 ALA   A CA    1 
ATOM   7922  C  C     . ALA   A 1  1070 ? 13.197  62.180  111.239 1.00 19.72 ? 1068 ALA   A C     1 
ATOM   7923  O  O     . ALA   A 1  1070 ? 11.972  62.169  111.088 1.00 21.29 ? 1068 ALA   A O     1 
ATOM   7924  C  CB    . ALA   A 1  1070 ? 14.082  63.283  113.296 1.00 24.04 ? 1068 ALA   A CB    1 
ATOM   7925  N  N     . ALA   A 1  1071 ? 14.041  62.382  110.229 1.00 19.93 ? 1069 ALA   A N     1 
ATOM   7926  C  CA    . ALA   A 1  1071 ? 13.535  62.550  108.876 1.00 16.97 ? 1069 ALA   A CA    1 
ATOM   7927  C  C     . ALA   A 1  1071 ? 12.857  61.275  108.390 1.00 20.03 ? 1069 ALA   A C     1 
ATOM   7928  O  O     . ALA   A 1  1071 ? 11.746  61.314  107.846 1.00 17.53 ? 1069 ALA   A O     1 
ATOM   7929  C  CB    . ALA   A 1  1071 ? 14.672  62.969  107.944 1.00 19.33 ? 1069 ALA   A CB    1 
ATOM   7930  N  N     . ARG   A 1  1072 ? 13.500  60.125  108.599 1.00 18.70 ? 1070 ARG   A N     1 
ATOM   7931  C  CA    . ARG   A 1  1072 ? 12.860  58.875  108.207 1.00 19.57 ? 1070 ARG   A CA    1 
ATOM   7932  C  C     . ARG   A 1  1072 ? 11.550  58.676  108.952 1.00 19.46 ? 1070 ARG   A C     1 
ATOM   7933  O  O     . ARG   A 1  1072 ? 10.563  58.213  108.372 1.00 20.98 ? 1070 ARG   A O     1 
ATOM   7934  C  CB    . ARG   A 1  1072 ? 13.796  57.691  108.439 1.00 19.11 ? 1070 ARG   A CB    1 
ATOM   7935  C  CG    . ARG   A 1  1072 ? 14.890  57.591  107.395 1.00 22.74 ? 1070 ARG   A CG    1 
ATOM   7936  C  CD    . ARG   A 1  1072 ? 15.700  56.329  107.607 1.00 24.32 ? 1070 ARG   A CD    1 
ATOM   7937  N  NE    . ARG   A 1  1072 ? 16.450  56.373  108.854 1.00 28.25 ? 1070 ARG   A NE    1 
ATOM   7938  C  CZ    . ARG   A 1  1072 ? 17.676  56.866  108.973 1.00 27.13 ? 1070 ARG   A CZ    1 
ATOM   7939  N  NH1   . ARG   A 1  1072 ? 18.322  57.374  107.931 1.00 29.91 ? 1070 ARG   A NH1   1 
ATOM   7940  N  NH2   . ARG   A 1  1072 ? 18.268  56.846  110.165 1.00 29.92 ? 1070 ARG   A NH2   1 
ATOM   7941  N  N     . ASN   A 1  1073 ? 11.514  59.028  110.240 1.00 18.98 ? 1071 ASN   A N     1 
ATOM   7942  C  CA    . ASN   A 1  1073 ? 10.273  58.896  110.995 1.00 20.09 ? 1071 ASN   A CA    1 
ATOM   7943  C  C     . ASN   A 1  1073 ? 9.192   59.808  110.437 1.00 20.89 ? 1071 ASN   A C     1 
ATOM   7944  O  O     . ASN   A 1  1073 ? 8.023   59.412  110.343 1.00 22.01 ? 1071 ASN   A O     1 
ATOM   7945  C  CB    . ASN   A 1  1073 ? 10.514  59.186  112.475 1.00 22.61 ? 1071 ASN   A CB    1 
ATOM   7946  C  CG    . ASN   A 1  1073 ? 11.278  58.075  113.163 1.00 26.30 ? 1071 ASN   A CG    1 
ATOM   7947  O  OD1   . ASN   A 1  1073 ? 11.372  56.961  112.646 1.00 30.61 ? 1071 ASN   A OD1   1 
ATOM   7948  N  ND2   . ASN   A 1  1073 ? 11.821  58.369  114.332 1.00 29.45 ? 1071 ASN   A ND2   1 
ATOM   7949  N  N     . ALA   A 1  1074 ? 9.565   61.035  110.063 1.00 18.21 ? 1072 ALA   A N     1 
ATOM   7950  C  CA    . ALA   A 1  1074 ? 8.606   61.938  109.433 1.00 17.96 ? 1072 ALA   A CA    1 
ATOM   7951  C  C     . ALA   A 1  1074 ? 8.093   61.357  108.128 1.00 19.74 ? 1072 ALA   A C     1 
ATOM   7952  O  O     . ALA   A 1  1074 ? 6.899   61.461  107.824 1.00 18.25 ? 1072 ALA   A O     1 
ATOM   7953  C  CB    . ALA   A 1  1074 ? 9.244   63.308  109.199 1.00 23.24 ? 1072 ALA   A CB    1 
ATOM   7954  N  N     . GLY   A 1  1075 ? 8.982   60.741  107.346 1.00 18.37 ? 1073 GLY   A N     1 
ATOM   7955  C  CA    . GLY   A 1  1075 ? 8.556   60.139  106.095 1.00 17.70 ? 1073 GLY   A CA    1 
ATOM   7956  C  C     . GLY   A 1  1075 ? 7.495   59.075  106.290 1.00 19.07 ? 1073 GLY   A C     1 
ATOM   7957  O  O     . GLY   A 1  1075 ? 6.548   58.980  105.503 1.00 20.66 ? 1073 GLY   A O     1 
ATOM   7958  N  N     . SER   A 1  1076 ? 7.655   58.245  107.326 1.00 19.14 ? 1074 SER   A N     1 
ATOM   7959  C  CA    . SER   A 1  1076 ? 6.664   57.216  107.632 1.00 19.82 ? 1074 SER   A CA    1 
ATOM   7960  C  C     . SER   A 1  1076 ? 5.404   57.813  108.238 1.00 20.33 ? 1074 SER   A C     1 
ATOM   7961  O  O     . SER   A 1  1076 ? 4.293   57.374  107.922 1.00 22.87 ? 1074 SER   A O     1 
ATOM   7962  C  CB    . SER   A 1  1076 ? 7.248   56.199  108.615 1.00 23.03 ? 1074 SER   A CB    1 
ATOM   7963  O  OG    . SER   A 1  1076 ? 8.309   55.479  108.034 1.00 33.16 ? 1074 SER   A OG    1 
ATOM   7964  N  N     . SER   A 1  1077 ? 5.559   58.801  109.124 1.00 19.59 ? 1075 SER   A N     1 
ATOM   7965  C  CA    A SER   A 1  1077 ? 4.410   59.348  109.837 0.48 20.81 ? 1075 SER   A CA    1 
ATOM   7966  C  CA    B SER   A 1  1077 ? 4.418   59.362  109.842 0.52 20.81 ? 1075 SER   A CA    1 
ATOM   7967  C  C     . SER   A 1  1077 ? 3.527   60.192  108.929 1.00 19.39 ? 1075 SER   A C     1 
ATOM   7968  O  O     . SER   A 1  1077 ? 2.319   60.317  109.179 1.00 21.03 ? 1075 SER   A O     1 
ATOM   7969  C  CB    A SER   A 1  1077 ? 4.885   60.169  111.036 0.48 20.32 ? 1075 SER   A CB    1 
ATOM   7970  C  CB    B SER   A 1  1077 ? 4.917   60.227  111.001 0.52 20.27 ? 1075 SER   A CB    1 
ATOM   7971  O  OG    A SER   A 1  1077 ? 5.413   59.326  112.044 0.48 25.31 ? 1075 SER   A OG    1 
ATOM   7972  O  OG    B SER   A 1  1077 ? 3.838   60.859  111.674 0.52 24.66 ? 1075 SER   A OG    1 
ATOM   7973  N  N     . SER   A 1  1078 ? 4.099   60.766  107.886 1.00 16.95 ? 1076 SER   A N     1 
ATOM   7974  C  CA    . SER   A 1  1078 ? 3.333   61.585  106.970 1.00 16.71 ? 1076 SER   A CA    1 
ATOM   7975  C  C     . SER   A 1  1078 ? 2.207   60.772  106.347 1.00 17.92 ? 1076 SER   A C     1 
ATOM   7976  O  O     . SER   A 1  1078 ? 2.380   59.610  105.981 1.00 18.82 ? 1076 SER   A O     1 
ATOM   7977  C  CB    . SER   A 1  1078 ? 4.266   62.068  105.872 1.00 18.02 ? 1076 SER   A CB    1 
ATOM   7978  O  OG    . SER   A 1  1078 ? 3.528   62.757  104.883 1.00 17.49 ? 1076 SER   A OG    1 
ATOM   7979  N  N     . ALA   A 1  1079 ? 1.040   61.392  106.228 1.00 15.93 ? 1077 ALA   A N     1 
ATOM   7980  C  CA    . ALA   A 1  1079 ? -0.074  60.770  105.538 1.00 16.14 ? 1077 ALA   A CA    1 
ATOM   7981  C  C     . ALA   A 1  1079 ? -0.219  61.283  104.118 1.00 18.14 ? 1077 ALA   A C     1 
ATOM   7982  O  O     . ALA   A 1  1079 ? -1.233  61.016  103.469 1.00 16.19 ? 1077 ALA   A O     1 
ATOM   7983  C  CB    . ALA   A 1  1079 ? -1.367  60.975  106.326 1.00 17.06 ? 1077 ALA   A CB    1 
ATOM   7984  N  N     . LEU   A 1  1080 ? 0.771   62.016  103.623 1.00 16.31 ? 1078 LEU   A N     1 
ATOM   7985  C  CA    . LEU   A 1  1080 ? 0.808   62.389  102.216 1.00 15.39 ? 1078 LEU   A CA    1 
ATOM   7986  C  C     . LEU   A 1  1080 ? 0.569   61.167  101.341 1.00 15.46 ? 1078 LEU   A C     1 
ATOM   7987  O  O     . LEU   A 1  1080 ? 1.223   60.137  101.505 1.00 16.21 ? 1078 LEU   A O     1 
ATOM   7988  C  CB    . LEU   A 1  1080 ? 2.192   62.955  101.903 1.00 14.97 ? 1078 LEU   A CB    1 
ATOM   7989  C  CG    . LEU   A 1  1080 ? 2.419   63.250  100.424 1.00 15.75 ? 1078 LEU   A CG    1 
ATOM   7990  C  CD1   . LEU   A 1  1080 ? 1.561   64.427  99.994  1.00 19.03 ? 1078 LEU   A CD1   1 
ATOM   7991  C  CD2   . LEU   A 1  1080 ? 3.895   63.542  100.177 1.00 17.11 ? 1078 LEU   A CD2   1 
ATOM   7992  N  N     . GLY   A 1  1081 ? -0.374  61.281  100.409 1.00 15.73 ? 1079 GLY   A N     1 
ATOM   7993  C  CA    . GLY   A 1  1081 ? -0.681  60.161  99.546  1.00 16.83 ? 1079 GLY   A CA    1 
ATOM   7994  C  C     . GLY   A 1  1081 ? -1.883  59.350  99.977  1.00 16.86 ? 1079 GLY   A C     1 
ATOM   7995  O  O     . GLY   A 1  1081 ? -2.289  58.434  99.245  1.00 18.62 ? 1079 GLY   A O     1 
ATOM   7996  N  N     . LEU   A 1  1082 ? -2.433  59.624  101.158 1.00 16.25 ? 1080 LEU   A N     1 
ATOM   7997  C  CA    A LEU   A 1  1082 ? -3.705  59.031  101.539 0.48 16.25 ? 1080 LEU   A CA    1 
ATOM   7998  C  CA    B LEU   A 1  1082 ? -3.707  59.034  101.541 0.52 16.24 ? 1080 LEU   A CA    1 
ATOM   7999  C  C     . LEU   A 1  1082 ? -4.715  59.257  100.425 1.00 17.84 ? 1080 LEU   A C     1 
ATOM   8000  O  O     . LEU   A 1  1082 ? -4.784  60.338  99.843  1.00 17.96 ? 1080 LEU   A O     1 
ATOM   8001  C  CB    A LEU   A 1  1082 ? -4.201  59.683  102.828 0.48 16.81 ? 1080 LEU   A CB    1 
ATOM   8002  C  CB    B LEU   A 1  1082 ? -4.199  59.692  102.832 0.52 16.81 ? 1080 LEU   A CB    1 
ATOM   8003  C  CG    A LEU   A 1  1082 ? -5.541  59.181  103.364 0.48 17.98 ? 1080 LEU   A CG    1 
ATOM   8004  C  CG    B LEU   A 1  1082 ? -5.559  59.270  103.394 0.52 17.97 ? 1080 LEU   A CG    1 
ATOM   8005  C  CD1   A LEU   A 1  1082 ? -5.502  57.683  103.594 0.48 17.03 ? 1080 LEU   A CD1   1 
ATOM   8006  C  CD1   B LEU   A 1  1082 ? -5.569  59.387  104.900 0.52 17.71 ? 1080 LEU   A CD1   1 
ATOM   8007  C  CD2   A LEU   A 1  1082 ? -5.911  59.911  104.637 0.48 17.54 ? 1080 LEU   A CD2   1 
ATOM   8008  C  CD2   B LEU   A 1  1082 ? -6.677  60.118  102.802 0.52 15.65 ? 1080 LEU   A CD2   1 
ATOM   8009  N  N     . ASP   A 1  1083 ? -5.481  58.217  100.114 1.00 18.08 ? 1081 ASP   A N     1 
ATOM   8010  C  CA    . ASP   A 1  1083 ? -6.406  58.283  98.984  1.00 18.75 ? 1081 ASP   A CA    1 
ATOM   8011  C  C     . ASP   A 1  1083 ? -7.554  57.336  99.307  1.00 19.75 ? 1081 ASP   A C     1 
ATOM   8012  O  O     . ASP   A 1  1083 ? -7.404  56.116  99.203  1.00 23.34 ? 1081 ASP   A O     1 
ATOM   8013  C  CB    . ASP   A 1  1083 ? -5.686  57.871  97.708  1.00 21.99 ? 1081 ASP   A CB    1 
ATOM   8014  C  CG    . ASP   A 1  1083 ? -6.549  58.010  96.472  1.00 29.52 ? 1081 ASP   A CG    1 
ATOM   8015  O  OD1   . ASP   A 1  1083 ? -7.637  58.612  96.564  1.00 33.38 ? 1081 ASP   A OD1   1 
ATOM   8016  O  OD2   . ASP   A 1  1083 ? -6.127  57.513  95.404  1.00 31.74 ? 1081 ASP   A OD2   1 
ATOM   8017  N  N     . LEU   A 1  1084 ? -8.686  57.904  99.708  1.00 18.74 ? 1082 LEU   A N     1 
ATOM   8018  C  CA    . LEU   A 1  1084 ? -9.786  57.115  100.222 1.00 19.59 ? 1082 LEU   A CA    1 
ATOM   8019  C  C     . LEU   A 1  1084 ? -11.044 57.427  99.444  1.00 19.48 ? 1082 LEU   A C     1 
ATOM   8020  O  O     . LEU   A 1  1084 ? -11.209 58.524  98.904  1.00 20.68 ? 1082 LEU   A O     1 
ATOM   8021  C  CB    . LEU   A 1  1084 ? -10.089 57.477  101.668 1.00 20.59 ? 1082 LEU   A CB    1 
ATOM   8022  C  CG    . LEU   A 1  1084 ? -8.988  57.245  102.682 1.00 23.52 ? 1082 LEU   A CG    1 
ATOM   8023  C  CD1   . LEU   A 1  1084 ? -9.404  57.901  103.977 1.00 24.61 ? 1082 LEU   A CD1   1 
ATOM   8024  C  CD2   . LEU   A 1  1084 ? -8.763  55.763  102.854 1.00 26.43 ? 1082 LEU   A CD2   1 
ATOM   8025  N  N     . GLU   A 1  1085 ? -11.926 56.443  99.391  1.00 19.00 ? 1083 GLU   A N     1 
ATOM   8026  C  CA    . GLU   A 1  1085 ? -13.286 56.670  98.934  1.00 17.56 ? 1083 GLU   A CA    1 
ATOM   8027  C  C     . GLU   A 1  1085 ? -14.189 56.674  100.154 1.00 19.14 ? 1083 GLU   A C     1 
ATOM   8028  O  O     . GLU   A 1  1085 ? -14.151 55.743  100.964 1.00 23.79 ? 1083 GLU   A O     1 
ATOM   8029  C  CB    . GLU   A 1  1085 ? -13.746 55.611  97.932  1.00 20.24 ? 1083 GLU   A CB    1 
ATOM   8030  C  CG    . GLU   A 1  1085 ? -15.197 55.875  97.539  1.00 20.98 ? 1083 GLU   A CG    1 
ATOM   8031  C  CD    . GLU   A 1  1085 ? -15.692 55.080  96.353  1.00 28.56 ? 1083 GLU   A CD    1 
ATOM   8032  O  OE1   . GLU   A 1  1085 ? -14.867 54.474  95.640  1.00 28.59 ? 1083 GLU   A OE1   1 
ATOM   8033  O  OE2   . GLU   A 1  1085 ? -16.927 55.072  96.140  1.00 28.86 ? 1083 GLU   A OE2   1 
ATOM   8034  N  N     . LEU   A 1  1086 ? -14.980 57.726  100.291 1.00 19.11 ? 1084 LEU   A N     1 
ATOM   8035  C  CA    . LEU   A 1  1086 ? -15.860 57.894  101.439 1.00 18.59 ? 1084 LEU   A CA    1 
ATOM   8036  C  C     . LEU   A 1  1086 ? -17.249 57.357  101.113 1.00 21.20 ? 1084 LEU   A C     1 
ATOM   8037  O  O     . LEU   A 1  1086 ? -17.743 57.559  100.000 1.00 20.46 ? 1084 LEU   A O     1 
ATOM   8038  C  CB    . LEU   A 1  1086 ? -15.970 59.370  101.790 1.00 19.02 ? 1084 LEU   A CB    1 
ATOM   8039  C  CG    . LEU   A 1  1086 ? -14.615 60.010  102.114 1.00 22.57 ? 1084 LEU   A CG    1 
ATOM   8040  C  CD1   . LEU   A 1  1086 ? -14.773 61.461  102.524 1.00 21.63 ? 1084 LEU   A CD1   1 
ATOM   8041  C  CD2   . LEU   A 1  1086 ? -13.885 59.218  103.196 1.00 24.33 ? 1084 LEU   A CD2   1 
ATOM   8042  N  N     . PRO   A 1  1087 ? -17.871 56.665  102.064 1.00 21.53 ? 1085 PRO   A N     1 
ATOM   8043  C  CA    . PRO   A 1  1087 ? -19.217 56.130  101.825 1.00 21.57 ? 1085 PRO   A CA    1 
ATOM   8044  C  C     . PRO   A 1  1087 ? -20.204 57.248  101.553 1.00 20.04 ? 1085 PRO   A C     1 
ATOM   8045  O  O     . PRO   A 1  1087 ? -20.175 58.302  102.189 1.00 23.88 ? 1085 PRO   A O     1 
ATOM   8046  C  CB    . PRO   A 1  1087 ? -19.557 55.413  103.137 1.00 28.09 ? 1085 PRO   A CB    1 
ATOM   8047  C  CG    . PRO   A 1  1087 ? -18.255 55.179  103.808 1.00 27.67 ? 1085 PRO   A CG    1 
ATOM   8048  C  CD    . PRO   A 1  1087 ? -17.339 56.284  103.385 1.00 21.28 ? 1085 PRO   A CD    1 
ATOM   8049  N  N     . GLY   A 1  1088 ? -21.075 57.015  100.582 1.00 22.08 ? 1086 GLY   A N     1 
ATOM   8050  C  CA    . GLY   A 1  1088 ? -22.066 57.992  100.225 1.00 23.36 ? 1086 GLY   A CA    1 
ATOM   8051  C  C     . GLY   A 1  1088 ? -23.163 57.386  99.381  1.00 18.16 ? 1086 GLY   A C     1 
ATOM   8052  O  O     . GLY   A 1  1088 ? -23.372 56.173  99.354  1.00 20.11 ? 1086 GLY   A O     1 
ATOM   8053  N  N     . PRO   A 1  1089 ? -23.875 58.236  98.660  1.00 21.57 ? 1087 PRO   A N     1 
ATOM   8054  C  CA    . PRO   A 1  1089 ? -24.996 57.756  97.852  1.00 20.66 ? 1087 PRO   A CA    1 
ATOM   8055  C  C     . PRO   A 1  1089 ? -24.506 56.980  96.640  1.00 21.64 ? 1087 PRO   A C     1 
ATOM   8056  O  O     . PRO   A 1  1089 ? -23.372 57.128  96.178  1.00 21.37 ? 1087 PRO   A O     1 
ATOM   8057  C  CB    . PRO   A 1  1089 ? -25.675 59.055  97.413  1.00 23.06 ? 1087 PRO   A CB    1 
ATOM   8058  C  CG    . PRO   A 1  1089 ? -24.523 60.054  97.357  1.00 23.57 ? 1087 PRO   A CG    1 
ATOM   8059  C  CD    . PRO   A 1  1089 ? -23.661 59.688  98.533  1.00 21.45 ? 1087 PRO   A CD    1 
ATOM   8060  N  N     . VAL   A 1  1090 ? -25.398 56.139  96.118  1.00 20.75 ? 1088 VAL   A N     1 
ATOM   8061  C  CA    . VAL   A 1  1090 ? -25.117 55.484  94.852  1.00 16.60 ? 1088 VAL   A CA    1 
ATOM   8062  C  C     . VAL   A 1  1090 ? -24.993 56.528  93.751  1.00 18.32 ? 1088 VAL   A C     1 
ATOM   8063  O  O     . VAL   A 1  1090 ? -25.473 57.663  93.862  1.00 19.47 ? 1088 VAL   A O     1 
ATOM   8064  C  CB    . VAL   A 1  1090 ? -26.168 54.427  94.483  1.00 19.97 ? 1088 VAL   A CB    1 
ATOM   8065  C  CG1   . VAL   A 1  1090 ? -26.264 53.373  95.564  1.00 21.28 ? 1088 VAL   A CG1   1 
ATOM   8066  C  CG2   . VAL   A 1  1090 ? -27.528 55.083  94.249  1.00 19.96 ? 1088 VAL   A CG2   1 
ATOM   8067  N  N     . GLY   A 1  1091 ? -24.337 56.130  92.667  1.00 18.24 ? 1089 GLY   A N     1 
ATOM   8068  C  CA    . GLY   A 1  1091 ? -24.218 57.021  91.534  1.00 19.23 ? 1089 GLY   A CA    1 
ATOM   8069  C  C     . GLY   A 1  1091 ? -23.251 58.152  91.743  1.00 17.88 ? 1089 GLY   A C     1 
ATOM   8070  O  O     . GLY   A 1  1091 ? -23.267 59.125  90.985  1.00 17.75 ? 1089 GLY   A O     1 
ATOM   8071  N  N     . GLU   A 1  1092 ? -22.406 58.058  92.759  1.00 18.25 ? 1090 GLU   A N     1 
ATOM   8072  C  CA    . GLU   A 1  1092 ? -21.424 59.091  93.006  1.00 18.69 ? 1090 GLU   A CA    1 
ATOM   8073  C  C     . GLU   A 1  1092 ? -20.212 58.413  93.617  1.00 17.44 ? 1090 GLU   A C     1 
ATOM   8074  O  O     . GLU   A 1  1092 ? -20.334 57.414  94.330  1.00 19.56 ? 1090 GLU   A O     1 
ATOM   8075  C  CB    . GLU   A 1  1092 ? -21.987 60.099  94.008  1.00 22.25 ? 1090 GLU   A CB    1 
ATOM   8076  C  CG    . GLU   A 1  1092 ? -21.453 61.513  93.931  1.00 26.52 ? 1090 GLU   A CG    1 
ATOM   8077  C  CD    . GLU   A 1  1092 ? -22.274 62.439  94.823  1.00 28.22 ? 1090 GLU   A CD    1 
ATOM   8078  O  OE1   . GLU   A 1  1092 ? -22.107 62.354  96.056  1.00 23.67 ? 1090 GLU   A OE1   1 
ATOM   8079  O  OE2   . GLU   A 1  1092 ? -23.115 63.209  94.303  1.00 30.14 ? 1090 GLU   A OE2   1 
ATOM   8080  N  N     . ARG   A 1  1093 ? -19.038 58.931  93.292  1.00 16.15 ? 1091 ARG   A N     1 
ATOM   8081  C  CA    A ARG   A 1  1093 ? -17.796 58.509  93.929  0.50 18.16 ? 1091 ARG   A CA    1 
ATOM   8082  C  CA    B ARG   A 1  1093 ? -17.790 58.511  93.913  0.50 18.17 ? 1091 ARG   A CA    1 
ATOM   8083  C  C     . ARG   A 1  1093 ? -17.218 59.717  94.639  1.00 15.94 ? 1091 ARG   A C     1 
ATOM   8084  O  O     . ARG   A 1  1093 ? -16.993 60.762  94.024  1.00 18.26 ? 1091 ARG   A O     1 
ATOM   8085  C  CB    A ARG   A 1  1093 ? -16.795 57.921  92.932  0.50 21.84 ? 1091 ARG   A CB    1 
ATOM   8086  C  CB    B ARG   A 1  1093 ? -16.812 57.997  92.857  0.50 21.89 ? 1091 ARG   A CB    1 
ATOM   8087  C  CG    A ARG   A 1  1093 ? -17.155 56.525  92.471  0.50 24.15 ? 1091 ARG   A CG    1 
ATOM   8088  C  CG    B ARG   A 1  1093 ? -15.607 57.285  93.416  0.50 23.38 ? 1091 ARG   A CG    1 
ATOM   8089  C  CD    A ARG   A 1  1093 ? -16.015 55.856  91.708  0.50 31.34 ? 1091 ARG   A CD    1 
ATOM   8090  C  CD    B ARG   A 1  1093 ? -14.702 56.778  92.294  0.50 26.59 ? 1091 ARG   A CD    1 
ATOM   8091  N  NE    A ARG   A 1  1093 ? -14.914 55.466  92.580  0.50 29.78 ? 1091 ARG   A NE    1 
ATOM   8092  N  NE    B ARG   A 1  1093 ? -15.440 56.037  91.278  0.50 31.10 ? 1091 ARG   A NE    1 
ATOM   8093  C  CZ    A ARG   A 1  1093 ? -13.670 55.915  92.473  0.50 32.03 ? 1091 ARG   A CZ    1 
ATOM   8094  C  CZ    B ARG   A 1  1093 ? -15.561 56.408  90.010  0.50 31.33 ? 1091 ARG   A CZ    1 
ATOM   8095  N  NH1   A ARG   A 1  1093 ? -13.317 56.757  91.515  0.50 31.56 ? 1091 ARG   A NH1   1 
ATOM   8096  N  NH1   B ARG   A 1  1093 ? -14.982 57.507  89.549  0.50 33.38 ? 1091 ARG   A NH1   1 
ATOM   8097  N  NH2   A ARG   A 1  1093 ? -12.755 55.501  93.346  0.50 32.17 ? 1091 ARG   A NH2   1 
ATOM   8098  N  NH2   B ARG   A 1  1093 ? -16.272 55.652  89.177  0.50 34.83 ? 1091 ARG   A NH2   1 
ATOM   8099  N  N     . ASN   A 1  1094 ? -17.018 59.581  95.939  1.00 17.63 ? 1092 ASN   A N     1 
ATOM   8100  C  CA    . ASN   A 1  1094 ? -16.575 60.694  96.747  1.00 15.91 ? 1092 ASN   A CA    1 
ATOM   8101  C  C     . ASN   A 1  1094 ? -15.220 60.333  97.317  1.00 16.62 ? 1092 ASN   A C     1 
ATOM   8102  O  O     . ASN   A 1  1094 ? -15.099 59.365  98.077  1.00 18.35 ? 1092 ASN   A O     1 
ATOM   8103  C  CB    . ASN   A 1  1094 ? -17.617 60.989  97.814  1.00 15.81 ? 1092 ASN   A CB    1 
ATOM   8104  C  CG    . ASN   A 1  1094 ? -18.827 61.663  97.228  1.00 15.89 ? 1092 ASN   A CG    1 
ATOM   8105  O  OD1   . ASN   A 1  1094 ? -18.730 62.799  96.789  1.00 17.34 ? 1092 ASN   A OD1   1 
ATOM   8106  N  ND2   . ASN   A 1  1094 ? -19.967 60.971  97.199  1.00 20.00 ? 1092 ASN   A ND2   1 
ATOM   8107  N  N     . LEU   A 1  1095 ? -14.212 61.086  96.908  1.00 17.17 ? 1093 LEU   A N     1 
ATOM   8108  C  CA    . LEU   A 1  1095 ? -12.824 60.741  97.147  1.00 15.96 ? 1093 LEU   A CA    1 
ATOM   8109  C  C     . LEU   A 1  1095 ? -12.218 61.785  98.059  1.00 18.16 ? 1093 LEU   A C     1 
ATOM   8110  O  O     . LEU   A 1  1095 ? -12.597 62.952  98.034  1.00 17.28 ? 1093 LEU   A O     1 
ATOM   8111  C  CB    . LEU   A 1  1095 ? -12.043 60.722  95.837  1.00 19.08 ? 1093 LEU   A CB    1 
ATOM   8112  C  CG    . LEU   A 1  1095 ? -12.670 59.781  94.807  1.00 22.49 ? 1093 LEU   A CG    1 
ATOM   8113  C  CD1   . LEU   A 1  1095 ? -11.852 59.762  93.529  1.00 28.42 ? 1093 LEU   A CD1   1 
ATOM   8114  C  CD2   . LEU   A 1  1095 ? -12.832 58.372  95.374  1.00 25.55 ? 1093 LEU   A CD2   1 
ATOM   8115  N  N     . TYR   A 1  1096 ? -11.249 61.349  98.848  1.00 17.42 ? 1094 TYR   A N     1 
ATOM   8116  C  CA    . TYR   A 1  1096 ? -10.620 62.216  99.826  1.00 17.07 ? 1094 TYR   A CA    1 
ATOM   8117  C  C     . TYR   A 1  1096 ? -9.149  61.880  99.786  1.00 15.37 ? 1094 TYR   A C     1 
ATOM   8118  O  O     . TYR   A 1  1096 ? -8.779  60.718  99.967  1.00 17.34 ? 1094 TYR   A O     1 
ATOM   8119  C  CB    . TYR   A 1  1096 ? -11.194 61.913  101.204 1.00 16.91 ? 1094 TYR   A CB    1 
ATOM   8120  C  CG    . TYR   A 1  1096 ? -10.499 62.609  102.350 1.00 16.70 ? 1094 TYR   A CG    1 
ATOM   8121  C  CD1   . TYR   A 1  1096 ? -10.840 63.904  102.718 1.00 17.93 ? 1094 TYR   A CD1   1 
ATOM   8122  C  CD2   . TYR   A 1  1096 ? -9.510  61.962  103.073 1.00 17.12 ? 1094 TYR   A CD2   1 
ATOM   8123  C  CE1   . TYR   A 1  1096 ? -10.209 64.534  103.785 1.00 16.49 ? 1094 TYR   A CE1   1 
ATOM   8124  C  CE2   . TYR   A 1  1096 ? -8.874  62.586  104.137 1.00 19.43 ? 1094 TYR   A CE2   1 
ATOM   8125  C  CZ    . TYR   A 1  1096 ? -9.223  63.871  104.483 1.00 18.23 ? 1094 TYR   A CZ    1 
ATOM   8126  O  OH    . TYR   A 1  1096 ? -8.610  64.488  105.549 1.00 18.34 ? 1094 TYR   A OH    1 
ATOM   8127  N  N     . THR   A 1  1097 ? -8.315  62.885  99.537  1.00 15.74 ? 1095 THR   A N     1 
ATOM   8128  C  CA    . THR   A 1  1097 ? -6.902  62.633  99.316  1.00 16.19 ? 1095 THR   A CA    1 
ATOM   8129  C  C     . THR   A 1  1097 ? -6.095  63.682  100.059 1.00 18.51 ? 1095 THR   A C     1 
ATOM   8130  O  O     . THR   A 1  1097 ? -6.557  64.804  100.274 1.00 17.23 ? 1095 THR   A O     1 
ATOM   8131  C  CB    . THR   A 1  1097 ? -6.559  62.705  97.824  1.00 21.25 ? 1095 THR   A CB    1 
ATOM   8132  O  OG1   . THR   A 1  1097 ? -6.939  63.984  97.315  1.00 24.94 ? 1095 THR   A OG1   1 
ATOM   8133  C  CG2   . THR   A 1  1097 ? -7.308  61.656  97.052  1.00 20.23 ? 1095 THR   A CG2   1 
ATOM   8134  N  N     . LEU   A 1  1098 ? -4.876  63.312  100.447 1.00 17.32 ? 1096 LEU   A N     1 
ATOM   8135  C  CA    . LEU   A 1  1098 ? -3.958  64.237  101.097 1.00 18.10 ? 1096 LEU   A CA    1 
ATOM   8136  C  C     . LEU   A 1  1098 ? -2.797  64.533  100.164 1.00 14.83 ? 1096 LEU   A C     1 
ATOM   8137  O  O     . LEU   A 1  1098 ? -2.083  63.619  99.734  1.00 16.31 ? 1096 LEU   A O     1 
ATOM   8138  C  CB    . LEU   A 1  1098 ? -3.443  63.686  102.426 1.00 15.56 ? 1096 LEU   A CB    1 
ATOM   8139  C  CG    . LEU   A 1  1098 ? -4.546  63.485  103.459 1.00 15.95 ? 1096 LEU   A CG    1 
ATOM   8140  C  CD1   . LEU   A 1  1098 ? -3.918  62.965  104.725 1.00 18.14 ? 1096 LEU   A CD1   1 
ATOM   8141  C  CD2   . LEU   A 1  1098 ? -5.310  64.780  103.718 1.00 17.07 ? 1096 LEU   A CD2   1 
ATOM   8142  N  N     . HIS   A 1  1099 ? -2.593  65.813  99.894  1.00 15.36 ? 1097 HIS   A N     1 
ATOM   8143  C  CA    . HIS   A 1  1099 ? -1.557  66.300  99.001  1.00 15.52 ? 1097 HIS   A CA    1 
ATOM   8144  C  C     . HIS   A 1  1099 ? -0.640  67.230  99.768  1.00 16.70 ? 1097 HIS   A C     1 
ATOM   8145  O  O     . HIS   A 1  1099 ? -0.888  67.582  100.920 1.00 16.78 ? 1097 HIS   A O     1 
ATOM   8146  C  CB    . HIS   A 1  1099 ? -2.184  67.105  97.860  1.00 18.14 ? 1097 HIS   A CB    1 
ATOM   8147  C  CG    . HIS   A 1  1099 ? -3.125  66.314  97.012  1.00 20.11 ? 1097 HIS   A CG    1 
ATOM   8148  N  ND1   . HIS   A 1  1099 ? -2.772  65.822  95.774  1.00 26.31 ? 1097 HIS   A ND1   1 
ATOM   8149  C  CD2   . HIS   A 1  1099 ? -4.400  65.915  97.229  1.00 22.92 ? 1097 HIS   A CD2   1 
ATOM   8150  C  CE1   . HIS   A 1  1099 ? -3.796  65.163  95.259  1.00 24.73 ? 1097 HIS   A CE1   1 
ATOM   8151  N  NE2   . HIS   A 1  1099 ? -4.795  65.205  96.120  1.00 24.69 ? 1097 HIS   A NE2   1 
ATOM   8152  N  N     . ALA   A 1  1100 ? 0.435   67.637  99.108  1.00 16.50 ? 1098 ALA   A N     1 
ATOM   8153  C  CA    . ALA   A 1  1100 ? 1.272   68.674  99.673  1.00 17.28 ? 1098 ALA   A CA    1 
ATOM   8154  C  C     . ALA   A 1  1100 ? 0.499   69.981  99.711  1.00 18.23 ? 1098 ALA   A C     1 
ATOM   8155  O  O     . ALA   A 1  1100 ? -0.409  70.216  98.906  1.00 19.35 ? 1098 ALA   A O     1 
ATOM   8156  C  CB    . ALA   A 1  1100 ? 2.511   68.845  98.803  1.00 18.11 ? 1098 ALA   A CB    1 
ATOM   8157  N  N     . ARG   A 1  1101 ? 0.852   70.829  100.673 1.00 17.92 ? 1099 ARG   A N     1 
ATOM   8158  C  CA    A ARG   A 1  1101 ? 0.245   72.153  100.740 0.55 19.53 ? 1099 ARG   A CA    1 
ATOM   8159  C  CA    B ARG   A 1  1101 ? 0.249   72.152  100.742 0.45 19.54 ? 1099 ARG   A CA    1 
ATOM   8160  C  C     . ARG   A 1  1101 ? 0.824   73.081  99.684  1.00 19.05 ? 1099 ARG   A C     1 
ATOM   8161  O  O     . ARG   A 1  1101 ? 0.100   73.900  99.116  1.00 20.64 ? 1099 ARG   A O     1 
ATOM   8162  C  CB    A ARG   A 1  1101 ? 0.438   72.760  102.130 0.55 20.30 ? 1099 ARG   A CB    1 
ATOM   8163  C  CB    B ARG   A 1  1101 ? 0.460   72.747  102.131 0.45 20.30 ? 1099 ARG   A CB    1 
ATOM   8164  C  CG    A ARG   A 1  1101 ? -0.297  72.030  103.229 0.55 21.32 ? 1099 ARG   A CG    1 
ATOM   8165  C  CG    B ARG   A 1  1101 ? -0.442  72.161  103.183 0.45 21.49 ? 1099 ARG   A CG    1 
ATOM   8166  C  CD    A ARG   A 1  1101 ? -0.158  72.740  104.564 0.55 20.39 ? 1099 ARG   A CD    1 
ATOM   8167  C  CD    B ARG   A 1  1101 ? -1.151  73.269  103.924 0.45 23.09 ? 1099 ARG   A CD    1 
ATOM   8168  N  NE    A ARG   A 1  1101 ? -1.008  73.917  104.679 0.55 18.76 ? 1099 ARG   A NE    1 
ATOM   8169  N  NE    B ARG   A 1  1101 ? -2.251  72.776  104.740 0.45 21.66 ? 1099 ARG   A NE    1 
ATOM   8170  C  CZ    A ARG   A 1  1101 ? -2.284  73.885  105.048 0.55 21.47 ? 1099 ARG   A CZ    1 
ATOM   8171  C  CZ    B ARG   A 1  1101 ? -3.019  73.553  105.490 0.45 22.42 ? 1099 ARG   A CZ    1 
ATOM   8172  N  NH1   A ARG   A 1  1101 ? -2.887  72.746  105.350 0.55 22.64 ? 1099 ARG   A NH1   1 
ATOM   8173  N  NH1   B ARG   A 1  1101 ? -2.835  74.863  105.544 0.45 22.07 ? 1099 ARG   A NH1   1 
ATOM   8174  N  NH2   A ARG   A 1  1101 ? -2.969  75.023  105.113 0.55 23.41 ? 1099 ARG   A NH2   1 
ATOM   8175  N  NH2   B ARG   A 1  1101 ? -3.993  73.003  106.207 0.45 19.46 ? 1099 ARG   A NH2   1 
ATOM   8176  N  N     . GLY   A 1  1102 ? 2.116   72.965  99.416  1.00 19.68 ? 1100 GLY   A N     1 
ATOM   8177  C  CA    . GLY   A 1  1102 ? 2.749   73.860  98.472  1.00 20.67 ? 1100 GLY   A CA    1 
ATOM   8178  C  C     . GLY   A 1  1102 ? 4.109   74.272  98.974  1.00 17.36 ? 1100 GLY   A C     1 
ATOM   8179  O  O     . GLY   A 1  1102 ? 4.932   73.410  99.298  1.00 20.18 ? 1100 GLY   A O     1 
ATOM   8180  N  N     . ARG   A 1  1103 ? 4.373   75.569  99.054  1.00 18.49 ? 1101 ARG   A N     1 
ATOM   8181  C  CA    . ARG   A 1  1103 ? 5.662   76.043  99.536  1.00 18.08 ? 1101 ARG   A CA    1 
ATOM   8182  C  C     . ARG   A 1  1103 ? 5.490   76.515  100.971 1.00 18.29 ? 1101 ARG   A C     1 
ATOM   8183  O  O     . ARG   A 1  1103 ? 4.673   77.405  101.248 1.00 19.83 ? 1101 ARG   A O     1 
ATOM   8184  C  CB    . ARG   A 1  1103 ? 6.249   77.155  98.663  1.00 20.78 ? 1101 ARG   A CB    1 
ATOM   8185  C  CG    . ARG   A 1  1103 ? 7.696   77.485  99.063  1.00 23.19 ? 1101 ARG   A CG    1 
ATOM   8186  C  CD    . ARG   A 1  1103 ? 8.429   78.333  98.031  1.00 26.10 ? 1101 ARG   A CD    1 
ATOM   8187  N  NE    . ARG   A 1  1103 ? 8.489   77.691  96.721  1.00 30.80 ? 1101 ARG   A NE    1 
ATOM   8188  C  CZ    . ARG   A 1  1103 ? 9.516   76.995  96.239  1.00 35.25 ? 1101 ARG   A CZ    1 
ATOM   8189  N  NH1   . ARG   A 1  1103 ? 10.617  76.768  96.955  1.00 27.16 ? 1101 ARG   A NH1   1 
ATOM   8190  N  NH2   . ARG   A 1  1103 ? 9.436   76.506  95.004  1.00 35.55 ? 1101 ARG   A NH2   1 
ATOM   8191  N  N     . ILE   A 1  1104 ? 6.237   75.900  101.880 1.00 16.67 ? 1102 ILE   A N     1 
ATOM   8192  C  CA    . ILE   A 1  1104 ? 6.170   76.221  103.299 1.00 16.37 ? 1102 ILE   A CA    1 
ATOM   8193  C  C     . ILE   A 1  1104 ? 7.303   77.179  103.612 1.00 17.95 ? 1102 ILE   A C     1 
ATOM   8194  O  O     . ILE   A 1  1104 ? 8.458   76.921  103.251 1.00 18.96 ? 1102 ILE   A O     1 
ATOM   8195  C  CB    . ILE   A 1  1104 ? 6.314   74.958  104.163 1.00 17.57 ? 1102 ILE   A CB    1 
ATOM   8196  C  CG1   . ILE   A 1  1104 ? 5.317   73.871  103.740 1.00 18.63 ? 1102 ILE   A CG1   1 
ATOM   8197  C  CG2   . ILE   A 1  1104 ? 6.168   75.314  105.649 1.00 18.45 ? 1102 ILE   A CG2   1 
ATOM   8198  C  CD1   . ILE   A 1  1104 ? 3.875   74.268  103.920 1.00 19.45 ? 1102 ILE   A CD1   1 
ATOM   8199  N  N     . LEU   A 1  1105 ? 6.979   78.277  104.283 1.00 17.91 ? 1103 LEU   A N     1 
ATOM   8200  C  CA    . LEU   A 1  1105 ? 8.000   79.180  104.798 1.00 18.56 ? 1103 LEU   A CA    1 
ATOM   8201  C  C     . LEU   A 1  1105 ? 8.629   78.571  106.043 1.00 18.46 ? 1103 LEU   A C     1 
ATOM   8202  O  O     . LEU   A 1  1105 ? 7.933   78.265  107.012 1.00 18.93 ? 1103 LEU   A O     1 
ATOM   8203  C  CB    . LEU   A 1  1105 ? 7.354   80.517  105.143 1.00 20.33 ? 1103 LEU   A CB    1 
ATOM   8204  C  CG    . LEU   A 1  1105 ? 8.258   81.544  105.825 1.00 20.06 ? 1103 LEU   A CG    1 
ATOM   8205  C  CD1   . LEU   A 1  1105 ? 9.364   82.005  104.875 1.00 22.83 ? 1103 LEU   A CD1   1 
ATOM   8206  C  CD2   . LEU   A 1  1105 ? 7.405   82.716  106.301 1.00 21.29 ? 1103 LEU   A CD2   1 
ATOM   8207  N  N     . LEU   A 1  1106 ? 9.941   78.391  106.022 1.00 16.34 ? 1104 LEU   A N     1 
ATOM   8208  C  CA    . LEU   A 1  1106 ? 10.678  77.896  107.179 1.00 17.56 ? 1104 LEU   A CA    1 
ATOM   8209  C  C     . LEU   A 1  1106 ? 11.427  79.054  107.812 1.00 22.84 ? 1104 LEU   A C     1 
ATOM   8210  O  O     . LEU   A 1  1106 ? 12.194  79.745  107.138 1.00 20.76 ? 1104 LEU   A O     1 
ATOM   8211  C  CB    . LEU   A 1  1106 ? 11.695  76.823  106.786 1.00 18.77 ? 1104 LEU   A CB    1 
ATOM   8212  C  CG    . LEU   A 1  1106 ? 11.177  75.561  106.104 1.00 26.47 ? 1104 LEU   A CG    1 
ATOM   8213  C  CD1   . LEU   A 1  1106 ? 12.212  74.453  106.222 1.00 21.38 ? 1104 LEU   A CD1   1 
ATOM   8214  C  CD2   . LEU   A 1  1106 ? 9.835   75.100  106.633 1.00 23.82 ? 1104 LEU   A CD2   1 
ATOM   8215  N  N     . VAL   A 1  1107 ? 11.215  79.251  109.105 1.00 18.93 ? 1105 VAL   A N     1 
ATOM   8216  C  CA    . VAL   A 1  1107 ? 11.919  80.284  109.850 1.00 19.99 ? 1105 VAL   A CA    1 
ATOM   8217  C  C     . VAL   A 1  1107 ? 12.680  79.571  110.956 1.00 19.72 ? 1105 VAL   A C     1 
ATOM   8218  O  O     . VAL   A 1  1107 ? 12.195  79.472  112.090 1.00 19.61 ? 1105 VAL   A O     1 
ATOM   8219  C  CB    . VAL   A 1  1107 ? 10.948  81.352  110.374 1.00 19.84 ? 1105 VAL   A CB    1 
ATOM   8220  C  CG1   . VAL   A 1  1107 ? 11.718  82.516  110.960 1.00 22.19 ? 1105 VAL   A CG1   1 
ATOM   8221  C  CG2   . VAL   A 1  1107 ? 10.029  81.825  109.224 1.00 21.48 ? 1105 VAL   A CG2   1 
ATOM   8222  N  N     . PRO   A 1  1108 ? 13.853  79.034  110.667 1.00 18.00 ? 1106 PRO   A N     1 
ATOM   8223  C  CA    . PRO   A 1  1108 ? 14.607  78.299  111.679 1.00 18.63 ? 1106 PRO   A CA    1 
ATOM   8224  C  C     . PRO   A 1  1108 ? 15.462  79.246  112.507 1.00 22.09 ? 1106 PRO   A C     1 
ATOM   8225  O  O     . PRO   A 1  1108 ? 15.663  80.413  112.163 1.00 23.49 ? 1106 PRO   A O     1 
ATOM   8226  C  CB    . PRO   A 1  1108 ? 15.510  77.396  110.828 1.00 20.96 ? 1106 PRO   A CB    1 
ATOM   8227  C  CG    . PRO   A 1  1108 ? 15.770  78.216  109.612 1.00 20.59 ? 1106 PRO   A CG    1 
ATOM   8228  C  CD    . PRO   A 1  1108 ? 14.493  78.963  109.341 1.00 21.08 ? 1106 PRO   A CD    1 
ATOM   8229  N  N     . ALA   A 1  1109 ? 15.932  78.720  113.627 1.00 19.96 ? 1107 ALA   A N     1 
ATOM   8230  C  CA    . ALA   A 1  1109 ? 16.902  79.390  114.479 1.00 20.83 ? 1107 ALA   A CA    1 
ATOM   8231  C  C     . ALA   A 1  1109 ? 18.205  78.621  114.615 1.00 24.60 ? 1107 ALA   A C     1 
ATOM   8232  O  O     . ALA   A 1  1109 ? 19.260  79.237  114.800 1.00 25.85 ? 1107 ALA   A O     1 
ATOM   8233  C  CB    . ALA   A 1  1109 ? 16.314  79.614  115.884 1.00 22.90 ? 1107 ALA   A CB    1 
ATOM   8234  N  N     . THR   A 1  1110 ? 18.164  77.296  114.544 1.00 21.60 ? 1108 THR   A N     1 
ATOM   8235  C  CA    . THR   A 1  1110 ? 19.332  76.458  114.732 1.00 22.30 ? 1108 THR   A CA    1 
ATOM   8236  C  C     . THR   A 1  1110 ? 19.417  75.470  113.580 1.00 20.42 ? 1108 THR   A C     1 
ATOM   8237  O  O     . THR   A 1  1110 ? 18.431  75.190  112.893 1.00 20.67 ? 1108 THR   A O     1 
ATOM   8238  C  CB    . THR   A 1  1110 ? 19.277  75.671  116.051 1.00 23.33 ? 1108 THR   A CB    1 
ATOM   8239  O  OG1   . THR   A 1  1110 ? 18.163  74.767  116.025 1.00 22.22 ? 1108 THR   A OG1   1 
ATOM   8240  C  CG2   . THR   A 1  1110 ? 19.125  76.611  117.243 1.00 23.57 ? 1108 THR   A CG2   1 
ATOM   8241  N  N     . GLU   A 1  1111 ? 20.617  74.934  113.382 1.00 23.19 ? 1109 GLU   A N     1 
ATOM   8242  C  CA    . GLU   A 1  1111 ? 20.804  73.949  112.324 1.00 21.86 ? 1109 GLU   A CA    1 
ATOM   8243  C  C     . GLU   A 1  1111 ? 19.914  72.732  112.542 1.00 23.62 ? 1109 GLU   A C     1 
ATOM   8244  O  O     . GLU   A 1  1111 ? 19.241  72.272  111.611 1.00 21.67 ? 1109 GLU   A O     1 
ATOM   8245  C  CB    . GLU   A 1  1111 ? 22.271  73.549  112.248 1.00 23.58 ? 1109 GLU   A CB    1 
ATOM   8246  C  CG    . GLU   A 1  1111 ? 22.512  72.357  111.352 1.00 24.26 ? 1109 GLU   A CG    1 
ATOM   8247  C  CD    . GLU   A 1  1111 ? 23.986  72.071  111.180 1.00 26.93 ? 1109 GLU   A CD    1 
ATOM   8248  O  OE1   . GLU   A 1  1111 ? 24.656  72.873  110.498 1.00 30.89 ? 1109 GLU   A OE1   1 
ATOM   8249  O  OE2   . GLU   A 1  1111 ? 24.468  71.057  111.723 1.00 30.49 ? 1109 GLU   A OE2   1 
ATOM   8250  N  N     . SER   A 1  1112 ? 19.890  72.200  113.768 1.00 22.65 ? 1110 SER   A N     1 
ATOM   8251  C  CA    . SER   A 1  1112 ? 19.026  71.054  114.041 1.00 20.82 ? 1110 SER   A CA    1 
ATOM   8252  C  C     . SER   A 1  1112 ? 17.564  71.410  113.835 1.00 22.30 ? 1110 SER   A C     1 
ATOM   8253  O  O     . SER   A 1  1112 ? 16.797  70.611  113.288 1.00 21.67 ? 1110 SER   A O     1 
ATOM   8254  C  CB    . SER   A 1  1112 ? 19.248  70.523  115.449 1.00 24.60 ? 1110 SER   A CB    1 
ATOM   8255  O  OG    . SER   A 1  1112 ? 18.478  69.354  115.645 1.00 24.73 ? 1110 SER   A OG    1 
ATOM   8256  N  N     . GLY   A 1  1113 ? 17.157  72.604  114.265 1.00 20.82 ? 1111 GLY   A N     1 
ATOM   8257  C  CA    . GLY   A 1  1113 ? 15.789  73.030  114.015 1.00 18.16 ? 1111 GLY   A CA    1 
ATOM   8258  C  C     . GLY   A 1  1113 ? 15.471  73.094  112.534 1.00 17.97 ? 1111 GLY   A C     1 
ATOM   8259  O  O     . GLY   A 1  1113 ? 14.406  72.644  112.092 1.00 19.31 ? 1111 GLY   A O     1 
ATOM   8260  N  N     . LEU   A 1  1114 ? 16.404  73.622  111.737 1.00 19.46 ? 1112 LEU   A N     1 
ATOM   8261  C  CA    . LEU   A 1  1114 ? 16.197  73.664  110.295 1.00 19.91 ? 1112 LEU   A CA    1 
ATOM   8262  C  C     . LEU   A 1  1114 ? 16.046  72.264  109.721 1.00 20.29 ? 1112 LEU   A C     1 
ATOM   8263  O  O     . LEU   A 1  1114 ? 15.167  72.023  108.884 1.00 18.85 ? 1112 LEU   A O     1 
ATOM   8264  C  CB    . LEU   A 1  1114 ? 17.361  74.385  109.626 1.00 20.57 ? 1112 LEU   A CB    1 
ATOM   8265  C  CG    . LEU   A 1  1114 ? 17.349  74.321  108.102 1.00 21.16 ? 1112 LEU   A CG    1 
ATOM   8266  C  CD1   . LEU   A 1  1114 ? 16.032  74.859  107.522 1.00 21.42 ? 1112 LEU   A CD1   1 
ATOM   8267  C  CD2   . LEU   A 1  1114 ? 18.553  75.057  107.517 1.00 23.21 ? 1112 LEU   A CD2   1 
ATOM   8268  N  N     . TYR   A 1  1115 ? 16.890  71.328  110.158 1.00 20.03 ? 1113 TYR   A N     1 
ATOM   8269  C  CA    . TYR   A 1  1115 ? 16.792  69.971  109.631 1.00 19.28 ? 1113 TYR   A CA    1 
ATOM   8270  C  C     . TYR   A 1  1115 ? 15.448  69.350  109.984 1.00 18.88 ? 1113 TYR   A C     1 
ATOM   8271  O  O     . TYR   A 1  1115 ? 14.835  68.666  109.155 1.00 19.81 ? 1113 TYR   A O     1 
ATOM   8272  C  CB    . TYR   A 1  1115 ? 17.937  69.108  110.159 1.00 17.87 ? 1113 TYR   A CB    1 
ATOM   8273  C  CG    . TYR   A 1  1115 ? 19.304  69.510  109.658 1.00 18.35 ? 1113 TYR   A CG    1 
ATOM   8274  C  CD1   . TYR   A 1  1115 ? 19.455  70.351  108.564 1.00 18.41 ? 1113 TYR   A CD1   1 
ATOM   8275  C  CD2   . TYR   A 1  1115 ? 20.442  69.052  110.294 1.00 21.28 ? 1113 TYR   A CD2   1 
ATOM   8276  C  CE1   . TYR   A 1  1115 ? 20.724  70.708  108.106 1.00 22.65 ? 1113 TYR   A CE1   1 
ATOM   8277  C  CE2   . TYR   A 1  1115 ? 21.700  69.398  109.844 1.00 22.30 ? 1113 TYR   A CE2   1 
ATOM   8278  C  CZ    . TYR   A 1  1115 ? 21.828  70.228  108.753 1.00 24.24 ? 1113 TYR   A CZ    1 
ATOM   8279  O  OH    . TYR   A 1  1115 ? 23.091  70.579  108.314 1.00 24.15 ? 1113 TYR   A OH    1 
ATOM   8280  N  N     . HIS   A 1  1116 ? 14.979  69.569  111.212 1.00 19.57 ? 1114 HIS   A N     1 
ATOM   8281  C  CA    . HIS   A 1  1116 ? 13.665  69.064  111.599 1.00 21.47 ? 1114 HIS   A CA    1 
ATOM   8282  C  C     . HIS   A 1  1116 ? 12.550  69.722  110.796 1.00 18.59 ? 1114 HIS   A C     1 
ATOM   8283  O  O     . HIS   A 1  1116 ? 11.587  69.058  110.394 1.00 18.32 ? 1114 HIS   A O     1 
ATOM   8284  C  CB    . HIS   A 1  1116 ? 13.438  69.277  113.095 1.00 21.75 ? 1114 HIS   A CB    1 
ATOM   8285  C  CG    . HIS   A 1  1116 ? 14.073  68.230  113.952 1.00 22.02 ? 1114 HIS   A CG    1 
ATOM   8286  N  ND1   . HIS   A 1  1116 ? 15.375  68.316  114.399 1.00 25.13 ? 1114 HIS   A ND1   1 
ATOM   8287  C  CD2   . HIS   A 1  1116 ? 13.584  67.066  114.440 1.00 24.69 ? 1114 HIS   A CD2   1 
ATOM   8288  C  CE1   . HIS   A 1  1116 ? 15.655  67.254  115.135 1.00 25.50 ? 1114 HIS   A CE1   1 
ATOM   8289  N  NE2   . HIS   A 1  1116 ? 14.585  66.482  115.176 1.00 28.68 ? 1114 HIS   A NE2   1 
ATOM   8290  N  N     . GLN   A 1  1117 ? 12.635  71.037  110.590 1.00 17.48 ? 1115 GLN   A N     1 
ATOM   8291  C  CA    . GLN   A 1  1117 ? 11.614  71.717  109.806 1.00 16.87 ? 1115 GLN   A CA    1 
ATOM   8292  C  C     . GLN   A 1  1117 ? 11.596  71.194  108.384 1.00 16.58 ? 1115 GLN   A C     1 
ATOM   8293  O  O     . GLN   A 1  1117 ? 10.524  70.942  107.817 1.00 17.36 ? 1115 GLN   A O     1 
ATOM   8294  C  CB    . GLN   A 1  1117 ? 11.880  73.218  109.791 1.00 18.69 ? 1115 GLN   A CB    1 
ATOM   8295  C  CG    . GLN   A 1  1117 ? 11.624  73.904  111.107 1.00 20.23 ? 1115 GLN   A CG    1 
ATOM   8296  C  CD    . GLN   A 1  1117 ? 11.900  75.383  111.011 1.00 21.75 ? 1115 GLN   A CD    1 
ATOM   8297  O  OE1   . GLN   A 1  1117 ? 12.477  75.851  110.031 1.00 20.13 ? 1115 GLN   A OE1   1 
ATOM   8298  N  NE2   . GLN   A 1  1117 ? 11.481  76.131  112.022 1.00 19.71 ? 1115 GLN   A NE2   1 
ATOM   8299  N  N     . LEU   A 1  1118 ? 12.780  71.048  107.785 1.00 16.59 ? 1116 LEU   A N     1 
ATOM   8300  C  CA    A LEU   A 1  1118 ? 12.856  70.550  106.420 0.50 17.21 ? 1116 LEU   A CA    1 
ATOM   8301  C  CA    B LEU   A 1  1118 ? 12.872  70.537  106.421 0.50 17.22 ? 1116 LEU   A CA    1 
ATOM   8302  C  C     . LEU   A 1  1118 ? 12.330  69.123  106.331 1.00 17.51 ? 1116 LEU   A C     1 
ATOM   8303  O  O     . LEU   A 1  1118 ? 11.608  68.783  105.384 1.00 17.51 ? 1116 LEU   A O     1 
ATOM   8304  C  CB    A LEU   A 1  1118 ? 14.297  70.653  105.926 0.50 16.95 ? 1116 LEU   A CB    1 
ATOM   8305  C  CB    B LEU   A 1  1118 ? 14.328  70.550  105.970 0.50 16.99 ? 1116 LEU   A CB    1 
ATOM   8306  C  CG    A LEU   A 1  1118 ? 14.551  70.489  104.433 0.50 17.73 ? 1116 LEU   A CG    1 
ATOM   8307  C  CG    B LEU   A 1  1118 ? 14.867  71.885  105.495 0.50 18.23 ? 1116 LEU   A CG    1 
ATOM   8308  C  CD1   A LEU   A 1  1118 ? 13.578  71.327  103.616 0.50 18.50 ? 1116 LEU   A CD1   1 
ATOM   8309  C  CD1   B LEU   A 1  1118 ? 16.366  71.780  105.378 0.50 18.23 ? 1116 LEU   A CD1   1 
ATOM   8310  C  CD2   A LEU   A 1  1118 ? 15.971  70.908  104.142 0.50 18.43 ? 1116 LEU   A CD2   1 
ATOM   8311  C  CD2   B LEU   A 1  1118 ? 14.251  72.239  104.161 0.50 18.45 ? 1116 LEU   A CD2   1 
ATOM   8312  N  N     . ALA   A 1  1119 ? 12.668  68.280  107.302 1.00 19.23 ? 1117 ALA   A N     1 
ATOM   8313  C  CA    . ALA   A 1  1119 ? 12.151  66.915  107.293 1.00 20.16 ? 1117 ALA   A CA    1 
ATOM   8314  C  C     . ALA   A 1  1119 ? 10.632  66.914  107.321 1.00 19.91 ? 1117 ALA   A C     1 
ATOM   8315  O  O     . ALA   A 1  1119 ? 9.989   66.205  106.539 1.00 19.05 ? 1117 ALA   A O     1 
ATOM   8316  C  CB    . ALA   A 1  1119 ? 12.708  66.118  108.469 1.00 21.30 ? 1117 ALA   A CB    1 
ATOM   8317  N  N     . ALA   A 1  1120 ? 10.034  67.719  108.204 1.00 17.69 ? 1118 ALA   A N     1 
ATOM   8318  C  CA    . ALA   A 1  1120 ? 8.575   67.764  108.292 1.00 16.81 ? 1118 ALA   A CA    1 
ATOM   8319  C  C     . ALA   A 1  1120 ? 7.964   68.220  106.978 1.00 17.45 ? 1118 ALA   A C     1 
ATOM   8320  O  O     . ALA   A 1  1120 ? 6.991   67.631  106.490 1.00 17.59 ? 1118 ALA   A O     1 
ATOM   8321  C  CB    . ALA   A 1  1120 ? 8.148   68.705  109.419 1.00 17.11 ? 1118 ALA   A CB    1 
ATOM   8322  N  N     . ALA   A 1  1121 ? 8.523   69.279  106.394 1.00 17.23 ? 1119 ALA   A N     1 
ATOM   8323  C  CA    . ALA   A 1  1121 ? 7.967   69.837  105.167 1.00 16.38 ? 1119 ALA   A CA    1 
ATOM   8324  C  C     . ALA   A 1  1121 ? 8.151   68.894  103.986 1.00 15.56 ? 1119 ALA   A C     1 
ATOM   8325  O  O     . ALA   A 1  1121 ? 7.231   68.709  103.181 1.00 16.49 ? 1119 ALA   A O     1 
ATOM   8326  C  CB    . ALA   A 1  1121 ? 8.622   71.182  104.870 1.00 18.74 ? 1119 ALA   A CB    1 
ATOM   8327  N  N     . LEU   A 1  1122 ? 9.343   68.316  103.849 1.00 15.98 ? 1120 LEU   A N     1 
ATOM   8328  C  CA    . LEU   A 1  1122 ? 9.587   67.416  102.726 1.00 15.50 ? 1120 LEU   A CA    1 
ATOM   8329  C  C     . LEU   A 1  1122 ? 8.780   66.136  102.857 1.00 17.08 ? 1120 LEU   A C     1 
ATOM   8330  O  O     . LEU   A 1  1122 ? 8.291   65.607  101.856 1.00 16.62 ? 1120 LEU   A O     1 
ATOM   8331  C  CB    . LEU   A 1  1122 ? 11.072  67.079  102.619 1.00 18.81 ? 1120 LEU   A CB    1 
ATOM   8332  C  CG    . LEU   A 1  1122 ? 11.987  68.258  102.302 1.00 16.53 ? 1120 LEU   A CG    1 
ATOM   8333  C  CD1   . LEU   A 1  1122 ? 13.431  67.802  102.330 1.00 20.31 ? 1120 LEU   A CD1   1 
ATOM   8334  C  CD2   . LEU   A 1  1122 ? 11.618  68.877  100.955 1.00 19.02 ? 1120 LEU   A CD2   1 
ATOM   8335  N  N     . ALA   A 1  1123 ? 8.641   65.615  104.078 1.00 16.91 ? 1121 ALA   A N     1 
ATOM   8336  C  CA    . ALA   A 1  1123 ? 7.894   64.377  104.282 1.00 14.84 ? 1121 ALA   A CA    1 
ATOM   8337  C  C     . ALA   A 1  1123 ? 6.447   64.525  103.868 1.00 16.57 ? 1121 ALA   A C     1 
ATOM   8338  O  O     . ALA   A 1  1123 ? 5.802   63.524  103.552 1.00 17.78 ? 1121 ALA   A O     1 
ATOM   8339  C  CB    . ALA   A 1  1123 ? 7.915   63.993  105.761 1.00 16.35 ? 1121 ALA   A CB    1 
ATOM   8340  N  N     . THR   A 1  1124 ? 5.935   65.753  103.865 1.00 14.85 ? 1122 THR   A N     1 
ATOM   8341  C  CA    . THR   A 1  1124 ? 4.564   66.041  103.477 1.00 15.25 ? 1122 THR   A CA    1 
ATOM   8342  C  C     . THR   A 1  1124 ? 4.473   66.592  102.061 1.00 15.47 ? 1122 THR   A C     1 
ATOM   8343  O  O     . THR   A 1  1124 ? 3.433   67.131  101.671 1.00 16.38 ? 1122 THR   A O     1 
ATOM   8344  C  CB    . THR   A 1  1124 ? 3.917   66.967  104.508 1.00 17.14 ? 1122 THR   A CB    1 
ATOM   8345  O  OG1   . THR   A 1  1124 ? 4.819   68.034  104.818 1.00 17.36 ? 1122 THR   A OG1   1 
ATOM   8346  C  CG2   . THR   A 1  1124 ? 3.608   66.191  105.798 1.00 17.74 ? 1122 THR   A CG2   1 
ATOM   8347  N  N     . GLY   A 1  1125 ? 5.551   66.455  101.283 1.00 15.13 ? 1123 GLY   A N     1 
ATOM   8348  C  CA    . GLY   A 1  1125 ? 5.530   66.713  99.855  1.00 16.67 ? 1123 GLY   A CA    1 
ATOM   8349  C  C     . GLY   A 1  1125 ? 5.753   68.149  99.460  1.00 15.84 ? 1123 GLY   A C     1 
ATOM   8350  O  O     . GLY   A 1  1125 ? 5.650   68.475  98.268  1.00 17.29 ? 1123 GLY   A O     1 
ATOM   8351  N  N     . ASN   A 1  1126 ? 6.054   69.019  100.414 1.00 16.58 ? 1124 ASN   A N     1 
ATOM   8352  C  CA    . ASN   A 1  1126 ? 6.131   70.445  100.162 1.00 16.68 ? 1124 ASN   A CA    1 
ATOM   8353  C  C     . ASN   A 1  1126 ? 7.511   70.852  99.685  1.00 16.29 ? 1124 ASN   A C     1 
ATOM   8354  O  O     . ASN   A 1  1126 ? 8.512   70.170  99.925  1.00 18.02 ? 1124 ASN   A O     1 
ATOM   8355  C  CB    . ASN   A 1  1126 ? 5.852   71.200  101.454 1.00 16.90 ? 1124 ASN   A CB    1 
ATOM   8356  C  CG    . ASN   A 1  1126 ? 4.484   70.923  101.973 1.00 17.98 ? 1124 ASN   A CG    1 
ATOM   8357  O  OD1   . ASN   A 1  1126 ? 3.499   71.309  101.364 1.00 18.05 ? 1124 ASN   A OD1   1 
ATOM   8358  N  ND2   . ASN   A 1  1126 ? 4.410   70.224  103.091 1.00 16.64 ? 1124 ASN   A ND2   1 
ATOM   8359  N  N     . SER   A 1  1127 ? 7.548   72.003  99.020  1.00 18.53 ? 1125 SER   A N     1 
ATOM   8360  C  CA    . SER   A 1  1127 ? 8.781   72.751  98.868  1.00 17.94 ? 1125 SER   A CA    1 
ATOM   8361  C  C     . SER   A 1  1127 ? 8.873   73.745  100.015 1.00 18.29 ? 1125 SER   A C     1 
ATOM   8362  O  O     . SER   A 1  1127 ? 7.932   73.927  100.793 1.00 18.09 ? 1125 SER   A O     1 
ATOM   8363  C  CB    . SER   A 1  1127 ? 8.818   73.478  97.524  1.00 19.03 ? 1125 SER   A CB    1 
ATOM   8364  O  OG    . SER   A 1  1127 ? 7.736   74.380  97.407  1.00 25.14 ? 1125 SER   A OG    1 
ATOM   8365  N  N     . VAL   A 1  1128 ? 10.024  74.393  100.131 1.00 19.74 ? 1126 VAL   A N     1 
ATOM   8366  C  CA    . VAL   A 1  1128 ? 10.241  75.309  101.239 1.00 19.15 ? 1126 VAL   A CA    1 
ATOM   8367  C  C     . VAL   A 1  1128 ? 10.920  76.572  100.752 1.00 21.26 ? 1126 VAL   A C     1 
ATOM   8368  O  O     . VAL   A 1  1128 ? 11.681  76.566  99.779  1.00 21.77 ? 1126 VAL   A O     1 
ATOM   8369  C  CB    . VAL   A 1  1128 ? 11.074  74.683  102.375 1.00 18.94 ? 1126 VAL   A CB    1 
ATOM   8370  C  CG1   . VAL   A 1  1128 ? 10.411  73.437  102.895 1.00 22.47 ? 1126 VAL   A CG1   1 
ATOM   8371  C  CG2   . VAL   A 1  1128 ? 12.493  74.387  101.881 1.00 22.10 ? 1126 VAL   A CG2   1 
ATOM   8372  N  N     . ALA   A 1  1129 ? 10.643  77.661  101.454 1.00 18.36 ? 1127 ALA   A N     1 
ATOM   8373  C  CA    . ALA   A 1  1129 ? 11.441  78.872  101.365 1.00 19.43 ? 1127 ALA   A CA    1 
ATOM   8374  C  C     . ALA   A 1  1129 ? 11.998  79.111  102.756 1.00 18.26 ? 1127 ALA   A C     1 
ATOM   8375  O  O     . ALA   A 1  1129 ? 11.231  79.268  103.713 1.00 21.04 ? 1127 ALA   A O     1 
ATOM   8376  C  CB    . ALA   A 1  1129 ? 10.589  80.056  100.918 1.00 23.83 ? 1127 ALA   A CB    1 
ATOM   8377  N  N     . ILE   A 1  1130 ? 13.317  79.107  102.876 1.00 20.10 ? 1128 ILE   A N     1 
ATOM   8378  C  CA    . ILE   A 1  1130 ? 13.970  79.219  104.171 1.00 19.26 ? 1128 ILE   A CA    1 
ATOM   8379  C  C     . ILE   A 1  1130 ? 14.374  80.666  104.381 1.00 23.58 ? 1128 ILE   A C     1 
ATOM   8380  O  O     . ILE   A 1  1130 ? 14.985  81.283  103.504 1.00 23.56 ? 1128 ILE   A O     1 
ATOM   8381  C  CB    . ILE   A 1  1130 ? 15.193  78.295  104.277 1.00 18.15 ? 1128 ILE   A CB    1 
ATOM   8382  C  CG1   . ILE   A 1  1130 ? 14.837  76.877  103.859 1.00 22.09 ? 1128 ILE   A CG1   1 
ATOM   8383  C  CG2   . ILE   A 1  1130 ? 15.730  78.294  105.712 1.00 19.59 ? 1128 ILE   A CG2   1 
ATOM   8384  C  CD1   . ILE   A 1  1130 ? 16.063  76.027  103.675 1.00 20.04 ? 1128 ILE   A CD1   1 
ATOM   8385  N  N     . ASP   A 1  1131 ? 14.039  81.202  105.548 1.00 20.76 ? 1129 ASP   A N     1 
ATOM   8386  C  CA    . ASP   A 1  1131 ? 14.438  82.551  105.920 1.00 21.08 ? 1129 ASP   A CA    1 
ATOM   8387  C  C     . ASP   A 1  1131 ? 15.945  82.728  105.812 1.00 21.66 ? 1129 ASP   A C     1 
ATOM   8388  O  O     . ASP   A 1  1131 ? 16.706  82.112  106.561 1.00 22.12 ? 1129 ASP   A O     1 
ATOM   8389  C  CB    . ASP   A 1  1131 ? 14.005  82.829  107.352 1.00 21.40 ? 1129 ASP   A CB    1 
ATOM   8390  C  CG    . ASP   A 1  1131 ? 14.365  84.218  107.799 1.00 27.37 ? 1129 ASP   A CG    1 
ATOM   8391  O  OD1   . ASP   A 1  1131 ? 14.469  85.108  106.929 1.00 24.36 ? 1129 ASP   A OD1   1 
ATOM   8392  O  OD2   . ASP   A 1  1131 ? 14.553  84.413  109.013 1.00 24.63 ? 1129 ASP   A OD2   1 
ATOM   8393  N  N     . ALA   A 1  1132 ? 16.381  83.573  104.878 1.00 23.68 ? 1130 ALA   A N     1 
ATOM   8394  C  CA    . ALA   A 1  1132 ? 17.805  83.822  104.711 1.00 26.58 ? 1130 ALA   A CA    1 
ATOM   8395  C  C     . ALA   A 1  1132 ? 18.395  84.573  105.894 1.00 29.83 ? 1130 ALA   A C     1 
ATOM   8396  O  O     . ALA   A 1  1132 ? 19.599  84.460  106.147 1.00 27.89 ? 1130 ALA   A O     1 
ATOM   8397  C  CB    . ALA   A 1  1132 ? 18.051  84.584  103.410 1.00 26.96 ? 1130 ALA   A CB    1 
ATOM   8398  N  N     . ALA   A 1  1133 ? 17.575  85.316  106.638 1.00 25.87 ? 1131 ALA   A N     1 
ATOM   8399  C  CA    . ALA   A 1  1133 ? 18.080  86.027  107.806 1.00 29.24 ? 1131 ALA   A CA    1 
ATOM   8400  C  C     . ALA   A 1  1133 ? 18.455  85.092  108.945 1.00 28.30 ? 1131 ALA   A C     1 
ATOM   8401  O  O     . ALA   A 1  1133 ? 19.037  85.546  109.931 1.00 28.83 ? 1131 ALA   A O     1 
ATOM   8402  C  CB    . ALA   A 1  1133 ? 17.065  87.074  108.274 1.00 28.60 ? 1131 ALA   A CB    1 
ATOM   8403  N  N     . SER   A 1  1134 ? 18.146  83.800  108.836 1.00 28.11 ? 1132 SER   A N     1 
ATOM   8404  C  CA    . SER   A 1  1134 ? 18.573  82.844  109.846 1.00 26.08 ? 1132 SER   A CA    1 
ATOM   8405  C  C     . SER   A 1  1134 ? 20.078  82.643  109.838 1.00 25.65 ? 1132 SER   A C     1 
ATOM   8406  O  O     . SER   A 1  1134 ? 20.629  82.154  110.830 1.00 27.33 ? 1132 SER   A O     1 
ATOM   8407  C  CB    . SER   A 1  1134 ? 17.913  81.492  109.584 1.00 25.20 ? 1132 SER   A CB    1 
ATOM   8408  O  OG    . SER   A 1  1134 ? 18.401  80.923  108.378 1.00 24.36 ? 1132 SER   A OG    1 
ATOM   8409  N  N     . GLY   A 1  1135 ? 20.743  82.985  108.735 1.00 28.93 ? 1133 GLY   A N     1 
ATOM   8410  C  CA    . GLY   A 1  1135 ? 22.168  82.761  108.621 1.00 28.03 ? 1133 GLY   A CA    1 
ATOM   8411  C  C     . GLY   A 1  1135 ? 22.575  81.310  108.542 1.00 29.13 ? 1133 GLY   A C     1 
ATOM   8412  O  O     . GLY   A 1  1135 ? 23.749  80.996  108.746 1.00 31.01 ? 1133 GLY   A O     1 
ATOM   8413  N  N     . LEU   A 1  1136 ? 21.641  80.405  108.242 1.00 23.56 ? 1134 LEU   A N     1 
ATOM   8414  C  CA    . LEU   A 1  1136 ? 21.921  78.976  108.286 1.00 24.95 ? 1134 LEU   A CA    1 
ATOM   8415  C  C     . LEU   A 1  1136 ? 22.250  78.391  106.916 1.00 25.44 ? 1134 LEU   A C     1 
ATOM   8416  O  O     . LEU   A 1  1136 ? 22.248  77.166  106.761 1.00 25.56 ? 1134 LEU   A O     1 
ATOM   8417  C  CB    . LEU   A 1  1136 ? 20.758  78.219  108.932 1.00 23.17 ? 1134 LEU   A CB    1 
ATOM   8418  C  CG    . LEU   A 1  1136 ? 20.528  78.493  110.417 1.00 24.71 ? 1134 LEU   A CG    1 
ATOM   8419  C  CD1   . LEU   A 1  1136 ? 19.220  77.831  110.877 1.00 22.31 ? 1134 LEU   A CD1   1 
ATOM   8420  C  CD2   . LEU   A 1  1136 ? 21.715  78.003  111.227 1.00 27.30 ? 1134 LEU   A CD2   1 
ATOM   8421  N  N     . GLN   A 1  1137 ? 22.553  79.242  105.932 1.00 26.13 ? 1135 GLN   A N     1 
ATOM   8422  C  CA    . GLN   A 1  1137 ? 22.873  78.763  104.587 1.00 30.08 ? 1135 GLN   A CA    1 
ATOM   8423  C  C     . GLN   A 1  1137 ? 23.940  77.672  104.602 1.00 27.94 ? 1135 GLN   A C     1 
ATOM   8424  O  O     . GLN   A 1  1137 ? 23.829  76.676  103.874 1.00 27.87 ? 1135 GLN   A O     1 
ATOM   8425  C  CB    . GLN   A 1  1137 ? 23.325  79.927  103.703 1.00 28.18 ? 1135 GLN   A CB    1 
ATOM   8426  C  CG    . GLN   A 1  1137 ? 22.210  80.864  103.259 1.00 26.32 ? 1135 GLN   A CG    1 
ATOM   8427  C  CD    . GLN   A 1  1137 ? 21.879  81.917  104.300 1.00 25.12 ? 1135 GLN   A CD    1 
ATOM   8428  O  OE1   . GLN   A 1  1137 ? 22.343  81.851  105.441 1.00 28.90 ? 1135 GLN   A OE1   1 
ATOM   8429  N  NE2   . GLN   A 1  1137 ? 21.074  82.898  103.909 1.00 30.85 ? 1135 GLN   A NE2   1 
ATOM   8430  N  N     . ALA   A 1  1138 ? 24.982  77.838  105.418 1.00 28.71 ? 1136 ALA   A N     1 
ATOM   8431  C  CA    . ALA   A 1  1138 ? 26.066  76.859  105.440 1.00 26.77 ? 1136 ALA   A CA    1 
ATOM   8432  C  C     . ALA   A 1  1138 ? 25.634  75.497  105.967 1.00 31.59 ? 1136 ALA   A C     1 
ATOM   8433  O  O     . ALA   A 1  1138 ? 26.382  74.528  105.810 1.00 34.93 ? 1136 ALA   A O     1 
ATOM   8434  C  CB    . ALA   A 1  1138 ? 27.258  77.388  106.248 1.00 28.22 ? 1136 ALA   A CB    1 
ATOM   8435  N  N     . SER   A 1  1139 ? 24.451  75.393  106.572 1.00 27.80 ? 1137 SER   A N     1 
ATOM   8436  C  CA    . SER   A 1  1139 ? 23.963  74.111  107.054 1.00 26.87 ? 1137 SER   A CA    1 
ATOM   8437  C  C     . SER   A 1  1139 ? 23.383  73.241  105.948 1.00 25.95 ? 1137 SER   A C     1 
ATOM   8438  O  O     . SER   A 1  1139 ? 23.117  72.062  106.193 1.00 29.12 ? 1137 SER   A O     1 
ATOM   8439  C  CB    . SER   A 1  1139 ? 22.892  74.321  108.134 1.00 27.08 ? 1137 SER   A CB    1 
ATOM   8440  O  OG    . SER   A 1  1139 ? 23.439  74.892  109.307 1.00 30.02 ? 1137 SER   A OG    1 
ATOM   8441  N  N     . LEU   A 1  1140 ? 23.171  73.786  104.756 1.00 25.88 ? 1138 LEU   A N     1 
ATOM   8442  C  CA    . LEU   A 1  1140 ? 22.538  73.061  103.659 1.00 26.15 ? 1138 LEU   A CA    1 
ATOM   8443  C  C     . LEU   A 1  1140 ? 23.441  72.987  102.435 1.00 29.41 ? 1138 LEU   A C     1 
ATOM   8444  O  O     . LEU   A 1  1140 ? 22.983  73.118  101.298 1.00 33.71 ? 1138 LEU   A O     1 
ATOM   8445  C  CB    . LEU   A 1  1140 ? 21.189  73.672  103.286 1.00 26.39 ? 1138 LEU   A CB    1 
ATOM   8446  C  CG    . LEU   A 1  1140 ? 19.982  73.355  104.163 1.00 32.14 ? 1138 LEU   A CG    1 
ATOM   8447  C  CD1   . LEU   A 1  1140 ? 18.733  73.791  103.437 1.00 31.56 ? 1138 LEU   A CD1   1 
ATOM   8448  C  CD2   . LEU   A 1  1140 ? 19.909  71.875  104.513 1.00 26.13 ? 1138 LEU   A CD2   1 
ATOM   8449  N  N     . LYS   A 1  1141 ? 24.734  72.779  102.652 1.00 28.84 ? 1139 LYS   A N     1 
ATOM   8450  C  CA    . LYS   A 1  1141 ? 25.674  72.675  101.546 1.00 33.33 ? 1139 LYS   A CA    1 
ATOM   8451  C  C     . LYS   A 1  1141 ? 25.568  71.308  100.877 1.00 30.34 ? 1139 LYS   A C     1 
ATOM   8452  O  O     . LYS   A 1  1141 ? 25.401  70.283  101.543 1.00 29.55 ? 1139 LYS   A O     1 
ATOM   8453  C  CB    . LYS   A 1  1141 ? 27.103  72.890  102.046 1.00 37.47 ? 1139 LYS   A CB    1 
ATOM   8454  N  N     . ASN   A 1  1142 ? 25.664  71.305  99.548  1.00 30.81 ? 1140 ASN   A N     1 
ATOM   8455  C  CA    . ASN   A 1  1142 ? 25.795  70.076  98.763  1.00 32.53 ? 1140 ASN   A CA    1 
ATOM   8456  C  C     . ASN   A 1  1142 ? 24.531  69.216  98.803  1.00 30.50 ? 1140 ASN   A C     1 
ATOM   8457  O  O     . ASN   A 1  1142 ? 24.607  67.986  98.808  1.00 26.87 ? 1140 ASN   A O     1 
ATOM   8458  C  CB    . ASN   A 1  1142 ? 27.028  69.257  99.164  1.00 36.74 ? 1140 ASN   A CB    1 
ATOM   8459  C  CG    . ASN   A 1  1142 ? 28.291  70.100  99.258  1.00 45.22 ? 1140 ASN   A CG    1 
ATOM   8460  O  OD1   . ASN   A 1  1142 ? 28.897  70.212  100.324 1.00 47.87 ? 1140 ASN   A OD1   1 
ATOM   8461  N  ND2   . ASN   A 1  1142 ? 28.693  70.694  98.140  1.00 41.11 ? 1140 ASN   A ND2   1 
ATOM   8462  N  N     . LEU   A 1  1143 ? 23.362  69.852  98.834  1.00 31.72 ? 1141 LEU   A N     1 
ATOM   8463  C  CA    . LEU   A 1  1143 ? 22.132  69.078  98.807  1.00 27.46 ? 1141 LEU   A CA    1 
ATOM   8464  C  C     . LEU   A 1  1143 ? 22.048  68.268  97.516  1.00 29.37 ? 1141 LEU   A C     1 
ATOM   8465  O  O     . LEU   A 1  1143 ? 22.512  68.710  96.460  1.00 28.96 ? 1141 LEU   A O     1 
ATOM   8466  C  CB    . LEU   A 1  1143 ? 20.910  69.987  98.871  1.00 25.72 ? 1141 LEU   A CB    1 
ATOM   8467  C  CG    . LEU   A 1  1143 ? 20.473  70.518  100.225 1.00 29.95 ? 1141 LEU   A CG    1 
ATOM   8468  C  CD1   . LEU   A 1  1143 ? 19.316  71.468  100.006 1.00 27.30 ? 1141 LEU   A CD1   1 
ATOM   8469  C  CD2   . LEU   A 1  1143 ? 20.084  69.372  101.158 1.00 25.63 ? 1141 LEU   A CD2   1 
ATOM   8470  N  N     . PRO   A 1  1144 ? 21.457  67.078  97.571  1.00 26.75 ? 1142 PRO   A N     1 
ATOM   8471  C  CA    . PRO   A 1  1144 ? 21.083  66.391  96.332  1.00 26.42 ? 1142 PRO   A CA    1 
ATOM   8472  C  C     . PRO   A 1  1144 ? 20.208  67.311  95.497  1.00 27.13 ? 1142 PRO   A C     1 
ATOM   8473  O  O     . PRO   A 1  1144 ? 19.415  68.094  96.028  1.00 24.21 ? 1142 PRO   A O     1 
ATOM   8474  C  CB    . PRO   A 1  1144 ? 20.279  65.182  96.828  1.00 30.76 ? 1142 PRO   A CB    1 
ATOM   8475  C  CG    . PRO   A 1  1144 ? 20.671  65.009  98.265  1.00 32.14 ? 1142 PRO   A CG    1 
ATOM   8476  C  CD    . PRO   A 1  1144 ? 20.991  66.372  98.775  1.00 28.82 ? 1142 PRO   A CD    1 
ATOM   8477  N  N     . GLN   A 1  1145 ? 20.355  67.212  94.174  1.00 26.76 ? 1143 GLN   A N     1 
ATOM   8478  C  CA    . GLN   A 1  1145 ? 19.551  68.043  93.284  1.00 26.81 ? 1143 GLN   A CA    1 
ATOM   8479  C  C     . GLN   A 1  1145 ? 18.055  67.882  93.535  1.00 24.39 ? 1143 GLN   A C     1 
ATOM   8480  O  O     . GLN   A 1  1145 ? 17.306  68.857  93.409  1.00 24.93 ? 1143 GLN   A O     1 
ATOM   8481  C  CB    . GLN   A 1  1145 ? 19.886  67.740  91.822  1.00 32.56 ? 1143 GLN   A CB    1 
ATOM   8482  N  N     . THR   A 1  1146 ? 17.596  66.672  93.879  1.00 26.04 ? 1144 THR   A N     1 
ATOM   8483  C  CA    . THR   A 1  1146 ? 16.169  66.481  94.138  1.00 28.03 ? 1144 THR   A CA    1 
ATOM   8484  C  C     . THR   A 1  1146 ? 15.699  67.344  95.299  1.00 22.74 ? 1144 THR   A C     1 
ATOM   8485  O  O     . THR   A 1  1146 ? 14.592  67.896  95.266  1.00 24.24 ? 1144 THR   A O     1 
ATOM   8486  C  CB    . THR   A 1  1146 ? 15.871  65.018  94.450  1.00 27.99 ? 1144 THR   A CB    1 
ATOM   8487  O  OG1   . THR   A 1  1146 ? 16.770  64.552  95.465  1.00 27.40 ? 1144 THR   A OG1   1 
ATOM   8488  C  CG2   . THR   A 1  1146 ? 15.995  64.162  93.204  1.00 24.61 ? 1144 THR   A CG2   1 
ATOM   8489  N  N     . VAL   A 1  1147 ? 16.520  67.458  96.339  1.00 22.87 ? 1145 VAL   A N     1 
ATOM   8490  C  CA    . VAL   A 1  1147 ? 16.159  68.293  97.477  1.00 22.12 ? 1145 VAL   A CA    1 
ATOM   8491  C  C     . VAL   A 1  1147 ? 16.361  69.761  97.140  1.00 21.71 ? 1145 VAL   A C     1 
ATOM   8492  O  O     . VAL   A 1  1147 ? 15.521  70.604  97.462  1.00 21.65 ? 1145 VAL   A O     1 
ATOM   8493  C  CB    . VAL   A 1  1147 ? 16.948  67.877  98.730  1.00 19.90 ? 1145 VAL   A CB    1 
ATOM   8494  C  CG1   . VAL   A 1  1147 ? 16.468  68.673  99.929  1.00 19.56 ? 1145 VAL   A CG1   1 
ATOM   8495  C  CG2   . VAL   A 1  1147 ? 16.817  66.373  98.990  1.00 22.07 ? 1145 VAL   A CG2   1 
ATOM   8496  N  N     . GLY   A 1  1148 ? 17.463  70.087  96.454  1.00 22.01 ? 1146 GLY   A N     1 
ATOM   8497  C  CA    . GLY   A 1  1148 ? 17.681  71.463  96.045  1.00 21.92 ? 1146 GLY   A CA    1 
ATOM   8498  C  C     . GLY   A 1  1148 ? 16.528  72.036  95.244  1.00 23.74 ? 1146 GLY   A C     1 
ATOM   8499  O  O     . GLY   A 1  1148 ? 16.189  73.213  95.387  1.00 23.60 ? 1146 GLY   A O     1 
ATOM   8500  N  N     . LEU   A 1  1149 ? 15.899  71.210  94.396  1.00 21.69 ? 1147 LEU   A N     1 
ATOM   8501  C  CA    . LEU   A 1  1149 ? 14.756  71.680  93.622  1.00 23.81 ? 1147 LEU   A CA    1 
ATOM   8502  C  C     . LEU   A 1  1149 ? 13.618  72.144  94.518  1.00 22.30 ? 1147 LEU   A C     1 
ATOM   8503  O  O     . LEU   A 1  1149 ? 12.827  73.004  94.117  1.00 26.93 ? 1147 LEU   A O     1 
ATOM   8504  C  CB    . LEU   A 1  1149 ? 14.251  70.582  92.686  1.00 24.77 ? 1147 LEU   A CB    1 
ATOM   8505  C  CG    . LEU   A 1  1149 ? 15.071  70.339  91.419  1.00 33.33 ? 1147 LEU   A CG    1 
ATOM   8506  C  CD1   . LEU   A 1  1149 ? 14.519  69.140  90.669  1.00 35.93 ? 1147 LEU   A CD1   1 
ATOM   8507  C  CD2   . LEU   A 1  1149 ? 15.052  71.586  90.544  1.00 30.86 ? 1147 LEU   A CD2   1 
ATOM   8508  N  N     . ARG   A 1  1150 ? 13.525  71.595  95.729  1.00 20.81 ? 1148 ARG   A N     1 
ATOM   8509  C  CA    . ARG   A 1  1150 ? 12.456  71.949  96.645  1.00 20.50 ? 1148 ARG   A CA    1 
ATOM   8510  C  C     . ARG   A 1  1150 ? 12.836  73.063  97.597  1.00 21.46 ? 1148 ARG   A C     1 
ATOM   8511  O  O     . ARG   A 1  1150 ? 11.977  73.512  98.355  1.00 21.46 ? 1148 ARG   A O     1 
ATOM   8512  C  CB    . ARG   A 1  1150 ? 12.069  70.738  97.483  1.00 21.34 ? 1148 ARG   A CB    1 
ATOM   8513  C  CG    . ARG   A 1  1150 ? 11.370  69.672  96.701  1.00 24.35 ? 1148 ARG   A CG    1 
ATOM   8514  C  CD    . ARG   A 1  1150 ? 10.110  69.292  97.410  1.00 23.40 ? 1148 ARG   A CD    1 
ATOM   8515  N  NE    . ARG   A 1  1150 ? 9.559   68.065  96.866  1.00 22.74 ? 1148 ARG   A NE    1 
ATOM   8516  C  CZ    . ARG   A 1  1150 ? 9.036   67.107  97.611  1.00 22.83 ? 1148 ARG   A CZ    1 
ATOM   8517  N  NH1   . ARG   A 1  1150 ? 8.949   67.232  98.927  1.00 19.36 ? 1148 ARG   A NH1   1 
ATOM   8518  N  NH2   . ARG   A 1  1150 ? 8.602   65.996  97.025  1.00 18.90 ? 1148 ARG   A NH2   1 
ATOM   8519  N  N     . VAL   A 1  1151 ? 14.088  73.504  97.590  1.00 20.48 ? 1149 VAL   A N     1 
ATOM   8520  C  CA    . VAL   A 1  1151 ? 14.607  74.424  98.597  1.00 19.57 ? 1149 VAL   A CA    1 
ATOM   8521  C  C     . VAL   A 1  1151 ? 14.934  75.748  97.923  1.00 25.56 ? 1149 VAL   A C     1 
ATOM   8522  O  O     . VAL   A 1  1151 ? 15.687  75.791  96.944  1.00 27.69 ? 1149 VAL   A O     1 
ATOM   8523  C  CB    . VAL   A 1  1151 ? 15.842  73.843  99.303  1.00 21.67 ? 1149 VAL   A CB    1 
ATOM   8524  C  CG1   . VAL   A 1  1151 ? 16.498  74.897  100.199 1.00 25.17 ? 1149 VAL   A CG1   1 
ATOM   8525  C  CG2   . VAL   A 1  1151 ? 15.456  72.623  100.114 1.00 22.53 ? 1149 VAL   A CG2   1 
ATOM   8526  N  N     . SER   A 1  1152 ? 14.366  76.827  98.441  1.00 22.00 ? 1150 SER   A N     1 
ATOM   8527  C  CA    . SER   A 1  1152 ? 14.790  78.170  98.089  1.00 25.11 ? 1150 SER   A CA    1 
ATOM   8528  C  C     . SER   A 1  1152 ? 15.066  78.920  99.382  1.00 24.78 ? 1150 SER   A C     1 
ATOM   8529  O  O     . SER   A 1  1152 ? 14.591  78.540  100.453 1.00 23.90 ? 1150 SER   A O     1 
ATOM   8530  C  CB    . SER   A 1  1152 ? 13.734  78.913  97.259  1.00 26.95 ? 1150 SER   A CB    1 
ATOM   8531  O  OG    . SER   A 1  1152 ? 12.531  79.095  97.987  1.00 31.31 ? 1150 SER   A OG    1 
ATOM   8532  N  N     . TRP   A 1  1153 ? 15.854  79.980  99.275  1.00 22.67 ? 1151 TRP   A N     1 
ATOM   8533  C  CA    . TRP   A 1  1153 ? 16.141  80.855  100.399 1.00 25.60 ? 1151 TRP   A CA    1 
ATOM   8534  C  C     . TRP   A 1  1153 ? 15.498  82.207  100.140 1.00 27.07 ? 1151 TRP   A C     1 
ATOM   8535  O  O     . TRP   A 1  1153 ? 15.544  82.721  99.016  1.00 31.92 ? 1151 TRP   A O     1 
ATOM   8536  C  CB    . TRP   A 1  1153 ? 17.647  81.015  100.577 1.00 23.80 ? 1151 TRP   A CB    1 
ATOM   8537  C  CG    . TRP   A 1  1153 ? 18.302  79.789  101.102 1.00 24.18 ? 1151 TRP   A CG    1 
ATOM   8538  C  CD1   . TRP   A 1  1153 ? 18.758  78.721  100.377 1.00 26.84 ? 1151 TRP   A CD1   1 
ATOM   8539  C  CD2   . TRP   A 1  1153 ? 18.565  79.488  102.469 1.00 23.90 ? 1151 TRP   A CD2   1 
ATOM   8540  N  NE1   . TRP   A 1  1153 ? 19.300  77.780  101.218 1.00 28.13 ? 1151 TRP   A NE1   1 
ATOM   8541  C  CE2   . TRP   A 1  1153 ? 19.191  78.226  102.509 1.00 24.97 ? 1151 TRP   A CE2   1 
ATOM   8542  C  CE3   . TRP   A 1  1153 ? 18.339  80.167  103.669 1.00 23.17 ? 1151 TRP   A CE3   1 
ATOM   8543  C  CZ2   . TRP   A 1  1153 ? 19.591  77.629  103.705 1.00 23.77 ? 1151 TRP   A CZ2   1 
ATOM   8544  C  CZ3   . TRP   A 1  1153 ? 18.746  79.577  104.856 1.00 26.49 ? 1151 TRP   A CZ3   1 
ATOM   8545  C  CH2   . TRP   A 1  1153 ? 19.364  78.320  104.865 1.00 26.20 ? 1151 TRP   A CH2   1 
ATOM   8546  N  N     . SER   A 1  1154 ? 14.889  82.781  101.175 1.00 24.52 ? 1152 SER   A N     1 
ATOM   8547  C  CA    . SER   A 1  1154 ? 14.084  83.982  101.015 1.00 25.04 ? 1152 SER   A CA    1 
ATOM   8548  C  C     . SER   A 1  1154 ? 14.610  85.074  101.928 1.00 27.03 ? 1152 SER   A C     1 
ATOM   8549  O  O     . SER   A 1  1154 ? 14.618  84.913  103.155 1.00 26.69 ? 1152 SER   A O     1 
ATOM   8550  C  CB    . SER   A 1  1154 ? 12.619  83.703  101.332 1.00 25.49 ? 1152 SER   A CB    1 
ATOM   8551  O  OG    . SER   A 1  1154 ? 11.857  84.889  101.204 1.00 27.27 ? 1152 SER   A OG    1 
ATOM   8552  N  N     . LYS   A 1  1155 ? 15.044  86.183  101.331 1.00 26.81 ? 1153 LYS   A N     1 
ATOM   8553  C  CA    . LYS   A 1  1155 ? 15.368  87.373  102.107 1.00 31.30 ? 1153 LYS   A CA    1 
ATOM   8554  C  C     . LYS   A 1  1155 ? 14.177  88.310  102.249 1.00 33.36 ? 1153 LYS   A C     1 
ATOM   8555  O  O     . LYS   A 1  1155 ? 14.104  89.066  103.224 1.00 46.60 ? 1153 LYS   A O     1 
ATOM   8556  C  CB    . LYS   A 1  1155 ? 16.550  88.120  101.475 1.00 34.72 ? 1153 LYS   A CB    1 
ATOM   8557  N  N     . ASP   A 1  1156 ? 13.240  88.274  101.308 1.00 28.82 ? 1154 ASP   A N     1 
ATOM   8558  C  CA    . ASP   A 1  1156 ? 12.053  89.121  101.331 1.00 28.30 ? 1154 ASP   A CA    1 
ATOM   8559  C  C     . ASP   A 1  1156 ? 10.862  88.176  101.232 1.00 28.25 ? 1154 ASP   A C     1 
ATOM   8560  O  O     . ASP   A 1  1156 ? 10.442  87.800  100.134 1.00 29.04 ? 1154 ASP   A O     1 
ATOM   8561  C  CB    . ASP   A 1  1156 ? 12.082  90.131  100.168 1.00 33.78 ? 1154 ASP   A CB    1 
ATOM   8562  C  CG    . ASP   A 1  1156 ? 10.862  91.045  100.147 1.00 42.73 ? 1154 ASP   A CG    1 
ATOM   8563  O  OD1   . ASP   A 1  1156 ? 9.958   90.881  100.997 1.00 45.24 ? 1154 ASP   A OD1   1 
ATOM   8564  O  OD2   . ASP   A 1  1156 ? 10.808  91.939  99.273  1.00 45.08 ? 1154 ASP   A OD2   1 
ATOM   8565  N  N     . TRP   A 1  1157 ? 10.314  87.796  102.389 1.00 25.98 ? 1155 TRP   A N     1 
ATOM   8566  C  CA    . TRP   A 1  1157 ? 9.263   86.785  102.398 1.00 24.44 ? 1155 TRP   A CA    1 
ATOM   8567  C  C     . TRP   A 1  1157 ? 8.064   87.214  101.568 1.00 25.26 ? 1155 TRP   A C     1 
ATOM   8568  O  O     . TRP   A 1  1157 ? 7.428   86.381  100.918 1.00 25.67 ? 1155 TRP   A O     1 
ATOM   8569  C  CB    . TRP   A 1  1157 ? 8.809   86.499  103.822 1.00 25.72 ? 1155 TRP   A CB    1 
ATOM   8570  C  CG    . TRP   A 1  1157 ? 9.870   86.060  104.761 1.00 24.39 ? 1155 TRP   A CG    1 
ATOM   8571  C  CD1   . TRP   A 1  1157 ? 11.142  85.668  104.466 1.00 23.96 ? 1155 TRP   A CD1   1 
ATOM   8572  C  CD2   . TRP   A 1  1157 ? 9.737   85.967  106.177 1.00 23.51 ? 1155 TRP   A CD2   1 
ATOM   8573  N  NE1   . TRP   A 1  1157 ? 11.812  85.333  105.622 1.00 24.02 ? 1155 TRP   A NE1   1 
ATOM   8574  C  CE2   . TRP   A 1  1157 ? 10.964  85.509  106.685 1.00 24.64 ? 1155 TRP   A CE2   1 
ATOM   8575  C  CE3   . TRP   A 1  1157 ? 8.688   86.227  107.067 1.00 22.98 ? 1155 TRP   A CE3   1 
ATOM   8576  C  CZ2   . TRP   A 1  1157 ? 11.174  85.307  108.047 1.00 24.27 ? 1155 TRP   A CZ2   1 
ATOM   8577  C  CZ3   . TRP   A 1  1157 ? 8.896   86.026  108.415 1.00 24.53 ? 1155 TRP   A CZ3   1 
ATOM   8578  C  CH2   . TRP   A 1  1157 ? 10.130  85.572  108.894 1.00 26.97 ? 1155 TRP   A CH2   1 
ATOM   8579  N  N     . ALA   A 1  1158 ? 7.723   88.504  101.596 1.00 26.23 ? 1156 ALA   A N     1 
ATOM   8580  C  CA    . ALA   A 1  1158 ? 6.553   88.971  100.860 1.00 29.30 ? 1156 ALA   A CA    1 
ATOM   8581  C  C     . ALA   A 1  1158 ? 6.728   88.845  99.354  1.00 31.53 ? 1156 ALA   A C     1 
ATOM   8582  O  O     . ALA   A 1  1158 ? 5.731   88.726  98.631  1.00 39.18 ? 1156 ALA   A O     1 
ATOM   8583  C  CB    . ALA   A 1  1158 ? 6.236   90.417  101.237 1.00 34.20 ? 1156 ALA   A CB    1 
ATOM   8584  N  N     . ALA   A 1  1159 ? 7.968   88.869  98.866  1.00 30.33 ? 1157 ALA   A N     1 
ATOM   8585  C  CA    . ALA   A 1  1159 ? 8.211   88.735  97.436  1.00 31.92 ? 1157 ALA   A CA    1 
ATOM   8586  C  C     . ALA   A 1  1159 ? 8.135   87.290  96.972  1.00 34.70 ? 1157 ALA   A C     1 
ATOM   8587  O  O     . ALA   A 1  1159 ? 7.857   87.037  95.797  1.00 34.11 ? 1157 ALA   A O     1 
ATOM   8588  C  CB    . ALA   A 1  1159 ? 9.589   89.305  97.086  1.00 32.98 ? 1157 ALA   A CB    1 
ATOM   8589  N  N     . ASP   A 1  1160 ? 8.372   86.338  97.868  1.00 31.89 ? 1158 ASP   A N     1 
ATOM   8590  C  CA    . ASP   A 1  1160 ? 8.582   84.949  97.491  1.00 31.87 ? 1158 ASP   A CA    1 
ATOM   8591  C  C     . ASP   A 1  1160 ? 7.373   84.063  97.753  1.00 28.31 ? 1158 ASP   A C     1 
ATOM   8592  O  O     . ASP   A 1  1160 ? 7.459   82.847  97.560  1.00 30.29 ? 1158 ASP   A O     1 
ATOM   8593  C  CB    . ASP   A 1  1160 ? 9.820   84.400  98.196  1.00 28.56 ? 1158 ASP   A CB    1 
ATOM   8594  C  CG    . ASP   A 1  1160 ? 11.079  85.134  97.798  1.00 32.14 ? 1158 ASP   A CG    1 
ATOM   8595  O  OD1   . ASP   A 1  1160 ? 11.080  85.769  96.720  1.00 41.16 ? 1158 ASP   A OD1   1 
ATOM   8596  O  OD2   . ASP   A 1  1160 ? 12.067  85.078  98.557  1.00 31.94 ? 1158 ASP   A OD2   1 
ATOM   8597  N  N     . GLY   A 1  1161 ? 6.254   84.639  98.178  1.00 27.11 ? 1159 GLY   A N     1 
ATOM   8598  C  CA    . GLY   A 1  1161 ? 5.052   83.875  98.388  1.00 29.31 ? 1159 GLY   A CA    1 
ATOM   8599  C  C     . GLY   A 1  1161 ? 4.255   83.723  97.107  1.00 29.29 ? 1159 GLY   A C     1 
ATOM   8600  O  O     . GLY   A 1  1161 ? 4.746   84.007  96.013  1.00 31.98 ? 1159 GLY   A O     1 
ATOM   8601  N  N     . PRO   A 1  1162 ? 3.001   83.267  97.218  1.00 27.34 ? 1160 PRO   A N     1 
ATOM   8602  C  CA    . PRO   A 1  1162 ? 2.289   82.905  98.446  1.00 26.92 ? 1160 PRO   A CA    1 
ATOM   8603  C  C     . PRO   A 1  1162 ? 2.831   81.613  99.035  1.00 26.34 ? 1160 PRO   A C     1 
ATOM   8604  O  O     . PRO   A 1  1162 ? 3.238   80.687  98.334  1.00 26.40 ? 1160 PRO   A O     1 
ATOM   8605  C  CB    . PRO   A 1  1162 ? 0.840   82.736  97.964  1.00 27.40 ? 1160 PRO   A CB    1 
ATOM   8606  C  CG    . PRO   A 1  1162 ? 0.996   82.235  96.558  1.00 28.27 ? 1160 PRO   A CG    1 
ATOM   8607  C  CD    . PRO   A 1  1162 ? 2.178   83.013  96.022  1.00 29.22 ? 1160 PRO   A CD    1 
ATOM   8608  N  N     . PHE   A 1  1163 ? 2.876   81.542  100.352 1.00 22.22 ? 1161 PHE   A N     1 
ATOM   8609  C  CA    . PHE   A 1  1163 ? 3.206   80.300  101.023 1.00 20.03 ? 1161 PHE   A CA    1 
ATOM   8610  C  C     . PHE   A 1  1163 ? 1.915   79.573  101.380 1.00 21.30 ? 1161 PHE   A C     1 
ATOM   8611  O  O     . PHE   A 1  1163 ? 0.814   80.122  101.271 1.00 24.79 ? 1161 PHE   A O     1 
ATOM   8612  C  CB    . PHE   A 1  1163 ? 4.074   80.593  102.248 1.00 20.23 ? 1161 PHE   A CB    1 
ATOM   8613  C  CG    . PHE   A 1  1163 ? 5.320   81.345  101.903 1.00 20.43 ? 1161 PHE   A CG    1 
ATOM   8614  C  CD1   . PHE   A 1  1163 ? 6.289   80.755  101.109 1.00 23.48 ? 1161 PHE   A CD1   1 
ATOM   8615  C  CD2   . PHE   A 1  1163 ? 5.513   82.648  102.330 1.00 21.43 ? 1161 PHE   A CD2   1 
ATOM   8616  C  CE1   . PHE   A 1  1163 ? 7.438   81.445  100.759 1.00 25.60 ? 1161 PHE   A CE1   1 
ATOM   8617  C  CE2   . PHE   A 1  1163 ? 6.669   83.340  101.990 1.00 24.93 ? 1161 PHE   A CE2   1 
ATOM   8618  C  CZ    . PHE   A 1  1163 ? 7.627   82.740  101.204 1.00 22.92 ? 1161 PHE   A CZ    1 
ATOM   8619  N  N     . ALA   A 1  1164 ? 2.053   78.299  101.750 1.00 18.16 ? 1162 ALA   A N     1 
ATOM   8620  C  CA    . ALA   A 1  1164 ? 0.902   77.491  102.132 1.00 20.15 ? 1162 ALA   A CA    1 
ATOM   8621  C  C     . ALA   A 1  1164 ? 0.958   77.075  103.594 1.00 19.31 ? 1162 ALA   A C     1 
ATOM   8622  O  O     . ALA   A 1  1164 ? 0.138   76.264  104.035 1.00 20.97 ? 1162 ALA   A O     1 
ATOM   8623  C  CB    . ALA   A 1  1164 ? 0.760   76.270  101.219 1.00 23.48 ? 1162 ALA   A CB    1 
ATOM   8624  N  N     . GLY   A 1  1165 ? 1.912   77.604  104.346 1.00 18.30 ? 1163 GLY   A N     1 
ATOM   8625  C  CA    . GLY   A 1  1165 ? 2.057   77.312  105.756 1.00 17.07 ? 1163 GLY   A CA    1 
ATOM   8626  C  C     . GLY   A 1  1165 ? 3.423   77.803  106.176 1.00 17.16 ? 1163 GLY   A C     1 
ATOM   8627  O  O     . GLY   A 1  1165 ? 4.214   78.269  105.353 1.00 17.84 ? 1163 GLY   A O     1 
ATOM   8628  N  N     . ALA   A 1  1166 ? 3.694   77.693  107.470 1.00 17.60 ? 1164 ALA   A N     1 
ATOM   8629  C  CA    . ALA   A 1  1166 ? 4.995   78.115  107.961 1.00 17.31 ? 1164 ALA   A CA    1 
ATOM   8630  C  C     . ALA   A 1  1166 ? 5.373   77.264  109.158 1.00 18.43 ? 1164 ALA   A C     1 
ATOM   8631  O  O     . ALA   A 1  1166 ? 4.505   76.800  109.905 1.00 20.65 ? 1164 ALA   A O     1 
ATOM   8632  C  CB    . ALA   A 1  1166 ? 5.012   79.595  108.352 1.00 19.38 ? 1164 ALA   A CB    1 
ATOM   8633  N  N     . LEU   A 1  1167 ? 6.679   77.072  109.324 1.00 17.46 ? 1165 LEU   A N     1 
ATOM   8634  C  CA    . LEU   A 1  1167 ? 7.268   76.427  110.490 1.00 16.79 ? 1165 LEU   A CA    1 
ATOM   8635  C  C     . LEU   A 1  1167 ? 8.270   77.402  111.077 1.00 19.63 ? 1165 LEU   A C     1 
ATOM   8636  O  O     . LEU   A 1  1167 ? 9.140   77.907  110.361 1.00 19.57 ? 1165 LEU   A O     1 
ATOM   8637  C  CB    . LEU   A 1  1167 ? 7.981   75.135  110.105 1.00 19.27 ? 1165 LEU   A CB    1 
ATOM   8638  C  CG    . LEU   A 1  1167 ? 7.076   74.077  109.475 1.00 17.58 ? 1165 LEU   A CG    1 
ATOM   8639  C  CD1   . LEU   A 1  1167 ? 7.921   72.882  109.056 1.00 21.97 ? 1165 LEU   A CD1   1 
ATOM   8640  C  CD2   . LEU   A 1  1167 ? 5.967   73.666  110.439 1.00 20.18 ? 1165 LEU   A CD2   1 
ATOM   8641  N  N     . VAL   A 1  1168 ? 8.153   77.656  112.376 1.00 18.49 ? 1166 VAL   A N     1 
ATOM   8642  C  CA    . VAL   A 1  1168 ? 8.942   78.678  113.051 1.00 18.77 ? 1166 VAL   A CA    1 
ATOM   8643  C  C     . VAL   A 1  1168 ? 9.635   78.041  114.237 1.00 20.82 ? 1166 VAL   A C     1 
ATOM   8644  O  O     . VAL   A 1  1168 ? 9.034   77.247  114.966 1.00 19.55 ? 1166 VAL   A O     1 
ATOM   8645  C  CB    . VAL   A 1  1168 ? 8.057   79.854  113.517 1.00 18.56 ? 1166 VAL   A CB    1 
ATOM   8646  C  CG1   . VAL   A 1  1168 ? 8.912   80.918  114.224 1.00 22.03 ? 1166 VAL   A CG1   1 
ATOM   8647  C  CG2   . VAL   A 1  1168 ? 7.311   80.458  112.322 1.00 19.62 ? 1166 VAL   A CG2   1 
ATOM   8648  N  N     . GLU   A 1  1169 ? 10.902  78.388  114.430 1.00 18.43 ? 1167 GLU   A N     1 
ATOM   8649  C  CA    . GLU   A 1  1169 ? 11.670  77.954  115.585 1.00 19.85 ? 1167 GLU   A CA    1 
ATOM   8650  C  C     . GLU   A 1  1169 ? 12.119  79.192  116.339 1.00 22.34 ? 1167 GLU   A C     1 
ATOM   8651  O  O     . GLU   A 1  1169 ? 12.623  80.142  115.731 1.00 22.58 ? 1167 GLU   A O     1 
ATOM   8652  C  CB    . GLU   A 1  1169 ? 12.893  77.154  115.151 1.00 20.16 ? 1167 GLU   A CB    1 
ATOM   8653  C  CG    . GLU   A 1  1169 ? 13.766  76.697  116.316 1.00 21.21 ? 1167 GLU   A CG    1 
ATOM   8654  C  CD    . GLU   A 1  1169 ? 15.097  76.140  115.851 1.00 20.99 ? 1167 GLU   A CD    1 
ATOM   8655  O  OE1   . GLU   A 1  1169 ? 15.395  76.242  114.635 1.00 20.32 ? 1167 GLU   A OE1   1 
ATOM   8656  O  OE2   . GLU   A 1  1169 ? 15.834  75.604  116.695 1.00 21.82 ? 1167 GLU   A OE2   1 
ATOM   8657  N  N     . GLY   A 1  1170 ? 11.918  79.196  117.645 1.00 20.15 ? 1168 GLY   A N     1 
ATOM   8658  C  CA    . GLY   A 1  1170 ? 12.456  80.284  118.435 1.00 24.68 ? 1168 GLY   A CA    1 
ATOM   8659  C  C     . GLY   A 1  1170 ? 11.855  80.297  119.818 1.00 23.07 ? 1168 GLY   A C     1 
ATOM   8660  O  O     . GLY   A 1  1170 ? 10.940  79.533  120.133 1.00 24.46 ? 1168 GLY   A O     1 
ATOM   8661  N  N     . ASP   A 1  1171 ? 12.380  81.202  120.639 1.00 24.03 ? 1169 ASP   A N     1 
ATOM   8662  C  CA    . ASP   A 1  1171 ? 11.755  81.452  121.926 1.00 23.25 ? 1169 ASP   A CA    1 
ATOM   8663  C  C     . ASP   A 1  1171 ? 10.457  82.235  121.720 1.00 24.50 ? 1169 ASP   A C     1 
ATOM   8664  O  O     . ASP   A 1  1171 ? 10.099  82.619  120.605 1.00 24.58 ? 1169 ASP   A O     1 
ATOM   8665  C  CB    . ASP   A 1  1171 ? 12.753  82.080  122.906 1.00 26.13 ? 1169 ASP   A CB    1 
ATOM   8666  C  CG    . ASP   A 1  1171 ? 13.243  83.462  122.480 1.00 34.40 ? 1169 ASP   A CG    1 
ATOM   8667  O  OD1   . ASP   A 1  1171 ? 12.603  84.125  121.638 1.00 27.63 ? 1169 ASP   A OD1   1 
ATOM   8668  O  OD2   . ASP   A 1  1171 ? 14.285  83.899  123.018 1.00 37.92 ? 1169 ASP   A OD2   1 
ATOM   8669  N  N     . ALA   A 1  1172 ? 9.736   82.470  122.815 1.00 26.34 ? 1170 ALA   A N     1 
ATOM   8670  C  CA    . ALA   A 1  1172 ? 8.391   83.028  122.722 1.00 25.88 ? 1170 ALA   A CA    1 
ATOM   8671  C  C     . ALA   A 1  1172 ? 8.381   84.367  121.994 1.00 24.90 ? 1170 ALA   A C     1 
ATOM   8672  O  O     . ALA   A 1  1172 ? 7.524   84.612  121.137 1.00 25.68 ? 1170 ALA   A O     1 
ATOM   8673  C  CB    . ALA   A 1  1172 ? 7.795   83.176  124.120 1.00 25.80 ? 1170 ALA   A CB    1 
ATOM   8674  N  N     . GLU   A 1  1173 ? 9.326   85.252  122.317 1.00 27.43 ? 1171 GLU   A N     1 
ATOM   8675  C  CA    . GLU   A 1  1173 ? 9.298   86.567  121.683 1.00 29.03 ? 1171 GLU   A CA    1 
ATOM   8676  C  C     . GLU   A 1  1173 ? 9.737   86.505  120.228 1.00 27.94 ? 1171 GLU   A C     1 
ATOM   8677  O  O     . GLU   A 1  1173 ? 9.240   87.280  119.400 1.00 28.08 ? 1171 GLU   A O     1 
ATOM   8678  C  CB    . GLU   A 1  1173 ? 10.099  87.590  122.481 1.00 31.93 ? 1171 GLU   A CB    1 
ATOM   8679  C  CG    . GLU   A 1  1173 ? 9.444   87.938  123.809 1.00 33.80 ? 1171 GLU   A CG    1 
ATOM   8680  C  CD    . GLU   A 1  1173 ? 7.970   88.328  123.666 1.00 37.12 ? 1171 GLU   A CD    1 
ATOM   8681  O  OE1   . GLU   A 1  1173 ? 7.611   89.012  122.679 1.00 36.45 ? 1171 GLU   A OE1   1 
ATOM   8682  O  OE2   . GLU   A 1  1173 ? 7.163   87.948  124.543 1.00 36.66 ? 1171 GLU   A OE2   1 
ATOM   8683  N  N     . ARG   A 1  1174 ? 10.643  85.584  119.892 1.00 23.81 ? 1172 ARG   A N     1 
ATOM   8684  C  CA    . ARG   A 1  1174 ? 10.963  85.363  118.486 1.00 23.04 ? 1172 ARG   A CA    1 
ATOM   8685  C  C     . ARG   A 1  1174 ? 9.742   84.857  117.730 1.00 26.29 ? 1172 ARG   A C     1 
ATOM   8686  O  O     . ARG   A 1  1174 ? 9.445   85.327  116.626 1.00 24.34 ? 1172 ARG   A O     1 
ATOM   8687  C  CB    . ARG   A 1  1174 ? 12.125  84.376  118.366 1.00 24.71 ? 1172 ARG   A CB    1 
ATOM   8688  C  CG    . ARG   A 1  1174 ? 12.449  83.959  116.938 1.00 27.02 ? 1172 ARG   A CG    1 
ATOM   8689  C  CD    . ARG   A 1  1174 ? 12.861  85.147  116.091 1.00 29.52 ? 1172 ARG   A CD    1 
ATOM   8690  N  NE    . ARG   A 1  1174 ? 13.214  84.745  114.734 1.00 25.27 ? 1172 ARG   A NE    1 
ATOM   8691  C  CZ    . ARG   A 1  1174 ? 13.258  85.573  113.701 1.00 26.63 ? 1172 ARG   A CZ    1 
ATOM   8692  N  NH1   . ARG   A 1  1174 ? 12.972  86.859  113.833 1.00 28.94 ? 1172 ARG   A NH1   1 
ATOM   8693  N  NH2   . ARG   A 1  1174 ? 13.581  85.097  112.502 1.00 26.15 ? 1172 ARG   A NH2   1 
ATOM   8694  N  N     . ILE   A 1  1175 ? 9.009   83.911  118.320 1.00 23.11 ? 1173 ILE   A N     1 
ATOM   8695  C  CA    . ILE   A 1  1175 ? 7.793   83.405  117.690 1.00 23.28 ? 1173 ILE   A CA    1 
ATOM   8696  C  C     . ILE   A 1  1175 ? 6.797   84.536  117.477 1.00 22.40 ? 1173 ILE   A C     1 
ATOM   8697  O  O     . ILE   A 1  1175 ? 6.195   84.657  116.404 1.00 24.23 ? 1173 ILE   A O     1 
ATOM   8698  C  CB    . ILE   A 1  1175 ? 7.194   82.257  118.523 1.00 26.49 ? 1173 ILE   A CB    1 
ATOM   8699  C  CG1   . ILE   A 1  1175 ? 8.132   81.048  118.510 1.00 23.32 ? 1173 ILE   A CG1   1 
ATOM   8700  C  CG2   . ILE   A 1  1175 ? 5.778   81.914  118.052 1.00 23.91 ? 1173 ILE   A CG2   1 
ATOM   8701  C  CD1   . ILE   A 1  1175 ? 7.772   79.961  119.510 1.00 25.85 ? 1173 ILE   A CD1   1 
ATOM   8702  N  N     . ARG   A 1  1176 ? 6.632   85.399  118.483 1.00 25.32 ? 1174 ARG   A N     1 
ATOM   8703  C  CA    . ARG   A 1  1176 ? 5.679   86.496  118.364 1.00 24.55 ? 1174 ARG   A CA    1 
ATOM   8704  C  C     . ARG   A 1  1176 ? 6.073   87.434  117.230 1.00 24.17 ? 1174 ARG   A C     1 
ATOM   8705  O  O     . ARG   A 1  1176 ? 5.233   87.824  116.409 1.00 24.43 ? 1174 ARG   A O     1 
ATOM   8706  C  CB    . ARG   A 1  1176 ? 5.576   87.255  119.692 1.00 23.37 ? 1174 ARG   A CB    1 
ATOM   8707  C  CG    . ARG   A 1  1176 ? 4.338   88.135  119.758 1.00 28.77 ? 1174 ARG   A CG    1 
ATOM   8708  C  CD    . ARG   A 1  1176 ? 4.421   89.158  120.879 1.00 30.70 ? 1174 ARG   A CD    1 
ATOM   8709  N  NE    . ARG   A 1  1176 ? 4.721   88.542  122.166 1.00 28.14 ? 1174 ARG   A NE    1 
ATOM   8710  C  CZ    . ARG   A 1  1176 ? 3.807   88.091  123.016 1.00 33.05 ? 1174 ARG   A CZ    1 
ATOM   8711  N  NH1   . ARG   A 1  1176 ? 2.516   88.118  122.723 1.00 31.45 ? 1174 ARG   A NH1   1 
ATOM   8712  N  NH2   . ARG   A 1  1176 ? 4.198   87.610  124.195 1.00 32.67 ? 1174 ARG   A NH2   1 
ATOM   8713  N  N     . ALA   A 1  1177 ? 7.359   87.787  117.160 1.00 25.75 ? 1175 ALA   A N     1 
ATOM   8714  C  CA    . ALA   A 1  1177 ? 7.832   88.683  116.109 1.00 28.62 ? 1175 ALA   A CA    1 
ATOM   8715  C  C     . ALA   A 1  1177 ? 7.644   88.054  114.737 1.00 25.40 ? 1175 ALA   A C     1 
ATOM   8716  O  O     . ALA   A 1  1177 ? 7.163   88.701  113.800 1.00 25.81 ? 1175 ALA   A O     1 
ATOM   8717  C  CB    . ALA   A 1  1177 ? 9.302   89.029  116.340 1.00 27.36 ? 1175 ALA   A CB    1 
ATOM   8718  N  N     . VAL   A 1  1178 ? 8.011   86.781  114.604 1.00 23.44 ? 1176 VAL   A N     1 
ATOM   8719  C  CA    . VAL   A 1  1178 ? 7.844   86.102  113.322 1.00 21.05 ? 1176 VAL   A CA    1 
ATOM   8720  C  C     . VAL   A 1  1178 ? 6.372   86.034  112.940 1.00 23.23 ? 1176 VAL   A C     1 
ATOM   8721  O  O     . VAL   A 1  1178 ? 6.007   86.242  111.774 1.00 23.19 ? 1176 VAL   A O     1 
ATOM   8722  C  CB    . VAL   A 1  1178 ? 8.497   84.709  113.353 1.00 21.16 ? 1176 VAL   A CB    1 
ATOM   8723  C  CG1   . VAL   A 1  1178 ? 8.105   83.943  112.101 1.00 20.33 ? 1176 VAL   A CG1   1 
ATOM   8724  C  CG2   . VAL   A 1  1178 ? 10.002  84.825  113.422 1.00 22.11 ? 1176 VAL   A CG2   1 
ATOM   8725  N  N     . ASN   A 1  1179 ? 5.506   85.736  113.912 1.00 23.06 ? 1177 ASN   A N     1 
ATOM   8726  C  CA    . ASN   A 1  1179 ? 4.076   85.640  113.649 1.00 21.56 ? 1177 ASN   A CA    1 
ATOM   8727  C  C     . ASN   A 1  1179 ? 3.534   86.959  113.118 1.00 23.46 ? 1177 ASN   A C     1 
ATOM   8728  O  O     . ASN   A 1  1179 ? 2.698   86.972  112.212 1.00 24.03 ? 1177 ASN   A O     1 
ATOM   8729  C  CB    . ASN   A 1  1179 ? 3.359   85.253  114.946 1.00 28.26 ? 1177 ASN   A CB    1 
ATOM   8730  C  CG    . ASN   A 1  1179 ? 2.225   84.280  114.730 1.00 34.19 ? 1177 ASN   A CG    1 
ATOM   8731  O  OD1   . ASN   A 1  1179 ? 2.043   83.738  113.635 1.00 37.10 ? 1177 ASN   A OD1   1 
ATOM   8732  N  ND2   . ASN   A 1  1179 ? 1.446   84.048  115.785 1.00 40.46 ? 1177 ASN   A ND2   1 
ATOM   8733  N  N     . LYS   A 1  1180 ? 4.007   88.081  113.667 1.00 22.97 ? 1178 LYS   A N     1 
ATOM   8734  C  CA    . LYS   A 1  1180 ? 3.599   89.383  113.149 1.00 24.75 ? 1178 LYS   A CA    1 
ATOM   8735  C  C     . LYS   A 1  1180 ? 4.112   89.597  111.730 1.00 23.04 ? 1178 LYS   A C     1 
ATOM   8736  O  O     . LYS   A 1  1180 ? 3.374   90.080  110.863 1.00 23.76 ? 1178 LYS   A O     1 
ATOM   8737  C  CB    . LYS   A 1  1180 ? 4.106   90.483  114.081 1.00 28.56 ? 1178 LYS   A CB    1 
ATOM   8738  C  CG    . LYS   A 1  1180 ? 3.447   90.457  115.453 1.00 26.48 ? 1178 LYS   A CG    1 
ATOM   8739  C  CD    . LYS   A 1  1180 ? 4.196   91.331  116.472 1.00 29.76 ? 1178 LYS   A CD    1 
ATOM   8740  C  CE    . LYS   A 1  1180 ? 4.379   92.766  115.975 1.00 39.67 ? 1178 LYS   A CE    1 
ATOM   8741  N  NZ    . LYS   A 1  1180 ? 4.940   93.679  117.021 1.00 42.04 ? 1178 LYS   A NZ    1 
ATOM   8742  N  N     . ALA   A 1  1181 ? 5.369   89.232  111.469 1.00 23.96 ? 1179 ALA   A N     1 
ATOM   8743  C  CA    . ALA   A 1  1181 ? 5.902   89.362  110.116 1.00 23.05 ? 1179 ALA   A CA    1 
ATOM   8744  C  C     . ALA   A 1  1181 ? 5.149   88.472  109.139 1.00 23.62 ? 1179 ALA   A C     1 
ATOM   8745  O  O     . ALA   A 1  1181 ? 4.883   88.875  108.002 1.00 23.37 ? 1179 ALA   A O     1 
ATOM   8746  C  CB    . ALA   A 1  1181 ? 7.392   89.027  110.102 1.00 23.27 ? 1179 ALA   A CB    1 
ATOM   8747  N  N     . ILE   A 1  1182 ? 4.773   87.269  109.571 1.00 21.24 ? 1180 ILE   A N     1 
ATOM   8748  C  CA    . ILE   A 1  1182 ? 4.029   86.375  108.686 1.00 21.67 ? 1180 ILE   A CA    1 
ATOM   8749  C  C     . ILE   A 1  1182 ? 2.638   86.927  108.405 1.00 22.76 ? 1180 ILE   A C     1 
ATOM   8750  O  O     . ILE   A 1  1182 ? 2.159   86.899  107.263 1.00 21.80 ? 1180 ILE   A O     1 
ATOM   8751  C  CB    . ILE   A 1  1182 ? 3.981   84.949  109.262 1.00 22.26 ? 1180 ILE   A CB    1 
ATOM   8752  C  CG1   . ILE   A 1  1182 ? 5.364   84.303  109.185 1.00 22.00 ? 1180 ILE   A CG1   1 
ATOM   8753  C  CG2   . ILE   A 1  1182 ? 2.909   84.118  108.547 1.00 23.16 ? 1180 ILE   A CG2   1 
ATOM   8754  C  CD1   . ILE   A 1  1182 ? 5.449   82.935  109.851 1.00 25.65 ? 1180 ILE   A CD1   1 
ATOM   8755  N  N     . ALA   A 1  1183 ? 1.964   87.436  109.435 1.00 22.72 ? 1181 ALA   A N     1 
ATOM   8756  C  CA    . ALA   A 1  1183 ? 0.633   87.992  109.231 1.00 22.82 ? 1181 ALA   A CA    1 
ATOM   8757  C  C     . ALA   A 1  1183 ? 0.659   89.155  108.248 1.00 24.38 ? 1181 ALA   A C     1 
ATOM   8758  O  O     . ALA   A 1  1183 ? -0.328  89.395  107.541 1.00 23.64 ? 1181 ALA   A O     1 
ATOM   8759  C  CB    . ALA   A 1  1183 ? 0.024   88.410  110.571 1.00 23.87 ? 1181 ALA   A CB    1 
ATOM   8760  N  N     . ALA   A 1  1184 ? 1.784   89.868  108.167 1.00 23.18 ? 1182 ALA   A N     1 
ATOM   8761  C  CA    . ALA   A 1  1184 ? 1.888   91.022  107.283 1.00 24.50 ? 1182 ALA   A CA    1 
ATOM   8762  C  C     . ALA   A 1  1184 ? 2.114   90.631  105.832 1.00 24.77 ? 1182 ALA   A C     1 
ATOM   8763  O  O     . ALA   A 1  1184 ? 2.039   91.500  104.955 1.00 24.26 ? 1182 ALA   A O     1 
ATOM   8764  C  CB    . ALA   A 1  1184 ? 3.018   91.952  107.739 1.00 24.35 ? 1182 ALA   A CB    1 
ATOM   8765  N  N     . LEU   A 1  1185 ? 2.385   89.360  105.560 1.00 22.12 ? 1183 LEU   A N     1 
ATOM   8766  C  CA    . LEU   A 1  1185 ? 2.600   88.949  104.182 1.00 23.19 ? 1183 LEU   A CA    1 
ATOM   8767  C  C     . LEU   A 1  1185 ? 1.301   89.104  103.402 1.00 24.08 ? 1183 LEU   A C     1 
ATOM   8768  O  O     . LEU   A 1  1185 ? 0.218   88.850  103.937 1.00 24.00 ? 1183 LEU   A O     1 
ATOM   8769  C  CB    . LEU   A 1  1185 ? 3.051   87.498  104.125 1.00 19.55 ? 1183 LEU   A CB    1 
ATOM   8770  C  CG    . LEU   A 1  1185 ? 4.359   87.198  104.857 1.00 21.75 ? 1183 LEU   A CG    1 
ATOM   8771  C  CD1   . LEU   A 1  1185 ? 4.673   85.711  104.796 1.00 23.02 ? 1183 LEU   A CD1   1 
ATOM   8772  C  CD2   . LEU   A 1  1185 ? 5.519   88.025  104.300 1.00 22.86 ? 1183 LEU   A CD2   1 
ATOM   8773  N  N     . PRO   A 1  1186 ? 1.369   89.516  102.141 1.00 23.64 ? 1184 PRO   A N     1 
ATOM   8774  C  CA    . PRO   A 1  1186 ? 0.145   89.640  101.349 1.00 22.80 ? 1184 PRO   A CA    1 
ATOM   8775  C  C     . PRO   A 1  1186 ? -0.463  88.277  101.071 1.00 19.82 ? 1184 PRO   A C     1 
ATOM   8776  O  O     . PRO   A 1  1186 ? 0.214   87.247  101.070 1.00 23.51 ? 1184 PRO   A O     1 
ATOM   8777  C  CB    . PRO   A 1  1186 ? 0.634   90.281  100.045 1.00 27.43 ? 1184 PRO   A CB    1 
ATOM   8778  C  CG    . PRO   A 1  1186 ? 2.061   89.849  99.940  1.00 29.94 ? 1184 PRO   A CG    1 
ATOM   8779  C  CD    . PRO   A 1  1186 ? 2.577   89.828  101.360 1.00 26.19 ? 1184 PRO   A CD    1 
ATOM   8780  N  N     . GLY   A 1  1187 ? -1.770  88.283  100.845 1.00 22.36 ? 1185 GLY   A N     1 
ATOM   8781  C  CA    . GLY   A 1  1187 ? -2.440  87.108  100.346 1.00 25.75 ? 1185 GLY   A CA    1 
ATOM   8782  C  C     . GLY   A 1  1187 ? -2.992  86.204  101.429 1.00 20.98 ? 1185 GLY   A C     1 
ATOM   8783  O  O     . GLY   A 1  1187 ? -3.657  86.652  102.369 1.00 23.14 ? 1185 GLY   A O     1 
ATOM   8784  N  N     . PRO   A 1  1188 ? -2.742  84.904  101.302 1.00 21.52 ? 1186 PRO   A N     1 
ATOM   8785  C  CA    . PRO   A 1  1188 ? -3.470  83.936  102.124 1.00 19.51 ? 1186 PRO   A CA    1 
ATOM   8786  C  C     . PRO   A 1  1188 ? -3.004  83.974  103.565 1.00 19.83 ? 1186 PRO   A C     1 
ATOM   8787  O  O     . PRO   A 1  1188 ? -1.856  84.303  103.867 1.00 20.89 ? 1186 PRO   A O     1 
ATOM   8788  C  CB    . PRO   A 1  1188 ? -3.123  82.595  101.474 1.00 23.30 ? 1186 PRO   A CB    1 
ATOM   8789  C  CG    . PRO   A 1  1188 ? -1.754  82.817  100.894 1.00 24.10 ? 1186 PRO   A CG    1 
ATOM   8790  C  CD    . PRO   A 1  1188 ? -1.762  84.258  100.415 1.00 21.30 ? 1186 PRO   A CD    1 
ATOM   8791  N  N     . LEU   A 1  1189 ? -3.922  83.637  104.460 1.00 19.50 ? 1187 LEU   A N     1 
ATOM   8792  C  CA    . LEU   A 1  1189 ? -3.537  83.378  105.837 1.00 19.07 ? 1187 LEU   A CA    1 
ATOM   8793  C  C     . LEU   A 1  1189 ? -2.705  82.105  105.867 1.00 20.88 ? 1187 LEU   A C     1 
ATOM   8794  O  O     . LEU   A 1  1189 ? -2.993  81.139  105.152 1.00 23.66 ? 1187 LEU   A O     1 
ATOM   8795  C  CB    . LEU   A 1  1189 ? -4.786  83.202  106.698 1.00 20.38 ? 1187 LEU   A CB    1 
ATOM   8796  C  CG    . LEU   A 1  1189 ? -5.542  84.460  107.149 1.00 21.52 ? 1187 LEU   A CG    1 
ATOM   8797  C  CD1   . LEU   A 1  1189 ? -6.286  85.122  105.996 1.00 23.09 ? 1187 LEU   A CD1   1 
ATOM   8798  C  CD2   . LEU   A 1  1189 ? -6.509  84.116  108.270 1.00 25.20 ? 1187 LEU   A CD2   1 
ATOM   8799  N  N     . LEU   A 1  1190 ? -1.638  82.115  106.652 1.00 20.79 ? 1188 LEU   A N     1 
ATOM   8800  C  CA    . LEU   A 1  1190 ? -0.751  80.964  106.731 1.00 20.15 ? 1188 LEU   A CA    1 
ATOM   8801  C  C     . LEU   A 1  1190 ? -1.003  80.217  108.026 1.00 19.15 ? 1188 LEU   A C     1 
ATOM   8802  O  O     . LEU   A 1  1190 ? -1.068  80.826  109.096 1.00 22.38 ? 1188 LEU   A O     1 
ATOM   8803  C  CB    . LEU   A 1  1190 ? 0.718   81.383  106.666 1.00 22.66 ? 1188 LEU   A CB    1 
ATOM   8804  C  CG    . LEU   A 1  1190 ? 1.110   82.118  105.385 1.00 22.02 ? 1188 LEU   A CG    1 
ATOM   8805  C  CD1   . LEU   A 1  1190 ? 2.617   82.257  105.367 1.00 27.65 ? 1188 LEU   A CD1   1 
ATOM   8806  C  CD2   . LEU   A 1  1190 ? 0.627   81.361  104.142 1.00 24.33 ? 1188 LEU   A CD2   1 
ATOM   8807  N  N     . LEU   A 1  1191 ? -1.139  78.898  107.923 1.00 19.19 ? 1189 LEU   A N     1 
ATOM   8808  C  CA    . LEU   A 1  1191 ? -1.181  78.052  109.110 1.00 19.63 ? 1189 LEU   A CA    1 
ATOM   8809  C  C     . LEU   A 1  1191 ? 0.250   77.914  109.603 1.00 19.64 ? 1189 LEU   A C     1 
ATOM   8810  O  O     . LEU   A 1  1191 ? 1.062   77.210  108.990 1.00 20.70 ? 1189 LEU   A O     1 
ATOM   8811  C  CB    . LEU   A 1  1191 ? -1.804  76.701  108.768 1.00 18.74 ? 1189 LEU   A CB    1 
ATOM   8812  C  CG    . LEU   A 1  1191 ? -2.343  75.855  109.921 1.00 19.54 ? 1189 LEU   A CG    1 
ATOM   8813  C  CD1   . LEU   A 1  1191 ? -3.176  74.710  109.365 1.00 19.39 ? 1189 LEU   A CD1   1 
ATOM   8814  C  CD2   . LEU   A 1  1191 ? -1.196  75.311  110.785 1.00 19.57 ? 1189 LEU   A CD2   1 
ATOM   8815  N  N     . VAL   A 1  1192 ? 0.550   78.595  110.705 1.00 20.23 ? 1190 VAL   A N     1 
ATOM   8816  C  CA    . VAL   A 1  1192 ? 1.892   78.666  111.264 1.00 20.77 ? 1190 VAL   A CA    1 
ATOM   8817  C  C     . VAL   A 1  1192 ? 1.980   77.684  112.420 1.00 20.08 ? 1190 VAL   A C     1 
ATOM   8818  O  O     . VAL   A 1  1192 ? 1.094   77.646  113.283 1.00 21.42 ? 1190 VAL   A O     1 
ATOM   8819  C  CB    . VAL   A 1  1192 ? 2.194   80.089  111.760 1.00 21.31 ? 1190 VAL   A CB    1 
ATOM   8820  C  CG1   . VAL   A 1  1192 ? 3.596   80.163  112.359 1.00 21.57 ? 1190 VAL   A CG1   1 
ATOM   8821  C  CG2   . VAL   A 1  1192 ? 2.025   81.100  110.636 1.00 23.74 ? 1190 VAL   A CG2   1 
ATOM   8822  N  N     . GLN   A 1  1193 ? 3.052   76.905  112.455 1.00 19.03 ? 1191 GLN   A N     1 
ATOM   8823  C  CA    . GLN   A 1  1193 ? 3.380   76.097  113.619 1.00 18.27 ? 1191 GLN   A CA    1 
ATOM   8824  C  C     . GLN   A 1  1193 ? 4.720   76.564  114.153 1.00 18.28 ? 1191 GLN   A C     1 
ATOM   8825  O  O     . GLN   A 1  1193 ? 5.677   76.722  113.386 1.00 20.08 ? 1191 GLN   A O     1 
ATOM   8826  C  CB    . GLN   A 1  1193 ? 3.484   74.629  113.249 1.00 20.05 ? 1191 GLN   A CB    1 
ATOM   8827  C  CG    . GLN   A 1  1193 ? 2.218   74.064  112.649 1.00 21.12 ? 1191 GLN   A CG    1 
ATOM   8828  C  CD    . GLN   A 1  1193 ? 2.281   72.562  112.586 1.00 19.84 ? 1191 GLN   A CD    1 
ATOM   8829  O  OE1   . GLN   A 1  1193 ? 2.215   71.894  113.613 1.00 21.43 ? 1191 GLN   A OE1   1 
ATOM   8830  N  NE2   . GLN   A 1  1193 ? 2.424   72.021  111.385 1.00 20.77 ? 1191 GLN   A NE2   1 
ATOM   8831  N  N     . ALA   A 1  1194 ? 4.795   76.765  115.461 1.00 18.65 ? 1192 ALA   A N     1 
ATOM   8832  C  CA    . ALA   A 1  1194 ? 6.006   77.262  116.077 1.00 17.96 ? 1192 ALA   A CA    1 
ATOM   8833  C  C     . ALA   A 1  1194 ? 6.441   76.301  117.169 1.00 20.01 ? 1192 ALA   A C     1 
ATOM   8834  O  O     . ALA   A 1  1194 ? 5.616   75.622  117.791 1.00 21.13 ? 1192 ALA   A O     1 
ATOM   8835  C  CB    . ALA   A 1  1194 ? 5.768   78.638  116.691 1.00 20.93 ? 1192 ALA   A CB    1 
ATOM   8836  N  N     . ALA   A 1  1195 ? 7.743   76.274  117.413 1.00 19.59 ? 1193 ALA   A N     1 
ATOM   8837  C  CA    . ALA   A 1  1195 ? 8.299   75.464  118.479 1.00 20.84 ? 1193 ALA   A CA    1 
ATOM   8838  C  C     . ALA   A 1  1195 ? 9.614   76.090  118.905 1.00 19.79 ? 1193 ALA   A C     1 
ATOM   8839  O  O     . ALA   A 1  1195 ? 10.299  76.732  118.103 1.00 21.30 ? 1193 ALA   A O     1 
ATOM   8840  C  CB    . ALA   A 1  1195 ? 8.549   74.032  118.007 1.00 21.33 ? 1193 ALA   A CB    1 
ATOM   8841  N  N     . SER   A 1  1196 ? 9.954   75.914  120.174 1.00 19.56 ? 1194 SER   A N     1 
ATOM   8842  C  CA    . SER   A 1  1196 ? 11.276  76.300  120.631 1.00 21.38 ? 1194 SER   A CA    1 
ATOM   8843  C  C     . SER   A 1  1196 ? 12.293  75.247  120.208 1.00 21.32 ? 1194 SER   A C     1 
ATOM   8844  O  O     . SER   A 1  1196 ? 11.950  74.126  119.833 1.00 21.25 ? 1194 SER   A O     1 
ATOM   8845  C  CB    . SER   A 1  1196 ? 11.289  76.409  122.151 1.00 25.35 ? 1194 SER   A CB    1 
ATOM   8846  O  OG    . SER   A 1  1196 ? 11.099  75.134  122.733 1.00 23.31 ? 1194 SER   A OG    1 
ATOM   8847  N  N     . SER   A 1  1197 ? 13.567  75.618  120.271 1.00 22.34 ? 1195 SER   A N     1 
ATOM   8848  C  CA    . SER   A 1  1197 ? 14.606  74.633  119.996 1.00 20.15 ? 1195 SER   A CA    1 
ATOM   8849  C  C     . SER   A 1  1197 ? 14.511  73.459  120.963 1.00 22.12 ? 1195 SER   A C     1 
ATOM   8850  O  O     . SER   A 1  1197 ? 14.666  72.301  120.560 1.00 23.37 ? 1195 SER   A O     1 
ATOM   8851  C  CB    . SER   A 1  1197 ? 15.978  75.292  120.104 1.00 24.34 ? 1195 SER   A CB    1 
ATOM   8852  O  OG    . SER   A 1  1197 ? 16.108  76.354  119.180 1.00 24.97 ? 1195 SER   A OG    1 
ATOM   8853  N  N     . GLY   A 1  1198 ? 14.252  73.739  122.241 1.00 23.44 ? 1196 GLY   A N     1 
ATOM   8854  C  CA    . GLY   A 1  1198 ? 14.112  72.663  123.212 1.00 24.97 ? 1196 GLY   A CA    1 
ATOM   8855  C  C     . GLY   A 1  1198 ? 12.934  71.756  122.910 1.00 24.94 ? 1196 GLY   A C     1 
ATOM   8856  O  O     . GLY   A 1  1198 ? 13.017  70.535  123.072 1.00 25.32 ? 1196 GLY   A O     1 
ATOM   8857  N  N     . GLU   A 1  1199 ? 11.824  72.341  122.455 1.00 23.13 ? 1197 GLU   A N     1 
ATOM   8858  C  CA    . GLU   A 1  1199 ? 10.664  71.542  122.087 1.00 23.98 ? 1197 GLU   A CA    1 
ATOM   8859  C  C     . GLU   A 1  1199 ? 10.976  70.640  120.902 1.00 23.58 ? 1197 GLU   A C     1 
ATOM   8860  O  O     . GLU   A 1  1199 ? 10.569  69.473  120.872 1.00 23.94 ? 1197 GLU   A O     1 
ATOM   8861  C  CB    . GLU   A 1  1199 ? 9.511   72.489  121.774 1.00 22.97 ? 1197 GLU   A CB    1 
ATOM   8862  C  CG    . GLU   A 1  1199 ? 8.178   71.852  121.534 1.00 28.77 ? 1197 GLU   A CG    1 
ATOM   8863  C  CD    . GLU   A 1  1199 ? 7.108   72.911  121.395 1.00 43.36 ? 1197 GLU   A CD    1 
ATOM   8864  O  OE1   . GLU   A 1  1199 ? 7.445   74.109  121.582 1.00 36.16 ? 1197 GLU   A OE1   1 
ATOM   8865  O  OE2   . GLU   A 1  1199 ? 5.946   72.553  121.104 1.00 46.06 ? 1197 GLU   A OE2   1 
ATOM   8866  N  N     . ILE   A 1  1200 ? 11.697  71.163  119.907 1.00 22.85 ? 1198 ILE   A N     1 
ATOM   8867  C  CA    . ILE   A 1  1200 ? 12.120  70.327  118.789 1.00 23.27 ? 1198 ILE   A CA    1 
ATOM   8868  C  C     . ILE   A 1  1200 ? 12.961  69.160  119.289 1.00 26.33 ? 1198 ILE   A C     1 
ATOM   8869  O  O     . ILE   A 1  1200 ? 12.839  68.033  118.797 1.00 23.76 ? 1198 ILE   A O     1 
ATOM   8870  C  CB    . ILE   A 1  1200 ? 12.867  71.182  117.750 1.00 21.85 ? 1198 ILE   A CB    1 
ATOM   8871  C  CG1   . ILE   A 1  1200 ? 11.899  72.176  117.112 1.00 21.26 ? 1198 ILE   A CG1   1 
ATOM   8872  C  CG2   . ILE   A 1  1200 ? 13.535  70.294  116.690 1.00 23.13 ? 1198 ILE   A CG2   1 
ATOM   8873  C  CD1   . ILE   A 1  1200 ? 12.553  73.189  116.197 1.00 23.47 ? 1198 ILE   A CD1   1 
ATOM   8874  N  N     . ALA   A 1  1201 ? 13.803  69.403  120.295 1.00 22.61 ? 1199 ALA   A N     1 
ATOM   8875  C  CA    . ALA   A 1  1201 ? 14.660  68.335  120.800 1.00 26.30 ? 1199 ALA   A CA    1 
ATOM   8876  C  C     . ALA   A 1  1201 ? 13.859  67.306  121.585 1.00 25.31 ? 1199 ALA   A C     1 
ATOM   8877  O  O     . ALA   A 1  1201 ? 14.169  66.108  121.545 1.00 27.10 ? 1199 ALA   A O     1 
ATOM   8878  C  CB    . ALA   A 1  1201 ? 15.775  68.915  121.673 1.00 26.12 ? 1199 ALA   A CB    1 
ATOM   8879  N  N     . ARG   A 1  1202 ? 12.839  67.750  122.316 1.00 23.00 ? 1200 ARG   A N     1 
ATOM   8880  C  CA    . ARG   A 1  1202 ? 12.111  66.855  123.206 1.00 23.67 ? 1200 ARG   A CA    1 
ATOM   8881  C  C     . ARG   A 1  1202 ? 10.946  66.157  122.526 1.00 26.87 ? 1200 ARG   A C     1 
ATOM   8882  O  O     . ARG   A 1  1202 ? 10.635  65.013  122.874 1.00 29.77 ? 1200 ARG   A O     1 
ATOM   8883  C  CB    . ARG   A 1  1202 ? 11.585  67.620  124.422 1.00 24.30 ? 1200 ARG   A CB    1 
ATOM   8884  C  CG    . ARG   A 1  1202 ? 12.688  68.144  125.336 1.00 23.62 ? 1200 ARG   A CG    1 
ATOM   8885  C  CD    . ARG   A 1  1202 ? 12.120  68.812  126.577 1.00 28.65 ? 1200 ARG   A CD    1 
ATOM   8886  N  NE    . ARG   A 1  1202 ? 11.257  69.924  126.209 1.00 29.04 ? 1200 ARG   A NE    1 
ATOM   8887  C  CZ    . ARG   A 1  1202 ? 11.616  71.202  126.207 1.00 31.04 ? 1200 ARG   A CZ    1 
ATOM   8888  N  NH1   . ARG   A 1  1202 ? 12.793  71.597  126.675 1.00 27.59 ? 1200 ARG   A NH1   1 
ATOM   8889  N  NH2   . ARG   A 1  1202 ? 10.771  72.109  125.717 1.00 30.34 ? 1200 ARG   A NH2   1 
ATOM   8890  N  N     . ASN   A 1  1203 ? 10.298  66.807  121.569 1.00 23.67 ? 1201 ASN   A N     1 
ATOM   8891  C  CA    . ASN   A 1  1203 ? 9.030   66.314  121.040 1.00 22.35 ? 1201 ASN   A CA    1 
ATOM   8892  C  C     . ASN   A 1  1203 ? 9.158   66.024  119.555 1.00 27.73 ? 1201 ASN   A C     1 
ATOM   8893  O  O     . ASN   A 1  1203 ? 9.188   66.967  118.740 1.00 25.84 ? 1201 ASN   A O     1 
ATOM   8894  C  CB    . ASN   A 1  1203 ? 7.923   67.337  121.285 1.00 26.64 ? 1201 ASN   A CB    1 
ATOM   8895  C  CG    . ASN   A 1  1203 ? 6.569   66.859  120.795 1.00 30.74 ? 1201 ASN   A CG    1 
ATOM   8896  O  OD1   . ASN   A 1  1203 ? 6.419   65.714  120.363 1.00 28.58 ? 1201 ASN   A OD1   1 
ATOM   8897  N  ND2   . ASN   A 1  1203 ? 5.571   67.736  120.867 1.00 30.40 ? 1201 ASN   A ND2   1 
ATOM   8898  N  N     . PRO   A 1  1204 ? 9.201   64.754  119.152 1.00 27.89 ? 1202 PRO   A N     1 
ATOM   8899  C  CA    . PRO   A 1  1204 ? 9.247   64.442  117.715 1.00 30.45 ? 1202 PRO   A CA    1 
ATOM   8900  C  C     . PRO   A 1  1204 ? 8.080   65.009  116.930 1.00 28.44 ? 1202 PRO   A C     1 
ATOM   8901  O  O     . PRO   A 1  1204 ? 8.199   65.182  115.713 1.00 27.61 ? 1202 PRO   A O     1 
ATOM   8902  C  CB    . PRO   A 1  1204 ? 9.261   62.908  117.688 1.00 37.66 ? 1202 PRO   A CB    1 
ATOM   8903  C  CG    . PRO   A 1  1204 ? 9.840   62.521  119.009 1.00 35.39 ? 1202 PRO   A CG    1 
ATOM   8904  C  CD    . PRO   A 1  1204 ? 9.295   63.543  119.985 1.00 32.24 ? 1202 PRO   A CD    1 
ATOM   8905  N  N     . ASP   A 1  1205 ? 6.962   65.315  117.587 1.00 29.07 ? 1203 ASP   A N     1 
ATOM   8906  C  CA    . ASP   A 1  1205 ? 5.802   65.902  116.931 1.00 26.85 ? 1203 ASP   A CA    1 
ATOM   8907  C  C     . ASP   A 1  1205 ? 5.685   67.399  117.191 1.00 27.17 ? 1203 ASP   A C     1 
ATOM   8908  O  O     . ASP   A 1  1205 ? 4.581   67.951  117.103 1.00 30.49 ? 1203 ASP   A O     1 
ATOM   8909  C  CB    . ASP   A 1  1205 ? 4.523   65.187  117.373 1.00 30.71 ? 1203 ASP   A CB    1 
ATOM   8910  C  CG    . ASP   A 1  1205 ? 4.558   63.699  117.092 1.00 39.82 ? 1203 ASP   A CG    1 
ATOM   8911  O  OD1   . ASP   A 1  1205 ? 5.256   63.283  116.142 1.00 33.99 ? 1203 ASP   A OD1   1 
ATOM   8912  O  OD2   . ASP   A 1  1205 ? 3.887   62.944  117.829 1.00 41.00 ? 1203 ASP   A OD2   1 
ATOM   8913  N  N     . ALA   A 1  1206 ? 6.798   68.055  117.535 1.00 23.35 ? 1204 ALA   A N     1 
ATOM   8914  C  CA    . ALA   A 1  1206 ? 6.795   69.500  117.744 1.00 25.85 ? 1204 ALA   A CA    1 
ATOM   8915  C  C     . ALA   A 1  1206 ? 6.094   70.214  116.600 1.00 24.15 ? 1204 ALA   A C     1 
ATOM   8916  O  O     . ALA   A 1  1206 ? 5.294   71.131  116.819 1.00 26.89 ? 1204 ALA   A O     1 
ATOM   8917  C  CB    . ALA   A 1  1206 ? 8.234   70.001  117.862 1.00 26.41 ? 1204 ALA   A CB    1 
ATOM   8918  N  N     . TYR   A 1  1207 ? 6.378   69.800  115.372 1.00 23.44 ? 1205 TYR   A N     1 
ATOM   8919  C  CA    . TYR   A 1  1207 ? 5.634   70.243  114.203 1.00 22.43 ? 1205 TYR   A CA    1 
ATOM   8920  C  C     . TYR   A 1  1207 ? 4.732   69.098  113.766 1.00 23.90 ? 1205 TYR   A C     1 
ATOM   8921  O  O     . TYR   A 1  1207 ? 5.214   68.004  113.463 1.00 30.18 ? 1205 TYR   A O     1 
ATOM   8922  C  CB    . TYR   A 1  1207 ? 6.590   70.615  113.075 1.00 21.40 ? 1205 TYR   A CB    1 
ATOM   8923  C  CG    . TYR   A 1  1207 ? 7.518   71.742  113.439 1.00 19.09 ? 1205 TYR   A CG    1 
ATOM   8924  C  CD1   . TYR   A 1  1207 ? 7.014   72.993  113.782 1.00 21.50 ? 1205 TYR   A CD1   1 
ATOM   8925  C  CD2   . TYR   A 1  1207 ? 8.894   71.557  113.453 1.00 20.62 ? 1205 TYR   A CD2   1 
ATOM   8926  C  CE1   . TYR   A 1  1207 ? 7.852   74.030  114.116 1.00 19.90 ? 1205 TYR   A CE1   1 
ATOM   8927  C  CE2   . TYR   A 1  1207 ? 9.744   72.597  113.790 1.00 21.30 ? 1205 TYR   A CE2   1 
ATOM   8928  C  CZ    . TYR   A 1  1207 ? 9.210   73.828  114.116 1.00 20.78 ? 1205 TYR   A CZ    1 
ATOM   8929  O  OH    . TYR   A 1  1207 ? 10.040  74.866  114.447 1.00 21.52 ? 1205 TYR   A OH    1 
ATOM   8930  N  N     . CYS   A 1  1208 ? 3.437   69.348  113.730 1.00 23.54 ? 1206 CYS   A N     1 
ATOM   8931  C  CA    . CYS   A 1  1208 ? 2.479   68.295  113.452 1.00 22.09 ? 1206 CYS   A CA    1 
ATOM   8932  C  C     . CYS   A 1  1208 ? 2.292   68.163  111.947 1.00 20.55 ? 1206 CYS   A C     1 
ATOM   8933  O  O     . CYS   A 1  1208 ? 2.012   69.150  111.258 1.00 20.81 ? 1206 CYS   A O     1 
ATOM   8934  C  CB    . CYS   A 1  1208 ? 1.160   68.630  114.140 1.00 23.64 ? 1206 CYS   A CB    1 
ATOM   8935  S  SG    . CYS   A 1  1208 ? -0.139  67.430  113.842 1.00 28.47 ? 1206 CYS   A SG    1 
ATOM   8936  N  N     . LEU   A 1  1209 ? 2.458   66.942  111.441 1.00 19.51 ? 1207 LEU   A N     1 
ATOM   8937  C  CA    . LEU   A 1  1209 ? 2.351   66.726  110.008 1.00 18.34 ? 1207 LEU   A CA    1 
ATOM   8938  C  C     . LEU   A 1  1209 ? 0.921   66.861  109.497 1.00 20.23 ? 1207 LEU   A C     1 
ATOM   8939  O  O     . LEU   A 1  1209 ? 0.740   67.041  108.291 1.00 20.26 ? 1207 LEU   A O     1 
ATOM   8940  C  CB    . LEU   A 1  1209 ? 2.930   65.364  109.627 1.00 17.99 ? 1207 LEU   A CB    1 
ATOM   8941  C  CG    . LEU   A 1  1209 ? 4.373   65.145  110.074 1.00 19.64 ? 1207 LEU   A CG    1 
ATOM   8942  C  CD1   . LEU   A 1  1209 ? 4.849   63.784  109.606 1.00 22.76 ? 1207 LEU   A CD1   1 
ATOM   8943  C  CD2   . LEU   A 1  1209 ? 5.281   66.239  109.533 1.00 21.33 ? 1207 LEU   A CD2   1 
ATOM   8944  N  N     . ASN   A 1  1210 ? -0.084  66.786  110.380 1.00 20.19 ? 1208 ASN   A N     1 
ATOM   8945  C  CA    . ASN   A 1  1210 ? -1.472  66.963  109.949 1.00 20.27 ? 1208 ASN   A CA    1 
ATOM   8946  C  C     . ASN   A 1  1210 ? -1.654  68.277  109.203 1.00 19.89 ? 1208 ASN   A C     1 
ATOM   8947  O  O     . ASN   A 1  1210 ? -2.445  68.363  108.263 1.00 21.72 ? 1208 ASN   A O     1 
ATOM   8948  C  CB    . ASN   A 1  1210 ? -2.427  66.983  111.152 1.00 23.00 ? 1208 ASN   A CB    1 
ATOM   8949  C  CG    . ASN   A 1  1210 ? -2.549  65.641  111.854 1.00 23.73 ? 1208 ASN   A CG    1 
ATOM   8950  O  OD1   . ASN   A 1  1210 ? -1.774  64.722  111.619 1.00 31.69 ? 1208 ASN   A OD1   1 
ATOM   8951  N  ND2   . ASN   A 1  1210 ? -3.526  65.543  112.753 1.00 32.47 ? 1208 ASN   A ND2   1 
ATOM   8952  N  N     . TRP   A 1  1211 ? -0.952  69.325  109.633 1.00 19.58 ? 1209 TRP   A N     1 
ATOM   8953  C  CA    . TRP   A 1  1211 ? -1.185  70.669  109.122 1.00 19.52 ? 1209 TRP   A CA    1 
ATOM   8954  C  C     . TRP   A 1  1211 ? -0.240  71.039  107.995 1.00 19.79 ? 1209 TRP   A C     1 
ATOM   8955  O  O     . TRP   A 1  1211 ? -0.255  72.187  107.538 1.00 22.69 ? 1209 TRP   A O     1 
ATOM   8956  C  CB    . TRP   A 1  1211 ? -1.096  71.700  110.252 1.00 20.79 ? 1209 TRP   A CB    1 
ATOM   8957  C  CG    . TRP   A 1  1211 ? -1.668  71.196  111.533 1.00 21.26 ? 1209 TRP   A CG    1 
ATOM   8958  C  CD1   . TRP   A 1  1211 ? -1.049  71.166  112.755 1.00 22.15 ? 1209 TRP   A CD1   1 
ATOM   8959  C  CD2   . TRP   A 1  1211 ? -2.962  70.615  111.728 1.00 20.04 ? 1209 TRP   A CD2   1 
ATOM   8960  N  NE1   . TRP   A 1  1211 ? -1.876  70.603  113.686 1.00 23.49 ? 1209 TRP   A NE1   1 
ATOM   8961  C  CE2   . TRP   A 1  1211 ? -3.059  70.261  113.084 1.00 19.80 ? 1209 TRP   A CE2   1 
ATOM   8962  C  CE3   . TRP   A 1  1211 ? -4.046  70.353  110.882 1.00 19.55 ? 1209 TRP   A CE3   1 
ATOM   8963  C  CZ2   . TRP   A 1  1211 ? -4.197  69.662  113.624 1.00 22.94 ? 1209 TRP   A CZ2   1 
ATOM   8964  C  CZ3   . TRP   A 1  1211 ? -5.186  69.761  111.424 1.00 20.81 ? 1209 TRP   A CZ3   1 
ATOM   8965  C  CH2   . TRP   A 1  1211 ? -5.246  69.417  112.778 1.00 20.93 ? 1209 TRP   A CH2   1 
ATOM   8966  N  N     . LEU   A 1  1212 ? 0.577   70.091  107.538 1.00 18.41 ? 1210 LEU   A N     1 
ATOM   8967  C  CA    . LEU   A 1  1212 ? 1.502   70.292  106.436 1.00 18.02 ? 1210 LEU   A CA    1 
ATOM   8968  C  C     . LEU   A 1  1212 ? 1.059   69.569  105.173 1.00 16.31 ? 1210 LEU   A C     1 
ATOM   8969  O  O     . LEU   A 1  1212 ? 1.758   69.624  104.159 1.00 17.18 ? 1210 LEU   A O     1 
ATOM   8970  C  CB    . LEU   A 1  1212 ? 2.905   69.835  106.846 1.00 15.78 ? 1210 LEU   A CB    1 
ATOM   8971  C  CG    . LEU   A 1  1212 ? 3.606   70.798  107.796 1.00 17.50 ? 1210 LEU   A CG    1 
ATOM   8972  C  CD1   . LEU   A 1  1212 ? 4.769   70.114  108.507 1.00 19.70 ? 1210 LEU   A CD1   1 
ATOM   8973  C  CD2   . LEU   A 1  1212 ? 4.073   72.039  107.030 1.00 20.30 ? 1210 LEU   A CD2   1 
ATOM   8974  N  N     . VAL   A 1  1213 ? -0.076  68.882  105.217 1.00 17.18 ? 1211 VAL   A N     1 
ATOM   8975  C  CA    . VAL   A 1  1213 ? -0.718  68.358  104.024 1.00 18.54 ? 1211 VAL   A CA    1 
ATOM   8976  C  C     . VAL   A 1  1213 ? -1.978  69.158  103.765 1.00 17.40 ? 1211 VAL   A C     1 
ATOM   8977  O  O     . VAL   A 1  1213 ? -2.498  69.861  104.634 1.00 19.21 ? 1211 VAL   A O     1 
ATOM   8978  C  CB    . VAL   A 1  1213 ? -1.048  66.854  104.121 1.00 17.36 ? 1211 VAL   A CB    1 
ATOM   8979  C  CG1   . VAL   A 1  1213 ? 0.231   66.029  104.138 1.00 19.13 ? 1211 VAL   A CG1   1 
ATOM   8980  C  CG2   . VAL   A 1  1213 ? -1.876  66.570  105.350 1.00 19.65 ? 1211 VAL   A CG2   1 
ATOM   8981  N  N     . GLU   A 1  1214 ? -2.472  69.033  102.545 1.00 16.96 ? 1212 GLU   A N     1 
ATOM   8982  C  CA    . GLU   A 1  1214 ? -3.677  69.706  102.098 1.00 19.97 ? 1212 GLU   A CA    1 
ATOM   8983  C  C     . GLU   A 1  1214 ? -4.690  68.634  101.746 1.00 18.26 ? 1212 GLU   A C     1 
ATOM   8984  O  O     . GLU   A 1  1214 ? -4.378  67.704  100.998 1.00 17.35 ? 1212 GLU   A O     1 
ATOM   8985  C  CB    . GLU   A 1  1214 ? -3.332  70.491  100.842 1.00 23.94 ? 1212 GLU   A CB    1 
ATOM   8986  C  CG    . GLU   A 1  1214 ? -4.411  71.371  100.302 1.00 34.16 ? 1212 GLU   A CG    1 
ATOM   8987  C  CD    . GLU   A 1  1214 ? -3.860  72.263  99.214  1.00 36.63 ? 1212 GLU   A CD    1 
ATOM   8988  O  OE1   . GLU   A 1  1214 ? -3.141  73.232  99.548  1.00 38.55 ? 1212 GLU   A OE1   1 
ATOM   8989  O  OE2   . GLU   A 1  1214 ? -4.109  71.966  98.030  1.00 42.27 ? 1212 GLU   A OE2   1 
ATOM   8990  N  N     . GLU   A 1  1215 ? -5.887  68.756  102.296 1.00 17.09 ? 1213 GLU   A N     1 
ATOM   8991  C  CA    . GLU   A 1  1215 ? -6.961  67.832  101.979 1.00 16.51 ? 1213 GLU   A CA    1 
ATOM   8992  C  C     . GLU   A 1  1215 ? -7.651  68.263  100.692 1.00 16.49 ? 1213 GLU   A C     1 
ATOM   8993  O  O     . GLU   A 1  1215 ? -7.915  69.449  100.469 1.00 16.88 ? 1213 GLU   A O     1 
ATOM   8994  C  CB    . GLU   A 1  1215 ? -7.998  67.848  103.092 1.00 17.63 ? 1213 GLU   A CB    1 
ATOM   8995  C  CG    . GLU   A 1  1215 ? -7.495  67.416  104.453 1.00 17.45 ? 1213 GLU   A CG    1 
ATOM   8996  C  CD    . GLU   A 1  1215 ? -8.470  67.824  105.530 1.00 18.29 ? 1213 GLU   A CD    1 
ATOM   8997  O  OE1   . GLU   A 1  1215 ? -8.462  69.020  105.893 1.00 18.73 ? 1213 GLU   A OE1   1 
ATOM   8998  O  OE2   . GLU   A 1  1215 ? -9.241  66.956  105.975 1.00 19.90 ? 1213 GLU   A OE2   1 
ATOM   8999  N  N     . VAL   A 1  1216 ? -7.954  67.292  99.846  1.00 15.68 ? 1214 VAL   A N     1 
ATOM   9000  C  CA    . VAL   A 1  1216 ? -8.726  67.546  98.641  1.00 16.43 ? 1214 VAL   A CA    1 
ATOM   9001  C  C     . VAL   A 1  1216 ? -9.867  66.547  98.595  1.00 17.18 ? 1214 VAL   A C     1 
ATOM   9002  O  O     . VAL   A 1  1216 ? -9.659  65.344  98.762  1.00 18.01 ? 1214 VAL   A O     1 
ATOM   9003  C  CB    . VAL   A 1  1216 ? -7.864  67.453  97.375  1.00 17.16 ? 1214 VAL   A CB    1 
ATOM   9004  C  CG1   . VAL   A 1  1216 ? -8.741  67.658  96.152  1.00 18.42 ? 1214 VAL   A CG1   1 
ATOM   9005  C  CG2   . VAL   A 1  1216 ? -6.759  68.492  97.420  1.00 18.67 ? 1214 VAL   A CG2   1 
ATOM   9006  N  N     . SER   A 1  1217 ? -11.070 67.054  98.401  1.00 16.18 ? 1215 SER   A N     1 
ATOM   9007  C  CA    . SER   A 1  1217 ? -12.252 66.232  98.238  1.00 16.49 ? 1215 SER   A CA    1 
ATOM   9008  C  C     . SER   A 1  1217 ? -12.657 66.312  96.780  1.00 15.85 ? 1215 SER   A C     1 
ATOM   9009  O  O     . SER   A 1  1217 ? -12.601 67.384  96.178  1.00 16.56 ? 1215 SER   A O     1 
ATOM   9010  C  CB    . SER   A 1  1217 ? -13.393 66.800  99.077  1.00 16.42 ? 1215 SER   A CB    1 
ATOM   9011  O  OG    . SER   A 1  1217 ? -14.661 66.387  98.590  1.00 19.02 ? 1215 SER   A OG    1 
ATOM   9012  N  N     . ALA   A 1  1218 ? -13.034 65.178  96.212  1.00 15.31 ? 1216 ALA   A N     1 
ATOM   9013  C  CA    . ALA   A 1  1218 ? -13.513 65.152  94.837  1.00 15.18 ? 1216 ALA   A CA    1 
ATOM   9014  C  C     . ALA   A 1  1218 ? -14.788 64.337  94.783  1.00 16.38 ? 1216 ALA   A C     1 
ATOM   9015  O  O     . ALA   A 1  1218 ? -14.814 63.189  95.231  1.00 17.70 ? 1216 ALA   A O     1 
ATOM   9016  C  CB    . ALA   A 1  1218 ? -12.463 64.547  93.899  1.00 16.89 ? 1216 ALA   A CB    1 
ATOM   9017  N  N     . SER   A 1  1219 ? -15.838 64.928  94.222  1.00 15.40 ? 1217 SER   A N     1 
ATOM   9018  C  CA    . SER   A 1  1219 ? -17.125 64.261  94.096  1.00 16.44 ? 1217 SER   A CA    1 
ATOM   9019  C  C     . SER   A 1  1219 ? -17.417 64.088  92.621  1.00 13.86 ? 1217 SER   A C     1 
ATOM   9020  O  O     . SER   A 1  1219 ? -17.544 65.075  91.890  1.00 16.97 ? 1217 SER   A O     1 
ATOM   9021  C  CB    . SER   A 1  1219 ? -18.238 65.078  94.751  1.00 19.36 ? 1217 SER   A CB    1 
ATOM   9022  O  OG    . SER   A 1  1219 ? -19.464 64.363  94.671  1.00 18.21 ? 1217 SER   A OG    1 
ATOM   9023  N  N     . ILE   A 1  1220 ? -17.537 62.840  92.200  1.00 16.02 ? 1218 ILE   A N     1 
ATOM   9024  C  CA    . ILE   A 1  1220 ? -17.718 62.492  90.799  1.00 14.79 ? 1218 ILE   A CA    1 
ATOM   9025  C  C     . ILE   A 1  1220 ? -19.111 61.909  90.638  1.00 16.82 ? 1218 ILE   A C     1 
ATOM   9026  O  O     . ILE   A 1  1220 ? -19.441 60.886  91.247  1.00 16.92 ? 1218 ILE   A O     1 
ATOM   9027  C  CB    . ILE   A 1  1220 ? -16.667 61.467  90.364  1.00 17.87 ? 1218 ILE   A CB    1 
ATOM   9028  C  CG1   . ILE   A 1  1220 ? -15.268 62.035  90.593  1.00 21.68 ? 1218 ILE   A CG1   1 
ATOM   9029  C  CG2   . ILE   A 1  1220 ? -16.882 61.098  88.913  1.00 19.23 ? 1218 ILE   A CG2   1 
ATOM   9030  C  CD1   . ILE   A 1  1220 ? -14.220 60.980  90.818  1.00 32.18 ? 1218 ILE   A CD1   1 
ATOM   9031  N  N     . ASN   A 1  1221 ? -19.922 62.540  89.801  1.00 15.97 ? 1219 ASN   A N     1 
ATOM   9032  C  CA    . ASN   A 1  1221 ? -21.234 61.996  89.465  1.00 16.84 ? 1219 ASN   A CA    1 
ATOM   9033  C  C     . ASN   A 1  1221 ? -21.029 60.869  88.457  1.00 16.95 ? 1219 ASN   A C     1 
ATOM   9034  O  O     . ASN   A 1  1221 ? -20.755 61.124  87.281  1.00 21.43 ? 1219 ASN   A O     1 
ATOM   9035  C  CB    . ASN   A 1  1221 ? -22.099 63.103  88.875  1.00 19.41 ? 1219 ASN   A CB    1 
ATOM   9036  C  CG    . ASN   A 1  1221 ? -23.432 62.590  88.367  1.00 17.64 ? 1219 ASN   A CG    1 
ATOM   9037  O  OD1   . ASN   A 1  1221 ? -23.810 61.445  88.623  1.00 17.53 ? 1219 ASN   A OD1   1 
ATOM   9038  N  ND2   . ASN   A 1  1221 ? -24.148 63.435  87.640  1.00 20.91 ? 1219 ASN   A ND2   1 
ATOM   9039  N  N     . THR   A 1  1222 ? -21.176 59.625  88.906  1.00 16.09 ? 1220 THR   A N     1 
ATOM   9040  C  CA    . THR   A 1  1222 ? -20.958 58.473  88.047  1.00 19.34 ? 1220 THR   A CA    1 
ATOM   9041  C  C     . THR   A 1  1222 ? -22.228 58.030  87.349  1.00 21.98 ? 1220 THR   A C     1 
ATOM   9042  O  O     . THR   A 1  1222 ? -22.202 57.049  86.603  1.00 27.31 ? 1220 THR   A O     1 
ATOM   9043  C  CB    . THR   A 1  1222 ? -20.343 57.325  88.846  1.00 22.31 ? 1220 THR   A CB    1 
ATOM   9044  O  OG1   . THR   A 1  1222 ? -21.239 56.942  89.894  1.00 21.12 ? 1220 THR   A OG1   1 
ATOM   9045  C  CG2   . THR   A 1  1222 ? -19.022 57.770  89.462  1.00 20.48 ? 1220 THR   A CG2   1 
ATOM   9046  N  N     . ALA   A 1  1223 ? -23.331 58.725  87.578  1.00 18.51 ? 1221 ALA   A N     1 
ATOM   9047  C  CA    . ALA   A 1  1223 ? -24.562 58.494  86.842  1.00 22.79 ? 1221 ALA   A CA    1 
ATOM   9048  C  C     . ALA   A 1  1223 ? -24.737 59.467  85.683  1.00 26.77 ? 1221 ALA   A C     1 
ATOM   9049  O  O     . ALA   A 1  1223 ? -25.777 59.437  85.020  1.00 34.63 ? 1221 ALA   A O     1 
ATOM   9050  C  CB    . ALA   A 1  1223 ? -25.760 58.609  87.781  1.00 23.41 ? 1221 ALA   A CB    1 
ATOM   9051  N  N     . ALA   A 1  1224 ? -23.742 60.327  85.422  1.00 27.13 ? 1222 ALA   A N     1 
ATOM   9052  C  CA    . ALA   A 1  1224 ? -23.922 61.427  84.476  1.00 29.88 ? 1222 ALA   A CA    1 
ATOM   9053  C  C     . ALA   A 1  1224 ? -24.134 60.937  83.050  1.00 31.19 ? 1222 ALA   A C     1 
ATOM   9054  O  O     . ALA   A 1  1224 ? -24.770 61.631  82.250  1.00 39.11 ? 1222 ALA   A O     1 
ATOM   9055  C  CB    . ALA   A 1  1224 ? -22.732 62.385  84.536  1.00 29.36 ? 1222 ALA   A CB    1 
ATOM   9056  N  N     . ALA   A 1  1225 ? -23.616 59.755  82.707  1.00 31.46 ? 1223 ALA   A N     1 
ATOM   9057  C  CA    . ALA   A 1  1225 ? -23.800 59.232  81.355  1.00 33.74 ? 1223 ALA   A CA    1 
ATOM   9058  C  C     . ALA   A 1  1225 ? -25.234 58.798  81.079  1.00 40.09 ? 1223 ALA   A C     1 
ATOM   9059  O  O     . ALA   A 1  1225 ? -25.558 58.486  79.928  1.00 40.64 ? 1223 ALA   A O     1 
ATOM   9060  C  CB    . ALA   A 1  1225 ? -22.837 58.074  81.081  1.00 33.85 ? 1223 ALA   A CB    1 
ATOM   9061  N  N     . GLY   A 1  1226 ? -26.093 58.775  82.092  1.00 34.53 ? 1224 GLY   A N     1 
ATOM   9062  C  CA    . GLY   A 1  1226 ? -27.487 58.407  81.923  1.00 37.30 ? 1224 GLY   A CA    1 
ATOM   9063  C  C     . GLY   A 1  1226 ? -27.929 57.226  82.756  1.00 39.69 ? 1224 GLY   A C     1 
ATOM   9064  O  O     . GLY   A 1  1226 ? -29.133 56.931  82.793  1.00 35.35 ? 1224 GLY   A O     1 
ATOM   9065  N  N     . GLY   A 1  1227 ? -27.012 56.536  83.426  1.00 31.31 ? 1225 GLY   A N     1 
ATOM   9066  C  CA    . GLY   A 1  1227 ? -27.381 55.414  84.265  1.00 39.29 ? 1225 GLY   A CA    1 
ATOM   9067  C  C     . GLY   A 1  1227 ? -26.268 55.084  85.235  1.00 37.41 ? 1225 GLY   A C     1 
ATOM   9068  O  O     . GLY   A 1  1227 ? -25.185 55.674  85.205  1.00 34.71 ? 1225 GLY   A O     1 
ATOM   9069  N  N     . ASN   A 1  1228 ? -26.552 54.108  86.094  1.00 30.11 ? 1226 ASN   A N     1 
ATOM   9070  C  CA    . ASN   A 1  1228 ? -25.651 53.680  87.158  1.00 36.94 ? 1226 ASN   A CA    1 
ATOM   9071  C  C     . ASN   A 1  1228 ? -25.173 52.269  86.827  1.00 37.85 ? 1226 ASN   A C     1 
ATOM   9072  O  O     . ASN   A 1  1228 ? -25.955 51.311  86.881  1.00 35.54 ? 1226 ASN   A O     1 
ATOM   9073  C  CB    . ASN   A 1  1228 ? -26.386 53.725  88.500  1.00 36.25 ? 1226 ASN   A CB    1 
ATOM   9074  C  CG    . ASN   A 1  1228 ? -25.474 53.474  89.690  1.00 38.52 ? 1226 ASN   A CG    1 
ATOM   9075  O  OD1   . ASN   A 1  1228 ? -24.552 52.660  89.628  1.00 37.34 ? 1226 ASN   A OD1   1 
ATOM   9076  N  ND2   . ASN   A 1  1228 ? -25.744 54.167  90.792  1.00 36.51 ? 1226 ASN   A ND2   1 
ATOM   9077  N  N     . ALA   A 1  1229 ? -23.885 52.148  86.489  1.00 34.30 ? 1227 ALA   A N     1 
ATOM   9078  C  CA    . ALA   A 1  1229 ? -23.322 50.852  86.122  1.00 32.88 ? 1227 ALA   A CA    1 
ATOM   9079  C  C     . ALA   A 1  1229 ? -23.391 49.866  87.281  1.00 38.18 ? 1227 ALA   A C     1 
ATOM   9080  O  O     . ALA   A 1  1229 ? -23.790 48.709  87.105  1.00 37.12 ? 1227 ALA   A O     1 
ATOM   9081  C  CB    . ALA   A 1  1229 ? -21.874 51.031  85.667  1.00 32.90 ? 1227 ALA   A CB    1 
ATOM   9082  N  N     . SER   A 1  1230 ? -22.986 50.303  88.477  1.00 38.33 ? 1228 SER   A N     1 
ATOM   9083  C  CA    . SER   A 1  1230 ? -22.965 49.393  89.618  1.00 38.10 ? 1228 SER   A CA    1 
ATOM   9084  C  C     . SER   A 1  1230 ? -24.364 48.876  89.941  1.00 45.78 ? 1228 SER   A C     1 
ATOM   9085  O  O     . SER   A 1  1230 ? -24.533 47.703  90.301  1.00 43.28 ? 1228 SER   A O     1 
ATOM   9086  C  CB    . SER   A 1  1230 ? -22.329 50.078  90.830  1.00 42.14 ? 1228 SER   A CB    1 
ATOM   9087  N  N     . LEU   A 1  1231 ? -25.382 49.726  89.790  1.00 35.86 ? 1229 LEU   A N     1 
ATOM   9088  C  CA    . LEU   A 1  1231 ? -26.756 49.308  90.043  1.00 43.13 ? 1229 LEU   A CA    1 
ATOM   9089  C  C     . LEU   A 1  1231 ? -27.338 48.446  88.929  1.00 45.88 ? 1229 LEU   A C     1 
ATOM   9090  O  O     . LEU   A 1  1231 ? -28.396 47.838  89.130  1.00 44.92 ? 1229 LEU   A O     1 
ATOM   9091  C  CB    . LEU   A 1  1231 ? -27.655 50.519  90.315  1.00 39.54 ? 1229 LEU   A CB    1 
ATOM   9092  C  CG    . LEU   A 1  1231 ? -27.554 51.167  91.701  1.00 43.58 ? 1229 LEU   A CG    1 
ATOM   9093  C  CD1   . LEU   A 1  1231 ? -28.643 52.206  91.871  1.00 37.18 ? 1229 LEU   A CD1   1 
ATOM   9094  C  CD2   . LEU   A 1  1231 ? -27.650 50.126  92.799  1.00 44.41 ? 1229 LEU   A CD2   1 
ATOM   9095  N  N     . MET   A 1  1232 ? -26.679 48.368  87.769  1.00 45.90 ? 1230 MET   A N     1 
ATOM   9096  C  CA    . MET   A 1  1232 ? -27.109 47.425  86.741  1.00 45.98 ? 1230 MET   A CA    1 
ATOM   9097  C  C     . MET   A 1  1232 ? -27.008 45.979  87.216  1.00 49.79 ? 1230 MET   A C     1 
ATOM   9098  O  O     . MET   A 1  1232 ? -27.680 45.104  86.656  1.00 44.56 ? 1230 MET   A O     1 
ATOM   9099  C  CB    . MET   A 1  1232 ? -26.299 47.625  85.455  1.00 42.12 ? 1230 MET   A CB    1 
ATOM   9100  N  N     . ALA   A 1  1233 ? -26.194 45.714  88.238  1.00 54.46 ? 1231 ALA   A N     1 
ATOM   9101  C  CA    . ALA   A 1  1233 ? -26.043 44.384  88.814  1.00 56.15 ? 1231 ALA   A CA    1 
ATOM   9102  C  C     . ALA   A 1  1233 ? -26.881 44.183  90.072  1.00 58.95 ? 1231 ALA   A C     1 
ATOM   9103  O  O     . ALA   A 1  1233 ? -26.754 43.143  90.727  1.00 61.63 ? 1231 ALA   A O     1 
ATOM   9104  C  CB    . ALA   A 1  1233 ? -24.570 44.098  89.113  1.00 55.06 ? 1231 ALA   A CB    1 
ATOM   9105  N  N     . ILE   A 1  1234 ? -27.728 45.145  90.428  1.00 55.69 ? 1232 ILE   A N     1 
ATOM   9106  C  CA    . ILE   A 1  1234 ? -28.559 45.056  91.624  1.00 53.65 ? 1232 ILE   A CA    1 
ATOM   9107  C  C     . ILE   A 1  1234 ? -29.995 44.821  91.174  1.00 50.08 ? 1232 ILE   A C     1 
ATOM   9108  O  O     . ILE   A 1  1234 ? -30.679 45.738  90.703  1.00 44.92 ? 1232 ILE   A O     1 
ATOM   9109  C  CB    . ILE   A 1  1234 ? -28.425 46.286  92.527  1.00 47.10 ? 1232 ILE   A CB    1 
ATOM   9110  C  CG1   . ILE   A 1  1234 ? -26.970 46.438  92.987  1.00 52.00 ? 1232 ILE   A CG1   1 
ATOM   9111  C  CG2   . ILE   A 1  1234 ? -29.361 46.162  93.714  1.00 38.34 ? 1232 ILE   A CG2   1 
ATOM   9112  C  CD1   . ILE   A 1  1234 ? -26.798 47.067  94.355  1.00 44.08 ? 1232 ILE   A CD1   1 
ATOM   9113  N  N     . GLY   A 1  1235 ? -30.449 43.582  91.311  1.00 47.32 ? 1233 GLY   A N     1 
ATOM   9114  C  CA    . GLY   A 1  1235 ? -31.815 43.218  91.004  1.00 38.72 ? 1233 GLY   A CA    1 
ATOM   9115  C  C     . GLY   A 1  1235 ? -32.357 42.356  92.122  1.00 37.96 ? 1233 GLY   A C     1 
ATOM   9116  O  O     . GLY   A 1  1235 ? -31.645 41.521  92.683  1.00 46.29 ? 1233 GLY   A O     1 
ATOM   9117  O  OXT   . GLY   A 1  1235 ? -33.510 42.469  92.502  1.00 25.78 ? 1233 GLY   A OXT   1 
ATOM   9118  N  N     . ALA   B 1  16   ? 30.051  4.748   81.180  1.00 43.82 ? 14   ALA   B N     1 
ATOM   9119  C  CA    . ALA   B 1  16   ? 29.057  5.786   81.430  1.00 43.45 ? 14   ALA   B CA    1 
ATOM   9120  C  C     . ALA   B 1  16   ? 27.658  5.193   81.405  1.00 41.31 ? 14   ALA   B C     1 
ATOM   9121  O  O     . ALA   B 1  16   ? 27.340  4.382   80.535  1.00 42.38 ? 14   ALA   B O     1 
ATOM   9122  C  CB    . ALA   B 1  16   ? 29.172  6.902   80.398  1.00 38.99 ? 14   ALA   B CB    1 
ATOM   9123  N  N     . PRO   B 1  17   ? 26.819  5.599   82.354  1.00 39.76 ? 15   PRO   B N     1 
ATOM   9124  C  CA    . PRO   B 1  17   ? 25.436  5.114   82.358  1.00 36.96 ? 15   PRO   B CA    1 
ATOM   9125  C  C     . PRO   B 1  17   ? 24.694  5.584   81.115  1.00 33.70 ? 15   PRO   B C     1 
ATOM   9126  O  O     . PRO   B 1  17   ? 24.895  6.702   80.631  1.00 33.65 ? 15   PRO   B O     1 
ATOM   9127  C  CB    . PRO   B 1  17   ? 24.849  5.727   83.634  1.00 39.90 ? 15   PRO   B CB    1 
ATOM   9128  C  CG    . PRO   B 1  17   ? 25.703  6.921   83.906  1.00 43.77 ? 15   PRO   B CG    1 
ATOM   9129  C  CD    . PRO   B 1  17   ? 27.081  6.545   83.450  1.00 39.58 ? 15   PRO   B CD    1 
ATOM   9130  N  N     . ALA   B 1  18   ? 23.854  4.703   80.584  1.00 29.89 ? 16   ALA   B N     1 
ATOM   9131  C  CA    . ALA   B 1  18   ? 23.080  5.037   79.401  1.00 29.21 ? 16   ALA   B CA    1 
ATOM   9132  C  C     . ALA   B 1  18   ? 22.151  6.205   79.719  1.00 25.86 ? 16   ALA   B C     1 
ATOM   9133  O  O     . ALA   B 1  18   ? 21.595  6.272   80.820  1.00 28.03 ? 16   ALA   B O     1 
ATOM   9134  C  CB    . ALA   B 1  18   ? 22.245  3.836   78.958  1.00 27.10 ? 16   ALA   B CB    1 
ATOM   9135  N  N     . PRO   B 1  19   ? 21.969  7.141   78.794  1.00 23.67 ? 17   PRO   B N     1 
ATOM   9136  C  CA    . PRO   B 1  19   ? 21.121  8.305   79.075  1.00 22.47 ? 17   PRO   B CA    1 
ATOM   9137  C  C     . PRO   B 1  19   ? 19.704  7.890   79.440  1.00 22.43 ? 17   PRO   B C     1 
ATOM   9138  O  O     . PRO   B 1  19   ? 19.080  7.076   78.759  1.00 23.66 ? 17   PRO   B O     1 
ATOM   9139  C  CB    . PRO   B 1  19   ? 21.147  9.084   77.755  1.00 24.21 ? 17   PRO   B CB    1 
ATOM   9140  C  CG    . PRO   B 1  19   ? 22.436  8.712   77.142  1.00 26.05 ? 17   PRO   B CG    1 
ATOM   9141  C  CD    . PRO   B 1  19   ? 22.647  7.262   77.492  1.00 26.10 ? 17   PRO   B CD    1 
ATOM   9142  N  N     . PHE   B 1  20   ? 19.207  8.455   80.538  1.00 22.28 ? 18   PHE   B N     1 
ATOM   9143  C  CA    . PHE   B 1  20   ? 17.834  8.281   81.001  1.00 20.03 ? 18   PHE   B CA    1 
ATOM   9144  C  C     . PHE   B 1  20   ? 17.508  6.865   81.455  1.00 23.32 ? 18   PHE   B C     1 
ATOM   9145  O  O     . PHE   B 1  20   ? 16.337  6.558   81.678  1.00 25.42 ? 18   PHE   B O     1 
ATOM   9146  C  CB    . PHE   B 1  20   ? 16.800  8.767   79.979  1.00 21.14 ? 18   PHE   B CB    1 
ATOM   9147  C  CG    . PHE   B 1  20   ? 16.995  10.186  79.565  1.00 19.51 ? 18   PHE   B CG    1 
ATOM   9148  C  CD1   . PHE   B 1  20   ? 16.658  11.219  80.424  1.00 19.31 ? 18   PHE   B CD1   1 
ATOM   9149  C  CD2   . PHE   B 1  20   ? 17.526  10.491  78.320  1.00 21.06 ? 18   PHE   B CD2   1 
ATOM   9150  C  CE1   . PHE   B 1  20   ? 16.827  12.538  80.048  1.00 21.84 ? 18   PHE   B CE1   1 
ATOM   9151  C  CE2   . PHE   B 1  20   ? 17.704  11.808  77.942  1.00 20.82 ? 18   PHE   B CE2   1 
ATOM   9152  C  CZ    . PHE   B 1  20   ? 17.353  12.828  78.805  1.00 20.11 ? 18   PHE   B CZ    1 
ATOM   9153  N  N     . ALA   B 1  21   ? 18.509  5.998   81.605  1.00 27.55 ? 19   ALA   B N     1 
ATOM   9154  C  CA    . ALA   B 1  21   ? 18.251  4.626   82.023  1.00 29.57 ? 19   ALA   B CA    1 
ATOM   9155  C  C     . ALA   B 1  21   ? 17.678  4.547   83.432  1.00 33.47 ? 19   ALA   B C     1 
ATOM   9156  O  O     . ALA   B 1  21   ? 17.021  3.556   83.766  1.00 37.71 ? 19   ALA   B O     1 
ATOM   9157  C  CB    . ALA   B 1  21   ? 19.539  3.806   81.931  1.00 33.14 ? 19   ALA   B CB    1 
ATOM   9158  N  N     . ASP   B 1  22   ? 17.907  5.562   84.257  1.00 25.96 ? 20   ASP   B N     1 
ATOM   9159  C  CA    . ASP   B 1  22   ? 17.405  5.589   85.624  1.00 27.58 ? 20   ASP   B CA    1 
ATOM   9160  C  C     . ASP   B 1  22   ? 16.640  6.872   85.870  1.00 22.74 ? 20   ASP   B C     1 
ATOM   9161  O  O     . ASP   B 1  22   ? 16.714  7.462   86.952  1.00 24.63 ? 20   ASP   B O     1 
ATOM   9162  C  CB    . ASP   B 1  22   ? 18.535  5.445   86.639  1.00 34.90 ? 20   ASP   B CB    1 
ATOM   9163  C  CG    . ASP   B 1  22   ? 19.185  4.073   86.606  1.00 47.76 ? 20   ASP   B CG    1 
ATOM   9164  O  OD1   . ASP   B 1  22   ? 18.464  3.078   86.376  1.00 56.41 ? 20   ASP   B OD1   1 
ATOM   9165  O  OD2   . ASP   B 1  22   ? 20.416  3.990   86.815  1.00 56.47 ? 20   ASP   B OD2   1 
ATOM   9166  N  N     . PHE   B 1  23   ? 15.886  7.324   84.867  1.00 20.23 ? 21   PHE   B N     1 
ATOM   9167  C  CA    . PHE   B 1  23   ? 15.310  8.661   84.948  1.00 20.52 ? 21   PHE   B CA    1 
ATOM   9168  C  C     . PHE   B 1  23   ? 14.351  8.792   86.125  1.00 18.98 ? 21   PHE   B C     1 
ATOM   9169  O  O     . PHE   B 1  23   ? 14.515  9.668   86.977  1.00 19.49 ? 21   PHE   B O     1 
ATOM   9170  C  CB    . PHE   B 1  23   ? 14.606  9.034   83.650  1.00 18.74 ? 21   PHE   B CB    1 
ATOM   9171  C  CG    . PHE   B 1  23   ? 13.924  10.357  83.727  1.00 17.48 ? 21   PHE   B CG    1 
ATOM   9172  C  CD1   . PHE   B 1  23   ? 14.673  11.509  83.895  1.00 18.77 ? 21   PHE   B CD1   1 
ATOM   9173  C  CD2   . PHE   B 1  23   ? 12.536  10.454  83.681  1.00 19.91 ? 21   PHE   B CD2   1 
ATOM   9174  C  CE1   . PHE   B 1  23   ? 14.056  12.749  83.993  1.00 19.01 ? 21   PHE   B CE1   1 
ATOM   9175  C  CE2   . PHE   B 1  23   ? 11.919  11.688  83.788  1.00 20.27 ? 21   PHE   B CE2   1 
ATOM   9176  C  CZ    . PHE   B 1  23   ? 12.682  12.830  83.943  1.00 19.61 ? 21   PHE   B CZ    1 
ATOM   9177  N  N     . ALA   B 1  24   ? 13.324  7.956   86.164  1.00 17.91 ? 22   ALA   B N     1 
ATOM   9178  C  CA    . ALA   B 1  24   ? 12.357  8.066   87.250  1.00 18.20 ? 22   ALA   B CA    1 
ATOM   9179  C  C     . ALA   B 1  24   ? 11.638  6.744   87.472  1.00 18.49 ? 22   ALA   B C     1 
ATOM   9180  O  O     . ALA   B 1  24   ? 10.408  6.690   87.376  1.00 20.36 ? 22   ALA   B O     1 
ATOM   9181  C  CB    . ALA   B 1  24   ? 11.335  9.160   86.942  1.00 21.64 ? 22   ALA   B CB    1 
ATOM   9182  N  N     . PRO   B 1  25   ? 12.353  5.675   87.809  1.00 19.91 ? 23   PRO   B N     1 
ATOM   9183  C  CA    . PRO   B 1  25   ? 11.696  4.388   88.033  1.00 22.93 ? 23   PRO   B CA    1 
ATOM   9184  C  C     . PRO   B 1  25   ? 10.720  4.486   89.189  1.00 22.27 ? 23   PRO   B C     1 
ATOM   9185  O  O     . PRO   B 1  25   ? 11.028  5.105   90.217  1.00 22.47 ? 23   PRO   B O     1 
ATOM   9186  C  CB    . PRO   B 1  25   ? 12.865  3.454   88.380  1.00 25.99 ? 23   PRO   B CB    1 
ATOM   9187  C  CG    . PRO   B 1  25   ? 13.912  4.347   88.913  1.00 24.84 ? 23   PRO   B CG    1 
ATOM   9188  C  CD    . PRO   B 1  25   ? 13.782  5.639   88.163  1.00 21.82 ? 23   PRO   B CD    1 
ATOM   9189  N  N     . PRO   B 1  26   ? 9.536   3.899   89.065  1.00 21.41 ? 24   PRO   B N     1 
ATOM   9190  C  CA    . PRO   B 1  26   ? 8.582   3.954   90.173  1.00 21.59 ? 24   PRO   B CA    1 
ATOM   9191  C  C     . PRO   B 1  26   ? 9.073   3.138   91.354  1.00 21.61 ? 24   PRO   B C     1 
ATOM   9192  O  O     . PRO   B 1  26   ? 9.907   2.237   91.226  1.00 22.37 ? 24   PRO   B O     1 
ATOM   9193  C  CB    . PRO   B 1  26   ? 7.311   3.340   89.582  1.00 23.91 ? 24   PRO   B CB    1 
ATOM   9194  C  CG    . PRO   B 1  26   ? 7.810   2.422   88.529  1.00 24.03 ? 24   PRO   B CG    1 
ATOM   9195  C  CD    . PRO   B 1  26   ? 9.027   3.096   87.939  1.00 23.90 ? 24   PRO   B CD    1 
ATOM   9196  N  N     . VAL   B 1  27   ? 8.534   3.479   92.527  1.00 22.14 ? 25   VAL   B N     1 
ATOM   9197  C  CA    . VAL   B 1  27   ? 8.870   2.750   93.746  1.00 23.44 ? 25   VAL   B CA    1 
ATOM   9198  C  C     . VAL   B 1  27   ? 8.519   1.275   93.604  1.00 22.38 ? 25   VAL   B C     1 
ATOM   9199  O  O     . VAL   B 1  27   ? 9.266   0.395   94.055  1.00 25.17 ? 25   VAL   B O     1 
ATOM   9200  C  CB    . VAL   B 1  27   ? 8.169   3.391   94.957  1.00 21.08 ? 25   VAL   B CB    1 
ATOM   9201  C  CG1   . VAL   B 1  27   ? 8.297   2.481   96.175  1.00 24.19 ? 25   VAL   B CG1   1 
ATOM   9202  C  CG2   . VAL   B 1  27   ? 8.757   4.750   95.234  1.00 22.98 ? 25   VAL   B CG2   1 
ATOM   9203  N  N     . ARG   B 1  28   ? 7.390   0.980   92.973  1.00 21.61 ? 26   ARG   B N     1 
ATOM   9204  C  CA    . ARG   B 1  28   ? 6.958   -0.395  92.779  1.00 22.62 ? 26   ARG   B CA    1 
ATOM   9205  C  C     . ARG   B 1  28   ? 6.188   -0.475  91.474  1.00 27.31 ? 26   ARG   B C     1 
ATOM   9206  O  O     . ARG   B 1  28   ? 5.719   0.549   90.963  1.00 23.72 ? 26   ARG   B O     1 
ATOM   9207  C  CB    . ARG   B 1  28   ? 6.076   -0.867  93.946  1.00 24.27 ? 26   ARG   B CB    1 
ATOM   9208  C  CG    . ARG   B 1  28   ? 4.724   -0.156  94.020  1.00 25.90 ? 26   ARG   B CG    1 
ATOM   9209  C  CD    . ARG   B 1  28   ? 3.951   -0.531  95.285  1.00 26.38 ? 26   ARG   B CD    1 
ATOM   9210  N  NE    . ARG   B 1  28   ? 4.550   0.082   96.465  1.00 27.63 ? 26   ARG   B NE    1 
ATOM   9211  C  CZ    . ARG   B 1  28   ? 5.313   -0.561  97.338  1.00 34.57 ? 26   ARG   B CZ    1 
ATOM   9212  N  NH1   . ARG   B 1  28   ? 5.551   -1.857  97.224  1.00 33.04 ? 26   ARG   B NH1   1 
ATOM   9213  N  NH2   . ARG   B 1  28   ? 5.855   0.115   98.347  1.00 30.32 ? 26   ARG   B NH2   1 
ATOM   9214  N  N     . PRO   B 1  29   ? 6.059   -1.668  90.893  1.00 24.93 ? 27   PRO   B N     1 
ATOM   9215  C  CA    . PRO   B 1  29   ? 5.169   -1.815  89.739  1.00 24.97 ? 27   PRO   B CA    1 
ATOM   9216  C  C     . PRO   B 1  29   ? 3.758   -1.397  90.118  1.00 22.47 ? 27   PRO   B C     1 
ATOM   9217  O  O     . PRO   B 1  29   ? 3.267   -1.714  91.202  1.00 24.25 ? 27   PRO   B O     1 
ATOM   9218  C  CB    . PRO   B 1  29   ? 5.247   -3.311  89.418  1.00 29.29 ? 27   PRO   B CB    1 
ATOM   9219  C  CG    . PRO   B 1  29   ? 6.568   -3.737  89.974  1.00 29.70 ? 27   PRO   B CG    1 
ATOM   9220  C  CD    . PRO   B 1  29   ? 6.736   -2.934  91.225  1.00 27.71 ? 27   PRO   B CD    1 
ATOM   9221  N  N     . GLN   B 1  30   ? 3.118   -0.660  89.222  1.00 22.09 ? 28   GLN   B N     1 
ATOM   9222  C  CA    . GLN   B 1  30   ? 1.809   -0.084  89.508  1.00 23.60 ? 28   GLN   B CA    1 
ATOM   9223  C  C     . GLN   B 1  30   ? 0.728   -1.128  89.270  1.00 22.38 ? 28   GLN   B C     1 
ATOM   9224  O  O     . GLN   B 1  30   ? 0.554   -1.611  88.142  1.00 24.56 ? 28   GLN   B O     1 
ATOM   9225  C  CB    . GLN   B 1  30   ? 1.580   1.137   88.619  1.00 23.19 ? 28   GLN   B CB    1 
ATOM   9226  C  CG    . GLN   B 1  30   ? 2.657   2.204   88.757  1.00 23.13 ? 28   GLN   B CG    1 
ATOM   9227  C  CD    . GLN   B 1  30   ? 2.651   2.868   90.121  1.00 23.65 ? 28   GLN   B CD    1 
ATOM   9228  O  OE1   . GLN   B 1  30   ? 1.778   3.684   90.418  1.00 22.83 ? 28   GLN   B OE1   1 
ATOM   9229  N  NE2   . GLN   B 1  30   ? 3.628   2.528   90.959  1.00 19.91 ? 28   GLN   B NE2   1 
ATOM   9230  N  N     . SER   B 1  31   ? -0.012  -1.458  90.326  1.00 22.37 ? 29   SER   B N     1 
ATOM   9231  C  CA    . SER   B 1  31   ? -1.099  -2.415  90.236  1.00 21.80 ? 29   SER   B CA    1 
ATOM   9232  C  C     . SER   B 1  31   ? -2.263  -1.813  89.455  1.00 22.46 ? 29   SER   B C     1 
ATOM   9233  O  O     . SER   B 1  31   ? -2.294  -0.618  89.151  1.00 21.80 ? 29   SER   B O     1 
ATOM   9234  C  CB    . SER   B 1  31   ? -1.589  -2.779  91.634  1.00 22.09 ? 29   SER   B CB    1 
ATOM   9235  O  OG    . SER   B 1  31   ? -2.231  -1.667  92.238  1.00 23.49 ? 29   SER   B OG    1 
ATOM   9236  N  N     . THR   B 1  32   ? -3.229  -2.672  89.116  1.00 22.45 ? 30   THR   B N     1 
ATOM   9237  C  CA    . THR   B 1  32   ? -4.452  -2.194  88.479  1.00 24.35 ? 30   THR   B CA    1 
ATOM   9238  C  C     . THR   B 1  32   ? -5.095  -1.085  89.303  1.00 20.69 ? 30   THR   B C     1 
ATOM   9239  O  O     . THR   B 1  32   ? -5.468  -0.037  88.767  1.00 22.38 ? 30   THR   B O     1 
ATOM   9240  C  CB    . THR   B 1  32   ? -5.422  -3.362  88.287  1.00 25.75 ? 30   THR   B CB    1 
ATOM   9241  O  OG1   . THR   B 1  32   ? -4.856  -4.298  87.361  1.00 29.96 ? 30   THR   B OG1   1 
ATOM   9242  C  CG2   . THR   B 1  32   ? -6.778  -2.876  87.764  1.00 30.05 ? 30   THR   B CG2   1 
ATOM   9243  N  N     . LEU   B 1  33   ? -5.186  -1.279  90.620  1.00 22.33 ? 31   LEU   B N     1 
ATOM   9244  C  CA    . LEU   B 1  33   ? -5.796  -0.260  91.465  1.00 23.26 ? 31   LEU   B CA    1 
ATOM   9245  C  C     . LEU   B 1  33   ? -4.964  1.014   91.505  1.00 21.18 ? 31   LEU   B C     1 
ATOM   9246  O  O     . LEU   B 1  33   ? -5.517  2.118   91.493  1.00 19.75 ? 31   LEU   B O     1 
ATOM   9247  C  CB    . LEU   B 1  33   ? -6.023  -0.812  92.867  1.00 20.90 ? 31   LEU   B CB    1 
ATOM   9248  C  CG    . LEU   B 1  33   ? -7.090  -1.895  92.851  1.00 22.46 ? 31   LEU   B CG    1 
ATOM   9249  C  CD1   . LEU   B 1  33   ? -7.105  -2.629  94.166  1.00 24.65 ? 31   LEU   B CD1   1 
ATOM   9250  C  CD2   . LEU   B 1  33   ? -8.453  -1.277  92.554  1.00 27.83 ? 31   LEU   B CD2   1 
ATOM   9251  N  N     . ARG   B 1  34   ? -3.636  0.890   91.567  1.00 19.56 ? 32   ARG   B N     1 
ATOM   9252  C  CA    . ARG   B 1  34   ? -2.815  2.096   91.549  1.00 19.42 ? 32   ARG   B CA    1 
ATOM   9253  C  C     . ARG   B 1  34   ? -2.949  2.821   90.217  1.00 20.26 ? 32   ARG   B C     1 
ATOM   9254  O  O     . ARG   B 1  34   ? -2.990  4.058   90.174  1.00 19.73 ? 32   ARG   B O     1 
ATOM   9255  C  CB    . ARG   B 1  34   ? -1.351  1.757   91.830  1.00 19.75 ? 32   ARG   B CB    1 
ATOM   9256  C  CG    . ARG   B 1  34   ? -1.069  1.332   93.266  1.00 20.83 ? 32   ARG   B CG    1 
ATOM   9257  C  CD    . ARG   B 1  34   ? -1.156  2.510   94.234  1.00 22.15 ? 32   ARG   B CD    1 
ATOM   9258  N  NE    . ARG   B 1  34   ? -0.133  3.508   93.950  1.00 21.25 ? 32   ARG   B NE    1 
ATOM   9259  C  CZ    . ARG   B 1  34   ? 1.066   3.538   94.521  1.00 21.78 ? 32   ARG   B CZ    1 
ATOM   9260  N  NH1   . ARG   B 1  34   ? 1.426   2.635   95.423  1.00 21.89 ? 32   ARG   B NH1   1 
ATOM   9261  N  NH2   . ARG   B 1  34   ? 1.930   4.484   94.165  1.00 22.08 ? 32   ARG   B NH2   1 
ATOM   9262  N  N     . ARG   B 1  35   ? -3.023  2.067   89.120  1.00 20.26 ? 33   ARG   B N     1 
ATOM   9263  C  CA    . ARG   B 1  35   ? -3.160  2.698   87.817  1.00 22.10 ? 33   ARG   B CA    1 
ATOM   9264  C  C     . ARG   B 1  35   ? -4.488  3.419   87.689  1.00 19.49 ? 33   ARG   B C     1 
ATOM   9265  O  O     . ARG   B 1  35   ? -4.559  4.455   87.025  1.00 20.18 ? 33   ARG   B O     1 
ATOM   9266  C  CB    . ARG   B 1  35   ? -3.035  1.646   86.717  1.00 22.44 ? 33   ARG   B CB    1 
ATOM   9267  C  CG    . ARG   B 1  35   ? -1.625  1.142   86.557  1.00 25.56 ? 33   ARG   B CG    1 
ATOM   9268  C  CD    . ARG   B 1  35   ? -1.541  0.063   85.484  1.00 30.72 ? 33   ARG   B CD    1 
ATOM   9269  N  NE    . ARG   B 1  35   ? -0.183  -0.455  85.427  1.00 36.76 ? 33   ARG   B NE    1 
ATOM   9270  C  CZ    . ARG   B 1  35   ? 0.809   0.131   84.769  1.00 44.33 ? 33   ARG   B CZ    1 
ATOM   9271  N  NH1   . ARG   B 1  35   ? 0.604   1.213   84.034  1.00 45.50 ? 33   ARG   B NH1   1 
ATOM   9272  N  NH2   . ARG   B 1  35   ? 2.037   -0.376  84.856  1.00 39.77 ? 33   ARG   B NH2   1 
ATOM   9273  N  N     . ALA   B 1  36   ? -5.541  2.893   88.319  1.00 19.43 ? 34   ALA   B N     1 
ATOM   9274  C  CA    . ALA   B 1  36   ? -6.833  3.563   88.243  1.00 20.17 ? 34   ALA   B CA    1 
ATOM   9275  C  C     . ALA   B 1  36   ? -6.805  4.888   88.992  1.00 20.07 ? 34   ALA   B C     1 
ATOM   9276  O  O     . ALA   B 1  36   ? -7.484  5.842   88.601  1.00 22.37 ? 34   ALA   B O     1 
ATOM   9277  C  CB    . ALA   B 1  36   ? -7.947  2.646   88.754  1.00 20.25 ? 34   ALA   B CB    1 
ATOM   9278  N  N     . ILE   B 1  37   ? -6.019  4.963   90.065  1.00 19.34 ? 35   ILE   B N     1 
ATOM   9279  C  CA    . ILE   B 1  37   ? -5.809  6.233   90.746  1.00 18.66 ? 35   ILE   B CA    1 
ATOM   9280  C  C     . ILE   B 1  37   ? -5.140  7.224   89.811  1.00 19.21 ? 35   ILE   B C     1 
ATOM   9281  O  O     . ILE   B 1  37   ? -5.627  8.339   89.602  1.00 17.75 ? 35   ILE   B O     1 
ATOM   9282  C  CB    . ILE   B 1  37   ? -4.978  6.002   92.023  1.00 19.69 ? 35   ILE   B CB    1 
ATOM   9283  C  CG1   . ILE   B 1  37   ? -5.776  5.176   93.033  1.00 18.81 ? 35   ILE   B CG1   1 
ATOM   9284  C  CG2   . ILE   B 1  37   ? -4.481  7.334   92.610  1.00 18.09 ? 35   ILE   B CG2   1 
ATOM   9285  C  CD1   . ILE   B 1  37   ? -4.901  4.621   94.149  1.00 20.16 ? 35   ILE   B CD1   1 
ATOM   9286  N  N     . THR   B 1  38   ? -4.005  6.830   89.229  1.00 17.12 ? 36   THR   B N     1 
ATOM   9287  C  CA    . THR   B 1  38   ? -3.257  7.750   88.386  1.00 18.17 ? 36   THR   B CA    1 
ATOM   9288  C  C     . THR   B 1  38   ? -4.095  8.210   87.206  1.00 17.55 ? 36   THR   B C     1 
ATOM   9289  O  O     . THR   B 1  38   ? -4.034  9.382   86.815  1.00 18.63 ? 36   THR   B O     1 
ATOM   9290  C  CB    . THR   B 1  38   ? -1.976  7.066   87.915  1.00 17.19 ? 36   THR   B CB    1 
ATOM   9291  O  OG1   . THR   B 1  38   ? -1.299  6.528   89.056  1.00 18.53 ? 36   THR   B OG1   1 
ATOM   9292  C  CG2   . THR   B 1  38   ? -1.069  8.047   87.179  1.00 22.30 ? 36   THR   B CG2   1 
ATOM   9293  N  N     . ALA   B 1  39   ? -4.897  7.301   86.643  1.00 18.64 ? 37   ALA   B N     1 
ATOM   9294  C  CA    . ALA   B 1  39   ? -5.727  7.638   85.492  1.00 19.91 ? 37   ALA   B CA    1 
ATOM   9295  C  C     . ALA   B 1  39   ? -6.703  8.761   85.802  1.00 20.54 ? 37   ALA   B C     1 
ATOM   9296  O  O     . ALA   B 1  39   ? -7.096  9.497   84.892  1.00 21.09 ? 37   ALA   B O     1 
ATOM   9297  C  CB    . ALA   B 1  39   ? -6.484  6.398   85.006  1.00 21.63 ? 37   ALA   B CB    1 
ATOM   9298  N  N     . ALA   B 1  40   ? -7.070  8.936   87.068  1.00 17.91 ? 38   ALA   B N     1 
ATOM   9299  C  CA    . ALA   B 1  40   ? -8.074  9.919   87.446  1.00 19.48 ? 38   ALA   B CA    1 
ATOM   9300  C  C     . ALA   B 1  40   ? -7.473  11.269  87.810  1.00 17.03 ? 38   ALA   B C     1 
ATOM   9301  O  O     . ALA   B 1  40   ? -8.225  12.223  88.036  1.00 19.01 ? 38   ALA   B O     1 
ATOM   9302  C  CB    . ALA   B 1  40   ? -8.886  9.402   88.636  1.00 20.04 ? 38   ALA   B CB    1 
ATOM   9303  N  N     . TYR   B 1  41   ? -6.139  11.365  87.837  1.00 17.55 ? 39   TYR   B N     1 
ATOM   9304  C  CA    . TYR   B 1  41   ? -5.444  12.493  88.456  1.00 16.95 ? 39   TYR   B CA    1 
ATOM   9305  C  C     . TYR   B 1  41   ? -6.034  13.829  88.014  1.00 17.54 ? 39   TYR   B C     1 
ATOM   9306  O  O     . TYR   B 1  41   ? -6.372  14.681  88.845  1.00 18.51 ? 39   TYR   B O     1 
ATOM   9307  C  CB    . TYR   B 1  41   ? -3.965  12.390  88.079  1.00 17.15 ? 39   TYR   B CB    1 
ATOM   9308  C  CG    . TYR   B 1  41   ? -2.965  13.091  88.976  1.00 18.53 ? 39   TYR   B CG    1 
ATOM   9309  C  CD1   . TYR   B 1  41   ? -3.283  14.248  89.685  1.00 19.41 ? 39   TYR   B CD1   1 
ATOM   9310  C  CD2   . TYR   B 1  41   ? -1.673  12.597  89.081  1.00 19.06 ? 39   TYR   B CD2   1 
ATOM   9311  C  CE1   . TYR   B 1  41   ? -2.329  14.883  90.478  1.00 17.27 ? 39   TYR   B CE1   1 
ATOM   9312  C  CE2   . TYR   B 1  41   ? -0.720  13.219  89.871  1.00 18.26 ? 39   TYR   B CE2   1 
ATOM   9313  C  CZ    . TYR   B 1  41   ? -1.044  14.361  90.555  1.00 17.61 ? 39   TYR   B CZ    1 
ATOM   9314  O  OH    . TYR   B 1  41   ? -0.083  14.967  91.335  1.00 18.50 ? 39   TYR   B OH    1 
ATOM   9315  N  N     . ARG   B 1  42   ? -6.179  14.025  86.701  1.00 18.91 ? 40   ARG   B N     1 
ATOM   9316  C  CA    . ARG   B 1  42   ? -6.684  15.284  86.167  1.00 18.76 ? 40   ARG   B CA    1 
ATOM   9317  C  C     . ARG   B 1  42   ? -7.889  15.069  85.266  1.00 19.33 ? 40   ARG   B C     1 
ATOM   9318  O  O     . ARG   B 1  42   ? -8.091  15.808  84.299  1.00 21.14 ? 40   ARG   B O     1 
ATOM   9319  C  CB    . ARG   B 1  42   ? -5.585  16.082  85.478  1.00 21.13 ? 40   ARG   B CB    1 
ATOM   9320  C  CG    . ARG   B 1  42   ? -4.530  16.473  86.483  1.00 20.57 ? 40   ARG   B CG    1 
ATOM   9321  C  CD    . ARG   B 1  42   ? -3.324  17.137  85.885  1.00 20.78 ? 40   ARG   B CD    1 
ATOM   9322  N  NE    . ARG   B 1  42   ? -2.240  17.055  86.848  1.00 20.16 ? 40   ARG   B NE    1 
ATOM   9323  C  CZ    . ARG   B 1  42   ? -2.044  17.914  87.835  1.00 18.89 ? 40   ARG   B CZ    1 
ATOM   9324  N  NH1   . ARG   B 1  42   ? -2.796  19.001  87.971  1.00 19.33 ? 40   ARG   B NH1   1 
ATOM   9325  N  NH2   . ARG   B 1  42   ? -1.065  17.684  88.703  1.00 18.69 ? 40   ARG   B NH2   1 
ATOM   9326  N  N     . ARG   B 1  43   ? -8.700  14.073  85.599  1.00 18.56 ? 41   ARG   B N     1 
ATOM   9327  C  CA    . ARG   B 1  43   ? -9.859  13.736  84.792  1.00 18.89 ? 41   ARG   B CA    1 
ATOM   9328  C  C     . ARG   B 1  43   ? -10.790 14.941  84.695  1.00 19.83 ? 41   ARG   B C     1 
ATOM   9329  O  O     . ARG   B 1  43   ? -10.992 15.654  85.685  1.00 21.24 ? 41   ARG   B O     1 
ATOM   9330  C  CB    . ARG   B 1  43   ? -10.599 12.559  85.436  1.00 18.94 ? 41   ARG   B CB    1 
ATOM   9331  C  CG    . ARG   B 1  43   ? -11.854 12.108  84.687  1.00 18.75 ? 41   ARG   B CG    1 
ATOM   9332  C  CD    . ARG   B 1  43   ? -12.281 10.733  85.151  1.00 20.39 ? 41   ARG   B CD    1 
ATOM   9333  N  NE    . ARG   B 1  43   ? -11.283 9.732   84.793  1.00 21.80 ? 41   ARG   B NE    1 
ATOM   9334  C  CZ    . ARG   B 1  43   ? -11.022 8.645   85.506  1.00 25.60 ? 41   ARG   B CZ    1 
ATOM   9335  N  NH1   . ARG   B 1  43   ? -11.663 8.386   86.632  1.00 20.92 ? 41   ARG   B NH1   1 
ATOM   9336  N  NH2   . ARG   B 1  43   ? -10.089 7.798   85.080  1.00 22.01 ? 41   ARG   B NH2   1 
ATOM   9337  N  N     . PRO   B 1  44   ? -11.358 15.210  83.524  1.00 20.30 ? 42   PRO   B N     1 
ATOM   9338  C  CA    . PRO   B 1  44   ? -12.293 16.333  83.400  1.00 21.16 ? 42   PRO   B CA    1 
ATOM   9339  C  C     . PRO   B 1  44   ? -13.400 16.256  84.440  1.00 19.60 ? 42   PRO   B C     1 
ATOM   9340  O  O     . PRO   B 1  44   ? -13.905 15.180  84.773  1.00 19.56 ? 42   PRO   B O     1 
ATOM   9341  C  CB    . PRO   B 1  44   ? -12.838 16.173  81.979  1.00 21.77 ? 42   PRO   B CB    1 
ATOM   9342  C  CG    . PRO   B 1  44   ? -11.668 15.555  81.241  1.00 24.00 ? 42   PRO   B CG    1 
ATOM   9343  C  CD    . PRO   B 1  44   ? -11.074 14.580  82.223  1.00 21.00 ? 42   PRO   B CD    1 
ATOM   9344  N  N     . GLU   B 1  45   ? -13.768 17.427  84.959  1.00 20.48 ? 43   GLU   B N     1 
ATOM   9345  C  CA    . GLU   B 1  45   ? -14.771 17.498  86.006  1.00 20.44 ? 43   GLU   B CA    1 
ATOM   9346  C  C     . GLU   B 1  45   ? -16.102 16.916  85.543  1.00 22.03 ? 43   GLU   B C     1 
ATOM   9347  O  O     . GLU   B 1  45   ? -16.805 16.272  86.326  1.00 24.19 ? 43   GLU   B O     1 
ATOM   9348  C  CB    . GLU   B 1  45   ? -14.899 18.955  86.440  1.00 25.23 ? 43   GLU   B CB    1 
ATOM   9349  C  CG    . GLU   B 1  45   ? -15.268 19.111  87.874  1.00 28.06 ? 43   GLU   B CG    1 
ATOM   9350  C  CD    . GLU   B 1  45   ? -14.743 20.387  88.497  1.00 19.85 ? 43   GLU   B CD    1 
ATOM   9351  O  OE1   . GLU   B 1  45   ? -13.935 21.125  87.880  1.00 19.85 ? 43   GLU   B OE1   1 
ATOM   9352  O  OE2   . GLU   B 1  45   ? -15.159 20.625  89.642  1.00 21.71 ? 43   GLU   B OE2   1 
ATOM   9353  N  N     . THR   B 1  46   ? -16.443 17.089  84.264  1.00 20.90 ? 44   THR   B N     1 
ATOM   9354  C  CA    . THR   B 1  46   ? -17.683 16.522  83.749  1.00 22.27 ? 44   THR   B CA    1 
ATOM   9355  C  C     . THR   B 1  46   ? -17.649 15.009  83.681  1.00 21.84 ? 44   THR   B C     1 
ATOM   9356  O  O     . THR   B 1  46   ? -18.711 14.386  83.613  1.00 23.74 ? 44   THR   B O     1 
ATOM   9357  C  CB    . THR   B 1  46   ? -17.956 17.061  82.353  1.00 23.38 ? 44   THR   B CB    1 
ATOM   9358  O  OG1   . THR   B 1  46   ? -16.771 16.904  81.561  1.00 23.11 ? 44   THR   B OG1   1 
ATOM   9359  C  CG2   . THR   B 1  46   ? -18.339 18.529  82.428  1.00 24.20 ? 44   THR   B CG2   1 
ATOM   9360  N  N     . GLU   B 1  47   ? -16.466 14.401  83.644  1.00 21.75 ? 45   GLU   B N     1 
ATOM   9361  C  CA    . GLU   B 1  47   ? -16.405 12.948  83.716  1.00 22.87 ? 45   GLU   B CA    1 
ATOM   9362  C  C     . GLU   B 1  47   ? -16.423 12.446  85.148  1.00 21.98 ? 45   GLU   B C     1 
ATOM   9363  O  O     . GLU   B 1  47   ? -16.951 11.362  85.412  1.00 25.76 ? 45   GLU   B O     1 
ATOM   9364  C  CB    . GLU   B 1  47   ? -15.149 12.430  83.012  1.00 21.37 ? 45   GLU   B CB    1 
ATOM   9365  C  CG    . GLU   B 1  47   ? -15.103 12.739  81.526  1.00 28.71 ? 45   GLU   B CG    1 
ATOM   9366  C  CD    . GLU   B 1  47   ? -13.802 12.297  80.894  1.00 33.50 ? 45   GLU   B CD    1 
ATOM   9367  O  OE1   . GLU   B 1  47   ? -13.169 11.363  81.437  1.00 33.88 ? 45   GLU   B OE1   1 
ATOM   9368  O  OE2   . GLU   B 1  47   ? -13.414 12.887  79.868  1.00 36.79 ? 45   GLU   B OE2   1 
ATOM   9369  N  N     . CYS   B 1  48   ? -15.868 13.225  86.082  1.00 20.18 ? 46   CYS   B N     1 
ATOM   9370  C  CA    . CYS   B 1  48   ? -15.796 12.780  87.472  1.00 20.90 ? 46   CYS   B CA    1 
ATOM   9371  C  C     . CYS   B 1  48   ? -17.159 12.778  88.133  1.00 20.20 ? 46   CYS   B C     1 
ATOM   9372  O  O     . CYS   B 1  48   ? -17.457 11.900  88.948  1.00 21.79 ? 46   CYS   B O     1 
ATOM   9373  C  CB    . CYS   B 1  48   ? -14.894 13.713  88.277  1.00 19.63 ? 46   CYS   B CB    1 
ATOM   9374  S  SG    . CYS   B 1  48   ? -13.173 13.692  87.826  1.00 21.10 ? 46   CYS   B SG    1 
ATOM   9375  N  N     . LEU   B 1  49   ? -17.980 13.761  87.825  1.00 21.66 ? 47   LEU   B N     1 
ATOM   9376  C  CA    . LEU   B 1  49   ? -19.169 13.986  88.639  1.00 21.70 ? 47   LEU   B CA    1 
ATOM   9377  C  C     . LEU   B 1  49   ? -20.279 12.947  88.489  1.00 21.80 ? 47   LEU   B C     1 
ATOM   9378  O  O     . LEU   B 1  49   ? -20.861 12.551  89.502  1.00 22.44 ? 47   LEU   B O     1 
ATOM   9379  C  CB    . LEU   B 1  49   ? -19.694 15.418  88.495  1.00 21.48 ? 47   LEU   B CB    1 
ATOM   9380  C  CG    . LEU   B 1  49   ? -19.216 16.357  89.615  1.00 21.41 ? 47   LEU   B CG    1 
ATOM   9381  C  CD1   . LEU   B 1  49   ? -19.759 15.920  90.985  1.00 23.73 ? 47   LEU   B CD1   1 
ATOM   9382  C  CD2   . LEU   B 1  49   ? -17.696 16.420  89.639  1.00 21.71 ? 47   LEU   B CD2   1 
ATOM   9383  N  N     . PRO   B 1  50   ? -20.628 12.486  87.286  1.00 22.64 ? 48   PRO   B N     1 
ATOM   9384  C  CA    . PRO   B 1  50   ? -21.783 11.583  87.164  1.00 23.84 ? 48   PRO   B CA    1 
ATOM   9385  C  C     . PRO   B 1  50   ? -21.653 10.332  88.021  1.00 26.43 ? 48   PRO   B C     1 
ATOM   9386  O  O     . PRO   B 1  50   ? -22.610 9.984   88.723  1.00 25.24 ? 48   PRO   B O     1 
ATOM   9387  C  CB    . PRO   B 1  50   ? -21.831 11.261  85.663  1.00 24.28 ? 48   PRO   B CB    1 
ATOM   9388  C  CG    . PRO   B 1  50   ? -21.325 12.490  85.048  1.00 22.69 ? 48   PRO   B CG    1 
ATOM   9389  C  CD    . PRO   B 1  50   ? -20.184 12.943  85.957  1.00 20.64 ? 48   PRO   B CD    1 
ATOM   9390  N  N     . PRO   B 1  51   ? -20.511 9.627   88.033  1.00 24.37 ? 49   PRO   B N     1 
ATOM   9391  C  CA    . PRO   B 1  51   ? -20.436 8.470   88.942  1.00 23.65 ? 49   PRO   B CA    1 
ATOM   9392  C  C     . PRO   B 1  51   ? -20.533 8.849   90.410  1.00 21.35 ? 49   PRO   B C     1 
ATOM   9393  O  O     . PRO   B 1  51   ? -21.071 8.070   91.207  1.00 24.11 ? 49   PRO   B O     1 
ATOM   9394  C  CB    . PRO   B 1  51   ? -19.092 7.813   88.599  1.00 26.06 ? 49   PRO   B CB    1 
ATOM   9395  C  CG    . PRO   B 1  51   ? -18.289 8.888   87.950  1.00 27.84 ? 49   PRO   B CG    1 
ATOM   9396  C  CD    . PRO   B 1  51   ? -19.292 9.724   87.199  1.00 23.04 ? 49   PRO   B CD    1 
ATOM   9397  N  N     . LEU   B 1  52   ? -20.032 10.025  90.792  1.00 23.49 ? 50   LEU   B N     1 
ATOM   9398  C  CA    . LEU   B 1  52   ? -20.157 10.459  92.181  1.00 22.84 ? 50   LEU   B CA    1 
ATOM   9399  C  C     . LEU   B 1  52   ? -21.609 10.764  92.530  1.00 25.63 ? 50   LEU   B C     1 
ATOM   9400  O  O     . LEU   B 1  52   ? -22.084 10.388  93.605  1.00 23.26 ? 50   LEU   B O     1 
ATOM   9401  C  CB    . LEU   B 1  52   ? -19.275 11.683  92.425  1.00 22.42 ? 50   LEU   B CB    1 
ATOM   9402  C  CG    . LEU   B 1  52   ? -17.770 11.491  92.228  1.00 20.61 ? 50   LEU   B CG    1 
ATOM   9403  C  CD1   . LEU   B 1  52   ? -17.045 12.826  92.289  1.00 20.24 ? 50   LEU   B CD1   1 
ATOM   9404  C  CD2   . LEU   B 1  52   ? -17.227 10.539  93.276  1.00 22.29 ? 50   LEU   B CD2   1 
ATOM   9405  N  N     . VAL   B 1  53   ? -22.321 11.457  91.637  1.00 24.25 ? 51   VAL   B N     1 
ATOM   9406  C  CA    . VAL   B 1  53   ? -23.750 11.704  91.847  1.00 22.81 ? 51   VAL   B CA    1 
ATOM   9407  C  C     . VAL   B 1  53   ? -24.487 10.392  92.067  1.00 26.99 ? 51   VAL   B C     1 
ATOM   9408  O  O     . VAL   B 1  53   ? -25.293 10.259  92.996  1.00 25.72 ? 51   VAL   B O     1 
ATOM   9409  C  CB    . VAL   B 1  53   ? -24.343 12.499  90.669  1.00 23.86 ? 51   VAL   B CB    1 
ATOM   9410  C  CG1   . VAL   B 1  53   ? -25.874 12.510  90.744  1.00 25.07 ? 51   VAL   B CG1   1 
ATOM   9411  C  CG2   . VAL   B 1  53   ? -23.813 13.910  90.659  1.00 26.26 ? 51   VAL   B CG2   1 
ATOM   9412  N  N     . GLU   B 1  54   ? -24.207 9.395   91.223  1.00 25.11 ? 52   GLU   B N     1 
ATOM   9413  C  CA    . GLU   B 1  54   ? -24.855 8.094   91.370  1.00 28.57 ? 52   GLU   B CA    1 
ATOM   9414  C  C     . GLU   B 1  54   ? -24.548 7.475   92.727  1.00 26.85 ? 52   GLU   B C     1 
ATOM   9415  O  O     . GLU   B 1  54   ? -25.453 7.004   93.428  1.00 28.93 ? 52   GLU   B O     1 
ATOM   9416  C  CB    . GLU   B 1  54   ? -24.416 7.162   90.241  1.00 30.95 ? 52   GLU   B CB    1 
ATOM   9417  N  N     . ALA   B 1  55   ? -23.270 7.475   93.123  1.00 26.80 ? 53   ALA   B N     1 
ATOM   9418  C  CA    . ALA   B 1  55   ? -22.891 6.856   94.388  1.00 27.47 ? 53   ALA   B CA    1 
ATOM   9419  C  C     . ALA   B 1  55   ? -23.439 7.619   95.591  1.00 26.22 ? 53   ALA   B C     1 
ATOM   9420  O  O     . ALA   B 1  55   ? -23.673 7.019   96.644  1.00 27.92 ? 53   ALA   B O     1 
ATOM   9421  C  CB    . ALA   B 1  55   ? -21.368 6.749   94.486  1.00 26.88 ? 53   ALA   B CB    1 
ATOM   9422  N  N     . ALA   B 1  56   ? -23.642 8.929   95.459  1.00 25.69 ? 54   ALA   B N     1 
ATOM   9423  C  CA    . ALA   B 1  56   ? -24.132 9.762   96.551  1.00 25.31 ? 54   ALA   B CA    1 
ATOM   9424  C  C     . ALA   B 1  56   ? -25.649 9.804   96.633  1.00 26.77 ? 54   ALA   B C     1 
ATOM   9425  O  O     . ALA   B 1  56   ? -26.193 10.454  97.533  1.00 30.55 ? 54   ALA   B O     1 
ATOM   9426  C  CB    . ALA   B 1  56   ? -23.602 11.188  96.398  1.00 27.29 ? 54   ALA   B CB    1 
ATOM   9427  N  N     . THR   B 1  57   ? -26.343 9.140   95.715  1.00 27.96 ? 55   THR   B N     1 
ATOM   9428  C  CA    . THR   B 1  57   ? -27.795 9.215   95.688  1.00 31.06 ? 55   THR   B CA    1 
ATOM   9429  C  C     . THR   B 1  57   ? -28.398 8.490   96.885  1.00 33.53 ? 55   THR   B C     1 
ATOM   9430  O  O     . THR   B 1  57   ? -27.967 7.394   97.252  1.00 32.39 ? 55   THR   B O     1 
ATOM   9431  C  CB    . THR   B 1  57   ? -28.306 8.615   94.381  1.00 35.76 ? 55   THR   B CB    1 
ATOM   9432  O  OG1   . THR   B 1  57   ? -27.947 9.487   93.304  1.00 32.52 ? 55   THR   B OG1   1 
ATOM   9433  C  CG2   . THR   B 1  57   ? -29.813 8.454   94.416  1.00 32.74 ? 55   THR   B CG2   1 
ATOM   9434  N  N     . GLN   B 1  58   ? -29.388 9.126   97.511  1.00 36.72 ? 56   GLN   B N     1 
ATOM   9435  C  CA    . GLN   B 1  58   ? -30.136 8.536   98.609  1.00 33.12 ? 56   GLN   B CA    1 
ATOM   9436  C  C     . GLN   B 1  58   ? -31.627 8.688   98.334  1.00 34.39 ? 56   GLN   B C     1 
ATOM   9437  O  O     . GLN   B 1  58   ? -32.054 9.560   97.571  1.00 36.04 ? 56   GLN   B O     1 
ATOM   9438  C  CB    . GLN   B 1  58   ? -29.777 9.181   99.958  1.00 34.17 ? 56   GLN   B CB    1 
ATOM   9439  C  CG    . GLN   B 1  58   ? -28.277 9.337   100.197 1.00 34.11 ? 56   GLN   B CG    1 
ATOM   9440  C  CD    . GLN   B 1  58   ? -27.916 9.299   101.668 1.00 41.71 ? 56   GLN   B CD    1 
ATOM   9441  O  OE1   . GLN   B 1  58   ? -28.071 8.270   102.326 1.00 41.64 ? 56   GLN   B OE1   1 
ATOM   9442  N  NE2   . GLN   B 1  58   ? -27.438 10.422  102.194 1.00 35.58 ? 56   GLN   B NE2   1 
ATOM   9443  N  N     . SER   B 1  59   ? -32.415 7.823   98.970  1.00 39.68 ? 57   SER   B N     1 
ATOM   9444  C  CA    . SER   B 1  59   ? -33.860 7.834   98.795  1.00 40.15 ? 57   SER   B CA    1 
ATOM   9445  C  C     . SER   B 1  59   ? -34.452 9.148   99.296  1.00 41.72 ? 57   SER   B C     1 
ATOM   9446  O  O     . SER   B 1  59   ? -33.831 9.893   100.055 1.00 36.65 ? 57   SER   B O     1 
ATOM   9447  C  CB    . SER   B 1  59   ? -34.489 6.700   99.600  1.00 39.71 ? 57   SER   B CB    1 
ATOM   9448  O  OG    . SER   B 1  59   ? -34.312 6.922   100.991 1.00 42.53 ? 57   SER   B OG    1 
ATOM   9449  N  N     . LYS   B 1  60   ? -35.686 9.425   98.866  1.00 37.36 ? 58   LYS   B N     1 
ATOM   9450  C  CA    . LYS   B 1  60   ? -36.377 10.619  99.344  1.00 40.02 ? 58   LYS   B CA    1 
ATOM   9451  C  C     . LYS   B 1  60   ? -36.547 10.581  100.857 1.00 37.35 ? 58   LYS   B C     1 
ATOM   9452  O  O     . LYS   B 1  60   ? -36.439 11.613  101.527 1.00 39.98 ? 58   LYS   B O     1 
ATOM   9453  C  CB    . LYS   B 1  60   ? -37.740 10.754  98.659  1.00 35.76 ? 58   LYS   B CB    1 
ATOM   9454  N  N     . GLU   B 1  61   ? -36.808 9.395   101.413 1.00 38.93 ? 59   GLU   B N     1 
ATOM   9455  C  CA    . GLU   B 1  61   ? -37.000 9.276   102.855 1.00 36.06 ? 59   GLU   B CA    1 
ATOM   9456  C  C     . GLU   B 1  61   ? -35.736 9.676   103.604 1.00 36.07 ? 59   GLU   B C     1 
ATOM   9457  O  O     . GLU   B 1  61   ? -35.783 10.467  104.553 1.00 41.01 ? 59   GLU   B O     1 
ATOM   9458  C  CB    . GLU   B 1  61   ? -37.408 7.846   103.209 1.00 45.21 ? 59   GLU   B CB    1 
ATOM   9459  N  N     . ILE   B 1  62   ? -34.588 9.146   103.180 1.00 38.55 ? 60   ILE   B N     1 
ATOM   9460  C  CA    . ILE   B 1  62   ? -33.326 9.493   103.826 1.00 35.87 ? 60   ILE   B CA    1 
ATOM   9461  C  C     . ILE   B 1  62   ? -33.008 10.970  103.625 1.00 33.16 ? 60   ILE   B C     1 
ATOM   9462  O  O     . ILE   B 1  62   ? -32.553 11.655  104.551 1.00 39.27 ? 60   ILE   B O     1 
ATOM   9463  C  CB    . ILE   B 1  62   ? -32.197 8.578   103.317 1.00 40.02 ? 60   ILE   B CB    1 
ATOM   9464  C  CG1   . ILE   B 1  62   ? -32.400 7.155   103.837 1.00 43.37 ? 60   ILE   B CG1   1 
ATOM   9465  C  CG2   . ILE   B 1  62   ? -30.832 9.118   103.726 1.00 41.24 ? 60   ILE   B CG2   1 
ATOM   9466  C  CD1   . ILE   B 1  62   ? -31.379 6.170   103.323 1.00 42.86 ? 60   ILE   B CD1   1 
ATOM   9467  N  N     . ARG   B 1  63   ? -33.246 11.484  102.416 1.00 34.90 ? 61   ARG   B N     1 
ATOM   9468  C  CA    . ARG   B 1  63   ? -32.942 12.883  102.133 1.00 34.91 ? 61   ARG   B CA    1 
ATOM   9469  C  C     . ARG   B 1  63   ? -33.797 13.821  102.971 1.00 37.63 ? 61   ARG   B C     1 
ATOM   9470  O  O     . ARG   B 1  63   ? -33.314 14.856  103.444 1.00 39.32 ? 61   ARG   B O     1 
ATOM   9471  C  CB    . ARG   B 1  63   ? -33.112 13.170  100.642 1.00 36.10 ? 61   ARG   B CB    1 
ATOM   9472  C  CG    . ARG   B 1  63   ? -32.056 12.493  99.799  1.00 36.49 ? 61   ARG   B CG    1 
ATOM   9473  C  CD    . ARG   B 1  63   ? -32.120 12.912  98.347  1.00 44.66 ? 61   ARG   B CD    1 
ATOM   9474  N  NE    . ARG   B 1  63   ? -33.257 12.336  97.642  1.00 38.71 ? 61   ARG   B NE    1 
ATOM   9475  C  CZ    . ARG   B 1  63   ? -34.266 13.044  97.153  1.00 46.84 ? 61   ARG   B CZ    1 
ATOM   9476  N  NH1   . ARG   B 1  63   ? -34.329 14.357  97.310  1.00 46.88 ? 61   ARG   B NH1   1 
ATOM   9477  N  NH2   . ARG   B 1  63   ? -35.229 12.422  96.482  1.00 46.59 ? 61   ARG   B NH2   1 
ATOM   9478  N  N     . ASP   B 1  64   ? -35.077 13.488  103.156 1.00 33.98 ? 62   ASP   B N     1 
ATOM   9479  C  CA    . ASP   B 1  64   ? -35.909 14.301  104.034 1.00 35.84 ? 62   ASP   B CA    1 
ATOM   9480  C  C     . ASP   B 1  64   ? -35.438 14.202  105.478 1.00 32.67 ? 62   ASP   B C     1 
ATOM   9481  O  O     . ASP   B 1  64   ? -35.378 15.212  106.186 1.00 38.77 ? 62   ASP   B O     1 
ATOM   9482  C  CB    . ASP   B 1  64   ? -37.375 13.877  103.928 1.00 33.20 ? 62   ASP   B CB    1 
ATOM   9483  C  CG    . ASP   B 1  64   ? -37.978 14.165  102.563 1.00 43.17 ? 62   ASP   B CG    1 
ATOM   9484  O  OD1   . ASP   B 1  64   ? -37.444 15.022  101.830 1.00 43.02 ? 62   ASP   B OD1   1 
ATOM   9485  O  OD2   . ASP   B 1  64   ? -39.009 13.536  102.234 1.00 43.97 ? 62   ASP   B OD2   1 
ATOM   9486  N  N     . ALA   B 1  65   ? -35.107 12.990  105.932 1.00 31.61 ? 63   ALA   B N     1 
ATOM   9487  C  CA    . ALA   B 1  65   ? -34.652 12.810  107.308 1.00 35.16 ? 63   ALA   B CA    1 
ATOM   9488  C  C     . ALA   B 1  65   ? -33.338 13.542  107.556 1.00 38.96 ? 63   ALA   B C     1 
ATOM   9489  O  O     . ALA   B 1  65   ? -33.137 14.127  108.628 1.00 40.33 ? 63   ALA   B O     1 
ATOM   9490  C  CB    . ALA   B 1  65   ? -34.519 11.321  107.630 1.00 34.41 ? 63   ALA   B CB    1 
ATOM   9491  N  N     . ALA   B 1  66   ? -32.436 13.533  106.573 1.00 34.41 ? 64   ALA   B N     1 
ATOM   9492  C  CA    . ALA   B 1  66   ? -31.169 14.242  106.734 1.00 33.77 ? 64   ALA   B CA    1 
ATOM   9493  C  C     . ALA   B 1  66   ? -31.370 15.751  106.691 1.00 31.34 ? 64   ALA   B C     1 
ATOM   9494  O  O     . ALA   B 1  66   ? -30.690 16.495  107.404 1.00 35.25 ? 64   ALA   B O     1 
ATOM   9495  C  CB    . ALA   B 1  66   ? -30.177 13.790  105.665 1.00 32.23 ? 64   ALA   B CB    1 
ATOM   9496  N  N     . ALA   B 1  67   ? -32.317 16.225  105.882 1.00 35.32 ? 65   ALA   B N     1 
ATOM   9497  C  CA    . ALA   B 1  67   ? -32.593 17.656  105.857 1.00 32.85 ? 65   ALA   B CA    1 
ATOM   9498  C  C     . ALA   B 1  67   ? -33.135 18.131  107.200 1.00 37.34 ? 65   ALA   B C     1 
ATOM   9499  O  O     . ALA   B 1  67   ? -32.783 19.221  107.669 1.00 35.78 ? 65   ALA   B O     1 
ATOM   9500  C  CB    . ALA   B 1  67   ? -33.572 17.982  104.729 1.00 36.70 ? 65   ALA   B CB    1 
ATOM   9501  N  N     . SER   B 1  68   ? -33.988 17.320  107.834 1.00 38.56 ? 66   SER   B N     1 
ATOM   9502  C  CA    . SER   B 1  68   ? -34.497 17.658  109.161 1.00 35.79 ? 66   SER   B CA    1 
ATOM   9503  C  C     . SER   B 1  68   ? -33.384 17.632  110.203 1.00 41.04 ? 66   SER   B C     1 
ATOM   9504  O  O     . SER   B 1  68   ? -33.302 18.524  111.054 1.00 41.17 ? 66   SER   B O     1 
ATOM   9505  C  CB    . SER   B 1  68   ? -35.623 16.699  109.549 1.00 43.45 ? 66   SER   B CB    1 
ATOM   9506  N  N     . THR   B 1  69   ? -32.517 16.618  110.149 1.00 35.05 ? 67   THR   B N     1 
ATOM   9507  C  CA    . THR   B 1  69   ? -31.411 16.546  111.098 1.00 35.45 ? 67   THR   B CA    1 
ATOM   9508  C  C     . THR   B 1  69   ? -30.454 17.714  110.915 1.00 36.57 ? 67   THR   B C     1 
ATOM   9509  O  O     . THR   B 1  69   ? -29.994 18.308  111.899 1.00 35.57 ? 67   THR   B O     1 
ATOM   9510  C  CB    . THR   B 1  69   ? -30.679 15.213  110.951 1.00 36.41 ? 67   THR   B CB    1 
ATOM   9511  O  OG1   . THR   B 1  69   ? -31.521 14.151  111.413 1.00 38.27 ? 67   THR   B OG1   1 
ATOM   9512  C  CG2   . THR   B 1  69   ? -29.378 15.215  111.759 1.00 34.20 ? 67   THR   B CG2   1 
ATOM   9513  N  N     . ALA   B 1  70   ? -30.135 18.055  109.662 1.00 32.39 ? 68   ALA   B N     1 
ATOM   9514  C  CA    . ALA   B 1  70   ? -29.288 19.214  109.410 1.00 35.70 ? 68   ALA   B CA    1 
ATOM   9515  C  C     . ALA   B 1  70   ? -29.924 20.487  109.952 1.00 34.60 ? 68   ALA   B C     1 
ATOM   9516  O  O     . ALA   B 1  70   ? -29.243 21.315  110.564 1.00 35.03 ? 68   ALA   B O     1 
ATOM   9517  C  CB    . ALA   B 1  70   ? -28.979 19.343  107.915 1.00 33.01 ? 68   ALA   B CB    1 
ATOM   9518  N  N     . ARG   B 1  71   ? -31.237 20.651  109.750 1.00 40.76 ? 69   ARG   B N     1 
ATOM   9519  C  CA    A ARG   B 1  71   ? -31.937 21.817  110.285 0.62 40.22 ? 69   ARG   B CA    1 
ATOM   9520  C  CA    B ARG   B 1  71   ? -31.914 21.828  110.283 0.38 40.17 ? 69   ARG   B CA    1 
ATOM   9521  C  C     . ARG   B 1  71   ? -31.815 21.878  111.802 1.00 31.34 ? 69   ARG   B C     1 
ATOM   9522  O  O     . ARG   B 1  71   ? -31.511 22.931  112.372 1.00 37.57 ? 69   ARG   B O     1 
ATOM   9523  C  CB    A ARG   B 1  71   ? -33.409 21.770  109.869 0.62 42.15 ? 69   ARG   B CB    1 
ATOM   9524  C  CB    B ARG   B 1  71   ? -33.372 21.868  109.817 0.38 42.10 ? 69   ARG   B CB    1 
ATOM   9525  C  CG    A ARG   B 1  71   ? -34.318 22.694  110.671 0.62 41.20 ? 69   ARG   B CG    1 
ATOM   9526  C  CG    B ARG   B 1  71   ? -34.168 23.033  110.390 0.38 41.55 ? 69   ARG   B CG    1 
ATOM   9527  C  CD    A ARG   B 1  71   ? -34.722 23.925  109.871 0.62 43.44 ? 69   ARG   B CD    1 
ATOM   9528  C  CD    B ARG   B 1  71   ? -35.526 23.195  109.713 0.38 41.38 ? 69   ARG   B CD    1 
ATOM   9529  N  NE    A ARG   B 1  71   ? -35.508 23.570  108.695 0.62 41.33 ? 69   ARG   B NE    1 
ATOM   9530  N  NE    B ARG   B 1  71   ? -35.434 23.943  108.465 0.38 42.78 ? 69   ARG   B NE    1 
ATOM   9531  C  CZ    A ARG   B 1  71   ? -35.808 24.410  107.714 0.62 44.37 ? 69   ARG   B CZ    1 
ATOM   9532  C  CZ    B ARG   B 1  71   ? -35.392 25.267  108.387 0.38 45.50 ? 69   ARG   B CZ    1 
ATOM   9533  N  NH1   A ARG   B 1  71   ? -35.429 25.677  107.747 0.62 46.44 ? 69   ARG   B NH1   1 
ATOM   9534  N  NH1   B ARG   B 1  71   ? -35.426 26.024  109.472 0.38 41.56 ? 69   ARG   B NH1   1 
ATOM   9535  N  NH2   A ARG   B 1  71   ? -36.498 23.964  106.668 0.62 44.32 ? 69   ARG   B NH2   1 
ATOM   9536  N  NH2   B ARG   B 1  71   ? -35.310 25.845  107.192 0.38 45.72 ? 69   ARG   B NH2   1 
ATOM   9537  N  N     . LYS   B 1  72   ? -32.048 20.745  112.471 1.00 34.91 ? 70   LYS   B N     1 
ATOM   9538  C  CA    . LYS   B 1  72   ? -31.941 20.696  113.926 1.00 35.39 ? 70   LYS   B CA    1 
ATOM   9539  C  C     . LYS   B 1  72   ? -30.544 21.091  114.391 1.00 37.66 ? 70   LYS   B C     1 
ATOM   9540  O  O     . LYS   B 1  72   ? -30.392 21.841  115.362 1.00 36.44 ? 70   LYS   B O     1 
ATOM   9541  C  CB    . LYS   B 1  72   ? -32.309 19.296  114.423 1.00 37.23 ? 70   LYS   B CB    1 
ATOM   9542  C  CG    . LYS   B 1  72   ? -32.257 19.098  115.939 1.00 39.00 ? 70   LYS   B CG    1 
ATOM   9543  C  CD    . LYS   B 1  72   ? -32.801 17.717  116.314 1.00 37.25 ? 70   LYS   B CD    1 
ATOM   9544  C  CE    . LYS   B 1  72   ? -32.624 17.402  117.791 1.00 43.11 ? 70   LYS   B CE    1 
ATOM   9545  N  NZ    . LYS   B 1  72   ? -33.422 18.289  118.681 1.00 40.09 ? 70   LYS   B NZ    1 
ATOM   9546  N  N     . LEU   B 1  73   ? -29.509 20.613  113.699 1.00 36.47 ? 71   LEU   B N     1 
ATOM   9547  C  CA    . LEU   B 1  73   ? -28.149 20.976  114.081 1.00 35.26 ? 71   LEU   B CA    1 
ATOM   9548  C  C     . LEU   B 1  73   ? -27.888 22.461  113.863 1.00 31.65 ? 71   LEU   B C     1 
ATOM   9549  O  O     . LEU   B 1  73   ? -27.254 23.111  114.701 1.00 35.01 ? 71   LEU   B O     1 
ATOM   9550  C  CB    . LEU   B 1  73   ? -27.145 20.139  113.291 1.00 30.66 ? 71   LEU   B CB    1 
ATOM   9551  C  CG    . LEU   B 1  73   ? -27.224 18.625  113.468 1.00 29.22 ? 71   LEU   B CG    1 
ATOM   9552  C  CD1   . LEU   B 1  73   ? -26.387 17.929  112.394 1.00 31.16 ? 71   LEU   B CD1   1 
ATOM   9553  C  CD2   . LEU   B 1  73   ? -26.767 18.221  114.858 1.00 33.61 ? 71   LEU   B CD2   1 
ATOM   9554  N  N     . ILE   B 1  74   ? -28.359 23.009  112.740 1.00 33.72 ? 72   ILE   B N     1 
ATOM   9555  C  CA    . ILE   B 1  74   ? -28.045 24.388  112.380 1.00 33.69 ? 72   ILE   B CA    1 
ATOM   9556  C  C     . ILE   B 1  74   ? -28.787 25.367  113.282 1.00 40.69 ? 72   ILE   B C     1 
ATOM   9557  O  O     . ILE   B 1  74   ? -28.224 26.378  113.724 1.00 36.11 ? 72   ILE   B O     1 
ATOM   9558  C  CB    . ILE   B 1  74   ? -28.343 24.631  110.890 1.00 36.17 ? 72   ILE   B CB    1 
ATOM   9559  C  CG1   . ILE   B 1  74   ? -27.331 23.876  110.021 1.00 36.89 ? 72   ILE   B CG1   1 
ATOM   9560  C  CG2   . ILE   B 1  74   ? -28.303 26.117  110.568 1.00 37.05 ? 72   ILE   B CG2   1 
ATOM   9561  C  CD1   . ILE   B 1  74   ? -27.778 23.696  108.596 1.00 36.63 ? 72   ILE   B CD1   1 
ATOM   9562  N  N     . GLU   B 1  75   ? -30.062 25.093  113.554 1.00 40.31 ? 73   GLU   B N     1 
ATOM   9563  C  CA    . GLU   B 1  75   ? -30.798 25.909  114.514 1.00 42.13 ? 73   GLU   B CA    1 
ATOM   9564  C  C     . GLU   B 1  75   ? -30.116 25.897  115.877 1.00 42.20 ? 73   GLU   B C     1 
ATOM   9565  O  O     . GLU   B 1  75   ? -29.945 26.951  116.502 1.00 42.83 ? 73   GLU   B O     1 
ATOM   9566  C  CB    . GLU   B 1  75   ? -32.248 25.433  114.595 1.00 41.31 ? 73   GLU   B CB    1 
ATOM   9567  C  CG    . GLU   B 1  75   ? -33.037 25.748  113.335 1.00 46.50 ? 73   GLU   B CG    1 
ATOM   9568  C  CD    . GLU   B 1  75   ? -34.420 25.129  113.313 1.00 53.64 ? 73   GLU   B CD    1 
ATOM   9569  O  OE1   . GLU   B 1  75   ? -34.653 24.146  114.050 1.00 56.40 ? 73   GLU   B OE1   1 
ATOM   9570  O  OE2   . GLU   B 1  75   ? -35.273 25.626  112.547 1.00 48.94 ? 73   GLU   B OE2   1 
ATOM   9571  N  N     . ALA   B 1  76   ? -29.686 24.717  116.333 1.00 36.05 ? 74   ALA   B N     1 
ATOM   9572  C  CA    . ALA   B 1  76   ? -28.905 24.630  117.565 1.00 41.69 ? 74   ALA   B CA    1 
ATOM   9573  C  C     . ALA   B 1  76   ? -27.630 25.464  117.484 1.00 41.84 ? 74   ALA   B C     1 
ATOM   9574  O  O     . ALA   B 1  76   ? -27.283 26.176  118.434 1.00 42.73 ? 74   ALA   B O     1 
ATOM   9575  C  CB    . ALA   B 1  76   ? -28.580 23.170  117.878 1.00 40.43 ? 74   ALA   B CB    1 
ATOM   9576  N  N     . LEU   B 1  77   ? -26.915 25.389  116.357 1.00 40.20 ? 75   LEU   B N     1 
ATOM   9577  C  CA    . LEU   B 1  77   ? -25.703 26.185  116.201 1.00 42.68 ? 75   LEU   B CA    1 
ATOM   9578  C  C     . LEU   B 1  77   ? -26.017 27.675  116.247 1.00 39.74 ? 75   LEU   B C     1 
ATOM   9579  O  O     . LEU   B 1  77   ? -25.343 28.444  116.945 1.00 41.35 ? 75   LEU   B O     1 
ATOM   9580  C  CB    . LEU   B 1  77   ? -24.997 25.823  114.891 1.00 36.09 ? 75   LEU   B CB    1 
ATOM   9581  C  CG    . LEU   B 1  77   ? -24.240 24.497  114.847 1.00 37.94 ? 75   LEU   B CG    1 
ATOM   9582  C  CD1   . LEU   B 1  77   ? -23.725 24.223  113.437 1.00 31.98 ? 75   LEU   B CD1   1 
ATOM   9583  C  CD2   . LEU   B 1  77   ? -23.088 24.532  115.826 1.00 37.18 ? 75   LEU   B CD2   1 
ATOM   9584  N  N     . ARG   B 1  78   ? -27.030 28.106  115.494 1.00 37.62 ? 76   ARG   B N     1 
ATOM   9585  C  CA    . ARG   B 1  78   ? -27.338 29.529  115.428 1.00 39.28 ? 76   ARG   B CA    1 
ATOM   9586  C  C     . ARG   B 1  78   ? -27.981 30.043  116.705 1.00 37.54 ? 76   ARG   B C     1 
ATOM   9587  O  O     . ARG   B 1  78   ? -27.997 31.257  116.931 1.00 41.22 ? 76   ARG   B O     1 
ATOM   9588  C  CB    . ARG   B 1  78   ? -28.230 29.821  114.226 1.00 44.77 ? 76   ARG   B CB    1 
ATOM   9589  C  CG    . ARG   B 1  78   ? -27.540 29.518  112.915 1.00 40.23 ? 76   ARG   B CG    1 
ATOM   9590  C  CD    . ARG   B 1  78   ? -28.306 30.060  111.733 1.00 42.63 ? 76   ARG   B CD    1 
ATOM   9591  N  NE    . ARG   B 1  78   ? -27.387 30.557  110.718 1.00 39.50 ? 76   ARG   B NE    1 
ATOM   9592  C  CZ    . ARG   B 1  78   ? -27.745 30.945  109.503 1.00 46.67 ? 76   ARG   B CZ    1 
ATOM   9593  N  NH1   . ARG   B 1  78   ? -28.999 30.852  109.090 1.00 46.76 ? 76   ARG   B NH1   1 
ATOM   9594  N  NH2   . ARG   B 1  78   ? -26.823 31.441  108.683 1.00 44.88 ? 76   ARG   B NH2   1 
ATOM   9595  N  N     . GLY   B 1  79   ? -28.500 29.151  117.541 1.00 39.19 ? 77   GLY   B N     1 
ATOM   9596  C  CA    . GLY   B 1  79   ? -29.133 29.574  118.774 1.00 41.69 ? 77   GLY   B CA    1 
ATOM   9597  C  C     . GLY   B 1  79   ? -28.190 29.909  119.906 1.00 44.94 ? 77   GLY   B C     1 
ATOM   9598  O  O     . GLY   B 1  79   ? -28.619 30.544  120.874 1.00 41.81 ? 77   GLY   B O     1 
ATOM   9599  N  N     . LYS   B 1  80   ? -26.923 29.516  119.810 1.00 49.22 ? 78   LYS   B N     1 
ATOM   9600  C  CA    . LYS   B 1  80   ? -25.997 29.670  120.929 1.00 46.74 ? 78   LYS   B CA    1 
ATOM   9601  C  C     . LYS   B 1  80   ? -24.755 30.486  120.575 1.00 41.76 ? 78   LYS   B C     1 
ATOM   9602  O  O     . LYS   B 1  80   ? -24.566 30.893  119.426 1.00 46.82 ? 78   LYS   B O     1 
ATOM   9603  C  CB    . LYS   B 1  80   ? -25.602 28.294  121.481 1.00 48.80 ? 78   LYS   B CB    1 
ATOM   9604  C  CG    . LYS   B 1  80   ? -24.931 27.384  120.456 1.00 42.58 ? 78   LYS   B CG    1 
ATOM   9605  C  CD    . LYS   B 1  80   ? -24.905 25.927  120.910 1.00 46.56 ? 78   LYS   B CD    1 
ATOM   9606  C  CE    . LYS   B 1  80   ? -24.112 25.053  119.931 1.00 37.54 ? 78   LYS   B CE    1 
ATOM   9607  N  NZ    . LYS   B 1  80   ? -24.133 23.597  120.288 1.00 38.76 ? 78   LYS   B NZ    1 
ATOM   9608  N  N     . GLY   B 1  85   ? -15.251 35.855  121.264 1.00 41.75 ? 83   GLY   B N     1 
ATOM   9609  C  CA    . GLY   B 1  85   ? -14.486 36.670  122.188 1.00 41.31 ? 83   GLY   B CA    1 
ATOM   9610  C  C     . GLY   B 1  85   ? -13.958 37.947  121.562 1.00 37.96 ? 83   GLY   B C     1 
ATOM   9611  O  O     . GLY   B 1  85   ? -14.016 39.018  122.170 1.00 37.62 ? 83   GLY   B O     1 
ATOM   9612  N  N     . VAL   B 1  86   ? -13.437 37.832  120.340 1.00 41.33 ? 84   VAL   B N     1 
ATOM   9613  C  CA    . VAL   B 1  86   ? -12.895 39.001  119.656 1.00 41.70 ? 84   VAL   B CA    1 
ATOM   9614  C  C     . VAL   B 1  86   ? -14.002 39.991  119.321 1.00 37.63 ? 84   VAL   B C     1 
ATOM   9615  O  O     . VAL   B 1  86   ? -13.819 41.209  119.437 1.00 37.28 ? 84   VAL   B O     1 
ATOM   9616  C  CB    . VAL   B 1  86   ? -12.074 38.579  118.424 1.00 40.40 ? 84   VAL   B CB    1 
ATOM   9617  C  CG1   . VAL   B 1  86   ? -11.853 39.758  117.487 1.00 42.17 ? 84   VAL   B CG1   1 
ATOM   9618  C  CG2   . VAL   B 1  86   ? -10.740 38.020  118.864 1.00 43.10 ? 84   VAL   B CG2   1 
ATOM   9619  N  N     . GLU   B 1  87   ? -15.174 39.489  118.925 1.00 41.42 ? 85   GLU   B N     1 
ATOM   9620  C  CA    . GLU   B 1  87   ? -16.303 40.375  118.657 1.00 41.48 ? 85   GLU   B CA    1 
ATOM   9621  C  C     . GLU   B 1  87   ? -16.668 41.192  119.891 1.00 36.76 ? 85   GLU   B C     1 
ATOM   9622  O  O     . GLU   B 1  87   ? -16.927 42.397  119.794 1.00 39.21 ? 85   GLU   B O     1 
ATOM   9623  C  CB    . GLU   B 1  87   ? -17.507 39.563  118.177 1.00 50.01 ? 85   GLU   B CB    1 
ATOM   9624  N  N     . GLY   B 1  88   ? -16.689 40.556  121.064 1.00 38.19 ? 86   GLY   B N     1 
ATOM   9625  C  CA    . GLY   B 1  88   ? -17.037 41.277  122.277 1.00 38.08 ? 86   GLY   B CA    1 
ATOM   9626  C  C     . GLY   B 1  88   ? -16.006 42.325  122.645 1.00 31.59 ? 86   GLY   B C     1 
ATOM   9627  O  O     . GLY   B 1  88   ? -16.347 43.396  123.154 1.00 34.18 ? 86   GLY   B O     1 
ATOM   9628  N  N     . LEU   B 1  89   ? -14.729 42.033  122.389 1.00 35.40 ? 87   LEU   B N     1 
ATOM   9629  C  CA    . LEU   B 1  89   ? -13.677 43.013  122.639 1.00 35.69 ? 87   LEU   B CA    1 
ATOM   9630  C  C     . LEU   B 1  89   ? -13.805 44.200  121.693 1.00 26.98 ? 87   LEU   B C     1 
ATOM   9631  O  O     . LEU   B 1  89   ? -13.717 45.357  122.120 1.00 29.60 ? 87   LEU   B O     1 
ATOM   9632  C  CB    . LEU   B 1  89   ? -12.318 42.338  122.477 1.00 35.03 ? 87   LEU   B CB    1 
ATOM   9633  C  CG    . LEU   B 1  89   ? -11.073 43.221  122.465 1.00 38.54 ? 87   LEU   B CG    1 
ATOM   9634  C  CD1   . LEU   B 1  89   ? -10.871 43.858  123.816 1.00 38.84 ? 87   LEU   B CD1   1 
ATOM   9635  C  CD2   . LEU   B 1  89   ? -9.854  42.400  122.058 1.00 40.87 ? 87   LEU   B CD2   1 
ATOM   9636  N  N     . VAL   B 1  90   ? -14.038 43.924  120.409 1.00 28.96 ? 88   VAL   B N     1 
ATOM   9637  C  CA    . VAL   B 1  90   ? -14.222 44.981  119.422 1.00 31.11 ? 88   VAL   B CA    1 
ATOM   9638  C  C     . VAL   B 1  90   ? -15.427 45.838  119.778 1.00 35.21 ? 88   VAL   B C     1 
ATOM   9639  O  O     . VAL   B 1  90   ? -15.386 47.070  119.667 1.00 32.55 ? 88   VAL   B O     1 
ATOM   9640  C  CB    . VAL   B 1  90   ? -14.333 44.371  118.012 1.00 32.12 ? 88   VAL   B CB    1 
ATOM   9641  C  CG1   . VAL   B 1  90   ? -14.802 45.406  116.998 1.00 33.81 ? 88   VAL   B CG1   1 
ATOM   9642  C  CG2   . VAL   B 1  90   ? -13.002 43.769  117.583 1.00 29.16 ? 88   VAL   B CG2   1 
ATOM   9643  N  N     . GLN   B 1  91   ? -16.512 45.205  120.233 1.00 36.22 ? 89   GLN   B N     1 
ATOM   9644  C  CA    . GLN   B 1  91   ? -17.703 45.962  120.608 1.00 37.41 ? 89   GLN   B CA    1 
ATOM   9645  C  C     . GLN   B 1  91   ? -17.467 46.792  121.865 1.00 35.22 ? 89   GLN   B C     1 
ATOM   9646  O  O     . GLN   B 1  91   ? -17.842 47.969  121.918 1.00 37.03 ? 89   GLN   B O     1 
ATOM   9647  C  CB    . GLN   B 1  91   ? -18.894 45.018  120.786 1.00 43.37 ? 89   GLN   B CB    1 
ATOM   9648  N  N     . GLU   B 1  92   ? -16.825 46.208  122.879 1.00 32.70 ? 90   GLU   B N     1 
ATOM   9649  C  CA    . GLU   B 1  92   ? -16.650 46.912  124.145 1.00 32.60 ? 90   GLU   B CA    1 
ATOM   9650  C  C     . GLU   B 1  92   ? -15.806 48.169  123.981 1.00 32.19 ? 90   GLU   B C     1 
ATOM   9651  O  O     . GLU   B 1  92   ? -16.108 49.210  124.573 1.00 35.53 ? 90   GLU   B O     1 
ATOM   9652  C  CB    . GLU   B 1  92   ? -16.036 45.985  125.194 1.00 38.25 ? 90   GLU   B CB    1 
ATOM   9653  C  CG    . GLU   B 1  92   ? -15.774 46.688  126.514 1.00 39.98 ? 90   GLU   B CG    1 
ATOM   9654  C  CD    . GLU   B 1  92   ? -15.209 45.777  127.586 1.00 39.99 ? 90   GLU   B CD    1 
ATOM   9655  O  OE1   . GLU   B 1  92   ? -14.991 44.576  127.313 1.00 43.89 ? 90   GLU   B OE1   1 
ATOM   9656  O  OE2   . GLU   B 1  92   ? -14.985 46.275  128.708 1.00 39.18 ? 90   GLU   B OE2   1 
ATOM   9657  N  N     . TYR   B 1  93   ? -14.747 48.100  123.179 1.00 32.30 ? 91   TYR   B N     1 
ATOM   9658  C  CA    . TYR   B 1  93   ? -13.864 49.243  123.005 1.00 32.83 ? 91   TYR   B CA    1 
ATOM   9659  C  C     . TYR   B 1  93   ? -14.095 49.977  121.696 1.00 32.02 ? 91   TYR   B C     1 
ATOM   9660  O  O     . TYR   B 1  93   ? -13.289 50.841  121.337 1.00 30.40 ? 91   TYR   B O     1 
ATOM   9661  C  CB    . TYR   B 1  93   ? -12.405 48.827  123.170 1.00 27.98 ? 91   TYR   B CB    1 
ATOM   9662  C  CG    . TYR   B 1  93   ? -12.133 48.449  124.595 1.00 28.22 ? 91   TYR   B CG    1 
ATOM   9663  C  CD1   . TYR   B 1  93   ? -11.831 49.419  125.534 1.00 28.67 ? 91   TYR   B CD1   1 
ATOM   9664  C  CD2   . TYR   B 1  93   ? -12.225 47.129  125.013 1.00 29.55 ? 91   TYR   B CD2   1 
ATOM   9665  C  CE1   . TYR   B 1  93   ? -11.601 49.092  126.848 1.00 31.22 ? 91   TYR   B CE1   1 
ATOM   9666  C  CE2   . TYR   B 1  93   ? -12.003 46.790  126.338 1.00 34.71 ? 91   TYR   B CE2   1 
ATOM   9667  C  CZ    . TYR   B 1  93   ? -11.687 47.778  127.245 1.00 32.14 ? 91   TYR   B CZ    1 
ATOM   9668  O  OH    . TYR   B 1  93   ? -11.462 47.459  128.564 1.00 33.71 ? 91   TYR   B OH    1 
ATOM   9669  N  N     . SER   B 1  94   ? -15.184 49.666  120.994 1.00 26.85 ? 92   SER   B N     1 
ATOM   9670  C  CA    . SER   B 1  94   ? -15.541 50.338  119.750 1.00 28.38 ? 92   SER   B CA    1 
ATOM   9671  C  C     . SER   B 1  94   ? -14.362 50.358  118.784 1.00 30.22 ? 92   SER   B C     1 
ATOM   9672  O  O     . SER   B 1  94   ? -14.013 51.388  118.202 1.00 30.00 ? 92   SER   B O     1 
ATOM   9673  C  CB    . SER   B 1  94   ? -16.079 51.742  120.013 1.00 28.14 ? 92   SER   B CB    1 
ATOM   9674  O  OG    . SER   B 1  94   ? -17.179 51.700  120.907 1.00 34.20 ? 92   SER   B OG    1 
ATOM   9675  N  N     . LEU   B 1  95   ? -13.729 49.201  118.635 1.00 24.68 ? 93   LEU   B N     1 
ATOM   9676  C  CA    . LEU   B 1  95   ? -12.565 49.100  117.775 1.00 23.37 ? 93   LEU   B CA    1 
ATOM   9677  C  C     . LEU   B 1  95   ? -12.980 49.031  116.316 1.00 26.43 ? 93   LEU   B C     1 
ATOM   9678  O  O     . LEU   B 1  95   ? -13.960 48.374  115.957 1.00 26.79 ? 93   LEU   B O     1 
ATOM   9679  C  CB    . LEU   B 1  95   ? -11.764 47.846  118.115 1.00 24.09 ? 93   LEU   B CB    1 
ATOM   9680  C  CG    . LEU   B 1  95   ? -11.268 47.770  119.554 1.00 25.42 ? 93   LEU   B CG    1 
ATOM   9681  C  CD1   . LEU   B 1  95   ? -10.323 46.596  119.726 1.00 27.92 ? 93   LEU   B CD1   1 
ATOM   9682  C  CD2   . LEU   B 1  95   ? -10.595 49.078  119.943 1.00 25.55 ? 93   LEU   B CD2   1 
ATOM   9683  N  N     . SER   B 1  96   ? -12.222 49.712  115.469 1.00 23.83 ? 94   SER   B N     1 
ATOM   9684  C  CA    . SER   B 1  96   ? -12.300 49.423  114.054 1.00 23.46 ? 94   SER   B CA    1 
ATOM   9685  C  C     . SER   B 1  96   ? -11.619 48.084  113.786 1.00 24.06 ? 94   SER   B C     1 
ATOM   9686  O  O     . SER   B 1  96   ? -10.935 47.527  114.653 1.00 22.73 ? 94   SER   B O     1 
ATOM   9687  C  CB    . SER   B 1  96   ? -11.566 50.502  113.269 1.00 25.01 ? 94   SER   B CB    1 
ATOM   9688  O  OG    . SER   B 1  96   ? -10.176 50.417  113.530 1.00 21.14 ? 94   SER   B OG    1 
ATOM   9689  N  N     . SER   B 1  97   ? -11.809 47.562  112.571 1.00 22.18 ? 95   SER   B N     1 
ATOM   9690  C  CA    . SER   B 1  97   ? -11.149 46.316  112.195 1.00 21.05 ? 95   SER   B CA    1 
ATOM   9691  C  C     . SER   B 1  97   ? -9.638  46.442  112.328 1.00 20.05 ? 95   SER   B C     1 
ATOM   9692  O  O     . SER   B 1  97   ? -8.984  45.580  112.921 1.00 21.95 ? 95   SER   B O     1 
ATOM   9693  C  CB    . SER   B 1  97   ? -11.534 45.911  110.772 1.00 27.67 ? 95   SER   B CB    1 
ATOM   9694  O  OG    . SER   B 1  97   ? -12.906 45.553  110.733 1.00 34.89 ? 95   SER   B OG    1 
ATOM   9695  N  N     . GLN   B 1  98   ? -9.068  47.522  111.788 1.00 20.80 ? 96   GLN   B N     1 
ATOM   9696  C  CA    . GLN   B 1  98   ? -7.619  47.693  111.849 1.00 21.23 ? 96   GLN   B CA    1 
ATOM   9697  C  C     . GLN   B 1  98   ? -7.147  47.825  113.292 1.00 18.84 ? 96   GLN   B C     1 
ATOM   9698  O  O     . GLN   B 1  98   ? -6.055  47.355  113.641 1.00 20.38 ? 96   GLN   B O     1 
ATOM   9699  C  CB    . GLN   B 1  98   ? -7.187  48.905  111.017 1.00 20.59 ? 96   GLN   B CB    1 
ATOM   9700  C  CG    . GLN   B 1  98   ? -7.251  48.684  109.522 1.00 20.72 ? 96   GLN   B CG    1 
ATOM   9701  C  CD    . GLN   B 1  98   ? -6.269  47.634  109.070 1.00 21.99 ? 96   GLN   B CD    1 
ATOM   9702  O  OE1   . GLN   B 1  98   ? -6.545  46.436  109.144 1.00 25.63 ? 96   GLN   B OE1   1 
ATOM   9703  N  NE2   . GLN   B 1  98   ? -5.102  48.074  108.607 1.00 22.03 ? 96   GLN   B NE2   1 
ATOM   9704  N  N     . GLU   B 1  99   ? -7.951  48.464  114.141 1.00 18.90 ? 97   GLU   B N     1 
ATOM   9705  C  CA    . GLU   B 1  99   ? -7.594  48.557  115.552 1.00 19.23 ? 97   GLU   B CA    1 
ATOM   9706  C  C     . GLU   B 1  99   ? -7.628  47.189  116.210 1.00 24.66 ? 97   GLU   B C     1 
ATOM   9707  O  O     . GLU   B 1  99   ? -6.741  46.855  117.002 1.00 21.58 ? 97   GLU   B O     1 
ATOM   9708  C  CB    . GLU   B 1  99   ? -8.519  49.536  116.265 1.00 22.54 ? 97   GLU   B CB    1 
ATOM   9709  C  CG    . GLU   B 1  99   ? -8.201  50.984  115.948 1.00 21.06 ? 97   GLU   B CG    1 
ATOM   9710  C  CD    . GLU   B 1  99   ? -9.297  51.917  116.407 1.00 22.35 ? 97   GLU   B CD    1 
ATOM   9711  O  OE1   . GLU   B 1  99   ? -10.308 51.422  116.950 1.00 23.46 ? 97   GLU   B OE1   1 
ATOM   9712  O  OE2   . GLU   B 1  99   ? -9.150  53.143  116.251 1.00 23.45 ? 97   GLU   B OE2   1 
ATOM   9713  N  N     . GLY   B 1  100  ? -8.631  46.378  115.876 1.00 21.07 ? 98   GLY   B N     1 
ATOM   9714  C  CA    . GLY   B 1  100  ? -8.675  45.024  116.397 1.00 22.19 ? 98   GLY   B CA    1 
ATOM   9715  C  C     . GLY   B 1  100  ? -7.467  44.211  115.981 1.00 22.39 ? 98   GLY   B C     1 
ATOM   9716  O  O     . GLY   B 1  100  ? -6.871  43.507  116.799 1.00 22.23 ? 98   GLY   B O     1 
ATOM   9717  N  N     . VAL   B 1  101  ? -7.075  44.320  114.708 1.00 19.81 ? 99   VAL   B N     1 
ATOM   9718  C  CA    . VAL   B 1  101  ? -5.899  43.600  114.227 1.00 19.06 ? 99   VAL   B CA    1 
ATOM   9719  C  C     . VAL   B 1  101  ? -4.650  44.107  114.932 1.00 20.09 ? 99   VAL   B C     1 
ATOM   9720  O  O     . VAL   B 1  101  ? -3.821  43.324  115.418 1.00 20.22 ? 99   VAL   B O     1 
ATOM   9721  C  CB    . VAL   B 1  101  ? -5.775  43.738  112.698 1.00 19.45 ? 99   VAL   B CB    1 
ATOM   9722  C  CG1   . VAL   B 1  101  ? -4.464  43.148  112.214 1.00 21.44 ? 99   VAL   B CG1   1 
ATOM   9723  C  CG2   . VAL   B 1  101  ? -6.943  43.066  112.023 1.00 21.19 ? 99   VAL   B CG2   1 
ATOM   9724  N  N     . ALA   B 1  102  ? -4.489  45.429  114.974 1.00 19.28 ? 100  ALA   B N     1 
ATOM   9725  C  CA    . ALA   B 1  102  ? -3.305  46.011  115.598 1.00 21.26 ? 100  ALA   B CA    1 
ATOM   9726  C  C     . ALA   B 1  102  ? -3.207  45.605  117.059 1.00 20.16 ? 100  ALA   B C     1 
ATOM   9727  O  O     . ALA   B 1  102  ? -2.113  45.320  117.563 1.00 20.64 ? 100  ALA   B O     1 
ATOM   9728  C  CB    . ALA   B 1  102  ? -3.352  47.535  115.478 1.00 20.08 ? 100  ALA   B CB    1 
ATOM   9729  N  N     . LEU   B 1  103  ? -4.345  45.572  117.755 1.00 18.56 ? 101  LEU   B N     1 
ATOM   9730  C  CA    . LEU   B 1  103  ? -4.342  45.197  119.162 1.00 19.27 ? 101  LEU   B CA    1 
ATOM   9731  C  C     . LEU   B 1  103  ? -3.883  43.759  119.341 1.00 23.41 ? 101  LEU   B C     1 
ATOM   9732  O  O     . LEU   B 1  103  ? -3.089  43.459  120.245 1.00 23.14 ? 101  LEU   B O     1 
ATOM   9733  C  CB    . LEU   B 1  103  ? -5.745  45.375  119.732 1.00 21.26 ? 101  LEU   B CB    1 
ATOM   9734  C  CG    . LEU   B 1  103  ? -5.931  44.921  121.166 1.00 22.93 ? 101  LEU   B CG    1 
ATOM   9735  C  CD1   . LEU   B 1  103  ? -5.066  45.774  122.075 1.00 26.35 ? 101  LEU   B CD1   1 
ATOM   9736  C  CD2   . LEU   B 1  103  ? -7.398  45.035  121.545 1.00 22.93 ? 101  LEU   B CD2   1 
ATOM   9737  N  N     . MET   B 1  104  ? -4.372  42.854  118.497 1.00 20.28 ? 102  MET   B N     1 
ATOM   9738  C  CA    . MET   B 1  104  ? -3.970  41.458  118.630 1.00 22.85 ? 102  MET   B CA    1 
ATOM   9739  C  C     . MET   B 1  104  ? -2.494  41.286  118.317 1.00 22.24 ? 102  MET   B C     1 
ATOM   9740  O  O     . MET   B 1  104  ? -1.812  40.476  118.951 1.00 23.44 ? 102  MET   B O     1 
ATOM   9741  C  CB    . MET   B 1  104  ? -4.839  40.559  117.752 1.00 22.92 ? 102  MET   B CB    1 
ATOM   9742  C  CG    . MET   B 1  104  ? -6.316  40.604  118.139 1.00 23.65 ? 102  MET   B CG    1 
ATOM   9743  S  SD    . MET   B 1  104  ? -6.611  40.255  119.896 1.00 33.58 ? 102  MET   B SD    1 
ATOM   9744  C  CE    . MET   B 1  104  ? -6.227  38.509  119.905 1.00 38.55 ? 102  MET   B CE    1 
ATOM   9745  N  N     . CYS   B 1  105  ? -1.981  42.049  117.353 1.00 20.53 ? 103  CYS   B N     1 
ATOM   9746  C  CA    . CYS   B 1  105  ? -0.546  42.030  117.084 1.00 22.86 ? 103  CYS   B CA    1 
ATOM   9747  C  C     . CYS   B 1  105  ? 0.240   42.489  118.300 1.00 20.80 ? 103  CYS   B C     1 
ATOM   9748  O  O     . CYS   B 1  105  ? 1.257   41.884  118.661 1.00 23.29 ? 103  CYS   B O     1 
ATOM   9749  C  CB    . CYS   B 1  105  ? -0.228  42.945  115.910 1.00 20.94 ? 103  CYS   B CB    1 
ATOM   9750  S  SG    . CYS   B 1  105  ? -0.799  42.313  114.346 1.00 21.28 ? 103  CYS   B SG    1 
ATOM   9751  N  N     . LEU   B 1  106  ? -0.190  43.592  118.916 1.00 20.34 ? 104  LEU   B N     1 
ATOM   9752  C  CA    . LEU   B 1  106  ? 0.444   44.038  120.148 1.00 21.13 ? 104  LEU   B CA    1 
ATOM   9753  C  C     . LEU   B 1  106  ? 0.352   42.964  121.219 1.00 24.06 ? 104  LEU   B C     1 
ATOM   9754  O  O     . LEU   B 1  106  ? 1.335   42.677  121.912 1.00 24.72 ? 104  LEU   B O     1 
ATOM   9755  C  CB    . LEU   B 1  106  ? -0.210  45.331  120.638 1.00 20.82 ? 104  LEU   B CB    1 
ATOM   9756  C  CG    . LEU   B 1  106  ? 0.291   45.803  122.010 1.00 21.15 ? 104  LEU   B CG    1 
ATOM   9757  C  CD1   . LEU   B 1  106  ? 1.747   46.217  121.947 1.00 26.56 ? 104  LEU   B CD1   1 
ATOM   9758  C  CD2   . LEU   B 1  106  ? -0.563  46.936  122.556 1.00 24.39 ? 104  LEU   B CD2   1 
ATOM   9759  N  N     . ALA   B 1  107  ? -0.831  42.360  121.371 1.00 21.98 ? 105  ALA   B N     1 
ATOM   9760  C  CA    . ALA   B 1  107  ? -1.008  41.328  122.389 1.00 21.73 ? 105  ALA   B CA    1 
ATOM   9761  C  C     . ALA   B 1  107  ? -0.088  40.143  122.123 1.00 24.90 ? 105  ALA   B C     1 
ATOM   9762  O  O     . ALA   B 1  107  ? 0.552   39.627  123.046 1.00 25.40 ? 105  ALA   B O     1 
ATOM   9763  C  CB    . ALA   B 1  107  ? -2.466  40.878  122.415 1.00 26.04 ? 105  ALA   B CB    1 
ATOM   9764  N  N     . GLU   B 1  108  ? 0.008   39.721  120.858 1.00 23.64 ? 106  GLU   B N     1 
ATOM   9765  C  CA    . GLU   B 1  108  ? 0.922   38.645  120.477 1.00 23.60 ? 106  GLU   B CA    1 
ATOM   9766  C  C     . GLU   B 1  108  ? 2.351   38.970  120.894 1.00 27.13 ? 106  GLU   B C     1 
ATOM   9767  O  O     . GLU   B 1  108  ? 3.055   38.127  121.462 1.00 26.46 ? 106  GLU   B O     1 
ATOM   9768  C  CB    . GLU   B 1  108  ? 0.849   38.427  118.963 1.00 24.74 ? 106  GLU   B CB    1 
ATOM   9769  C  CG    . GLU   B 1  108  ? 1.883   37.442  118.406 1.00 29.47 ? 106  GLU   B CG    1 
ATOM   9770  C  CD    . GLU   B 1  108  ? 2.066   37.560  116.897 1.00 34.51 ? 106  GLU   B CD    1 
ATOM   9771  O  OE1   . GLU   B 1  108  ? 1.146   38.059  116.216 1.00 29.29 ? 106  GLU   B OE1   1 
ATOM   9772  O  OE2   . GLU   B 1  108  ? 3.143   37.167  116.389 1.00 35.71 ? 106  GLU   B OE2   1 
ATOM   9773  N  N     . ALA   B 1  109  ? 2.793   40.200  120.629 1.00 25.36 ? 107  ALA   B N     1 
ATOM   9774  C  CA    . ALA   B 1  109  ? 4.155   40.581  120.985 1.00 26.01 ? 107  ALA   B CA    1 
ATOM   9775  C  C     . ALA   B 1  109  ? 4.348   40.589  122.497 1.00 25.26 ? 107  ALA   B C     1 
ATOM   9776  O  O     . ALA   B 1  109  ? 5.375   40.114  123.000 1.00 26.85 ? 107  ALA   B O     1 
ATOM   9777  C  CB    . ALA   B 1  109  ? 4.494   41.944  120.382 1.00 27.10 ? 107  ALA   B CB    1 
ATOM   9778  N  N     . LEU   B 1  110  ? 3.371   41.122  123.238 1.00 22.87 ? 108  LEU   B N     1 
ATOM   9779  C  CA    . LEU   B 1  110  ? 3.468   41.148  124.694 1.00 25.03 ? 108  LEU   B CA    1 
ATOM   9780  C  C     . LEU   B 1  110  ? 3.488   39.746  125.286 1.00 27.46 ? 108  LEU   B C     1 
ATOM   9781  O  O     . LEU   B 1  110  ? 4.100   39.530  126.340 1.00 29.39 ? 108  LEU   B O     1 
ATOM   9782  C  CB    . LEU   B 1  110  ? 2.310   41.953  125.289 1.00 24.50 ? 108  LEU   B CB    1 
ATOM   9783  C  CG    . LEU   B 1  110  ? 2.424   43.456  125.041 1.00 25.19 ? 108  LEU   B CG    1 
ATOM   9784  C  CD1   . LEU   B 1  110  ? 1.110   44.143  125.382 1.00 24.46 ? 108  LEU   B CD1   1 
ATOM   9785  C  CD2   . LEU   B 1  110  ? 3.573   44.054  125.858 1.00 28.92 ? 108  LEU   B CD2   1 
ATOM   9786  N  N     . LEU   B 1  111  ? 2.832   38.788  124.634 1.00 26.37 ? 109  LEU   B N     1 
ATOM   9787  C  CA    . LEU   B 1  111  ? 2.852   37.416  125.120 1.00 30.49 ? 109  LEU   B CA    1 
ATOM   9788  C  C     . LEU   B 1  111  ? 4.168   36.706  124.841 1.00 33.82 ? 109  LEU   B C     1 
ATOM   9789  O  O     . LEU   B 1  111  ? 4.404   35.636  125.411 1.00 36.08 ? 109  LEU   B O     1 
ATOM   9790  C  CB    . LEU   B 1  111  ? 1.692   36.620  124.534 1.00 30.85 ? 109  LEU   B CB    1 
ATOM   9791  C  CG    . LEU   B 1  111  ? 0.326   37.049  125.058 1.00 28.46 ? 109  LEU   B CG    1 
ATOM   9792  C  CD1   . LEU   B 1  111  ? -0.740  36.324  124.278 1.00 29.71 ? 109  LEU   B CD1   1 
ATOM   9793  C  CD2   . LEU   B 1  111  ? 0.211   36.750  126.539 1.00 30.92 ? 109  LEU   B CD2   1 
ATOM   9794  N  N     . ARG   B 1  112  ? 5.025   37.267  123.986 1.00 30.46 ? 110  ARG   B N     1 
ATOM   9795  C  CA    . ARG   B 1  112  ? 6.371   36.732  123.841 1.00 32.66 ? 110  ARG   B CA    1 
ATOM   9796  C  C     . ARG   B 1  112  ? 7.246   37.072  125.037 1.00 35.81 ? 110  ARG   B C     1 
ATOM   9797  O  O     . ARG   B 1  112  ? 8.333   36.503  125.172 1.00 36.13 ? 110  ARG   B O     1 
ATOM   9798  C  CB    . ARG   B 1  112  ? 7.007   37.208  122.533 1.00 32.34 ? 110  ARG   B CB    1 
ATOM   9799  C  CG    . ARG   B 1  112  ? 6.262   36.732  121.292 1.00 35.47 ? 110  ARG   B CG    1 
ATOM   9800  C  CD    . ARG   B 1  112  ? 7.082   36.877  120.011 1.00 42.81 ? 110  ARG   B CD    1 
ATOM   9801  N  NE    . ARG   B 1  112  ? 7.227   38.262  119.579 1.00 41.28 ? 110  ARG   B NE    1 
ATOM   9802  C  CZ    . ARG   B 1  112  ? 6.419   38.869  118.721 1.00 43.24 ? 110  ARG   B CZ    1 
ATOM   9803  N  NH1   . ARG   B 1  112  ? 5.378   38.246  118.191 1.00 46.15 ? 110  ARG   B NH1   1 
ATOM   9804  N  NH2   . ARG   B 1  112  ? 6.661   40.134  118.383 1.00 49.66 ? 110  ARG   B NH2   1 
ATOM   9805  N  N     . ILE   B 1  113  ? 6.801   37.980  125.897 1.00 31.75 ? 111  ILE   B N     1 
ATOM   9806  C  CA    . ILE   B 1  113  ? 7.449   38.218  127.182 1.00 31.78 ? 111  ILE   B CA    1 
ATOM   9807  C  C     . ILE   B 1  113  ? 6.933   37.142  128.129 1.00 37.98 ? 111  ILE   B C     1 
ATOM   9808  O  O     . ILE   B 1  113  ? 5.749   37.158  128.495 1.00 38.94 ? 111  ILE   B O     1 
ATOM   9809  C  CB    . ILE   B 1  113  ? 7.150   39.630  127.713 1.00 33.30 ? 111  ILE   B CB    1 
ATOM   9810  C  CG1   . ILE   B 1  113  ? 7.670   40.690  126.740 1.00 32.76 ? 111  ILE   B CG1   1 
ATOM   9811  C  CG2   . ILE   B 1  113  ? 7.755   39.819  129.102 1.00 33.85 ? 111  ILE   B CG2   1 
ATOM   9812  C  CD1   . ILE   B 1  113  ? 7.173   42.090  127.048 1.00 32.56 ? 111  ILE   B CD1   1 
ATOM   9813  N  N     . PRO   B 1  114  ? 7.770   36.183  128.535 1.00 40.98 ? 112  PRO   B N     1 
ATOM   9814  C  CA    . PRO   B 1  114  ? 7.253   35.061  129.335 1.00 40.13 ? 112  PRO   B CA    1 
ATOM   9815  C  C     . PRO   B 1  114  ? 6.927   35.427  130.772 1.00 36.21 ? 112  PRO   B C     1 
ATOM   9816  O  O     . PRO   B 1  114  ? 6.001   34.844  131.351 1.00 42.72 ? 112  PRO   B O     1 
ATOM   9817  C  CB    . PRO   B 1  114  ? 8.379   34.022  129.247 1.00 36.83 ? 112  PRO   B CB    1 
ATOM   9818  C  CG    . PRO   B 1  114  ? 9.607   34.830  129.011 1.00 41.09 ? 112  PRO   B CG    1 
ATOM   9819  C  CD    . PRO   B 1  114  ? 9.191   36.019  128.191 1.00 37.65 ? 112  PRO   B CD    1 
ATOM   9820  N  N     . ASP   B 1  115  ? 7.647   36.375  131.366 1.00 37.46 ? 113  ASP   B N     1 
ATOM   9821  C  CA    . ASP   B 1  115  ? 7.438   36.735  132.764 1.00 43.02 ? 113  ASP   B CA    1 
ATOM   9822  C  C     . ASP   B 1  115  ? 6.237   37.666  132.874 1.00 44.71 ? 113  ASP   B C     1 
ATOM   9823  O  O     . ASP   B 1  115  ? 6.260   38.783  132.344 1.00 40.86 ? 113  ASP   B O     1 
ATOM   9824  C  CB    . ASP   B 1  115  ? 8.693   37.407  133.319 1.00 40.35 ? 113  ASP   B CB    1 
ATOM   9825  C  CG    . ASP   B 1  115  ? 8.523   37.873  134.754 1.00 46.71 ? 113  ASP   B CG    1 
ATOM   9826  O  OD1   . ASP   B 1  115  ? 8.175   37.043  135.621 1.00 51.11 ? 113  ASP   B OD1   1 
ATOM   9827  O  OD2   . ASP   B 1  115  ? 8.748   39.072  135.020 1.00 46.65 ? 113  ASP   B OD2   1 
ATOM   9828  N  N     . THR   B 1  116  ? 5.192   37.207  133.569 1.00 39.30 ? 114  THR   B N     1 
ATOM   9829  C  CA    . THR   B 1  116  ? 3.970   37.999  133.694 1.00 42.14 ? 114  THR   B CA    1 
ATOM   9830  C  C     . THR   B 1  116  ? 4.244   39.366  134.315 1.00 41.93 ? 114  THR   B C     1 
ATOM   9831  O  O     . THR   B 1  116  ? 3.646   40.371  133.911 1.00 40.42 ? 114  THR   B O     1 
ATOM   9832  C  CB    . THR   B 1  116  ? 2.927   37.230  134.506 1.00 43.74 ? 114  THR   B CB    1 
ATOM   9833  N  N     . ALA   B 1  117  ? 5.151   39.430  135.292 1.00 39.48 ? 115  ALA   B N     1 
ATOM   9834  C  CA    . ALA   B 1  117  ? 5.406   40.703  135.959 1.00 40.67 ? 115  ALA   B CA    1 
ATOM   9835  C  C     . ALA   B 1  117  ? 6.108   41.688  135.033 1.00 36.28 ? 115  ALA   B C     1 
ATOM   9836  O  O     . ALA   B 1  117  ? 5.778   42.880  135.024 1.00 44.14 ? 115  ALA   B O     1 
ATOM   9837  C  CB    . ALA   B 1  117  ? 6.213   40.484  137.240 1.00 38.62 ? 115  ALA   B CB    1 
ATOM   9838  N  N     . THR   B 1  118  ? 7.085   41.216  134.257 1.00 38.86 ? 116  THR   B N     1 
ATOM   9839  C  CA    . THR   B 1  118  ? 7.776   42.105  133.329 1.00 38.07 ? 116  THR   B CA    1 
ATOM   9840  C  C     . THR   B 1  118  ? 6.824   42.603  132.253 1.00 38.11 ? 116  THR   B C     1 
ATOM   9841  O  O     . THR   B 1  118  ? 6.883   43.769  131.848 1.00 39.25 ? 116  THR   B O     1 
ATOM   9842  C  CB    . THR   B 1  118  ? 8.957   41.374  132.693 1.00 35.72 ? 116  THR   B CB    1 
ATOM   9843  O  OG1   . THR   B 1  118  ? 9.850   40.930  133.723 1.00 41.72 ? 116  THR   B OG1   1 
ATOM   9844  C  CG2   . THR   B 1  118  ? 9.710   42.292  131.741 1.00 39.87 ? 116  THR   B CG2   1 
ATOM   9845  N  N     . ARG   B 1  119  ? 5.935   41.726  131.788 1.00 37.29 ? 117  ARG   B N     1 
ATOM   9846  C  CA    . ARG   B 1  119  ? 4.966   42.104  130.766 1.00 31.90 ? 117  ARG   B CA    1 
ATOM   9847  C  C     . ARG   B 1  119  ? 3.987   43.138  131.303 1.00 37.73 ? 117  ARG   B C     1 
ATOM   9848  O  O     . ARG   B 1  119  ? 3.751   44.173  130.670 1.00 35.23 ? 117  ARG   B O     1 
ATOM   9849  C  CB    . ARG   B 1  119  ? 4.221   40.857  130.302 1.00 33.79 ? 117  ARG   B CB    1 
ATOM   9850  C  CG    . ARG   B 1  119  ? 3.239   41.103  129.170 1.00 31.14 ? 117  ARG   B CG    1 
ATOM   9851  C  CD    . ARG   B 1  119  ? 2.310   39.924  129.026 1.00 34.33 ? 117  ARG   B CD    1 
ATOM   9852  N  NE    . ARG   B 1  119  ? 3.048   38.672  128.926 1.00 34.25 ? 117  ARG   B NE    1 
ATOM   9853  C  CZ    . ARG   B 1  119  ? 2.652   37.528  129.469 1.00 42.41 ? 117  ARG   B CZ    1 
ATOM   9854  N  NH1   . ARG   B 1  119  ? 1.530   37.445  130.168 1.00 33.47 ? 117  ARG   B NH1   1 
ATOM   9855  N  NH2   . ARG   B 1  119  ? 3.405   36.443  129.317 1.00 45.82 ? 117  ARG   B NH2   1 
ATOM   9856  N  N     . ASP   B 1  120  ? 3.416   42.878  132.483 1.00 35.59 ? 118  ASP   B N     1 
ATOM   9857  C  CA    . ASP   B 1  120  ? 2.491   43.833  133.084 1.00 35.52 ? 118  ASP   B CA    1 
ATOM   9858  C  C     . ASP   B 1  120  ? 3.170   45.159  133.394 1.00 41.02 ? 118  ASP   B C     1 
ATOM   9859  O  O     . ASP   B 1  120  ? 2.545   46.219  133.270 1.00 36.58 ? 118  ASP   B O     1 
ATOM   9860  C  CB    . ASP   B 1  120  ? 1.847   43.236  134.335 1.00 35.84 ? 118  ASP   B CB    1 
ATOM   9861  C  CG    . ASP   B 1  120  ? 0.924   42.076  134.014 1.00 44.30 ? 118  ASP   B CG    1 
ATOM   9862  O  OD1   . ASP   B 1  120  ? 0.763   41.765  132.812 1.00 43.32 ? 118  ASP   B OD1   1 
ATOM   9863  O  OD2   . ASP   B 1  120  ? 0.360   41.474  134.954 1.00 48.04 ? 118  ASP   B OD2   1 
ATOM   9864  N  N     . ALA   B 1  121  ? 4.445   45.129  133.789 1.00 37.85 ? 119  ALA   B N     1 
ATOM   9865  C  CA    . ALA   B 1  121  ? 5.148   46.380  134.043 1.00 42.82 ? 119  ALA   B CA    1 
ATOM   9866  C  C     . ALA   B 1  121  ? 5.354   47.162  132.753 1.00 37.80 ? 119  ALA   B C     1 
ATOM   9867  O  O     . ALA   B 1  121  ? 5.212   48.389  132.735 1.00 39.09 ? 119  ALA   B O     1 
ATOM   9868  C  CB    . ALA   B 1  121  ? 6.478   46.118  134.753 1.00 40.55 ? 119  ALA   B CB    1 
ATOM   9869  N  N     . LEU   B 1  122  ? 5.676   46.469  131.658 1.00 35.89 ? 120  LEU   B N     1 
ATOM   9870  C  CA    . LEU   B 1  122  ? 5.873   47.155  130.386 1.00 35.33 ? 120  LEU   B CA    1 
ATOM   9871  C  C     . LEU   B 1  122  ? 4.573   47.785  129.898 1.00 36.66 ? 120  LEU   B C     1 
ATOM   9872  O  O     . LEU   B 1  122  ? 4.577   48.896  129.356 1.00 35.39 ? 120  LEU   B O     1 
ATOM   9873  C  CB    . LEU   B 1  122  ? 6.424   46.181  129.346 1.00 37.93 ? 120  LEU   B CB    1 
ATOM   9874  C  CG    . LEU   B 1  122  ? 6.837   46.815  128.017 1.00 37.61 ? 120  LEU   B CG    1 
ATOM   9875  C  CD1   . LEU   B 1  122  ? 8.050   47.712  128.219 1.00 42.16 ? 120  LEU   B CD1   1 
ATOM   9876  C  CD2   . LEU   B 1  122  ? 7.109   45.753  126.965 1.00 35.93 ? 120  LEU   B CD2   1 
ATOM   9877  N  N     . ILE   B 1  123  ? 3.453   47.084  130.087 1.00 31.94 ? 121  ILE   B N     1 
ATOM   9878  C  CA    . ILE   B 1  123  ? 2.150   47.605  129.679 1.00 34.68 ? 121  ILE   B CA    1 
ATOM   9879  C  C     . ILE   B 1  123  ? 1.826   48.882  130.443 1.00 39.70 ? 121  ILE   B C     1 
ATOM   9880  O  O     . ILE   B 1  123  ? 1.502   49.919  129.849 1.00 35.33 ? 121  ILE   B O     1 
ATOM   9881  C  CB    . ILE   B 1  123  ? 1.061   46.534  129.882 1.00 30.77 ? 121  ILE   B CB    1 
ATOM   9882  C  CG1   . ILE   B 1  123  ? 1.273   45.361  128.926 1.00 27.84 ? 121  ILE   B CG1   1 
ATOM   9883  C  CG2   . ILE   B 1  123  ? -0.330  47.132  129.708 1.00 32.07 ? 121  ILE   B CG2   1 
ATOM   9884  C  CD1   . ILE   B 1  123  ? 0.400   44.176  129.236 1.00 28.58 ? 121  ILE   B CD1   1 
ATOM   9885  N  N     . ARG   B 1  124  ? 1.919   48.824  131.775 1.00 35.04 ? 122  ARG   B N     1 
ATOM   9886  C  CA    . ARG   B 1  124  ? 1.504   49.946  132.610 1.00 42.85 ? 122  ARG   B CA    1 
ATOM   9887  C  C     . ARG   B 1  124  ? 2.471   51.120  132.521 1.00 44.70 ? 122  ARG   B C     1 
ATOM   9888  O  O     . ARG   B 1  124  ? 2.044   52.275  132.632 1.00 51.61 ? 122  ARG   B O     1 
ATOM   9889  C  CB    . ARG   B 1  124  ? 1.357   49.490  134.062 1.00 43.86 ? 122  ARG   B CB    1 
ATOM   9890  N  N     . ASP   B 1  125  ? 3.762   50.858  132.317 1.00 41.13 ? 123  ASP   B N     1 
ATOM   9891  C  CA    . ASP   B 1  125  ? 4.768   51.911  132.381 1.00 48.48 ? 123  ASP   B CA    1 
ATOM   9892  C  C     . ASP   B 1  125  ? 5.227   52.417  131.022 1.00 44.82 ? 123  ASP   B C     1 
ATOM   9893  O  O     . ASP   B 1  125  ? 5.738   53.539  130.943 1.00 48.18 ? 123  ASP   B O     1 
ATOM   9894  C  CB    . ASP   B 1  125  ? 6.002   51.441  133.165 1.00 50.06 ? 123  ASP   B CB    1 
ATOM   9895  C  CG    . ASP   B 1  125  ? 5.657   50.924  134.547 1.00 55.96 ? 123  ASP   B CG    1 
ATOM   9896  O  OD1   . ASP   B 1  125  ? 4.603   51.315  135.092 1.00 54.84 ? 123  ASP   B OD1   1 
ATOM   9897  O  OD2   . ASP   B 1  125  ? 6.449   50.123  135.088 1.00 57.80 ? 123  ASP   B OD2   1 
ATOM   9898  N  N     . LYS   B 1  126  ? 5.068   51.635  129.961 1.00 40.05 ? 124  LYS   B N     1 
ATOM   9899  C  CA    . LYS   B 1  126  ? 5.585   52.059  128.665 1.00 43.85 ? 124  LYS   B CA    1 
ATOM   9900  C  C     . LYS   B 1  126  ? 4.558   51.983  127.543 1.00 43.85 ? 124  LYS   B C     1 
ATOM   9901  O  O     . LYS   B 1  126  ? 4.525   52.877  126.693 1.00 47.49 ? 124  LYS   B O     1 
ATOM   9902  C  CB    . LYS   B 1  126  ? 6.835   51.242  128.293 1.00 45.86 ? 124  LYS   B CB    1 
ATOM   9903  N  N     . ILE   B 1  127  ? 3.725   50.943  127.511 1.00 39.15 ? 125  ILE   B N     1 
ATOM   9904  C  CA    . ILE   B 1  127  ? 2.825   50.769  126.372 1.00 34.88 ? 125  ILE   B CA    1 
ATOM   9905  C  C     . ILE   B 1  127  ? 1.582   51.637  126.514 1.00 40.06 ? 125  ILE   B C     1 
ATOM   9906  O  O     . ILE   B 1  127  ? 1.136   52.259  125.545 1.00 37.40 ? 125  ILE   B O     1 
ATOM   9907  C  CB    . ILE   B 1  127  ? 2.461   49.289  126.157 1.00 33.52 ? 125  ILE   B CB    1 
ATOM   9908  C  CG1   . ILE   B 1  127  ? 3.715   48.411  126.142 1.00 34.29 ? 125  ILE   B CG1   1 
ATOM   9909  C  CG2   . ILE   B 1  127  ? 1.673   49.136  124.855 1.00 32.86 ? 125  ILE   B CG2   1 
ATOM   9910  C  CD1   . ILE   B 1  127  ? 4.715   48.788  125.085 1.00 43.45 ? 125  ILE   B CD1   1 
ATOM   9911  N  N     . ALA   B 1  128  ? 0.988   51.670  127.708 1.00 33.16 ? 126  ALA   B N     1 
ATOM   9912  C  CA    . ALA   B 1  128  ? -0.229  52.446  127.920 1.00 35.54 ? 126  ALA   B CA    1 
ATOM   9913  C  C     . ALA   B 1  128  ? 0.002   53.941  127.754 1.00 45.28 ? 126  ALA   B C     1 
ATOM   9914  O  O     . ALA   B 1  128  ? -0.957  54.680  127.498 1.00 43.28 ? 126  ALA   B O     1 
ATOM   9915  C  CB    . ALA   B 1  128  ? -0.818  52.142  129.295 1.00 35.73 ? 126  ALA   B CB    1 
ATOM   9916  N  N     . ASP   B 1  129  ? 1.245   54.400  127.893 1.00 43.80 ? 127  ASP   B N     1 
ATOM   9917  C  CA    . ASP   B 1  129  ? 1.624   55.776  127.605 1.00 51.00 ? 127  ASP   B CA    1 
ATOM   9918  C  C     . ASP   B 1  129  ? 1.920   56.009  126.127 1.00 54.69 ? 127  ASP   B C     1 
ATOM   9919  O  O     . ASP   B 1  129  ? 2.538   57.022  125.781 1.00 63.00 ? 127  ASP   B O     1 
ATOM   9920  C  CB    . ASP   B 1  129  ? 2.821   56.193  128.466 1.00 53.81 ? 127  ASP   B CB    1 
ATOM   9921  N  N     . GLY   B 1  130  ? 1.509   55.088  125.254 1.00 55.01 ? 128  GLY   B N     1 
ATOM   9922  C  CA    . GLY   B 1  130  ? 1.661   55.250  123.823 1.00 54.19 ? 128  GLY   B CA    1 
ATOM   9923  C  C     . GLY   B 1  130  ? 3.047   55.001  123.270 1.00 60.54 ? 128  GLY   B C     1 
ATOM   9924  O  O     . GLY   B 1  130  ? 3.193   54.892  122.045 1.00 57.00 ? 128  GLY   B O     1 
ATOM   9925  N  N     . ASN   B 1  131  ? 4.071   54.899  124.117 1.00 65.11 ? 129  ASN   B N     1 
ATOM   9926  C  CA    . ASN   B 1  131  ? 5.433   54.701  123.634 1.00 67.13 ? 129  ASN   B CA    1 
ATOM   9927  C  C     . ASN   B 1  131  ? 5.651   53.259  123.188 1.00 61.99 ? 129  ASN   B C     1 
ATOM   9928  O  O     . ASN   B 1  131  ? 6.647   52.631  123.561 1.00 66.58 ? 129  ASN   B O     1 
ATOM   9929  C  CB    . ASN   B 1  131  ? 6.442   55.083  124.720 1.00 66.31 ? 129  ASN   B CB    1 
ATOM   9930  N  N     . TRP   B 1  132  ? 4.731   52.731  122.376 1.00 52.09 ? 130  TRP   B N     1 
ATOM   9931  C  CA    . TRP   B 1  132  ? 4.776   51.319  122.016 1.00 47.23 ? 130  TRP   B CA    1 
ATOM   9932  C  C     . TRP   B 1  132  ? 5.794   51.031  120.921 1.00 44.57 ? 130  TRP   B C     1 
ATOM   9933  O  O     . TRP   B 1  132  ? 6.298   49.906  120.832 1.00 52.68 ? 130  TRP   B O     1 
ATOM   9934  C  CB    . TRP   B 1  132  ? 3.382   50.825  121.612 1.00 43.55 ? 130  TRP   B CB    1 
ATOM   9935  C  CG    . TRP   B 1  132  ? 2.837   51.445  120.348 1.00 34.63 ? 130  TRP   B CG    1 
ATOM   9936  C  CD1   . TRP   B 1  132  ? 1.969   52.499  120.254 1.00 35.33 ? 130  TRP   B CD1   1 
ATOM   9937  C  CD2   . TRP   B 1  132  ? 3.127   51.046  119.005 1.00 31.49 ? 130  TRP   B CD2   1 
ATOM   9938  N  NE1   . TRP   B 1  132  ? 1.699   52.774  118.934 1.00 32.23 ? 130  TRP   B NE1   1 
ATOM   9939  C  CE2   . TRP   B 1  132  ? 2.400   51.897  118.148 1.00 27.48 ? 130  TRP   B CE2   1 
ATOM   9940  C  CE3   . TRP   B 1  132  ? 3.927   50.047  118.445 1.00 30.16 ? 130  TRP   B CE3   1 
ATOM   9941  C  CZ2   . TRP   B 1  132  ? 2.454   51.779  116.763 1.00 25.31 ? 130  TRP   B CZ2   1 
ATOM   9942  C  CZ3   . TRP   B 1  132  ? 3.982   49.934  117.073 1.00 26.23 ? 130  TRP   B CZ3   1 
ATOM   9943  C  CH2   . TRP   B 1  132  ? 3.250   50.793  116.246 1.00 28.27 ? 130  TRP   B CH2   1 
ATOM   9944  N  N     . LYS   B 1  133  ? 6.104   52.019  120.079 1.00 46.78 ? 131  LYS   B N     1 
ATOM   9945  C  CA    . LYS   B 1  133  ? 7.048   51.789  118.990 1.00 50.17 ? 131  LYS   B CA    1 
ATOM   9946  C  C     . LYS   B 1  133  ? 8.428   51.434  119.528 1.00 60.47 ? 131  LYS   B C     1 
ATOM   9947  O  O     . LYS   B 1  133  ? 9.024   50.425  119.132 1.00 63.62 ? 131  LYS   B O     1 
ATOM   9948  C  CB    . LYS   B 1  133  ? 7.114   53.022  118.088 1.00 50.05 ? 131  LYS   B CB    1 
ATOM   9949  N  N     . SER   B 1  134  ? 8.944   52.247  120.451 1.00 63.90 ? 132  SER   B N     1 
ATOM   9950  C  CA    . SER   B 1  134  ? 10.281  52.016  120.987 1.00 63.14 ? 132  SER   B CA    1 
ATOM   9951  C  C     . SER   B 1  134  ? 10.342  50.720  121.788 1.00 67.51 ? 132  SER   B C     1 
ATOM   9952  O  O     . SER   B 1  134  ? 11.194  49.860  121.531 1.00 68.22 ? 132  SER   B O     1 
ATOM   9953  C  CB    . SER   B 1  134  ? 10.703  53.206  121.850 1.00 56.34 ? 132  SER   B CB    1 
ATOM   9954  N  N     . HIS   B 1  135  ? 9.432   50.556  122.752 1.00 69.41 ? 133  HIS   B N     1 
ATOM   9955  C  CA    . HIS   B 1  135  ? 9.530   49.446  123.696 1.00 69.42 ? 133  HIS   B CA    1 
ATOM   9956  C  C     . HIS   B 1  135  ? 9.417   48.088  123.011 1.00 70.57 ? 133  HIS   B C     1 
ATOM   9957  O  O     . HIS   B 1  135  ? 10.009  47.109  123.480 1.00 74.26 ? 133  HIS   B O     1 
ATOM   9958  C  CB    . HIS   B 1  135  ? 8.474   49.593  124.792 1.00 60.54 ? 133  HIS   B CB    1 
ATOM   9959  N  N     . LEU   B 1  136  ? 8.674   48.001  121.912 1.00 65.39 ? 134  LEU   B N     1 
ATOM   9960  C  CA    . LEU   B 1  136  ? 8.520   46.729  121.210 1.00 60.56 ? 134  LEU   B CA    1 
ATOM   9961  C  C     . LEU   B 1  136  ? 8.931   46.833  119.744 1.00 60.95 ? 134  LEU   B C     1 
ATOM   9962  O  O     . LEU   B 1  136  ? 9.111   45.818  119.070 1.00 50.86 ? 134  LEU   B O     1 
ATOM   9963  C  CB    . LEU   B 1  136  ? 7.081   46.219  121.319 1.00 55.34 ? 134  LEU   B CB    1 
ATOM   9964  C  CG    . LEU   B 1  136  ? 6.602   45.813  122.714 1.00 46.18 ? 134  LEU   B CG    1 
ATOM   9965  C  CD1   . LEU   B 1  136  ? 5.146   45.400  122.667 1.00 40.69 ? 134  LEU   B CD1   1 
ATOM   9966  C  CD2   . LEU   B 1  136  ? 7.461   44.687  123.273 1.00 51.58 ? 134  LEU   B CD2   1 
ATOM   9967  N  N     . ARG   B 1  140  ? 11.983  43.947  114.522 1.00 37.38 ? 138  ARG   B N     1 
ATOM   9968  C  CA    . ARG   B 1  140  ? 10.893  43.248  113.851 1.00 42.02 ? 138  ARG   B CA    1 
ATOM   9969  C  C     . ARG   B 1  140  ? 9.572   43.977  114.073 1.00 41.28 ? 138  ARG   B C     1 
ATOM   9970  O  O     . ARG   B 1  140  ? 9.234   44.347  115.196 1.00 34.22 ? 138  ARG   B O     1 
ATOM   9971  C  CB    . ARG   B 1  140  ? 10.787  41.800  114.341 1.00 39.64 ? 138  ARG   B CB    1 
ATOM   9972  N  N     . SER   B 1  141  ? 8.834   44.180  112.985 1.00 32.32 ? 139  SER   B N     1 
ATOM   9973  C  CA    . SER   B 1  141  ? 7.558   44.874  113.061 1.00 28.02 ? 139  SER   B CA    1 
ATOM   9974  C  C     . SER   B 1  141  ? 6.630   44.164  114.038 1.00 29.54 ? 139  SER   B C     1 
ATOM   9975  O  O     . SER   B 1  141  ? 6.601   42.933  114.122 1.00 29.08 ? 139  SER   B O     1 
ATOM   9976  C  CB    . SER   B 1  141  ? 6.919   44.905  111.668 1.00 30.14 ? 139  SER   B CB    1 
ATOM   9977  O  OG    . SER   B 1  141  ? 5.638   45.531  111.689 1.00 32.36 ? 139  SER   B OG    1 
ATOM   9978  N  N     . LEU   B 1  142  ? 5.881   44.954  114.803 1.00 25.76 ? 140  LEU   B N     1 
ATOM   9979  C  CA    . LEU   B 1  142  ? 4.794   44.394  115.589 1.00 24.49 ? 140  LEU   B CA    1 
ATOM   9980  C  C     . LEU   B 1  142  ? 3.785   43.666  114.720 1.00 21.39 ? 140  LEU   B C     1 
ATOM   9981  O  O     . LEU   B 1  142  ? 3.089   42.769  115.207 1.00 22.15 ? 140  LEU   B O     1 
ATOM   9982  C  CB    . LEU   B 1  142  ? 4.063   45.538  116.285 1.00 23.04 ? 140  LEU   B CB    1 
ATOM   9983  C  CG    . LEU   B 1  142  ? 3.545   45.170  117.656 1.00 27.92 ? 140  LEU   B CG    1 
ATOM   9984  C  CD1   . LEU   B 1  142  ? 4.716   45.029  118.588 1.00 30.22 ? 140  LEU   B CD1   1 
ATOM   9985  C  CD2   . LEU   B 1  142  ? 2.615   46.248  118.120 1.00 30.79 ? 140  LEU   B CD2   1 
ATOM   9986  N  N     . PHE   B 1  143  ? 3.693   44.023  113.440 1.00 20.11 ? 141  PHE   B N     1 
ATOM   9987  C  CA    . PHE   B 1  143  ? 2.598   43.592  112.587 1.00 20.42 ? 141  PHE   B CA    1 
ATOM   9988  C  C     . PHE   B 1  143  ? 2.986   42.465  111.636 1.00 21.79 ? 141  PHE   B C     1 
ATOM   9989  O  O     . PHE   B 1  143  ? 2.256   42.204  110.679 1.00 22.49 ? 141  PHE   B O     1 
ATOM   9990  C  CB    . PHE   B 1  143  ? 2.025   44.806  111.852 1.00 19.69 ? 141  PHE   B CB    1 
ATOM   9991  C  CG    . PHE   B 1  143  ? 1.718   45.952  112.773 1.00 19.29 ? 141  PHE   B CG    1 
ATOM   9992  C  CD1   . PHE   B 1  143  ? 0.789   45.799  113.796 1.00 20.59 ? 141  PHE   B CD1   1 
ATOM   9993  C  CD2   . PHE   B 1  143  ? 2.374   47.170  112.647 1.00 18.80 ? 141  PHE   B CD2   1 
ATOM   9994  C  CE1   . PHE   B 1  143  ? 0.509   46.830  114.651 1.00 21.64 ? 141  PHE   B CE1   1 
ATOM   9995  C  CE2   . PHE   B 1  143  ? 2.104   48.207  113.511 1.00 20.56 ? 141  PHE   B CE2   1 
ATOM   9996  C  CZ    . PHE   B 1  143  ? 1.164   48.046  114.520 1.00 19.74 ? 141  PHE   B CZ    1 
ATOM   9997  N  N     . VAL   B 1  144  ? 4.091   41.759  111.915 1.00 22.49 ? 142  VAL   B N     1 
ATOM   9998  C  CA    . VAL   B 1  144  ? 4.544   40.665  111.049 1.00 22.95 ? 142  VAL   B CA    1 
ATOM   9999  C  C     . VAL   B 1  144  ? 3.429   39.659  110.785 1.00 25.98 ? 142  VAL   B C     1 
ATOM   10000 O  O     . VAL   B 1  144  ? 3.266   39.172  109.659 1.00 24.59 ? 142  VAL   B O     1 
ATOM   10001 C  CB    . VAL   B 1  144  ? 5.805   39.992  111.631 1.00 26.97 ? 142  VAL   B CB    1 
ATOM   10002 C  CG1   . VAL   B 1  144  ? 6.173   38.744  110.834 1.00 28.19 ? 142  VAL   B CG1   1 
ATOM   10003 C  CG2   . VAL   B 1  144  ? 6.960   40.959  111.638 1.00 28.21 ? 142  VAL   B CG2   1 
ATOM   10004 N  N     . ASN   B 1  145  ? 2.644   39.329  111.811 1.00 22.74 ? 143  ASN   B N     1 
ATOM   10005 C  CA    . ASN   B 1  145  ? 1.595   38.328  111.679 1.00 23.70 ? 143  ASN   B CA    1 
ATOM   10006 C  C     . ASN   B 1  145  ? 0.210   38.940  111.548 1.00 24.21 ? 143  ASN   B C     1 
ATOM   10007 O  O     . ASN   B 1  145  ? -0.788  38.269  111.832 1.00 25.02 ? 143  ASN   B O     1 
ATOM   10008 C  CB    . ASN   B 1  145  ? 1.639   37.341  112.843 1.00 26.72 ? 143  ASN   B CB    1 
ATOM   10009 C  CG    . ASN   B 1  145  ? 2.779   36.370  112.719 1.00 34.68 ? 143  ASN   B CG    1 
ATOM   10010 O  OD1   . ASN   B 1  145  ? 3.035   35.838  111.638 1.00 35.96 ? 143  ASN   B OD1   1 
ATOM   10011 N  ND2   . ASN   B 1  145  ? 3.483   36.141  113.815 1.00 33.85 ? 143  ASN   B ND2   1 
ATOM   10012 N  N     . ALA   B 1  146  ? 0.127   40.193  111.100 1.00 22.65 ? 144  ALA   B N     1 
ATOM   10013 C  CA    . ALA   B 1  146  ? -1.167  40.857  111.041 1.00 23.07 ? 144  ALA   B CA    1 
ATOM   10014 C  C     . ALA   B 1  146  ? -2.111  40.243  110.016 1.00 23.17 ? 144  ALA   B C     1 
ATOM   10015 O  O     . ALA   B 1  146  ? -3.328  40.395  110.153 1.00 25.33 ? 144  ALA   B O     1 
ATOM   10016 C  CB    . ALA   B 1  146  ? -0.990  42.353  110.774 1.00 21.82 ? 144  ALA   B CB    1 
ATOM   10017 N  N     . ALA   B 1  147  ? -1.597  39.576  108.985 1.00 22.06 ? 145  ALA   B N     1 
ATOM   10018 C  CA    . ALA   B 1  147  ? -2.511  38.908  108.067 1.00 23.22 ? 145  ALA   B CA    1 
ATOM   10019 C  C     . ALA   B 1  147  ? -3.278  37.812  108.788 1.00 25.77 ? 145  ALA   B C     1 
ATOM   10020 O  O     . ALA   B 1  147  ? -4.468  37.597  108.533 1.00 26.84 ? 145  ALA   B O     1 
ATOM   10021 C  CB    . ALA   B 1  147  ? -1.751  38.338  106.874 1.00 25.59 ? 145  ALA   B CB    1 
ATOM   10022 N  N     . THR   B 1  148  ? -2.613  37.118  109.707 1.00 24.94 ? 146  THR   B N     1 
ATOM   10023 C  CA    . THR   B 1  148  ? -3.296  36.092  110.480 1.00 24.39 ? 146  THR   B CA    1 
ATOM   10024 C  C     . THR   B 1  148  ? -4.327  36.713  111.410 1.00 25.82 ? 146  THR   B C     1 
ATOM   10025 O  O     . THR   B 1  148  ? -5.470  36.251  111.469 1.00 26.88 ? 146  THR   B O     1 
ATOM   10026 C  CB    . THR   B 1  148  ? -2.268  35.252  111.240 1.00 31.67 ? 146  THR   B CB    1 
ATOM   10027 O  OG1   . THR   B 1  148  ? -1.385  34.629  110.296 1.00 34.63 ? 146  THR   B OG1   1 
ATOM   10028 C  CG2   . THR   B 1  148  ? -2.960  34.175  112.067 1.00 34.68 ? 146  THR   B CG2   1 
ATOM   10029 N  N     . TRP   B 1  149  ? -3.960  37.784  112.115 1.00 24.82 ? 147  TRP   B N     1 
ATOM   10030 C  CA    . TRP   B 1  149  ? -4.937  38.435  112.975 1.00 24.15 ? 147  TRP   B CA    1 
ATOM   10031 C  C     . TRP   B 1  149  ? -6.034  39.107  112.167 1.00 23.55 ? 147  TRP   B C     1 
ATOM   10032 O  O     . TRP   B 1  149  ? -7.174  39.198  112.637 1.00 25.16 ? 147  TRP   B O     1 
ATOM   10033 C  CB    . TRP   B 1  149  ? -4.263  39.415  113.934 1.00 24.80 ? 147  TRP   B CB    1 
ATOM   10034 C  CG    . TRP   B 1  149  ? -3.360  38.720  114.896 1.00 23.18 ? 147  TRP   B CG    1 
ATOM   10035 C  CD1   . TRP   B 1  149  ? -1.999  38.806  114.950 1.00 25.87 ? 147  TRP   B CD1   1 
ATOM   10036 C  CD2   . TRP   B 1  149  ? -3.745  37.792  115.918 1.00 27.32 ? 147  TRP   B CD2   1 
ATOM   10037 N  NE1   . TRP   B 1  149  ? -1.516  38.007  115.957 1.00 26.08 ? 147  TRP   B NE1   1 
ATOM   10038 C  CE2   . TRP   B 1  149  ? -2.565  37.368  116.561 1.00 25.80 ? 147  TRP   B CE2   1 
ATOM   10039 C  CE3   . TRP   B 1  149  ? -4.973  37.282  116.354 1.00 30.71 ? 147  TRP   B CE3   1 
ATOM   10040 C  CZ2   . TRP   B 1  149  ? -2.577  36.461  117.628 1.00 29.27 ? 147  TRP   B CZ2   1 
ATOM   10041 C  CZ3   . TRP   B 1  149  ? -4.983  36.383  117.413 1.00 31.46 ? 147  TRP   B CZ3   1 
ATOM   10042 C  CH2   . TRP   B 1  149  ? -3.791  35.983  118.035 1.00 32.69 ? 147  TRP   B CH2   1 
ATOM   10043 N  N     . GLY   B 1  150  ? -5.714  39.578  110.961 1.00 23.61 ? 148  GLY   B N     1 
ATOM   10044 C  CA    . GLY   B 1  150  ? -6.749  40.096  110.086 1.00 24.83 ? 148  GLY   B CA    1 
ATOM   10045 C  C     . GLY   B 1  150  ? -7.801  39.049  109.781 1.00 24.45 ? 148  GLY   B C     1 
ATOM   10046 O  O     . GLY   B 1  150  ? -9.001  39.333  109.793 1.00 24.99 ? 148  GLY   B O     1 
ATOM   10047 N  N     . LEU   B 1  151  ? -7.364  37.816  109.524 1.00 25.49 ? 149  LEU   B N     1 
ATOM   10048 C  CA    A LEU   B 1  151  ? -8.313  36.726  109.322 0.52 29.72 ? 149  LEU   B CA    1 
ATOM   10049 C  CA    B LEU   B 1  151  ? -8.314  36.730  109.319 0.48 29.72 ? 149  LEU   B CA    1 
ATOM   10050 C  C     . LEU   B 1  151  ? -9.138  36.485  110.576 1.00 29.75 ? 149  LEU   B C     1 
ATOM   10051 O  O     . LEU   B 1  151  ? -10.353 36.266  110.499 1.00 31.72 ? 149  LEU   B O     1 
ATOM   10052 C  CB    A LEU   B 1  151  ? -7.567  35.454  108.925 0.52 31.69 ? 149  LEU   B CB    1 
ATOM   10053 C  CB    B LEU   B 1  151  ? -7.560  35.467  108.902 0.48 31.69 ? 149  LEU   B CB    1 
ATOM   10054 C  CG    A LEU   B 1  151  ? -7.755  34.963  107.491 0.52 31.89 ? 149  LEU   B CG    1 
ATOM   10055 C  CG    B LEU   B 1  151  ? -8.330  34.358  108.190 0.48 33.07 ? 149  LEU   B CG    1 
ATOM   10056 C  CD1   A LEU   B 1  151  ? -7.007  33.658  107.282 0.52 35.48 ? 149  LEU   B CD1   1 
ATOM   10057 C  CD1   B LEU   B 1  151  ? -9.198  34.935  107.084 0.48 33.87 ? 149  LEU   B CD1   1 
ATOM   10058 C  CD2   A LEU   B 1  151  ? -9.235  34.790  107.175 0.52 33.90 ? 149  LEU   B CD2   1 
ATOM   10059 C  CD2   B LEU   B 1  151  ? -7.343  33.357  107.615 0.48 35.29 ? 149  LEU   B CD2   1 
ATOM   10060 N  N     . VAL   B 1  152  ? -8.496  36.532  111.745 1.00 28.54 ? 150  VAL   B N     1 
ATOM   10061 C  CA    . VAL   B 1  152  ? -9.215  36.321  112.996 1.00 31.52 ? 150  VAL   B CA    1 
ATOM   10062 C  C     . VAL   B 1  152  ? -10.252 37.413  113.217 1.00 29.80 ? 150  VAL   B C     1 
ATOM   10063 O  O     . VAL   B 1  152  ? -11.387 37.139  113.625 1.00 32.24 ? 150  VAL   B O     1 
ATOM   10064 C  CB    . VAL   B 1  152  ? -8.225  36.238  114.169 1.00 24.90 ? 150  VAL   B CB    1 
ATOM   10065 C  CG1   . VAL   B 1  152  ? -8.980  36.210  115.485 1.00 33.39 ? 150  VAL   B CG1   1 
ATOM   10066 C  CG2   . VAL   B 1  152  ? -7.334  35.024  114.028 1.00 30.91 ? 150  VAL   B CG2   1 
ATOM   10067 N  N     . VAL   B 1  153  ? -9.885  38.664  112.945 1.00 27.53 ? 151  VAL   B N     1 
ATOM   10068 C  CA    . VAL   B 1  153  ? -10.737 39.790  113.308 1.00 26.73 ? 151  VAL   B CA    1 
ATOM   10069 C  C     . VAL   B 1  153  ? -11.811 40.035  112.255 1.00 28.47 ? 151  VAL   B C     1 
ATOM   10070 O  O     . VAL   B 1  153  ? -12.968 40.321  112.587 1.00 28.86 ? 151  VAL   B O     1 
ATOM   10071 C  CB    . VAL   B 1  153  ? -9.869  41.039  113.547 1.00 26.65 ? 151  VAL   B CB    1 
ATOM   10072 C  CG1   . VAL   B 1  153  ? -10.748 42.281  113.718 1.00 27.59 ? 151  VAL   B CG1   1 
ATOM   10073 C  CG2   . VAL   B 1  153  ? -8.969  40.834  114.753 1.00 27.04 ? 151  VAL   B CG2   1 
ATOM   10074 N  N     . THR   B 1  154  ? -11.452 39.942  110.981 1.00 27.76 ? 152  THR   B N     1 
ATOM   10075 C  CA    . THR   B 1  154  ? -12.337 40.351  109.901 1.00 30.36 ? 152  THR   B CA    1 
ATOM   10076 C  C     . THR   B 1  154  ? -12.840 39.194  109.058 1.00 33.56 ? 152  THR   B C     1 
ATOM   10077 O  O     . THR   B 1  154  ? -13.784 39.383  108.284 1.00 35.61 ? 152  THR   B O     1 
ATOM   10078 C  CB    . THR   B 1  154  ? -11.620 41.339  108.968 1.00 27.85 ? 152  THR   B CB    1 
ATOM   10079 O  OG1   . THR   B 1  154  ? -10.729 40.616  108.111 1.00 28.43 ? 152  THR   B OG1   1 
ATOM   10080 C  CG2   . THR   B 1  154  ? -10.825 42.350  109.767 1.00 32.45 ? 152  THR   B CG2   1 
ATOM   10081 N  N     . GLY   B 1  155  ? -12.235 38.016  109.170 1.00 28.08 ? 153  GLY   B N     1 
ATOM   10082 C  CA    . GLY   B 1  155  ? -12.578 36.916  108.300 1.00 31.98 ? 153  GLY   B CA    1 
ATOM   10083 C  C     . GLY   B 1  155  ? -11.997 37.004  106.910 1.00 34.06 ? 153  GLY   B C     1 
ATOM   10084 O  O     . GLY   B 1  155  ? -12.292 36.136  106.079 1.00 37.38 ? 153  GLY   B O     1 
ATOM   10085 N  N     . LYS   B 1  156  ? -11.183 38.016  106.626 1.00 32.42 ? 154  LYS   B N     1 
ATOM   10086 C  CA    . LYS   B 1  156  ? -10.606 38.211  105.305 1.00 34.16 ? 154  LYS   B CA    1 
ATOM   10087 C  C     . LYS   B 1  156  ? -9.089  38.109  105.385 1.00 31.95 ? 154  LYS   B C     1 
ATOM   10088 O  O     . LYS   B 1  156  ? -8.474  38.510  106.376 1.00 31.66 ? 154  LYS   B O     1 
ATOM   10089 C  CB    . LYS   B 1  156  ? -11.004 39.575  104.726 1.00 40.89 ? 154  LYS   B CB    1 
ATOM   10090 N  N     . LEU   B 1  157  ? -8.486  37.565  104.334 1.00 30.41 ? 155  LEU   B N     1 
ATOM   10091 C  CA    . LEU   B 1  157  ? -7.049  37.362  104.278 1.00 32.49 ? 155  LEU   B CA    1 
ATOM   10092 C  C     . LEU   B 1  157  ? -6.426  38.317  103.271 1.00 39.56 ? 155  LEU   B C     1 
ATOM   10093 O  O     . LEU   B 1  157  ? -7.003  38.586  102.215 1.00 41.70 ? 155  LEU   B O     1 
ATOM   10094 C  CB    . LEU   B 1  157  ? -6.721  35.927  103.865 1.00 36.58 ? 155  LEU   B CB    1 
ATOM   10095 C  CG    . LEU   B 1  157  ? -5.232  35.593  103.746 1.00 45.84 ? 155  LEU   B CG    1 
ATOM   10096 C  CD1   . LEU   B 1  157  ? -4.583  35.568  105.123 1.00 35.83 ? 155  LEU   B CD1   1 
ATOM   10097 C  CD2   . LEU   B 1  157  ? -5.024  34.272  103.018 1.00 40.21 ? 155  LEU   B CD2   1 
ATOM   10098 N  N     . THR   B 1  158  ? -5.250  38.833  103.608 1.00 39.57 ? 156  THR   B N     1 
ATOM   10099 C  CA    . THR   B 1  158  ? -4.397  39.523  102.655 1.00 40.82 ? 156  THR   B CA    1 
ATOM   10100 C  C     . THR   B 1  158  ? -3.018  38.889  102.718 1.00 41.22 ? 156  THR   B C     1 
ATOM   10101 O  O     . THR   B 1  158  ? -2.645  38.273  103.720 1.00 37.41 ? 156  THR   B O     1 
ATOM   10102 C  CB    . THR   B 1  158  ? -4.280  41.015  102.969 1.00 42.58 ? 156  THR   B CB    1 
ATOM   10103 O  OG1   . THR   B 1  158  ? -3.572  41.180  104.202 1.00 38.27 ? 156  THR   B OG1   1 
ATOM   10104 C  CG2   . THR   B 1  158  ? -5.657  41.649  103.094 1.00 41.17 ? 156  THR   B CG2   1 
ATOM   10105 N  N     . SER   B 1  159  ? -2.263  39.034  101.629 1.00 34.19 ? 157  SER   B N     1 
ATOM   10106 C  CA    . SER   B 1  159  ? -0.909  38.495  101.602 1.00 35.83 ? 157  SER   B CA    1 
ATOM   10107 C  C     . SER   B 1  159  ? 0.064   39.396  102.343 1.00 32.00 ? 157  SER   B C     1 
ATOM   10108 O  O     . SER   B 1  159  ? 1.052   38.912  102.909 1.00 33.14 ? 157  SER   B O     1 
ATOM   10109 C  CB    . SER   B 1  159  ? -0.445  38.304  100.155 1.00 34.66 ? 157  SER   B CB    1 
ATOM   10110 O  OG    . SER   B 1  159  ? -1.007  39.304  99.320  1.00 48.14 ? 157  SER   B OG    1 
ATOM   10111 N  N     . THR   B 1  160  ? -0.191  40.697  102.339 1.00 28.52 ? 158  THR   B N     1 
ATOM   10112 C  CA    . THR   B 1  160  ? 0.671   41.664  102.993 1.00 25.11 ? 158  THR   B CA    1 
ATOM   10113 C  C     . THR   B 1  160  ? -0.182  42.627  103.805 1.00 22.80 ? 158  THR   B C     1 
ATOM   10114 O  O     . THR   B 1  160  ? -1.409  42.681  103.679 1.00 27.53 ? 158  THR   B O     1 
ATOM   10115 C  CB    . THR   B 1  160  ? 1.534   42.433  101.984 1.00 27.41 ? 158  THR   B CB    1 
ATOM   10116 O  OG1   . THR   B 1  160  ? 0.678   43.087  101.044 1.00 29.35 ? 158  THR   B OG1   1 
ATOM   10117 C  CG2   . THR   B 1  160  ? 2.502   41.489  101.259 1.00 27.34 ? 158  THR   B CG2   1 
ATOM   10118 N  N     . VAL   B 1  161  ? 0.513   43.430  104.599 1.00 19.54 ? 159  VAL   B N     1 
ATOM   10119 C  CA    . VAL   B 1  161  ? -0.036  44.114  105.756 1.00 22.73 ? 159  VAL   B CA    1 
ATOM   10120 C  C     . VAL   B 1  161  ? 0.173   45.604  105.555 1.00 20.30 ? 159  VAL   B C     1 
ATOM   10121 O  O     . VAL   B 1  161  ? 1.272   46.033  105.188 1.00 19.27 ? 159  VAL   B O     1 
ATOM   10122 C  CB    . VAL   B 1  161  ? 0.706   43.620  107.014 1.00 27.28 ? 159  VAL   B CB    1 
ATOM   10123 C  CG1   . VAL   B 1  161  ? 0.694   44.644  108.108 1.00 34.90 ? 159  VAL   B CG1   1 
ATOM   10124 C  CG2   . VAL   B 1  161  ? 0.125   42.283  107.466 1.00 37.87 ? 159  VAL   B CG2   1 
ATOM   10125 N  N     . ASN   B 1  162  ? -0.874  46.397  105.783 1.00 19.05 ? 160  ASN   B N     1 
ATOM   10126 C  CA    . ASN   B 1  162  ? -0.689  47.843  105.747 1.00 19.82 ? 160  ASN   B CA    1 
ATOM   10127 C  C     . ASN   B 1  162  ? -0.195  48.266  107.119 1.00 18.41 ? 160  ASN   B C     1 
ATOM   10128 O  O     . ASN   B 1  162  ? -0.968  48.604  108.010 1.00 19.58 ? 160  ASN   B O     1 
ATOM   10129 C  CB    . ASN   B 1  162  ? -1.958  48.583  105.354 1.00 19.77 ? 160  ASN   B CB    1 
ATOM   10130 C  CG    . ASN   B 1  162  ? -1.715  50.071  105.186 1.00 19.66 ? 160  ASN   B CG    1 
ATOM   10131 O  OD1   . ASN   B 1  162  ? -0.766  50.615  105.744 1.00 20.18 ? 160  ASN   B OD1   1 
ATOM   10132 N  ND2   . ASN   B 1  162  ? -2.577  50.738  104.428 1.00 22.58 ? 160  ASN   B ND2   1 
ATOM   10133 N  N     . ASP   B 1  163  ? 1.128   48.234  107.280 1.00 18.52 ? 161  ASP   B N     1 
ATOM   10134 C  CA    . ASP   B 1  163  ? 1.728   48.521  108.571 1.00 18.28 ? 161  ASP   B CA    1 
ATOM   10135 C  C     . ASP   B 1  163  ? 1.592   49.975  108.980 1.00 18.73 ? 161  ASP   B C     1 
ATOM   10136 O  O     . ASP   B 1  163  ? 1.615   50.256  110.178 1.00 18.20 ? 161  ASP   B O     1 
ATOM   10137 C  CB    . ASP   B 1  163  ? 3.190   48.055  108.606 1.00 19.12 ? 161  ASP   B CB    1 
ATOM   10138 C  CG    . ASP   B 1  163  ? 4.005   48.559  107.443 1.00 22.25 ? 161  ASP   B CG    1 
ATOM   10139 O  OD1   . ASP   B 1  163  ? 3.552   48.452  106.289 1.00 19.36 ? 161  ASP   B OD1   1 
ATOM   10140 O  OD2   . ASP   B 1  163  ? 5.134   49.032  107.692 1.00 23.46 ? 161  ASP   B OD2   1 
ATOM   10141 N  N     . ARG   B 1  164  ? 1.435   50.902  108.030 1.00 18.08 ? 162  ARG   B N     1 
ATOM   10142 C  CA    . ARG   B 1  164  ? 1.180   52.282  108.428 1.00 16.81 ? 162  ARG   B CA    1 
ATOM   10143 C  C     . ARG   B 1  164  ? -0.226  52.440  108.979 1.00 15.82 ? 162  ARG   B C     1 
ATOM   10144 O  O     . ARG   B 1  164  ? -0.445  53.165  109.960 1.00 16.54 ? 162  ARG   B O     1 
ATOM   10145 C  CB    . ARG   B 1  164  ? 1.409   53.232  107.254 1.00 17.81 ? 162  ARG   B CB    1 
ATOM   10146 C  CG    . ARG   B 1  164  ? 2.858   53.265  106.778 1.00 18.19 ? 162  ARG   B CG    1 
ATOM   10147 C  CD    . ARG   B 1  164  ? 3.848   53.340  107.929 1.00 26.29 ? 162  ARG   B CD    1 
ATOM   10148 N  NE    . ARG   B 1  164  ? 3.567   54.425  108.856 1.00 33.96 ? 162  ARG   B NE    1 
ATOM   10149 C  CZ    . ARG   B 1  164  ? 3.984   54.452  110.114 1.00 37.31 ? 162  ARG   B CZ    1 
ATOM   10150 N  NH1   . ARG   B 1  164  ? 4.702   53.463  110.626 1.00 40.53 ? 162  ARG   B NH1   1 
ATOM   10151 N  NH2   . ARG   B 1  164  ? 3.675   55.496  110.877 1.00 33.20 ? 162  ARG   B NH2   1 
ATOM   10152 N  N     . SER   B 1  165  ? -1.192  51.774  108.349 1.00 18.77 ? 163  SER   B N     1 
ATOM   10153 C  CA    . SER   B 1  165  ? -2.556  51.808  108.853 1.00 16.80 ? 163  SER   B CA    1 
ATOM   10154 C  C     . SER   B 1  165  ? -2.629  51.152  110.223 1.00 16.12 ? 163  SER   B C     1 
ATOM   10155 O  O     . SER   B 1  165  ? -3.325  51.639  111.120 1.00 16.98 ? 163  SER   B O     1 
ATOM   10156 C  CB    . SER   B 1  165  ? -3.467  51.080  107.863 1.00 16.99 ? 163  SER   B CB    1 
ATOM   10157 O  OG    . SER   B 1  165  ? -4.756  50.882  108.415 1.00 20.13 ? 163  SER   B OG    1 
ATOM   10158 N  N     . LEU   B 1  166  ? -1.897  50.051  110.402 1.00 17.06 ? 164  LEU   B N     1 
ATOM   10159 C  CA    . LEU   B 1  166  ? -1.926  49.362  111.686 1.00 18.72 ? 164  LEU   B CA    1 
ATOM   10160 C  C     . LEU   B 1  166  ? -1.243  50.181  112.770 1.00 17.09 ? 164  LEU   B C     1 
ATOM   10161 O  O     . LEU   B 1  166  ? -1.721  50.224  113.903 1.00 18.39 ? 164  LEU   B O     1 
ATOM   10162 C  CB    . LEU   B 1  166  ? -1.275  47.989  111.543 1.00 16.46 ? 164  LEU   B CB    1 
ATOM   10163 C  CG    . LEU   B 1  166  ? -2.196  47.030  110.795 1.00 17.70 ? 164  LEU   B CG    1 
ATOM   10164 C  CD1   . LEU   B 1  166  ? -1.470  45.766  110.448 1.00 23.37 ? 164  LEU   B CD1   1 
ATOM   10165 C  CD2   . LEU   B 1  166  ? -3.457  46.748  111.615 1.00 19.77 ? 164  LEU   B CD2   1 
ATOM   10166 N  N     . ALA   B 1  167  ? -0.110  50.812  112.445 1.00 16.94 ? 165  ALA   B N     1 
ATOM   10167 C  CA    . ALA   B 1  167  ? 0.561   51.658  113.421 1.00 17.84 ? 165  ALA   B CA    1 
ATOM   10168 C  C     . ALA   B 1  167  ? -0.336  52.813  113.844 1.00 18.09 ? 165  ALA   B C     1 
ATOM   10169 O  O     . ALA   B 1  167  ? -0.449  53.123  115.033 1.00 19.66 ? 165  ALA   B O     1 
ATOM   10170 C  CB    . ALA   B 1  167  ? 1.882   52.160  112.840 1.00 20.30 ? 165  ALA   B CB    1 
ATOM   10171 N  N     . ALA   B 1  168  ? -1.006  53.442  112.875 1.00 19.15 ? 166  ALA   B N     1 
ATOM   10172 C  CA    . ALA   B 1  168  ? -1.959  54.496  113.190 1.00 16.85 ? 166  ALA   B CA    1 
ATOM   10173 C  C     . ALA   B 1  168  ? -3.083  53.969  114.071 1.00 17.10 ? 166  ALA   B C     1 
ATOM   10174 O  O     . ALA   B 1  168  ? -3.464  54.607  115.051 1.00 19.08 ? 166  ALA   B O     1 
ATOM   10175 C  CB    . ALA   B 1  168  ? -2.536  55.047  111.885 1.00 19.20 ? 166  ALA   B CB    1 
ATOM   10176 N  N     . ALA   B 1  169  ? -3.609  52.788  113.735 1.00 17.39 ? 167  ALA   B N     1 
ATOM   10177 C  CA    . ALA   B 1  169  ? -4.718  52.234  114.503 1.00 17.38 ? 167  ALA   B CA    1 
ATOM   10178 C  C     . ALA   B 1  169  ? -4.293  51.885  115.922 1.00 19.26 ? 167  ALA   B C     1 
ATOM   10179 O  O     . ALA   B 1  169  ? -5.066  52.068  116.865 1.00 18.48 ? 167  ALA   B O     1 
ATOM   10180 C  CB    . ALA   B 1  169  ? -5.273  51.003  113.791 1.00 17.95 ? 167  ALA   B CB    1 
ATOM   10181 N  N     . LEU   B 1  170  ? -3.072  51.376  116.095 1.00 18.43 ? 168  LEU   B N     1 
ATOM   10182 C  CA    . LEU   B 1  170  ? -2.625  51.025  117.439 1.00 17.40 ? 168  LEU   B CA    1 
ATOM   10183 C  C     . LEU   B 1  170  ? -2.413  52.271  118.284 1.00 17.87 ? 168  LEU   B C     1 
ATOM   10184 O  O     . LEU   B 1  170  ? -2.828  52.323  119.444 1.00 18.78 ? 168  LEU   B O     1 
ATOM   10185 C  CB    . LEU   B 1  170  ? -1.352  50.188  117.358 1.00 18.83 ? 168  LEU   B CB    1 
ATOM   10186 C  CG    . LEU   B 1  170  ? -0.879  49.642  118.706 1.00 19.39 ? 168  LEU   B CG    1 
ATOM   10187 C  CD1   . LEU   B 1  170  ? -1.942  48.780  119.371 1.00 22.92 ? 168  LEU   B CD1   1 
ATOM   10188 C  CD2   . LEU   B 1  170  ? 0.379   48.855  118.472 1.00 22.68 ? 168  LEU   B CD2   1 
ATOM   10189 N  N     . THR   B 1  171  ? -1.789  53.297  117.715 1.00 20.27 ? 169  THR   B N     1 
ATOM   10190 C  CA    . THR   B 1  171  ? -1.662  54.562  118.424 1.00 21.06 ? 169  THR   B CA    1 
ATOM   10191 C  C     . THR   B 1  171  ? -3.030  55.115  118.804 1.00 20.36 ? 169  THR   B C     1 
ATOM   10192 O  O     . THR   B 1  171  ? -3.245  55.569  119.935 1.00 20.91 ? 169  THR   B O     1 
ATOM   10193 C  CB    . THR   B 1  171  ? -0.914  55.555  117.543 1.00 21.53 ? 169  THR   B CB    1 
ATOM   10194 O  OG1   . THR   B 1  171  ? 0.403   55.055  117.300 1.00 24.46 ? 169  THR   B OG1   1 
ATOM   10195 C  CG2   . THR   B 1  171  ? -0.827  56.906  118.215 1.00 23.21 ? 169  THR   B CG2   1 
ATOM   10196 N  N     . ARG   B 1  172  ? -3.978  55.050  117.870 1.00 19.71 ? 170  ARG   B N     1 
ATOM   10197 C  CA    . ARG   B 1  172  ? -5.298  55.594  118.130 1.00 18.83 ? 170  ARG   B CA    1 
ATOM   10198 C  C     . ARG   B 1  172  ? -5.979  54.845  119.262 1.00 20.11 ? 170  ARG   B C     1 
ATOM   10199 O  O     . ARG   B 1  172  ? -6.527  55.456  120.178 1.00 20.38 ? 170  ARG   B O     1 
ATOM   10200 C  CB    . ARG   B 1  172  ? -6.143  55.547  116.865 1.00 18.65 ? 170  ARG   B CB    1 
ATOM   10201 C  CG    . ARG   B 1  172  ? -7.396  56.381  116.978 1.00 18.95 ? 170  ARG   B CG    1 
ATOM   10202 C  CD    . ARG   B 1  172  ? -8.291  56.223  115.749 1.00 19.39 ? 170  ARG   B CD    1 
ATOM   10203 N  NE    . ARG   B 1  172  ? -7.561  56.335  114.492 1.00 19.06 ? 170  ARG   B NE    1 
ATOM   10204 C  CZ    . ARG   B 1  172  ? -7.257  55.309  113.716 1.00 18.72 ? 170  ARG   B CZ    1 
ATOM   10205 N  NH1   . ARG   B 1  172  ? -7.579  54.072  114.050 1.00 19.90 ? 170  ARG   B NH1   1 
ATOM   10206 N  NH2   . ARG   B 1  172  ? -6.589  55.524  112.583 1.00 18.01 ? 170  ARG   B NH2   1 
ATOM   10207 N  N     . LEU   B 1  173  ? -5.952  53.511  119.215 1.00 20.01 ? 171  LEU   B N     1 
ATOM   10208 C  CA    . LEU   B 1  173  ? -6.680  52.759  120.233 1.00 19.96 ? 171  LEU   B CA    1 
ATOM   10209 C  C     . LEU   B 1  173  ? -6.037  52.906  121.606 1.00 20.84 ? 171  LEU   B C     1 
ATOM   10210 O  O     . LEU   B 1  173  ? -6.741  52.996  122.610 1.00 20.57 ? 171  LEU   B O     1 
ATOM   10211 C  CB    . LEU   B 1  173  ? -6.842  51.294  119.825 1.00 22.14 ? 171  LEU   B CB    1 
ATOM   10212 C  CG    . LEU   B 1  173  ? -5.659  50.331  119.871 1.00 23.57 ? 171  LEU   B CG    1 
ATOM   10213 C  CD1   . LEU   B 1  173  ? -5.610  49.626  121.226 1.00 24.79 ? 171  LEU   B CD1   1 
ATOM   10214 C  CD2   . LEU   B 1  173  ? -5.779  49.316  118.765 1.00 22.74 ? 171  LEU   B CD2   1 
ATOM   10215 N  N     . ILE   B 1  174  ? -4.706  52.932  121.675 1.00 20.58 ? 172  ILE   B N     1 
ATOM   10216 C  CA    . ILE   B 1  174  ? -4.068  53.088  122.980 1.00 19.68 ? 172  ILE   B CA    1 
ATOM   10217 C  C     . ILE   B 1  174  ? -4.317  54.480  123.538 1.00 21.80 ? 172  ILE   B C     1 
ATOM   10218 O  O     . ILE   B 1  174  ? -4.602  54.650  124.732 1.00 23.74 ? 172  ILE   B O     1 
ATOM   10219 C  CB    . ILE   B 1  174  ? -2.566  52.775  122.892 1.00 21.47 ? 172  ILE   B CB    1 
ATOM   10220 C  CG1   . ILE   B 1  174  ? -2.353  51.314  122.516 1.00 21.36 ? 172  ILE   B CG1   1 
ATOM   10221 C  CG2   . ILE   B 1  174  ? -1.897  53.104  124.221 1.00 23.51 ? 172  ILE   B CG2   1 
ATOM   10222 C  CD1   . ILE   B 1  174  ? -0.902  50.964  122.231 1.00 23.19 ? 172  ILE   B CD1   1 
ATOM   10223 N  N     . SER   B 1  175  ? -4.200  55.504  122.692 1.00 22.85 ? 173  SER   B N     1 
ATOM   10224 C  CA    . SER   B 1  175  ? -4.434  56.858  123.165 1.00 22.05 ? 173  SER   B CA    1 
ATOM   10225 C  C     . SER   B 1  175  ? -5.889  57.071  123.560 1.00 22.04 ? 173  SER   B C     1 
ATOM   10226 O  O     . SER   B 1  175  ? -6.181  57.925  124.399 1.00 25.78 ? 173  SER   B O     1 
ATOM   10227 C  CB    . SER   B 1  175  ? -4.008  57.875  122.107 1.00 25.05 ? 173  SER   B CB    1 
ATOM   10228 O  OG    . SER   B 1  175  ? -2.616  57.789  121.855 1.00 30.14 ? 173  SER   B OG    1 
ATOM   10229 N  N     . ARG   B 1  176  ? -6.805  56.310  122.968 1.00 21.94 ? 174  ARG   B N     1 
ATOM   10230 C  CA    . ARG   B 1  176  ? -8.218  56.443  123.289 1.00 22.45 ? 174  ARG   B CA    1 
ATOM   10231 C  C     . ARG   B 1  176  ? -8.607  55.616  124.512 1.00 23.02 ? 174  ARG   B C     1 
ATOM   10232 O  O     . ARG   B 1  176  ? -9.380  56.081  125.353 1.00 24.47 ? 174  ARG   B O     1 
ATOM   10233 C  CB    . ARG   B 1  176  ? -9.055  56.012  122.075 1.00 22.70 ? 174  ARG   B CB    1 
ATOM   10234 C  CG    . ARG   B 1  176  ? -10.550 56.325  122.193 1.00 24.43 ? 174  ARG   B CG    1 
ATOM   10235 C  CD    . ARG   B 1  176  ? -11.272 56.011  120.878 1.00 22.76 ? 174  ARG   B CD    1 
ATOM   10236 N  NE    . ARG   B 1  176  ? -11.417 54.576  120.668 1.00 22.73 ? 174  ARG   B NE    1 
ATOM   10237 C  CZ    . ARG   B 1  176  ? -10.829 53.871  119.707 1.00 24.48 ? 174  ARG   B CZ    1 
ATOM   10238 N  NH1   . ARG   B 1  176  ? -10.083 54.446  118.762 1.00 23.20 ? 174  ARG   B NH1   1 
ATOM   10239 N  NH2   . ARG   B 1  176  ? -10.999 52.552  119.680 1.00 28.09 ? 174  ARG   B NH2   1 
ATOM   10240 N  N     . CYS   B 1  177  ? -8.088  54.388  124.621 1.00 22.75 ? 175  CYS   B N     1 
ATOM   10241 C  CA    . CYS   B 1  177  ? -8.567  53.458  125.632 1.00 26.04 ? 175  CYS   B CA    1 
ATOM   10242 C  C     . CYS   B 1  177  ? -7.529  53.044  126.659 1.00 28.01 ? 175  CYS   B C     1 
ATOM   10243 O  O     . CYS   B 1  177  ? -7.914  52.501  127.701 1.00 29.86 ? 175  CYS   B O     1 
ATOM   10244 C  CB    . CYS   B 1  177  ? -9.147  52.196  124.983 1.00 24.46 ? 175  CYS   B CB    1 
ATOM   10245 S  SG    . CYS   B 1  177  ? -10.412 52.533  123.705 1.00 31.26 ? 175  CYS   B SG    1 
ATOM   10246 N  N     . GLY   B 1  178  ? -6.241  53.255  126.395 1.00 25.74 ? 176  GLY   B N     1 
ATOM   10247 C  CA    . GLY   B 1  178  ? -5.278  53.105  127.472 1.00 27.42 ? 176  GLY   B CA    1 
ATOM   10248 C  C     . GLY   B 1  178  ? -5.051  51.660  127.882 1.00 24.70 ? 176  GLY   B C     1 
ATOM   10249 O  O     . GLY   B 1  178  ? -5.342  50.712  127.158 1.00 25.80 ? 176  GLY   B O     1 
ATOM   10250 N  N     . GLU   B 1  179  ? -4.536  51.508  129.100 1.00 27.11 ? 177  GLU   B N     1 
ATOM   10251 C  CA    . GLU   B 1  179  ? -4.196  50.173  129.586 1.00 29.44 ? 177  GLU   B CA    1 
ATOM   10252 C  C     . GLU   B 1  179  ? -5.356  49.179  129.567 1.00 23.64 ? 177  GLU   B C     1 
ATOM   10253 O  O     . GLU   B 1  179  ? -5.111  48.005  129.240 1.00 25.91 ? 177  GLU   B O     1 
ATOM   10254 C  CB    . GLU   B 1  179  ? -3.535  50.255  130.969 1.00 30.13 ? 177  GLU   B CB    1 
ATOM   10255 C  CG    . GLU   B 1  179  ? -3.025  48.910  131.449 1.00 31.80 ? 177  GLU   B CG    1 
ATOM   10256 C  CD    . GLU   B 1  179  ? -2.442  48.954  132.843 1.00 47.66 ? 177  GLU   B CD    1 
ATOM   10257 O  OE1   . GLU   B 1  179  ? -2.160  50.064  133.345 1.00 52.15 ? 177  GLU   B OE1   1 
ATOM   10258 O  OE2   . GLU   B 1  179  ? -2.265  47.868  133.435 1.00 51.39 ? 177  GLU   B OE2   1 
ATOM   10259 N  N     . PRO   B 1  180  ? -6.602  49.546  129.901 1.00 25.57 ? 178  PRO   B N     1 
ATOM   10260 C  CA    . PRO   B 1  180  ? -7.665  48.524  129.898 1.00 27.35 ? 178  PRO   B CA    1 
ATOM   10261 C  C     . PRO   B 1  180  ? -7.832  47.788  128.579 1.00 28.75 ? 178  PRO   B C     1 
ATOM   10262 O  O     . PRO   B 1  180  ? -8.090  46.579  128.588 1.00 27.67 ? 178  PRO   B O     1 
ATOM   10263 C  CB    . PRO   B 1  180  ? -8.915  49.316  130.298 1.00 29.51 ? 178  PRO   B CB    1 
ATOM   10264 C  CG    . PRO   B 1  180  ? -8.383  50.414  131.161 1.00 30.84 ? 178  PRO   B CG    1 
ATOM   10265 C  CD    . PRO   B 1  180  ? -7.069  50.802  130.522 1.00 30.70 ? 178  PRO   B CD    1 
ATOM   10266 N  N     . VAL   B 1  181  ? -7.693  48.462  127.437 1.00 24.38 ? 179  VAL   B N     1 
ATOM   10267 C  CA    . VAL   B 1  181  ? -7.851  47.720  126.194 1.00 23.34 ? 179  VAL   B CA    1 
ATOM   10268 C  C     . VAL   B 1  181  ? -6.652  46.814  125.934 1.00 23.97 ? 179  VAL   B C     1 
ATOM   10269 O  O     . VAL   B 1  181  ? -6.801  45.725  125.363 1.00 25.54 ? 179  VAL   B O     1 
ATOM   10270 C  CB    . VAL   B 1  181  ? -8.158  48.650  125.004 1.00 24.28 ? 179  VAL   B CB    1 
ATOM   10271 C  CG1   . VAL   B 1  181  ? -6.916  49.422  124.593 1.00 23.39 ? 179  VAL   B CG1   1 
ATOM   10272 C  CG2   . VAL   B 1  181  ? -8.676  47.840  123.841 1.00 27.15 ? 179  VAL   B CG2   1 
ATOM   10273 N  N     . ILE   B 1  182  ? -5.451  47.245  126.328 1.00 23.20 ? 180  ILE   B N     1 
ATOM   10274 C  CA    . ILE   B 1  182  ? -4.270  46.400  126.188 1.00 22.33 ? 180  ILE   B CA    1 
ATOM   10275 C  C     . ILE   B 1  182  ? -4.424  45.137  127.021 1.00 25.89 ? 180  ILE   B C     1 
ATOM   10276 O  O     . ILE   B 1  182  ? -4.159  44.024  126.547 1.00 26.10 ? 180  ILE   B O     1 
ATOM   10277 C  CB    . ILE   B 1  182  ? -3.000  47.184  126.562 1.00 23.05 ? 180  ILE   B CB    1 
ATOM   10278 C  CG1   . ILE   B 1  182  ? -2.841  48.399  125.649 1.00 22.63 ? 180  ILE   B CG1   1 
ATOM   10279 C  CG2   . ILE   B 1  182  ? -1.778  46.286  126.445 1.00 26.42 ? 180  ILE   B CG2   1 
ATOM   10280 C  CD1   . ILE   B 1  182  ? -1.802  49.382  126.147 1.00 25.86 ? 180  ILE   B CD1   1 
ATOM   10281 N  N     . ARG   B 1  183  ? -4.860  45.294  128.275 1.00 27.28 ? 181  ARG   B N     1 
ATOM   10282 C  CA    . ARG   B 1  183  ? -5.076  44.149  129.153 1.00 29.07 ? 181  ARG   B CA    1 
ATOM   10283 C  C     . ARG   B 1  183  ? -6.090  43.180  128.557 1.00 29.19 ? 181  ARG   B C     1 
ATOM   10284 O  O     . ARG   B 1  183  ? -5.858  41.966  128.523 1.00 29.16 ? 181  ARG   B O     1 
ATOM   10285 C  CB    . ARG   B 1  183  ? -5.521  44.636  130.536 1.00 29.58 ? 181  ARG   B CB    1 
ATOM   10286 C  CG    . ARG   B 1  183  ? -6.019  43.544  131.482 1.00 38.68 ? 181  ARG   B CG    1 
ATOM   10287 C  CD    . ARG   B 1  183  ? -5.046  42.372  131.556 1.00 40.53 ? 181  ARG   B CD    1 
ATOM   10288 N  NE    . ARG   B 1  183  ? -3.699  42.788  131.917 1.00 44.77 ? 181  ARG   B NE    1 
ATOM   10289 C  CZ    . ARG   B 1  183  ? -2.607  42.097  131.624 1.00 38.87 ? 181  ARG   B CZ    1 
ATOM   10290 N  NH1   . ARG   B 1  183  ? -2.668  40.970  130.933 1.00 39.42 ? 181  ARG   B NH1   1 
ATOM   10291 N  NH2   . ARG   B 1  183  ? -1.425  42.551  132.027 1.00 42.02 ? 181  ARG   B NH2   1 
ATOM   10292 N  N     . ARG   B 1  184  ? -7.222  43.699  128.075 1.00 27.52 ? 182  ARG   B N     1 
ATOM   10293 C  CA    . ARG   B 1  184  ? -8.215  42.838  127.437 1.00 26.65 ? 182  ARG   B CA    1 
ATOM   10294 C  C     . ARG   B 1  184  ? -7.641  42.134  126.213 1.00 27.98 ? 182  ARG   B C     1 
ATOM   10295 O  O     . ARG   B 1  184  ? -7.894  40.944  126.001 1.00 29.87 ? 182  ARG   B O     1 
ATOM   10296 C  CB    . ARG   B 1  184  ? -9.464  43.641  127.069 1.00 30.22 ? 182  ARG   B CB    1 
ATOM   10297 C  CG    . ARG   B 1  184  ? -10.387 43.932  128.244 1.00 36.57 ? 182  ARG   B CG    1 
ATOM   10298 C  CD    . ARG   B 1  184  ? -11.376 42.793  128.506 1.00 41.13 ? 182  ARG   B CD    1 
ATOM   10299 N  NE    . ARG   B 1  184  ? -12.592 42.907  127.705 1.00 39.42 ? 182  ARG   B NE    1 
ATOM   10300 C  CZ    . ARG   B 1  184  ? -13.015 42.001  126.832 1.00 35.36 ? 182  ARG   B CZ    1 
ATOM   10301 N  NH1   . ARG   B 1  184  ? -12.352 40.874  126.626 1.00 37.51 ? 182  ARG   B NH1   1 
ATOM   10302 N  NH2   . ARG   B 1  184  ? -14.134 42.230  126.151 1.00 39.59 ? 182  ARG   B NH2   1 
ATOM   10303 N  N     . GLY   B 1  185  ? -6.870  42.852  125.393 1.00 26.99 ? 183  GLY   B N     1 
ATOM   10304 C  CA    . GLY   B 1  185  ? -6.282  42.227  124.222 1.00 23.81 ? 183  GLY   B CA    1 
ATOM   10305 C  C     . GLY   B 1  185  ? -5.301  41.127  124.578 1.00 27.79 ? 183  GLY   B C     1 
ATOM   10306 O  O     . GLY   B 1  185  ? -5.302  40.060  123.961 1.00 26.23 ? 183  GLY   B O     1 
ATOM   10307 N  N     . VAL   B 1  186  ? -4.454  41.373  125.580 1.00 24.38 ? 184  VAL   B N     1 
ATOM   10308 C  CA    . VAL   B 1  186  ? -3.487  40.364  126.009 1.00 30.08 ? 184  VAL   B CA    1 
ATOM   10309 C  C     . VAL   B 1  186  ? -4.205  39.114  126.501 1.00 29.75 ? 184  VAL   B C     1 
ATOM   10310 O  O     . VAL   B 1  186  ? -3.896  37.990  126.085 1.00 29.55 ? 184  VAL   B O     1 
ATOM   10311 C  CB    . VAL   B 1  186  ? -2.551  40.945  127.083 1.00 27.63 ? 184  VAL   B CB    1 
ATOM   10312 C  CG1   . VAL   B 1  186  ? -1.799  39.828  127.791 1.00 27.88 ? 184  VAL   B CG1   1 
ATOM   10313 C  CG2   . VAL   B 1  186  ? -1.572  41.930  126.453 1.00 28.06 ? 184  VAL   B CG2   1 
ATOM   10314 N  N     . ASP   B 1  187  ? -5.186  39.295  127.386 1.00 27.54 ? 185  ASP   B N     1 
ATOM   10315 C  CA    . ASP   B 1  187  ? -5.924  38.152  127.913 1.00 31.98 ? 185  ASP   B CA    1 
ATOM   10316 C  C     . ASP   B 1  187  ? -6.656  37.417  126.805 1.00 33.45 ? 185  ASP   B C     1 
ATOM   10317 O  O     . ASP   B 1  187  ? -6.757  36.185  126.829 1.00 30.13 ? 185  ASP   B O     1 
ATOM   10318 C  CB    . ASP   B 1  187  ? -6.912  38.608  128.985 1.00 32.55 ? 185  ASP   B CB    1 
ATOM   10319 C  CG    . ASP   B 1  187  ? -6.222  39.163  130.215 1.00 32.62 ? 185  ASP   B CG    1 
ATOM   10320 O  OD1   . ASP   B 1  187  ? -5.014  38.895  130.392 1.00 39.87 ? 185  ASP   B OD1   1 
ATOM   10321 O  OD2   . ASP   B 1  187  ? -6.889  39.863  131.006 1.00 37.39 ? 185  ASP   B OD2   1 
ATOM   10322 N  N     . MET   B 1  188  ? -7.168  38.159  125.820 1.00 30.97 ? 186  MET   B N     1 
ATOM   10323 C  CA    . MET   B 1  188  ? -7.872  37.539  124.705 1.00 30.48 ? 186  MET   B CA    1 
ATOM   10324 C  C     . MET   B 1  188  ? -6.918  36.715  123.851 1.00 28.97 ? 186  MET   B C     1 
ATOM   10325 O  O     . MET   B 1  188  ? -7.222  35.574  123.484 1.00 31.48 ? 186  MET   B O     1 
ATOM   10326 C  CB    . MET   B 1  188  ? -8.549  38.621  123.865 1.00 31.38 ? 186  MET   B CB    1 
ATOM   10327 C  CG    . MET   B 1  188  ? -9.317  38.097  122.675 1.00 36.91 ? 186  MET   B CG    1 
ATOM   10328 S  SD    . MET   B 1  188  ? -10.686 37.049  123.185 1.00 54.62 ? 186  MET   B SD    1 
ATOM   10329 C  CE    . MET   B 1  188  ? -11.542 38.140  124.324 1.00 44.13 ? 186  MET   B CE    1 
ATOM   10330 N  N     . ALA   B 1  189  ? -5.754  37.275  123.522 1.00 30.57 ? 187  ALA   B N     1 
ATOM   10331 C  CA    . ALA   B 1  189  ? -4.803  36.534  122.701 1.00 29.54 ? 187  ALA   B CA    1 
ATOM   10332 C  C     . ALA   B 1  189  ? -4.252  35.331  123.455 1.00 30.42 ? 187  ALA   B C     1 
ATOM   10333 O  O     . ALA   B 1  189  ? -4.025  34.270  122.864 1.00 29.51 ? 187  ALA   B O     1 
ATOM   10334 C  CB    . ALA   B 1  189  ? -3.675  37.453  122.238 1.00 30.21 ? 187  ALA   B CB    1 
ATOM   10335 N  N     . MET   B 1  190  ? -4.037  35.477  124.762 1.00 28.02 ? 188  MET   B N     1 
ATOM   10336 C  CA    . MET   B 1  190  ? -3.571  34.354  125.569 1.00 29.92 ? 188  MET   B CA    1 
ATOM   10337 C  C     . MET   B 1  190  ? -4.551  33.189  125.498 1.00 31.34 ? 188  MET   B C     1 
ATOM   10338 O  O     . MET   B 1  190  ? -4.150  32.037  125.297 1.00 32.66 ? 188  MET   B O     1 
ATOM   10339 C  CB    . MET   B 1  190  ? -3.385  34.802  127.019 1.00 29.32 ? 188  MET   B CB    1 
ATOM   10340 C  CG    . MET   B 1  190  ? -2.536  33.864  127.841 1.00 35.64 ? 188  MET   B CG    1 
ATOM   10341 S  SD    . MET   B 1  190  ? -2.480  34.373  129.565 1.00 43.88 ? 188  MET   B SD    1 
ATOM   10342 C  CE    . MET   B 1  190  ? -2.188  36.136  129.408 1.00 36.61 ? 188  MET   B CE    1 
ATOM   10343 N  N     . ARG   B 1  191  ? -5.846  33.476  125.653 1.00 29.94 ? 189  ARG   B N     1 
ATOM   10344 C  CA    . ARG   B 1  191  ? -6.855  32.423  125.585 1.00 35.90 ? 189  ARG   B CA    1 
ATOM   10345 C  C     . ARG   B 1  191  ? -6.936  31.832  124.183 1.00 35.75 ? 189  ARG   B C     1 
ATOM   10346 O  O     . ARG   B 1  191  ? -6.983  30.607  124.015 1.00 32.27 ? 189  ARG   B O     1 
ATOM   10347 C  CB    . ARG   B 1  191  ? -8.219  32.962  126.029 1.00 30.56 ? 189  ARG   B CB    1 
ATOM   10348 N  N     . MET   B 1  192  ? -6.948  32.685  123.159 1.00 29.97 ? 190  MET   B N     1 
ATOM   10349 C  CA    . MET   B 1  192  ? -7.054  32.174  121.799 1.00 29.17 ? 190  MET   B CA    1 
ATOM   10350 C  C     . MET   B 1  192  ? -5.854  31.309  121.447 1.00 32.39 ? 190  MET   B C     1 
ATOM   10351 O  O     . MET   B 1  192  ? -6.003  30.183  120.959 1.00 30.12 ? 190  MET   B O     1 
ATOM   10352 C  CB    . MET   B 1  192  ? -7.194  33.328  120.810 1.00 31.51 ? 190  MET   B CB    1 
ATOM   10353 C  CG    . MET   B 1  192  ? -8.437  34.158  121.037 1.00 36.16 ? 190  MET   B CG    1 
ATOM   10354 S  SD    . MET   B 1  192  ? -8.656  35.337  119.701 1.00 44.46 ? 190  MET   B SD    1 
ATOM   10355 C  CE    . MET   B 1  192  ? -9.159  34.219  118.400 1.00 36.50 ? 190  MET   B CE    1 
ATOM   10356 N  N     . MET   B 1  193  ? -4.650  31.810  121.707 1.00 29.02 ? 191  MET   B N     1 
ATOM   10357 C  CA    A MET   B 1  193  ? -3.444  31.093  121.316 0.43 31.82 ? 191  MET   B CA    1 
ATOM   10358 C  CA    B MET   B 1  193  ? -3.459  31.079  121.304 0.57 31.80 ? 191  MET   B CA    1 
ATOM   10359 C  C     . MET   B 1  193  ? -3.125  29.925  122.237 1.00 32.40 ? 191  MET   B C     1 
ATOM   10360 O  O     . MET   B 1  193  ? -2.383  29.023  121.836 1.00 29.42 ? 191  MET   B O     1 
ATOM   10361 C  CB    A MET   B 1  193  ? -2.252  32.053  121.270 0.43 32.82 ? 191  MET   B CB    1 
ATOM   10362 C  CB    B MET   B 1  193  ? -2.270  32.030  121.170 0.57 32.82 ? 191  MET   B CB    1 
ATOM   10363 C  CG    A MET   B 1  193  ? -2.474  33.273  120.389 0.43 30.90 ? 191  MET   B CG    1 
ATOM   10364 C  CG    B MET   B 1  193  ? -2.342  32.898  119.926 0.57 31.94 ? 191  MET   B CG    1 
ATOM   10365 S  SD    A MET   B 1  193  ? -1.064  34.399  120.402 0.43 30.01 ? 191  MET   B SD    1 
ATOM   10366 S  SD    B MET   B 1  193  ? -0.791  33.742  119.580 0.57 35.63 ? 191  MET   B SD    1 
ATOM   10367 C  CE    A MET   B 1  193  ? -0.027  33.630  119.166 0.43 37.42 ? 191  MET   B CE    1 
ATOM   10368 C  CE    B MET   B 1  193  ? -0.736  34.915  120.932 0.57 33.35 ? 191  MET   B CE    1 
ATOM   10369 N  N     . GLY   B 1  194  ? -3.667  29.919  123.449 1.00 31.11 ? 192  GLY   B N     1 
ATOM   10370 C  CA    . GLY   B 1  194  ? -3.347  28.873  124.396 1.00 31.99 ? 192  GLY   B CA    1 
ATOM   10371 C  C     . GLY   B 1  194  ? -4.426  27.826  124.560 1.00 31.23 ? 192  GLY   B C     1 
ATOM   10372 O  O     . GLY   B 1  194  ? -4.140  26.721  125.033 1.00 29.82 ? 192  GLY   B O     1 
ATOM   10373 N  N     . GLU   B 1  195  ? -5.663  28.153  124.173 1.00 30.06 ? 193  GLU   B N     1 
ATOM   10374 C  CA    . GLU   B 1  195  ? -6.796  27.283  124.482 1.00 33.09 ? 193  GLU   B CA    1 
ATOM   10375 C  C     . GLU   B 1  195  ? -7.699  27.003  123.288 1.00 32.45 ? 193  GLU   B C     1 
ATOM   10376 O  O     . GLU   B 1  195  ? -8.398  25.985  123.267 1.00 30.16 ? 193  GLU   B O     1 
ATOM   10377 C  CB    . GLU   B 1  195  ? -7.640  27.876  125.612 1.00 36.18 ? 193  GLU   B CB    1 
ATOM   10378 C  CG    . GLU   B 1  195  ? -6.909  28.015  126.928 1.00 47.55 ? 193  GLU   B CG    1 
ATOM   10379 C  CD    . GLU   B 1  195  ? -7.748  28.715  127.972 1.00 48.98 ? 193  GLU   B CD    1 
ATOM   10380 O  OE1   . GLU   B 1  195  ? -8.933  28.990  127.689 1.00 53.64 ? 193  GLU   B OE1   1 
ATOM   10381 O  OE2   . GLU   B 1  195  ? -7.223  28.991  129.071 1.00 62.58 ? 193  GLU   B OE2   1 
ATOM   10382 N  N     . GLN   B 1  196  ? -7.726  27.903  122.308 1.00 33.54 ? 194  GLN   B N     1 
ATOM   10383 C  CA    . GLN   B 1  196  ? -8.611  27.754  121.159 1.00 31.33 ? 194  GLN   B CA    1 
ATOM   10384 C  C     . GLN   B 1  196  ? -7.878  27.271  119.913 1.00 33.99 ? 194  GLN   B C     1 
ATOM   10385 O  O     . GLN   B 1  196  ? -8.274  26.271  119.310 1.00 36.56 ? 194  GLN   B O     1 
ATOM   10386 C  CB    . GLN   B 1  196  ? -9.352  29.068  120.877 1.00 34.88 ? 194  GLN   B CB    1 
ATOM   10387 N  N     . PHE   B 1  197  ? -6.809  27.960  119.515 1.00 30.73 ? 195  PHE   B N     1 
ATOM   10388 C  CA    . PHE   B 1  197  ? -6.042  27.524  118.354 1.00 34.87 ? 195  PHE   B CA    1 
ATOM   10389 C  C     . PHE   B 1  197  ? -5.303  26.224  118.629 1.00 30.71 ? 195  PHE   B C     1 
ATOM   10390 O  O     . PHE   B 1  197  ? -5.007  25.470  117.695 1.00 33.21 ? 195  PHE   B O     1 
ATOM   10391 C  CB    . PHE   B 1  197  ? -5.040  28.601  117.946 1.00 33.78 ? 195  PHE   B CB    1 
ATOM   10392 C  CG    . PHE   B 1  197  ? -5.675  29.886  117.506 1.00 33.94 ? 195  PHE   B CG    1 
ATOM   10393 C  CD1   . PHE   B 1  197  ? -6.903  29.886  116.867 1.00 38.85 ? 195  PHE   B CD1   1 
ATOM   10394 C  CD2   . PHE   B 1  197  ? -5.039  31.094  117.730 1.00 35.99 ? 195  PHE   B CD2   1 
ATOM   10395 C  CE1   . PHE   B 1  197  ? -7.487  31.071  116.457 1.00 41.30 ? 195  PHE   B CE1   1 
ATOM   10396 C  CE2   . PHE   B 1  197  ? -5.617  32.284  117.324 1.00 36.55 ? 195  PHE   B CE2   1 
ATOM   10397 C  CZ    . PHE   B 1  197  ? -6.841  32.270  116.688 1.00 39.29 ? 195  PHE   B CZ    1 
ATOM   10398 N  N     . VAL   B 1  198  ? -4.964  25.963  119.887 1.00 29.61 ? 196  VAL   B N     1 
ATOM   10399 C  CA    . VAL   B 1  198  ? -4.355  24.702  120.282 1.00 27.73 ? 196  VAL   B CA    1 
ATOM   10400 C  C     . VAL   B 1  198  ? -5.133  24.155  121.465 1.00 28.72 ? 196  VAL   B C     1 
ATOM   10401 O  O     . VAL   B 1  198  ? -5.755  24.901  122.228 1.00 28.63 ? 196  VAL   B O     1 
ATOM   10402 C  CB    . VAL   B 1  198  ? -2.859  24.826  120.648 1.00 25.26 ? 196  VAL   B CB    1 
ATOM   10403 C  CG1   . VAL   B 1  198  ? -2.046  25.284  119.459 1.00 27.19 ? 196  VAL   B CG1   1 
ATOM   10404 C  CG2   . VAL   B 1  198  ? -2.679  25.758  121.839 1.00 30.37 ? 196  VAL   B CG2   1 
ATOM   10405 N  N     . THR   B 1  199  ? -5.092  22.837  121.615 1.00 24.81 ? 197  THR   B N     1 
ATOM   10406 C  CA    . THR   B 1  199  ? -5.640  22.222  122.812 1.00 26.30 ? 197  THR   B CA    1 
ATOM   10407 C  C     . THR   B 1  199  ? -4.736  22.471  124.002 1.00 29.61 ? 197  THR   B C     1 
ATOM   10408 O  O     . THR   B 1  199  ? -5.218  22.625  125.126 1.00 31.51 ? 197  THR   B O     1 
ATOM   10409 C  CB    . THR   B 1  199  ? -5.830  20.736  122.549 1.00 26.15 ? 197  THR   B CB    1 
ATOM   10410 O  OG1   . THR   B 1  199  ? -6.682  20.595  121.406 1.00 28.53 ? 197  THR   B OG1   1 
ATOM   10411 C  CG2   . THR   B 1  199  ? -6.464  20.046  123.739 1.00 27.87 ? 197  THR   B CG2   1 
ATOM   10412 N  N     . GLY   B 1  200  ? -3.433  22.543  123.775 1.00 24.19 ? 198  GLY   B N     1 
ATOM   10413 C  CA    . GLY   B 1  200  ? -2.511  22.884  124.835 1.00 26.50 ? 198  GLY   B CA    1 
ATOM   10414 C  C     . GLY   B 1  200  ? -1.182  23.245  124.223 1.00 25.61 ? 198  GLY   B C     1 
ATOM   10415 O  O     . GLY   B 1  200  ? -0.913  22.943  123.057 1.00 25.68 ? 198  GLY   B O     1 
ATOM   10416 N  N     . GLU   B 1  201  ? -0.346  23.899  125.025 1.00 30.25 ? 199  GLU   B N     1 
ATOM   10417 C  CA    . GLU   B 1  201  ? 0.976   24.261  124.537 1.00 29.67 ? 199  GLU   B CA    1 
ATOM   10418 C  C     . GLU   B 1  201  ? 1.914   23.065  124.513 1.00 27.22 ? 199  GLU   B C     1 
ATOM   10419 O  O     . GLU   B 1  201  ? 2.824   23.017  123.680 1.00 33.78 ? 199  GLU   B O     1 
ATOM   10420 C  CB    . GLU   B 1  201  ? 1.562   25.390  125.384 1.00 35.42 ? 199  GLU   B CB    1 
ATOM   10421 C  CG    . GLU   B 1  201  ? 2.768   26.061  124.750 1.00 45.55 ? 199  GLU   B CG    1 
ATOM   10422 C  CD    . GLU   B 1  201  ? 3.441   27.044  125.685 1.00 50.81 ? 199  GLU   B CD    1 
ATOM   10423 O  OE1   . GLU   B 1  201  ? 3.042   27.104  126.867 1.00 47.35 ? 199  GLU   B OE1   1 
ATOM   10424 O  OE2   . GLU   B 1  201  ? 4.368   27.753  125.235 1.00 57.73 ? 199  GLU   B OE2   1 
ATOM   10425 N  N     . THR   B 1  202  ? 1.718   22.106  125.414 1.00 25.28 ? 200  THR   B N     1 
ATOM   10426 C  CA    . THR   B 1  202  ? 2.498   20.878  125.461 1.00 25.60 ? 200  THR   B CA    1 
ATOM   10427 C  C     . THR   B 1  202  ? 1.537   19.698  125.443 1.00 27.94 ? 200  THR   B C     1 
ATOM   10428 O  O     . THR   B 1  202  ? 0.343   19.845  125.729 1.00 26.32 ? 200  THR   B O     1 
ATOM   10429 C  CB    . THR   B 1  202  ? 3.296   20.783  126.758 1.00 28.74 ? 200  THR   B CB    1 
ATOM   10430 O  OG1   . THR   B 1  202  ? 2.385   20.632  127.853 1.00 31.19 ? 200  THR   B OG1   1 
ATOM   10431 C  CG2   . THR   B 1  202  ? 4.119   22.041  126.973 1.00 32.77 ? 200  THR   B CG2   1 
ATOM   10432 N  N     . ILE   B 1  203  ? 2.072   18.520  125.113 1.00 26.33 ? 201  ILE   B N     1 
ATOM   10433 C  CA    . ILE   B 1  203  ? 1.235   17.323  125.088 1.00 25.09 ? 201  ILE   B CA    1 
ATOM   10434 C  C     . ILE   B 1  203  ? 0.671   17.045  126.471 1.00 28.04 ? 201  ILE   B C     1 
ATOM   10435 O  O     . ILE   B 1  203  ? -0.478  16.606  126.606 1.00 25.88 ? 201  ILE   B O     1 
ATOM   10436 C  CB    . ILE   B 1  203  ? 1.975   16.110  124.485 1.00 25.17 ? 201  ILE   B CB    1 
ATOM   10437 C  CG1   . ILE   B 1  203  ? 0.983   14.985  124.159 1.00 25.53 ? 201  ILE   B CG1   1 
ATOM   10438 C  CG2   . ILE   B 1  203  ? 3.060   15.598  125.430 1.00 27.02 ? 201  ILE   B CG2   1 
ATOM   10439 C  CD1   . ILE   B 1  203  ? -0.092  15.388  123.135 1.00 22.55 ? 201  ILE   B CD1   1 
ATOM   10440 N  N     . ARG   B 1  204  ? 1.442   17.345  127.522 1.00 28.31 ? 202  ARG   B N     1 
ATOM   10441 C  CA    . ARG   B 1  204  ? 0.963   17.160  128.888 1.00 27.50 ? 202  ARG   B CA    1 
ATOM   10442 C  C     . ARG   B 1  204  ? -0.286  17.991  129.139 1.00 25.55 ? 202  ARG   B C     1 
ATOM   10443 O  O     . ARG   B 1  204  ? -1.285  17.493  129.677 1.00 30.17 ? 202  ARG   B O     1 
ATOM   10444 C  CB    . ARG   B 1  204  ? 2.072   17.561  129.866 1.00 31.29 ? 202  ARG   B CB    1 
ATOM   10445 C  CG    . ARG   B 1  204  ? 1.989   16.924  131.226 1.00 44.36 ? 202  ARG   B CG    1 
ATOM   10446 C  CD    . ARG   B 1  204  ? 3.280   17.173  132.000 1.00 39.18 ? 202  ARG   B CD    1 
ATOM   10447 N  NE    . ARG   B 1  204  ? 3.514   18.595  132.228 1.00 32.52 ? 202  ARG   B NE    1 
ATOM   10448 C  CZ    . ARG   B 1  204  ? 2.879   19.310  133.144 1.00 39.16 ? 202  ARG   B CZ    1 
ATOM   10449 N  NH1   . ARG   B 1  204  ? 1.940   18.774  133.911 1.00 41.79 ? 202  ARG   B NH1   1 
ATOM   10450 N  NH2   . ARG   B 1  204  ? 3.191   20.593  133.299 1.00 38.32 ? 202  ARG   B NH2   1 
ATOM   10451 N  N     . GLU   B 1  205  ? -0.241  19.270  128.764 1.00 27.05 ? 203  GLU   B N     1 
ATOM   10452 C  CA    . GLU   B 1  205  ? -1.389  20.144  128.955 1.00 28.86 ? 203  GLU   B CA    1 
ATOM   10453 C  C     . GLU   B 1  205  ? -2.557  19.704  128.087 1.00 26.81 ? 203  GLU   B C     1 
ATOM   10454 O  O     . GLU   B 1  205  ? -3.703  19.671  128.550 1.00 26.81 ? 203  GLU   B O     1 
ATOM   10455 C  CB    . GLU   B 1  205  ? -0.998  21.583  128.635 1.00 31.44 ? 203  GLU   B CB    1 
ATOM   10456 C  CG    . GLU   B 1  205  ? -2.058  22.607  128.970 1.00 33.79 ? 203  GLU   B CG    1 
ATOM   10457 C  CD    . GLU   B 1  205  ? -1.591  24.027  128.709 1.00 42.41 ? 203  GLU   B CD    1 
ATOM   10458 O  OE1   . GLU   B 1  205  ? -1.149  24.311  127.577 1.00 39.17 ? 203  GLU   B OE1   1 
ATOM   10459 O  OE2   . GLU   B 1  205  ? -1.652  24.857  129.640 1.00 55.41 ? 203  GLU   B OE2   1 
ATOM   10460 N  N     . ALA   B 1  206  ? -2.283  19.344  126.835 1.00 24.40 ? 204  ALA   B N     1 
ATOM   10461 C  CA    . ALA   B 1  206  ? -3.357  18.943  125.936 1.00 22.54 ? 204  ALA   B CA    1 
ATOM   10462 C  C     . ALA   B 1  206  ? -4.057  17.692  126.444 1.00 27.31 ? 204  ALA   B C     1 
ATOM   10463 O  O     . ALA   B 1  206  ? -5.290  17.612  126.427 1.00 24.79 ? 204  ALA   B O     1 
ATOM   10464 C  CB    . ALA   B 1  206  ? -2.801  18.718  124.533 1.00 23.62 ? 204  ALA   B CB    1 
ATOM   10465 N  N     . LEU   B 1  207  ? -3.285  16.706  126.902 1.00 23.31 ? 205  LEU   B N     1 
ATOM   10466 C  CA    . LEU   B 1  207  ? -3.878  15.500  127.473 1.00 25.60 ? 205  LEU   B CA    1 
ATOM   10467 C  C     . LEU   B 1  207  ? -4.730  15.823  128.691 1.00 27.95 ? 205  LEU   B C     1 
ATOM   10468 O  O     . LEU   B 1  207  ? -5.830  15.278  128.850 1.00 28.36 ? 205  LEU   B O     1 
ATOM   10469 C  CB    . LEU   B 1  207  ? -2.782  14.494  127.832 1.00 29.09 ? 205  LEU   B CB    1 
ATOM   10470 C  CG    . LEU   B 1  207  ? -2.090  13.843  126.634 1.00 30.70 ? 205  LEU   B CG    1 
ATOM   10471 C  CD1   . LEU   B 1  207  ? -0.796  13.146  127.054 1.00 32.23 ? 205  LEU   B CD1   1 
ATOM   10472 C  CD2   . LEU   B 1  207  ? -3.030  12.869  125.929 1.00 25.20 ? 205  LEU   B CD2   1 
ATOM   10473 N  N     . LYS   B 1  208  ? -4.241  16.704  129.569 1.00 23.25 ? 206  LYS   B N     1 
ATOM   10474 C  CA    . LYS   B 1  208  ? -5.016  17.060  130.754 1.00 26.34 ? 206  LYS   B CA    1 
ATOM   10475 C  C     . LYS   B 1  208  ? -6.340  17.713  130.370 1.00 28.23 ? 206  LYS   B C     1 
ATOM   10476 O  O     . LYS   B 1  208  ? -7.385  17.423  130.968 1.00 27.73 ? 206  LYS   B O     1 
ATOM   10477 C  CB    . LYS   B 1  208  ? -4.196  17.978  131.667 1.00 30.91 ? 206  LYS   B CB    1 
ATOM   10478 N  N     . ARG   B 1  209  ? -6.320  18.585  129.368 1.00 26.72 ? 207  ARG   B N     1 
ATOM   10479 C  CA    . ARG   B 1  209  ? -7.521  19.286  128.943 1.00 26.71 ? 207  ARG   B CA    1 
ATOM   10480 C  C     . ARG   B 1  209  ? -8.460  18.403  128.142 1.00 31.52 ? 207  ARG   B C     1 
ATOM   10481 O  O     . ARG   B 1  209  ? -9.613  18.787  127.923 1.00 30.50 ? 207  ARG   B O     1 
ATOM   10482 C  CB    . ARG   B 1  209  ? -7.139  20.511  128.123 1.00 28.05 ? 207  ARG   B CB    1 
ATOM   10483 C  CG    . ARG   B 1  209  ? -6.389  21.547  128.944 1.00 30.60 ? 207  ARG   B CG    1 
ATOM   10484 C  CD    . ARG   B 1  209  ? -5.984  22.696  128.071 1.00 32.50 ? 207  ARG   B CD    1 
ATOM   10485 N  NE    . ARG   B 1  209  ? -5.406  23.797  128.827 1.00 43.72 ? 207  ARG   B NE    1 
ATOM   10486 C  CZ    . ARG   B 1  209  ? -4.918  24.895  128.268 1.00 45.15 ? 207  ARG   B CZ    1 
ATOM   10487 N  NH1   . ARG   B 1  209  ? -4.909  25.051  126.954 1.00 34.19 ? 207  ARG   B NH1   1 
ATOM   10488 N  NH2   . ARG   B 1  209  ? -4.432  25.858  129.046 1.00 47.47 ? 207  ARG   B NH2   1 
ATOM   10489 N  N     . SER   B 1  210  ? -8.005  17.223  127.731 1.00 25.08 ? 208  SER   B N     1 
ATOM   10490 C  CA    . SER   B 1  210  ? -8.838  16.349  126.919 1.00 24.54 ? 208  SER   B CA    1 
ATOM   10491 C  C     . SER   B 1  210  ? -9.815  15.527  127.745 1.00 26.96 ? 208  SER   B C     1 
ATOM   10492 O  O     . SER   B 1  210  ? -10.790 15.008  127.190 1.00 26.95 ? 208  SER   B O     1 
ATOM   10493 C  CB    . SER   B 1  210  ? -7.946  15.426  126.093 1.00 22.00 ? 208  SER   B CB    1 
ATOM   10494 O  OG    . SER   B 1  210  ? -7.133  16.186  125.197 1.00 26.01 ? 208  SER   B OG    1 
ATOM   10495 N  N     . LYS   B 1  211  ? -9.586  15.402  129.051 1.00 25.55 ? 209  LYS   B N     1 
ATOM   10496 C  CA    . LYS   B 1  211  ? -10.416 14.521  129.866 1.00 24.92 ? 209  LYS   B CA    1 
ATOM   10497 C  C     . LYS   B 1  211  ? -11.875 14.954  129.848 1.00 26.27 ? 209  LYS   B C     1 
ATOM   10498 O  O     . LYS   B 1  211  ? -12.774 14.111  129.805 1.00 30.59 ? 209  LYS   B O     1 
ATOM   10499 C  CB    . LYS   B 1  211  ? -9.892  14.489  131.298 1.00 30.50 ? 209  LYS   B CB    1 
ATOM   10500 C  CG    . LYS   B 1  211  ? -8.396  14.229  131.391 1.00 32.59 ? 209  LYS   B CG    1 
ATOM   10501 C  CD    . LYS   B 1  211  ? -8.003  12.918  130.724 1.00 36.26 ? 209  LYS   B CD    1 
ATOM   10502 C  CE    . LYS   B 1  211  ? -6.494  12.711  130.783 1.00 42.34 ? 209  LYS   B CE    1 
ATOM   10503 N  NZ    . LYS   B 1  211  ? -6.039  11.456  130.110 1.00 45.82 ? 209  LYS   B NZ    1 
ATOM   10504 N  N     . GLU   B 1  212  ? -12.125 16.266  129.852 1.00 27.18 ? 210  GLU   B N     1 
ATOM   10505 C  CA    . GLU   B 1  212  ? -13.491 16.774  129.953 1.00 31.72 ? 210  GLU   B CA    1 
ATOM   10506 C  C     . GLU   B 1  212  ? -14.368 16.248  128.823 1.00 30.34 ? 210  GLU   B C     1 
ATOM   10507 O  O     . GLU   B 1  212  ? -15.446 15.694  129.067 1.00 29.24 ? 210  GLU   B O     1 
ATOM   10508 C  CB    . GLU   B 1  212  ? -13.478 18.303  129.948 1.00 37.41 ? 210  GLU   B CB    1 
ATOM   10509 C  CG    . GLU   B 1  212  ? -14.863 18.923  130.012 1.00 47.92 ? 210  GLU   B CG    1 
ATOM   10510 C  CD    . GLU   B 1  212  ? -14.857 20.403  129.678 1.00 56.68 ? 210  GLU   B CD    1 
ATOM   10511 O  OE1   . GLU   B 1  212  ? -13.764 21.008  129.666 1.00 65.28 ? 210  GLU   B OE1   1 
ATOM   10512 O  OE2   . GLU   B 1  212  ? -15.946 20.960  129.418 1.00 68.42 ? 210  GLU   B OE2   1 
ATOM   10513 N  N     . LEU   B 1  213  ? -13.924 16.419  127.577 1.00 26.51 ? 211  LEU   B N     1 
ATOM   10514 C  CA    . LEU   B 1  213  ? -14.728 15.961  126.449 1.00 28.28 ? 211  LEU   B CA    1 
ATOM   10515 C  C     . LEU   B 1  213  ? -14.640 14.453  126.250 1.00 27.09 ? 211  LEU   B C     1 
ATOM   10516 O  O     . LEU   B 1  213  ? -15.589 13.851  125.741 1.00 25.87 ? 211  LEU   B O     1 
ATOM   10517 C  CB    . LEU   B 1  213  ? -14.392 16.736  125.172 1.00 25.15 ? 211  LEU   B CB    1 
ATOM   10518 C  CG    . LEU   B 1  213  ? -14.824 18.209  125.188 1.00 27.84 ? 211  LEU   B CG    1 
ATOM   10519 C  CD1   . LEU   B 1  213  ? -14.529 18.925  123.878 1.00 31.38 ? 211  LEU   B CD1   1 
ATOM   10520 C  CD2   . LEU   B 1  213  ? -16.305 18.328  125.531 1.00 32.62 ? 211  LEU   B CD2   1 
ATOM   10521 N  N     . GLU   B 1  214  ? -13.528 13.822  126.644 1.00 25.50 ? 212  GLU   B N     1 
ATOM   10522 C  CA    . GLU   B 1  214  ? -13.467 12.364  126.587 1.00 23.56 ? 212  GLU   B CA    1 
ATOM   10523 C  C     . GLU   B 1  214  ? -14.543 11.733  127.461 1.00 26.21 ? 212  GLU   B C     1 
ATOM   10524 O  O     . GLU   B 1  214  ? -15.176 10.751  127.058 1.00 29.01 ? 212  GLU   B O     1 
ATOM   10525 C  CB    . GLU   B 1  214  ? -12.079 11.861  126.978 1.00 25.30 ? 212  GLU   B CB    1 
ATOM   10526 C  CG    . GLU   B 1  214  ? -11.048 12.077  125.883 1.00 25.93 ? 212  GLU   B CG    1 
ATOM   10527 C  CD    . GLU   B 1  214  ? -9.713  11.433  126.195 1.00 26.44 ? 212  GLU   B CD    1 
ATOM   10528 O  OE1   . GLU   B 1  214  ? -9.456  11.116  127.374 1.00 29.61 ? 212  GLU   B OE1   1 
ATOM   10529 O  OE2   . GLU   B 1  214  ? -8.916  11.250  125.249 1.00 25.92 ? 212  GLU   B OE2   1 
ATOM   10530 N  N     . GLU   B 1  215  ? -14.777 12.291  128.653 1.00 27.11 ? 213  GLU   B N     1 
ATOM   10531 C  CA    . GLU   B 1  215  ? -15.825 11.773  129.525 1.00 28.13 ? 213  GLU   B CA    1 
ATOM   10532 C  C     . GLU   B 1  215  ? -17.209 11.899  128.901 1.00 30.43 ? 213  GLU   B C     1 
ATOM   10533 O  O     . GLU   B 1  215  ? -18.111 11.138  129.268 1.00 33.52 ? 213  GLU   B O     1 
ATOM   10534 C  CB    . GLU   B 1  215  ? -15.767 12.467  130.886 1.00 31.06 ? 213  GLU   B CB    1 
ATOM   10535 C  CG    . GLU   B 1  215  ? -14.515 12.119  131.683 1.00 34.83 ? 213  GLU   B CG    1 
ATOM   10536 C  CD    . GLU   B 1  215  ? -14.437 12.853  133.007 1.00 45.39 ? 213  GLU   B CD    1 
ATOM   10537 O  OE1   . GLU   B 1  215  ? -15.496 13.050  133.637 1.00 60.10 ? 213  GLU   B OE1   1 
ATOM   10538 O  OE2   . GLU   B 1  215  ? -13.317 13.236  133.413 1.00 50.28 ? 213  GLU   B OE2   1 
ATOM   10539 N  N     . LYS   B 1  216  ? -17.393 12.832  127.966 1.00 27.45 ? 214  LYS   B N     1 
ATOM   10540 C  CA    . LYS   B 1  216  ? -18.655 12.979  127.254 1.00 27.66 ? 214  LYS   B CA    1 
ATOM   10541 C  C     . LYS   B 1  216  ? -18.771 12.054  126.048 1.00 31.85 ? 214  LYS   B C     1 
ATOM   10542 O  O     . LYS   B 1  216  ? -19.859 11.955  125.470 1.00 31.86 ? 214  LYS   B O     1 
ATOM   10543 C  CB    . LYS   B 1  216  ? -18.861 14.431  126.804 1.00 30.01 ? 214  LYS   B CB    1 
ATOM   10544 C  CG    . LYS   B 1  216  ? -18.973 15.440  127.948 1.00 34.98 ? 214  LYS   B CG    1 
ATOM   10545 C  CD    . LYS   B 1  216  ? -19.096 16.858  127.396 1.00 44.04 ? 214  LYS   B CD    1 
ATOM   10546 C  CE    . LYS   B 1  216  ? -18.767 17.905  128.452 1.00 54.97 ? 214  LYS   B CE    1 
ATOM   10547 N  NZ    . LYS   B 1  216  ? -18.699 19.282  127.876 1.00 54.13 ? 214  LYS   B NZ    1 
ATOM   10548 N  N     . GLY   B 1  217  ? -17.695 11.371  125.659 1.00 25.96 ? 215  GLY   B N     1 
ATOM   10549 C  CA    . GLY   B 1  217  ? -17.721 10.472  124.520 1.00 25.68 ? 215  GLY   B CA    1 
ATOM   10550 C  C     . GLY   B 1  217  ? -16.915 10.931  123.326 1.00 29.42 ? 215  GLY   B C     1 
ATOM   10551 O  O     . GLY   B 1  217  ? -16.933 10.253  122.292 1.00 27.34 ? 215  GLY   B O     1 
ATOM   10552 N  N     . PHE   B 1  218  ? -16.233 12.065  123.417 1.00 24.59 ? 216  PHE   B N     1 
ATOM   10553 C  CA    . PHE   B 1  218  ? -15.297 12.438  122.372 1.00 21.91 ? 216  PHE   B CA    1 
ATOM   10554 C  C     . PHE   B 1  218  ? -14.006 11.651  122.530 1.00 25.49 ? 216  PHE   B C     1 
ATOM   10555 O  O     . PHE   B 1  218  ? -13.708 11.099  123.591 1.00 24.19 ? 216  PHE   B O     1 
ATOM   10556 C  CB    . PHE   B 1  218  ? -14.950 13.923  122.456 1.00 23.76 ? 216  PHE   B CB    1 
ATOM   10557 C  CG    . PHE   B 1  218  ? -16.070 14.837  122.056 1.00 25.23 ? 216  PHE   B CG    1 
ATOM   10558 C  CD1   . PHE   B 1  218  ? -17.058 15.180  122.964 1.00 26.03 ? 216  PHE   B CD1   1 
ATOM   10559 C  CD2   . PHE   B 1  218  ? -16.122 15.372  120.783 1.00 26.48 ? 216  PHE   B CD2   1 
ATOM   10560 C  CE1   . PHE   B 1  218  ? -18.080 16.029  122.600 1.00 26.39 ? 216  PHE   B CE1   1 
ATOM   10561 C  CE2   . PHE   B 1  218  ? -17.142 16.223  120.414 1.00 28.01 ? 216  PHE   B CE2   1 
ATOM   10562 C  CZ    . PHE   B 1  218  ? -18.124 16.552  121.323 1.00 25.68 ? 216  PHE   B CZ    1 
ATOM   10563 N  N     . SER   B 1  219  ? -13.239 11.601  121.447 1.00 23.90 ? 217  SER   B N     1 
ATOM   10564 C  CA    . SER   B 1  219  ? -11.875 11.101  121.468 1.00 23.85 ? 217  SER   B CA    1 
ATOM   10565 C  C     . SER   B 1  219  ? -10.986 12.164  120.845 1.00 21.33 ? 217  SER   B C     1 
ATOM   10566 O  O     . SER   B 1  219  ? -11.457 13.223  120.421 1.00 21.66 ? 217  SER   B O     1 
ATOM   10567 C  CB    . SER   B 1  219  ? -11.749 9.760   120.740 1.00 22.67 ? 217  SER   B CB    1 
ATOM   10568 O  OG    . SER   B 1  219  ? -12.100 9.904   119.376 1.00 25.50 ? 217  SER   B OG    1 
ATOM   10569 N  N     . TYR   B 1  220  ? -9.686  11.882  120.780 1.00 21.42 ? 218  TYR   B N     1 
ATOM   10570 C  CA    . TYR   B 1  220  ? -8.720  12.878  120.354 1.00 20.66 ? 218  TYR   B CA    1 
ATOM   10571 C  C     . TYR   B 1  220  ? -7.708  12.283  119.393 1.00 19.02 ? 218  TYR   B C     1 
ATOM   10572 O  O     . TYR   B 1  220  ? -7.354  11.105  119.476 1.00 20.64 ? 218  TYR   B O     1 
ATOM   10573 C  CB    . TYR   B 1  220  ? -7.974  13.469  121.562 1.00 20.06 ? 218  TYR   B CB    1 
ATOM   10574 C  CG    . TYR   B 1  220  ? -8.756  14.575  122.216 1.00 20.01 ? 218  TYR   B CG    1 
ATOM   10575 C  CD1   . TYR   B 1  220  ? -9.738  14.296  123.163 1.00 21.65 ? 218  TYR   B CD1   1 
ATOM   10576 C  CD2   . TYR   B 1  220  ? -8.550  15.895  121.853 1.00 19.88 ? 218  TYR   B CD2   1 
ATOM   10577 C  CE1   . TYR   B 1  220  ? -10.473 15.313  123.749 1.00 21.10 ? 218  TYR   B CE1   1 
ATOM   10578 C  CE2   . TYR   B 1  220  ? -9.280  16.922  122.435 1.00 21.51 ? 218  TYR   B CE2   1 
ATOM   10579 C  CZ    . TYR   B 1  220  ? -10.241 16.619  123.381 1.00 20.98 ? 218  TYR   B CZ    1 
ATOM   10580 O  OH    . TYR   B 1  220  ? -10.972 17.625  123.969 1.00 25.51 ? 218  TYR   B OH    1 
ATOM   10581 N  N     . SER   B 1  221  ? -7.227  13.134  118.494 1.00 18.27 ? 219  SER   B N     1 
ATOM   10582 C  CA    . SER   B 1  221  ? -6.048  12.859  117.685 1.00 17.90 ? 219  SER   B CA    1 
ATOM   10583 C  C     . SER   B 1  221  ? -5.169  14.092  117.768 1.00 19.57 ? 219  SER   B C     1 
ATOM   10584 O  O     . SER   B 1  221  ? -5.597  15.180  117.377 1.00 21.69 ? 219  SER   B O     1 
ATOM   10585 C  CB    . SER   B 1  221  ? -6.432  12.595  116.232 1.00 19.15 ? 219  SER   B CB    1 
ATOM   10586 O  OG    . SER   B 1  221  ? -5.267  12.337  115.459 1.00 19.66 ? 219  SER   B OG    1 
ATOM   10587 N  N     . TYR   B 1  222  ? -3.953  13.927  118.282 1.00 17.94 ? 220  TYR   B N     1 
ATOM   10588 C  CA    . TYR   B 1  222  ? -3.085  15.070  118.540 1.00 18.95 ? 220  TYR   B CA    1 
ATOM   10589 C  C     . TYR   B 1  222  ? -2.185  15.380  117.357 1.00 20.62 ? 220  TYR   B C     1 
ATOM   10590 O  O     . TYR   B 1  222  ? -1.620  14.480  116.731 1.00 20.44 ? 220  TYR   B O     1 
ATOM   10591 C  CB    . TYR   B 1  222  ? -2.250  14.841  119.799 1.00 17.95 ? 220  TYR   B CB    1 
ATOM   10592 C  CG    . TYR   B 1  222  ? -3.148  14.710  120.984 1.00 18.56 ? 220  TYR   B CG    1 
ATOM   10593 C  CD1   . TYR   B 1  222  ? -3.738  15.835  121.552 1.00 19.57 ? 220  TYR   B CD1   1 
ATOM   10594 C  CD2   . TYR   B 1  222  ? -3.468  13.466  121.498 1.00 18.40 ? 220  TYR   B CD2   1 
ATOM   10595 C  CE1   . TYR   B 1  222  ? -4.600  15.723  122.618 1.00 18.78 ? 220  TYR   B CE1   1 
ATOM   10596 C  CE2   . TYR   B 1  222  ? -4.320  13.345  122.575 1.00 19.60 ? 220  TYR   B CE2   1 
ATOM   10597 C  CZ    . TYR   B 1  222  ? -4.881  14.474  123.132 1.00 19.82 ? 220  TYR   B CZ    1 
ATOM   10598 O  OH    . TYR   B 1  222  ? -5.751  14.357  124.192 1.00 21.83 ? 220  TYR   B OH    1 
ATOM   10599 N  N     . ASP   B 1  223  ? -2.067  16.670  117.061 1.00 21.08 ? 221  ASP   B N     1 
ATOM   10600 C  CA    . ASP   B 1  223  ? -1.250  17.192  115.971 1.00 22.46 ? 221  ASP   B CA    1 
ATOM   10601 C  C     . ASP   B 1  223  ? -0.159  18.035  116.611 1.00 22.41 ? 221  ASP   B C     1 
ATOM   10602 O  O     . ASP   B 1  223  ? -0.436  19.125  117.122 1.00 24.72 ? 221  ASP   B O     1 
ATOM   10603 C  CB    . ASP   B 1  223  ? -2.117  18.056  115.063 1.00 26.27 ? 221  ASP   B CB    1 
ATOM   10604 C  CG    . ASP   B 1  223  ? -1.303  18.849  114.054 1.00 30.46 ? 221  ASP   B CG    1 
ATOM   10605 O  OD1   . ASP   B 1  223  ? -0.196  18.407  113.693 1.00 30.20 ? 221  ASP   B OD1   1 
ATOM   10606 O  OD2   . ASP   B 1  223  ? -1.776  19.925  113.640 1.00 36.21 ? 221  ASP   B OD2   1 
ATOM   10607 N  N     . MET   B 1  224  ? 1.080   17.541  116.582 1.00 23.16 ? 222  MET   B N     1 
ATOM   10608 C  CA    . MET   B 1  224  ? 2.191   18.266  117.180 1.00 27.43 ? 222  MET   B CA    1 
ATOM   10609 C  C     . MET   B 1  224  ? 2.696   19.413  116.311 1.00 29.90 ? 222  MET   B C     1 
ATOM   10610 O  O     . MET   B 1  224  ? 3.747   19.982  116.620 1.00 37.69 ? 222  MET   B O     1 
ATOM   10611 C  CB    . MET   B 1  224  ? 3.332   17.312  117.549 1.00 28.43 ? 222  MET   B CB    1 
ATOM   10612 C  CG    . MET   B 1  224  ? 2.918   16.184  118.482 1.00 24.02 ? 222  MET   B CG    1 
ATOM   10613 S  SD    . MET   B 1  224  ? 2.028   16.748  119.946 1.00 28.75 ? 222  MET   B SD    1 
ATOM   10614 C  CE    . MET   B 1  224  ? 3.290   17.768  120.686 1.00 29.90 ? 222  MET   B CE    1 
ATOM   10615 N  N     . LEU   B 1  225  ? 1.981   19.746  115.242 1.00 35.98 ? 223  LEU   B N     1 
ATOM   10616 C  CA    . LEU   B 1  225  ? 2.190   20.941  114.429 1.00 31.18 ? 223  LEU   B CA    1 
ATOM   10617 C  C     . LEU   B 1  225  ? 3.417   20.878  113.524 1.00 42.63 ? 223  LEU   B C     1 
ATOM   10618 O  O     . LEU   B 1  225  ? 3.776   21.890  112.913 1.00 41.42 ? 223  LEU   B O     1 
ATOM   10619 C  CB    . LEU   B 1  225  ? 2.165   22.234  115.253 1.00 35.16 ? 223  LEU   B CB    1 
ATOM   10620 C  CG    . LEU   B 1  225  ? 0.829   22.581  115.923 1.00 39.65 ? 223  LEU   B CG    1 
ATOM   10621 C  CD1   . LEU   B 1  225  ? 0.956   23.870  116.712 1.00 41.16 ? 223  LEU   B CD1   1 
ATOM   10622 C  CD2   . LEU   B 1  225  ? -0.295  22.686  114.905 1.00 38.87 ? 223  LEU   B CD2   1 
ATOM   10623 N  N     . GLY   B 1  226  ? 4.062   19.719  113.399 1.00 39.55 ? 224  GLY   B N     1 
ATOM   10624 C  CA    . GLY   B 1  226  ? 5.195   19.602  112.488 1.00 38.65 ? 224  GLY   B CA    1 
ATOM   10625 C  C     . GLY   B 1  226  ? 4.731   19.536  111.041 1.00 31.63 ? 224  GLY   B C     1 
ATOM   10626 O  O     . GLY   B 1  226  ? 3.756   18.866  110.707 1.00 31.02 ? 224  GLY   B O     1 
ATOM   10627 N  N     . GLU   B 1  227  ? 5.449   20.244  110.173 1.00 28.66 ? 225  GLU   B N     1 
ATOM   10628 C  CA    . GLU   B 1  227  ? 5.072   20.271  108.768 1.00 31.82 ? 225  GLU   B CA    1 
ATOM   10629 C  C     . GLU   B 1  227  ? 6.238   20.800  107.949 1.00 25.62 ? 225  GLU   B C     1 
ATOM   10630 O  O     . GLU   B 1  227  ? 6.976   21.671  108.414 1.00 27.69 ? 225  GLU   B O     1 
ATOM   10631 C  CB    . GLU   B 1  227  ? 3.849   21.173  108.569 1.00 35.66 ? 225  GLU   B CB    1 
ATOM   10632 C  CG    . GLU   B 1  227  ? 3.248   21.141  107.189 1.00 38.72 ? 225  GLU   B CG    1 
ATOM   10633 C  CD    . GLU   B 1  227  ? 1.960   21.934  107.130 1.00 40.71 ? 225  GLU   B CD    1 
ATOM   10634 O  OE1   . GLU   B 1  227  ? 1.338   22.140  108.201 1.00 38.87 ? 225  GLU   B OE1   1 
ATOM   10635 O  OE2   . GLU   B 1  227  ? 1.579   22.359  106.022 1.00 43.63 ? 225  GLU   B OE2   1 
ATOM   10636 N  N     . ALA   B 1  228  ? 6.395   20.257  106.742 1.00 22.81 ? 226  ALA   B N     1 
ATOM   10637 C  CA    . ALA   B 1  228  ? 7.296   20.798  105.732 1.00 24.39 ? 226  ALA   B CA    1 
ATOM   10638 C  C     . ALA   B 1  228  ? 8.680   21.097  106.311 1.00 22.50 ? 226  ALA   B C     1 
ATOM   10639 O  O     . ALA   B 1  228  ? 9.124   22.245  106.380 1.00 24.73 ? 226  ALA   B O     1 
ATOM   10640 C  CB    . ALA   B 1  228  ? 6.688   22.033  105.068 1.00 27.48 ? 226  ALA   B CB    1 
ATOM   10641 N  N     . ALA   B 1  229  ? 9.349   20.024  106.735 1.00 20.12 ? 227  ALA   B N     1 
ATOM   10642 C  CA    . ALA   B 1  229  ? 10.753  20.135  107.100 1.00 20.23 ? 227  ALA   B CA    1 
ATOM   10643 C  C     . ALA   B 1  229  ? 11.532  20.760  105.950 1.00 17.32 ? 227  ALA   B C     1 
ATOM   10644 O  O     . ALA   B 1  229  ? 11.341  20.396  104.789 1.00 20.88 ? 227  ALA   B O     1 
ATOM   10645 C  CB    . ALA   B 1  229  ? 11.305  18.746  107.410 1.00 19.16 ? 227  ALA   B CB    1 
ATOM   10646 N  N     . THR   B 1  230  ? 12.377  21.736  106.284 1.00 19.11 ? 228  THR   B N     1 
ATOM   10647 C  CA    . THR   B 1  230  ? 13.258  22.375  105.316 1.00 17.91 ? 228  THR   B CA    1 
ATOM   10648 C  C     . THR   B 1  230  ? 14.666  21.809  105.371 1.00 17.26 ? 228  THR   B C     1 
ATOM   10649 O  O     . THR   B 1  230  ? 15.357  21.770  104.347 1.00 18.58 ? 228  THR   B O     1 
ATOM   10650 C  CB    . THR   B 1  230  ? 13.326  23.879  105.609 1.00 20.08 ? 228  THR   B CB    1 
ATOM   10651 O  OG1   . THR   B 1  230  ? 11.998  24.404  105.685 1.00 24.58 ? 228  THR   B OG1   1 
ATOM   10652 C  CG2   . THR   B 1  230  ? 14.107  24.626  104.528 1.00 18.61 ? 228  THR   B CG2   1 
ATOM   10653 N  N     . THR   B 1  231  ? 15.092  21.350  106.541 1.00 17.45 ? 229  THR   B N     1 
ATOM   10654 C  CA    . THR   B 1  231  ? 16.434  20.838  106.746 1.00 16.97 ? 229  THR   B CA    1 
ATOM   10655 C  C     . THR   B 1  231  ? 16.342  19.478  107.415 1.00 16.19 ? 229  THR   B C     1 
ATOM   10656 O  O     . THR   B 1  231  ? 15.303  19.095  107.964 1.00 17.10 ? 229  THR   B O     1 
ATOM   10657 C  CB    . THR   B 1  231  ? 17.255  21.770  107.639 1.00 17.60 ? 229  THR   B CB    1 
ATOM   10658 O  OG1   . THR   B 1  231  ? 16.763  21.693  108.983 1.00 19.54 ? 229  THR   B OG1   1 
ATOM   10659 C  CG2   . THR   B 1  231  ? 17.182  23.212  107.151 1.00 20.28 ? 229  THR   B CG2   1 
ATOM   10660 N  N     . ALA   B 1  232  ? 17.463  18.758  107.369 1.00 18.15 ? 230  ALA   B N     1 
ATOM   10661 C  CA    . ALA   B 1  232  ? 17.570  17.501  108.101 1.00 18.99 ? 230  ALA   B CA    1 
ATOM   10662 C  C     . ALA   B 1  232  ? 17.290  17.703  109.580 1.00 17.21 ? 230  ALA   B C     1 
ATOM   10663 O  O     . ALA   B 1  232  ? 16.618  16.878  110.208 1.00 20.08 ? 230  ALA   B O     1 
ATOM   10664 C  CB    . ALA   B 1  232  ? 18.965  16.908  107.909 1.00 18.35 ? 230  ALA   B CB    1 
ATOM   10665 N  N     . ALA   B 1  233  ? 17.811  18.787  110.160 1.00 17.74 ? 231  ALA   B N     1 
ATOM   10666 C  CA    . ALA   B 1  233  ? 17.580  19.046  111.575 1.00 19.47 ? 231  ALA   B CA    1 
ATOM   10667 C  C     . ALA   B 1  233  ? 16.102  19.239  111.866 1.00 20.67 ? 231  ALA   B C     1 
ATOM   10668 O  O     . ALA   B 1  233  ? 15.617  18.809  112.918 1.00 19.75 ? 231  ALA   B O     1 
ATOM   10669 C  CB    . ALA   B 1  233  ? 18.374  20.265  112.033 1.00 21.47 ? 231  ALA   B CB    1 
ATOM   10670 N  N     . ASP   B 1  234  ? 15.373  19.898  110.956 1.00 18.32 ? 232  ASP   B N     1 
ATOM   10671 C  CA    . ASP   B 1  234  ? 13.933  20.053  111.141 1.00 18.74 ? 232  ASP   B CA    1 
ATOM   10672 C  C     . ASP   B 1  234  ? 13.267  18.695  111.220 1.00 18.72 ? 232  ASP   B C     1 
ATOM   10673 O  O     . ASP   B 1  234  ? 12.471  18.427  112.129 1.00 18.67 ? 232  ASP   B O     1 
ATOM   10674 C  CB    . ASP   B 1  234  ? 13.308  20.791  109.957 1.00 20.57 ? 232  ASP   B CB    1 
ATOM   10675 C  CG    . ASP   B 1  234  ? 13.672  22.249  109.892 1.00 24.38 ? 232  ASP   B CG    1 
ATOM   10676 O  OD1   . ASP   B 1  234  ? 14.010  22.858  110.930 1.00 25.96 ? 232  ASP   B OD1   1 
ATOM   10677 O  OD2   . ASP   B 1  234  ? 13.594  22.787  108.764 1.00 24.45 ? 232  ASP   B OD2   1 
ATOM   10678 N  N     . ALA   B 1  235  ? 13.573  17.830  110.255 1.00 18.17 ? 233  ALA   B N     1 
ATOM   10679 C  CA    . ALA   B 1  235  ? 12.922  16.533  110.170 1.00 17.83 ? 233  ALA   B CA    1 
ATOM   10680 C  C     . ALA   B 1  235  ? 13.275  15.666  111.366 1.00 17.51 ? 233  ALA   B C     1 
ATOM   10681 O  O     . ALA   B 1  235  ? 12.417  14.955  111.895 1.00 19.11 ? 233  ALA   B O     1 
ATOM   10682 C  CB    . ALA   B 1  235  ? 13.297  15.846  108.857 1.00 17.98 ? 233  ALA   B CB    1 
ATOM   10683 N  N     . GLU   B 1  236  ? 14.530  15.722  111.809 1.00 16.84 ? 234  GLU   B N     1 
ATOM   10684 C  CA    . GLU   B 1  236  ? 14.914  14.960  112.987 1.00 18.65 ? 234  GLU   B CA    1 
ATOM   10685 C  C     . GLU   B 1  236  ? 14.185  15.463  114.221 1.00 20.74 ? 234  GLU   B C     1 
ATOM   10686 O  O     . GLU   B 1  236  ? 13.738  14.665  115.051 1.00 19.58 ? 234  GLU   B O     1 
ATOM   10687 C  CB    . GLU   B 1  236  ? 16.426  15.020  113.181 1.00 20.31 ? 234  GLU   B CB    1 
ATOM   10688 C  CG    . GLU   B 1  236  ? 16.922  13.999  114.177 1.00 23.64 ? 234  GLU   B CG    1 
ATOM   10689 C  CD    . GLU   B 1  236  ? 18.420  14.062  114.361 1.00 35.33 ? 234  GLU   B CD    1 
ATOM   10690 O  OE1   . GLU   B 1  236  ? 19.035  15.022  113.853 1.00 36.78 ? 234  GLU   B OE1   1 
ATOM   10691 O  OE2   . GLU   B 1  236  ? 18.977  13.154  115.012 1.00 38.05 ? 234  GLU   B OE2   1 
ATOM   10692 N  N     . ARG   B 1  237  ? 14.041  16.779  114.355 1.00 17.74 ? 235  ARG   B N     1 
ATOM   10693 C  CA    . ARG   B 1  237  ? 13.329  17.305  115.508 1.00 20.09 ? 235  ARG   B CA    1 
ATOM   10694 C  C     . ARG   B 1  237  ? 11.866  16.896  115.473 1.00 20.48 ? 235  ARG   B C     1 
ATOM   10695 O  O     . ARG   B 1  237  ? 11.308  16.469  116.489 1.00 20.84 ? 235  ARG   B O     1 
ATOM   10696 C  CB    . ARG   B 1  237  ? 13.456  18.823  115.571 1.00 21.95 ? 235  ARG   B CB    1 
ATOM   10697 C  CG    . ARG   B 1  237  ? 12.701  19.388  116.751 1.00 23.07 ? 235  ARG   B CG    1 
ATOM   10698 C  CD    . ARG   B 1  237  ? 12.607  20.883  116.726 1.00 27.95 ? 235  ARG   B CD    1 
ATOM   10699 N  NE    . ARG   B 1  237  ? 11.942  21.329  117.944 1.00 31.62 ? 235  ARG   B NE    1 
ATOM   10700 C  CZ    . ARG   B 1  237  ? 11.975  22.569  118.405 1.00 30.52 ? 235  ARG   B CZ    1 
ATOM   10701 N  NH1   . ARG   B 1  237  ? 12.640  23.523  117.773 1.00 36.56 ? 235  ARG   B NH1   1 
ATOM   10702 N  NH2   . ARG   B 1  237  ? 11.329  22.856  119.531 1.00 31.89 ? 235  ARG   B NH2   1 
ATOM   10703 N  N     . TYR   B 1  238  ? 11.226  17.014  114.306 1.00 18.48 ? 236  TYR   B N     1 
ATOM   10704 C  CA    . TYR   B 1  238  ? 9.822   16.633  114.212 1.00 18.40 ? 236  TYR   B CA    1 
ATOM   10705 C  C     . TYR   B 1  238  ? 9.644   15.159  114.531 1.00 18.11 ? 236  TYR   B C     1 
ATOM   10706 O  O     . TYR   B 1  238  ? 8.677   14.774  115.202 1.00 17.78 ? 236  TYR   B O     1 
ATOM   10707 C  CB    . TYR   B 1  238  ? 9.289   16.929  112.808 1.00 17.79 ? 236  TYR   B CB    1 
ATOM   10708 C  CG    . TYR   B 1  238  ? 9.082   18.396  112.499 1.00 22.90 ? 236  TYR   B CG    1 
ATOM   10709 C  CD1   . TYR   B 1  238  ? 8.632   19.286  113.466 1.00 28.46 ? 236  TYR   B CD1   1 
ATOM   10710 C  CD2   . TYR   B 1  238  ? 9.346   18.888  111.233 1.00 24.52 ? 236  TYR   B CD2   1 
ATOM   10711 C  CE1   . TYR   B 1  238  ? 8.453   20.630  113.172 1.00 34.98 ? 236  TYR   B CE1   1 
ATOM   10712 C  CE2   . TYR   B 1  238  ? 9.166   20.217  110.928 1.00 26.03 ? 236  TYR   B CE2   1 
ATOM   10713 C  CZ    . TYR   B 1  238  ? 8.719   21.086  111.895 1.00 33.68 ? 236  TYR   B CZ    1 
ATOM   10714 O  OH    . TYR   B 1  238  ? 8.552   22.417  111.577 1.00 38.91 ? 236  TYR   B OH    1 
ATOM   10715 N  N     . TYR   B 1  239  ? 10.568  14.323  114.062 1.00 18.66 ? 237  TYR   B N     1 
ATOM   10716 C  CA    . TYR   B 1  239  ? 10.526  12.905  114.390 1.00 17.76 ? 237  TYR   B CA    1 
ATOM   10717 C  C     . TYR   B 1  239  ? 10.585  12.696  115.895 1.00 19.80 ? 237  TYR   B C     1 
ATOM   10718 O  O     . TYR   B 1  239  ? 9.767   11.969  116.469 1.00 19.77 ? 237  TYR   B O     1 
ATOM   10719 C  CB    . TYR   B 1  239  ? 11.692  12.174  113.726 1.00 19.04 ? 237  TYR   B CB    1 
ATOM   10720 C  CG    . TYR   B 1  239  ? 11.820  10.748  114.202 1.00 22.95 ? 237  TYR   B CG    1 
ATOM   10721 C  CD1   . TYR   B 1  239  ? 11.000  9.758   113.695 1.00 21.65 ? 237  TYR   B CD1   1 
ATOM   10722 C  CD2   . TYR   B 1  239  ? 12.744  10.394  115.178 1.00 33.01 ? 237  TYR   B CD2   1 
ATOM   10723 C  CE1   . TYR   B 1  239  ? 11.101  8.463   114.121 1.00 21.43 ? 237  TYR   B CE1   1 
ATOM   10724 C  CE2   . TYR   B 1  239  ? 12.847  9.084   115.624 1.00 33.30 ? 237  TYR   B CE2   1 
ATOM   10725 C  CZ    . TYR   B 1  239  ? 12.018  8.125   115.085 1.00 33.14 ? 237  TYR   B CZ    1 
ATOM   10726 O  OH    . TYR   B 1  239  ? 12.105  6.819   115.504 1.00 39.12 ? 237  TYR   B OH    1 
ATOM   10727 N  N     . ARG   B 1  240  ? 11.569  13.313  116.552 1.00 19.00 ? 238  ARG   B N     1 
ATOM   10728 C  CA    . ARG   B 1  240  ? 11.705  13.132  117.989 1.00 20.09 ? 238  ARG   B CA    1 
ATOM   10729 C  C     . ARG   B 1  240  ? 10.505  13.692  118.729 1.00 20.33 ? 238  ARG   B C     1 
ATOM   10730 O  O     . ARG   B 1  240  ? 10.100  13.142  119.760 1.00 20.82 ? 238  ARG   B O     1 
ATOM   10731 C  CB    . ARG   B 1  240  ? 12.987  13.805  118.475 1.00 20.65 ? 238  ARG   B CB    1 
ATOM   10732 C  CG    . ARG   B 1  240  ? 14.252  13.149  117.969 1.00 24.02 ? 238  ARG   B CG    1 
ATOM   10733 C  CD    . ARG   B 1  240  ? 14.358  11.703  118.438 1.00 26.46 ? 238  ARG   B CD    1 
ATOM   10734 N  NE    . ARG   B 1  240  ? 15.528  11.061  117.858 1.00 30.50 ? 238  ARG   B NE    1 
ATOM   10735 C  CZ    . ARG   B 1  240  ? 15.768  9.757   117.894 1.00 38.67 ? 238  ARG   B CZ    1 
ATOM   10736 N  NH1   . ARG   B 1  240  ? 14.920  8.912   118.460 1.00 34.15 ? 238  ARG   B NH1   1 
ATOM   10737 N  NH2   . ARG   B 1  240  ? 16.887  9.289   117.352 1.00 39.88 ? 238  ARG   B NH2   1 
ATOM   10738 N  N     . ASP   B 1  241  ? 9.922   14.780  118.219 1.00 20.27 ? 239  ASP   B N     1 
ATOM   10739 C  CA    . ASP   B 1  241  ? 8.735   15.347  118.842 1.00 22.10 ? 239  ASP   B CA    1 
ATOM   10740 C  C     . ASP   B 1  241  ? 7.538   14.408  118.711 1.00 20.41 ? 239  ASP   B C     1 
ATOM   10741 O  O     . ASP   B 1  241  ? 6.763   14.257  119.656 1.00 20.02 ? 239  ASP   B O     1 
ATOM   10742 C  CB    . ASP   B 1  241  ? 8.428   16.733  118.266 1.00 24.71 ? 239  ASP   B CB    1 
ATOM   10743 C  CG    . ASP   B 1  241  ? 9.434   17.801  118.707 1.00 29.57 ? 239  ASP   B CG    1 
ATOM   10744 O  OD1   . ASP   B 1  241  ? 10.249  17.554  119.627 1.00 31.22 ? 239  ASP   B OD1   1 
ATOM   10745 O  OD2   . ASP   B 1  241  ? 9.403   18.898  118.116 1.00 35.84 ? 239  ASP   B OD2   1 
ATOM   10746 N  N     . TYR   B 1  242  ? 7.369   13.766  117.549 1.00 20.08 ? 240  TYR   B N     1 
ATOM   10747 C  CA    . TYR   B 1  242  ? 6.309   12.771  117.415 1.00 17.96 ? 240  TYR   B CA    1 
ATOM   10748 C  C     . TYR   B 1  242  ? 6.563   11.588  118.335 1.00 18.86 ? 240  TYR   B C     1 
ATOM   10749 O  O     . TYR   B 1  242  ? 5.639   11.066  118.964 1.00 18.98 ? 240  TYR   B O     1 
ATOM   10750 C  CB    . TYR   B 1  242  ? 6.245   12.256  115.981 1.00 18.79 ? 240  TYR   B CB    1 
ATOM   10751 C  CG    . TYR   B 1  242  ? 5.648   13.177  114.940 1.00 17.74 ? 240  TYR   B CG    1 
ATOM   10752 C  CD1   . TYR   B 1  242  ? 4.550   13.990  115.214 1.00 21.82 ? 240  TYR   B CD1   1 
ATOM   10753 C  CD2   . TYR   B 1  242  ? 6.166   13.194  113.663 1.00 19.50 ? 240  TYR   B CD2   1 
ATOM   10754 C  CE1   . TYR   B 1  242  ? 3.997   14.810  114.225 1.00 22.94 ? 240  TYR   B CE1   1 
ATOM   10755 C  CE2   . TYR   B 1  242  ? 5.633   13.994  112.686 1.00 20.51 ? 240  TYR   B CE2   1 
ATOM   10756 C  CZ    . TYR   B 1  242  ? 4.555   14.803  112.958 1.00 20.58 ? 240  TYR   B CZ    1 
ATOM   10757 O  OH    . TYR   B 1  242  ? 4.045   15.595  111.931 1.00 21.12 ? 240  TYR   B OH    1 
ATOM   10758 N  N     . GLU   B 1  243  ? 7.814   11.136  118.404 1.00 20.16 ? 241  GLU   B N     1 
ATOM   10759 C  CA    . GLU   B 1  243  ? 8.143   9.998   119.252 1.00 20.16 ? 241  GLU   B CA    1 
ATOM   10760 C  C     . GLU   B 1  243  ? 7.798   10.294  120.705 1.00 18.28 ? 241  GLU   B C     1 
ATOM   10761 O  O     . GLU   B 1  243  ? 7.186   9.471   121.401 1.00 18.21 ? 241  GLU   B O     1 
ATOM   10762 C  CB    . GLU   B 1  243  ? 9.634   9.708   119.113 1.00 19.87 ? 241  GLU   B CB    1 
ATOM   10763 C  CG    . GLU   B 1  243  ? 10.129  8.576   119.972 1.00 23.67 ? 241  GLU   B CG    1 
ATOM   10764 C  CD    . GLU   B 1  243  ? 11.640  8.450   119.928 1.00 32.02 ? 241  GLU   B CD    1 
ATOM   10765 O  OE1   . GLU   B 1  243  ? 12.324  9.486   119.783 1.00 32.88 ? 241  GLU   B OE1   1 
ATOM   10766 O  OE2   . GLU   B 1  243  ? 12.139  7.315   120.028 1.00 35.12 ? 241  GLU   B OE2   1 
ATOM   10767 N  N     . SER   B 1  244  ? 8.201   11.473  121.186 1.00 18.55 ? 242  SER   B N     1 
ATOM   10768 C  CA    A SER   B 1  244  ? 7.901   11.865  122.555 0.66 19.80 ? 242  SER   B CA    1 
ATOM   10769 C  CA    B SER   B 1  244  ? 7.900   11.854  122.560 0.34 19.83 ? 242  SER   B CA    1 
ATOM   10770 C  C     . SER   B 1  244  ? 6.399   11.951  122.784 1.00 18.67 ? 242  SER   B C     1 
ATOM   10771 O  O     . SER   B 1  244  ? 5.888   11.513  123.823 1.00 19.41 ? 242  SER   B O     1 
ATOM   10772 C  CB    A SER   B 1  244  ? 8.551   13.218  122.826 0.66 20.39 ? 242  SER   B CB    1 
ATOM   10773 C  CB    B SER   B 1  244  ? 8.570   13.186  122.892 0.34 20.48 ? 242  SER   B CB    1 
ATOM   10774 O  OG    A SER   B 1  244  ? 8.284   13.659  124.137 0.66 21.80 ? 242  SER   B OG    1 
ATOM   10775 O  OG    B SER   B 1  244  ? 9.981   13.070  122.863 0.34 21.24 ? 242  SER   B OG    1 
ATOM   10776 N  N     . ALA   B 1  245  ? 5.679   12.523  121.823 1.00 18.65 ? 243  ALA   B N     1 
ATOM   10777 C  CA    . ALA   B 1  245  ? 4.235   12.633  121.950 1.00 19.67 ? 243  ALA   B CA    1 
ATOM   10778 C  C     . ALA   B 1  245  ? 3.577   11.259  121.964 1.00 19.70 ? 243  ALA   B C     1 
ATOM   10779 O  O     . ALA   B 1  245  ? 2.624   11.033  122.714 1.00 20.44 ? 243  ALA   B O     1 
ATOM   10780 C  CB    . ALA   B 1  245  ? 3.683   13.471  120.800 1.00 19.71 ? 243  ALA   B CB    1 
ATOM   10781 N  N     . ILE   B 1  246  ? 4.054   10.330  121.129 1.00 18.40 ? 244  ILE   B N     1 
ATOM   10782 C  CA    . ILE   B 1  246  ? 3.459   8.995   121.135 1.00 19.56 ? 244  ILE   B CA    1 
ATOM   10783 C  C     . ILE   B 1  246  ? 3.593   8.352   122.504 1.00 21.13 ? 244  ILE   B C     1 
ATOM   10784 O  O     . ILE   B 1  246  ? 2.643   7.754   123.018 1.00 21.66 ? 244  ILE   B O     1 
ATOM   10785 C  CB    . ILE   B 1  246  ? 4.036   8.110   120.020 1.00 19.26 ? 244  ILE   B CB    1 
ATOM   10786 C  CG1   . ILE   B 1  246  ? 3.521   8.580   118.671 1.00 21.74 ? 244  ILE   B CG1   1 
ATOM   10787 C  CG2   . ILE   B 1  246  ? 3.646   6.656   120.253 1.00 20.34 ? 244  ILE   B CG2   1 
ATOM   10788 C  CD1   . ILE   B 1  246  ? 4.252   7.945   117.496 1.00 21.55 ? 244  ILE   B CD1   1 
ATOM   10789 N  N     . HIS   B 1  247  ? 4.763   8.470   123.127 1.00 19.28 ? 245  HIS   B N     1 
ATOM   10790 C  CA    . HIS   B 1  247  ? 4.905   7.937   124.478 1.00 19.90 ? 245  HIS   B CA    1 
ATOM   10791 C  C     . HIS   B 1  247  ? 3.901   8.564   125.430 1.00 19.27 ? 245  HIS   B C     1 
ATOM   10792 O  O     . HIS   B 1  247  ? 3.306   7.864   126.255 1.00 21.20 ? 245  HIS   B O     1 
ATOM   10793 C  CB    . HIS   B 1  247  ? 6.329   8.133   124.997 1.00 19.84 ? 245  HIS   B CB    1 
ATOM   10794 C  CG    . HIS   B 1  247  ? 7.320   7.201   124.379 1.00 21.04 ? 245  HIS   B CG    1 
ATOM   10795 N  ND1   . HIS   B 1  247  ? 7.293   5.841   124.595 1.00 21.88 ? 245  HIS   B ND1   1 
ATOM   10796 C  CD2   . HIS   B 1  247  ? 8.368   7.432   123.556 1.00 23.67 ? 245  HIS   B CD2   1 
ATOM   10797 C  CE1   . HIS   B 1  247  ? 8.275   5.271   123.921 1.00 24.00 ? 245  HIS   B CE1   1 
ATOM   10798 N  NE2   . HIS   B 1  247  ? 8.943   6.215   123.283 1.00 25.81 ? 245  HIS   B NE2   1 
ATOM   10799 N  N     . ALA   B 1  248  ? 3.701   9.880   125.336 1.00 19.17 ? 246  ALA   B N     1 
ATOM   10800 C  CA    . ALA   B 1  248  ? 2.786   10.544  126.258 1.00 18.95 ? 246  ALA   B CA    1 
ATOM   10801 C  C     . ALA   B 1  248  ? 1.346   10.145  125.973 1.00 19.02 ? 246  ALA   B C     1 
ATOM   10802 O  O     . ALA   B 1  248  ? 0.584   9.824   126.896 1.00 21.87 ? 246  ALA   B O     1 
ATOM   10803 C  CB    . ALA   B 1  248  ? 2.959   12.061  126.154 1.00 22.21 ? 246  ALA   B CB    1 
ATOM   10804 N  N     . ILE   B 1  249  ? 0.964   10.161  124.693 1.00 20.42 ? 247  ILE   B N     1 
ATOM   10805 C  CA    . ILE   B 1  249  ? -0.390  9.785   124.301 1.00 18.79 ? 247  ILE   B CA    1 
ATOM   10806 C  C     . ILE   B 1  249  ? -0.645  8.318   124.601 1.00 21.12 ? 247  ILE   B C     1 
ATOM   10807 O  O     . ILE   B 1  249  ? -1.717  7.947   125.095 1.00 22.11 ? 247  ILE   B O     1 
ATOM   10808 C  CB    . ILE   B 1  249  ? -0.606  10.097  122.812 1.00 18.95 ? 247  ILE   B CB    1 
ATOM   10809 C  CG1   . ILE   B 1  249  ? -0.502  11.595  122.551 1.00 19.91 ? 247  ILE   B CG1   1 
ATOM   10810 C  CG2   . ILE   B 1  249  ? -1.961  9.548   122.344 1.00 21.38 ? 247  ILE   B CG2   1 
ATOM   10811 C  CD1   . ILE   B 1  249  ? -0.228  11.931  121.098 1.00 19.77 ? 247  ILE   B CD1   1 
ATOM   10812 N  N     . GLY   B 1  250  ? 0.329   7.462   124.295 1.00 21.13 ? 248  GLY   B N     1 
ATOM   10813 C  CA    . GLY   B 1  250  ? 0.163   6.043   124.548 1.00 21.77 ? 248  GLY   B CA    1 
ATOM   10814 C  C     . GLY   B 1  250  ? 0.003   5.726   126.019 1.00 26.03 ? 248  GLY   B C     1 
ATOM   10815 O  O     . GLY   B 1  250  ? -0.831  4.904   126.403 1.00 25.66 ? 248  GLY   B O     1 
ATOM   10816 N  N     . LYS   B 1  251  ? 0.807   6.367   126.865 1.00 22.79 ? 249  LYS   B N     1 
ATOM   10817 C  CA    . LYS   B 1  251  ? 0.653   6.146   128.295 1.00 25.66 ? 249  LYS   B CA    1 
ATOM   10818 C  C     . LYS   B 1  251  ? -0.697  6.660   128.784 1.00 22.41 ? 249  LYS   B C     1 
ATOM   10819 O  O     . LYS   B 1  251  ? -1.369  5.995   129.586 1.00 25.79 ? 249  LYS   B O     1 
ATOM   10820 C  CB    . LYS   B 1  251  ? 1.817   6.787   129.055 1.00 26.76 ? 249  LYS   B CB    1 
ATOM   10821 N  N     . ALA   B 1  252  ? -1.129  7.820   128.278 1.00 22.57 ? 250  ALA   B N     1 
ATOM   10822 C  CA    . ALA   B 1  252  ? -2.431  8.364   128.665 1.00 23.53 ? 250  ALA   B CA    1 
ATOM   10823 C  C     . ALA   B 1  252  ? -3.575  7.490   128.166 1.00 23.54 ? 250  ALA   B C     1 
ATOM   10824 O  O     . ALA   B 1  252  ? -4.600  7.354   128.848 1.00 25.49 ? 250  ALA   B O     1 
ATOM   10825 C  CB    . ALA   B 1  252  ? -2.594  9.783   128.129 1.00 24.67 ? 250  ALA   B CB    1 
ATOM   10826 N  N     . SER   B 1  253  ? -3.432  6.920   126.968 1.00 25.19 ? 251  SER   B N     1 
ATOM   10827 C  CA    . SER   B 1  253  ? -4.457  6.016   126.457 1.00 23.07 ? 251  SER   B CA    1 
ATOM   10828 C  C     . SER   B 1  253  ? -4.727  4.885   127.438 1.00 23.97 ? 251  SER   B C     1 
ATOM   10829 O  O     . SER   B 1  253  ? -5.884  4.508   127.659 1.00 26.22 ? 251  SER   B O     1 
ATOM   10830 C  CB    . SER   B 1  253  ? -4.028  5.451   125.109 1.00 22.66 ? 251  SER   B CB    1 
ATOM   10831 O  OG    . SER   B 1  253  ? -4.986  4.509   124.657 1.00 24.10 ? 251  SER   B OG    1 
ATOM   10832 N  N     . ALA   B 1  254  ? -3.667  4.331   128.033 1.00 23.93 ? 252  ALA   B N     1 
ATOM   10833 C  CA    . ALA   B 1  254  ? -3.779  3.346   129.110 1.00 27.50 ? 252  ALA   B CA    1 
ATOM   10834 C  C     . ALA   B 1  254  ? -4.621  2.140   128.700 1.00 27.91 ? 252  ALA   B C     1 
ATOM   10835 O  O     . ALA   B 1  254  ? -5.421  1.625   129.481 1.00 30.61 ? 252  ALA   B O     1 
ATOM   10836 C  CB    . ALA   B 1  254  ? -4.278  3.973   130.414 1.00 28.11 ? 252  ALA   B CB    1 
ATOM   10837 N  N     . GLY   B 1  255  ? -4.450  1.694   127.457 1.00 31.14 ? 253  GLY   B N     1 
ATOM   10838 C  CA    . GLY   B 1  255  ? -5.159  0.527   126.978 1.00 28.88 ? 253  GLY   B CA    1 
ATOM   10839 C  C     . GLY   B 1  255  ? -6.581  0.765   126.525 1.00 26.48 ? 253  GLY   B C     1 
ATOM   10840 O  O     . GLY   B 1  255  ? -7.319  -0.206  126.338 1.00 29.54 ? 253  GLY   B O     1 
ATOM   10841 N  N     . ARG   B 1  256  ? -6.997  2.018   126.347 1.00 25.47 ? 254  ARG   B N     1 
ATOM   10842 C  CA    . ARG   B 1  256  ? -8.348  2.270   125.856 1.00 28.17 ? 254  ARG   B CA    1 
ATOM   10843 C  C     . ARG   B 1  256  ? -8.547  1.824   124.419 1.00 24.89 ? 254  ARG   B C     1 
ATOM   10844 O  O     . ARG   B 1  256  ? -9.696  1.718   123.978 1.00 26.65 ? 254  ARG   B O     1 
ATOM   10845 C  CB    . ARG   B 1  256  ? -8.725  3.743   126.016 1.00 23.90 ? 254  ARG   B CB    1 
ATOM   10846 C  CG    . ARG   B 1  256  ? -9.168  4.069   127.437 1.00 25.39 ? 254  ARG   B CG    1 
ATOM   10847 C  CD    . ARG   B 1  256  ? -9.464  5.535   127.588 1.00 27.24 ? 254  ARG   B CD    1 
ATOM   10848 N  NE    . ARG   B 1  256  ? -8.235  6.321   127.607 1.00 24.86 ? 254  ARG   B NE    1 
ATOM   10849 C  CZ    . ARG   B 1  256  ? -8.190  7.633   127.455 1.00 25.88 ? 254  ARG   B CZ    1 
ATOM   10850 N  NH1   . ARG   B 1  256  ? -9.277  8.333   127.174 1.00 28.08 ? 254  ARG   B NH1   1 
ATOM   10851 N  NH2   . ARG   B 1  256  ? -7.026  8.265   127.604 1.00 27.43 ? 254  ARG   B NH2   1 
ATOM   10852 N  N     . GLY   B 1  257  ? -7.469  1.563   123.685 1.00 25.82 ? 255  GLY   B N     1 
ATOM   10853 C  CA    . GLY   B 1  257  ? -7.587  1.105   122.316 1.00 23.33 ? 255  GLY   B CA    1 
ATOM   10854 C  C     . GLY   B 1  257  ? -7.724  2.252   121.346 1.00 25.18 ? 255  GLY   B C     1 
ATOM   10855 O  O     . GLY   B 1  257  ? -7.788  3.425   121.708 1.00 24.44 ? 255  GLY   B O     1 
ATOM   10856 N  N     . ILE   B 1  258  ? -7.797  1.894   120.066 1.00 23.93 ? 256  ILE   B N     1 
ATOM   10857 C  CA    . ILE   B 1  258  ? -7.709  2.903   119.018 1.00 23.93 ? 256  ILE   B CA    1 
ATOM   10858 C  C     . ILE   B 1  258  ? -9.001  3.688   118.807 1.00 22.41 ? 256  ILE   B C     1 
ATOM   10859 O  O     . ILE   B 1  258  ? -8.962  4.755   118.190 1.00 23.50 ? 256  ILE   B O     1 
ATOM   10860 C  CB    . ILE   B 1  258  ? -7.258  2.270   117.697 1.00 24.36 ? 256  ILE   B CB    1 
ATOM   10861 C  CG1   . ILE   B 1  258  ? -8.286  1.235   117.252 1.00 23.72 ? 256  ILE   B CG1   1 
ATOM   10862 C  CG2   . ILE   B 1  258  ? -5.903  1.610   117.863 1.00 25.03 ? 256  ILE   B CG2   1 
ATOM   10863 C  CD1   . ILE   B 1  258  ? -7.953  0.586   115.932 1.00 24.90 ? 256  ILE   B CD1   1 
ATOM   10864 N  N     . TYR   B 1  259  ? -10.140 3.201   119.299 1.00 23.81 ? 257  TYR   B N     1 
ATOM   10865 C  CA    . TYR   B 1  259  ? -11.410 3.887   119.080 1.00 24.69 ? 257  TYR   B CA    1 
ATOM   10866 C  C     . TYR   B 1  259  ? -11.758 4.833   120.222 1.00 25.07 ? 257  TYR   B C     1 
ATOM   10867 O  O     . TYR   B 1  259  ? -11.993 6.025   119.998 1.00 23.38 ? 257  TYR   B O     1 
ATOM   10868 C  CB    . TYR   B 1  259  ? -12.532 2.863   118.859 1.00 23.95 ? 257  TYR   B CB    1 
ATOM   10869 C  CG    . TYR   B 1  259  ? -12.180 1.896   117.749 1.00 25.17 ? 257  TYR   B CG    1 
ATOM   10870 C  CD1   . TYR   B 1  259  ? -12.065 2.337   116.442 1.00 27.15 ? 257  TYR   B CD1   1 
ATOM   10871 C  CD2   . TYR   B 1  259  ? -11.930 0.556   118.013 1.00 28.76 ? 257  TYR   B CD2   1 
ATOM   10872 C  CE1   . TYR   B 1  259  ? -11.721 1.473   115.420 1.00 25.42 ? 257  TYR   B CE1   1 
ATOM   10873 C  CE2   . TYR   B 1  259  ? -11.593 -0.318  116.996 1.00 25.31 ? 257  TYR   B CE2   1 
ATOM   10874 C  CZ    . TYR   B 1  259  ? -11.482 0.151   115.704 1.00 27.05 ? 257  TYR   B CZ    1 
ATOM   10875 O  OH    . TYR   B 1  259  ? -11.137 -0.703  114.679 1.00 29.17 ? 257  TYR   B OH    1 
ATOM   10876 N  N     . GLU   B 1  260  ? -11.791 4.318   121.448 1.00 25.17 ? 258  GLU   B N     1 
ATOM   10877 C  CA    . GLU   B 1  260  ? -12.064 5.180   122.589 1.00 24.68 ? 258  GLU   B CA    1 
ATOM   10878 C  C     . GLU   B 1  260  ? -10.864 6.058   122.908 1.00 27.99 ? 258  GLU   B C     1 
ATOM   10879 O  O     . GLU   B 1  260  ? -11.018 7.236   123.260 1.00 28.43 ? 258  GLU   B O     1 
ATOM   10880 C  CB    . GLU   B 1  260  ? -12.444 4.343   123.805 1.00 26.23 ? 258  GLU   B CB    1 
ATOM   10881 C  CG    . GLU   B 1  260  ? -12.670 5.176   125.051 1.00 36.29 ? 258  GLU   B CG    1 
ATOM   10882 C  CD    . GLU   B 1  260  ? -12.894 4.329   126.287 1.00 38.78 ? 258  GLU   B CD    1 
ATOM   10883 O  OE1   . GLU   B 1  260  ? -13.105 3.104   126.144 1.00 43.68 ? 258  GLU   B OE1   1 
ATOM   10884 O  OE2   . GLU   B 1  260  ? -12.854 4.895   127.402 1.00 40.73 ? 258  GLU   B OE2   1 
ATOM   10885 N  N     . GLY   B 1  261  ? -9.664  5.513   122.766 1.00 23.14 ? 259  GLY   B N     1 
ATOM   10886 C  CA    . GLY   B 1  261  ? -8.475  6.176   123.236 1.00 24.49 ? 259  GLY   B CA    1 
ATOM   10887 C  C     . GLY   B 1  261  ? -7.898  7.117   122.204 1.00 24.68 ? 259  GLY   B C     1 
ATOM   10888 O  O     . GLY   B 1  261  ? -8.255  7.089   121.023 1.00 23.10 ? 259  GLY   B O     1 
ATOM   10889 N  N     . PRO   B 1  262  ? -6.981  7.967   122.642 1.00 21.79 ? 260  PRO   B N     1 
ATOM   10890 C  CA    . PRO   B 1  262  ? -6.435  8.997   121.759 1.00 20.45 ? 260  PRO   B CA    1 
ATOM   10891 C  C     . PRO   B 1  262  ? -5.453  8.416   120.758 1.00 22.32 ? 260  PRO   B C     1 
ATOM   10892 O  O     . PRO   B 1  262  ? -4.877  7.339   120.946 1.00 24.01 ? 260  PRO   B O     1 
ATOM   10893 C  CB    . PRO   B 1  262  ? -5.706  9.931   122.731 1.00 21.20 ? 260  PRO   B CB    1 
ATOM   10894 C  CG    . PRO   B 1  262  ? -5.324  9.027   123.877 1.00 23.18 ? 260  PRO   B CG    1 
ATOM   10895 C  CD    . PRO   B 1  262  ? -6.499  8.103   124.026 1.00 21.98 ? 260  PRO   B CD    1 
ATOM   10896 N  N     . GLY   B 1  263  ? -5.265  9.162   119.678 1.00 19.76 ? 261  GLY   B N     1 
ATOM   10897 C  CA    . GLY   B 1  263  ? -4.248  8.829   118.707 1.00 20.25 ? 261  GLY   B CA    1 
ATOM   10898 C  C     . GLY   B 1  263  ? -3.410  10.038  118.365 1.00 19.21 ? 261  GLY   B C     1 
ATOM   10899 O  O     . GLY   B 1  263  ? -3.536  11.098  118.989 1.00 19.76 ? 261  GLY   B O     1 
ATOM   10900 N  N     . ILE   B 1  264  ? -2.555  9.892   117.363 1.00 19.95 ? 262  ILE   B N     1 
ATOM   10901 C  CA    . ILE   B 1  264  ? -1.699  10.975  116.901 1.00 18.49 ? 262  ILE   B CA    1 
ATOM   10902 C  C     . ILE   B 1  264  ? -1.866  11.083  115.397 1.00 19.94 ? 262  ILE   B C     1 
ATOM   10903 O  O     . ILE   B 1  264  ? -2.212  10.106  114.728 1.00 21.24 ? 262  ILE   B O     1 
ATOM   10904 C  CB    . ILE   B 1  264  ? -0.224  10.734  117.301 1.00 20.42 ? 262  ILE   B CB    1 
ATOM   10905 C  CG1   . ILE   B 1  264  ? 0.609   12.001  117.116 1.00 19.15 ? 262  ILE   B CG1   1 
ATOM   10906 C  CG2   . ILE   B 1  264  ? 0.363   9.589   116.509 1.00 21.36 ? 262  ILE   B CG2   1 
ATOM   10907 C  CD1   . ILE   B 1  264  ? 2.025   11.887  117.670 1.00 21.99 ? 262  ILE   B CD1   1 
ATOM   10908 N  N     . SER   B 1  265  ? -1.673  12.291  114.871 1.00 16.56 ? 263  SER   B N     1 
ATOM   10909 C  CA    . SER   B 1  265  ? -1.664  12.545  113.437 1.00 16.91 ? 263  SER   B CA    1 
ATOM   10910 C  C     . SER   B 1  265  ? -0.294  13.093  113.082 1.00 19.80 ? 263  SER   B C     1 
ATOM   10911 O  O     . SER   B 1  265  ? 0.252   13.922  113.811 1.00 22.28 ? 263  SER   B O     1 
ATOM   10912 C  CB    . SER   B 1  265  ? -2.713  13.582  113.069 1.00 20.33 ? 263  SER   B CB    1 
ATOM   10913 O  OG    . SER   B 1  265  ? -4.014  13.012  113.101 1.00 21.22 ? 263  SER   B OG    1 
ATOM   10914 N  N     . ILE   B 1  266  ? 0.265   12.625  111.967 1.00 17.71 ? 264  ILE   B N     1 
ATOM   10915 C  CA    . ILE   B 1  266  ? 1.577   13.070  111.525 1.00 16.68 ? 264  ILE   B CA    1 
ATOM   10916 C  C     . ILE   B 1  266  ? 1.463   13.540  110.086 1.00 17.52 ? 264  ILE   B C     1 
ATOM   10917 O  O     . ILE   B 1  266  ? 0.538   13.175  109.361 1.00 18.42 ? 264  ILE   B O     1 
ATOM   10918 C  CB    . ILE   B 1  266  ? 2.649   11.964  111.646 1.00 19.43 ? 264  ILE   B CB    1 
ATOM   10919 C  CG1   . ILE   B 1  266  ? 2.321   10.794  110.717 1.00 23.38 ? 264  ILE   B CG1   1 
ATOM   10920 C  CG2   . ILE   B 1  266  ? 2.778   11.505  113.093 1.00 20.21 ? 264  ILE   B CG2   1 
ATOM   10921 C  CD1   . ILE   B 1  266  ? 3.469   9.811   110.525 1.00 24.16 ? 264  ILE   B CD1   1 
ATOM   10922 N  N     . LYS   B 1  267  ? 2.426   14.355  109.678 1.00 17.21 ? 265  LYS   B N     1 
ATOM   10923 C  CA    . LYS   B 1  267  ? 2.567   14.759  108.288 1.00 17.24 ? 265  LYS   B CA    1 
ATOM   10924 C  C     . LYS   B 1  267  ? 3.887   14.206  107.781 1.00 16.63 ? 265  LYS   B C     1 
ATOM   10925 O  O     . LYS   B 1  267  ? 4.940   14.445  108.386 1.00 17.56 ? 265  LYS   B O     1 
ATOM   10926 C  CB    . LYS   B 1  267  ? 2.543   16.280  108.175 1.00 19.28 ? 265  LYS   B CB    1 
ATOM   10927 C  CG    . LYS   B 1  267  ? 1.140   16.860  108.311 1.00 25.91 ? 265  LYS   B CG    1 
ATOM   10928 C  CD    . LYS   B 1  267  ? 1.160   18.375  108.297 1.00 31.85 ? 265  LYS   B CD    1 
ATOM   10929 C  CE    . LYS   B 1  267  ? -0.249  18.951  108.375 1.00 35.70 ? 265  LYS   B CE    1 
ATOM   10930 N  NZ    . LYS   B 1  267  ? -1.044  18.397  109.511 1.00 35.05 ? 265  LYS   B NZ    1 
ATOM   10931 N  N     . LEU   B 1  268  ? 3.833   13.459  106.678 1.00 16.47 ? 266  LEU   B N     1 
ATOM   10932 C  CA    . LEU   B 1  268  ? 5.069   12.922  106.122 1.00 17.33 ? 266  LEU   B CA    1 
ATOM   10933 C  C     . LEU   B 1  268  ? 6.044   14.028  105.748 1.00 18.43 ? 266  LEU   B C     1 
ATOM   10934 O  O     . LEU   B 1  268  ? 7.258   13.836  105.865 1.00 17.50 ? 266  LEU   B O     1 
ATOM   10935 C  CB    . LEU   B 1  268  ? 4.773   12.027  104.922 1.00 17.65 ? 266  LEU   B CB    1 
ATOM   10936 C  CG    . LEU   B 1  268  ? 3.868   10.838  105.243 1.00 18.14 ? 266  LEU   B CG    1 
ATOM   10937 C  CD1   . LEU   B 1  268  ? 3.663   9.994   104.008 1.00 21.23 ? 266  LEU   B CD1   1 
ATOM   10938 C  CD2   . LEU   B 1  268  ? 4.421   9.994   106.385 1.00 21.40 ? 266  LEU   B CD2   1 
ATOM   10939 N  N     . SER   B 1  269  ? 5.550   15.201  105.339 1.00 17.32 ? 267  SER   B N     1 
ATOM   10940 C  CA    . SER   B 1  269  ? 6.470   16.280  104.989 1.00 16.78 ? 267  SER   B CA    1 
ATOM   10941 C  C     . SER   B 1  269  ? 7.260   16.781  106.187 1.00 17.76 ? 267  SER   B C     1 
ATOM   10942 O  O     . SER   B 1  269  ? 8.312   17.400  105.998 1.00 17.98 ? 267  SER   B O     1 
ATOM   10943 C  CB    . SER   B 1  269  ? 5.724   17.457  104.361 1.00 19.28 ? 267  SER   B CB    1 
ATOM   10944 O  OG    . SER   B 1  269  ? 4.926   18.107  105.340 1.00 19.26 ? 267  SER   B OG    1 
ATOM   10945 N  N     . ALA   B 1  270  ? 6.781   16.534  107.402 1.00 15.26 ? 268  ALA   B N     1 
ATOM   10946 C  CA    . ALA   B 1  270  ? 7.553   16.893  108.582 1.00 17.40 ? 268  ALA   B CA    1 
ATOM   10947 C  C     . ALA   B 1  270  ? 8.761   15.994  108.761 1.00 19.46 ? 268  ALA   B C     1 
ATOM   10948 O  O     . ALA   B 1  270  ? 9.698   16.371  109.474 1.00 17.38 ? 268  ALA   B O     1 
ATOM   10949 C  CB    . ALA   B 1  270  ? 6.696   16.769  109.843 1.00 18.94 ? 268  ALA   B CB    1 
ATOM   10950 N  N     . LEU   B 1  271  ? 8.747   14.799  108.173 1.00 17.41 ? 269  LEU   B N     1 
ATOM   10951 C  CA    . LEU   B 1  271  ? 9.726   13.775  108.503 1.00 19.52 ? 269  LEU   B CA    1 
ATOM   10952 C  C     . LEU   B 1  271  ? 10.868  13.689  107.509 1.00 16.88 ? 269  LEU   B C     1 
ATOM   10953 O  O     . LEU   B 1  271  ? 11.784  12.882  107.707 1.00 19.14 ? 269  LEU   B O     1 
ATOM   10954 C  CB    . LEU   B 1  271  ? 9.048   12.414  108.644 1.00 16.86 ? 269  LEU   B CB    1 
ATOM   10955 C  CG    . LEU   B 1  271  ? 8.086   12.378  109.831 1.00 19.15 ? 269  LEU   B CG    1 
ATOM   10956 C  CD1   . LEU   B 1  271  ? 7.316   11.071  109.787 1.00 23.47 ? 269  LEU   B CD1   1 
ATOM   10957 C  CD2   . LEU   B 1  271  ? 8.853   12.513  111.135 1.00 21.47 ? 269  LEU   B CD2   1 
ATOM   10958 N  N     . HIS   B 1  272  ? 10.844  14.503  106.456 1.00 17.62 ? 270  HIS   B N     1 
ATOM   10959 C  CA    . HIS   B 1  272  ? 11.951  14.473  105.520 1.00 17.71 ? 270  HIS   B CA    1 
ATOM   10960 C  C     . HIS   B 1  272  ? 11.966  15.778  104.756 1.00 15.54 ? 270  HIS   B C     1 
ATOM   10961 O  O     . HIS   B 1  272  ? 10.899  16.240  104.342 1.00 18.60 ? 270  HIS   B O     1 
ATOM   10962 C  CB    . HIS   B 1  272  ? 11.799  13.309  104.544 1.00 18.50 ? 270  HIS   B CB    1 
ATOM   10963 C  CG    . HIS   B 1  272  ? 13.078  12.960  103.867 1.00 19.70 ? 270  HIS   B CG    1 
ATOM   10964 N  ND1   . HIS   B 1  272  ? 13.577  13.689  102.811 1.00 19.92 ? 270  HIS   B ND1   1 
ATOM   10965 C  CD2   . HIS   B 1  272  ? 13.998  12.006  104.140 1.00 24.18 ? 270  HIS   B CD2   1 
ATOM   10966 C  CE1   . HIS   B 1  272  ? 14.738  13.180  102.440 1.00 21.28 ? 270  HIS   B CE1   1 
ATOM   10967 N  NE2   . HIS   B 1  272  ? 15.018  12.159  103.232 1.00 23.63 ? 270  HIS   B NE2   1 
ATOM   10968 N  N     . PRO   B 1  273  ? 13.133  16.400  104.554 1.00 16.74 ? 271  PRO   B N     1 
ATOM   10969 C  CA    . PRO   B 1  273  ? 13.165  17.685  103.835 1.00 18.17 ? 271  PRO   B CA    1 
ATOM   10970 C  C     . PRO   B 1  273  ? 12.930  17.569  102.342 1.00 16.09 ? 271  PRO   B C     1 
ATOM   10971 O  O     . PRO   B 1  273  ? 12.715  18.602  101.694 1.00 18.46 ? 271  PRO   B O     1 
ATOM   10972 C  CB    . PRO   B 1  273  ? 14.567  18.225  104.126 1.00 18.97 ? 271  PRO   B CB    1 
ATOM   10973 C  CG    . PRO   B 1  273  ? 15.383  17.009  104.456 1.00 21.40 ? 271  PRO   B CG    1 
ATOM   10974 C  CD    . PRO   B 1  273  ? 14.441  16.036  105.120 1.00 17.47 ? 271  PRO   B CD    1 
ATOM   10975 N  N     . ARG   B 1  274  ? 12.947  16.368  101.776 1.00 16.12 ? 272  ARG   B N     1 
ATOM   10976 C  CA    . ARG   B 1  274  ? 12.744  16.158  100.346 1.00 15.89 ? 272  ARG   B CA    1 
ATOM   10977 C  C     . ARG   B 1  274  ? 11.633  15.151  100.124 1.00 17.29 ? 272  ARG   B C     1 
ATOM   10978 O  O     . ARG   B 1  274  ? 11.783  14.156  99.415  1.00 18.47 ? 272  ARG   B O     1 
ATOM   10979 C  CB    . ARG   B 1  274  ? 14.029  15.716  99.645  1.00 17.88 ? 272  ARG   B CB    1 
ATOM   10980 C  CG    . ARG   B 1  274  ? 15.168  16.727  99.693  1.00 18.67 ? 272  ARG   B CG    1 
ATOM   10981 C  CD    . ARG   B 1  274  ? 14.758  18.069  99.098  1.00 19.05 ? 272  ARG   B CD    1 
ATOM   10982 N  NE    . ARG   B 1  274  ? 14.292  17.963  97.718  1.00 19.19 ? 272  ARG   B NE    1 
ATOM   10983 C  CZ    . ARG   B 1  274  ? 15.086  17.888  96.658  1.00 18.45 ? 272  ARG   B CZ    1 
ATOM   10984 N  NH1   . ARG   B 1  274  ? 16.405  17.824  96.784  1.00 18.11 ? 272  ARG   B NH1   1 
ATOM   10985 N  NH2   . ARG   B 1  274  ? 14.545  17.870  95.446  1.00 19.11 ? 272  ARG   B NH2   1 
ATOM   10986 N  N     . TYR   B 1  275  ? 10.488  15.389  100.763 1.00 15.67 ? 273  TYR   B N     1 
ATOM   10987 C  CA    . TYR   B 1  275  ? 9.327   14.521  100.599 1.00 18.70 ? 273  TYR   B CA    1 
ATOM   10988 C  C     . TYR   B 1  275  ? 8.649   14.855  99.272  1.00 17.45 ? 273  TYR   B C     1 
ATOM   10989 O  O     . TYR   B 1  275  ? 7.797   15.741  99.175  1.00 17.56 ? 273  TYR   B O     1 
ATOM   10990 C  CB    . TYR   B 1  275  ? 8.392   14.659  101.796 1.00 17.09 ? 273  TYR   B CB    1 
ATOM   10991 C  CG    . TYR   B 1  275  ? 7.140   13.855  101.641 1.00 16.12 ? 273  TYR   B CG    1 
ATOM   10992 C  CD1   . TYR   B 1  275  ? 7.198   12.520  101.267 1.00 18.05 ? 273  TYR   B CD1   1 
ATOM   10993 C  CD2   . TYR   B 1  275  ? 5.905   14.427  101.852 1.00 15.99 ? 273  TYR   B CD2   1 
ATOM   10994 C  CE1   . TYR   B 1  275  ? 6.060   11.774  101.096 1.00 18.54 ? 273  TYR   B CE1   1 
ATOM   10995 C  CE2   . TYR   B 1  275  ? 4.742   13.688  101.691 1.00 17.43 ? 273  TYR   B CE2   1 
ATOM   10996 C  CZ    . TYR   B 1  275  ? 4.834   12.362  101.309 1.00 17.30 ? 273  TYR   B CZ    1 
ATOM   10997 O  OH    . TYR   B 1  275  ? 3.705   11.616  101.132 1.00 19.64 ? 273  TYR   B OH    1 
ATOM   10998 N  N     . SER   B 1  276  ? 9.046   14.146  98.221  1.00 16.45 ? 274  SER   B N     1 
ATOM   10999 C  CA    . SER   B 1  276  ? 8.520   14.440  96.893  1.00 17.28 ? 274  SER   B CA    1 
ATOM   11000 C  C     . SER   B 1  276  ? 8.761   13.242  95.995  1.00 17.30 ? 274  SER   B C     1 
ATOM   11001 O  O     . SER   B 1  276  ? 9.660   12.434  96.234  1.00 16.71 ? 274  SER   B O     1 
ATOM   11002 C  CB    . SER   B 1  276  ? 9.189   15.672  96.287  1.00 20.43 ? 274  SER   B CB    1 
ATOM   11003 O  OG    . SER   B 1  276  ? 10.529  15.386  95.952  1.00 24.72 ? 274  SER   B OG    1 
ATOM   11004 N  N     . ARG   B 1  277  ? 7.940   13.141  94.947  1.00 16.91 ? 275  ARG   B N     1 
ATOM   11005 C  CA    . ARG   B 1  277  ? 8.123   12.061  93.992  1.00 15.47 ? 275  ARG   B CA    1 
ATOM   11006 C  C     . ARG   B 1  277  ? 9.493   12.129  93.336  1.00 16.05 ? 275  ARG   B C     1 
ATOM   11007 O  O     . ARG   B 1  277  ? 10.082  11.089  93.035  1.00 16.66 ? 275  ARG   B O     1 
ATOM   11008 C  CB    . ARG   B 1  277  ? 7.004   12.111  92.953  1.00 17.14 ? 275  ARG   B CB    1 
ATOM   11009 C  CG    . ARG   B 1  277  ? 7.171   11.146  91.781  1.00 18.18 ? 275  ARG   B CG    1 
ATOM   11010 C  CD    . ARG   B 1  277  ? 7.225   9.705   92.263  1.00 17.92 ? 275  ARG   B CD    1 
ATOM   11011 N  NE    . ARG   B 1  277  ? 7.377   8.768   91.156  1.00 18.17 ? 275  ARG   B NE    1 
ATOM   11012 C  CZ    . ARG   B 1  277  ? 8.542   8.395   90.644  1.00 18.99 ? 275  ARG   B CZ    1 
ATOM   11013 N  NH1   . ARG   B 1  277  ? 9.681   8.928   91.059  1.00 20.27 ? 275  ARG   B NH1   1 
ATOM   11014 N  NH2   . ARG   B 1  277  ? 8.564   7.454   89.700  1.00 18.56 ? 275  ARG   B NH2   1 
ATOM   11015 N  N     . ALA   B 1  278  ? 10.021  13.337  93.129  1.00 16.80 ? 276  ALA   B N     1 
ATOM   11016 C  CA    . ALA   B 1  278  ? 11.339  13.454  92.516  1.00 17.74 ? 276  ALA   B CA    1 
ATOM   11017 C  C     . ALA   B 1  278  ? 12.408  12.786  93.361  1.00 16.86 ? 276  ALA   B C     1 
ATOM   11018 O  O     . ALA   B 1  278  ? 13.448  12.379  92.835  1.00 18.51 ? 276  ALA   B O     1 
ATOM   11019 C  CB    . ALA   B 1  278  ? 11.692  14.923  92.293  1.00 19.59 ? 276  ALA   B CB    1 
ATOM   11020 N  N     . GLN   B 1  279  ? 12.184  12.674  94.666  1.00 17.20 ? 277  GLN   B N     1 
ATOM   11021 C  CA    . GLN   B 1  279  ? 13.143  12.067  95.581  1.00 16.35 ? 277  GLN   B CA    1 
ATOM   11022 C  C     . GLN   B 1  279  ? 12.581  10.794  96.191  1.00 18.53 ? 277  GLN   B C     1 
ATOM   11023 O  O     . GLN   B 1  279  ? 12.861  10.468  97.345  1.00 17.36 ? 277  GLN   B O     1 
ATOM   11024 C  CB    . GLN   B 1  279  ? 13.557  13.054  96.668  1.00 19.57 ? 277  GLN   B CB    1 
ATOM   11025 C  CG    . GLN   B 1  279  ? 14.190  14.307  96.108  1.00 18.58 ? 277  GLN   B CG    1 
ATOM   11026 C  CD    . GLN   B 1  279  ? 15.478  14.009  95.361  1.00 22.17 ? 277  GLN   B CD    1 
ATOM   11027 O  OE1   . GLN   B 1  279  ? 16.165  13.017  95.636  1.00 24.42 ? 277  GLN   B OE1   1 
ATOM   11028 N  NE2   . GLN   B 1  279  ? 15.803  14.859  94.396  1.00 19.84 ? 277  GLN   B NE2   1 
ATOM   11029 N  N     . ALA   B 1  280  ? 11.795  10.055  95.409  1.00 18.50 ? 278  ALA   B N     1 
ATOM   11030 C  CA    . ALA   B 1  280  ? 11.097  8.896   95.948  1.00 17.89 ? 278  ALA   B CA    1 
ATOM   11031 C  C     . ALA   B 1  280  ? 12.056  7.900   96.583  1.00 18.61 ? 278  ALA   B C     1 
ATOM   11032 O  O     . ALA   B 1  280  ? 11.724  7.277   97.592  1.00 18.42 ? 278  ALA   B O     1 
ATOM   11033 C  CB    . ALA   B 1  280  ? 10.276  8.221   94.848  1.00 19.37 ? 278  ALA   B CB    1 
ATOM   11034 N  N     . ALA   B 1  281  ? 13.244  7.723   96.003  1.00 17.43 ? 279  ALA   B N     1 
ATOM   11035 C  CA    . ALA   B 1  281  ? 14.179  6.762   96.581  1.00 18.17 ? 279  ALA   B CA    1 
ATOM   11036 C  C     . ALA   B 1  281  ? 14.591  7.176   97.985  1.00 18.58 ? 279  ALA   B C     1 
ATOM   11037 O  O     . ALA   B 1  281  ? 14.638  6.342   98.895  1.00 19.66 ? 279  ALA   B O     1 
ATOM   11038 C  CB    . ALA   B 1  281  ? 15.403  6.583   95.677  1.00 21.66 ? 279  ALA   B CB    1 
ATOM   11039 N  N     . ARG   B 1  282  ? 14.883  8.460   98.183  1.00 16.67 ? 280  ARG   B N     1 
ATOM   11040 C  CA    . ARG   B 1  282  ? 15.225  8.938   99.516  1.00 18.19 ? 280  ARG   B CA    1 
ATOM   11041 C  C     . ARG   B 1  282  ? 14.032  8.862   100.449 1.00 18.54 ? 280  ARG   B C     1 
ATOM   11042 O  O     . ARG   B 1  282  ? 14.197  8.610   101.642 1.00 19.53 ? 280  ARG   B O     1 
ATOM   11043 C  CB    . ARG   B 1  282  ? 15.723  10.376  99.439  1.00 20.14 ? 280  ARG   B CB    1 
ATOM   11044 C  CG    . ARG   B 1  282  ? 17.078  10.523  98.778  1.00 19.46 ? 280  ARG   B CG    1 
ATOM   11045 C  CD    . ARG   B 1  282  ? 17.603  11.923  99.026  1.00 21.07 ? 280  ARG   B CD    1 
ATOM   11046 N  NE    . ARG   B 1  282  ? 17.920  12.111  100.438 1.00 21.29 ? 280  ARG   B NE    1 
ATOM   11047 C  CZ    . ARG   B 1  282  ? 18.060  13.289  101.028 1.00 20.30 ? 280  ARG   B CZ    1 
ATOM   11048 N  NH1   . ARG   B 1  282  ? 17.911  14.425  100.355 1.00 20.55 ? 280  ARG   B NH1   1 
ATOM   11049 N  NH2   . ARG   B 1  282  ? 18.350  13.332  102.325 1.00 22.80 ? 280  ARG   B NH2   1 
ATOM   11050 N  N     . VAL   B 1  283  ? 12.827  9.072   99.924  1.00 17.62 ? 281  VAL   B N     1 
ATOM   11051 C  CA    . VAL   B 1  283  ? 11.632  8.939   100.749 1.00 20.10 ? 281  VAL   B CA    1 
ATOM   11052 C  C     . VAL   B 1  283  ? 11.504  7.515   101.264 1.00 18.51 ? 281  VAL   B C     1 
ATOM   11053 O  O     . VAL   B 1  283  ? 11.338  7.285   102.468 1.00 18.60 ? 281  VAL   B O     1 
ATOM   11054 C  CB    . VAL   B 1  283  ? 10.392  9.393   99.965  1.00 17.54 ? 281  VAL   B CB    1 
ATOM   11055 C  CG1   . VAL   B 1  283  ? 9.114   9.001   100.708 1.00 20.52 ? 281  VAL   B CG1   1 
ATOM   11056 C  CG2   . VAL   B 1  283  ? 10.451  10.898  99.764  1.00 18.44 ? 281  VAL   B CG2   1 
ATOM   11057 N  N     . MET   B 1  284  ? 11.614  6.534   100.368 1.00 17.59 ? 282  MET   B N     1 
ATOM   11058 C  CA    . MET   B 1  284  ? 11.488  5.147   100.796 1.00 19.95 ? 282  MET   B CA    1 
ATOM   11059 C  C     . MET   B 1  284  ? 12.657  4.723   101.672 1.00 21.14 ? 282  MET   B C     1 
ATOM   11060 O  O     . MET   B 1  284  ? 12.480  3.915   102.591 1.00 22.59 ? 282  MET   B O     1 
ATOM   11061 C  CB    . MET   B 1  284  ? 11.342  4.219   99.587  1.00 18.41 ? 282  MET   B CB    1 
ATOM   11062 C  CG    . MET   B 1  284  ? 10.146  4.535   98.700  1.00 20.90 ? 282  MET   B CG    1 
ATOM   11063 S  SD    . MET   B 1  284  ? 8.579   4.483   99.590  1.00 23.19 ? 282  MET   B SD    1 
ATOM   11064 C  CE    . MET   B 1  284  ? 8.446   2.733   99.925  1.00 25.17 ? 282  MET   B CE    1 
ATOM   11065 N  N     . GLY   B 1  285  ? 13.851  5.259   101.411 1.00 18.54 ? 283  GLY   B N     1 
ATOM   11066 C  CA    . GLY   B 1  285  ? 15.023  4.835   102.158 1.00 20.29 ? 283  GLY   B CA    1 
ATOM   11067 C  C     . GLY   B 1  285  ? 15.176  5.502   103.505 1.00 22.41 ? 283  GLY   B C     1 
ATOM   11068 O  O     . GLY   B 1  285  ? 15.727  4.902   104.435 1.00 23.96 ? 283  GLY   B O     1 
ATOM   11069 N  N     . GLU   B 1  286  ? 14.702  6.735   103.639 1.00 18.24 ? 284  GLU   B N     1 
ATOM   11070 C  CA    . GLU   B 1  286  ? 14.963  7.558   104.814 1.00 17.40 ? 284  GLU   B CA    1 
ATOM   11071 C  C     . GLU   B 1  286  ? 13.708  7.971   105.561 1.00 20.46 ? 284  GLU   B C     1 
ATOM   11072 O  O     . GLU   B 1  286  ? 13.701  7.953   106.796 1.00 23.37 ? 284  GLU   B O     1 
ATOM   11073 C  CB    . GLU   B 1  286  ? 15.747  8.813   104.412 1.00 20.20 ? 284  GLU   B CB    1 
ATOM   11074 C  CG    . GLU   B 1  286  ? 17.023  8.505   103.616 1.00 20.79 ? 284  GLU   B CG    1 
ATOM   11075 C  CD    . GLU   B 1  286  ? 17.621  9.731   102.951 1.00 24.38 ? 284  GLU   B CD    1 
ATOM   11076 O  OE1   . GLU   B 1  286  ? 17.414  10.846  103.462 1.00 23.26 ? 284  GLU   B OE1   1 
ATOM   11077 O  OE2   . GLU   B 1  286  ? 18.292  9.580   101.909 1.00 28.74 ? 284  GLU   B OE2   1 
ATOM   11078 N  N     . LEU   B 1  287  ? 12.651  8.353   104.849 1.00 19.31 ? 285  LEU   B N     1 
ATOM   11079 C  CA    . LEU   B 1  287  ? 11.411  8.747   105.505 1.00 20.59 ? 285  LEU   B CA    1 
ATOM   11080 C  C     . LEU   B 1  287  ? 10.662  7.526   106.019 1.00 21.94 ? 285  LEU   B C     1 
ATOM   11081 O  O     . LEU   B 1  287  ? 10.225  7.500   107.173 1.00 18.41 ? 285  LEU   B O     1 
ATOM   11082 C  CB    . LEU   B 1  287  ? 10.548  9.544   104.522 1.00 19.06 ? 285  LEU   B CB    1 
ATOM   11083 C  CG    . LEU   B 1  287  ? 9.514   10.527  105.093 1.00 22.82 ? 285  LEU   B CG    1 
ATOM   11084 C  CD1   . LEU   B 1  287  ? 8.943   11.377  103.985 1.00 21.53 ? 285  LEU   B CD1   1 
ATOM   11085 C  CD2   . LEU   B 1  287  ? 8.393   9.832   105.818 1.00 25.38 ? 285  LEU   B CD2   1 
ATOM   11086 N  N     . LEU   B 1  288  ? 10.503  6.508   105.177 1.00 19.81 ? 286  LEU   B N     1 
ATOM   11087 C  CA    . LEU   B 1  288  ? 9.726   5.334   105.569 1.00 20.75 ? 286  LEU   B CA    1 
ATOM   11088 C  C     . LEU   B 1  288  ? 10.203  4.691   106.864 1.00 20.76 ? 286  LEU   B C     1 
ATOM   11089 O  O     . LEU   B 1  288  ? 9.360   4.423   107.734 1.00 19.73 ? 286  LEU   B O     1 
ATOM   11090 C  CB    . LEU   B 1  288  ? 9.656   4.327   104.415 1.00 22.86 ? 286  LEU   B CB    1 
ATOM   11091 C  CG    . LEU   B 1  288  ? 9.037   2.983   104.774 1.00 24.04 ? 286  LEU   B CG    1 
ATOM   11092 C  CD1   . LEU   B 1  288  ? 7.601   3.156   105.251 1.00 24.90 ? 286  LEU   B CD1   1 
ATOM   11093 C  CD2   . LEU   B 1  288  ? 9.094   2.080   103.560 1.00 31.61 ? 286  LEU   B CD2   1 
ATOM   11094 N  N     . PRO   B 1  289  ? 11.496  4.432   107.075 1.00 19.67 ? 287  PRO   B N     1 
ATOM   11095 C  CA    . PRO   B 1  289  ? 11.909  3.880   108.377 1.00 21.19 ? 287  PRO   B CA    1 
ATOM   11096 C  C     . PRO   B 1  289  ? 11.483  4.732   109.564 1.00 19.46 ? 287  PRO   B C     1 
ATOM   11097 O  O     . PRO   B 1  289  ? 11.200  4.183   110.637 1.00 20.50 ? 287  PRO   B O     1 
ATOM   11098 C  CB    . PRO   B 1  289  ? 13.436  3.797   108.254 1.00 25.42 ? 287  PRO   B CB    1 
ATOM   11099 C  CG    . PRO   B 1  289  ? 13.667  3.640   106.781 1.00 23.26 ? 287  PRO   B CG    1 
ATOM   11100 C  CD    . PRO   B 1  289  ? 12.629  4.505   106.131 1.00 21.30 ? 287  PRO   B CD    1 
ATOM   11101 N  N     . ARG   B 1  290  ? 11.417  6.057   109.401 1.00 18.80 ? 288  ARG   B N     1 
ATOM   11102 C  CA    . ARG   B 1  290  ? 10.965  6.907   110.495 1.00 20.21 ? 288  ARG   B CA    1 
ATOM   11103 C  C     . ARG   B 1  290  ? 9.490   6.684   110.782 1.00 18.05 ? 288  ARG   B C     1 
ATOM   11104 O  O     . ARG   B 1  290  ? 9.088   6.588   111.947 1.00 18.51 ? 288  ARG   B O     1 
ATOM   11105 C  CB    . ARG   B 1  290  ? 11.239  8.371   110.177 1.00 21.94 ? 288  ARG   B CB    1 
ATOM   11106 C  CG    . ARG   B 1  290  ? 12.715  8.697   110.221 1.00 24.29 ? 288  ARG   B CG    1 
ATOM   11107 C  CD    . ARG   B 1  290  ? 12.984  10.099  109.725 1.00 32.18 ? 288  ARG   B CD    1 
ATOM   11108 N  NE    . ARG   B 1  290  ? 14.205  10.641  110.308 1.00 35.43 ? 288  ARG   B NE    1 
ATOM   11109 C  CZ    . ARG   B 1  290  ? 14.785  11.767  109.915 1.00 39.17 ? 288  ARG   B CZ    1 
ATOM   11110 N  NH1   . ARG   B 1  290  ? 14.304  12.476  108.905 1.00 33.91 ? 288  ARG   B NH1   1 
ATOM   11111 N  NH2   . ARG   B 1  290  ? 15.873  12.190  110.549 1.00 37.01 ? 288  ARG   B NH2   1 
ATOM   11112 N  N     . VAL   B 1  291  ? 8.670   6.603   109.733 1.00 19.47 ? 289  VAL   B N     1 
ATOM   11113 C  CA    . VAL   B 1  291  ? 7.256   6.342   109.955 1.00 18.68 ? 289  VAL   B CA    1 
ATOM   11114 C  C     . VAL   B 1  291  ? 7.066   4.969   110.566 1.00 19.83 ? 289  VAL   B C     1 
ATOM   11115 O  O     . VAL   B 1  291  ? 6.229   4.786   111.462 1.00 19.90 ? 289  VAL   B O     1 
ATOM   11116 C  CB    . VAL   B 1  291  ? 6.450   6.480   108.656 1.00 19.27 ? 289  VAL   B CB    1 
ATOM   11117 C  CG1   . VAL   B 1  291  ? 4.972   6.317   108.977 1.00 21.00 ? 289  VAL   B CG1   1 
ATOM   11118 C  CG2   . VAL   B 1  291  ? 6.706   7.813   108.020 1.00 23.57 ? 289  VAL   B CG2   1 
ATOM   11119 N  N     . LYS   B 1  292  ? 7.829   3.979   110.094 1.00 19.40 ? 290  LYS   B N     1 
ATOM   11120 C  CA    . LYS   B 1  292  ? 7.691   2.644   110.663 1.00 20.35 ? 290  LYS   B CA    1 
ATOM   11121 C  C     . LYS   B 1  292  ? 8.009   2.659   112.149 1.00 22.46 ? 290  LYS   B C     1 
ATOM   11122 O  O     . LYS   B 1  292  ? 7.312   2.025   112.948 1.00 21.66 ? 290  LYS   B O     1 
ATOM   11123 C  CB    . LYS   B 1  292  ? 8.578   1.643   109.921 1.00 22.63 ? 290  LYS   B CB    1 
ATOM   11124 C  CG    . LYS   B 1  292  ? 8.373   0.199   110.380 1.00 26.13 ? 290  LYS   B CG    1 
ATOM   11125 C  CD    . LYS   B 1  292  ? 9.357   -0.201  111.458 1.00 30.53 ? 290  LYS   B CD    1 
ATOM   11126 C  CE    . LYS   B 1  292  ? 9.080   -1.618  111.959 1.00 30.53 ? 290  LYS   B CE    1 
ATOM   11127 N  NZ    . LYS   B 1  292  ? 9.295   -2.637  110.901 1.00 27.91 ? 290  LYS   B NZ    1 
ATOM   11128 N  N     . ALA   B 1  293  ? 9.049   3.396   112.540 1.00 18.87 ? 291  ALA   B N     1 
ATOM   11129 C  CA    . ALA   B 1  293  ? 9.412   3.455   113.950 1.00 19.46 ? 291  ALA   B CA    1 
ATOM   11130 C  C     . ALA   B 1  293  ? 8.297   4.075   114.776 1.00 22.95 ? 291  ALA   B C     1 
ATOM   11131 O  O     . ALA   B 1  293  ? 7.984   3.596   115.873 1.00 20.53 ? 291  ALA   B O     1 
ATOM   11132 C  CB    . ALA   B 1  293  ? 10.697  4.257   114.111 1.00 20.63 ? 291  ALA   B CB    1 
ATOM   11133 N  N     . LEU   B 1  294  ? 7.703   5.156   114.277 1.00 18.21 ? 292  LEU   B N     1 
ATOM   11134 C  CA    . LEU   B 1  294  ? 6.595   5.776   114.987 1.00 18.84 ? 292  LEU   B CA    1 
ATOM   11135 C  C     . LEU   B 1  294  ? 5.387   4.854   115.018 1.00 20.00 ? 292  LEU   B C     1 
ATOM   11136 O  O     . LEU   B 1  294  ? 4.702   4.751   116.039 1.00 20.89 ? 292  LEU   B O     1 
ATOM   11137 C  CB    . LEU   B 1  294  ? 6.232   7.105   114.326 1.00 19.12 ? 292  LEU   B CB    1 
ATOM   11138 C  CG    . LEU   B 1  294  ? 7.356   8.143   114.298 1.00 19.23 ? 292  LEU   B CG    1 
ATOM   11139 C  CD1   . LEU   B 1  294  ? 6.926   9.339   113.477 1.00 21.29 ? 292  LEU   B CD1   1 
ATOM   11140 C  CD2   . LEU   B 1  294  ? 7.743   8.557   115.722 1.00 20.05 ? 292  LEU   B CD2   1 
ATOM   11141 N  N     . ALA   B 1  295  ? 5.111   4.170   113.908 1.00 19.93 ? 293  ALA   B N     1 
ATOM   11142 C  CA    . ALA   B 1  295  ? 3.971   3.264   113.868 1.00 20.38 ? 293  ALA   B CA    1 
ATOM   11143 C  C     . ALA   B 1  295  ? 4.166   2.107   114.837 1.00 21.37 ? 293  ALA   B C     1 
ATOM   11144 O  O     . ALA   B 1  295  ? 3.223   1.681   115.509 1.00 20.59 ? 293  ALA   B O     1 
ATOM   11145 C  CB    . ALA   B 1  295  ? 3.765   2.763   112.437 1.00 19.87 ? 293  ALA   B CB    1 
ATOM   11146 N  N     . LEU   B 1  296  ? 5.395   1.607   114.947 1.00 21.72 ? 294  LEU   B N     1 
ATOM   11147 C  CA    . LEU   B 1  296  ? 5.671   0.538   115.900 1.00 22.60 ? 294  LEU   B CA    1 
ATOM   11148 C  C     . LEU   B 1  296  ? 5.427   1.000   117.329 1.00 22.42 ? 294  LEU   B C     1 
ATOM   11149 O  O     . LEU   B 1  296  ? 4.879   0.252   118.149 1.00 22.39 ? 294  LEU   B O     1 
ATOM   11150 C  CB    . LEU   B 1  296  ? 7.108   0.052   115.723 1.00 23.67 ? 294  LEU   B CB    1 
ATOM   11151 C  CG    . LEU   B 1  296  ? 7.543   -1.138  116.577 1.00 29.71 ? 294  LEU   B CG    1 
ATOM   11152 C  CD1   . LEU   B 1  296  ? 6.575   -2.305  116.409 1.00 31.82 ? 294  LEU   B CD1   1 
ATOM   11153 C  CD2   . LEU   B 1  296  ? 8.963   -1.548  116.202 1.00 34.29 ? 294  LEU   B CD2   1 
ATOM   11154 N  N     . LEU   B 1  297  ? 5.824   2.231   117.650 1.00 20.35 ? 295  LEU   B N     1 
ATOM   11155 C  CA    . LEU   B 1  297  ? 5.520   2.762   118.976 1.00 22.14 ? 295  LEU   B CA    1 
ATOM   11156 C  C     . LEU   B 1  297  ? 4.017   2.862   119.182 1.00 21.33 ? 295  LEU   B C     1 
ATOM   11157 O  O     . LEU   B 1  297  ? 3.493   2.471   120.231 1.00 20.85 ? 295  LEU   B O     1 
ATOM   11158 C  CB    . LEU   B 1  297  ? 6.172   4.132   119.154 1.00 21.12 ? 295  LEU   B CB    1 
ATOM   11159 C  CG    . LEU   B 1  297  ? 7.676   4.161   119.414 1.00 31.05 ? 295  LEU   B CG    1 
ATOM   11160 C  CD1   . LEU   B 1  297  ? 8.185   5.596   119.355 1.00 26.97 ? 295  LEU   B CD1   1 
ATOM   11161 C  CD2   . LEU   B 1  297  ? 7.977   3.543   120.765 1.00 29.66 ? 295  LEU   B CD2   1 
ATOM   11162 N  N     . ALA   B 1  298  ? 3.303   3.395   118.188 1.00 20.22 ? 296  ALA   B N     1 
ATOM   11163 C  CA    . ALA   B 1  298  ? 1.853   3.507   118.308 1.00 19.06 ? 296  ALA   B CA    1 
ATOM   11164 C  C     . ALA   B 1  298  ? 1.212   2.136   118.476 1.00 22.47 ? 296  ALA   B C     1 
ATOM   11165 O  O     . ALA   B 1  298  ? 0.309   1.957   119.303 1.00 23.76 ? 296  ALA   B O     1 
ATOM   11166 C  CB    . ALA   B 1  298  ? 1.277   4.212   117.081 1.00 19.96 ? 296  ALA   B CB    1 
ATOM   11167 N  N     . LYS   B 1  299  ? 1.679   1.151   117.708 1.00 22.06 ? 297  LYS   B N     1 
ATOM   11168 C  CA    . LYS   B 1  299  ? 1.181   -0.210  117.866 1.00 23.29 ? 297  LYS   B CA    1 
ATOM   11169 C  C     . LYS   B 1  299  ? 1.425   -0.726  119.278 1.00 25.65 ? 297  LYS   B C     1 
ATOM   11170 O  O     . LYS   B 1  299  ? 0.543   -1.351  119.882 1.00 26.01 ? 297  LYS   B O     1 
ATOM   11171 C  CB    . LYS   B 1  299  ? 1.848   -1.130  116.848 1.00 24.26 ? 297  LYS   B CB    1 
ATOM   11172 C  CG    . LYS   B 1  299  ? 1.512   -2.596  117.069 1.00 29.69 ? 297  LYS   B CG    1 
ATOM   11173 C  CD    . LYS   B 1  299  ? 2.538   -3.502  116.435 1.00 40.12 ? 297  LYS   B CD    1 
ATOM   11174 C  CE    . LYS   B 1  299  ? 2.160   -4.962  116.612 1.00 34.86 ? 297  LYS   B CE    1 
ATOM   11175 N  NZ    . LYS   B 1  299  ? 2.099   -5.341  118.040 1.00 41.42 ? 297  LYS   B NZ    1 
ATOM   11176 N  N     . ASN   B 1  300  ? 2.616   -0.477  119.824 1.00 24.22 ? 298  ASN   B N     1 
ATOM   11177 C  CA    . ASN   B 1  300  ? 2.934   -1.010  121.144 1.00 27.84 ? 298  ASN   B CA    1 
ATOM   11178 C  C     . ASN   B 1  300  ? 2.020   -0.438  122.218 1.00 25.43 ? 298  ASN   B C     1 
ATOM   11179 O  O     . ASN   B 1  300  ? 1.711   -1.127  123.196 1.00 26.71 ? 298  ASN   B O     1 
ATOM   11180 C  CB    . ASN   B 1  300  ? 4.413   -0.788  121.467 1.00 25.36 ? 298  ASN   B CB    1 
ATOM   11181 C  CG    . ASN   B 1  300  ? 5.326   -1.711  120.656 1.00 29.70 ? 298  ASN   B CG    1 
ATOM   11182 O  OD1   . ASN   B 1  300  ? 4.895   -2.759  120.177 1.00 39.25 ? 298  ASN   B OD1   1 
ATOM   11183 N  ND2   . ASN   B 1  300  ? 6.590   -1.323  120.507 1.00 39.00 ? 298  ASN   B ND2   1 
ATOM   11184 N  N     . TYR   B 1  301  ? 1.557   0.797   122.047 1.00 23.16 ? 299  TYR   B N     1 
ATOM   11185 C  CA    . TYR   B 1  301  ? 0.590   1.394   122.957 1.00 23.93 ? 299  TYR   B CA    1 
ATOM   11186 C  C     . TYR   B 1  301  ? -0.848  1.173   122.518 1.00 22.44 ? 299  TYR   B C     1 
ATOM   11187 O  O     . TYR   B 1  301  ? -1.765  1.585   123.235 1.00 24.23 ? 299  TYR   B O     1 
ATOM   11188 C  CB    . TYR   B 1  301  ? 0.828   2.900   123.083 1.00 22.59 ? 299  TYR   B CB    1 
ATOM   11189 C  CG    . TYR   B 1  301  ? 2.077   3.295   123.841 1.00 22.16 ? 299  TYR   B CG    1 
ATOM   11190 C  CD1   . TYR   B 1  301  ? 2.165   3.116   125.217 1.00 23.00 ? 299  TYR   B CD1   1 
ATOM   11191 C  CD2   . TYR   B 1  301  ? 3.151   3.868   123.183 1.00 22.61 ? 299  TYR   B CD2   1 
ATOM   11192 C  CE1   . TYR   B 1  301  ? 3.306   3.488   125.908 1.00 24.10 ? 299  TYR   B CE1   1 
ATOM   11193 C  CE2   . TYR   B 1  301  ? 4.287   4.252   123.862 1.00 23.30 ? 299  TYR   B CE2   1 
ATOM   11194 C  CZ    . TYR   B 1  301  ? 4.356   4.057   125.220 1.00 23.03 ? 299  TYR   B CZ    1 
ATOM   11195 O  OH    . TYR   B 1  301  ? 5.479   4.427   125.912 1.00 23.75 ? 299  TYR   B OH    1 
ATOM   11196 N  N     . ASP   B 1  302  ? -1.057  0.543   121.362 1.00 22.06 ? 300  ASP   B N     1 
ATOM   11197 C  CA    . ASP   B 1  302  ? -2.378  0.374   120.753 1.00 26.16 ? 300  ASP   B CA    1 
ATOM   11198 C  C     . ASP   B 1  302  ? -3.138  1.694   120.648 1.00 22.97 ? 300  ASP   B C     1 
ATOM   11199 O  O     . ASP   B 1  302  ? -4.269  1.833   121.121 1.00 25.23 ? 300  ASP   B O     1 
ATOM   11200 C  CB    . ASP   B 1  302  ? -3.218  -0.717  121.418 1.00 25.39 ? 300  ASP   B CB    1 
ATOM   11201 C  CG    . ASP   B 1  302  ? -4.292  -1.253  120.477 1.00 26.15 ? 300  ASP   B CG    1 
ATOM   11202 O  OD1   . ASP   B 1  302  ? -4.047  -1.249  119.249 1.00 29.46 ? 300  ASP   B OD1   1 
ATOM   11203 O  OD2   . ASP   B 1  302  ? -5.377  -1.640  120.955 1.00 33.05 ? 300  ASP   B OD2   1 
ATOM   11204 N  N     . ILE   B 1  303  ? -2.497  2.677   120.022 1.00 20.54 ? 301  ILE   B N     1 
ATOM   11205 C  CA    . ILE   B 1  303  ? -3.143  3.933   119.681 1.00 21.46 ? 301  ILE   B CA    1 
ATOM   11206 C  C     . ILE   B 1  303  ? -3.171  4.052   118.166 1.00 22.80 ? 301  ILE   B C     1 
ATOM   11207 O  O     . ILE   B 1  303  ? -2.445  3.363   117.440 1.00 22.17 ? 301  ILE   B O     1 
ATOM   11208 C  CB    . ILE   B 1  303  ? -2.450  5.170   120.297 1.00 18.81 ? 301  ILE   B CB    1 
ATOM   11209 C  CG1   . ILE   B 1  303  ? -1.087  5.409   119.642 1.00 22.39 ? 301  ILE   B CG1   1 
ATOM   11210 C  CG2   . ILE   B 1  303  ? -2.300  5.014   121.785 1.00 21.26 ? 301  ILE   B CG2   1 
ATOM   11211 C  CD1   . ILE   B 1  303  ? -0.465  6.764   119.997 1.00 23.43 ? 301  ILE   B CD1   1 
ATOM   11212 N  N     . GLY   B 1  304  ? -4.010  4.966   117.693 1.00 19.51 ? 302  GLY   B N     1 
ATOM   11213 C  CA    . GLY   B 1  304  ? -4.051  5.265   116.274 1.00 18.33 ? 302  GLY   B CA    1 
ATOM   11214 C  C     . GLY   B 1  304  ? -2.921  6.204   115.877 1.00 20.08 ? 302  GLY   B C     1 
ATOM   11215 O  O     . GLY   B 1  304  ? -2.547  7.112   116.616 1.00 22.11 ? 302  GLY   B O     1 
ATOM   11216 N  N     . LEU   B 1  305  ? -2.366  5.963   114.695 1.00 18.04 ? 303  LEU   B N     1 
ATOM   11217 C  CA    . LEU   B 1  305  ? -1.394  6.864   114.092 1.00 20.08 ? 303  LEU   B CA    1 
ATOM   11218 C  C     . LEU   B 1  305  ? -1.886  7.159   112.691 1.00 19.46 ? 303  LEU   B C     1 
ATOM   11219 O  O     . LEU   B 1  305  ? -1.960  6.250   111.854 1.00 19.54 ? 303  LEU   B O     1 
ATOM   11220 C  CB    . LEU   B 1  305  ? 0.002   6.239   114.046 1.00 19.76 ? 303  LEU   B CB    1 
ATOM   11221 C  CG    . LEU   B 1  305  ? 1.092   7.148   113.463 1.00 19.89 ? 303  LEU   B CG    1 
ATOM   11222 C  CD1   . LEU   B 1  305  ? 2.395   6.971   114.217 1.00 25.76 ? 303  LEU   B CD1   1 
ATOM   11223 C  CD2   . LEU   B 1  305  ? 1.299   6.860   111.992 1.00 24.53 ? 303  LEU   B CD2   1 
ATOM   11224 N  N     . ASN   B 1  306  ? -2.220  8.416   112.443 1.00 18.13 ? 304  ASN   B N     1 
ATOM   11225 C  CA    . ASN   B 1  306  ? -2.844  8.840   111.204 1.00 17.96 ? 304  ASN   B CA    1 
ATOM   11226 C  C     . ASN   B 1  306  ? -1.869  9.647   110.363 1.00 18.24 ? 304  ASN   B C     1 
ATOM   11227 O  O     . ASN   B 1  306  ? -1.190  10.545  110.870 1.00 18.67 ? 304  ASN   B O     1 
ATOM   11228 C  CB    . ASN   B 1  306  ? -4.058  9.715   111.497 1.00 20.44 ? 304  ASN   B CB    1 
ATOM   11229 C  CG    . ASN   B 1  306  ? -4.636  10.295  110.247 1.00 21.41 ? 304  ASN   B CG    1 
ATOM   11230 O  OD1   . ASN   B 1  306  ? -5.360  9.617   109.524 1.00 22.62 ? 304  ASN   B OD1   1 
ATOM   11231 N  ND2   . ASN   B 1  306  ? -4.284  11.541  109.945 1.00 19.91 ? 304  ASN   B ND2   1 
ATOM   11232 N  N     . ILE   B 1  307  ? -1.818  9.337   109.074 1.00 18.55 ? 305  ILE   B N     1 
ATOM   11233 C  CA    . ILE   B 1  307  ? -1.020  10.089  108.117 1.00 18.37 ? 305  ILE   B CA    1 
ATOM   11234 C  C     . ILE   B 1  307  ? -1.930  11.124  107.473 1.00 18.71 ? 305  ILE   B C     1 
ATOM   11235 O  O     . ILE   B 1  307  ? -2.838  10.781  106.705 1.00 17.55 ? 305  ILE   B O     1 
ATOM   11236 C  CB    . ILE   B 1  307  ? -0.393  9.177   107.057 1.00 18.50 ? 305  ILE   B CB    1 
ATOM   11237 C  CG1   . ILE   B 1  307  ? 0.583   8.192   107.707 1.00 20.20 ? 305  ILE   B CG1   1 
ATOM   11238 C  CG2   . ILE   B 1  307  ? 0.286   10.010  105.963 1.00 19.42 ? 305  ILE   B CG2   1 
ATOM   11239 C  CD1   . ILE   B 1  307  ? 1.119   7.187   106.708 1.00 23.36 ? 305  ILE   B CD1   1 
ATOM   11240 N  N     . ASP   B 1  308  ? -1.689  12.391  107.789 1.00 18.54 ? 306  ASP   B N     1 
ATOM   11241 C  CA    . ASP   B 1  308  ? -2.456  13.472  107.195 1.00 18.25 ? 306  ASP   B CA    1 
ATOM   11242 C  C     . ASP   B 1  308  ? -2.156  13.555  105.707 1.00 17.58 ? 306  ASP   B C     1 
ATOM   11243 O  O     . ASP   B 1  308  ? -1.075  13.184  105.244 1.00 19.67 ? 306  ASP   B O     1 
ATOM   11244 C  CB    . ASP   B 1  308  ? -2.080  14.809  107.846 1.00 18.11 ? 306  ASP   B CB    1 
ATOM   11245 C  CG    . ASP   B 1  308  ? -2.599  14.946  109.269 1.00 21.77 ? 306  ASP   B CG    1 
ATOM   11246 O  OD1   . ASP   B 1  308  ? -3.416  14.112  109.697 1.00 19.74 ? 306  ASP   B OD1   1 
ATOM   11247 O  OD2   . ASP   B 1  308  ? -2.179  15.897  109.967 1.00 22.26 ? 306  ASP   B OD2   1 
ATOM   11248 N  N     . ALA   B 1  309  ? -3.122  14.059  104.957 1.00 15.78 ? 307  ALA   B N     1 
ATOM   11249 C  CA    . ALA   B 1  309  ? -2.967  14.202  103.519 1.00 15.32 ? 307  ALA   B CA    1 
ATOM   11250 C  C     . ALA   B 1  309  ? -2.554  15.627  103.186 1.00 16.72 ? 307  ALA   B C     1 
ATOM   11251 O  O     . ALA   B 1  309  ? -3.059  16.588  103.773 1.00 18.09 ? 307  ALA   B O     1 
ATOM   11252 C  CB    . ALA   B 1  309  ? -4.278  13.869  102.810 1.00 17.39 ? 307  ALA   B CB    1 
ATOM   11253 N  N     . GLU   B 1  310  ? -1.616  15.758  102.252 1.00 16.04 ? 308  GLU   B N     1 
ATOM   11254 C  CA    . GLU   B 1  310  ? -1.043  17.064  101.965 1.00 17.26 ? 308  GLU   B CA    1 
ATOM   11255 C  C     . GLU   B 1  310  ? -1.327  17.444  100.518 1.00 15.16 ? 308  GLU   B C     1 
ATOM   11256 O  O     . GLU   B 1  310  ? -2.458  17.277  100.054 1.00 15.75 ? 308  GLU   B O     1 
ATOM   11257 C  CB    . GLU   B 1  310  ? 0.439   17.077  102.342 1.00 16.48 ? 308  GLU   B CB    1 
ATOM   11258 C  CG    . GLU   B 1  310  ? 0.620   16.744  103.819 1.00 19.49 ? 308  GLU   B CG    1 
ATOM   11259 C  CD    . GLU   B 1  310  ? 2.064   16.828  104.269 1.00 20.36 ? 308  GLU   B CD    1 
ATOM   11260 O  OE1   . GLU   B 1  310  ? 2.560   17.961  104.389 1.00 21.80 ? 308  GLU   B OE1   1 
ATOM   11261 O  OE2   . GLU   B 1  310  ? 2.685   15.772  104.500 1.00 19.41 ? 308  GLU   B OE2   1 
ATOM   11262 N  N     . GLU   B 1  311  ? -0.334  17.948  99.796  1.00 15.64 ? 309  GLU   B N     1 
ATOM   11263 C  CA    . GLU   B 1  311  ? -0.581  18.418  98.445  1.00 14.88 ? 309  GLU   B CA    1 
ATOM   11264 C  C     . GLU   B 1  311  ? -0.885  17.255  97.511  1.00 15.77 ? 309  GLU   B C     1 
ATOM   11265 O  O     . GLU   B 1  311  ? -0.537  16.100  97.772  1.00 16.65 ? 309  GLU   B O     1 
ATOM   11266 C  CB    . GLU   B 1  311  ? 0.637   19.164  97.914  1.00 16.61 ? 309  GLU   B CB    1 
ATOM   11267 C  CG    . GLU   B 1  311  ? 0.954   20.465  98.657  1.00 19.37 ? 309  GLU   B CG    1 
ATOM   11268 C  CD    . GLU   B 1  311  ? 1.836   20.288  99.890  1.00 22.14 ? 309  GLU   B CD    1 
ATOM   11269 O  OE1   . GLU   B 1  311  ? 2.060   19.144  100.358 1.00 19.02 ? 309  GLU   B OE1   1 
ATOM   11270 O  OE2   . GLU   B 1  311  ? 2.312   21.330  100.404 1.00 27.95 ? 309  GLU   B OE2   1 
ATOM   11271 N  N     . ALA   B 1  312  ? -1.561  17.579  96.403  1.00 15.72 ? 310  ALA   B N     1 
ATOM   11272 C  CA    . ALA   B 1  312  ? -1.993  16.536  95.485  1.00 16.41 ? 310  ALA   B CA    1 
ATOM   11273 C  C     . ALA   B 1  312  ? -0.818  15.750  94.925  1.00 15.61 ? 310  ALA   B C     1 
ATOM   11274 O  O     . ALA   B 1  312  ? -0.955  14.552  94.679  1.00 15.80 ? 310  ALA   B O     1 
ATOM   11275 C  CB    . ALA   B 1  312  ? -2.806  17.138  94.336  1.00 17.88 ? 310  ALA   B CB    1 
ATOM   11276 N  N     . ASP   B 1  313  ? 0.342   16.389  94.744  1.00 15.86 ? 311  ASP   B N     1 
ATOM   11277 C  CA    . ASP   B 1  313  ? 1.484   15.670  94.182  1.00 15.79 ? 311  ASP   B CA    1 
ATOM   11278 C  C     . ASP   B 1  313  ? 2.190   14.777  95.186  1.00 17.75 ? 311  ASP   B C     1 
ATOM   11279 O  O     . ASP   B 1  313  ? 3.190   14.147  94.835  1.00 18.12 ? 311  ASP   B O     1 
ATOM   11280 C  CB    . ASP   B 1  313  ? 2.472   16.601  93.461  1.00 18.67 ? 311  ASP   B CB    1 
ATOM   11281 C  CG    . ASP   B 1  313  ? 3.137   17.610  94.377  1.00 20.01 ? 311  ASP   B CG    1 
ATOM   11282 O  OD1   . ASP   B 1  313  ? 2.920   17.583  95.610  1.00 19.90 ? 311  ASP   B OD1   1 
ATOM   11283 O  OD2   . ASP   B 1  313  ? 3.916   18.443  93.848  1.00 22.22 ? 311  ASP   B OD2   1 
ATOM   11284 N  N     . ARG   B 1  314  ? 1.679   14.693  96.409  1.00 15.77 ? 312  ARG   B N     1 
ATOM   11285 C  CA    . ARG   B 1  314  ? 2.202   13.774  97.404  1.00 16.30 ? 312  ARG   B CA    1 
ATOM   11286 C  C     . ARG   B 1  314  ? 1.269   12.609  97.678  1.00 15.73 ? 312  ARG   B C     1 
ATOM   11287 O  O     . ARG   B 1  314  ? 1.656   11.686  98.398  1.00 17.22 ? 312  ARG   B O     1 
ATOM   11288 C  CB    . ARG   B 1  314  ? 2.487   14.522  98.712  1.00 17.06 ? 312  ARG   B CB    1 
ATOM   11289 C  CG    . ARG   B 1  314  ? 3.760   15.338  98.604  1.00 16.31 ? 312  ARG   B CG    1 
ATOM   11290 C  CD    . ARG   B 1  314  ? 3.850   16.408  99.677  1.00 19.54 ? 312  ARG   B CD    1 
ATOM   11291 N  NE    . ARG   B 1  314  ? 5.218   16.893  99.809  1.00 17.42 ? 312  ARG   B NE    1 
ATOM   11292 C  CZ    . ARG   B 1  314  ? 5.574   17.935  100.547 1.00 17.33 ? 312  ARG   B CZ    1 
ATOM   11293 N  NH1   . ARG   B 1  314  ? 4.675   18.695  101.155 1.00 18.71 ? 312  ARG   B NH1   1 
ATOM   11294 N  NH2   . ARG   B 1  314  ? 6.869   18.212  100.693 1.00 19.37 ? 312  ARG   B NH2   1 
ATOM   11295 N  N     . LEU   B 1  315  ? 0.063   12.624  97.104  1.00 15.74 ? 313  LEU   B N     1 
ATOM   11296 C  CA    . LEU   B 1  315  ? -0.928  11.596  97.399  1.00 16.87 ? 313  LEU   B CA    1 
ATOM   11297 C  C     . LEU   B 1  315  ? -0.392  10.207  97.067  1.00 17.44 ? 313  LEU   B C     1 
ATOM   11298 O  O     . LEU   B 1  315  ? -0.314  9.327   97.933  1.00 17.55 ? 313  LEU   B O     1 
ATOM   11299 C  CB    . LEU   B 1  315  ? -2.204  11.892  96.614  1.00 16.53 ? 313  LEU   B CB    1 
ATOM   11300 C  CG    . LEU   B 1  315  ? -3.500  11.247  97.123  1.00 18.62 ? 313  LEU   B CG    1 
ATOM   11301 C  CD1   . LEU   B 1  315  ? -4.659  11.739  96.275  1.00 18.82 ? 313  LEU   B CD1   1 
ATOM   11302 C  CD2   . LEU   B 1  315  ? -3.481  9.724   97.091  1.00 22.29 ? 313  LEU   B CD2   1 
ATOM   11303 N  N     . GLU   B 1  316  ? -0.038  9.983   95.804  1.00 17.12 ? 314  GLU   B N     1 
ATOM   11304 C  CA    . GLU   B 1  316  ? 0.315   8.628   95.403  1.00 18.03 ? 314  GLU   B CA    1 
ATOM   11305 C  C     . GLU   B 1  316  ? 1.624   8.177   96.031  1.00 17.68 ? 314  GLU   B C     1 
ATOM   11306 O  O     . GLU   B 1  316  ? 1.753   7.004   96.403  1.00 18.82 ? 314  GLU   B O     1 
ATOM   11307 C  CB    . GLU   B 1  316  ? 0.344   8.529   93.882  1.00 17.65 ? 314  GLU   B CB    1 
ATOM   11308 C  CG    . GLU   B 1  316  ? -1.056  8.745   93.314  1.00 18.58 ? 314  GLU   B CG    1 
ATOM   11309 C  CD    . GLU   B 1  316  ? -1.144  8.615   91.804  1.00 21.48 ? 314  GLU   B CD    1 
ATOM   11310 O  OE1   . GLU   B 1  316  ? -0.495  7.719   91.225  1.00 20.03 ? 314  GLU   B OE1   1 
ATOM   11311 O  OE2   . GLU   B 1  316  ? -1.889  9.407   91.206  1.00 20.46 ? 314  GLU   B OE2   1 
ATOM   11312 N  N     . LEU   B 1  317  ? 2.581   9.095   96.193  1.00 18.29 ? 315  LEU   B N     1 
ATOM   11313 C  CA    . LEU   B 1  317  ? 3.797   8.768   96.933  1.00 20.14 ? 315  LEU   B CA    1 
ATOM   11314 C  C     . LEU   B 1  317  ? 3.468   8.241   98.322  1.00 20.65 ? 315  LEU   B C     1 
ATOM   11315 O  O     . LEU   B 1  317  ? 4.023   7.228   98.753  1.00 19.89 ? 315  LEU   B O     1 
ATOM   11316 C  CB    . LEU   B 1  317  ? 4.690   9.999   97.031  1.00 21.01 ? 315  LEU   B CB    1 
ATOM   11317 C  CG    . LEU   B 1  317  ? 6.002   9.735   97.756  1.00 21.26 ? 315  LEU   B CG    1 
ATOM   11318 C  CD1   . LEU   B 1  317  ? 6.750   8.552   97.142  1.00 23.80 ? 315  LEU   B CD1   1 
ATOM   11319 C  CD2   . LEU   B 1  317  ? 6.859   10.980  97.723  1.00 21.97 ? 315  LEU   B CD2   1 
ATOM   11320 N  N     . SER   B 1  318  ? 2.536   8.890   99.025  1.00 16.82 ? 316  SER   B N     1 
ATOM   11321 C  CA    . SER   B 1  318  ? 2.198   8.428   100.368 1.00 16.92 ? 316  SER   B CA    1 
ATOM   11322 C  C     . SER   B 1  318  ? 1.628   7.011   100.361 1.00 17.80 ? 316  SER   B C     1 
ATOM   11323 O  O     . SER   B 1  318  ? 1.815   6.271   101.334 1.00 19.21 ? 316  SER   B O     1 
ATOM   11324 C  CB    . SER   B 1  318  ? 1.219   9.391   101.043 1.00 18.35 ? 316  SER   B CB    1 
ATOM   11325 O  OG    . SER   B 1  318  ? -0.075  9.287   100.480 1.00 18.74 ? 316  SER   B OG    1 
ATOM   11326 N  N     . LEU   B 1  319  ? 0.961   6.607   99.273  1.00 17.44 ? 317  LEU   B N     1 
ATOM   11327 C  CA    . LEU   B 1  319  ? 0.406   5.260   99.209  1.00 17.24 ? 317  LEU   B CA    1 
ATOM   11328 C  C     . LEU   B 1  319  ? 1.496   4.203   99.201  1.00 19.35 ? 317  LEU   B C     1 
ATOM   11329 O  O     . LEU   B 1  319  ? 1.276   3.081   99.673  1.00 19.93 ? 317  LEU   B O     1 
ATOM   11330 C  CB    . LEU   B 1  319  ? -0.461  5.100   97.961  1.00 17.16 ? 317  LEU   B CB    1 
ATOM   11331 C  CG    . LEU   B 1  319  ? -1.686  6.005   97.865  1.00 19.65 ? 317  LEU   B CG    1 
ATOM   11332 C  CD1   . LEU   B 1  319  ? -2.311  5.845   96.473  1.00 19.99 ? 317  LEU   B CD1   1 
ATOM   11333 C  CD2   . LEU   B 1  319  ? -2.698  5.702   98.957  1.00 22.15 ? 317  LEU   B CD2   1 
ATOM   11334 N  N     . ASP   B 1  320  ? 2.666   4.526   98.653  1.00 19.31 ? 318  ASP   B N     1 
ATOM   11335 C  CA    . ASP   B 1  320  ? 3.755   3.562   98.686  1.00 21.18 ? 318  ASP   B CA    1 
ATOM   11336 C  C     . ASP   B 1  320  ? 4.240   3.315   100.100 1.00 20.30 ? 318  ASP   B C     1 
ATOM   11337 O  O     . ASP   B 1  320  ? 4.684   2.208   100.409 1.00 23.02 ? 318  ASP   B O     1 
ATOM   11338 C  CB    . ASP   B 1  320  ? 4.894   4.023   97.797  1.00 21.96 ? 318  ASP   B CB    1 
ATOM   11339 C  CG    . ASP   B 1  320  ? 4.579   3.828   96.339  1.00 19.46 ? 318  ASP   B CG    1 
ATOM   11340 O  OD1   . ASP   B 1  320  ? 4.239   2.685   95.958  1.00 23.64 ? 318  ASP   B OD1   1 
ATOM   11341 O  OD2   . ASP   B 1  320  ? 4.645   4.814   95.583  1.00 22.82 ? 318  ASP   B OD2   1 
ATOM   11342 N  N     . LEU   B 1  321  ? 4.174   4.325   100.969 1.00 17.46 ? 319  LEU   B N     1 
ATOM   11343 C  CA    . LEU   B 1  321  ? 4.497   4.096   102.371 1.00 20.54 ? 319  LEU   B CA    1 
ATOM   11344 C  C     . LEU   B 1  321  ? 3.390   3.321   103.061 1.00 19.84 ? 319  LEU   B C     1 
ATOM   11345 O  O     . LEU   B 1  321  ? 3.657   2.386   103.826 1.00 22.02 ? 319  LEU   B O     1 
ATOM   11346 C  CB    . LEU   B 1  321  ? 4.746   5.422   103.086 1.00 20.39 ? 319  LEU   B CB    1 
ATOM   11347 C  CG    . LEU   B 1  321  ? 6.096   6.059   102.758 1.00 20.40 ? 319  LEU   B CG    1 
ATOM   11348 C  CD1   . LEU   B 1  321  ? 6.003   6.910   101.513 1.00 23.57 ? 319  LEU   B CD1   1 
ATOM   11349 C  CD2   . LEU   B 1  321  ? 6.592   6.878   103.941 1.00 25.03 ? 319  LEU   B CD2   1 
ATOM   11350 N  N     . LEU   B 1  322  ? 2.139   3.684   102.788 1.00 19.31 ? 320  LEU   B N     1 
ATOM   11351 C  CA    . LEU   B 1  322  ? 1.029   2.975   103.406 1.00 19.15 ? 320  LEU   B CA    1 
ATOM   11352 C  C     . LEU   B 1  322  ? 1.086   1.497   103.072 1.00 19.21 ? 320  LEU   B C     1 
ATOM   11353 O  O     . LEU   B 1  322  ? 0.850   0.648   103.940 1.00 20.63 ? 320  LEU   B O     1 
ATOM   11354 C  CB    . LEU   B 1  322  ? -0.285  3.564   102.910 1.00 18.76 ? 320  LEU   B CB    1 
ATOM   11355 C  CG    . LEU   B 1  322  ? -1.516  2.876   103.510 1.00 20.04 ? 320  LEU   B CG    1 
ATOM   11356 C  CD1   . LEU   B 1  322  ? -1.559  3.116   105.018 1.00 20.48 ? 320  LEU   B CD1   1 
ATOM   11357 C  CD2   . LEU   B 1  322  ? -2.792  3.364   102.831 1.00 21.56 ? 320  LEU   B CD2   1 
ATOM   11358 N  N     . GLU   B 1  323  ? 1.409   1.177   101.815 1.00 19.93 ? 321  GLU   B N     1 
ATOM   11359 C  CA    . GLU   B 1  323  ? 1.497   -0.215  101.392 1.00 21.90 ? 321  GLU   B CA    1 
ATOM   11360 C  C     . GLU   B 1  323  ? 2.520   -0.974  102.224 1.00 23.94 ? 321  GLU   B C     1 
ATOM   11361 O  O     . GLU   B 1  323  ? 2.227   -2.053  102.746 1.00 23.54 ? 321  GLU   B O     1 
ATOM   11362 C  CB    . GLU   B 1  323  ? 1.865   -0.277  99.911  1.00 25.61 ? 321  GLU   B CB    1 
ATOM   11363 C  CG    . GLU   B 1  323  ? 2.220   -1.674  99.415  1.00 29.03 ? 321  GLU   B CG    1 
ATOM   11364 C  CD    . GLU   B 1  323  ? 1.051   -2.383  98.750  1.00 31.80 ? 321  GLU   B CD    1 
ATOM   11365 O  OE1   . GLU   B 1  323  ? 0.035   -1.719  98.467  1.00 28.90 ? 321  GLU   B OE1   1 
ATOM   11366 O  OE2   . GLU   B 1  323  ? 1.146   -3.605  98.516  1.00 28.84 ? 321  GLU   B OE2   1 
ATOM   11367 N  N     . VAL   B 1  324  ? 3.725   -0.411  102.373 1.00 20.67 ? 322  VAL   B N     1 
ATOM   11368 C  CA    . VAL   B 1  324  ? 4.775   -1.099  103.121 1.00 22.35 ? 322  VAL   B CA    1 
ATOM   11369 C  C     . VAL   B 1  324  ? 4.363   -1.287  104.574 1.00 19.51 ? 322  VAL   B C     1 
ATOM   11370 O  O     . VAL   B 1  324  ? 4.560   -2.361  105.160 1.00 22.46 ? 322  VAL   B O     1 
ATOM   11371 C  CB    . VAL   B 1  324  ? 6.113   -0.338  102.998 1.00 21.98 ? 322  VAL   B CB    1 
ATOM   11372 C  CG1   . VAL   B 1  324  ? 7.182   -0.967  103.897 1.00 25.65 ? 322  VAL   B CG1   1 
ATOM   11373 C  CG2   . VAL   B 1  324  ? 6.579   -0.296  101.555 1.00 25.67 ? 322  VAL   B CG2   1 
ATOM   11374 N  N     . LEU   B 1  325  ? 3.791   -0.249  105.182 1.00 19.35 ? 323  LEU   B N     1 
ATOM   11375 C  CA    . LEU   B 1  325  ? 3.419   -0.348  106.588 1.00 21.87 ? 323  LEU   B CA    1 
ATOM   11376 C  C     . LEU   B 1  325  ? 2.361   -1.421  106.814 1.00 22.29 ? 323  LEU   B C     1 
ATOM   11377 O  O     . LEU   B 1  325  ? 2.423   -2.163  107.799 1.00 21.68 ? 323  LEU   B O     1 
ATOM   11378 C  CB    . LEU   B 1  325  ? 2.941   1.008   107.092 1.00 21.24 ? 323  LEU   B CB    1 
ATOM   11379 C  CG    . LEU   B 1  325  ? 4.040   2.065   107.065 1.00 21.10 ? 323  LEU   B CG    1 
ATOM   11380 C  CD1   . LEU   B 1  325  ? 3.443   3.439   107.254 1.00 25.53 ? 323  LEU   B CD1   1 
ATOM   11381 C  CD2   . LEU   B 1  325  ? 5.073   1.775   108.142 1.00 23.45 ? 323  LEU   B CD2   1 
ATOM   11382 N  N     . CYS   B 1  326  ? 1.380   -1.524  105.911 1.00 21.18 ? 324  CYS   B N     1 
ATOM   11383 C  CA    . CYS   B 1  326  ? 0.316   -2.503  106.088 1.00 20.12 ? 324  CYS   B CA    1 
ATOM   11384 C  C     . CYS   B 1  326  ? 0.799   -3.932  105.887 1.00 22.52 ? 324  CYS   B C     1 
ATOM   11385 O  O     . CYS   B 1  326  ? 0.163   -4.861  106.394 1.00 21.95 ? 324  CYS   B O     1 
ATOM   11386 C  CB    . CYS   B 1  326  ? -0.847  -2.208  105.140 1.00 21.80 ? 324  CYS   B CB    1 
ATOM   11387 S  SG    . CYS   B 1  326  ? -1.752  -0.728  105.595 1.00 24.41 ? 324  CYS   B SG    1 
ATOM   11388 N  N     . LEU   B 1  327  ? 1.909   -4.123  105.171 1.00 21.55 ? 325  LEU   B N     1 
ATOM   11389 C  CA    . LEU   B 1  327  ? 2.486   -5.441  104.940 1.00 24.68 ? 325  LEU   B CA    1 
ATOM   11390 C  C     . LEU   B 1  327  ? 3.624   -5.762  105.895 1.00 26.84 ? 325  LEU   B C     1 
ATOM   11391 O  O     . LEU   B 1  327  ? 4.203   -6.849  105.810 1.00 27.66 ? 325  LEU   B O     1 
ATOM   11392 C  CB    . LEU   B 1  327  ? 2.979   -5.552  103.492 1.00 22.81 ? 325  LEU   B CB    1 
ATOM   11393 C  CG    . LEU   B 1  327  ? 1.889   -5.421  102.429 1.00 28.70 ? 325  LEU   B CG    1 
ATOM   11394 C  CD1   . LEU   B 1  327  ? 2.492   -5.463  101.036 1.00 33.55 ? 325  LEU   B CD1   1 
ATOM   11395 C  CD2   . LEU   B 1  327  ? 0.876   -6.513  102.601 1.00 30.21 ? 325  LEU   B CD2   1 
ATOM   11396 N  N     . ASP   B 1  328  ? 3.951   -4.850  106.805 1.00 21.38 ? 326  ASP   B N     1 
ATOM   11397 C  CA    . ASP   B 1  328  ? 5.069   -5.037  107.724 1.00 23.34 ? 326  ASP   B CA    1 
ATOM   11398 C  C     . ASP   B 1  328  ? 4.605   -5.877  108.908 1.00 25.42 ? 326  ASP   B C     1 
ATOM   11399 O  O     . ASP   B 1  328  ? 3.797   -5.423  109.727 1.00 26.79 ? 326  ASP   B O     1 
ATOM   11400 C  CB    . ASP   B 1  328  ? 5.551   -3.665  108.184 1.00 23.50 ? 326  ASP   B CB    1 
ATOM   11401 C  CG    . ASP   B 1  328  ? 6.809   -3.734  109.040 1.00 31.14 ? 326  ASP   B CG    1 
ATOM   11402 O  OD1   . ASP   B 1  328  ? 7.087   -4.792  109.646 1.00 29.31 ? 326  ASP   B OD1   1 
ATOM   11403 O  OD2   . ASP   B 1  328  ? 7.515   -2.709  109.114 1.00 32.15 ? 326  ASP   B OD2   1 
ATOM   11404 N  N     . GLY   B 1  329  ? 5.135   -7.097  109.020 1.00 26.47 ? 327  GLY   B N     1 
ATOM   11405 C  CA    . GLY   B 1  329  ? 4.726   -7.991  110.091 1.00 25.34 ? 327  GLY   B CA    1 
ATOM   11406 C  C     . GLY   B 1  329  ? 5.024   -7.482  111.488 1.00 26.34 ? 327  GLY   B C     1 
ATOM   11407 O  O     . GLY   B 1  329  ? 4.412   -7.953  112.451 1.00 27.71 ? 327  GLY   B O     1 
ATOM   11408 N  N     . ASP   B 1  330  ? 5.950   -6.528  111.628 1.00 25.89 ? 328  ASP   B N     1 
ATOM   11409 C  CA    . ASP   B 1  330  ? 6.172   -5.919  112.937 1.00 23.92 ? 328  ASP   B CA    1 
ATOM   11410 C  C     . ASP   B 1  330  ? 4.935   -5.196  113.445 1.00 30.57 ? 328  ASP   B C     1 
ATOM   11411 O  O     . ASP   B 1  330  ? 4.809   -4.979  114.654 1.00 30.90 ? 328  ASP   B O     1 
ATOM   11412 C  CB    . ASP   B 1  330  ? 7.362   -4.949  112.900 1.00 27.57 ? 328  ASP   B CB    1 
ATOM   11413 C  CG    . ASP   B 1  330  ? 8.698   -5.658  112.727 1.00 34.11 ? 328  ASP   B CG    1 
ATOM   11414 O  OD1   . ASP   B 1  330  ? 8.795   -6.855  113.074 1.00 34.94 ? 328  ASP   B OD1   1 
ATOM   11415 O  OD2   . ASP   B 1  330  ? 9.657   -5.015  112.249 1.00 33.05 ? 328  ASP   B OD2   1 
ATOM   11416 N  N     . LEU   B 1  331  ? 4.020   -4.816  112.551 1.00 23.96 ? 329  LEU   B N     1 
ATOM   11417 C  CA    . LEU   B 1  331  ? 2.789   -4.141  112.927 1.00 23.41 ? 329  LEU   B CA    1 
ATOM   11418 C  C     . LEU   B 1  331  ? 1.604   -5.089  112.937 1.00 21.18 ? 329  LEU   B C     1 
ATOM   11419 O  O     . LEU   B 1  331  ? 0.455   -4.639  112.891 1.00 25.82 ? 329  LEU   B O     1 
ATOM   11420 C  CB    . LEU   B 1  331  ? 2.529   -2.954  112.000 1.00 23.44 ? 329  LEU   B CB    1 
ATOM   11421 C  CG    . LEU   B 1  331  ? 3.690   -1.962  111.943 1.00 23.95 ? 329  LEU   B CG    1 
ATOM   11422 C  CD1   . LEU   B 1  331  ? 3.448   -0.870  110.911 1.00 24.65 ? 329  LEU   B CD1   1 
ATOM   11423 C  CD2   . LEU   B 1  331  ? 3.925   -1.371  113.329 1.00 22.42 ? 329  LEU   B CD2   1 
ATOM   11424 N  N     . SER   B 1  332  ? 1.872   -6.390  113.008 1.00 26.24 ? 330  SER   B N     1 
ATOM   11425 C  CA    . SER   B 1  332  ? 0.842   -7.419  112.910 1.00 25.81 ? 330  SER   B CA    1 
ATOM   11426 C  C     . SER   B 1  332  ? -0.337  -7.147  113.841 1.00 26.13 ? 330  SER   B C     1 
ATOM   11427 O  O     . SER   B 1  332  ? -0.160  -6.879  115.034 1.00 28.33 ? 330  SER   B O     1 
ATOM   11428 C  CB    . SER   B 1  332  ? 1.465   -8.767  113.268 1.00 29.67 ? 330  SER   B CB    1 
ATOM   11429 O  OG    . SER   B 1  332  ? 0.510   -9.804  113.139 1.00 34.66 ? 330  SER   B OG    1 
ATOM   11430 N  N     . GLY   B 1  333  ? -1.547  -7.215  113.281 1.00 26.06 ? 331  GLY   B N     1 
ATOM   11431 C  CA    . GLY   B 1  333  ? -2.771  -7.112  114.050 1.00 26.80 ? 331  GLY   B CA    1 
ATOM   11432 C  C     . GLY   B 1  333  ? -3.130  -5.725  114.541 1.00 25.77 ? 331  GLY   B C     1 
ATOM   11433 O  O     . GLY   B 1  333  ? -4.147  -5.576  115.229 1.00 27.89 ? 331  GLY   B O     1 
ATOM   11434 N  N     . TRP   B 1  334  ? -2.334  -4.712  114.224 1.00 26.26 ? 332  TRP   B N     1 
ATOM   11435 C  CA    . TRP   B 1  334  ? -2.612  -3.351  114.662 1.00 23.57 ? 332  TRP   B CA    1 
ATOM   11436 C  C     . TRP   B 1  334  ? -3.578  -2.702  113.685 1.00 23.01 ? 332  TRP   B C     1 
ATOM   11437 O  O     . TRP   B 1  334  ? -3.288  -2.598  112.488 1.00 24.53 ? 332  TRP   B O     1 
ATOM   11438 C  CB    . TRP   B 1  334  ? -1.304  -2.573  114.724 1.00 26.45 ? 332  TRP   B CB    1 
ATOM   11439 C  CG    . TRP   B 1  334  ? -1.422  -1.117  115.060 1.00 25.15 ? 332  TRP   B CG    1 
ATOM   11440 C  CD1   . TRP   B 1  334  ? -2.007  -0.565  116.163 1.00 26.33 ? 332  TRP   B CD1   1 
ATOM   11441 C  CD2   . TRP   B 1  334  ? -0.880  -0.034  114.306 1.00 22.73 ? 332  TRP   B CD2   1 
ATOM   11442 N  NE1   . TRP   B 1  334  ? -1.878  0.806   116.130 1.00 21.47 ? 332  TRP   B NE1   1 
ATOM   11443 C  CE2   . TRP   B 1  334  ? -1.190  1.157   114.998 1.00 21.10 ? 332  TRP   B CE2   1 
ATOM   11444 C  CE3   . TRP   B 1  334  ? -0.180  0.050   113.100 1.00 21.56 ? 332  TRP   B CE3   1 
ATOM   11445 C  CZ2   . TRP   B 1  334  ? -0.815  2.412   114.524 1.00 21.41 ? 332  TRP   B CZ2   1 
ATOM   11446 C  CZ3   . TRP   B 1  334  ? 0.197   1.295   112.635 1.00 26.69 ? 332  TRP   B CZ3   1 
ATOM   11447 C  CH2   . TRP   B 1  334  ? -0.124  2.461   113.346 1.00 23.08 ? 332  TRP   B CH2   1 
ATOM   11448 N  N     . ASN   B 1  335  ? -4.732  -2.284  114.186 1.00 22.58 ? 333  ASN   B N     1 
ATOM   11449 C  CA    . ASN   B 1  335  ? -5.747  -1.656  113.358 1.00 21.96 ? 333  ASN   B CA    1 
ATOM   11450 C  C     . ASN   B 1  335  ? -5.723  -0.142  113.476 1.00 20.90 ? 333  ASN   B C     1 
ATOM   11451 O  O     . ASN   B 1  335  ? -6.663  0.525   113.035 1.00 24.59 ? 333  ASN   B O     1 
ATOM   11452 C  CB    . ASN   B 1  335  ? -7.123  -2.215  113.700 1.00 22.80 ? 333  ASN   B CB    1 
ATOM   11453 C  CG    . ASN   B 1  335  ? -7.269  -3.661  113.282 1.00 29.16 ? 333  ASN   B CG    1 
ATOM   11454 O  OD1   . ASN   B 1  335  ? -6.620  -4.101  112.328 1.00 24.66 ? 333  ASN   B OD1   1 
ATOM   11455 N  ND2   . ASN   B 1  335  ? -8.115  -4.407  113.985 1.00 29.04 ? 333  ASN   B ND2   1 
ATOM   11456 N  N     . GLY   B 1  336  ? -4.653  0.409   114.032 1.00 22.53 ? 334  GLY   B N     1 
ATOM   11457 C  CA    . GLY   B 1  336  ? -4.564  1.832   114.237 1.00 23.73 ? 334  GLY   B CA    1 
ATOM   11458 C  C     . GLY   B 1  336  ? -3.886  2.620   113.150 1.00 20.64 ? 334  GLY   B C     1 
ATOM   11459 O  O     . GLY   B 1  336  ? -3.715  3.829   113.312 1.00 20.28 ? 334  GLY   B O     1 
ATOM   11460 N  N     . MET   B 1  337  ? -3.503  2.006   112.031 1.00 21.92 ? 335  MET   B N     1 
ATOM   11461 C  CA    . MET   B 1  337  ? -2.929  2.789   110.947 1.00 21.45 ? 335  MET   B CA    1 
ATOM   11462 C  C     . MET   B 1  337  ? -4.028  3.638   110.330 1.00 21.20 ? 335  MET   B C     1 
ATOM   11463 O  O     . MET   B 1  337  ? -5.050  3.106   109.884 1.00 19.95 ? 335  MET   B O     1 
ATOM   11464 C  CB    . MET   B 1  337  ? -2.331  1.875   109.884 1.00 23.54 ? 335  MET   B CB    1 
ATOM   11465 C  CG    . MET   B 1  337  ? -1.708  2.621   108.715 1.00 23.87 ? 335  MET   B CG    1 
ATOM   11466 S  SD    . MET   B 1  337  ? -0.080  3.265   109.152 1.00 34.71 ? 335  MET   B SD    1 
ATOM   11467 C  CE    . MET   B 1  337  ? -0.394  5.027   109.186 1.00 28.71 ? 335  MET   B CE    1 
ATOM   11468 N  N     . GLY   B 1  338  ? -3.812  4.948   110.298 1.00 18.14 ? 336  GLY   B N     1 
ATOM   11469 C  CA    . GLY   B 1  338  ? -4.783  5.892   109.792 1.00 21.89 ? 336  GLY   B CA    1 
ATOM   11470 C  C     . GLY   B 1  338  ? -4.261  6.594   108.554 1.00 18.96 ? 336  GLY   B C     1 
ATOM   11471 O  O     . GLY   B 1  338  ? -3.060  6.844   108.420 1.00 18.52 ? 336  GLY   B O     1 
ATOM   11472 N  N     . PHE   B 1  339  ? -5.171  6.917   107.642 1.00 19.18 ? 337  PHE   B N     1 
ATOM   11473 C  CA    . PHE   B 1  339  ? -4.764  7.534   106.394 1.00 17.09 ? 337  PHE   B CA    1 
ATOM   11474 C  C     . PHE   B 1  339  ? -5.882  8.449   105.936 1.00 17.65 ? 337  PHE   B C     1 
ATOM   11475 O  O     . PHE   B 1  339  ? -7.039  8.024   105.871 1.00 19.33 ? 337  PHE   B O     1 
ATOM   11476 C  CB    . PHE   B 1  339  ? -4.490  6.444   105.356 1.00 19.69 ? 337  PHE   B CB    1 
ATOM   11477 C  CG    . PHE   B 1  339  ? -3.792  6.934   104.131 1.00 19.86 ? 337  PHE   B CG    1 
ATOM   11478 C  CD1   . PHE   B 1  339  ? -2.414  7.054   104.098 1.00 20.88 ? 337  PHE   B CD1   1 
ATOM   11479 C  CD2   . PHE   B 1  339  ? -4.519  7.273   103.007 1.00 17.96 ? 337  PHE   B CD2   1 
ATOM   11480 C  CE1   . PHE   B 1  339  ? -1.773  7.504   102.938 1.00 20.94 ? 337  PHE   B CE1   1 
ATOM   11481 C  CE2   . PHE   B 1  339  ? -3.888  7.712   101.848 1.00 21.07 ? 337  PHE   B CE2   1 
ATOM   11482 C  CZ    . PHE   B 1  339  ? -2.521  7.834   101.820 1.00 21.58 ? 337  PHE   B CZ    1 
ATOM   11483 N  N     . VAL   B 1  340  ? -5.537  9.693   105.633 1.00 16.85 ? 338  VAL   B N     1 
ATOM   11484 C  CA    . VAL   B 1  340  ? -6.500  10.688  105.182 1.00 15.67 ? 338  VAL   B CA    1 
ATOM   11485 C  C     . VAL   B 1  340  ? -6.659  10.582  103.677 1.00 18.46 ? 338  VAL   B C     1 
ATOM   11486 O  O     . VAL   B 1  340  ? -5.677  10.429  102.946 1.00 18.32 ? 338  VAL   B O     1 
ATOM   11487 C  CB    . VAL   B 1  340  ? -6.030  12.097  105.571 1.00 18.73 ? 338  VAL   B CB    1 
ATOM   11488 C  CG1   . VAL   B 1  340  ? -7.025  13.131  105.069 1.00 19.28 ? 338  VAL   B CG1   1 
ATOM   11489 C  CG2   . VAL   B 1  340  ? -5.879  12.180  107.066 1.00 18.61 ? 338  VAL   B CG2   1 
ATOM   11490 N  N     . VAL   B 1  341  ? -7.895  10.691  103.207 1.00 18.14 ? 339  VAL   B N     1 
ATOM   11491 C  CA    . VAL   B 1  341  ? -8.189  10.854  101.792 1.00 17.78 ? 339  VAL   B CA    1 
ATOM   11492 C  C     . VAL   B 1  341  ? -9.033  12.110  101.619 1.00 16.35 ? 339  VAL   B C     1 
ATOM   11493 O  O     . VAL   B 1  341  ? -9.967  12.354  102.394 1.00 18.03 ? 339  VAL   B O     1 
ATOM   11494 C  CB    . VAL   B 1  341  ? -8.885  9.611   101.208 1.00 18.74 ? 339  VAL   B CB    1 
ATOM   11495 C  CG1   . VAL   B 1  341  ? -8.007  8.395   101.383 1.00 22.90 ? 339  VAL   B CG1   1 
ATOM   11496 C  CG2   . VAL   B 1  341  ? -10.229 9.379   101.868 1.00 25.93 ? 339  VAL   B CG2   1 
ATOM   11497 N  N     . GLN   B 1  342  ? -8.694  12.906  100.609 1.00 15.82 ? 340  GLN   B N     1 
ATOM   11498 C  CA    . GLN   B 1  342  ? -9.284  14.224  100.388 1.00 17.73 ? 340  GLN   B CA    1 
ATOM   11499 C  C     . GLN   B 1  342  ? -10.347 14.126  99.303  1.00 17.27 ? 340  GLN   B C     1 
ATOM   11500 O  O     . GLN   B 1  342  ? -10.032 13.900  98.128  1.00 17.98 ? 340  GLN   B O     1 
ATOM   11501 C  CB    . GLN   B 1  342  ? -8.211  15.232  99.989  1.00 16.04 ? 340  GLN   B CB    1 
ATOM   11502 C  CG    . GLN   B 1  342  ? -7.161  15.436  101.060 1.00 15.37 ? 340  GLN   B CG    1 
ATOM   11503 C  CD    . GLN   B 1  342  ? -5.793  15.773  100.475 1.00 16.26 ? 340  GLN   B CD    1 
ATOM   11504 O  OE1   . GLN   B 1  342  ? -5.336  15.138  99.531  1.00 17.11 ? 340  GLN   B OE1   1 
ATOM   11505 N  NE2   . GLN   B 1  342  ? -5.143  16.779  101.037 1.00 15.57 ? 340  GLN   B NE2   1 
ATOM   11506 N  N     . ALA   B 1  343  ? -11.599 14.337  99.699  1.00 16.53 ? 341  ALA   B N     1 
ATOM   11507 C  CA    . ALA   B 1  343  ? -12.711 14.235  98.769  1.00 17.43 ? 341  ALA   B CA    1 
ATOM   11508 C  C     . ALA   B 1  343  ? -12.738 15.362  97.753  1.00 17.15 ? 341  ALA   B C     1 
ATOM   11509 O  O     . ALA   B 1  343  ? -13.417 15.226  96.726  1.00 18.90 ? 341  ALA   B O     1 
ATOM   11510 C  CB    . ALA   B 1  343  ? -14.016 14.198  99.553  1.00 17.94 ? 341  ALA   B CB    1 
ATOM   11511 N  N     . TYR   B 1  344  ? -12.001 16.457  97.979  1.00 17.03 ? 342  TYR   B N     1 
ATOM   11512 C  CA    . TYR   B 1  344  ? -11.908 17.440  96.912  1.00 16.78 ? 342  TYR   B CA    1 
ATOM   11513 C  C     . TYR   B 1  344  ? -11.041 16.967  95.763  1.00 16.22 ? 342  TYR   B C     1 
ATOM   11514 O  O     . TYR   B 1  344  ? -10.983 17.647  94.738  1.00 18.43 ? 342  TYR   B O     1 
ATOM   11515 C  CB    . TYR   B 1  344  ? -11.511 18.853  97.390  1.00 17.96 ? 342  TYR   B CB    1 
ATOM   11516 C  CG    . TYR   B 1  344  ? -10.068 19.127  97.800  1.00 17.29 ? 342  TYR   B CG    1 
ATOM   11517 C  CD1   . TYR   B 1  344  ? -9.097  18.134  97.840  1.00 15.55 ? 342  TYR   B CD1   1 
ATOM   11518 C  CD2   . TYR   B 1  344  ? -9.704  20.412  98.183  1.00 16.47 ? 342  TYR   B CD2   1 
ATOM   11519 C  CE1   . TYR   B 1  344  ? -7.802  18.424  98.236  1.00 16.07 ? 342  TYR   B CE1   1 
ATOM   11520 C  CE2   . TYR   B 1  344  ? -8.435  20.711  98.584  1.00 17.50 ? 342  TYR   B CE2   1 
ATOM   11521 C  CZ    . TYR   B 1  344  ? -7.479  19.725  98.602  1.00 17.70 ? 342  TYR   B CZ    1 
ATOM   11522 O  OH    . TYR   B 1  344  ? -6.214  20.062  99.033  1.00 16.18 ? 342  TYR   B OH    1 
ATOM   11523 N  N     . GLY   B 1  345  ? -10.380 15.825  95.906  1.00 16.79 ? 343  GLY   B N     1 
ATOM   11524 C  CA    . GLY   B 1  345  ? -9.491  15.322  94.883  1.00 18.03 ? 343  GLY   B CA    1 
ATOM   11525 C  C     . GLY   B 1  345  ? -10.220 14.344  93.978  1.00 17.92 ? 343  GLY   B C     1 
ATOM   11526 O  O     . GLY   B 1  345  ? -11.025 13.533  94.437  1.00 17.65 ? 343  GLY   B O     1 
ATOM   11527 N  N     . LYS   B 1  346  ? -9.897  14.418  92.687  1.00 17.01 ? 344  LYS   B N     1 
ATOM   11528 C  CA    . LYS   B 1  346  ? -10.544 13.578  91.691  1.00 17.28 ? 344  LYS   B CA    1 
ATOM   11529 C  C     . LYS   B 1  346  ? -10.197 12.109  91.852  1.00 16.84 ? 344  LYS   B C     1 
ATOM   11530 O  O     . LYS   B 1  346  ? -10.935 11.254  91.354  1.00 18.30 ? 344  LYS   B O     1 
ATOM   11531 C  CB    . LYS   B 1  346  ? -10.156 14.060  90.298  1.00 17.03 ? 344  LYS   B CB    1 
ATOM   11532 C  CG    . LYS   B 1  346  ? -10.633 15.466  90.027  1.00 16.99 ? 344  LYS   B CG    1 
ATOM   11533 C  CD    . LYS   B 1  346  ? -10.145 15.957  88.707  1.00 17.80 ? 344  LYS   B CD    1 
ATOM   11534 C  CE    . LYS   B 1  346  ? -10.756 17.301  88.400  1.00 18.41 ? 344  LYS   B CE    1 
ATOM   11535 N  NZ    . LYS   B 1  346  ? -10.194 17.868  87.147  1.00 18.38 ? 344  LYS   B NZ    1 
ATOM   11536 N  N     . ARG   B 1  347  ? -9.083  11.800  92.501  1.00 17.18 ? 345  ARG   B N     1 
ATOM   11537 C  CA    . ARG   B 1  347  ? -8.702  10.409  92.676  1.00 18.65 ? 345  ARG   B CA    1 
ATOM   11538 C  C     . ARG   B 1  347  ? -9.354  9.753   93.882  1.00 17.41 ? 345  ARG   B C     1 
ATOM   11539 O  O     . ARG   B 1  347  ? -9.210  8.538   94.056  1.00 19.06 ? 345  ARG   B O     1 
ATOM   11540 C  CB    . ARG   B 1  347  ? -7.185  10.299  92.756  1.00 15.76 ? 345  ARG   B CB    1 
ATOM   11541 C  CG    . ARG   B 1  347  ? -6.521  10.680  91.448  1.00 16.23 ? 345  ARG   B CG    1 
ATOM   11542 C  CD    . ARG   B 1  347  ? -5.057  10.940  91.651  1.00 17.68 ? 345  ARG   B CD    1 
ATOM   11543 N  NE    . ARG   B 1  347  ? -4.822  12.189  92.362  1.00 16.51 ? 345  ARG   B NE    1 
ATOM   11544 C  CZ    . ARG   B 1  347  ? -3.641  12.547  92.838  1.00 17.40 ? 345  ARG   B CZ    1 
ATOM   11545 N  NH1   . ARG   B 1  347  ? -2.571  11.780  92.672  1.00 16.75 ? 345  ARG   B NH1   1 
ATOM   11546 N  NH2   . ARG   B 1  347  ? -3.526  13.702  93.492  1.00 16.90 ? 345  ARG   B NH2   1 
ATOM   11547 N  N     . CYS   B 1  348  ? -10.081 10.519  94.694  1.00 18.59 ? 346  CYS   B N     1 
ATOM   11548 C  CA    . CYS   B 1  348  ? -10.534 10.040  95.997  1.00 19.63 ? 346  CYS   B CA    1 
ATOM   11549 C  C     . CYS   B 1  348  ? -11.204 8.670   95.963  1.00 19.62 ? 346  CYS   B C     1 
ATOM   11550 O  O     . CYS   B 1  348  ? -10.772 7.778   96.713  1.00 20.22 ? 346  CYS   B O     1 
ATOM   11551 C  CB    . CYS   B 1  348  ? -11.395 11.106  96.671  1.00 17.96 ? 346  CYS   B CB    1 
ATOM   11552 S  SG    . CYS   B 1  348  ? -11.695 10.739  98.422  1.00 23.58 ? 346  CYS   B SG    1 
ATOM   11553 N  N     . PRO   B 1  349  ? -12.237 8.422   95.148  1.00 19.54 ? 347  PRO   B N     1 
ATOM   11554 C  CA    . PRO   B 1  349  ? -12.859 7.087   95.186  1.00 21.25 ? 347  PRO   B CA    1 
ATOM   11555 C  C     . PRO   B 1  349  ? -11.909 5.979   94.776  1.00 20.09 ? 347  PRO   B C     1 
ATOM   11556 O  O     . PRO   B 1  349  ? -11.997 4.869   95.318  1.00 19.48 ? 347  PRO   B O     1 
ATOM   11557 C  CB    . PRO   B 1  349  ? -14.052 7.209   94.230  1.00 20.91 ? 347  PRO   B CB    1 
ATOM   11558 C  CG    . PRO   B 1  349  ? -13.769 8.384   93.388  1.00 22.08 ? 347  PRO   B CG    1 
ATOM   11559 C  CD    . PRO   B 1  349  ? -12.852 9.299   94.136  1.00 21.47 ? 347  PRO   B CD    1 
ATOM   11560 N  N     . PHE   B 1  350  ? -10.990 6.259   93.848  1.00 19.13 ? 348  PHE   B N     1 
ATOM   11561 C  CA    . PHE   B 1  350  ? -10.016 5.258   93.425  1.00 18.43 ? 348  PHE   B CA    1 
ATOM   11562 C  C     . PHE   B 1  350  ? -8.974  5.006   94.498  1.00 17.56 ? 348  PHE   B C     1 
ATOM   11563 O  O     . PHE   B 1  350  ? -8.547  3.861   94.686  1.00 19.76 ? 348  PHE   B O     1 
ATOM   11564 C  CB    . PHE   B 1  350  ? -9.412  5.682   92.092  1.00 18.46 ? 348  PHE   B CB    1 
ATOM   11565 C  CG    . PHE   B 1  350  ? -10.453 6.065   91.098  1.00 19.90 ? 348  PHE   B CG    1 
ATOM   11566 C  CD1   . PHE   B 1  350  ? -11.165 5.089   90.427  1.00 21.86 ? 348  PHE   B CD1   1 
ATOM   11567 C  CD2   . PHE   B 1  350  ? -10.777 7.397   90.888  1.00 20.43 ? 348  PHE   B CD2   1 
ATOM   11568 C  CE1   . PHE   B 1  350  ? -12.171 5.438   89.533  1.00 26.70 ? 348  PHE   B CE1   1 
ATOM   11569 C  CE2   . PHE   B 1  350  ? -11.778 7.753   90.010  1.00 22.39 ? 348  PHE   B CE2   1 
ATOM   11570 C  CZ    . PHE   B 1  350  ? -12.477 6.769   89.327  1.00 22.75 ? 348  PHE   B CZ    1 
ATOM   11571 N  N     . VAL   B 1  351  ? -8.598  6.043   95.244  1.00 17.52 ? 349  VAL   B N     1 
ATOM   11572 C  CA    . VAL   B 1  351  ? -7.713  5.838   96.388  1.00 17.07 ? 349  VAL   B CA    1 
ATOM   11573 C  C     . VAL   B 1  351  ? -8.408  4.990   97.444  1.00 18.68 ? 349  VAL   B C     1 
ATOM   11574 O  O     . VAL   B 1  351  ? -7.815  4.071   98.015  1.00 18.20 ? 349  VAL   B O     1 
ATOM   11575 C  CB    . VAL   B 1  351  ? -7.256  7.193   96.951  1.00 18.17 ? 349  VAL   B CB    1 
ATOM   11576 C  CG1   . VAL   B 1  351  ? -6.412  6.980   98.221  1.00 18.91 ? 349  VAL   B CG1   1 
ATOM   11577 C  CG2   . VAL   B 1  351  ? -6.452  7.940   95.910  1.00 18.65 ? 349  VAL   B CG2   1 
ATOM   11578 N  N     . LEU   B 1  352  ? -9.686  5.265   97.699  1.00 17.93 ? 350  LEU   B N     1 
ATOM   11579 C  CA    . LEU   B 1  352  ? -10.432 4.443   98.641  1.00 19.75 ? 350  LEU   B CA    1 
ATOM   11580 C  C     . LEU   B 1  352  ? -10.485 2.990   98.187  1.00 20.37 ? 350  LEU   B C     1 
ATOM   11581 O  O     . LEU   B 1  352  ? -10.314 2.078   99.000  1.00 21.09 ? 350  LEU   B O     1 
ATOM   11582 C  CB    . LEU   B 1  352  ? -11.833 5.006   98.839  1.00 20.84 ? 350  LEU   B CB    1 
ATOM   11583 C  CG    . LEU   B 1  352  ? -11.875 6.337   99.581  1.00 20.02 ? 350  LEU   B CG    1 
ATOM   11584 C  CD1   . LEU   B 1  352  ? -13.293 6.853   99.575  1.00 21.76 ? 350  LEU   B CD1   1 
ATOM   11585 C  CD2   . LEU   B 1  352  ? -11.404 6.142   101.013 1.00 23.13 ? 350  LEU   B CD2   1 
ATOM   11586 N  N     . ASP   B 1  353  ? -10.714 2.751   96.888  1.00 20.11 ? 351  ASP   B N     1 
ATOM   11587 C  CA    . ASP   B 1  353  ? -10.706 1.378   96.389  1.00 21.33 ? 351  ASP   B CA    1 
ATOM   11588 C  C     . ASP   B 1  353  ? -9.367  0.718   96.663  1.00 19.09 ? 351  ASP   B C     1 
ATOM   11589 O  O     . ASP   B 1  353  ? -9.308  -0.453  97.055  1.00 21.61 ? 351  ASP   B O     1 
ATOM   11590 C  CB    . ASP   B 1  353  ? -10.943 1.346   94.878  1.00 22.04 ? 351  ASP   B CB    1 
ATOM   11591 C  CG    . ASP   B 1  353  ? -12.349 1.740   94.476  1.00 26.11 ? 351  ASP   B CG    1 
ATOM   11592 O  OD1   . ASP   B 1  353  ? -13.296 1.546   95.268  1.00 26.14 ? 351  ASP   B OD1   1 
ATOM   11593 O  OD2   . ASP   B 1  353  ? -12.491 2.239   93.335  1.00 27.69 ? 351  ASP   B OD2   1 
ATOM   11594 N  N     . PHE   B 1  354  ? -8.277  1.455   96.444  1.00 19.38 ? 352  PHE   B N     1 
ATOM   11595 C  CA    . PHE   B 1  354  ? -6.954  0.918   96.723  1.00 20.00 ? 352  PHE   B CA    1 
ATOM   11596 C  C     . PHE   B 1  354  ? -6.791  0.603   98.203  1.00 20.11 ? 352  PHE   B C     1 
ATOM   11597 O  O     . PHE   B 1  354  ? -6.251  -0.449  98.566  1.00 20.46 ? 352  PHE   B O     1 
ATOM   11598 C  CB    . PHE   B 1  354  ? -5.881  1.909   96.281  1.00 19.56 ? 352  PHE   B CB    1 
ATOM   11599 C  CG    . PHE   B 1  354  ? -4.511  1.566   96.792  1.00 20.27 ? 352  PHE   B CG    1 
ATOM   11600 C  CD1   . PHE   B 1  354  ? -3.721  0.639   96.127  1.00 22.32 ? 352  PHE   B CD1   1 
ATOM   11601 C  CD2   . PHE   B 1  354  ? -4.027  2.151   97.951  1.00 20.85 ? 352  PHE   B CD2   1 
ATOM   11602 C  CE1   . PHE   B 1  354  ? -2.460  0.311   96.607  1.00 20.97 ? 352  PHE   B CE1   1 
ATOM   11603 C  CE2   . PHE   B 1  354  ? -2.776  1.821   98.444  1.00 21.50 ? 352  PHE   B CE2   1 
ATOM   11604 C  CZ    . PHE   B 1  354  ? -1.993  0.904   97.777  1.00 21.97 ? 352  PHE   B CZ    1 
ATOM   11605 N  N     . ILE   B 1  355  ? -7.253  1.502   99.077  1.00 19.21 ? 353  ILE   B N     1 
ATOM   11606 C  CA    . ILE   B 1  355  ? -7.071  1.305   100.513 1.00 19.59 ? 353  ILE   B CA    1 
ATOM   11607 C  C     . ILE   B 1  355  ? -7.924  0.146   101.007 1.00 19.44 ? 353  ILE   B C     1 
ATOM   11608 O  O     . ILE   B 1  355  ? -7.477  -0.677  101.814 1.00 21.21 ? 353  ILE   B O     1 
ATOM   11609 C  CB    . ILE   B 1  355  ? -7.385  2.606   101.272 1.00 17.93 ? 353  ILE   B CB    1 
ATOM   11610 C  CG1   . ILE   B 1  355  ? -6.343  3.665   100.959 1.00 22.14 ? 353  ILE   B CG1   1 
ATOM   11611 C  CG2   . ILE   B 1  355  ? -7.464  2.347   102.783 1.00 20.74 ? 353  ILE   B CG2   1 
ATOM   11612 C  CD1   . ILE   B 1  355  ? -6.745  5.032   101.455 1.00 21.21 ? 353  ILE   B CD1   1 
ATOM   11613 N  N     . ILE   B 1  356  ? -9.168  0.072   100.540 1.00 20.24 ? 354  ILE   B N     1 
ATOM   11614 C  CA    . ILE   B 1  356  ? -10.039 -1.020  100.946 1.00 21.69 ? 354  ILE   B CA    1 
ATOM   11615 C  C     . ILE   B 1  356  ? -9.442  -2.357  100.534 1.00 20.76 ? 354  ILE   B C     1 
ATOM   11616 O  O     . ILE   B 1  356  ? -9.460  -3.327  101.302 1.00 21.73 ? 354  ILE   B O     1 
ATOM   11617 C  CB    . ILE   B 1  356  ? -11.448 -0.808  100.370 1.00 22.01 ? 354  ILE   B CB    1 
ATOM   11618 C  CG1   . ILE   B 1  356  ? -12.118 0.381   101.065 1.00 23.09 ? 354  ILE   B CG1   1 
ATOM   11619 C  CG2   . ILE   B 1  356  ? -12.271 -2.064  100.539 1.00 22.27 ? 354  ILE   B CG2   1 
ATOM   11620 C  CD1   . ILE   B 1  356  ? -13.376 0.895   100.361 1.00 22.81 ? 354  ILE   B CD1   1 
ATOM   11621 N  N     . ASP   B 1  357  ? -8.904  -2.429  99.312  1.00 20.55 ? 355  ASP   B N     1 
ATOM   11622 C  CA    . ASP   B 1  357  ? -8.267  -3.662  98.873  1.00 23.34 ? 355  ASP   B CA    1 
ATOM   11623 C  C     . ASP   B 1  357  ? -7.029  -3.967  99.703  1.00 19.26 ? 355  ASP   B C     1 
ATOM   11624 O  O     . ASP   B 1  357  ? -6.806  -5.118  100.089 1.00 21.13 ? 355  ASP   B O     1 
ATOM   11625 C  CB    . ASP   B 1  357  ? -7.912  -3.576  97.393  1.00 22.06 ? 355  ASP   B CB    1 
ATOM   11626 C  CG    . ASP   B 1  357  ? -7.063  -4.747  96.938  1.00 21.21 ? 355  ASP   B CG    1 
ATOM   11627 O  OD1   . ASP   B 1  357  ? -7.636  -5.845  96.742  1.00 26.56 ? 355  ASP   B OD1   1 
ATOM   11628 O  OD2   . ASP   B 1  357  ? -5.834  -4.578  96.809  1.00 23.12 ? 355  ASP   B OD2   1 
ATOM   11629 N  N     . LEU   B 1  358  ? -6.207  -2.953  99.973  1.00 20.93 ? 356  LEU   B N     1 
ATOM   11630 C  CA    . LEU   B 1  358  ? -5.021  -3.165  100.794 1.00 19.41 ? 356  LEU   B CA    1 
ATOM   11631 C  C     . LEU   B 1  358  ? -5.401  -3.690  102.169 1.00 19.30 ? 356  LEU   B C     1 
ATOM   11632 O  O     . LEU   B 1  358  ? -4.779  -4.628  102.679 1.00 21.66 ? 356  LEU   B O     1 
ATOM   11633 C  CB    . LEU   B 1  358  ? -4.244  -1.858  100.924 1.00 18.70 ? 356  LEU   B CB    1 
ATOM   11634 C  CG    . LEU   B 1  358  ? -3.040  -1.847  101.871 1.00 19.30 ? 356  LEU   B CG    1 
ATOM   11635 C  CD1   . LEU   B 1  358  ? -2.019  -2.904  101.482 1.00 20.56 ? 356  LEU   B CD1   1 
ATOM   11636 C  CD2   . LEU   B 1  358  ? -2.414  -0.453  101.849 1.00 20.57 ? 356  LEU   B CD2   1 
ATOM   11637 N  N     . ALA   B 1  359  ? -6.437  -3.106  102.776 1.00 19.68 ? 357  ALA   B N     1 
ATOM   11638 C  CA    . ALA   B 1  359  ? -6.886  -3.576  104.079 1.00 19.52 ? 357  ALA   B CA    1 
ATOM   11639 C  C     . ALA   B 1  359  ? -7.292  -5.041  104.012 1.00 22.92 ? 357  ALA   B C     1 
ATOM   11640 O  O     . ALA   B 1  359  ? -6.914  -5.840  104.874 1.00 23.37 ? 357  ALA   B O     1 
ATOM   11641 C  CB    . ALA   B 1  359  ? -8.062  -2.720  104.549 1.00 23.45 ? 357  ALA   B CB    1 
ATOM   11642 N  N     . ARG   B 1  360  ? -8.024  -5.414  102.958 1.00 21.87 ? 358  ARG   B N     1 
ATOM   11643 C  CA    A ARG   B 1  360  ? -8.499  -6.786  102.818 0.58 24.50 ? 358  ARG   B CA    1 
ATOM   11644 C  CA    B ARG   B 1  360  ? -8.501  -6.785  102.825 0.42 24.49 ? 358  ARG   B CA    1 
ATOM   11645 C  C     . ARG   B 1  360  ? -7.346  -7.765  102.665 1.00 20.74 ? 358  ARG   B C     1 
ATOM   11646 O  O     . ARG   B 1  360  ? -7.321  -8.821  103.308 1.00 23.98 ? 358  ARG   B O     1 
ATOM   11647 C  CB    A ARG   B 1  360  ? -9.433  -6.885  101.614 0.58 25.06 ? 358  ARG   B CB    1 
ATOM   11648 C  CB    B ARG   B 1  360  ? -9.460  -6.887  101.639 0.42 25.09 ? 358  ARG   B CB    1 
ATOM   11649 C  CG    A ARG   B 1  360  ? -10.826 -6.425  101.919 0.58 25.85 ? 358  ARG   B CG    1 
ATOM   11650 C  CG    B ARG   B 1  360  ? -10.899 -7.128  102.043 0.42 30.03 ? 358  ARG   B CG    1 
ATOM   11651 C  CD    A ARG   B 1  360  ? -11.721 -6.459  100.697 0.58 27.86 ? 358  ARG   B CD    1 
ATOM   11652 C  CD    B ARG   B 1  360  ? -11.771 -7.443  100.835 0.42 26.73 ? 358  ARG   B CD    1 
ATOM   11653 N  NE    A ARG   B 1  360  ? -13.119 -6.307  101.081 0.58 28.59 ? 358  ARG   B NE    1 
ATOM   11654 N  NE    B ARG   B 1  360  ? -12.345 -6.246  100.232 0.42 29.55 ? 358  ARG   B NE    1 
ATOM   11655 C  CZ    A ARG   B 1  360  ? -14.023 -5.651  100.367 0.58 31.37 ? 358  ARG   B CZ    1 
ATOM   11656 C  CZ    B ARG   B 1  360  ? -13.550 -5.772  100.521 0.42 31.08 ? 358  ARG   B CZ    1 
ATOM   11657 N  NH1   A ARG   B 1  360  ? -13.706 -5.059  99.227  0.58 34.23 ? 358  ARG   B NH1   1 
ATOM   11658 N  NH1   B ARG   B 1  360  ? -14.326 -6.358  101.420 0.42 34.37 ? 358  ARG   B NH1   1 
ATOM   11659 N  NH2   A ARG   B 1  360  ? -15.275 -5.582  100.812 0.58 35.88 ? 358  ARG   B NH2   1 
ATOM   11660 N  NH2   B ARG   B 1  360  ? -13.991 -4.690  99.887  0.42 33.22 ? 358  ARG   B NH2   1 
ATOM   11661 N  N     . ARG   B 1  361  ? -6.385  -7.440  101.804 1.00 22.90 ? 359  ARG   B N     1 
ATOM   11662 C  CA    . ARG   B 1  361  ? -5.325  -8.405  101.555 1.00 23.76 ? 359  ARG   B CA    1 
ATOM   11663 C  C     . ARG   B 1  361  ? -4.274  -8.429  102.651 1.00 21.89 ? 359  ARG   B C     1 
ATOM   11664 O  O     . ARG   B 1  361  ? -3.553  -9.424  102.772 1.00 23.53 ? 359  ARG   B O     1 
ATOM   11665 C  CB    . ARG   B 1  361  ? -4.701  -8.198  100.175 1.00 26.84 ? 359  ARG   B CB    1 
ATOM   11666 C  CG    . ARG   B 1  361  ? -4.019  -6.874  99.992  1.00 26.27 ? 359  ARG   B CG    1 
ATOM   11667 C  CD    . ARG   B 1  361  ? -3.622  -6.701  98.526  1.00 22.89 ? 359  ARG   B CD    1 
ATOM   11668 N  NE    . ARG   B 1  361  ? -3.399  -5.300  98.193  1.00 21.75 ? 359  ARG   B NE    1 
ATOM   11669 C  CZ    . ARG   B 1  361  ? -2.227  -4.686  98.265  1.00 19.61 ? 359  ARG   B CZ    1 
ATOM   11670 N  NH1   . ARG   B 1  361  ? -1.144  -5.314  98.692  1.00 23.40 ? 359  ARG   B NH1   1 
ATOM   11671 N  NH2   . ARG   B 1  361  ? -2.138  -3.410  97.900  1.00 21.72 ? 359  ARG   B NH2   1 
ATOM   11672 N  N     . SER   B 1  362  ? -4.180  -7.372  103.462 1.00 22.07 ? 360  SER   B N     1 
ATOM   11673 C  CA    . SER   B 1  362  ? -3.163  -7.299  104.501 1.00 22.82 ? 360  SER   B CA    1 
ATOM   11674 C  C     . SER   B 1  362  ? -3.673  -7.722  105.871 1.00 21.67 ? 360  SER   B C     1 
ATOM   11675 O  O     . SER   B 1  362  ? -2.867  -7.877  106.797 1.00 25.24 ? 360  SER   B O     1 
ATOM   11676 C  CB    . SER   B 1  362  ? -2.598  -5.877  104.577 1.00 23.01 ? 360  SER   B CB    1 
ATOM   11677 O  OG    . SER   B 1  362  ? -3.578  -4.997  105.091 1.00 22.56 ? 360  SER   B OG    1 
ATOM   11678 N  N     . GLY   B 1  363  ? -4.975  -7.907  106.035 1.00 20.63 ? 361  GLY   B N     1 
ATOM   11679 C  CA    . GLY   B 1  363  ? -5.462  -8.257  107.356 1.00 21.06 ? 361  GLY   B CA    1 
ATOM   11680 C  C     . GLY   B 1  363  ? -5.325  -7.126  108.352 1.00 22.08 ? 361  GLY   B C     1 
ATOM   11681 O  O     . GLY   B 1  363  ? -5.071  -7.375  109.536 1.00 25.59 ? 361  GLY   B O     1 
ATOM   11682 N  N     . ARG   B 1  364  ? -5.487  -5.890  107.897 1.00 23.37 ? 362  ARG   B N     1 
ATOM   11683 C  CA    . ARG   B 1  364  ? -5.428  -4.709  108.748 1.00 23.72 ? 362  ARG   B CA    1 
ATOM   11684 C  C     . ARG   B 1  364  ? -6.717  -3.943  108.536 1.00 23.13 ? 362  ARG   B C     1 
ATOM   11685 O  O     . ARG   B 1  364  ? -7.103  -3.682  107.395 1.00 24.70 ? 362  ARG   B O     1 
ATOM   11686 C  CB    . ARG   B 1  364  ? -4.288  -3.778  108.318 1.00 22.35 ? 362  ARG   B CB    1 
ATOM   11687 C  CG    . ARG   B 1  364  ? -2.906  -4.373  108.361 1.00 22.70 ? 362  ARG   B CG    1 
ATOM   11688 C  CD    . ARG   B 1  364  ? -2.406  -4.455  109.792 1.00 24.16 ? 362  ARG   B CD    1 
ATOM   11689 N  NE    . ARG   B 1  364  ? -1.125  -5.146  109.839 1.00 21.14 ? 362  ARG   B NE    1 
ATOM   11690 C  CZ    . ARG   B 1  364  ? 0.048   -4.566  109.626 1.00 22.85 ? 362  ARG   B CZ    1 
ATOM   11691 N  NH1   . ARG   B 1  364  ? 0.149   -3.260  109.406 1.00 22.77 ? 362  ARG   B NH1   1 
ATOM   11692 N  NH2   . ARG   B 1  364  ? 1.146   -5.317  109.628 1.00 25.07 ? 362  ARG   B NH2   1 
ATOM   11693 N  N     . ARG   B 1  365  ? -7.391  -3.575  109.610 1.00 23.72 ? 363  ARG   B N     1 
ATOM   11694 C  CA    . ARG   B 1  365  ? -8.391  -2.540  109.449 1.00 22.38 ? 363  ARG   B CA    1 
ATOM   11695 C  C     . ARG   B 1  365  ? -7.648  -1.223  109.403 1.00 22.79 ? 363  ARG   B C     1 
ATOM   11696 O  O     . ARG   B 1  365  ? -6.801  -0.955  110.258 1.00 25.61 ? 363  ARG   B O     1 
ATOM   11697 C  CB    . ARG   B 1  365  ? -9.385  -2.542  110.599 1.00 24.19 ? 363  ARG   B CB    1 
ATOM   11698 C  CG    . ARG   B 1  365  ? -10.670 -1.798  110.252 1.00 24.87 ? 363  ARG   B CG    1 
ATOM   11699 C  CD    . ARG   B 1  365  ? -11.725 -2.050  111.314 1.00 29.88 ? 363  ARG   B CD    1 
ATOM   11700 N  NE    . ARG   B 1  365  ? -13.013 -1.468  110.959 1.00 29.42 ? 363  ARG   B NE    1 
ATOM   11701 C  CZ    . ARG   B 1  365  ? -13.759 -0.746  111.784 1.00 27.60 ? 363  ARG   B CZ    1 
ATOM   11702 N  NH1   . ARG   B 1  365  ? -13.376 -0.502  113.029 1.00 26.19 ? 363  ARG   B NH1   1 
ATOM   11703 N  NH2   . ARG   B 1  365  ? -14.923 -0.267  111.355 1.00 24.66 ? 363  ARG   B NH2   1 
ATOM   11704 N  N     . ILE   B 1  366  ? -7.893  -0.446  108.365 1.00 21.42 ? 364  ILE   B N     1 
ATOM   11705 C  CA    . ILE   B 1  366  ? -7.237  0.838   108.188 1.00 21.83 ? 364  ILE   B CA    1 
ATOM   11706 C  C     . ILE   B 1  366  ? -8.238  1.916   108.556 1.00 23.55 ? 364  ILE   B C     1 
ATOM   11707 O  O     . ILE   B 1  366  ? -9.397  1.867   108.123 1.00 22.50 ? 364  ILE   B O     1 
ATOM   11708 C  CB    . ILE   B 1  366  ? -6.743  1.004   106.742 1.00 20.78 ? 364  ILE   B CB    1 
ATOM   11709 C  CG1   . ILE   B 1  366  ? -5.737  -0.104  106.410 1.00 23.60 ? 364  ILE   B CG1   1 
ATOM   11710 C  CG2   . ILE   B 1  366  ? -6.148  2.401   106.526 1.00 20.48 ? 364  ILE   B CG2   1 
ATOM   11711 C  CD1   . ILE   B 1  366  ? -5.279  -0.105  104.962 1.00 22.85 ? 364  ILE   B CD1   1 
ATOM   11712 N  N     . MET   B 1  367  ? -7.809  2.864   109.386 1.00 20.86 ? 365  MET   B N     1 
ATOM   11713 C  CA    . MET   B 1  367  ? -8.659  3.989   109.745 1.00 21.34 ? 365  MET   B CA    1 
ATOM   11714 C  C     . MET   B 1  367  ? -8.552  5.009   108.630 1.00 22.60 ? 365  MET   B C     1 
ATOM   11715 O  O     . MET   B 1  367  ? -7.452  5.451   108.301 1.00 22.79 ? 365  MET   B O     1 
ATOM   11716 C  CB    . MET   B 1  367  ? -8.191  4.590   111.065 1.00 20.44 ? 365  MET   B CB    1 
ATOM   11717 C  CG    . MET   B 1  367  ? -8.014  3.541   112.149 1.00 20.50 ? 365  MET   B CG    1 
ATOM   11718 S  SD    . MET   B 1  367  ? -7.484  4.248   113.727 1.00 23.36 ? 365  MET   B SD    1 
ATOM   11719 C  CE    . MET   B 1  367  ? -8.997  4.415   114.661 1.00 30.93 ? 365  MET   B CE    1 
ATOM   11720 N  N     . VAL   B 1  368  ? -9.671  5.349   108.012 1.00 18.80 ? 366  VAL   B N     1 
ATOM   11721 C  CA    . VAL   B 1  368  ? -9.655  6.228   106.856 1.00 19.37 ? 366  VAL   B CA    1 
ATOM   11722 C  C     . VAL   B 1  368  ? -10.372 7.512   107.221 1.00 20.91 ? 366  VAL   B C     1 
ATOM   11723 O  O     . VAL   B 1  368  ? -11.593 7.517   107.417 1.00 20.81 ? 366  VAL   B O     1 
ATOM   11724 C  CB    . VAL   B 1  368  ? -10.297 5.578   105.628 1.00 20.36 ? 366  VAL   B CB    1 
ATOM   11725 C  CG1   . VAL   B 1  368  ? -10.270 6.563   104.479 1.00 21.08 ? 366  VAL   B CG1   1 
ATOM   11726 C  CG2   . VAL   B 1  368  ? -9.545  4.303   105.260 1.00 22.74 ? 366  VAL   B CG2   1 
ATOM   11727 N  N     . ARG   B 1  369  ? -9.630  8.607   107.312 1.00 18.35 ? 367  ARG   B N     1 
ATOM   11728 C  CA    . ARG   B 1  369  ? -10.248 9.893   107.588 1.00 18.66 ? 367  ARG   B CA    1 
ATOM   11729 C  C     . ARG   B 1  369  ? -10.620 10.507  106.258 1.00 19.01 ? 367  ARG   B C     1 
ATOM   11730 O  O     . ARG   B 1  369  ? -9.748  10.816  105.444 1.00 19.54 ? 367  ARG   B O     1 
ATOM   11731 C  CB    . ARG   B 1  369  ? -9.314  10.827  108.357 1.00 18.01 ? 367  ARG   B CB    1 
ATOM   11732 C  CG    . ARG   B 1  369  ? -9.985  12.168  108.666 1.00 21.05 ? 367  ARG   B CG    1 
ATOM   11733 C  CD    . ARG   B 1  369  ? -8.967  13.204  109.023 1.00 20.63 ? 367  ARG   B CD    1 
ATOM   11734 N  NE    . ARG   B 1  369  ? -8.299  12.861  110.263 1.00 19.67 ? 367  ARG   B NE    1 
ATOM   11735 C  CZ    . ARG   B 1  369  ? -7.094  13.289  110.599 1.00 19.41 ? 367  ARG   B CZ    1 
ATOM   11736 N  NH1   . ARG   B 1  369  ? -6.391  14.078  109.797 1.00 19.27 ? 367  ARG   B NH1   1 
ATOM   11737 N  NH2   . ARG   B 1  369  ? -6.578  12.905  111.761 1.00 20.54 ? 367  ARG   B NH2   1 
ATOM   11738 N  N     . LEU   B 1  370  ? -11.912 10.674  106.029 1.00 17.81 ? 368  LEU   B N     1 
ATOM   11739 C  CA    . LEU   B 1  370  ? -12.375 11.357  104.837 1.00 17.37 ? 368  LEU   B CA    1 
ATOM   11740 C  C     . LEU   B 1  370  ? -12.513 12.833  105.164 1.00 18.54 ? 368  LEU   B C     1 
ATOM   11741 O  O     . LEU   B 1  370  ? -13.227 13.207  106.103 1.00 19.62 ? 368  LEU   B O     1 
ATOM   11742 C  CB    . LEU   B 1  370  ? -13.705 10.761  104.393 1.00 20.20 ? 368  LEU   B CB    1 
ATOM   11743 C  CG    . LEU   B 1  370  ? -14.278 11.343  103.109 1.00 18.62 ? 368  LEU   B CG    1 
ATOM   11744 C  CD1   . LEU   B 1  370  ? -13.390 11.010  101.926 1.00 22.04 ? 368  LEU   B CD1   1 
ATOM   11745 C  CD2   . LEU   B 1  370  ? -15.694 10.817  102.893 1.00 20.50 ? 368  LEU   B CD2   1 
ATOM   11746 N  N     . VAL   B 1  371  ? -11.779 13.663  104.437 1.00 16.59 ? 369  VAL   B N     1 
ATOM   11747 C  CA    . VAL   B 1  371  ? -11.840 15.107  104.574 1.00 18.02 ? 369  VAL   B CA    1 
ATOM   11748 C  C     . VAL   B 1  371  ? -12.218 15.669  103.225 1.00 19.05 ? 369  VAL   B C     1 
ATOM   11749 O  O     . VAL   B 1  371  ? -12.178 14.974  102.210 1.00 18.67 ? 369  VAL   B O     1 
ATOM   11750 C  CB    . VAL   B 1  371  ? -10.501 15.698  105.039 1.00 16.70 ? 369  VAL   B CB    1 
ATOM   11751 C  CG1   . VAL   B 1  371  ? -10.045 14.988  106.282 1.00 18.05 ? 369  VAL   B CG1   1 
ATOM   11752 C  CG2   . VAL   B 1  371  ? -9.459  15.576  103.942 1.00 17.87 ? 369  VAL   B CG2   1 
ATOM   11753 N  N     . LYS   B 1  372  ? -12.569 16.948  103.208 1.00 17.13 ? 370  LYS   B N     1 
ATOM   11754 C  CA    . LYS   B 1  372  ? -12.695 17.594  101.911 1.00 17.84 ? 370  LYS   B CA    1 
ATOM   11755 C  C     . LYS   B 1  372  ? -11.325 17.969  101.356 1.00 16.96 ? 370  LYS   B C     1 
ATOM   11756 O  O     . LYS   B 1  372  ? -10.897 17.425  100.336 1.00 19.01 ? 370  LYS   B O     1 
ATOM   11757 C  CB    . LYS   B 1  372  ? -13.716 18.734  101.970 1.00 19.62 ? 370  LYS   B CB    1 
ATOM   11758 C  CG    . LYS   B 1  372  ? -15.090 18.142  102.205 1.00 18.90 ? 370  LYS   B CG    1 
ATOM   11759 C  CD    . LYS   B 1  372  ? -16.202 19.152  102.292 1.00 20.05 ? 370  LYS   B CD    1 
ATOM   11760 C  CE    . LYS   B 1  372  ? -17.465 18.439  102.772 1.00 21.47 ? 370  LYS   B CE    1 
ATOM   11761 N  NZ    . LYS   B 1  372  ? -18.577 19.407  103.037 1.00 22.45 ? 370  LYS   B NZ    1 
ATOM   11762 N  N     . GLY   B 1  373  ? -10.590 18.835  102.047 1.00 18.06 ? 371  GLY   B N     1 
ATOM   11763 C  CA    . GLY   B 1  373  ? -9.210  19.081  101.655 1.00 17.25 ? 371  GLY   B CA    1 
ATOM   11764 C  C     . GLY   B 1  373  ? -8.769  20.488  101.982 1.00 16.50 ? 371  GLY   B C     1 
ATOM   11765 O  O     . GLY   B 1  373  ? -9.562  21.421  101.855 1.00 18.22 ? 371  GLY   B O     1 
ATOM   11766 N  N     . ALA   B 1  374  ? -7.510  20.662  102.383 1.00 16.20 ? 372  ALA   B N     1 
ATOM   11767 C  CA    . ALA   B 1  374  ? -7.056  21.913  102.973 1.00 17.47 ? 372  ALA   B CA    1 
ATOM   11768 C  C     . ALA   B 1  374  ? -6.228  22.780  102.037 1.00 18.00 ? 372  ALA   B C     1 
ATOM   11769 O  O     . ALA   B 1  374  ? -5.858  23.891  102.423 1.00 19.78 ? 372  ALA   B O     1 
ATOM   11770 C  CB    . ALA   B 1  374  ? -6.241  21.641  104.240 1.00 19.01 ? 372  ALA   B CB    1 
ATOM   11771 N  N     . TYR   B 1  375  ? -5.934  22.321  100.821 1.00 16.60 ? 373  TYR   B N     1 
ATOM   11772 C  CA    . TYR   B 1  375  ? -4.989  23.028  99.970  1.00 16.95 ? 373  TYR   B CA    1 
ATOM   11773 C  C     . TYR   B 1  375  ? -5.629  23.562  98.696  1.00 17.69 ? 373  TYR   B C     1 
ATOM   11774 O  O     . TYR   B 1  375  ? -4.948  23.735  97.698  1.00 16.48 ? 373  TYR   B O     1 
ATOM   11775 C  CB    . TYR   B 1  375  ? -3.793  22.145  99.624  1.00 19.50 ? 373  TYR   B CB    1 
ATOM   11776 C  CG    . TYR   B 1  375  ? -3.094  21.553  100.830 1.00 17.91 ? 373  TYR   B CG    1 
ATOM   11777 C  CD1   . TYR   B 1  375  ? -3.649  20.484  101.527 1.00 17.98 ? 373  TYR   B CD1   1 
ATOM   11778 C  CD2   . TYR   B 1  375  ? -1.859  22.032  101.235 1.00 21.03 ? 373  TYR   B CD2   1 
ATOM   11779 C  CE1   . TYR   B 1  375  ? -3.004  19.938  102.626 1.00 18.67 ? 373  TYR   B CE1   1 
ATOM   11780 C  CE2   . TYR   B 1  375  ? -1.201  21.490  102.314 1.00 21.56 ? 373  TYR   B CE2   1 
ATOM   11781 C  CZ    . TYR   B 1  375  ? -1.776  20.445  103.003 1.00 20.72 ? 373  TYR   B CZ    1 
ATOM   11782 O  OH    . TYR   B 1  375  ? -1.107  19.907  104.070 1.00 24.87 ? 373  TYR   B OH    1 
ATOM   11783 N  N     . TRP   B 1  376  ? -6.927  23.852  98.721  1.00 16.97 ? 374  TRP   B N     1 
ATOM   11784 C  CA    . TRP   B 1  376  ? -7.647  24.067  97.471  1.00 16.52 ? 374  TRP   B CA    1 
ATOM   11785 C  C     . TRP   B 1  376  ? -7.060  25.214  96.654  1.00 15.93 ? 374  TRP   B C     1 
ATOM   11786 O  O     . TRP   B 1  376  ? -6.738  25.039  95.472  1.00 16.32 ? 374  TRP   B O     1 
ATOM   11787 C  CB    . TRP   B 1  376  ? -9.134  24.277  97.738  1.00 16.29 ? 374  TRP   B CB    1 
ATOM   11788 C  CG    . TRP   B 1  376  ? -9.875  24.441  96.464  1.00 17.85 ? 374  TRP   B CG    1 
ATOM   11789 C  CD1   . TRP   B 1  376  ? -10.271 23.451  95.610  1.00 16.82 ? 374  TRP   B CD1   1 
ATOM   11790 C  CD2   . TRP   B 1  376  ? -10.292 25.670  95.882  1.00 18.12 ? 374  TRP   B CD2   1 
ATOM   11791 N  NE1   . TRP   B 1  376  ? -10.919 24.000  94.528  1.00 17.40 ? 374  TRP   B NE1   1 
ATOM   11792 C  CE2   . TRP   B 1  376  ? -10.939 25.360  94.671  1.00 18.00 ? 374  TRP   B CE2   1 
ATOM   11793 C  CE3   . TRP   B 1  376  ? -10.179 27.010  96.269  1.00 22.26 ? 374  TRP   B CE3   1 
ATOM   11794 C  CZ2   . TRP   B 1  376  ? -11.462 26.338  93.835  1.00 19.64 ? 374  TRP   B CZ2   1 
ATOM   11795 C  CZ3   . TRP   B 1  376  ? -10.716 27.978  95.452  1.00 23.14 ? 374  TRP   B CZ3   1 
ATOM   11796 C  CH2   . TRP   B 1  376  ? -11.353 27.640  94.246  1.00 21.65 ? 374  TRP   B CH2   1 
ATOM   11797 N  N     . ASP   B 1  377  ? -6.932  26.402  97.258  1.00 17.30 ? 375  ASP   B N     1 
ATOM   11798 C  CA    . ASP   B 1  377  ? -6.422  27.555  96.521  1.00 19.94 ? 375  ASP   B CA    1 
ATOM   11799 C  C     . ASP   B 1  377  ? -5.057  27.256  95.934  1.00 16.53 ? 375  ASP   B C     1 
ATOM   11800 O  O     . ASP   B 1  377  ? -4.762  27.650  94.800  1.00 18.13 ? 375  ASP   B O     1 
ATOM   11801 C  CB    . ASP   B 1  377  ? -6.287  28.772  97.440  1.00 23.46 ? 375  ASP   B CB    1 
ATOM   11802 C  CG    . ASP   B 1  377  ? -7.601  29.258  97.986  1.00 35.33 ? 375  ASP   B CG    1 
ATOM   11803 O  OD1   . ASP   B 1  377  ? -8.550  29.403  97.204  1.00 44.92 ? 375  ASP   B OD1   1 
ATOM   11804 O  OD2   . ASP   B 1  377  ? -7.674  29.517  99.205  1.00 49.25 ? 375  ASP   B OD2   1 
ATOM   11805 N  N     . ALA   B 1  378  ? -4.199  26.586  96.705  1.00 15.74 ? 376  ALA   B N     1 
ATOM   11806 C  CA    . ALA   B 1  378  ? -2.848  26.316  96.239  1.00 15.69 ? 376  ALA   B CA    1 
ATOM   11807 C  C     . ALA   B 1  378  ? -2.859  25.323  95.092  1.00 17.55 ? 376  ALA   B C     1 
ATOM   11808 O  O     . ALA   B 1  378  ? -2.005  25.399  94.198  1.00 17.01 ? 376  ALA   B O     1 
ATOM   11809 C  CB    . ALA   B 1  378  ? -1.994  25.785  97.393  1.00 18.37 ? 376  ALA   B CB    1 
ATOM   11810 N  N     . GLU   B 1  379  ? -3.808  24.387  95.102  1.00 15.60 ? 377  GLU   B N     1 
ATOM   11811 C  CA    . GLU   B 1  379  ? -3.864  23.418  94.017  1.00 15.54 ? 377  GLU   B CA    1 
ATOM   11812 C  C     . GLU   B 1  379  ? -4.305  24.083  92.727  1.00 17.21 ? 377  GLU   B C     1 
ATOM   11813 O  O     . GLU   B 1  379  ? -3.803  23.750  91.649  1.00 17.26 ? 377  GLU   B O     1 
ATOM   11814 C  CB    . GLU   B 1  379  ? -4.792  22.250  94.359  1.00 15.96 ? 377  GLU   B CB    1 
ATOM   11815 C  CG    . GLU   B 1  379  ? -4.392  21.438  95.583  1.00 17.41 ? 377  GLU   B CG    1 
ATOM   11816 C  CD    . GLU   B 1  379  ? -3.118  20.620  95.427  1.00 18.30 ? 377  GLU   B CD    1 
ATOM   11817 O  OE1   . GLU   B 1  379  ? -2.504  20.584  94.332  1.00 20.23 ? 377  GLU   B OE1   1 
ATOM   11818 O  OE2   . GLU   B 1  379  ? -2.726  19.978  96.422  1.00 20.10 ? 377  GLU   B OE2   1 
ATOM   11819 N  N     . ILE   B 1  380  ? -5.234  25.035  92.812  1.00 16.18 ? 378  ILE   B N     1 
ATOM   11820 C  CA    . ILE   B 1  380  ? -5.632  25.768  91.613  1.00 15.56 ? 378  ILE   B CA    1 
ATOM   11821 C  C     . ILE   B 1  380  ? -4.444  26.527  91.050  1.00 16.68 ? 378  ILE   B C     1 
ATOM   11822 O  O     . ILE   B 1  380  ? -4.146  26.455  89.852  1.00 16.15 ? 378  ILE   B O     1 
ATOM   11823 C  CB    . ILE   B 1  380  ? -6.797  26.719  91.922  1.00 17.10 ? 378  ILE   B CB    1 
ATOM   11824 C  CG1   . ILE   B 1  380  ? -7.993  25.950  92.490  1.00 16.35 ? 378  ILE   B CG1   1 
ATOM   11825 C  CG2   . ILE   B 1  380  ? -7.179  27.479  90.667  1.00 16.68 ? 378  ILE   B CG2   1 
ATOM   11826 C  CD1   . ILE   B 1  380  ? -8.498  24.823  91.589  1.00 18.95 ? 378  ILE   B CD1   1 
ATOM   11827 N  N     . LYS   B 1  381  ? -3.754  27.274  91.912  1.00 14.80 ? 379  LYS   B N     1 
ATOM   11828 C  CA    . LYS   B 1  381  ? -2.619  28.059  91.458  1.00 14.79 ? 379  LYS   B CA    1 
ATOM   11829 C  C     . LYS   B 1  381  ? -1.556  27.169  90.841  1.00 16.19 ? 379  LYS   B C     1 
ATOM   11830 O  O     . LYS   B 1  381  ? -1.038  27.468  89.762  1.00 15.83 ? 379  LYS   B O     1 
ATOM   11831 C  CB    . LYS   B 1  381  ? -2.025  28.866  92.611  1.00 15.96 ? 379  LYS   B CB    1 
ATOM   11832 C  CG    . LYS   B 1  381  ? -0.792  29.651  92.190  1.00 17.50 ? 379  LYS   B CG    1 
ATOM   11833 C  CD    . LYS   B 1  381  ? -0.356  30.585  93.293  1.00 16.26 ? 379  LYS   B CD    1 
ATOM   11834 C  CE    . LYS   B 1  381  ? 0.817   31.431  92.837  1.00 17.64 ? 379  LYS   B CE    1 
ATOM   11835 N  NZ    . LYS   B 1  381  ? 1.211   32.353  93.944  1.00 17.59 ? 379  LYS   B NZ    1 
ATOM   11836 N  N     . ARG   B 1  382  ? -1.236  26.054  91.499  1.00 15.22 ? 380  ARG   B N     1 
ATOM   11837 C  CA    . ARG   B 1  382  ? -0.129  25.229  91.025  1.00 16.02 ? 380  ARG   B CA    1 
ATOM   11838 C  C     . ARG   B 1  382  ? -0.428  24.635  89.658  1.00 15.67 ? 380  ARG   B C     1 
ATOM   11839 O  O     . ARG   B 1  382  ? 0.438   24.620  88.774  1.00 16.94 ? 380  ARG   B O     1 
ATOM   11840 C  CB    . ARG   B 1  382  ? 0.144   24.114  92.038  1.00 17.99 ? 380  ARG   B CB    1 
ATOM   11841 C  CG    . ARG   B 1  382  ? 1.312   23.213  91.667  1.00 22.90 ? 380  ARG   B CG    1 
ATOM   11842 C  CD    . ARG   B 1  382  ? 2.609   23.990  91.436  1.00 25.93 ? 380  ARG   B CD    1 
ATOM   11843 N  NE    . ARG   B 1  382  ? 3.712   23.071  91.172  1.00 37.57 ? 380  ARG   B NE    1 
ATOM   11844 C  CZ    . ARG   B 1  382  ? 4.427   22.465  92.111  1.00 46.17 ? 380  ARG   B CZ    1 
ATOM   11845 N  NH1   . ARG   B 1  382  ? 4.223   22.702  93.398  1.00 39.39 ? 380  ARG   B NH1   1 
ATOM   11846 N  NH2   . ARG   B 1  382  ? 5.368   21.597  91.751  1.00 45.24 ? 380  ARG   B NH2   1 
ATOM   11847 N  N     . ALA   B 1  383  ? -1.647  24.156  89.455  1.00 15.69 ? 381  ALA   B N     1 
ATOM   11848 C  CA    . ALA   B 1  383  ? -1.964  23.565  88.167  1.00 14.33 ? 381  ALA   B CA    1 
ATOM   11849 C  C     . ALA   B 1  383  ? -1.921  24.620  87.073  1.00 15.66 ? 381  ALA   B C     1 
ATOM   11850 O  O     . ALA   B 1  383  ? -1.479  24.346  85.952  1.00 16.08 ? 381  ALA   B O     1 
ATOM   11851 C  CB    . ALA   B 1  383  ? -3.332  22.905  88.250  1.00 16.25 ? 381  ALA   B CB    1 
ATOM   11852 N  N     . GLN   B 1  384  ? -2.370  25.837  87.383  1.00 14.87 ? 382  GLN   B N     1 
ATOM   11853 C  CA    . GLN   B 1  384  ? -2.283  26.913  86.405  1.00 16.33 ? 382  GLN   B CA    1 
ATOM   11854 C  C     . GLN   B 1  384  ? -0.840  27.265  86.099  1.00 15.82 ? 382  GLN   B C     1 
ATOM   11855 O  O     . GLN   B 1  384  ? -0.469  27.396  84.929  1.00 15.98 ? 382  GLN   B O     1 
ATOM   11856 C  CB    . GLN   B 1  384  ? -3.044  28.139  86.890  1.00 15.30 ? 382  GLN   B CB    1 
ATOM   11857 C  CG    . GLN   B 1  384  ? -4.529  27.937  86.852  1.00 14.76 ? 382  GLN   B CG    1 
ATOM   11858 C  CD    . GLN   B 1  384  ? -5.262  29.175  87.250  1.00 16.24 ? 382  GLN   B CD    1 
ATOM   11859 O  OE1   . GLN   B 1  384  ? -4.692  30.057  87.882  1.00 19.00 ? 382  GLN   B OE1   1 
ATOM   11860 N  NE2   . GLN   B 1  384  ? -6.539  29.255  86.900  1.00 16.30 ? 382  GLN   B NE2   1 
ATOM   11861 N  N     . LEU   B 1  385  ? -0.012  27.434  87.136  1.00 15.78 ? 383  LEU   B N     1 
ATOM   11862 C  CA    . LEU   B 1  385  ? 1.393   27.746  86.909  1.00 15.68 ? 383  LEU   B CA    1 
ATOM   11863 C  C     . LEU   B 1  385  ? 2.057   26.687  86.051  1.00 16.70 ? 383  LEU   B C     1 
ATOM   11864 O  O     . LEU   B 1  385  ? 2.886   27.011  85.190  1.00 16.33 ? 383  LEU   B O     1 
ATOM   11865 C  CB    . LEU   B 1  385  ? 2.139   27.839  88.237  1.00 17.09 ? 383  LEU   B CB    1 
ATOM   11866 C  CG    . LEU   B 1  385  ? 1.858   29.073  89.073  1.00 21.25 ? 383  LEU   B CG    1 
ATOM   11867 C  CD1   . LEU   B 1  385  ? 2.663   28.966  90.336  1.00 21.85 ? 383  LEU   B CD1   1 
ATOM   11868 C  CD2   . LEU   B 1  385  ? 2.260   30.311  88.306  1.00 24.65 ? 383  LEU   B CD2   1 
ATOM   11869 N  N     . ASP   B 1  386  ? 1.723   25.422  86.279  1.00 16.52 ? 384  ASP   B N     1 
ATOM   11870 C  CA    . ASP   B 1  386  ? 2.413   24.325  85.612  1.00 15.45 ? 384  ASP   B CA    1 
ATOM   11871 C  C     . ASP   B 1  386  ? 1.809   23.975  84.265  1.00 15.57 ? 384  ASP   B C     1 
ATOM   11872 O  O     . ASP   B 1  386  ? 2.334   23.092  83.583  1.00 17.96 ? 384  ASP   B O     1 
ATOM   11873 C  CB    . ASP   B 1  386  ? 2.487   23.090  86.525  1.00 18.17 ? 384  ASP   B CB    1 
ATOM   11874 C  CG    . ASP   B 1  386  ? 3.399   23.304  87.734  1.00 23.17 ? 384  ASP   B CG    1 
ATOM   11875 O  OD1   . ASP   B 1  386  ? 4.133   24.320  87.787  1.00 24.55 ? 384  ASP   B OD1   1 
ATOM   11876 O  OD2   . ASP   B 1  386  ? 3.380   22.443  88.642  1.00 26.02 ? 384  ASP   B OD2   1 
ATOM   11877 N  N     . GLY   B 1  387  ? 0.735   24.647  83.862  1.00 15.73 ? 385  GLY   B N     1 
ATOM   11878 C  CA    . GLY   B 1  387  ? 0.159   24.406  82.553  1.00 16.30 ? 385  GLY   B CA    1 
ATOM   11879 C  C     . GLY   B 1  387  ? -0.336  22.990  82.383  1.00 19.27 ? 385  GLY   B C     1 
ATOM   11880 O  O     . GLY   B 1  387  ? -0.214  22.413  81.297  1.00 18.65 ? 385  GLY   B O     1 
ATOM   11881 N  N     . LEU   B 1  388  ? -0.889  22.409  83.438  1.00 16.86 ? 386  LEU   B N     1 
ATOM   11882 C  CA    . LEU   B 1  388  ? -1.280  21.013  83.354  1.00 18.41 ? 386  LEU   B CA    1 
ATOM   11883 C  C     . LEU   B 1  388  ? -2.681  20.871  82.771  1.00 18.75 ? 386  LEU   B C     1 
ATOM   11884 O  O     . LEU   B 1  388  ? -3.416  21.846  82.587  1.00 17.63 ? 386  LEU   B O     1 
ATOM   11885 C  CB    . LEU   B 1  388  ? -1.119  20.327  84.706  1.00 17.32 ? 386  LEU   B CB    1 
ATOM   11886 C  CG    . LEU   B 1  388  ? 0.347   20.376  85.120  1.00 16.66 ? 386  LEU   B CG    1 
ATOM   11887 C  CD1   . LEU   B 1  388  ? 0.585   19.686  86.468  1.00 20.38 ? 386  LEU   B CD1   1 
ATOM   11888 C  CD2   . LEU   B 1  388  ? 1.302   19.814  84.048  1.00 20.08 ? 386  LEU   B CD2   1 
ATOM   11889 N  N     . ALA   B 1  389  ? -3.043  19.629  82.462  1.00 18.85 ? 387  ALA   B N     1 
ATOM   11890 C  CA    . ALA   B 1  389  ? -4.231  19.404  81.643  1.00 18.71 ? 387  ALA   B CA    1 
ATOM   11891 C  C     . ALA   B 1  389  ? -5.497  19.853  82.356  1.00 17.75 ? 387  ALA   B C     1 
ATOM   11892 O  O     . ALA   B 1  389  ? -6.436  20.354  81.724  1.00 21.27 ? 387  ALA   B O     1 
ATOM   11893 C  CB    . ALA   B 1  389  ? -4.339  17.927  81.270  1.00 21.80 ? 387  ALA   B CB    1 
ATOM   11894 N  N     . ASP   B 1  390  ? -5.540  19.686  83.666  1.00 19.09 ? 388  ASP   B N     1 
ATOM   11895 C  CA    . ASP   B 1  390  ? -6.711  20.042  84.449  1.00 18.79 ? 388  ASP   B CA    1 
ATOM   11896 C  C     . ASP   B 1  390  ? -6.240  20.147  85.888  1.00 15.79 ? 388  ASP   B C     1 
ATOM   11897 O  O     . ASP   B 1  390  ? -5.060  19.954  86.190  1.00 17.49 ? 388  ASP   B O     1 
ATOM   11898 C  CB    . ASP   B 1  390  ? -7.813  18.983  84.285  1.00 17.66 ? 388  ASP   B CB    1 
ATOM   11899 C  CG    . ASP   B 1  390  ? -9.213  19.547  84.454  1.00 21.70 ? 388  ASP   B CG    1 
ATOM   11900 O  OD1   . ASP   B 1  390  ? -9.458  20.305  85.411  1.00 19.49 ? 388  ASP   B OD1   1 
ATOM   11901 O  OD2   . ASP   B 1  390  ? -10.076 19.216  83.614  1.00 23.91 ? 388  ASP   B OD2   1 
ATOM   11902 N  N     . PHE   B 1  391  ? -7.157  20.433  86.756  1.00 17.44 ? 389  PHE   B N     1 
ATOM   11903 C  CA    . PHE   B 1  391  ? -6.846  20.454  88.172  1.00 16.52 ? 389  PHE   B CA    1 
ATOM   11904 C  C     . PHE   B 1  391  ? -6.949  19.055  88.758  1.00 16.44 ? 389  PHE   B C     1 
ATOM   11905 O  O     . PHE   B 1  391  ? -7.674  18.208  88.237  1.00 17.49 ? 389  PHE   B O     1 
ATOM   11906 C  CB    . PHE   B 1  391  ? -7.832  21.368  88.887  1.00 17.14 ? 389  PHE   B CB    1 
ATOM   11907 C  CG    . PHE   B 1  391  ? -7.814  22.756  88.339  1.00 15.88 ? 389  PHE   B CG    1 
ATOM   11908 C  CD1   . PHE   B 1  391  ? -6.747  23.586  88.634  1.00 15.84 ? 389  PHE   B CD1   1 
ATOM   11909 C  CD2   . PHE   B 1  391  ? -8.786  23.195  87.448  1.00 17.84 ? 389  PHE   B CD2   1 
ATOM   11910 C  CE1   . PHE   B 1  391  ? -6.674  24.851  88.109  1.00 16.28 ? 389  PHE   B CE1   1 
ATOM   11911 C  CE2   . PHE   B 1  391  ? -8.722  24.480  86.921  1.00 17.79 ? 389  PHE   B CE2   1 
ATOM   11912 C  CZ    . PHE   B 1  391  ? -7.667  25.302  87.245  1.00 16.57 ? 389  PHE   B CZ    1 
ATOM   11913 N  N     . PRO   B 1  392  ? -6.223  18.787  89.842  1.00 15.77 ? 390  PRO   B N     1 
ATOM   11914 C  CA    . PRO   B 1  392  ? -6.372  17.515  90.553  1.00 14.40 ? 390  PRO   B CA    1 
ATOM   11915 C  C     . PRO   B 1  392  ? -7.442  17.574  91.627  1.00 16.74 ? 390  PRO   B C     1 
ATOM   11916 O  O     . PRO   B 1  392  ? -7.618  16.602  92.365  1.00 17.40 ? 390  PRO   B O     1 
ATOM   11917 C  CB    . PRO   B 1  392  ? -4.988  17.365  91.196  1.00 17.10 ? 390  PRO   B CB    1 
ATOM   11918 C  CG    . PRO   B 1  392  ? -4.631  18.780  91.564  1.00 16.84 ? 390  PRO   B CG    1 
ATOM   11919 C  CD    . PRO   B 1  392  ? -5.164  19.629  90.428  1.00 14.93 ? 390  PRO   B CD    1 
ATOM   11920 N  N     . VAL   B 1  393  ? -8.124  18.706  91.720  1.00 15.97 ? 391  VAL   B N     1 
ATOM   11921 C  CA    . VAL   B 1  393  ? -9.225  18.916  92.643  1.00 16.25 ? 391  VAL   B CA    1 
ATOM   11922 C  C     . VAL   B 1  393  ? -10.402 19.461  91.851  1.00 16.48 ? 391  VAL   B C     1 
ATOM   11923 O  O     . VAL   B 1  393  ? -10.256 19.938  90.722  1.00 17.63 ? 391  VAL   B O     1 
ATOM   11924 C  CB    . VAL   B 1  393  ? -8.849  19.887  93.786  1.00 16.71 ? 391  VAL   B CB    1 
ATOM   11925 C  CG1   . VAL   B 1  393  ? -7.745  19.294  94.645  1.00 17.05 ? 391  VAL   B CG1   1 
ATOM   11926 C  CG2   . VAL   B 1  393  ? -8.410  21.248  93.220  1.00 18.01 ? 391  VAL   B CG2   1 
ATOM   11927 N  N     . PHE   B 1  394  ? -11.583 19.379  92.462  1.00 16.50 ? 392  PHE   B N     1 
ATOM   11928 C  CA    . PHE   B 1  394  ? -12.762 19.998  91.886  1.00 16.71 ? 392  PHE   B CA    1 
ATOM   11929 C  C     . PHE   B 1  394  ? -12.659 21.515  91.979  1.00 17.73 ? 392  PHE   B C     1 
ATOM   11930 O  O     . PHE   B 1  394  ? -11.874 22.067  92.757  1.00 17.44 ? 392  PHE   B O     1 
ATOM   11931 C  CB    . PHE   B 1  394  ? -14.022 19.469  92.571  1.00 16.43 ? 392  PHE   B CB    1 
ATOM   11932 C  CG    . PHE   B 1  394  ? -14.154 17.991  92.439  1.00 16.76 ? 392  PHE   B CG    1 
ATOM   11933 C  CD1   . PHE   B 1  394  ? -14.389 17.422  91.196  1.00 18.69 ? 392  PHE   B CD1   1 
ATOM   11934 C  CD2   . PHE   B 1  394  ? -13.960 17.163  93.526  1.00 17.03 ? 392  PHE   B CD2   1 
ATOM   11935 C  CE1   . PHE   B 1  394  ? -14.458 16.058  91.052  1.00 20.15 ? 392  PHE   B CE1   1 
ATOM   11936 C  CE2   . PHE   B 1  394  ? -14.019 15.798  93.389  1.00 16.76 ? 392  PHE   B CE2   1 
ATOM   11937 C  CZ    . PHE   B 1  394  ? -14.265 15.243  92.144  1.00 17.98 ? 392  PHE   B CZ    1 
ATOM   11938 N  N     . THR   B 1  395  ? -13.433 22.192  91.130  1.00 18.48 ? 393  THR   B N     1 
ATOM   11939 C  CA    . THR   B 1  395  ? -13.426 23.646  91.090  1.00 17.25 ? 393  THR   B CA    1 
ATOM   11940 C  C     . THR   B 1  395  ? -14.721 24.272  91.574  1.00 16.07 ? 393  THR   B C     1 
ATOM   11941 O  O     . THR   B 1  395  ? -14.746 25.486  91.782  1.00 20.12 ? 393  THR   B O     1 
ATOM   11942 C  CB    . THR   B 1  395  ? -13.117 24.176  89.684  1.00 18.23 ? 393  THR   B CB    1 
ATOM   11943 O  OG1   . THR   B 1  395  ? -14.125 23.722  88.771  1.00 18.65 ? 393  THR   B OG1   1 
ATOM   11944 C  CG2   . THR   B 1  395  ? -11.747 23.710  89.216  1.00 17.88 ? 393  THR   B CG2   1 
ATOM   11945 N  N     . ARG   B 1  396  ? -15.786 23.493  91.738  1.00 17.77 ? 394  ARG   B N     1 
ATOM   11946 C  CA    . ARG   B 1  396  ? -17.008 23.959  92.380  1.00 19.40 ? 394  ARG   B CA    1 
ATOM   11947 C  C     . ARG   B 1  396  ? -17.103 23.295  93.736  1.00 18.60 ? 394  ARG   B C     1 
ATOM   11948 O  O     . ARG   B 1  396  ? -16.937 22.077  93.856  1.00 19.55 ? 394  ARG   B O     1 
ATOM   11949 C  CB    . ARG   B 1  396  ? -18.258 23.633  91.562  1.00 19.05 ? 394  ARG   B CB    1 
ATOM   11950 C  CG    . ARG   B 1  396  ? -18.254 24.281  90.205  1.00 22.15 ? 394  ARG   B CG    1 
ATOM   11951 C  CD    . ARG   B 1  396  ? -19.625 24.157  89.539  1.00 22.39 ? 394  ARG   B CD    1 
ATOM   11952 N  NE    . ARG   B 1  396  ? -19.560 24.648  88.168  1.00 25.83 ? 394  ARG   B NE    1 
ATOM   11953 C  CZ    . ARG   B 1  396  ? -20.405 25.517  87.628  1.00 29.47 ? 394  ARG   B CZ    1 
ATOM   11954 N  NH1   . ARG   B 1  396  ? -21.450 25.976  88.300  1.00 28.89 ? 394  ARG   B NH1   1 
ATOM   11955 N  NH2   . ARG   B 1  396  ? -20.209 25.917  86.373  1.00 28.12 ? 394  ARG   B NH2   1 
ATOM   11956 N  N     . LYS   B 1  397  ? -17.382 24.097  94.758  1.00 19.60 ? 395  LYS   B N     1 
ATOM   11957 C  CA    . LYS   B 1  397  ? -17.430 23.558  96.108  1.00 20.50 ? 395  LYS   B CA    1 
ATOM   11958 C  C     . LYS   B 1  397  ? -18.485 22.459  96.225  1.00 20.60 ? 395  LYS   B C     1 
ATOM   11959 O  O     . LYS   B 1  397  ? -18.275 21.448  96.905  1.00 20.62 ? 395  LYS   B O     1 
ATOM   11960 C  CB    . LYS   B 1  397  ? -17.686 24.707  97.077  1.00 23.95 ? 395  LYS   B CB    1 
ATOM   11961 C  CG    . LYS   B 1  397  ? -17.368 24.407  98.509  1.00 24.83 ? 395  LYS   B CG    1 
ATOM   11962 C  CD    . LYS   B 1  397  ? -18.568 23.888  99.223  1.00 28.02 ? 395  LYS   B CD    1 
ATOM   11963 C  CE    . LYS   B 1  397  ? -18.247 23.638  100.675 1.00 24.78 ? 395  LYS   B CE    1 
ATOM   11964 N  NZ    . LYS   B 1  397  ? -19.450 23.089  101.341 1.00 23.23 ? 395  LYS   B NZ    1 
ATOM   11965 N  N     . ILE   B 1  398  ? -19.609 22.619  95.528  1.00 20.16 ? 396  ILE   B N     1 
ATOM   11966 C  CA    . ILE   B 1  398  ? -20.656 21.609  95.580  1.00 24.00 ? 396  ILE   B CA    1 
ATOM   11967 C  C     . ILE   B 1  398  ? -20.171 20.272  95.023  1.00 19.68 ? 396  ILE   B C     1 
ATOM   11968 O  O     . ILE   B 1  398  ? -20.647 19.207  95.436  1.00 21.71 ? 396  ILE   B O     1 
ATOM   11969 C  CB    . ILE   B 1  398  ? -21.904 22.147  94.861  1.00 28.17 ? 396  ILE   B CB    1 
ATOM   11970 C  CG1   . ILE   B 1  398  ? -23.122 21.334  95.244  1.00 33.30 ? 396  ILE   B CG1   1 
ATOM   11971 C  CG2   . ILE   B 1  398  ? -21.701 22.145  93.361  1.00 25.42 ? 396  ILE   B CG2   1 
ATOM   11972 C  CD1   . ILE   B 1  398  ? -24.402 22.028  94.909  1.00 36.28 ? 396  ILE   B CD1   1 
ATOM   11973 N  N     . HIS   B 1  399  ? -19.181 20.295  94.123  1.00 20.30 ? 397  HIS   B N     1 
ATOM   11974 C  CA    . HIS   B 1  399  ? -18.635 19.043  93.607  1.00 20.57 ? 397  HIS   B CA    1 
ATOM   11975 C  C     . HIS   B 1  399  ? -17.861 18.301  94.680  1.00 18.29 ? 397  HIS   B C     1 
ATOM   11976 O  O     . HIS   B 1  399  ? -17.960 17.076  94.796  1.00 20.47 ? 397  HIS   B O     1 
ATOM   11977 C  CB    . HIS   B 1  399  ? -17.734 19.331  92.418  1.00 20.03 ? 397  HIS   B CB    1 
ATOM   11978 C  CG    . HIS   B 1  399  ? -18.483 19.825  91.229  1.00 20.86 ? 397  HIS   B CG    1 
ATOM   11979 N  ND1   . HIS   B 1  399  ? -17.861 20.357  90.123  1.00 22.51 ? 397  HIS   B ND1   1 
ATOM   11980 C  CD2   . HIS   B 1  399  ? -19.814 19.868  90.978  1.00 23.24 ? 397  HIS   B CD2   1 
ATOM   11981 C  CE1   . HIS   B 1  399  ? -18.778 20.703  89.235  1.00 22.01 ? 397  HIS   B CE1   1 
ATOM   11982 N  NE2   . HIS   B 1  399  ? -19.970 20.415  89.728  1.00 22.62 ? 397  HIS   B NE2   1 
ATOM   11983 N  N     . THR   B 1  400  ? -17.071 19.027  95.460  1.00 19.18 ? 398  THR   B N     1 
ATOM   11984 C  CA    . THR   B 1  400  ? -16.395 18.408  96.585  1.00 19.05 ? 398  THR   B CA    1 
ATOM   11985 C  C     . THR   B 1  400  ? -17.396 17.822  97.568  1.00 17.82 ? 398  THR   B C     1 
ATOM   11986 O  O     . THR   B 1  400  ? -17.182 16.733  98.111  1.00 19.76 ? 398  THR   B O     1 
ATOM   11987 C  CB    . THR   B 1  400  ? -15.505 19.448  97.248  1.00 18.86 ? 398  THR   B CB    1 
ATOM   11988 O  OG1   . THR   B 1  400  ? -14.409 19.710  96.369  1.00 17.61 ? 398  THR   B OG1   1 
ATOM   11989 C  CG2   . THR   B 1  400  ? -14.979 18.933  98.563  1.00 20.06 ? 398  THR   B CG2   1 
ATOM   11990 N  N     . ASP   B 1  401  ? -18.514 18.522  97.787  1.00 19.49 ? 399  ASP   B N     1 
ATOM   11991 C  CA    . ASP   B 1  401  ? -19.533 18.017  98.701  1.00 22.24 ? 399  ASP   B CA    1 
ATOM   11992 C  C     . ASP   B 1  401  ? -20.140 16.722  98.183  1.00 19.12 ? 399  ASP   B C     1 
ATOM   11993 O  O     . ASP   B 1  401  ? -20.323 15.768  98.943  1.00 21.97 ? 399  ASP   B O     1 
ATOM   11994 C  CB    . ASP   B 1  401  ? -20.627 19.068  98.890  1.00 24.43 ? 399  ASP   B CB    1 
ATOM   11995 C  CG    . ASP   B 1  401  ? -20.174 20.239  99.744  1.00 27.65 ? 399  ASP   B CG    1 
ATOM   11996 O  OD1   . ASP   B 1  401  ? -19.210 20.077  100.529 1.00 26.34 ? 399  ASP   B OD1   1 
ATOM   11997 O  OD2   . ASP   B 1  401  ? -20.793 21.319  99.648  1.00 27.96 ? 399  ASP   B OD2   1 
ATOM   11998 N  N     . VAL   B 1  402  ? -20.448 16.666  96.885  1.00 20.51 ? 400  VAL   B N     1 
ATOM   11999 C  CA    . VAL   B 1  402  ? -20.970 15.433  96.306  1.00 22.18 ? 400  VAL   B CA    1 
ATOM   12000 C  C     . VAL   B 1  402  ? -19.925 14.337  96.372  1.00 18.06 ? 400  VAL   B C     1 
ATOM   12001 O  O     . VAL   B 1  402  ? -20.230 13.185  96.701  1.00 21.09 ? 400  VAL   B O     1 
ATOM   12002 C  CB    . VAL   B 1  402  ? -21.438 15.680  94.862  1.00 20.36 ? 400  VAL   B CB    1 
ATOM   12003 C  CG1   . VAL   B 1  402  ? -21.797 14.363  94.179  1.00 24.51 ? 400  VAL   B CG1   1 
ATOM   12004 C  CG2   . VAL   B 1  402  ? -22.618 16.642  94.867  1.00 21.65 ? 400  VAL   B CG2   1 
ATOM   12005 N  N     . SER   B 1  403  ? -18.673 14.681  96.063  1.00 18.98 ? 401  SER   B N     1 
ATOM   12006 C  CA    . SER   B 1  403  ? -17.599 13.701  96.137  1.00 22.12 ? 401  SER   B CA    1 
ATOM   12007 C  C     . SER   B 1  403  ? -17.475 13.134  97.544  1.00 18.01 ? 401  SER   B C     1 
ATOM   12008 O  O     . SER   B 1  403  ? -17.316 11.924  97.727  1.00 19.62 ? 401  SER   B O     1 
ATOM   12009 C  CB    . SER   B 1  403  ? -16.287 14.364  95.722  1.00 18.72 ? 401  SER   B CB    1 
ATOM   12010 O  OG    . SER   B 1  403  ? -15.206 13.469  95.904  1.00 19.44 ? 401  SER   B OG    1 
ATOM   12011 N  N     . TYR   B 1  404  ? -17.588 13.996  98.552  1.00 19.89 ? 402  TYR   B N     1 
ATOM   12012 C  CA    . TYR   B 1  404  ? -17.495 13.543  99.933  1.00 21.45 ? 402  TYR   B CA    1 
ATOM   12013 C  C     . TYR   B 1  404  ? -18.599 12.542  100.248 1.00 20.01 ? 402  TYR   B C     1 
ATOM   12014 O  O     . TYR   B 1  404  ? -18.345 11.467  100.803 1.00 21.60 ? 402  TYR   B O     1 
ATOM   12015 C  CB    . TYR   B 1  404  ? -17.565 14.756  100.860 1.00 21.59 ? 402  TYR   B CB    1 
ATOM   12016 C  CG    . TYR   B 1  404  ? -17.204 14.465  102.294 1.00 20.53 ? 402  TYR   B CG    1 
ATOM   12017 C  CD1   . TYR   B 1  404  ? -18.130 13.896  103.163 1.00 21.21 ? 402  TYR   B CD1   1 
ATOM   12018 C  CD2   . TYR   B 1  404  ? -15.938 14.767  102.782 1.00 21.06 ? 402  TYR   B CD2   1 
ATOM   12019 C  CE1   . TYR   B 1  404  ? -17.802 13.645  104.480 1.00 20.92 ? 402  TYR   B CE1   1 
ATOM   12020 C  CE2   . TYR   B 1  404  ? -15.602 14.515  104.084 1.00 20.63 ? 402  TYR   B CE2   1 
ATOM   12021 C  CZ    . TYR   B 1  404  ? -16.532 13.954  104.930 1.00 23.07 ? 402  TYR   B CZ    1 
ATOM   12022 O  OH    . TYR   B 1  404  ? -16.195 13.701  106.236 1.00 22.89 ? 402  TYR   B OH    1 
ATOM   12023 N  N     . ILE   B 1  405  ? -19.836 12.868  99.872  1.00 21.81 ? 403  ILE   B N     1 
ATOM   12024 C  CA    . ILE   B 1  405  ? -20.955 11.984  100.174 1.00 23.66 ? 403  ILE   B CA    1 
ATOM   12025 C  C     . ILE   B 1  405  ? -20.832 10.668  99.412  1.00 20.74 ? 403  ILE   B C     1 
ATOM   12026 O  O     . ILE   B 1  405  ? -21.109 9.593   99.954  1.00 24.01 ? 403  ILE   B O     1 
ATOM   12027 C  CB    . ILE   B 1  405  ? -22.280 12.718  99.905  1.00 24.19 ? 403  ILE   B CB    1 
ATOM   12028 C  CG1   . ILE   B 1  405  ? -22.414 13.896  100.868 1.00 27.34 ? 403  ILE   B CG1   1 
ATOM   12029 C  CG2   . ILE   B 1  405  ? -23.457 11.782  100.073 1.00 23.28 ? 403  ILE   B CG2   1 
ATOM   12030 C  CD1   . ILE   B 1  405  ? -23.408 14.934  100.432 1.00 35.36 ? 403  ILE   B CD1   1 
ATOM   12031 N  N     . ALA   B 1  406  ? -20.394 10.731  98.148  1.00 21.74 ? 404  ALA   B N     1 
ATOM   12032 C  CA    . ALA   B 1  406  ? -20.176 9.514   97.370  1.00 25.38 ? 404  ALA   B CA    1 
ATOM   12033 C  C     . ALA   B 1  406  ? -19.086 8.655   97.986  1.00 21.08 ? 404  ALA   B C     1 
ATOM   12034 O  O     . ALA   B 1  406  ? -19.193 7.424   98.025  1.00 23.83 ? 404  ALA   B O     1 
ATOM   12035 C  CB    . ALA   B 1  406  ? -19.795 9.878   95.935  1.00 23.66 ? 404  ALA   B CB    1 
ATOM   12036 N  N     . CYS   B 1  407  ? -18.017 9.287   98.465  1.00 21.83 ? 405  CYS   B N     1 
ATOM   12037 C  CA    . CYS   B 1  407  ? -16.954 8.529   99.108  1.00 22.90 ? 405  CYS   B CA    1 
ATOM   12038 C  C     . CYS   B 1  407  ? -17.389 8.004   100.471 1.00 21.21 ? 405  CYS   B C     1 
ATOM   12039 O  O     . CYS   B 1  407  ? -16.967 6.917   100.878 1.00 24.06 ? 405  CYS   B O     1 
ATOM   12040 C  CB    . CYS   B 1  407  ? -15.696 9.386   99.188  1.00 20.12 ? 405  CYS   B CB    1 
ATOM   12041 S  SG    . CYS   B 1  407  ? -14.962 9.627   97.535  1.00 25.54 ? 405  CYS   B SG    1 
ATOM   12042 N  N     . ALA   B 1  408  ? -18.251 8.743   101.173 1.00 19.69 ? 406  ALA   B N     1 
ATOM   12043 C  CA    . ALA   B 1  408  ? -18.804 8.228   102.418 1.00 22.67 ? 406  ALA   B CA    1 
ATOM   12044 C  C     . ALA   B 1  408  ? -19.645 6.991   102.159 1.00 22.09 ? 406  ALA   B C     1 
ATOM   12045 O  O     . ALA   B 1  408  ? -19.585 6.022   102.920 1.00 24.59 ? 406  ALA   B O     1 
ATOM   12046 C  CB    . ALA   B 1  408  ? -19.634 9.308   103.108 1.00 24.79 ? 406  ALA   B CB    1 
ATOM   12047 N  N     . ALA   B 1  409  ? -20.409 6.991   101.063 1.00 24.59 ? 407  ALA   B N     1 
ATOM   12048 C  CA    . ALA   B 1  409  ? -21.187 5.807   100.726 1.00 26.00 ? 407  ALA   B CA    1 
ATOM   12049 C  C     . ALA   B 1  409  ? -20.283 4.598   100.538 1.00 24.80 ? 407  ALA   B C     1 
ATOM   12050 O  O     . ALA   B 1  409  ? -20.589 3.502   101.018 1.00 29.66 ? 407  ALA   B O     1 
ATOM   12051 C  CB    . ALA   B 1  409  ? -22.025 6.071   99.476  1.00 24.56 ? 407  ALA   B CB    1 
ATOM   12052 N  N     . LYS   B 1  410  ? -19.153 4.789   99.859  1.00 23.82 ? 408  LYS   B N     1 
ATOM   12053 C  CA    . LYS   B 1  410  ? -18.226 3.688   99.648  1.00 22.23 ? 408  LYS   B CA    1 
ATOM   12054 C  C     . LYS   B 1  410  ? -17.613 3.243   100.965 1.00 26.58 ? 408  LYS   B C     1 
ATOM   12055 O  O     . LYS   B 1  410  ? -17.480 2.041   101.224 1.00 27.96 ? 408  LYS   B O     1 
ATOM   12056 C  CB    . LYS   B 1  410  ? -17.130 4.132   98.677  1.00 23.45 ? 408  LYS   B CB    1 
ATOM   12057 C  CG    . LYS   B 1  410  ? -16.096 3.059   98.355  1.00 25.59 ? 408  LYS   B CG    1 
ATOM   12058 C  CD    . LYS   B 1  410  ? -14.927 3.609   97.552  1.00 27.20 ? 408  LYS   B CD    1 
ATOM   12059 C  CE    . LYS   B 1  410  ? -15.324 4.078   96.162  1.00 28.13 ? 408  LYS   B CE    1 
ATOM   12060 N  NZ    . LYS   B 1  410  ? -15.636 2.939   95.244  1.00 29.64 ? 408  LYS   B NZ    1 
ATOM   12061 N  N     . LEU   B 1  411  ? -17.229 4.207   101.804 1.00 24.97 ? 409  LEU   B N     1 
ATOM   12062 C  CA    . LEU   B 1  411  ? -16.678 3.871   103.110 1.00 25.46 ? 409  LEU   B CA    1 
ATOM   12063 C  C     . LEU   B 1  411  ? -17.703 3.160   103.978 1.00 24.81 ? 409  LEU   B C     1 
ATOM   12064 O  O     . LEU   B 1  411  ? -17.380 2.159   104.622 1.00 25.36 ? 409  LEU   B O     1 
ATOM   12065 C  CB    . LEU   B 1  411  ? -16.165 5.131   103.797 1.00 22.83 ? 409  LEU   B CB    1 
ATOM   12066 C  CG    . LEU   B 1  411  ? -14.804 5.568   103.264 1.00 24.66 ? 409  LEU   B CG    1 
ATOM   12067 C  CD1   . LEU   B 1  411  ? -14.471 6.964   103.752 1.00 24.51 ? 409  LEU   B CD1   1 
ATOM   12068 C  CD2   . LEU   B 1  411  ? -13.735 4.580   103.697 1.00 24.49 ? 409  LEU   B CD2   1 
ATOM   12069 N  N     . LEU   B 1  412  ? -18.946 3.657   104.003 1.00 26.81 ? 410  LEU   B N     1 
ATOM   12070 C  CA    . LEU   B 1  412  ? -19.958 3.054   104.867 1.00 25.70 ? 410  LEU   B CA    1 
ATOM   12071 C  C     . LEU   B 1  412  ? -20.309 1.641   104.426 1.00 27.51 ? 410  LEU   B C     1 
ATOM   12072 O  O     . LEU   B 1  412  ? -20.715 0.820   105.253 1.00 32.27 ? 410  LEU   B O     1 
ATOM   12073 C  CB    . LEU   B 1  412  ? -21.206 3.937   104.945 1.00 30.09 ? 410  LEU   B CB    1 
ATOM   12074 C  CG    . LEU   B 1  412  ? -21.024 5.201   105.790 1.00 28.22 ? 410  LEU   B CG    1 
ATOM   12075 C  CD1   . LEU   B 1  412  ? -22.172 6.169   105.588 1.00 32.99 ? 410  LEU   B CD1   1 
ATOM   12076 C  CD2   . LEU   B 1  412  ? -20.875 4.840   107.259 1.00 28.84 ? 410  LEU   B CD2   1 
ATOM   12077 N  N     . ALA   B 1  413  ? -20.161 1.335   103.139 1.00 26.70 ? 411  ALA   B N     1 
ATOM   12078 C  CA    . ALA   B 1  413  ? -20.363 -0.033  102.688 1.00 30.95 ? 411  ALA   B CA    1 
ATOM   12079 C  C     . ALA   B 1  413  ? -19.173 -0.927  102.999 1.00 31.15 ? 411  ALA   B C     1 
ATOM   12080 O  O     . ALA   B 1  413  ? -19.244 -2.136  102.759 1.00 31.32 ? 411  ALA   B O     1 
ATOM   12081 C  CB    . ALA   B 1  413  ? -20.661 -0.058  101.189 1.00 29.53 ? 411  ALA   B CB    1 
ATOM   12082 N  N     . ALA   B 1  414  ? -18.091 -0.369  103.544 1.00 28.28 ? 412  ALA   B N     1 
ATOM   12083 C  CA    . ALA   B 1  414  ? -16.882 -1.133  103.814 1.00 25.61 ? 412  ALA   B CA    1 
ATOM   12084 C  C     . ALA   B 1  414  ? -16.462 -1.069  105.281 1.00 30.22 ? 412  ALA   B C     1 
ATOM   12085 O  O     . ALA   B 1  414  ? -15.283 -1.270  105.585 1.00 27.50 ? 412  ALA   B O     1 
ATOM   12086 C  CB    . ALA   B 1  414  ? -15.740 -0.665  102.908 1.00 27.11 ? 412  ALA   B CB    1 
ATOM   12087 N  N     . THR   B 1  415  ? -17.395 -0.799  106.204 1.00 26.98 ? 413  THR   B N     1 
ATOM   12088 C  CA    . THR   B 1  415  ? -17.009 -0.663  107.609 1.00 26.60 ? 413  THR   B CA    1 
ATOM   12089 C  C     . THR   B 1  415  ? -16.494 -1.968  108.189 1.00 29.46 ? 413  THR   B C     1 
ATOM   12090 O  O     . THR   B 1  415  ? -15.840 -1.957  109.238 1.00 28.85 ? 413  THR   B O     1 
ATOM   12091 C  CB    . THR   B 1  415  ? -18.173 -0.160  108.459 1.00 27.10 ? 413  THR   B CB    1 
ATOM   12092 O  OG1   . THR   B 1  415  ? -19.230 -1.123  108.418 1.00 31.78 ? 413  THR   B OG1   1 
ATOM   12093 C  CG2   . THR   B 1  415  ? -18.680 1.165   107.940 1.00 28.89 ? 413  THR   B CG2   1 
ATOM   12094 N  N     . ASP   B 1  416  ? -16.785 -3.096  107.542 1.00 29.89 ? 414  ASP   B N     1 
ATOM   12095 C  CA    . ASP   B 1  416  ? -16.185 -4.356  107.952 1.00 32.46 ? 414  ASP   B CA    1 
ATOM   12096 C  C     . ASP   B 1  416  ? -14.701 -4.418  107.624 1.00 28.63 ? 414  ASP   B C     1 
ATOM   12097 O  O     . ASP   B 1  416  ? -14.005 -5.294  108.143 1.00 32.30 ? 414  ASP   B O     1 
ATOM   12098 C  CB    . ASP   B 1  416  ? -16.922 -5.524  107.284 1.00 27.51 ? 414  ASP   B CB    1 
ATOM   12099 C  CG    . ASP   B 1  416  ? -17.078 -5.337  105.772 1.00 42.43 ? 414  ASP   B CG    1 
ATOM   12100 O  OD1   . ASP   B 1  416  ? -17.406 -4.214  105.332 1.00 37.96 ? 414  ASP   B OD1   1 
ATOM   12101 O  OD2   . ASP   B 1  416  ? -16.875 -6.319  105.021 1.00 45.81 ? 414  ASP   B OD2   1 
ATOM   12102 N  N     . VAL   B 1  417  ? -14.197 -3.505  106.793 1.00 26.70 ? 415  VAL   B N     1 
ATOM   12103 C  CA    . VAL   B 1  417  ? -12.846 -3.613  106.253 1.00 24.63 ? 415  VAL   B CA    1 
ATOM   12104 C  C     . VAL   B 1  417  ? -11.992 -2.410  106.644 1.00 25.78 ? 415  VAL   B C     1 
ATOM   12105 O  O     . VAL   B 1  417  ? -10.775 -2.527  106.816 1.00 24.97 ? 415  VAL   B O     1 
ATOM   12106 C  CB    . VAL   B 1  417  ? -12.912 -3.777  104.726 1.00 31.12 ? 415  VAL   B CB    1 
ATOM   12107 C  CG1   . VAL   B 1  417  ? -11.530 -3.848  104.139 1.00 27.34 ? 415  VAL   B CG1   1 
ATOM   12108 C  CG2   . VAL   B 1  417  ? -13.716 -5.023  104.377 1.00 29.69 ? 415  VAL   B CG2   1 
ATOM   12109 N  N     . VAL   B 1  418  ? -12.614 -1.239  106.742 1.00 24.16 ? 416  VAL   B N     1 
ATOM   12110 C  CA    . VAL   B 1  418  ? -11.926 -0.020  107.135 1.00 22.07 ? 416  VAL   B CA    1 
ATOM   12111 C  C     . VAL   B 1  418  ? -12.769 0.662   108.197 1.00 24.65 ? 416  VAL   B C     1 
ATOM   12112 O  O     . VAL   B 1  418  ? -13.947 0.353   108.386 1.00 23.33 ? 416  VAL   B O     1 
ATOM   12113 C  CB    . VAL   B 1  418  ? -11.684 0.945   105.958 1.00 23.23 ? 416  VAL   B CB    1 
ATOM   12114 C  CG1   . VAL   B 1  418  ? -10.716 0.335   104.953 1.00 23.12 ? 416  VAL   B CG1   1 
ATOM   12115 C  CG2   . VAL   B 1  418  ? -13.017 1.321   105.290 1.00 22.54 ? 416  VAL   B CG2   1 
ATOM   12116 N  N     . PHE   B 1  419  ? -12.142 1.601   108.898 1.00 22.42 ? 417  PHE   B N     1 
ATOM   12117 C  CA    . PHE   B 1  419  ? -12.829 2.365   109.930 1.00 20.88 ? 417  PHE   B CA    1 
ATOM   12118 C  C     . PHE   B 1  419  ? -13.016 3.778   109.410 1.00 21.22 ? 417  PHE   B C     1 
ATOM   12119 O  O     . PHE   B 1  419  ? -12.067 4.581   109.434 1.00 19.96 ? 417  PHE   B O     1 
ATOM   12120 C  CB    . PHE   B 1  419  ? -12.003 2.382   111.215 1.00 20.83 ? 417  PHE   B CB    1 
ATOM   12121 C  CG    . PHE   B 1  419  ? -12.602 3.219   112.304 1.00 23.68 ? 417  PHE   B CG    1 
ATOM   12122 C  CD1   . PHE   B 1  419  ? -13.875 2.949   112.777 1.00 25.18 ? 417  PHE   B CD1   1 
ATOM   12123 C  CD2   . PHE   B 1  419  ? -11.887 4.264   112.865 1.00 23.16 ? 417  PHE   B CD2   1 
ATOM   12124 C  CE1   . PHE   B 1  419  ? -14.434 3.713   113.785 1.00 24.99 ? 417  PHE   B CE1   1 
ATOM   12125 C  CE2   . PHE   B 1  419  ? -12.435 5.032   113.881 1.00 23.38 ? 417  PHE   B CE2   1 
ATOM   12126 C  CZ    . PHE   B 1  419  ? -13.711 4.760   114.339 1.00 22.82 ? 417  PHE   B CZ    1 
ATOM   12127 N  N     . PRO   B 1  420  ? -14.200 4.136   108.928 1.00 19.94 ? 418  PRO   B N     1 
ATOM   12128 C  CA    . PRO   B 1  420  ? -14.380 5.464   108.340 1.00 21.64 ? 418  PRO   B CA    1 
ATOM   12129 C  C     . PRO   B 1  420  ? -14.463 6.530   109.416 1.00 19.90 ? 418  PRO   B C     1 
ATOM   12130 O  O     . PRO   B 1  420  ? -15.104 6.354   110.452 1.00 21.48 ? 418  PRO   B O     1 
ATOM   12131 C  CB    . PRO   B 1  420  ? -15.713 5.338   107.591 1.00 23.64 ? 418  PRO   B CB    1 
ATOM   12132 C  CG    . PRO   B 1  420  ? -15.929 3.864   107.434 1.00 23.01 ? 418  PRO   B CG    1 
ATOM   12133 C  CD    . PRO   B 1  420  ? -15.370 3.276   108.689 1.00 20.16 ? 418  PRO   B CD    1 
ATOM   12134 N  N     . GLN   B 1  421  ? -13.776 7.638   109.170 1.00 20.64 ? 419  GLN   B N     1 
ATOM   12135 C  CA    . GLN   B 1  421  ? -13.723 8.758   110.097 1.00 20.93 ? 419  GLN   B CA    1 
ATOM   12136 C  C     . GLN   B 1  421  ? -14.120 9.982   109.291 1.00 19.86 ? 419  GLN   B C     1 
ATOM   12137 O  O     . GLN   B 1  421  ? -13.365 10.437  108.431 1.00 19.26 ? 419  GLN   B O     1 
ATOM   12138 C  CB    . GLN   B 1  421  ? -12.315 8.906   110.660 1.00 20.61 ? 419  GLN   B CB    1 
ATOM   12139 C  CG    . GLN   B 1  421  ? -11.836 7.635   111.317 1.00 21.26 ? 419  GLN   B CG    1 
ATOM   12140 C  CD    . GLN   B 1  421  ? -10.346 7.632   111.543 1.00 20.38 ? 419  GLN   B CD    1 
ATOM   12141 O  OE1   . GLN   B 1  421  ? -9.570  7.752   110.607 1.00 22.46 ? 419  GLN   B OE1   1 
ATOM   12142 N  NE2   . GLN   B 1  421  ? -9.941  7.498   112.802 1.00 20.49 ? 419  GLN   B NE2   1 
ATOM   12143 N  N     . PHE   B 1  422  ? -15.314 10.505  109.535 1.00 21.19 ? 420  PHE   B N     1 
ATOM   12144 C  CA    . PHE   B 1  422  ? -15.854 11.558  108.682 1.00 19.71 ? 420  PHE   B CA    1 
ATOM   12145 C  C     . PHE   B 1  422  ? -15.551 12.918  109.286 1.00 21.02 ? 420  PHE   B C     1 
ATOM   12146 O  O     . PHE   B 1  422  ? -16.279 13.405  110.155 1.00 21.06 ? 420  PHE   B O     1 
ATOM   12147 C  CB    . PHE   B 1  422  ? -17.340 11.334  108.449 1.00 18.65 ? 420  PHE   B CB    1 
ATOM   12148 C  CG    . PHE   B 1  422  ? -17.638 10.030  107.782 1.00 21.99 ? 420  PHE   B CG    1 
ATOM   12149 C  CD1   . PHE   B 1  422  ? -17.253 9.819   106.475 1.00 23.92 ? 420  PHE   B CD1   1 
ATOM   12150 C  CD2   . PHE   B 1  422  ? -18.281 9.015   108.461 1.00 22.27 ? 420  PHE   B CD2   1 
ATOM   12151 C  CE1   . PHE   B 1  422  ? -17.512 8.616   105.853 1.00 25.94 ? 420  PHE   B CE1   1 
ATOM   12152 C  CE2   . PHE   B 1  422  ? -18.539 7.806   107.837 1.00 23.80 ? 420  PHE   B CE2   1 
ATOM   12153 C  CZ    . PHE   B 1  422  ? -18.162 7.618   106.531 1.00 24.72 ? 420  PHE   B CZ    1 
ATOM   12154 N  N     . ALA   B 1  423  ? -14.468 13.531  108.821 1.00 20.39 ? 421  ALA   B N     1 
ATOM   12155 C  CA    . ALA   B 1  423  ? -14.044 14.836  109.300 1.00 19.92 ? 421  ALA   B CA    1 
ATOM   12156 C  C     . ALA   B 1  423  ? -14.793 15.905  108.522 1.00 22.23 ? 421  ALA   B C     1 
ATOM   12157 O  O     . ALA   B 1  423  ? -14.559 16.088  107.325 1.00 24.80 ? 421  ALA   B O     1 
ATOM   12158 C  CB    . ALA   B 1  423  ? -12.542 14.993  109.089 1.00 18.91 ? 421  ALA   B CB    1 
ATOM   12159 N  N     . THR   B 1  424  ? -15.663 16.639  109.203 1.00 21.63 ? 422  THR   B N     1 
ATOM   12160 C  CA    . THR   B 1  424  ? -16.362 17.744  108.566 1.00 21.21 ? 422  THR   B CA    1 
ATOM   12161 C  C     . THR   B 1  424  ? -16.990 18.609  109.645 1.00 20.93 ? 422  THR   B C     1 
ATOM   12162 O  O     . THR   B 1  424  ? -17.389 18.113  110.705 1.00 23.38 ? 422  THR   B O     1 
ATOM   12163 C  CB    . THR   B 1  424  ? -17.449 17.254  107.592 1.00 24.90 ? 422  THR   B CB    1 
ATOM   12164 O  OG1   . THR   B 1  424  ? -18.089 18.384  106.994 1.00 23.95 ? 422  THR   B OG1   1 
ATOM   12165 C  CG2   . THR   B 1  424  ? -18.508 16.425  108.325 1.00 25.33 ? 422  THR   B CG2   1 
ATOM   12166 N  N     . HIS   B 1  425  ? -17.047 19.908  109.374 1.00 22.00 ? 423  HIS   B N     1 
ATOM   12167 C  CA    . HIS   B 1  425  ? -17.786 20.831  110.228 1.00 22.67 ? 423  HIS   B CA    1 
ATOM   12168 C  C     . HIS   B 1  425  ? -19.116 21.225  109.620 1.00 25.82 ? 423  HIS   B C     1 
ATOM   12169 O  O     . HIS   B 1  425  ? -19.813 22.073  110.181 1.00 26.68 ? 423  HIS   B O     1 
ATOM   12170 C  CB    . HIS   B 1  425  ? -16.956 22.082  110.495 1.00 22.73 ? 423  HIS   B CB    1 
ATOM   12171 C  CG    . HIS   B 1  425  ? -15.677 21.803  111.216 1.00 24.44 ? 423  HIS   B CG    1 
ATOM   12172 N  ND1   . HIS   B 1  425  ? -14.477 22.357  110.837 1.00 26.60 ? 423  HIS   B ND1   1 
ATOM   12173 C  CD2   . HIS   B 1  425  ? -15.412 21.026  112.294 1.00 23.83 ? 423  HIS   B CD2   1 
ATOM   12174 C  CE1   . HIS   B 1  425  ? -13.522 21.931  111.646 1.00 25.84 ? 423  HIS   B CE1   1 
ATOM   12175 N  NE2   . HIS   B 1  425  ? -14.062 21.121  112.538 1.00 22.98 ? 423  HIS   B NE2   1 
ATOM   12176 N  N     . ASN   B 1  426  ? -19.472 20.625  108.490 1.00 25.52 ? 424  ASN   B N     1 
ATOM   12177 C  CA    . ASN   B 1  426  ? -20.671 20.975  107.742 1.00 23.35 ? 424  ASN   B CA    1 
ATOM   12178 C  C     . ASN   B 1  426  ? -21.821 20.109  108.245 1.00 24.37 ? 424  ASN   B C     1 
ATOM   12179 O  O     . ASN   B 1  426  ? -21.802 18.883  108.090 1.00 23.39 ? 424  ASN   B O     1 
ATOM   12180 C  CB    . ASN   B 1  426  ? -20.397 20.727  106.260 1.00 24.51 ? 424  ASN   B CB    1 
ATOM   12181 C  CG    . ASN   B 1  426  ? -21.493 21.255  105.360 1.00 26.04 ? 424  ASN   B CG    1 
ATOM   12182 O  OD1   . ASN   B 1  426  ? -22.684 21.090  105.637 1.00 27.64 ? 424  ASN   B OD1   1 
ATOM   12183 N  ND2   . ASN   B 1  426  ? -21.091 21.885  104.256 1.00 25.96 ? 424  ASN   B ND2   1 
ATOM   12184 N  N     . ALA   B 1  427  ? -22.829 20.755  108.847 1.00 26.55 ? 425  ALA   B N     1 
ATOM   12185 C  CA    . ALA   B 1  427  ? -23.968 20.035  109.405 1.00 29.00 ? 425  ALA   B CA    1 
ATOM   12186 C  C     . ALA   B 1  427  ? -24.774 19.320  108.329 1.00 22.54 ? 425  ALA   B C     1 
ATOM   12187 O  O     . ALA   B 1  427  ? -25.353 18.258  108.593 1.00 26.93 ? 425  ALA   B O     1 
ATOM   12188 C  CB    . ALA   B 1  427  ? -24.865 21.004  110.173 1.00 29.93 ? 425  ALA   B CB    1 
ATOM   12189 N  N     . GLN   B 1  428  ? -24.813 19.870  107.114 1.00 26.23 ? 426  GLN   B N     1 
ATOM   12190 C  CA    . GLN   B 1  428  ? -25.512 19.179  106.038 1.00 29.12 ? 426  GLN   B CA    1 
ATOM   12191 C  C     . GLN   B 1  428  ? -24.769 17.912  105.637 1.00 25.65 ? 426  GLN   B C     1 
ATOM   12192 O  O     . GLN   B 1  428  ? -25.378 16.848  105.488 1.00 28.01 ? 426  GLN   B O     1 
ATOM   12193 C  CB    . GLN   B 1  428  ? -25.714 20.111  104.845 1.00 28.19 ? 426  GLN   B CB    1 
ATOM   12194 C  CG    . GLN   B 1  428  ? -26.740 19.607  103.828 1.00 31.29 ? 426  GLN   B CG    1 
ATOM   12195 C  CD    . GLN   B 1  428  ? -26.223 18.458  102.975 1.00 28.69 ? 426  GLN   B CD    1 
ATOM   12196 O  OE1   . GLN   B 1  428  ? -25.046 18.422  102.613 1.00 31.32 ? 426  GLN   B OE1   1 
ATOM   12197 N  NE2   . GLN   B 1  428  ? -27.098 17.501  102.671 1.00 30.99 ? 426  GLN   B NE2   1 
ATOM   12198 N  N     . THR   B 1  429  ? -23.444 18.003  105.486 1.00 27.23 ? 427  THR   B N     1 
ATOM   12199 C  CA    . THR   B 1  429  ? -22.651 16.816  105.187 1.00 29.97 ? 427  THR   B CA    1 
ATOM   12200 C  C     . THR   B 1  429  ? -22.816 15.766  106.275 1.00 23.94 ? 427  THR   B C     1 
ATOM   12201 O  O     . THR   B 1  429  ? -23.022 14.580  105.989 1.00 25.59 ? 427  THR   B O     1 
ATOM   12202 C  CB    . THR   B 1  429  ? -21.181 17.204  105.078 1.00 25.07 ? 427  THR   B CB    1 
ATOM   12203 O  OG1   . THR   B 1  429  ? -21.032 18.285  104.157 1.00 25.34 ? 427  THR   B OG1   1 
ATOM   12204 C  CG2   . THR   B 1  429  ? -20.376 16.024  104.605 1.00 27.21 ? 427  THR   B CG2   1 
ATOM   12205 N  N     . LEU   B 1  430  ? -22.702 16.190  107.538 1.00 28.68 ? 428  LEU   B N     1 
ATOM   12206 C  CA    . LEU   B 1  430  ? -22.839 15.273  108.664 1.00 26.25 ? 428  LEU   B CA    1 
ATOM   12207 C  C     . LEU   B 1  430  ? -24.204 14.598  108.658 1.00 25.12 ? 428  LEU   B C     1 
ATOM   12208 O  O     . LEU   B 1  430  ? -24.304 13.379  108.820 1.00 27.70 ? 428  LEU   B O     1 
ATOM   12209 C  CB    . LEU   B 1  430  ? -22.643 16.044  109.968 1.00 28.19 ? 428  LEU   B CB    1 
ATOM   12210 C  CG    . LEU   B 1  430  ? -22.500 15.331  111.323 1.00 25.88 ? 428  LEU   B CG    1 
ATOM   12211 C  CD1   . LEU   B 1  430  ? -22.104 16.371  112.342 1.00 31.06 ? 428  LEU   B CD1   1 
ATOM   12212 C  CD2   . LEU   B 1  430  ? -23.747 14.612  111.801 1.00 32.10 ? 428  LEU   B CD2   1 
ATOM   12213 N  N     . ALA   B 1  431  ? -25.268 15.389  108.504 1.00 29.28 ? 429  ALA   B N     1 
ATOM   12214 C  CA    . ALA   B 1  431  ? -26.616 14.828  108.531 1.00 31.10 ? 429  ALA   B CA    1 
ATOM   12215 C  C     . ALA   B 1  431  ? -26.802 13.799  107.425 1.00 29.56 ? 429  ALA   B C     1 
ATOM   12216 O  O     . ALA   B 1  431  ? -27.420 12.751  107.641 1.00 31.67 ? 429  ALA   B O     1 
ATOM   12217 C  CB    . ALA   B 1  431  ? -27.648 15.948  108.410 1.00 29.62 ? 429  ALA   B CB    1 
ATOM   12218 N  N     . ALA   B 1  432  ? -26.234 14.063  106.245 1.00 29.95 ? 430  ALA   B N     1 
ATOM   12219 C  CA    . ALA   B 1  432  ? -26.353 13.121  105.136 1.00 27.83 ? 430  ALA   B CA    1 
ATOM   12220 C  C     . ALA   B 1  432  ? -25.698 11.791  105.479 1.00 28.57 ? 430  ALA   B C     1 
ATOM   12221 O  O     . ALA   B 1  432  ? -26.265 10.723  105.231 1.00 30.82 ? 430  ALA   B O     1 
ATOM   12222 C  CB    . ALA   B 1  432  ? -25.721 13.720  103.878 1.00 28.08 ? 430  ALA   B CB    1 
ATOM   12223 N  N     . ILE   B 1  433  ? -24.488 11.840  106.042 1.00 28.80 ? 431  ILE   B N     1 
ATOM   12224 C  CA    . ILE   B 1  433  ? -23.785 10.611  106.393 1.00 29.79 ? 431  ILE   B CA    1 
ATOM   12225 C  C     . ILE   B 1  433  ? -24.448 9.924   107.575 1.00 25.91 ? 431  ILE   B C     1 
ATOM   12226 O  O     . ILE   B 1  433  ? -24.535 8.690   107.630 1.00 26.79 ? 431  ILE   B O     1 
ATOM   12227 C  CB    . ILE   B 1  433  ? -22.308 10.927  106.674 1.00 27.96 ? 431  ILE   B CB    1 
ATOM   12228 C  CG1   . ILE   B 1  433  ? -21.615 11.320  105.375 1.00 33.94 ? 431  ILE   B CG1   1 
ATOM   12229 C  CG2   . ILE   B 1  433  ? -21.608 9.749   107.348 1.00 31.91 ? 431  ILE   B CG2   1 
ATOM   12230 C  CD1   . ILE   B 1  433  ? -20.240 11.772  105.595 1.00 33.83 ? 431  ILE   B CD1   1 
ATOM   12231 N  N     . TYR   B 1  434  ? -24.897 10.708  108.556 1.00 28.78 ? 432  TYR   B N     1 
ATOM   12232 C  CA    . TYR   B 1  434  ? -25.569 10.135  109.714 1.00 29.54 ? 432  TYR   B CA    1 
ATOM   12233 C  C     . TYR   B 1  434  ? -26.742 9.261   109.293 1.00 30.22 ? 432  TYR   B C     1 
ATOM   12234 O  O     . TYR   B 1  434  ? -26.905 8.141   109.789 1.00 29.73 ? 432  TYR   B O     1 
ATOM   12235 C  CB    . TYR   B 1  434  ? -26.013 11.267  110.638 1.00 28.97 ? 432  TYR   B CB    1 
ATOM   12236 C  CG    . TYR   B 1  434  ? -26.927 10.831  111.750 1.00 28.52 ? 432  TYR   B CG    1 
ATOM   12237 C  CD1   . TYR   B 1  434  ? -26.449 10.074  112.813 1.00 31.27 ? 432  TYR   B CD1   1 
ATOM   12238 C  CD2   . TYR   B 1  434  ? -28.272 11.178  111.743 1.00 32.04 ? 432  TYR   B CD2   1 
ATOM   12239 C  CE1   . TYR   B 1  434  ? -27.283 9.680   113.839 1.00 36.32 ? 432  TYR   B CE1   1 
ATOM   12240 C  CE2   . TYR   B 1  434  ? -29.112 10.786  112.765 1.00 32.41 ? 432  TYR   B CE2   1 
ATOM   12241 C  CZ    . TYR   B 1  434  ? -28.614 10.035  113.808 1.00 34.39 ? 432  TYR   B CZ    1 
ATOM   12242 O  OH    . TYR   B 1  434  ? -29.445 9.639   114.828 1.00 37.41 ? 432  TYR   B OH    1 
ATOM   12243 N  N     . HIS   B 1  435  ? -27.533 9.730   108.332 1.00 32.05 ? 433  HIS   B N     1 
ATOM   12244 C  CA    . HIS   B 1  435  ? -28.664 8.935   107.875 1.00 33.75 ? 433  HIS   B CA    1 
ATOM   12245 C  C     . HIS   B 1  435  ? -28.259 7.873   106.866 1.00 29.09 ? 433  HIS   B C     1 
ATOM   12246 O  O     . HIS   B 1  435  ? -28.842 6.783   106.857 1.00 34.10 ? 433  HIS   B O     1 
ATOM   12247 C  CB    . HIS   B 1  435  ? -29.761 9.849   107.343 1.00 36.92 ? 433  HIS   B CB    1 
ATOM   12248 C  CG    . HIS   B 1  435  ? -30.490 10.571  108.428 1.00 38.71 ? 433  HIS   B CG    1 
ATOM   12249 N  ND1   . HIS   B 1  435  ? -31.484 9.975   109.172 1.00 33.77 ? 433  HIS   B ND1   1 
ATOM   12250 C  CD2   . HIS   B 1  435  ? -30.336 11.816  108.933 1.00 34.07 ? 433  HIS   B CD2   1 
ATOM   12251 C  CE1   . HIS   B 1  435  ? -31.932 10.832  110.071 1.00 39.91 ? 433  HIS   B CE1   1 
ATOM   12252 N  NE2   . HIS   B 1  435  ? -31.256 11.959  109.945 1.00 29.93 ? 433  HIS   B NE2   1 
ATOM   12253 N  N     . MET   B 1  436  ? -27.259 8.161   106.030 1.00 28.98 ? 434  MET   B N     1 
ATOM   12254 C  CA    . MET   B 1  436  ? -26.779 7.157   105.093 1.00 29.51 ? 434  MET   B CA    1 
ATOM   12255 C  C     . MET   B 1  436  ? -26.279 5.913   105.813 1.00 29.08 ? 434  MET   B C     1 
ATOM   12256 O  O     . MET   B 1  436  ? -26.409 4.799   105.292 1.00 33.51 ? 434  MET   B O     1 
ATOM   12257 C  CB    . MET   B 1  436  ? -25.661 7.758   104.247 1.00 32.58 ? 434  MET   B CB    1 
ATOM   12258 C  CG    . MET   B 1  436  ? -24.984 6.776   103.322 1.00 31.79 ? 434  MET   B CG    1 
ATOM   12259 S  SD    . MET   B 1  436  ? -23.581 7.568   102.519 1.00 35.84 ? 434  MET   B SD    1 
ATOM   12260 C  CE    . MET   B 1  436  ? -24.427 8.557   101.298 1.00 30.04 ? 434  MET   B CE    1 
ATOM   12261 N  N     . ALA   B 1  437  ? -25.713 6.077   107.012 1.00 29.40 ? 435  ALA   B N     1 
ATOM   12262 C  CA    . ALA   B 1  437  ? -25.153 4.956   107.756 1.00 31.32 ? 435  ALA   B CA    1 
ATOM   12263 C  C     . ALA   B 1  437  ? -26.220 4.050   108.359 1.00 33.45 ? 435  ALA   B C     1 
ATOM   12264 O  O     . ALA   B 1  437  ? -25.896 2.939   108.793 1.00 37.98 ? 435  ALA   B O     1 
ATOM   12265 C  CB    . ALA   B 1  437  ? -24.223 5.469   108.859 1.00 32.64 ? 435  ALA   B CB    1 
ATOM   12266 N  N     . GLY   B 1  438  ? -27.471 4.490   108.395 1.00 35.16 ? 436  GLY   B N     1 
ATOM   12267 C  CA    . GLY   B 1  438  ? -28.549 3.646   108.867 1.00 35.31 ? 436  GLY   B CA    1 
ATOM   12268 C  C     . GLY   B 1  438  ? -28.681 3.643   110.377 1.00 44.84 ? 436  GLY   B C     1 
ATOM   12269 O  O     . GLY   B 1  438  ? -27.925 4.279   111.118 1.00 38.13 ? 436  GLY   B O     1 
ATOM   12270 N  N     . LYS   B 1  439  ? -29.677 2.883   110.836 1.00 43.98 ? 437  LYS   B N     1 
ATOM   12271 C  CA    . LYS   B 1  439  ? -30.025 2.859   112.251 1.00 39.91 ? 437  LYS   B CA    1 
ATOM   12272 C  C     . LYS   B 1  439  ? -29.019 2.089   113.096 1.00 40.83 ? 437  LYS   B C     1 
ATOM   12273 O  O     . LYS   B 1  439  ? -28.927 2.340   114.302 1.00 49.87 ? 437  LYS   B O     1 
ATOM   12274 C  CB    . LYS   B 1  439  ? -31.416 2.246   112.434 1.00 37.39 ? 437  LYS   B CB    1 
ATOM   12275 N  N     . ASP   B 1  440  ? -28.274 1.159   112.503 1.00 38.69 ? 438  ASP   B N     1 
ATOM   12276 C  CA    . ASP   B 1  440  ? -27.390 0.291   113.272 1.00 41.72 ? 438  ASP   B CA    1 
ATOM   12277 C  C     . ASP   B 1  440  ? -26.073 1.013   113.522 1.00 38.81 ? 438  ASP   B C     1 
ATOM   12278 O  O     . ASP   B 1  440  ? -25.412 1.447   112.573 1.00 40.58 ? 438  ASP   B O     1 
ATOM   12279 C  CB    . ASP   B 1  440  ? -27.147 -1.009  112.509 1.00 44.56 ? 438  ASP   B CB    1 
ATOM   12280 N  N     . PHE   B 1  441  ? -25.693 1.149   114.790 1.00 36.61 ? 439  PHE   B N     1 
ATOM   12281 C  CA    . PHE   B 1  441  ? -24.431 1.798   115.113 1.00 34.34 ? 439  PHE   B CA    1 
ATOM   12282 C  C     . PHE   B 1  441  ? -23.814 1.200   116.368 1.00 35.04 ? 439  PHE   B C     1 
ATOM   12283 O  O     . PHE   B 1  441  ? -24.510 0.837   117.322 1.00 34.85 ? 439  PHE   B O     1 
ATOM   12284 C  CB    . PHE   B 1  441  ? -24.560 3.311   115.311 1.00 32.04 ? 439  PHE   B CB    1 
ATOM   12285 C  CG    . PHE   B 1  441  ? -23.239 3.975   115.545 1.00 34.61 ? 439  PHE   B CG    1 
ATOM   12286 C  CD1   . PHE   B 1  441  ? -22.407 4.246   114.479 1.00 29.75 ? 439  PHE   B CD1   1 
ATOM   12287 C  CD2   . PHE   B 1  441  ? -22.800 4.269   116.828 1.00 30.56 ? 439  PHE   B CD2   1 
ATOM   12288 C  CE1   . PHE   B 1  441  ? -21.170 4.830   114.672 1.00 29.77 ? 439  PHE   B CE1   1 
ATOM   12289 C  CE2   . PHE   B 1  441  ? -21.561 4.855   117.029 1.00 30.68 ? 439  PHE   B CE2   1 
ATOM   12290 C  CZ    . PHE   B 1  441  ? -20.747 5.128   115.944 1.00 31.17 ? 439  PHE   B CZ    1 
ATOM   12291 N  N     . HIS   B 1  442  ? -22.488 1.129   116.358 1.00 34.71 ? 440  HIS   B N     1 
ATOM   12292 C  CA    . HIS   B 1  442  ? -21.717 0.785   117.538 1.00 31.92 ? 440  HIS   B CA    1 
ATOM   12293 C  C     . HIS   B 1  442  ? -20.381 1.498   117.438 1.00 28.70 ? 440  HIS   B C     1 
ATOM   12294 O  O     . HIS   B 1  442  ? -19.886 1.759   116.336 1.00 30.42 ? 440  HIS   B O     1 
ATOM   12295 C  CB    . HIS   B 1  442  ? -21.478 -0.721  117.630 1.00 32.56 ? 440  HIS   B CB    1 
ATOM   12296 C  CG    . HIS   B 1  442  ? -20.899 -1.314  116.386 1.00 37.14 ? 440  HIS   B CG    1 
ATOM   12297 N  ND1   . HIS   B 1  442  ? -19.542 -1.349  116.138 1.00 40.11 ? 440  HIS   B ND1   1 
ATOM   12298 C  CD2   . HIS   B 1  442  ? -21.495 -1.887  115.313 1.00 36.91 ? 440  HIS   B CD2   1 
ATOM   12299 C  CE1   . HIS   B 1  442  ? -19.327 -1.923  114.968 1.00 39.51 ? 440  HIS   B CE1   1 
ATOM   12300 N  NE2   . HIS   B 1  442  ? -20.495 -2.260  114.447 1.00 39.25 ? 440  HIS   B NE2   1 
ATOM   12301 N  N     . VAL   B 1  443  ? -19.802 1.823   118.596 1.00 31.27 ? 441  VAL   B N     1 
ATOM   12302 C  CA    . VAL   B 1  443  ? -18.470 2.410   118.590 1.00 28.38 ? 441  VAL   B CA    1 
ATOM   12303 C  C     . VAL   B 1  443  ? -17.511 1.438   117.924 1.00 28.31 ? 441  VAL   B C     1 
ATOM   12304 O  O     . VAL   B 1  443  ? -17.514 0.234   118.212 1.00 32.14 ? 441  VAL   B O     1 
ATOM   12305 C  CB    . VAL   B 1  443  ? -18.031 2.788   120.011 1.00 33.04 ? 441  VAL   B CB    1 
ATOM   12306 C  CG1   . VAL   B 1  443  ? -16.562 3.170   120.017 1.00 31.00 ? 441  VAL   B CG1   1 
ATOM   12307 C  CG2   . VAL   B 1  443  ? -18.878 3.945   120.525 1.00 34.29 ? 441  VAL   B CG2   1 
ATOM   12308 N  N     . GLY   B 1  444  ? -16.714 1.951   116.995 1.00 27.77 ? 442  GLY   B N     1 
ATOM   12309 C  CA    . GLY   B 1  444  ? -15.865 1.131   116.169 1.00 28.49 ? 442  GLY   B CA    1 
ATOM   12310 C  C     . GLY   B 1  444  ? -16.380 0.928   114.760 1.00 26.67 ? 442  GLY   B C     1 
ATOM   12311 O  O     . GLY   B 1  444  ? -15.614 0.491   113.897 1.00 26.97 ? 442  GLY   B O     1 
ATOM   12312 N  N     . LYS   B 1  445  ? -17.654 1.235   114.501 1.00 27.49 ? 443  LYS   B N     1 
ATOM   12313 C  CA    . LYS   B 1  445  ? -18.166 1.130   113.139 1.00 28.05 ? 443  LYS   B CA    1 
ATOM   12314 C  C     . LYS   B 1  445  ? -17.645 2.276   112.279 1.00 26.43 ? 443  LYS   B C     1 
ATOM   12315 O  O     . LYS   B 1  445  ? -17.055 2.056   111.216 1.00 26.79 ? 443  LYS   B O     1 
ATOM   12316 C  CB    . LYS   B 1  445  ? -19.697 1.095   113.140 1.00 27.05 ? 443  LYS   B CB    1 
ATOM   12317 C  CG    . LYS   B 1  445  ? -20.279 0.767   111.779 1.00 30.13 ? 443  LYS   B CG    1 
ATOM   12318 C  CD    . LYS   B 1  445  ? -21.801 0.753   111.802 1.00 36.80 ? 443  LYS   B CD    1 
ATOM   12319 C  CE    . LYS   B 1  445  ? -22.363 0.307   110.461 1.00 41.96 ? 443  LYS   B CE    1 
ATOM   12320 N  NZ    . LYS   B 1  445  ? -23.855 0.239   110.496 1.00 44.73 ? 443  LYS   B NZ    1 
ATOM   12321 N  N     . TYR   B 1  446  ? -17.860 3.506   112.729 1.00 24.51 ? 444  TYR   B N     1 
ATOM   12322 C  CA    . TYR   B 1  446  ? -17.307 4.700   112.110 1.00 22.77 ? 444  TYR   B CA    1 
ATOM   12323 C  C     . TYR   B 1  446  ? -17.363 5.793   113.164 1.00 23.60 ? 444  TYR   B C     1 
ATOM   12324 O  O     . TYR   B 1  446  ? -17.992 5.636   114.207 1.00 24.42 ? 444  TYR   B O     1 
ATOM   12325 C  CB    . TYR   B 1  446  ? -18.090 5.098   110.855 1.00 25.79 ? 444  TYR   B CB    1 
ATOM   12326 C  CG    . TYR   B 1  446  ? -19.501 5.570   111.123 1.00 30.43 ? 444  TYR   B CG    1 
ATOM   12327 C  CD1   . TYR   B 1  446  ? -19.773 6.909   111.389 1.00 26.32 ? 444  TYR   B CD1   1 
ATOM   12328 C  CD2   . TYR   B 1  446  ? -20.563 4.682   111.082 1.00 29.13 ? 444  TYR   B CD2   1 
ATOM   12329 C  CE1   . TYR   B 1  446  ? -21.063 7.340   111.629 1.00 34.31 ? 444  TYR   B CE1   1 
ATOM   12330 C  CE2   . TYR   B 1  446  ? -21.847 5.100   111.325 1.00 31.89 ? 444  TYR   B CE2   1 
ATOM   12331 C  CZ    . TYR   B 1  446  ? -22.094 6.429   111.594 1.00 29.63 ? 444  TYR   B CZ    1 
ATOM   12332 O  OH    . TYR   B 1  446  ? -23.389 6.835   111.825 1.00 39.24 ? 444  TYR   B OH    1 
ATOM   12333 N  N     . GLU   B 1  447  ? -16.716 6.911   112.880 1.00 24.12 ? 445  GLU   B N     1 
ATOM   12334 C  CA    . GLU   B 1  447  ? -16.833 8.059   113.757 1.00 23.60 ? 445  GLU   B CA    1 
ATOM   12335 C  C     . GLU   B 1  447  ? -16.855 9.309   112.909 1.00 21.04 ? 445  GLU   B C     1 
ATOM   12336 O  O     . GLU   B 1  447  ? -16.562 9.286   111.710 1.00 20.94 ? 445  GLU   B O     1 
ATOM   12337 C  CB    . GLU   B 1  447  ? -15.676 8.137   114.756 1.00 20.68 ? 445  GLU   B CB    1 
ATOM   12338 C  CG    . GLU   B 1  447  ? -14.344 8.368   114.065 1.00 20.27 ? 445  GLU   B CG    1 
ATOM   12339 C  CD    . GLU   B 1  447  ? -13.173 8.276   115.015 1.00 22.26 ? 445  GLU   B CD    1 
ATOM   12340 O  OE1   . GLU   B 1  447  ? -13.368 7.845   116.173 1.00 23.50 ? 445  GLU   B OE1   1 
ATOM   12341 O  OE2   . GLU   B 1  447  ? -12.059 8.639   114.585 1.00 22.89 ? 445  GLU   B OE2   1 
ATOM   12342 N  N     . PHE   B 1  448  ? -17.219 10.409  113.541 1.00 22.41 ? 446  PHE   B N     1 
ATOM   12343 C  CA    . PHE   B 1  448  ? -16.990 11.725  112.985 1.00 21.04 ? 446  PHE   B CA    1 
ATOM   12344 C  C     . PHE   B 1  448  ? -15.690 12.278  113.554 1.00 18.82 ? 446  PHE   B C     1 
ATOM   12345 O  O     . PHE   B 1  448  ? -15.134 11.751  114.519 1.00 20.60 ? 446  PHE   B O     1 
ATOM   12346 C  CB    . PHE   B 1  448  ? -18.163 12.647  113.301 1.00 24.65 ? 446  PHE   B CB    1 
ATOM   12347 C  CG    . PHE   B 1  448  ? -19.425 12.227  112.639 1.00 21.55 ? 446  PHE   B CG    1 
ATOM   12348 C  CD1   . PHE   B 1  448  ? -19.649 12.525  111.304 1.00 23.99 ? 446  PHE   B CD1   1 
ATOM   12349 C  CD2   . PHE   B 1  448  ? -20.375 11.501  113.336 1.00 24.02 ? 446  PHE   B CD2   1 
ATOM   12350 C  CE1   . PHE   B 1  448  ? -20.808 12.123  110.679 1.00 23.95 ? 446  PHE   B CE1   1 
ATOM   12351 C  CE2   . PHE   B 1  448  ? -21.537 11.095  112.713 1.00 28.27 ? 446  PHE   B CE2   1 
ATOM   12352 C  CZ    . PHE   B 1  448  ? -21.755 11.410  111.388 1.00 26.60 ? 446  PHE   B CZ    1 
ATOM   12353 N  N     . GLN   B 1  449  ? -15.199 13.335  112.922 1.00 20.82 ? 447  GLN   B N     1 
ATOM   12354 C  CA    . GLN   B 1  449  ? -14.046 14.055  113.435 1.00 20.69 ? 447  GLN   B CA    1 
ATOM   12355 C  C     . GLN   B 1  449  ? -14.255 15.541  113.222 1.00 21.38 ? 447  GLN   B C     1 
ATOM   12356 O  O     . GLN   B 1  449  ? -14.967 15.966  112.305 1.00 20.78 ? 447  GLN   B O     1 
ATOM   12357 C  CB    . GLN   B 1  449  ? -12.736 13.630  112.763 1.00 20.93 ? 447  GLN   B CB    1 
ATOM   12358 C  CG    . GLN   B 1  449  ? -12.454 12.152  112.847 1.00 22.14 ? 447  GLN   B CG    1 
ATOM   12359 C  CD    . GLN   B 1  449  ? -10.999 11.854  112.662 1.00 20.95 ? 447  GLN   B CD    1 
ATOM   12360 O  OE1   . GLN   B 1  449  ? -10.256 12.691  112.149 1.00 22.77 ? 447  GLN   B OE1   1 
ATOM   12361 N  NE2   . GLN   B 1  449  ? -10.571 10.670  113.090 1.00 19.43 ? 447  GLN   B NE2   1 
ATOM   12362 N  N     . CYS   B 1  450  ? -13.617 16.330  114.079 1.00 18.78 ? 448  CYS   B N     1 
ATOM   12363 C  CA    . CYS   B 1  450  ? -13.681 17.773  113.955 1.00 21.40 ? 448  CYS   B CA    1 
ATOM   12364 C  C     . CYS   B 1  450  ? -12.387 18.362  114.484 1.00 18.96 ? 448  CYS   B C     1 
ATOM   12365 O  O     . CYS   B 1  450  ? -11.554 17.668  115.073 1.00 21.57 ? 448  CYS   B O     1 
ATOM   12366 C  CB    . CYS   B 1  450  ? -14.869 18.348  114.735 1.00 20.33 ? 448  CYS   B CB    1 
ATOM   12367 S  SG    . CYS   B 1  450  ? -14.685 18.294  116.536 1.00 23.76 ? 448  CYS   B SG    1 
ATOM   12368 N  N     . LEU   B 1  451  ? -12.241 19.660  114.277 1.00 20.42 ? 449  LEU   B N     1 
ATOM   12369 C  CA    . LEU   B 1  451  ? -11.072 20.386  114.734 1.00 20.16 ? 449  LEU   B CA    1 
ATOM   12370 C  C     . LEU   B 1  451  ? -11.349 20.965  116.112 1.00 25.10 ? 449  LEU   B C     1 
ATOM   12371 O  O     . LEU   B 1  451  ? -12.437 21.480  116.376 1.00 25.38 ? 449  LEU   B O     1 
ATOM   12372 C  CB    . LEU   B 1  451  ? -10.770 21.517  113.758 1.00 23.48 ? 449  LEU   B CB    1 
ATOM   12373 C  CG    . LEU   B 1  451  ? -9.532  22.376  113.986 1.00 28.00 ? 449  LEU   B CG    1 
ATOM   12374 C  CD1   . LEU   B 1  451  ? -8.263  21.517  114.056 1.00 24.40 ? 449  LEU   B CD1   1 
ATOM   12375 C  CD2   . LEU   B 1  451  ? -9.433  23.381  112.849 1.00 33.89 ? 449  LEU   B CD2   1 
ATOM   12376 N  N     . HIS   B 1  452  ? -10.361 20.858  116.995 1.00 20.48 ? 450  HIS   B N     1 
ATOM   12377 C  CA    . HIS   B 1  452  ? -10.454 21.499  118.297 1.00 25.76 ? 450  HIS   B CA    1 
ATOM   12378 C  C     . HIS   B 1  452  ? -10.775 22.977  118.135 1.00 25.59 ? 450  HIS   B C     1 
ATOM   12379 O  O     . HIS   B 1  452  ? -10.211 23.656  117.275 1.00 28.56 ? 450  HIS   B O     1 
ATOM   12380 C  CB    . HIS   B 1  452  ? -9.104  21.383  119.003 1.00 21.43 ? 450  HIS   B CB    1 
ATOM   12381 C  CG    . HIS   B 1  452  ? -9.014  22.229  120.228 1.00 22.73 ? 450  HIS   B CG    1 
ATOM   12382 N  ND1   . HIS   B 1  452  ? -9.500  21.816  121.449 1.00 26.67 ? 450  HIS   B ND1   1 
ATOM   12383 C  CD2   . HIS   B 1  452  ? -8.533  23.480  120.415 1.00 24.39 ? 450  HIS   B CD2   1 
ATOM   12384 C  CE1   . HIS   B 1  452  ? -9.307  22.769  122.342 1.00 26.38 ? 450  HIS   B CE1   1 
ATOM   12385 N  NE2   . HIS   B 1  452  ? -8.725  23.790  121.740 1.00 23.89 ? 450  HIS   B NE2   1 
ATOM   12386 N  N     . GLY   B 1  453  ? -11.671 23.477  118.984 1.00 31.54 ? 451  GLY   B N     1 
ATOM   12387 C  CA    . GLY   B 1  453  ? -11.956 24.901  119.006 1.00 38.55 ? 451  GLY   B CA    1 
ATOM   12388 C  C     . GLY   B 1  453  ? -12.643 25.423  117.769 1.00 43.20 ? 451  GLY   B C     1 
ATOM   12389 O  O     . GLY   B 1  453  ? -12.640 26.633  117.527 1.00 46.35 ? 451  GLY   B O     1 
ATOM   12390 N  N     . MET   B 1  454  ? -13.212 24.535  116.963 1.00 30.43 ? 452  MET   B N     1 
ATOM   12391 C  CA    . MET   B 1  454  ? -13.988 24.921  115.794 1.00 28.95 ? 452  MET   B CA    1 
ATOM   12392 C  C     . MET   B 1  454  ? -15.212 24.025  115.724 1.00 32.10 ? 452  MET   B C     1 
ATOM   12393 O  O     . MET   B 1  454  ? -16.335 24.499  115.519 1.00 30.31 ? 452  MET   B O     1 
ATOM   12394 C  CB    . MET   B 1  454  ? -13.153 24.760  114.519 1.00 25.65 ? 452  MET   B CB    1 
ATOM   12395 C  CG    . MET   B 1  454  ? -13.950 24.963  113.240 1.00 31.98 ? 452  MET   B CG    1 
ATOM   12396 S  SD    . MET   B 1  454  ? -14.805 26.548  113.236 1.00 41.24 ? 452  MET   B SD    1 
ATOM   12397 C  CE    . MET   B 1  454  ? -13.407 27.669  113.284 1.00 39.23 ? 452  MET   B CE    1 
ATOM   12398 N  N     . GLY   B 1  455  ? -15.002 22.726  115.917 1.00 24.83 ? 453  GLY   B N     1 
ATOM   12399 C  CA    . GLY   B 1  455  ? -16.051 21.746  115.732 1.00 27.19 ? 453  GLY   B CA    1 
ATOM   12400 C  C     . GLY   B 1  455  ? -16.898 21.427  116.940 1.00 31.05 ? 453  GLY   B C     1 
ATOM   12401 O  O     . GLY   B 1  455  ? -17.929 20.769  116.788 1.00 29.42 ? 453  GLY   B O     1 
ATOM   12402 N  N     . GLU   B 1  456  ? -16.490 21.853  118.138 1.00 33.37 ? 454  GLU   B N     1 
ATOM   12403 C  CA    . GLU   B 1  456  ? -17.251 21.502  119.337 1.00 31.78 ? 454  GLU   B CA    1 
ATOM   12404 C  C     . GLU   B 1  456  ? -18.706 21.945  119.291 1.00 31.56 ? 454  GLU   B C     1 
ATOM   12405 O  O     . GLU   B 1  456  ? -19.580 21.135  119.646 1.00 33.41 ? 454  GLU   B O     1 
ATOM   12406 C  CB    . GLU   B 1  456  ? -16.541 21.981  120.607 1.00 35.56 ? 454  GLU   B CB    1 
ATOM   12407 C  CG    . GLU   B 1  456  ? -15.292 21.199  120.954 1.00 41.26 ? 454  GLU   B CG    1 
ATOM   12408 C  CD    . GLU   B 1  456  ? -14.057 21.809  120.343 1.00 43.38 ? 454  GLU   B CD    1 
ATOM   12409 O  OE1   . GLU   B 1  456  ? -14.201 22.523  119.324 1.00 41.67 ? 454  GLU   B OE1   1 
ATOM   12410 O  OE2   . GLU   B 1  456  ? -12.952 21.590  120.887 1.00 33.31 ? 454  GLU   B OE2   1 
ATOM   12411 N  N     . PRO   B 1  457  ? -19.042 23.180  118.895 1.00 32.20 ? 455  PRO   B N     1 
ATOM   12412 C  CA    . PRO   B 1  457  ? -20.463 23.564  118.860 1.00 33.17 ? 455  PRO   B CA    1 
ATOM   12413 C  C     . PRO   B 1  457  ? -21.332 22.621  118.051 1.00 33.83 ? 455  PRO   B C     1 
ATOM   12414 O  O     . PRO   B 1  457  ? -22.464 22.322  118.451 1.00 35.24 ? 455  PRO   B O     1 
ATOM   12415 C  CB    . PRO   B 1  457  ? -20.421 24.972  118.257 1.00 35.30 ? 455  PRO   B CB    1 
ATOM   12416 C  CG    . PRO   B 1  457  ? -19.110 25.505  118.688 1.00 35.23 ? 455  PRO   B CG    1 
ATOM   12417 C  CD    . PRO   B 1  457  ? -18.168 24.335  118.620 1.00 34.35 ? 455  PRO   B CD    1 
ATOM   12418 N  N     . LEU   B 1  458  ? -20.831 22.135  116.918 1.00 30.59 ? 456  LEU   B N     1 
ATOM   12419 C  CA    . LEU   B 1  458  ? -21.603 21.184  116.130 1.00 28.35 ? 456  LEU   B CA    1 
ATOM   12420 C  C     . LEU   B 1  458  ? -21.654 19.830  116.816 1.00 27.91 ? 456  LEU   B C     1 
ATOM   12421 O  O     . LEU   B 1  458  ? -22.727 19.241  116.978 1.00 28.02 ? 456  LEU   B O     1 
ATOM   12422 C  CB    . LEU   B 1  458  ? -20.996 21.052  114.735 1.00 27.68 ? 456  LEU   B CB    1 
ATOM   12423 C  CG    . LEU   B 1  458  ? -21.658 20.046  113.797 1.00 25.76 ? 456  LEU   B CG    1 
ATOM   12424 C  CD1   . LEU   B 1  458  ? -23.137 20.382  113.603 1.00 30.18 ? 456  LEU   B CD1   1 
ATOM   12425 C  CD2   . LEU   B 1  458  ? -20.948 20.037  112.461 1.00 29.07 ? 456  LEU   B CD2   1 
ATOM   12426 N  N     . TYR   B 1  459  ? -20.503 19.326  117.249 1.00 27.64 ? 457  TYR   B N     1 
ATOM   12427 C  CA    . TYR   B 1  459  ? -20.461 17.957  117.731 1.00 25.92 ? 457  TYR   B CA    1 
ATOM   12428 C  C     . TYR   B 1  459  ? -20.985 17.796  119.148 1.00 26.55 ? 457  TYR   B C     1 
ATOM   12429 O  O     . TYR   B 1  459  ? -21.298 16.672  119.550 1.00 28.20 ? 457  TYR   B O     1 
ATOM   12430 C  CB    . TYR   B 1  459  ? -19.079 17.352  117.501 1.00 26.70 ? 457  TYR   B CB    1 
ATOM   12431 C  CG    . TYR   B 1  459  ? -18.928 17.022  116.045 1.00 25.46 ? 457  TYR   B CG    1 
ATOM   12432 C  CD1   . TYR   B 1  459  ? -19.477 15.858  115.533 1.00 24.19 ? 457  TYR   B CD1   1 
ATOM   12433 C  CD2   . TYR   B 1  459  ? -18.303 17.901  115.165 1.00 24.18 ? 457  TYR   B CD2   1 
ATOM   12434 C  CE1   . TYR   B 1  459  ? -19.378 15.556  114.189 1.00 23.62 ? 457  TYR   B CE1   1 
ATOM   12435 C  CE2   . TYR   B 1  459  ? -18.197 17.600  113.801 1.00 24.72 ? 457  TYR   B CE2   1 
ATOM   12436 C  CZ    . TYR   B 1  459  ? -18.736 16.421  113.330 1.00 22.66 ? 457  TYR   B CZ    1 
ATOM   12437 O  OH    . TYR   B 1  459  ? -18.647 16.096  111.990 1.00 24.19 ? 457  TYR   B OH    1 
ATOM   12438 N  N     . GLU   B 1  460  ? -21.121 18.884  119.900 1.00 27.17 ? 458  GLU   B N     1 
ATOM   12439 C  CA    . GLU   B 1  460  ? -21.857 18.763  121.151 1.00 32.16 ? 458  GLU   B CA    1 
ATOM   12440 C  C     . GLU   B 1  460  ? -23.340 18.514  120.902 1.00 38.02 ? 458  GLU   B C     1 
ATOM   12441 O  O     . GLU   B 1  460  ? -24.052 18.108  121.826 1.00 34.35 ? 458  GLU   B O     1 
ATOM   12442 C  CB    . GLU   B 1  460  ? -21.610 19.975  122.055 1.00 34.11 ? 458  GLU   B CB    1 
ATOM   12443 C  CG    . GLU   B 1  460  ? -22.162 21.279  121.522 1.00 44.15 ? 458  GLU   B CG    1 
ATOM   12444 C  CD    . GLU   B 1  460  ? -21.770 22.468  122.382 1.00 52.67 ? 458  GLU   B CD    1 
ATOM   12445 O  OE1   . GLU   B 1  460  ? -20.948 22.287  123.305 1.00 47.02 ? 458  GLU   B OE1   1 
ATOM   12446 O  OE2   . GLU   B 1  460  ? -22.281 23.583  122.132 1.00 50.69 ? 458  GLU   B OE2   1 
ATOM   12447 N  N     . GLU   B 1  461  ? -23.808 18.728  119.672 1.00 30.55 ? 459  GLU   B N     1 
ATOM   12448 C  CA    . GLU   B 1  461  ? -25.146 18.340  119.244 1.00 35.24 ? 459  GLU   B CA    1 
ATOM   12449 C  C     . GLU   B 1  461  ? -25.183 16.948  118.631 1.00 35.76 ? 459  GLU   B C     1 
ATOM   12450 O  O     . GLU   B 1  461  ? -26.229 16.535  118.117 1.00 32.55 ? 459  GLU   B O     1 
ATOM   12451 C  CB    . GLU   B 1  461  ? -25.694 19.348  118.233 1.00 32.70 ? 459  GLU   B CB    1 
ATOM   12452 C  CG    . GLU   B 1  461  ? -25.583 20.794  118.661 1.00 32.26 ? 459  GLU   B CG    1 
ATOM   12453 C  CD    . GLU   B 1  461  ? -26.404 21.093  119.902 1.00 42.03 ? 459  GLU   B CD    1 
ATOM   12454 O  OE1   . GLU   B 1  461  ? -27.354 20.330  120.191 1.00 39.76 ? 459  GLU   B OE1   1 
ATOM   12455 O  OE2   . GLU   B 1  461  ? -26.092 22.090  120.589 1.00 44.60 ? 459  GLU   B OE2   1 
ATOM   12456 N  N     . VAL   B 1  462  ? -24.063 16.224  118.669 1.00 33.32 ? 460  VAL   B N     1 
ATOM   12457 C  CA    . VAL   B 1  462  ? -23.919 14.926  118.025 1.00 30.05 ? 460  VAL   B CA    1 
ATOM   12458 C  C     . VAL   B 1  462  ? -23.524 13.847  119.025 1.00 30.59 ? 460  VAL   B C     1 
ATOM   12459 O  O     . VAL   B 1  462  ? -24.170 12.798  119.115 1.00 29.43 ? 460  VAL   B O     1 
ATOM   12460 C  CB    . VAL   B 1  462  ? -22.913 14.990  116.848 1.00 28.97 ? 460  VAL   B CB    1 
ATOM   12461 C  CG1   . VAL   B 1  462  ? -22.684 13.611  116.249 1.00 27.16 ? 460  VAL   B CG1   1 
ATOM   12462 C  CG2   . VAL   B 1  462  ? -23.401 15.967  115.790 1.00 29.54 ? 460  VAL   B CG2   1 
ATOM   12463 N  N     . VAL   B 1  463  ? -22.457 14.089  119.789 1.00 27.96 ? 461  VAL   B N     1 
ATOM   12464 C  CA    . VAL   B 1  463  ? -21.979 13.110  120.758 1.00 25.39 ? 461  VAL   B CA    1 
ATOM   12465 C  C     . VAL   B 1  463  ? -22.932 13.041  121.944 1.00 29.72 ? 461  VAL   B C     1 
ATOM   12466 O  O     . VAL   B 1  463  ? -23.402 14.069  122.455 1.00 34.15 ? 461  VAL   B O     1 
ATOM   12467 C  CB    . VAL   B 1  463  ? -20.553 13.472  121.212 1.00 27.03 ? 461  VAL   B CB    1 
ATOM   12468 C  CG1   . VAL   B 1  463  ? -20.053 12.466  122.226 1.00 30.67 ? 461  VAL   B CG1   1 
ATOM   12469 C  CG2   . VAL   B 1  463  ? -19.609 13.539  120.013 1.00 28.12 ? 461  VAL   B CG2   1 
ATOM   12470 N  N     . GLY   B 1  464  ? -23.216 11.822  122.393 1.00 31.02 ? 462  GLY   B N     1 
ATOM   12471 C  CA    . GLY   B 1  464  ? -24.016 11.628  123.587 1.00 30.09 ? 462  GLY   B CA    1 
ATOM   12472 C  C     . GLY   B 1  464  ? -25.338 10.941  123.332 1.00 36.96 ? 462  GLY   B C     1 
ATOM   12473 O  O     . GLY   B 1  464  ? -25.935 11.123  122.269 1.00 34.98 ? 462  GLY   B O     1 
ATOM   12474 N  N     . ARG   B 1  465  ? -25.798 10.151  124.310 1.00 41.23 ? 463  ARG   B N     1 
ATOM   12475 C  CA    . ARG   B 1  465  ? -27.077 9.463   124.172 1.00 43.11 ? 463  ARG   B CA    1 
ATOM   12476 C  C     . ARG   B 1  465  ? -28.223 10.441  123.942 1.00 44.03 ? 463  ARG   B C     1 
ATOM   12477 O  O     . ARG   B 1  465  ? -29.177 10.119  123.226 1.00 48.81 ? 463  ARG   B O     1 
ATOM   12478 C  CB    . ARG   B 1  465  ? -27.346 8.605   125.407 1.00 49.34 ? 463  ARG   B CB    1 
ATOM   12479 N  N     . GLY   B 1  466  ? -28.142 11.634  124.526 1.00 39.79 ? 464  GLY   B N     1 
ATOM   12480 C  CA    . GLY   B 1  466  ? -29.139 12.669  124.358 1.00 42.86 ? 464  GLY   B CA    1 
ATOM   12481 C  C     . GLY   B 1  466  ? -29.078 13.428  123.064 1.00 45.31 ? 464  GLY   B C     1 
ATOM   12482 O  O     . GLY   B 1  466  ? -29.925 14.292  122.814 1.00 42.81 ? 464  GLY   B O     1 
ATOM   12483 N  N     . LYS   B 1  467  ? -28.083 13.136  122.218 1.00 38.56 ? 465  LYS   B N     1 
ATOM   12484 C  CA    . LYS   B 1  467  ? -27.948 13.769  120.917 1.00 38.54 ? 465  LYS   B CA    1 
ATOM   12485 C  C     . LYS   B 1  467  ? -28.122 12.736  119.814 1.00 40.87 ? 465  LYS   B C     1 
ATOM   12486 O  O     . LYS   B 1  467  ? -29.140 12.048  119.765 1.00 38.92 ? 465  LYS   B O     1 
ATOM   12487 C  CB    . LYS   B 1  467  ? -26.597 14.486  120.806 1.00 35.12 ? 465  LYS   B CB    1 
ATOM   12488 C  CG    . LYS   B 1  467  ? -26.414 15.573  121.854 1.00 39.56 ? 465  LYS   B CG    1 
ATOM   12489 C  CD    . LYS   B 1  467  ? -27.456 16.671  121.678 1.00 39.61 ? 465  LYS   B CD    1 
ATOM   12490 C  CE    . LYS   B 1  467  ? -27.406 17.720  122.791 1.00 41.03 ? 465  LYS   B CE    1 
ATOM   12491 N  NZ    . LYS   B 1  467  ? -28.220 18.927  122.442 1.00 45.27 ? 465  LYS   B NZ    1 
ATOM   12492 N  N     . LEU   B 1  468  ? -27.147 12.627  118.911 1.00 34.93 ? 466  LEU   B N     1 
ATOM   12493 C  CA    . LEU   B 1  468  ? -27.208 11.601  117.883 1.00 33.25 ? 466  LEU   B CA    1 
ATOM   12494 C  C     . LEU   B 1  468  ? -26.501 10.319  118.292 1.00 31.55 ? 466  LEU   B C     1 
ATOM   12495 O  O     . LEU   B 1  468  ? -26.557 9.331   117.551 1.00 32.75 ? 466  LEU   B O     1 
ATOM   12496 C  CB    . LEU   B 1  468  ? -26.639 12.114  116.555 1.00 32.82 ? 466  LEU   B CB    1 
ATOM   12497 C  CG    . LEU   B 1  468  ? -27.244 13.408  116.016 1.00 34.01 ? 466  LEU   B CG    1 
ATOM   12498 C  CD1   . LEU   B 1  468  ? -26.666 13.731  114.646 1.00 36.15 ? 466  LEU   B CD1   1 
ATOM   12499 C  CD2   . LEU   B 1  468  ? -28.769 13.313  115.967 1.00 36.92 ? 466  LEU   B CD2   1 
ATOM   12500 N  N     . ASP   B 1  469  ? -25.847 10.311  119.452 1.00 31.25 ? 467  ASP   B N     1 
ATOM   12501 C  CA    . ASP   B 1  469  ? -25.154 9.125   119.951 1.00 37.47 ? 467  ASP   B CA    1 
ATOM   12502 C  C     . ASP   B 1  469  ? -24.112 8.632   118.951 1.00 27.66 ? 467  ASP   B C     1 
ATOM   12503 O  O     . ASP   B 1  469  ? -23.996 7.435   118.678 1.00 30.59 ? 467  ASP   B O     1 
ATOM   12504 C  CB    . ASP   B 1  469  ? -26.126 8.014   120.360 1.00 36.81 ? 467  ASP   B CB    1 
ATOM   12505 C  CG    . ASP   B 1  469  ? -25.528 7.065   121.370 1.00 43.98 ? 467  ASP   B CG    1 
ATOM   12506 O  OD1   . ASP   B 1  469  ? -24.504 7.427   121.993 1.00 41.16 ? 467  ASP   B OD1   1 
ATOM   12507 O  OD2   . ASP   B 1  469  ? -26.074 5.952   121.536 1.00 47.98 ? 467  ASP   B OD2   1 
ATOM   12508 N  N     . ARG   B 1  470  ? -23.356 9.572   118.396 1.00 30.75 ? 468  ARG   B N     1 
ATOM   12509 C  CA    . ARG   B 1  470  ? -22.269 9.268   117.489 1.00 27.49 ? 468  ARG   B CA    1 
ATOM   12510 C  C     . ARG   B 1  470  ? -20.982 9.886   118.013 1.00 27.71 ? 468  ARG   B C     1 
ATOM   12511 O  O     . ARG   B 1  470  ? -20.982 11.043  118.446 1.00 27.83 ? 468  ARG   B O     1 
ATOM   12512 C  CB    . ARG   B 1  470  ? -22.549 9.818   116.082 1.00 31.73 ? 468  ARG   B CB    1 
ATOM   12513 C  CG    . ARG   B 1  470  ? -23.783 9.214   115.416 1.00 29.42 ? 468  ARG   B CG    1 
ATOM   12514 C  CD    . ARG   B 1  470  ? -23.632 7.715   115.205 1.00 27.71 ? 468  ARG   B CD    1 
ATOM   12515 N  NE    . ARG   B 1  470  ? -24.813 7.122   114.580 1.00 31.33 ? 468  ARG   B NE    1 
ATOM   12516 C  CZ    . ARG   B 1  470  ? -25.804 6.548   115.247 1.00 38.42 ? 468  ARG   B CZ    1 
ATOM   12517 N  NH1   . ARG   B 1  470  ? -25.803 6.485   116.569 1.00 33.50 ? 468  ARG   B NH1   1 
ATOM   12518 N  NH2   . ARG   B 1  470  ? -26.822 6.021   114.570 1.00 38.34 ? 468  ARG   B NH2   1 
ATOM   12519 N  N     . PRO   B 1  471  ? -19.881 9.147   117.993 1.00 26.27 ? 469  PRO   B N     1 
ATOM   12520 C  CA    . PRO   B 1  471  ? -18.628 9.668   118.537 1.00 26.27 ? 469  PRO   B CA    1 
ATOM   12521 C  C     . PRO   B 1  471  ? -17.987 10.645  117.569 1.00 22.86 ? 469  PRO   B C     1 
ATOM   12522 O  O     . PRO   B 1  471  ? -18.241 10.645  116.360 1.00 22.04 ? 469  PRO   B O     1 
ATOM   12523 C  CB    . PRO   B 1  471  ? -17.766 8.412   118.667 1.00 25.72 ? 469  PRO   B CB    1 
ATOM   12524 C  CG    . PRO   B 1  471  ? -18.226 7.560   117.545 1.00 30.32 ? 469  PRO   B CG    1 
ATOM   12525 C  CD    . PRO   B 1  471  ? -19.712 7.797   117.440 1.00 27.49 ? 469  PRO   B CD    1 
ATOM   12526 N  N     . CYS   B 1  472  ? -17.134 11.489  118.134 1.00 22.41 ? 470  CYS   B N     1 
ATOM   12527 C  CA    . CYS   B 1  472  ? -16.383 12.448  117.354 1.00 21.35 ? 470  CYS   B CA    1 
ATOM   12528 C  C     . CYS   B 1  472  ? -14.971 12.494  117.912 1.00 22.38 ? 470  CYS   B C     1 
ATOM   12529 O  O     . CYS   B 1  472  ? -14.788 12.618  119.128 1.00 23.16 ? 470  CYS   B O     1 
ATOM   12530 C  CB    . CYS   B 1  472  ? -17.013 13.836  117.429 1.00 24.68 ? 470  CYS   B CB    1 
ATOM   12531 S  SG    . CYS   B 1  472  ? -16.116 15.018  116.422 1.00 26.24 ? 470  CYS   B SG    1 
ATOM   12532 N  N     . ARG   B 1  473  ? -13.986 12.359  117.032 1.00 21.58 ? 471  ARG   B N     1 
ATOM   12533 C  CA    . ARG   B 1  473  ? -12.589 12.508  117.402 1.00 23.77 ? 471  ARG   B CA    1 
ATOM   12534 C  C     . ARG   B 1  473  ? -12.144 13.928  117.102 1.00 20.92 ? 471  ARG   B C     1 
ATOM   12535 O  O     . ARG   B 1  473  ? -12.303 14.416  115.979 1.00 23.08 ? 471  ARG   B O     1 
ATOM   12536 C  CB    . ARG   B 1  473  ? -11.704 11.525  116.647 1.00 20.80 ? 471  ARG   B CB    1 
ATOM   12537 C  CG    . ARG   B 1  473  ? -10.254 11.573  117.117 1.00 20.65 ? 471  ARG   B CG    1 
ATOM   12538 C  CD    . ARG   B 1  473  ? -9.454  10.445  116.487 1.00 19.09 ? 471  ARG   B CD    1 
ATOM   12539 N  NE    . ARG   B 1  473  ? -10.144 9.167   116.615 1.00 21.40 ? 471  ARG   B NE    1 
ATOM   12540 C  CZ    . ARG   B 1  473  ? -10.051 8.357   117.661 1.00 23.46 ? 471  ARG   B CZ    1 
ATOM   12541 N  NH1   . ARG   B 1  473  ? -9.234  8.622   118.673 1.00 22.23 ? 471  ARG   B NH1   1 
ATOM   12542 N  NH2   . ARG   B 1  473  ? -10.804 7.259   117.700 1.00 23.51 ? 471  ARG   B NH2   1 
ATOM   12543 N  N     . ILE   B 1  474  ? -11.578 14.579  118.108 1.00 22.73 ? 472  ILE   B N     1 
ATOM   12544 C  CA    . ILE   B 1  474  ? -11.142 15.960  117.988 1.00 19.72 ? 472  ILE   B CA    1 
ATOM   12545 C  C     . ILE   B 1  474  ? -9.685  15.973  117.553 1.00 21.91 ? 472  ILE   B C     1 
ATOM   12546 O  O     . ILE   B 1  474  ? -8.825  15.407  118.235 1.00 23.18 ? 472  ILE   B O     1 
ATOM   12547 C  CB    . ILE   B 1  474  ? -11.313 16.694  119.323 1.00 21.16 ? 472  ILE   B CB    1 
ATOM   12548 C  CG1   . ILE   B 1  474  ? -12.802 16.744  119.696 1.00 21.23 ? 472  ILE   B CG1   1 
ATOM   12549 C  CG2   . ILE   B 1  474  ? -10.699 18.078  119.220 1.00 21.47 ? 472  ILE   B CG2   1 
ATOM   12550 C  CD1   . ILE   B 1  474  ? -13.046 17.251  121.090 1.00 26.31 ? 472  ILE   B CD1   1 
ATOM   12551 N  N     . TYR   B 1  475  ? -9.417  16.614  116.418 1.00 20.26 ? 473  TYR   B N     1 
ATOM   12552 C  CA    . TYR   B 1  475  ? -8.058  16.865  115.954 1.00 19.39 ? 473  TYR   B CA    1 
ATOM   12553 C  C     . TYR   B 1  475  ? -7.533  18.028  116.776 1.00 22.20 ? 473  TYR   B C     1 
ATOM   12554 O  O     . TYR   B 1  475  ? -8.050  19.145  116.689 1.00 20.65 ? 473  TYR   B O     1 
ATOM   12555 C  CB    . TYR   B 1  475  ? -8.095  17.205  114.468 1.00 21.53 ? 473  TYR   B CB    1 
ATOM   12556 C  CG    . TYR   B 1  475  ? -6.761  17.281  113.771 1.00 19.74 ? 473  TYR   B CG    1 
ATOM   12557 C  CD1   . TYR   B 1  475  ? -6.052  18.472  113.725 1.00 22.73 ? 473  TYR   B CD1   1 
ATOM   12558 C  CD2   . TYR   B 1  475  ? -6.231  16.175  113.124 1.00 20.12 ? 473  TYR   B CD2   1 
ATOM   12559 C  CE1   . TYR   B 1  475  ? -4.835  18.561  113.055 1.00 22.19 ? 473  TYR   B CE1   1 
ATOM   12560 C  CE2   . TYR   B 1  475  ? -5.017  16.248  112.462 1.00 18.10 ? 473  TYR   B CE2   1 
ATOM   12561 C  CZ    . TYR   B 1  475  ? -4.329  17.440  112.431 1.00 23.85 ? 473  TYR   B CZ    1 
ATOM   12562 O  OH    . TYR   B 1  475  ? -3.123  17.514  111.775 1.00 25.10 ? 473  TYR   B OH    1 
ATOM   12563 N  N     . ALA   B 1  476  ? -6.523  17.757  117.591 1.00 20.24 ? 474  ALA   B N     1 
ATOM   12564 C  CA    . ALA   B 1  476  ? -6.119  18.667  118.657 1.00 22.97 ? 474  ALA   B CA    1 
ATOM   12565 C  C     . ALA   B 1  476  ? -4.705  19.157  118.398 1.00 23.02 ? 474  ALA   B C     1 
ATOM   12566 O  O     . ALA   B 1  476  ? -3.731  18.420  118.645 1.00 21.80 ? 474  ALA   B O     1 
ATOM   12567 C  CB    . ALA   B 1  476  ? -6.194  17.931  119.990 1.00 23.09 ? 474  ALA   B CB    1 
ATOM   12568 N  N     . PRO   B 1  477  ? -4.543  20.377  117.890 1.00 23.09 ? 475  PRO   B N     1 
ATOM   12569 C  CA    . PRO   B 1  477  ? -3.196  20.925  117.723 1.00 20.62 ? 475  PRO   B CA    1 
ATOM   12570 C  C     . PRO   B 1  477  ? -2.548  21.131  119.075 1.00 21.04 ? 475  PRO   B C     1 
ATOM   12571 O  O     . PRO   B 1  477  ? -3.202  21.517  120.044 1.00 22.51 ? 475  PRO   B O     1 
ATOM   12572 C  CB    . PRO   B 1  477  ? -3.440  22.268  117.031 1.00 23.98 ? 475  PRO   B CB    1 
ATOM   12573 C  CG    . PRO   B 1  477  ? -4.796  22.144  116.419 1.00 24.39 ? 475  PRO   B CG    1 
ATOM   12574 C  CD    . PRO   B 1  477  ? -5.577  21.272  117.348 1.00 23.51 ? 475  PRO   B CD    1 
ATOM   12575 N  N     . VAL   B 1  478  ? -1.244  20.891  119.125 1.00 20.95 ? 476  VAL   B N     1 
ATOM   12576 C  CA    . VAL   B 1  478  ? -0.456  21.021  120.338 1.00 21.71 ? 476  VAL   B CA    1 
ATOM   12577 C  C     . VAL   B 1  478  ? 0.813   21.754  119.960 1.00 22.47 ? 476  VAL   B C     1 
ATOM   12578 O  O     . VAL   B 1  478  ? 1.563   21.289  119.098 1.00 24.80 ? 476  VAL   B O     1 
ATOM   12579 C  CB    . VAL   B 1  478  ? -0.107  19.650  120.937 1.00 21.83 ? 476  VAL   B CB    1 
ATOM   12580 C  CG1   . VAL   B 1  478  ? 0.699   19.826  122.203 1.00 25.59 ? 476  VAL   B CG1   1 
ATOM   12581 C  CG2   . VAL   B 1  478  ? -1.369  18.844  121.199 1.00 23.16 ? 476  VAL   B CG2   1 
ATOM   12582 N  N     . GLY   B 1  479  ? 1.054   22.889  120.587 1.00 27.67 ? 477  GLY   B N     1 
ATOM   12583 C  CA    . GLY   B 1  479  ? 2.291   23.593  120.332 1.00 31.13 ? 477  GLY   B CA    1 
ATOM   12584 C  C     . GLY   B 1  479  ? 2.235   25.027  120.802 1.00 30.11 ? 477  GLY   B C     1 
ATOM   12585 O  O     . GLY   B 1  479  ? 1.222   25.512  121.314 1.00 26.22 ? 477  GLY   B O     1 
ATOM   12586 N  N     . THR   B 1  480  ? 3.359   25.701  120.579 1.00 34.53 ? 478  THR   B N     1 
ATOM   12587 C  CA    . THR   B 1  480  ? 3.614   27.041  121.068 1.00 39.31 ? 478  THR   B CA    1 
ATOM   12588 C  C     . THR   B 1  480  ? 2.949   28.067  120.158 1.00 39.07 ? 478  THR   B C     1 
ATOM   12589 O  O     . THR   B 1  480  ? 2.389   27.743  119.106 1.00 38.45 ? 478  THR   B O     1 
ATOM   12590 C  CB    . THR   B 1  480  ? 5.120   27.300  121.097 1.00 38.63 ? 478  THR   B CB    1 
ATOM   12591 O  OG1   . THR   B 1  480  ? 5.642   27.180  119.764 1.00 47.31 ? 478  THR   B OG1   1 
ATOM   12592 C  CG2   . THR   B 1  480  ? 5.817   26.296  121.995 1.00 34.50 ? 478  THR   B CG2   1 
ATOM   12593 N  N     . HIS   B 1  481  ? 3.030   29.331  120.578 1.00 43.43 ? 479  HIS   B N     1 
ATOM   12594 C  CA    . HIS   B 1  481  ? 2.465   30.417  119.785 1.00 42.53 ? 479  HIS   B CA    1 
ATOM   12595 C  C     . HIS   B 1  481  ? 3.110   30.485  118.408 1.00 46.32 ? 479  HIS   B C     1 
ATOM   12596 O  O     . HIS   B 1  481  ? 2.419   30.627  117.392 1.00 46.76 ? 479  HIS   B O     1 
ATOM   12597 C  CB    . HIS   B 1  481  ? 2.640   31.739  120.528 1.00 40.11 ? 479  HIS   B CB    1 
ATOM   12598 C  CG    . HIS   B 1  481  ? 1.816   31.838  121.772 1.00 42.78 ? 479  HIS   B CG    1 
ATOM   12599 N  ND1   . HIS   B 1  481  ? 1.770   32.977  122.547 1.00 47.88 ? 479  HIS   B ND1   1 
ATOM   12600 C  CD2   . HIS   B 1  481  ? 1.000   30.939  122.373 1.00 40.59 ? 479  HIS   B CD2   1 
ATOM   12601 C  CE1   . HIS   B 1  481  ? 0.962   32.775  123.573 1.00 48.90 ? 479  HIS   B CE1   1 
ATOM   12602 N  NE2   . HIS   B 1  481  ? 0.482   31.547  123.492 1.00 48.65 ? 479  HIS   B NE2   1 
ATOM   12603 N  N     . GLU   B 1  482  ? 4.439   30.380  118.355 1.00 47.65 ? 480  GLU   B N     1 
ATOM   12604 C  CA    . GLU   B 1  482  ? 5.137   30.468  117.077 1.00 40.30 ? 480  GLU   B CA    1 
ATOM   12605 C  C     . GLU   B 1  482  ? 4.733   29.332  116.146 1.00 44.68 ? 480  GLU   B C     1 
ATOM   12606 O  O     . GLU   B 1  482  ? 4.507   29.550  114.949 1.00 49.05 ? 480  GLU   B O     1 
ATOM   12607 C  CB    . GLU   B 1  482  ? 6.649   30.474  117.307 1.00 52.33 ? 480  GLU   B CB    1 
ATOM   12608 N  N     . THR   B 1  483  ? 4.624   28.113  116.679 1.00 47.19 ? 481  THR   B N     1 
ATOM   12609 C  CA    . THR   B 1  483  ? 4.293   26.966  115.838 1.00 49.12 ? 481  THR   B CA    1 
ATOM   12610 C  C     . THR   B 1  483  ? 2.886   27.078  115.265 1.00 44.13 ? 481  THR   B C     1 
ATOM   12611 O  O     . THR   B 1  483  ? 2.673   26.810  114.076 1.00 49.62 ? 481  THR   B O     1 
ATOM   12612 C  CB    . THR   B 1  483  ? 4.457   25.665  116.627 1.00 46.85 ? 481  THR   B CB    1 
ATOM   12613 N  N     . LEU   B 1  484  ? 1.911   27.477  116.088 1.00 46.87 ? 482  LEU   B N     1 
ATOM   12614 C  CA    . LEU   B 1  484  ? 0.528   27.509  115.618 1.00 48.71 ? 482  LEU   B CA    1 
ATOM   12615 C  C     . LEU   B 1  484  ? 0.304   28.630  114.609 1.00 44.04 ? 482  LEU   B C     1 
ATOM   12616 O  O     . LEU   B 1  484  ? -0.487  28.480  113.670 1.00 47.85 ? 482  LEU   B O     1 
ATOM   12617 C  CB    . LEU   B 1  484  ? -0.442  27.610  116.800 1.00 45.82 ? 482  LEU   B CB    1 
ATOM   12618 C  CG    . LEU   B 1  484  ? -0.590  28.936  117.551 1.00 45.13 ? 482  LEU   B CG    1 
ATOM   12619 C  CD1   . LEU   B 1  484  ? -1.697  29.798  116.953 1.00 43.10 ? 482  LEU   B CD1   1 
ATOM   12620 C  CD2   . LEU   B 1  484  ? -0.848  28.691  119.025 1.00 42.81 ? 482  LEU   B CD2   1 
ATOM   12621 N  N     . LEU   B 1  485  ? 0.987   29.762  114.785 1.00 41.49 ? 483  LEU   B N     1 
ATOM   12622 C  CA    . LEU   B 1  485  ? 0.824   30.874  113.856 1.00 47.56 ? 483  LEU   B CA    1 
ATOM   12623 C  C     . LEU   B 1  485  ? 1.320   30.536  112.457 1.00 47.68 ? 483  LEU   B C     1 
ATOM   12624 O  O     . LEU   B 1  485  ? 0.866   31.152  111.486 1.00 43.91 ? 483  LEU   B O     1 
ATOM   12625 C  CB    . LEU   B 1  485  ? 1.559   32.111  114.385 1.00 41.80 ? 483  LEU   B CB    1 
ATOM   12626 C  CG    . LEU   B 1  485  ? 0.913   32.852  115.559 1.00 41.46 ? 483  LEU   B CG    1 
ATOM   12627 C  CD1   . LEU   B 1  485  ? 1.823   33.964  116.050 1.00 44.62 ? 483  LEU   B CD1   1 
ATOM   12628 C  CD2   . LEU   B 1  485  ? -0.453  33.405  115.176 1.00 44.62 ? 483  LEU   B CD2   1 
ATOM   12629 N  N     . ALA   B 1  486  ? 2.223   29.558  112.334 1.00 47.94 ? 484  ALA   B N     1 
ATOM   12630 C  CA    . ALA   B 1  486  ? 2.894   29.286  111.068 1.00 42.27 ? 484  ALA   B CA    1 
ATOM   12631 C  C     . ALA   B 1  486  ? 1.953   28.760  109.990 1.00 50.89 ? 484  ALA   B C     1 
ATOM   12632 O  O     . ALA   B 1  486  ? 2.243   28.924  108.800 1.00 49.19 ? 484  ALA   B O     1 
ATOM   12633 C  CB    . ALA   B 1  486  ? 4.053   28.310  111.284 1.00 45.28 ? 484  ALA   B CB    1 
ATOM   12634 N  N     . TYR   B 1  487  ? 0.843   28.120  110.368 1.00 50.61 ? 485  TYR   B N     1 
ATOM   12635 C  CA    . TYR   B 1  487  ? -0.119  27.665  109.371 1.00 45.51 ? 485  TYR   B CA    1 
ATOM   12636 C  C     . TYR   B 1  487  ? -1.557  27.923  109.805 1.00 47.72 ? 485  TYR   B C     1 
ATOM   12637 O  O     . TYR   B 1  487  ? -2.474  27.242  109.327 1.00 38.74 ? 485  TYR   B O     1 
ATOM   12638 C  CB    . TYR   B 1  487  ? 0.078   26.188  109.004 1.00 55.49 ? 485  TYR   B CB    1 
ATOM   12639 C  CG    . TYR   B 1  487  ? 1.374   25.904  108.274 1.00 57.31 ? 485  TYR   B CG    1 
ATOM   12640 C  CD1   . TYR   B 1  487  ? 1.518   26.213  106.925 1.00 57.81 ? 485  TYR   B CD1   1 
ATOM   12641 C  CD2   . TYR   B 1  487  ? 2.452   25.319  108.931 1.00 56.71 ? 485  TYR   B CD2   1 
ATOM   12642 C  CE1   . TYR   B 1  487  ? 2.701   25.955  106.252 1.00 59.21 ? 485  TYR   B CE1   1 
ATOM   12643 C  CE2   . TYR   B 1  487  ? 3.638   25.055  108.267 1.00 56.04 ? 485  TYR   B CE2   1 
ATOM   12644 C  CZ    . TYR   B 1  487  ? 3.758   25.375  106.928 1.00 59.37 ? 485  TYR   B CZ    1 
ATOM   12645 O  OH    . TYR   B 1  487  ? 4.938   25.113  106.266 1.00 62.69 ? 485  TYR   B OH    1 
ATOM   12646 N  N     . LEU   B 1  488  ? -1.779  28.889  110.695 1.00 48.30 ? 486  LEU   B N     1 
ATOM   12647 C  CA    . LEU   B 1  488  ? -3.145  29.217  111.083 1.00 43.28 ? 486  LEU   B CA    1 
ATOM   12648 C  C     . LEU   B 1  488  ? -3.935  29.783  109.911 1.00 40.62 ? 486  LEU   B C     1 
ATOM   12649 O  O     . LEU   B 1  488  ? -5.159  29.621  109.851 1.00 34.17 ? 486  LEU   B O     1 
ATOM   12650 C  CB    . LEU   B 1  488  ? -3.137  30.197  112.253 1.00 40.90 ? 486  LEU   B CB    1 
ATOM   12651 C  CG    . LEU   B 1  488  ? -4.502  30.398  112.893 1.00 41.50 ? 486  LEU   B CG    1 
ATOM   12652 C  CD1   . LEU   B 1  488  ? -5.072  29.041  113.245 1.00 49.11 ? 486  LEU   B CD1   1 
ATOM   12653 C  CD2   . LEU   B 1  488  ? -4.363  31.258  114.129 1.00 33.99 ? 486  LEU   B CD2   1 
ATOM   12654 N  N     . VAL   B 1  489  ? -3.255  30.447  108.970 1.00 42.05 ? 487  VAL   B N     1 
ATOM   12655 C  CA    . VAL   B 1  489  ? -3.938  30.984  107.793 1.00 34.43 ? 487  VAL   B CA    1 
ATOM   12656 C  C     . VAL   B 1  489  ? -4.726  29.883  107.092 1.00 37.89 ? 487  VAL   B C     1 
ATOM   12657 O  O     . VAL   B 1  489  ? -5.936  30.000  106.871 1.00 42.99 ? 487  VAL   B O     1 
ATOM   12658 C  CB    . VAL   B 1  489  ? -2.935  31.664  106.846 1.00 38.81 ? 487  VAL   B CB    1 
ATOM   12659 N  N     . ARG   B 1  490  ? -4.049  28.779  106.765 1.00 42.87 ? 488  ARG   B N     1 
ATOM   12660 C  CA    . ARG   B 1  490  ? -4.703  27.686  106.050 1.00 43.23 ? 488  ARG   B CA    1 
ATOM   12661 C  C     . ARG   B 1  490  ? -5.807  27.057  106.890 1.00 43.07 ? 488  ARG   B C     1 
ATOM   12662 O  O     . ARG   B 1  490  ? -6.866  26.694  106.364 1.00 42.30 ? 488  ARG   B O     1 
ATOM   12663 C  CB    . ARG   B 1  490  ? -3.663  26.638  105.647 1.00 43.64 ? 488  ARG   B CB    1 
ATOM   12664 C  CG    . ARG   B 1  490  ? -4.169  25.538  104.722 1.00 43.06 ? 488  ARG   B CG    1 
ATOM   12665 C  CD    . ARG   B 1  490  ? -3.085  24.478  104.525 1.00 41.72 ? 488  ARG   B CD    1 
ATOM   12666 N  NE    . ARG   B 1  490  ? -2.785  23.788  105.777 1.00 43.14 ? 488  ARG   B NE    1 
ATOM   12667 C  CZ    . ARG   B 1  490  ? -1.590  23.319  106.114 1.00 41.13 ? 488  ARG   B CZ    1 
ATOM   12668 N  NH1   . ARG   B 1  490  ? -0.535  23.487  105.331 1.00 37.73 ? 488  ARG   B NH1   1 
ATOM   12669 N  NH2   . ARG   B 1  490  ? -1.447  22.677  107.271 1.00 34.99 ? 488  ARG   B NH2   1 
ATOM   12670 N  N     . ARG   B 1  491  ? -5.584  26.937  108.202 1.00 38.26 ? 489  ARG   B N     1 
ATOM   12671 C  CA    . ARG   B 1  491  ? -6.580  26.314  109.066 1.00 42.30 ? 489  ARG   B CA    1 
ATOM   12672 C  C     . ARG   B 1  491  ? -7.846  27.155  109.143 1.00 44.86 ? 489  ARG   B C     1 
ATOM   12673 O  O     . ARG   B 1  491  ? -8.957  26.614  109.120 1.00 44.48 ? 489  ARG   B O     1 
ATOM   12674 C  CB    . ARG   B 1  491  ? -5.993  26.092  110.461 1.00 48.11 ? 489  ARG   B CB    1 
ATOM   12675 N  N     . LEU   B 1  492  ? -7.695  28.484  109.212 1.00 47.32 ? 490  LEU   B N     1 
ATOM   12676 C  CA    . LEU   B 1  492  ? -8.850  29.371  109.330 1.00 47.84 ? 490  LEU   B CA    1 
ATOM   12677 C  C     . LEU   B 1  492  ? -9.617  29.470  108.016 1.00 48.69 ? 490  LEU   B C     1 
ATOM   12678 O  O     . LEU   B 1  492  ? -10.851 29.561  108.016 1.00 37.67 ? 490  LEU   B O     1 
ATOM   12679 C  CB    . LEU   B 1  492  ? -8.397  30.757  109.794 1.00 41.17 ? 490  LEU   B CB    1 
ATOM   12680 N  N     . LEU   B 1  493  ? -8.904  29.465  106.885 1.00 49.56 ? 491  LEU   B N     1 
ATOM   12681 C  CA    . LEU   B 1  493  ? -9.575  29.509  105.590 1.00 36.13 ? 491  LEU   B CA    1 
ATOM   12682 C  C     . LEU   B 1  493  ? -10.493 28.315  105.376 1.00 48.40 ? 491  LEU   B C     1 
ATOM   12683 O  O     . LEU   B 1  493  ? -11.418 28.398  104.559 1.00 51.30 ? 491  LEU   B O     1 
ATOM   12684 C  CB    . LEU   B 1  493  ? -8.550  29.586  104.460 1.00 45.69 ? 491  LEU   B CB    1 
ATOM   12685 C  CG    . LEU   B 1  493  ? -8.057  30.989  104.132 1.00 38.33 ? 491  LEU   B CG    1 
ATOM   12686 C  CD1   . LEU   B 1  493  ? -7.263  30.965  102.833 1.00 42.99 ? 491  LEU   B CD1   1 
ATOM   12687 C  CD2   . LEU   B 1  493  ? -9.233  31.970  104.055 1.00 44.09 ? 491  LEU   B CD2   1 
ATOM   12688 N  N     . GLU   B 1  494  ? -10.258 27.214  106.081 1.00 48.84 ? 492  GLU   B N     1 
ATOM   12689 C  CA    . GLU   B 1  494  ? -11.106 26.034  105.978 1.00 45.48 ? 492  GLU   B CA    1 
ATOM   12690 C  C     . GLU   B 1  494  ? -12.463 26.303  106.610 1.00 42.25 ? 492  GLU   B C     1 
ATOM   12691 O  O     . GLU   B 1  494  ? -13.455 25.675  106.242 1.00 50.48 ? 492  GLU   B O     1 
ATOM   12692 C  CB    . GLU   B 1  494  ? -10.447 24.845  106.668 1.00 38.03 ? 492  GLU   B CB    1 
ATOM   12693 N  N     . GLY   B 1  496  ? -13.320 29.614  107.071 1.00 53.86 ? 494  GLY   B N     1 
ATOM   12694 C  CA    . GLY   B 1  496  ? -13.651 31.025  107.135 1.00 51.31 ? 494  GLY   B CA    1 
ATOM   12695 C  C     . GLY   B 1  496  ? -13.833 31.686  105.779 1.00 61.52 ? 494  GLY   B C     1 
ATOM   12696 O  O     . GLY   B 1  496  ? -14.121 32.883  105.705 1.00 66.42 ? 494  GLY   B O     1 
ATOM   12697 N  N     . ALA   B 1  497  ? -13.655 30.916  104.706 1.00 61.92 ? 495  ALA   B N     1 
ATOM   12698 C  CA    . ALA   B 1  497  ? -13.893 31.421  103.362 1.00 57.05 ? 495  ALA   B CA    1 
ATOM   12699 C  C     . ALA   B 1  497  ? -15.392 31.532  103.103 1.00 44.91 ? 495  ALA   B C     1 
ATOM   12700 O  O     . ALA   B 1  497  ? -16.206 30.843  103.723 1.00 51.55 ? 495  ALA   B O     1 
ATOM   12701 C  CB    . ALA   B 1  497  ? -13.251 30.510  102.316 1.00 46.34 ? 495  ALA   B CB    1 
ATOM   12702 N  N     . ASN   B 1  498  ? -15.749 32.415  102.162 1.00 48.73 ? 496  ASN   B N     1 
ATOM   12703 C  CA    . ASN   B 1  498  ? -17.157 32.724  101.913 1.00 47.12 ? 496  ASN   B CA    1 
ATOM   12704 C  C     . ASN   B 1  498  ? -17.975 31.467  101.642 1.00 47.12 ? 496  ASN   B C     1 
ATOM   12705 O  O     . ASN   B 1  498  ? -19.132 31.362  102.068 1.00 42.21 ? 496  ASN   B O     1 
ATOM   12706 C  CB    . ASN   B 1  498  ? -17.281 33.704  100.745 1.00 50.45 ? 496  ASN   B CB    1 
ATOM   12707 N  N     . SER   B 1  499  ? -17.389 30.498  100.942 1.00 37.40 ? 497  SER   B N     1 
ATOM   12708 C  CA    . SER   B 1  499  ? -18.080 29.252  100.641 1.00 40.42 ? 497  SER   B CA    1 
ATOM   12709 C  C     . SER   B 1  499  ? -18.062 28.263  101.800 1.00 32.45 ? 497  SER   B C     1 
ATOM   12710 O  O     . SER   B 1  499  ? -18.746 27.238  101.722 1.00 34.65 ? 497  SER   B O     1 
ATOM   12711 C  CB    . SER   B 1  499  ? -17.437 28.596  99.419  1.00 37.27 ? 497  SER   B CB    1 
ATOM   12712 O  OG    . SER   B 1  499  ? -16.042 28.472  99.619  1.00 39.62 ? 497  SER   B OG    1 
ATOM   12713 N  N     . SER   B 1  500  ? -17.289 28.531  102.849 1.00 34.92 ? 498  SER   B N     1 
ATOM   12714 C  CA    . SER   B 1  500  ? -17.156 27.581  103.943 1.00 31.21 ? 498  SER   B CA    1 
ATOM   12715 C  C     . SER   B 1  500  ? -18.406 27.571  104.807 1.00 36.55 ? 498  SER   B C     1 
ATOM   12716 O  O     . SER   B 1  500  ? -19.010 28.615  105.063 1.00 41.06 ? 498  SER   B O     1 
ATOM   12717 C  CB    . SER   B 1  500  ? -15.954 27.940  104.817 1.00 37.82 ? 498  SER   B CB    1 
ATOM   12718 O  OG    . SER   B 1  500  ? -14.749 27.529  104.214 1.00 44.04 ? 498  SER   B OG    1 
ATOM   12719 N  N     . PHE   B 1  501  ? -18.791 26.374  105.258 1.00 30.56 ? 499  PHE   B N     1 
ATOM   12720 C  CA    . PHE   B 1  501  ? -19.909 26.259  106.189 1.00 35.41 ? 499  PHE   B CA    1 
ATOM   12721 C  C     . PHE   B 1  501  ? -19.665 27.078  107.451 1.00 42.93 ? 499  PHE   B C     1 
ATOM   12722 O  O     . PHE   B 1  501  ? -20.606 27.650  108.016 1.00 46.96 ? 499  PHE   B O     1 
ATOM   12723 C  CB    . PHE   B 1  501  ? -20.159 24.790  106.543 1.00 33.50 ? 499  PHE   B CB    1 
ATOM   12724 C  CG    . PHE   B 1  501  ? -21.351 24.573  107.445 1.00 31.46 ? 499  PHE   B CG    1 
ATOM   12725 C  CD1   . PHE   B 1  501  ? -21.218 24.638  108.824 1.00 37.56 ? 499  PHE   B CD1   1 
ATOM   12726 C  CD2   . PHE   B 1  501  ? -22.597 24.295  106.911 1.00 34.56 ? 499  PHE   B CD2   1 
ATOM   12727 C  CE1   . PHE   B 1  501  ? -22.320 24.442  109.655 1.00 34.87 ? 499  PHE   B CE1   1 
ATOM   12728 C  CE2   . PHE   B 1  501  ? -23.693 24.095  107.733 1.00 39.47 ? 499  PHE   B CE2   1 
ATOM   12729 C  CZ    . PHE   B 1  501  ? -23.552 24.169  109.106 1.00 35.88 ? 499  PHE   B CZ    1 
ATOM   12730 N  N     . VAL   B 1  502  ? -18.411 27.151  107.906 1.00 45.26 ? 500  VAL   B N     1 
ATOM   12731 C  CA    . VAL   B 1  502  ? -18.108 27.848  109.153 1.00 55.31 ? 500  VAL   B CA    1 
ATOM   12732 C  C     . VAL   B 1  502  ? -18.230 29.360  109.015 1.00 54.63 ? 500  VAL   B C     1 
ATOM   12733 O  O     . VAL   B 1  502  ? -18.454 30.052  110.014 1.00 58.73 ? 500  VAL   B O     1 
ATOM   12734 C  CB    . VAL   B 1  502  ? -16.740 27.427  109.725 1.00 55.87 ? 500  VAL   B CB    1 
ATOM   12735 C  CG1   . VAL   B 1  502  ? -16.707 25.924  109.959 1.00 50.22 ? 500  VAL   B CG1   1 
ATOM   12736 C  CG2   . VAL   B 1  502  ? -15.611 27.870  108.802 1.00 47.60 ? 500  VAL   B CG2   1 
ATOM   12737 N  N     . HIS   B 1  503  ? -18.077 29.898  107.805 1.00 43.49 ? 501  HIS   B N     1 
ATOM   12738 C  CA    . HIS   B 1  503  ? -18.388 31.304  107.587 1.00 45.67 ? 501  HIS   B CA    1 
ATOM   12739 C  C     . HIS   B 1  503  ? -19.877 31.505  107.329 1.00 49.13 ? 501  HIS   B C     1 
ATOM   12740 O  O     . HIS   B 1  503  ? -20.470 32.475  107.817 1.00 45.28 ? 501  HIS   B O     1 
ATOM   12741 C  CB    . HIS   B 1  503  ? -17.561 31.857  106.425 1.00 48.71 ? 501  HIS   B CB    1 
ATOM   12742 C  CG    . HIS   B 1  503  ? -18.056 33.171  105.902 1.00 47.96 ? 501  HIS   B CG    1 
ATOM   12743 N  ND1   . HIS   B 1  503  ? -19.062 33.266  104.962 1.00 48.09 ? 501  HIS   B ND1   1 
ATOM   12744 C  CD2   . HIS   B 1  503  ? -17.685 34.442  106.186 1.00 46.77 ? 501  HIS   B CD2   1 
ATOM   12745 C  CE1   . HIS   B 1  503  ? -19.291 34.539  104.692 1.00 41.90 ? 501  HIS   B CE1   1 
ATOM   12746 N  NE2   . HIS   B 1  503  ? -18.468 35.273  105.421 1.00 44.36 ? 501  HIS   B NE2   1 
ATOM   12747 N  N     . ARG   B 1  504  ? -20.496 30.587  106.583 1.00 39.98 ? 502  ARG   B N     1 
ATOM   12748 C  CA    . ARG   B 1  504  ? -21.898 30.740  106.214 1.00 37.82 ? 502  ARG   B CA    1 
ATOM   12749 C  C     . ARG   B 1  504  ? -22.824 30.590  107.413 1.00 42.23 ? 502  ARG   B C     1 
ATOM   12750 O  O     . ARG   B 1  504  ? -23.886 31.220  107.450 1.00 40.80 ? 502  ARG   B O     1 
ATOM   12751 C  CB    . ARG   B 1  504  ? -22.259 29.736  105.124 1.00 39.76 ? 502  ARG   B CB    1 
ATOM   12752 C  CG    . ARG   B 1  504  ? -21.587 30.045  103.803 1.00 41.38 ? 502  ARG   B CG    1 
ATOM   12753 C  CD    . ARG   B 1  504  ? -21.566 28.842  102.872 1.00 34.78 ? 502  ARG   B CD    1 
ATOM   12754 N  NE    . ARG   B 1  504  ? -22.889 28.286  102.629 1.00 34.28 ? 502  ARG   B NE    1 
ATOM   12755 C  CZ    . ARG   B 1  504  ? -23.813 28.856  101.868 1.00 39.89 ? 502  ARG   B CZ    1 
ATOM   12756 N  NH1   . ARG   B 1  504  ? -23.619 30.045  101.319 1.00 40.78 ? 502  ARG   B NH1   1 
ATOM   12757 N  NH2   . ARG   B 1  504  ? -24.958 28.217  101.651 1.00 37.06 ? 502  ARG   B NH2   1 
ATOM   12758 N  N     . ILE   B 1  505  ? -22.447 29.762  108.391 1.00 41.05 ? 503  ILE   B N     1 
ATOM   12759 C  CA    . ILE   B 1  505  ? -23.286 29.568  109.572 1.00 44.58 ? 503  ILE   B CA    1 
ATOM   12760 C  C     . ILE   B 1  505  ? -23.462 30.877  110.333 1.00 45.51 ? 503  ILE   B C     1 
ATOM   12761 O  O     . ILE   B 1  505  ? -24.506 31.108  110.958 1.00 40.80 ? 503  ILE   B O     1 
ATOM   12762 C  CB    . ILE   B 1  505  ? -22.709 28.440  110.456 1.00 39.57 ? 503  ILE   B CB    1 
ATOM   12763 C  CG1   . ILE   B 1  505  ? -23.711 28.022  111.534 1.00 44.43 ? 503  ILE   B CG1   1 
ATOM   12764 C  CG2   . ILE   B 1  505  ? -21.383 28.861  111.082 1.00 48.57 ? 503  ILE   B CG2   1 
ATOM   12765 C  CD1   . ILE   B 1  505  ? -24.875 27.228  110.999 1.00 40.57 ? 503  ILE   B CD1   1 
ATOM   12766 N  N     . ASN   B 1  506  ? -22.466 31.760  110.273 1.00 43.15 ? 504  ASN   B N     1 
ATOM   12767 C  CA    . ASN   B 1  506  ? -22.498 33.039  110.967 1.00 47.95 ? 504  ASN   B CA    1 
ATOM   12768 C  C     . ASN   B 1  506  ? -22.929 34.189  110.068 1.00 50.37 ? 504  ASN   B C     1 
ATOM   12769 O  O     . ASN   B 1  506  ? -22.851 35.348  110.484 1.00 50.03 ? 504  ASN   B O     1 
ATOM   12770 C  CB    . ASN   B 1  506  ? -21.135 33.335  111.592 1.00 50.10 ? 504  ASN   B CB    1 
ATOM   12771 C  CG    . ASN   B 1  506  ? -20.769 32.345  112.679 1.00 51.19 ? 504  ASN   B CG    1 
ATOM   12772 O  OD1   . ASN   B 1  506  ? -21.606 31.971  113.501 1.00 52.97 ? 504  ASN   B OD1   1 
ATOM   12773 N  ND2   . ASN   B 1  506  ? -19.518 31.903  112.679 1.00 61.14 ? 504  ASN   B ND2   1 
ATOM   12774 N  N     . ASP   B 1  507  ? -23.373 33.900  108.846 1.00 47.23 ? 505  ASP   B N     1 
ATOM   12775 C  CA    . ASP   B 1  507  ? -23.864 34.939  107.958 1.00 49.00 ? 505  ASP   B CA    1 
ATOM   12776 C  C     . ASP   B 1  507  ? -25.382 34.947  108.028 1.00 55.96 ? 505  ASP   B C     1 
ATOM   12777 O  O     . ASP   B 1  507  ? -26.016 33.964  107.613 1.00 48.94 ? 505  ASP   B O     1 
ATOM   12778 C  CB    . ASP   B 1  507  ? -23.402 34.676  106.527 1.00 52.94 ? 505  ASP   B CB    1 
ATOM   12779 C  CG    . ASP   B 1  507  ? -23.463 35.918  105.659 1.00 58.08 ? 505  ASP   B CG    1 
ATOM   12780 O  OD1   . ASP   B 1  507  ? -24.358 36.760  105.881 1.00 64.75 ? 505  ASP   B OD1   1 
ATOM   12781 O  OD2   . ASP   B 1  507  ? -22.609 36.056  104.759 1.00 65.58 ? 505  ASP   B OD2   1 
ATOM   12782 N  N     . PRO   B 1  508  ? -26.010 36.007  108.547 1.00 61.26 ? 506  PRO   B N     1 
ATOM   12783 C  CA    . PRO   B 1  508  ? -27.479 36.021  108.626 1.00 55.90 ? 506  PRO   B CA    1 
ATOM   12784 C  C     . PRO   B 1  508  ? -28.157 36.109  107.271 1.00 59.56 ? 506  PRO   B C     1 
ATOM   12785 O  O     . PRO   B 1  508  ? -29.361 35.839  107.182 1.00 61.74 ? 506  PRO   B O     1 
ATOM   12786 C  CB    . PRO   B 1  508  ? -27.783 37.258  109.487 1.00 63.05 ? 506  PRO   B CB    1 
ATOM   12787 C  CG    . PRO   B 1  508  ? -26.463 37.656  110.101 1.00 63.75 ? 506  PRO   B CG    1 
ATOM   12788 C  CD    . PRO   B 1  508  ? -25.416 37.220  109.129 1.00 54.95 ? 506  PRO   B CD    1 
ATOM   12789 N  N     . LYS   B 1  509  ? -27.426 36.483  106.218 1.00 56.10 ? 507  LYS   B N     1 
ATOM   12790 C  CA    . LYS   B 1  509  ? -28.009 36.505  104.882 1.00 58.13 ? 507  LYS   B CA    1 
ATOM   12791 C  C     . LYS   B 1  509  ? -28.238 35.098  104.347 1.00 61.49 ? 507  LYS   B C     1 
ATOM   12792 O  O     . LYS   B 1  509  ? -29.115 34.894  103.500 1.00 65.84 ? 507  LYS   B O     1 
ATOM   12793 C  CB    . LYS   B 1  509  ? -27.114 37.299  103.931 1.00 54.08 ? 507  LYS   B CB    1 
ATOM   12794 N  N     . VAL   B 1  510  ? -27.471 34.123  104.823 1.00 60.10 ? 508  VAL   B N     1 
ATOM   12795 C  CA    . VAL   B 1  510  ? -27.629 32.734  104.410 1.00 53.96 ? 508  VAL   B CA    1 
ATOM   12796 C  C     . VAL   B 1  510  ? -28.665 32.083  105.318 1.00 51.08 ? 508  VAL   B C     1 
ATOM   12797 O  O     . VAL   B 1  510  ? -28.501 32.055  106.542 1.00 53.96 ? 508  VAL   B O     1 
ATOM   12798 C  CB    . VAL   B 1  510  ? -26.288 31.985  104.467 1.00 46.55 ? 508  VAL   B CB    1 
ATOM   12799 N  N     . SER   B 1  511  ? -29.734 31.565  104.721 1.00 48.19 ? 509  SER   B N     1 
ATOM   12800 C  CA    . SER   B 1  511  ? -30.800 30.945  105.488 1.00 51.73 ? 509  SER   B CA    1 
ATOM   12801 C  C     . SER   B 1  511  ? -30.467 29.488  105.786 1.00 53.20 ? 509  SER   B C     1 
ATOM   12802 O  O     . SER   B 1  511  ? -29.534 28.903  105.228 1.00 50.82 ? 509  SER   B O     1 
ATOM   12803 C  CB    . SER   B 1  511  ? -32.114 30.996  104.715 1.00 53.21 ? 509  SER   B CB    1 
ATOM   12804 O  OG    . SER   B 1  511  ? -32.180 29.935  103.776 1.00 54.22 ? 509  SER   B OG    1 
ATOM   12805 N  N     . ILE   B 1  512  ? -31.264 28.895  106.672 1.00 46.12 ? 510  ILE   B N     1 
ATOM   12806 C  CA    . ILE   B 1  512  ? -31.085 27.484  106.990 1.00 47.20 ? 510  ILE   B CA    1 
ATOM   12807 C  C     . ILE   B 1  512  ? -31.478 26.612  105.803 1.00 51.84 ? 510  ILE   B C     1 
ATOM   12808 O  O     . ILE   B 1  512  ? -30.851 25.578  105.542 1.00 45.73 ? 510  ILE   B O     1 
ATOM   12809 C  CB    . ILE   B 1  512  ? -31.840 27.129  108.281 1.00 43.68 ? 510  ILE   B CB    1 
ATOM   12810 C  CG1   . ILE   B 1  512  ? -31.251 27.935  109.440 1.00 44.10 ? 510  ILE   B CG1   1 
ATOM   12811 C  CG2   . ILE   B 1  512  ? -31.770 25.633  108.559 1.00 44.66 ? 510  ILE   B CG2   1 
ATOM   12812 C  CD1   . ILE   B 1  512  ? -32.028 27.835  110.719 1.00 46.10 ? 510  ILE   B CD1   1 
ATOM   12813 N  N     . ASP   B 1  513  ? -32.503 27.026  105.053 1.00 47.21 ? 511  ASP   B N     1 
ATOM   12814 C  CA    . ASP   B 1  513  ? -32.869 26.310  103.835 1.00 49.09 ? 511  ASP   B CA    1 
ATOM   12815 C  C     . ASP   B 1  513  ? -31.682 26.209  102.885 1.00 44.78 ? 511  ASP   B C     1 
ATOM   12816 O  O     . ASP   B 1  513  ? -31.411 25.141  102.323 1.00 46.74 ? 511  ASP   B O     1 
ATOM   12817 C  CB    . ASP   B 1  513  ? -34.047 27.004  103.148 1.00 51.87 ? 511  ASP   B CB    1 
ATOM   12818 C  CG    . ASP   B 1  513  ? -35.367 26.759  103.855 1.00 59.45 ? 511  ASP   B CG    1 
ATOM   12819 O  OD1   . ASP   B 1  513  ? -35.620 25.612  104.290 1.00 55.00 ? 511  ASP   B OD1   1 
ATOM   12820 O  OD2   . ASP   B 1  513  ? -36.157 27.719  103.973 1.00 67.60 ? 511  ASP   B OD2   1 
ATOM   12821 N  N     . GLU   B 1  514  ? -30.957 27.315  102.700 1.00 44.39 ? 512  GLU   B N     1 
ATOM   12822 C  CA    . GLU   B 1  514  ? -29.760 27.279  101.866 1.00 45.21 ? 512  GLU   B CA    1 
ATOM   12823 C  C     . GLU   B 1  514  ? -28.720 26.323  102.439 1.00 43.67 ? 512  GLU   B C     1 
ATOM   12824 O  O     . GLU   B 1  514  ? -28.103 25.549  101.701 1.00 40.75 ? 512  GLU   B O     1 
ATOM   12825 C  CB    . GLU   B 1  514  ? -29.171 28.683  101.732 1.00 45.73 ? 512  GLU   B CB    1 
ATOM   12826 C  CG    . GLU   B 1  514  ? -30.164 29.740  101.278 1.00 58.43 ? 512  GLU   B CG    1 
ATOM   12827 C  CD    . GLU   B 1  514  ? -29.590 31.144  101.347 1.00 61.92 ? 512  GLU   B CD    1 
ATOM   12828 O  OE1   . GLU   B 1  514  ? -28.422 31.328  100.946 1.00 66.05 ? 512  GLU   B OE1   1 
ATOM   12829 O  OE2   . GLU   B 1  514  ? -30.303 32.061  101.812 1.00 63.46 ? 512  GLU   B OE2   1 
ATOM   12830 N  N     . LEU   B 1  515  ? -28.525 26.352  103.759 1.00 40.36 ? 513  LEU   B N     1 
ATOM   12831 C  CA    . LEU   B 1  515  ? -27.487 25.532  104.373 1.00 38.20 ? 513  LEU   B CA    1 
ATOM   12832 C  C     . LEU   B 1  515  ? -27.815 24.049  104.302 1.00 37.05 ? 513  LEU   B C     1 
ATOM   12833 O  O     . LEU   B 1  515  ? -26.903 23.216  104.276 1.00 37.56 ? 513  LEU   B O     1 
ATOM   12834 C  CB    . LEU   B 1  515  ? -27.263 25.964  105.821 1.00 36.41 ? 513  LEU   B CB    1 
ATOM   12835 C  CG    . LEU   B 1  515  ? -26.716 27.375  106.033 1.00 37.84 ? 513  LEU   B CG    1 
ATOM   12836 C  CD1   . LEU   B 1  515  ? -26.852 27.750  107.499 1.00 41.47 ? 513  LEU   B CD1   1 
ATOM   12837 C  CD2   . LEU   B 1  515  ? -25.269 27.463  105.597 1.00 38.40 ? 513  LEU   B CD2   1 
ATOM   12838 N  N     . ILE   B 1  516  ? -29.103 23.698  104.276 1.00 34.43 ? 514  ILE   B N     1 
ATOM   12839 C  CA    . ILE   B 1  516  ? -29.521 22.302  104.211 1.00 32.32 ? 514  ILE   B CA    1 
ATOM   12840 C  C     . ILE   B 1  516  ? -29.760 21.830  102.787 1.00 30.19 ? 514  ILE   B C     1 
ATOM   12841 O  O     . ILE   B 1  516  ? -30.171 20.678  102.591 1.00 34.76 ? 514  ILE   B O     1 
ATOM   12842 C  CB    . ILE   B 1  516  ? -30.737 22.010  105.112 1.00 37.45 ? 514  ILE   B CB    1 
ATOM   12843 C  CG1   . ILE   B 1  516  ? -32.003 22.649  104.531 1.00 35.23 ? 514  ILE   B CG1   1 
ATOM   12844 C  CG2   . ILE   B 1  516  ? -30.486 22.510  106.522 1.00 40.42 ? 514  ILE   B CG2   1 
ATOM   12845 C  CD1   . ILE   B 1  516  ? -33.246 22.433  105.375 1.00 41.89 ? 514  ILE   B CD1   1 
ATOM   12846 N  N     . ALA   B 1  517  ? -29.526 22.685  101.791 1.00 36.26 ? 515  ALA   B N     1 
ATOM   12847 C  CA    . ALA   B 1  517  ? -29.614 22.258  100.402 1.00 38.38 ? 515  ALA   B CA    1 
ATOM   12848 C  C     . ALA   B 1  517  ? -28.761 21.018  100.177 1.00 33.30 ? 515  ALA   B C     1 
ATOM   12849 O  O     . ALA   B 1  517  ? -27.628 20.929  100.660 1.00 34.88 ? 515  ALA   B O     1 
ATOM   12850 C  CB    . ALA   B 1  517  ? -29.131 23.376  99.474  1.00 35.69 ? 515  ALA   B CB    1 
ATOM   12851 N  N     . ASP   B 1  518  ? -29.315 20.059  99.440  1.00 32.32 ? 516  ASP   B N     1 
ATOM   12852 C  CA    . ASP   B 1  518  ? -28.633 18.804  99.166  1.00 33.44 ? 516  ASP   B CA    1 
ATOM   12853 C  C     . ASP   B 1  518  ? -27.714 19.014  97.968  1.00 29.46 ? 516  ASP   B C     1 
ATOM   12854 O  O     . ASP   B 1  518  ? -28.190 19.253  96.854  1.00 29.64 ? 516  ASP   B O     1 
ATOM   12855 C  CB    . ASP   B 1  518  ? -29.663 17.710  98.880  1.00 31.33 ? 516  ASP   B CB    1 
ATOM   12856 C  CG    . ASP   B 1  518  ? -29.037 16.341  98.677  1.00 38.31 ? 516  ASP   B CG    1 
ATOM   12857 O  OD1   . ASP   B 1  518  ? -27.792 16.227  98.652  1.00 31.45 ? 516  ASP   B OD1   1 
ATOM   12858 O  OD2   . ASP   B 1  518  ? -29.808 15.367  98.533  1.00 39.59 ? 516  ASP   B OD2   1 
ATOM   12859 N  N     . PRO   B 1  519  ? -26.396 18.949  98.155  1.00 25.95 ? 517  PRO   B N     1 
ATOM   12860 C  CA    . PRO   B 1  519  ? -25.497 19.146  97.012  1.00 30.51 ? 517  PRO   B CA    1 
ATOM   12861 C  C     . PRO   B 1  519  ? -25.721 18.134  95.909  1.00 24.62 ? 517  PRO   B C     1 
ATOM   12862 O  O     . PRO   B 1  519  ? -25.572 18.472  94.729  1.00 26.44 ? 517  PRO   B O     1 
ATOM   12863 C  CB    . PRO   B 1  519  ? -24.097 19.022  97.635  1.00 27.98 ? 517  PRO   B CB    1 
ATOM   12864 C  CG    . PRO   B 1  519  ? -24.304 18.309  98.920  1.00 31.67 ? 517  PRO   B CG    1 
ATOM   12865 C  CD    . PRO   B 1  519  ? -25.669 18.672  99.403  1.00 27.68 ? 517  PRO   B CD    1 
ATOM   12866 N  N     . VAL   B 1  520  ? -26.088 16.902  96.270  1.00 26.84 ? 518  VAL   B N     1 
ATOM   12867 C  CA    . VAL   B 1  520  ? -26.260 15.841  95.284  1.00 26.89 ? 518  VAL   B CA    1 
ATOM   12868 C  C     . VAL   B 1  520  ? -27.377 16.194  94.313  1.00 29.40 ? 518  VAL   B C     1 
ATOM   12869 O  O     . VAL   B 1  520  ? -27.210 16.118  93.091  1.00 27.99 ? 518  VAL   B O     1 
ATOM   12870 C  CB    . VAL   B 1  520  ? -26.520 14.497  95.984  1.00 27.70 ? 518  VAL   B CB    1 
ATOM   12871 C  CG1   . VAL   B 1  520  ? -26.599 13.377  94.956  1.00 32.25 ? 518  VAL   B CG1   1 
ATOM   12872 C  CG2   . VAL   B 1  520  ? -25.436 14.220  97.035  1.00 26.14 ? 518  VAL   B CG2   1 
ATOM   12873 N  N     . GLU   B 1  521  ? -28.528 16.605  94.843  1.00 28.27 ? 519  GLU   B N     1 
ATOM   12874 C  CA    . GLU   B 1  521  ? -29.644 16.933  93.966  1.00 27.96 ? 519  GLU   B CA    1 
ATOM   12875 C  C     . GLU   B 1  521  ? -29.409 18.229  93.206  1.00 29.95 ? 519  GLU   B C     1 
ATOM   12876 O  O     . GLU   B 1  521  ? -29.859 18.362  92.063  1.00 33.30 ? 519  GLU   B O     1 
ATOM   12877 C  CB    . GLU   B 1  521  ? -30.950 16.973  94.757  1.00 31.61 ? 519  GLU   B CB    1 
ATOM   12878 C  CG    . GLU   B 1  521  ? -31.328 15.624  95.341  1.00 34.89 ? 519  GLU   B CG    1 
ATOM   12879 C  CD    . GLU   B 1  521  ? -31.391 14.531  94.286  1.00 42.80 ? 519  GLU   B CD    1 
ATOM   12880 O  OE1   . GLU   B 1  521  ? -31.801 14.826  93.142  1.00 44.13 ? 519  GLU   B OE1   1 
ATOM   12881 O  OE2   . GLU   B 1  521  ? -31.031 13.375  94.599  1.00 46.23 ? 519  GLU   B OE2   1 
ATOM   12882 N  N     . VAL   B 1  522  ? -28.708 19.189  93.807  1.00 29.30 ? 520  VAL   B N     1 
ATOM   12883 C  CA    . VAL   B 1  522  ? -28.392 20.417  93.086  1.00 27.76 ? 520  VAL   B CA    1 
ATOM   12884 C  C     . VAL   B 1  522  ? -27.472 20.124  91.905  1.00 32.58 ? 520  VAL   B C     1 
ATOM   12885 O  O     . VAL   B 1  522  ? -27.680 20.630  90.795  1.00 33.24 ? 520  VAL   B O     1 
ATOM   12886 C  CB    . VAL   B 1  522  ? -27.807 21.477  94.034  1.00 31.76 ? 520  VAL   B CB    1 
ATOM   12887 C  CG1   . VAL   B 1  522  ? -27.347 22.691  93.240  1.00 31.22 ? 520  VAL   B CG1   1 
ATOM   12888 C  CG2   . VAL   B 1  522  ? -28.840 21.876  95.074  1.00 40.19 ? 520  VAL   B CG2   1 
ATOM   12889 N  N     . VAL   B 1  523  ? -26.444 19.296  92.120  1.00 26.00 ? 521  VAL   B N     1 
ATOM   12890 C  CA    . VAL   B 1  523  ? -25.563 18.921  91.016  1.00 27.14 ? 521  VAL   B CA    1 
ATOM   12891 C  C     . VAL   B 1  523  ? -26.325 18.121  89.967  1.00 27.13 ? 521  VAL   B C     1 
ATOM   12892 O  O     . VAL   B 1  523  ? -26.115 18.294  88.760  1.00 28.17 ? 521  VAL   B O     1 
ATOM   12893 C  CB    . VAL   B 1  523  ? -24.327 18.167  91.540  1.00 27.42 ? 521  VAL   B CB    1 
ATOM   12894 C  CG1   . VAL   B 1  523  ? -23.588 17.500  90.399  1.00 26.76 ? 521  VAL   B CG1   1 
ATOM   12895 C  CG2   . VAL   B 1  523  ? -23.411 19.122  92.271  1.00 29.75 ? 521  VAL   B CG2   1 
ATOM   12896 N  N     . ARG   B 1  524  ? -27.219 17.238  90.406  1.00 27.71 ? 522  ARG   B N     1 
ATOM   12897 C  CA    . ARG   B 1  524  ? -27.939 16.396  89.459  1.00 32.57 ? 522  ARG   B CA    1 
ATOM   12898 C  C     . ARG   B 1  524  ? -28.723 17.237  88.460  1.00 33.62 ? 522  ARG   B C     1 
ATOM   12899 O  O     . ARG   B 1  524  ? -28.828 16.880  87.281  1.00 35.79 ? 522  ARG   B O     1 
ATOM   12900 C  CB    . ARG   B 1  524  ? -28.877 15.453  90.211  1.00 33.64 ? 522  ARG   B CB    1 
ATOM   12901 C  CG    . ARG   B 1  524  ? -29.485 14.382  89.332  1.00 36.93 ? 522  ARG   B CG    1 
ATOM   12902 C  CD    . ARG   B 1  524  ? -30.635 13.677  90.034  1.00 39.14 ? 522  ARG   B CD    1 
ATOM   12903 N  NE    . ARG   B 1  524  ? -30.240 13.159  91.338  1.00 35.89 ? 522  ARG   B NE    1 
ATOM   12904 C  CZ    . ARG   B 1  524  ? -29.562 12.034  91.526  1.00 37.30 ? 522  ARG   B CZ    1 
ATOM   12905 N  NH1   . ARG   B 1  524  ? -29.163 11.287  90.509  1.00 36.30 ? 522  ARG   B NH1   1 
ATOM   12906 N  NH2   . ARG   B 1  524  ? -29.273 11.650  92.768  1.00 36.47 ? 522  ARG   B NH2   1 
ATOM   12907 N  N     . ALA   B 1  525  ? -29.255 18.370  88.907  1.00 33.64 ? 523  ALA   B N     1 
ATOM   12908 C  CA    . ALA   B 1  525  ? -30.162 19.179  88.103  1.00 33.52 ? 523  ALA   B CA    1 
ATOM   12909 C  C     . ALA   B 1  525  ? -29.456 20.247  87.282  1.00 40.28 ? 523  ALA   B C     1 
ATOM   12910 O  O     . ALA   B 1  525  ? -30.126 20.984  86.551  1.00 39.86 ? 523  ALA   B O     1 
ATOM   12911 C  CB    . ALA   B 1  525  ? -31.223 19.828  88.994  1.00 35.39 ? 523  ALA   B CB    1 
ATOM   12912 N  N     . MET   B 1  526  ? -28.135 20.356  87.383  1.00 36.00 ? 524  MET   B N     1 
ATOM   12913 C  CA    A MET   B 1  526  ? -27.406 21.322  86.578  0.54 36.28 ? 524  MET   B CA    1 
ATOM   12914 C  CA    B MET   B 1  526  ? -27.415 21.326  86.578  0.46 36.29 ? 524  MET   B CA    1 
ATOM   12915 C  C     . MET   B 1  526  ? -27.495 20.940  85.101  1.00 35.63 ? 524  MET   B C     1 
ATOM   12916 O  O     . MET   B 1  526  ? -27.600 19.757  84.764  1.00 33.67 ? 524  MET   B O     1 
ATOM   12917 C  CB    A MET   B 1  526  ? -25.943 21.365  87.004  0.54 36.00 ? 524  MET   B CB    1 
ATOM   12918 C  CB    B MET   B 1  526  ? -25.958 21.405  87.024  0.46 36.01 ? 524  MET   B CB    1 
ATOM   12919 C  CG    A MET   B 1  526  ? -25.732 21.945  88.389  0.54 38.45 ? 524  MET   B CG    1 
ATOM   12920 C  CG    B MET   B 1  526  ? -25.725 22.380  88.172  0.46 38.97 ? 524  MET   B CG    1 
ATOM   12921 S  SD    A MET   B 1  526  ? -26.437 23.598  88.552  0.54 43.90 ? 524  MET   B SD    1 
ATOM   12922 S  SD    B MET   B 1  526  ? -24.047 22.318  88.830  0.46 43.88 ? 524  MET   B SD    1 
ATOM   12923 C  CE    A MET   B 1  526  ? -25.429 24.536  87.406  0.54 37.88 ? 524  MET   B CE    1 
ATOM   12924 C  CE    B MET   B 1  526  ? -23.904 23.936  89.583  0.46 42.15 ? 524  MET   B CE    1 
ATOM   12925 N  N     . PRO   B 1  527  ? -27.461 21.926  84.198  1.00 36.97 ? 525  PRO   B N     1 
ATOM   12926 C  CA    . PRO   B 1  527  ? -27.598 21.594  82.767  1.00 45.16 ? 525  PRO   B CA    1 
ATOM   12927 C  C     . PRO   B 1  527  ? -26.473 20.720  82.249  1.00 36.30 ? 525  PRO   B C     1 
ATOM   12928 O  O     . PRO   B 1  527  ? -26.702 19.837  81.413  1.00 34.04 ? 525  PRO   B O     1 
ATOM   12929 C  CB    . PRO   B 1  527  ? -27.628 22.970  82.089  1.00 45.35 ? 525  PRO   B CB    1 
ATOM   12930 C  CG    . PRO   B 1  527  ? -26.898 23.864  83.037  1.00 45.92 ? 525  PRO   B CG    1 
ATOM   12931 C  CD    . PRO   B 1  527  ? -27.249 23.368  84.411  1.00 44.42 ? 525  PRO   B CD    1 
ATOM   12932 N  N     . VAL   B 1  528  ? -25.256 20.941  82.732  1.00 34.03 ? 526  VAL   B N     1 
ATOM   12933 C  CA    . VAL   B 1  528  ? -24.109 20.105  82.415  1.00 31.49 ? 526  VAL   B CA    1 
ATOM   12934 C  C     . VAL   B 1  528  ? -23.552 19.625  83.746  1.00 27.68 ? 526  VAL   B C     1 
ATOM   12935 O  O     . VAL   B 1  528  ? -22.887 20.388  84.457  1.00 32.14 ? 526  VAL   B O     1 
ATOM   12936 C  CB    . VAL   B 1  528  ? -23.045 20.873  81.621  1.00 33.40 ? 526  VAL   B CB    1 
ATOM   12937 C  CG1   . VAL   B 1  528  ? -21.799 20.018  81.444  1.00 31.21 ? 526  VAL   B CG1   1 
ATOM   12938 C  CG2   . VAL   B 1  528  ? -23.598 21.300  80.271  1.00 34.22 ? 526  VAL   B CG2   1 
ATOM   12939 N  N     . VAL   B 1  529  ? -23.822 18.367  84.090  1.00 25.42 ? 527  VAL   B N     1 
ATOM   12940 C  CA    . VAL   B 1  529  ? -23.347 17.840  85.364  1.00 23.20 ? 527  VAL   B CA    1 
ATOM   12941 C  C     . VAL   B 1  529  ? -21.827 17.905  85.409  1.00 26.55 ? 527  VAL   B C     1 
ATOM   12942 O  O     . VAL   B 1  529  ? -21.133 17.439  84.495  1.00 26.36 ? 527  VAL   B O     1 
ATOM   12943 C  CB    . VAL   B 1  529  ? -23.866 16.414  85.588  1.00 22.79 ? 527  VAL   B CB    1 
ATOM   12944 C  CG1   . VAL   B 1  529  ? -23.268 15.828  86.859  1.00 24.07 ? 527  VAL   B CG1   1 
ATOM   12945 C  CG2   . VAL   B 1  529  ? -25.394 16.412  85.671  1.00 28.20 ? 527  VAL   B CG2   1 
ATOM   12946 N  N     . GLY   B 1  530  ? -21.304 18.518  86.467  1.00 24.14 ? 528  GLY   B N     1 
ATOM   12947 C  CA    . GLY   B 1  530  ? -19.879 18.539  86.694  1.00 24.36 ? 528  GLY   B CA    1 
ATOM   12948 C  C     . GLY   B 1  530  ? -19.113 19.580  85.918  1.00 23.43 ? 528  GLY   B C     1 
ATOM   12949 O  O     . GLY   B 1  530  ? -17.892 19.479  85.822  1.00 22.71 ? 528  GLY   B O     1 
ATOM   12950 N  N     . ALA   B 1  531  ? -19.783 20.588  85.364  1.00 23.59 ? 529  ALA   B N     1 
ATOM   12951 C  CA    . ALA   B 1  531  ? -19.067 21.626  84.638  1.00 23.58 ? 529  ALA   B CA    1 
ATOM   12952 C  C     . ALA   B 1  531  ? -18.123 22.363  85.576  1.00 21.37 ? 529  ALA   B C     1 
ATOM   12953 O  O     . ALA   B 1  531  ? -18.447 22.603  86.743  1.00 24.15 ? 529  ALA   B O     1 
ATOM   12954 C  CB    . ALA   B 1  531  ? -20.046 22.620  84.017  1.00 26.94 ? 529  ALA   B CB    1 
ATOM   12955 N  N     . LYS   B 1  532  ? -16.948 22.702  85.054  1.00 21.42 ? 530  LYS   B N     1 
ATOM   12956 C  CA    . LYS   B 1  532  ? -15.962 23.483  85.789  1.00 22.49 ? 530  LYS   B CA    1 
ATOM   12957 C  C     . LYS   B 1  532  ? -16.586 24.793  86.253  1.00 20.97 ? 530  LYS   B C     1 
ATOM   12958 O  O     . LYS   B 1  532  ? -17.543 25.296  85.655  1.00 21.44 ? 530  LYS   B O     1 
ATOM   12959 C  CB    . LYS   B 1  532  ? -14.780 23.779  84.855  1.00 24.31 ? 530  LYS   B CB    1 
ATOM   12960 C  CG    . LYS   B 1  532  ? -13.687 24.701  85.398  1.00 25.41 ? 530  LYS   B CG    1 
ATOM   12961 C  CD    . LYS   B 1  532  ? -12.634 25.001  84.328  1.00 26.50 ? 530  LYS   B CD    1 
ATOM   12962 C  CE    . LYS   B 1  532  ? -13.201 25.795  83.158  1.00 23.98 ? 530  LYS   B CE    1 
ATOM   12963 N  NZ    . LYS   B 1  532  ? -13.656 27.176  83.530  1.00 24.07 ? 530  LYS   B NZ    1 
ATOM   12964 N  N     . HIS   B 1  533  ? -16.052 25.337  87.341  1.00 19.47 ? 531  HIS   B N     1 
ATOM   12965 C  CA    . HIS   B 1  533  ? -16.429 26.675  87.766  1.00 19.93 ? 531  HIS   B CA    1 
ATOM   12966 C  C     . HIS   B 1  533  ? -16.259 27.647  86.607  1.00 22.09 ? 531  HIS   B C     1 
ATOM   12967 O  O     . HIS   B 1  533  ? -15.238 27.635  85.917  1.00 21.44 ? 531  HIS   B O     1 
ATOM   12968 C  CB    . HIS   B 1  533  ? -15.525 27.091  88.917  1.00 19.47 ? 531  HIS   B CB    1 
ATOM   12969 C  CG    . HIS   B 1  533  ? -16.063 28.219  89.733  1.00 23.75 ? 531  HIS   B CG    1 
ATOM   12970 N  ND1   . HIS   B 1  533  ? -16.177 29.501  89.242  1.00 25.82 ? 531  HIS   B ND1   1 
ATOM   12971 C  CD2   . HIS   B 1  533  ? -16.504 28.264  91.014  1.00 29.39 ? 531  HIS   B CD2   1 
ATOM   12972 C  CE1   . HIS   B 1  533  ? -16.686 30.283  90.177  1.00 33.64 ? 531  HIS   B CE1   1 
ATOM   12973 N  NE2   . HIS   B 1  533  ? -16.890 29.558  91.263  1.00 34.37 ? 531  HIS   B NE2   1 
ATOM   12974 N  N     . ASP   B 1  534  ? -17.273 28.495  86.402  1.00 22.67 ? 532  ASP   B N     1 
ATOM   12975 C  CA    . ASP   B 1  534  ? -17.242 29.457  85.302  1.00 27.36 ? 532  ASP   B CA    1 
ATOM   12976 C  C     . ASP   B 1  534  ? -16.111 30.465  85.448  1.00 25.05 ? 532  ASP   B C     1 
ATOM   12977 O  O     . ASP   B 1  534  ? -15.658 31.033  84.448  1.00 28.60 ? 532  ASP   B O     1 
ATOM   12978 C  CB    . ASP   B 1  534  ? -18.570 30.211  85.229  1.00 28.15 ? 532  ASP   B CB    1 
ATOM   12979 C  CG    . ASP   B 1  534  ? -19.682 29.369  84.661  1.00 37.84 ? 532  ASP   B CG    1 
ATOM   12980 O  OD1   . ASP   B 1  534  ? -19.408 28.575  83.734  1.00 45.87 ? 532  ASP   B OD1   1 
ATOM   12981 O  OD2   . ASP   B 1  534  ? -20.828 29.504  85.141  1.00 46.68 ? 532  ASP   B OD2   1 
ATOM   12982 N  N     . ARG   B 1  535  ? -15.647 30.713  86.669  1.00 21.86 ? 533  ARG   B N     1 
ATOM   12983 C  CA    . ARG   B 1  535  ? -14.710 31.798  86.921  1.00 22.24 ? 533  ARG   B CA    1 
ATOM   12984 C  C     . ARG   B 1  535  ? -13.307 31.311  87.251  1.00 23.40 ? 533  ARG   B C     1 
ATOM   12985 O  O     . ARG   B 1  535  ? -12.487 32.103  87.721  1.00 24.95 ? 533  ARG   B O     1 
ATOM   12986 C  CB    . ARG   B 1  535  ? -15.233 32.708  88.033  1.00 29.43 ? 533  ARG   B CB    1 
ATOM   12987 N  N     . ILE   B 1  536  ? -13.018 30.033  87.039  1.00 19.34 ? 534  ILE   B N     1 
ATOM   12988 C  CA    . ILE   B 1  536  ? -11.686 29.478  87.241  1.00 17.83 ? 534  ILE   B CA    1 
ATOM   12989 C  C     . ILE   B 1  536  ? -11.226 28.940  85.901  1.00 19.61 ? 534  ILE   B C     1 
ATOM   12990 O  O     . ILE   B 1  536  ? -11.861 28.038  85.339  1.00 22.05 ? 534  ILE   B O     1 
ATOM   12991 C  CB    . ILE   B 1  536  ? -11.683 28.361  88.287  1.00 19.62 ? 534  ILE   B CB    1 
ATOM   12992 C  CG1   . ILE   B 1  536  ? -12.129 28.912  89.636  1.00 21.57 ? 534  ILE   B CG1   1 
ATOM   12993 C  CG2   . ILE   B 1  536  ? -10.269 27.782  88.428  1.00 19.60 ? 534  ILE   B CG2   1 
ATOM   12994 C  CD1   . ILE   B 1  536  ? -12.164 27.853  90.701  1.00 25.68 ? 534  ILE   B CD1   1 
ATOM   12995 N  N     . ALA   B 1  537  ? -10.136 29.493  85.388  1.00 17.96 ? 535  ALA   B N     1 
ATOM   12996 C  CA    . ALA   B 1  537  ? -9.647  29.089  84.078  1.00 17.82 ? 535  ALA   B CA    1 
ATOM   12997 C  C     . ALA   B 1  537  ? -8.885  27.775  84.176  1.00 16.95 ? 535  ALA   B C     1 
ATOM   12998 O  O     . ALA   B 1  537  ? -8.084  27.577  85.090  1.00 17.86 ? 535  ALA   B O     1 
ATOM   12999 C  CB    . ALA   B 1  537  ? -8.757  30.183  83.496  1.00 18.74 ? 535  ALA   B CB    1 
ATOM   13000 N  N     . LEU   B 1  538  ? -9.168  26.859  83.257  1.00 16.93 ? 536  LEU   B N     1 
ATOM   13001 C  CA    . LEU   B 1  538  ? -8.241  25.763  83.057  1.00 16.49 ? 536  LEU   B CA    1 
ATOM   13002 C  C     . LEU   B 1  538  ? -6.868  26.346  82.742  1.00 17.25 ? 536  LEU   B C     1 
ATOM   13003 O  O     . LEU   B 1  538  ? -6.768  27.444  82.183  1.00 18.38 ? 536  LEU   B O     1 
ATOM   13004 C  CB    . LEU   B 1  538  ? -8.676  24.902  81.875  1.00 19.76 ? 536  LEU   B CB    1 
ATOM   13005 C  CG    . LEU   B 1  538  ? -9.861  23.969  82.092  1.00 23.16 ? 536  LEU   B CG    1 
ATOM   13006 C  CD1   . LEU   B 1  538  ? -10.254 23.328  80.769  1.00 26.00 ? 536  LEU   B CD1   1 
ATOM   13007 C  CD2   . LEU   B 1  538  ? -9.521  22.912  83.142  1.00 22.48 ? 536  LEU   B CD2   1 
ATOM   13008 N  N     . PRO   B 1  539  ? -5.795  25.633  83.087  1.00 16.11 ? 537  PRO   B N     1 
ATOM   13009 C  CA    . PRO   B 1  539  ? -4.455  26.154  82.786  1.00 15.64 ? 537  PRO   B CA    1 
ATOM   13010 C  C     . PRO   B 1  539  ? -4.297  26.536  81.329  1.00 16.46 ? 537  PRO   B C     1 
ATOM   13011 O  O     . PRO   B 1  539  ? -3.711  27.582  81.035  1.00 16.92 ? 537  PRO   B O     1 
ATOM   13012 C  CB    . PRO   B 1  539  ? -3.526  25.021  83.240  1.00 17.81 ? 537  PRO   B CB    1 
ATOM   13013 C  CG    . PRO   B 1  539  ? -4.315  24.358  84.357  1.00 18.05 ? 537  PRO   B CG    1 
ATOM   13014 C  CD    . PRO   B 1  539  ? -5.756  24.424  83.924  1.00 18.50 ? 537  PRO   B CD    1 
ATOM   13015 N  N     . ALA   B 1  540  ? -4.855  25.748  80.414  1.00 17.40 ? 538  ALA   B N     1 
ATOM   13016 C  CA    . ALA   B 1  540  ? -4.735  26.067  78.998  1.00 17.98 ? 538  ALA   B CA    1 
ATOM   13017 C  C     . ALA   B 1  540  ? -5.423  27.370  78.637  1.00 19.70 ? 538  ALA   B C     1 
ATOM   13018 O  O     . ALA   B 1  540  ? -5.099  27.964  77.600  1.00 18.94 ? 538  ALA   B O     1 
ATOM   13019 C  CB    . ALA   B 1  540  ? -5.307  24.929  78.157  1.00 19.11 ? 538  ALA   B CB    1 
ATOM   13020 N  N     . GLU   B 1  541  ? -6.370  27.821  79.458  1.00 19.16 ? 539  GLU   B N     1 
ATOM   13021 C  CA    . GLU   B 1  541  ? -7.244  28.933  79.106  1.00 17.09 ? 539  GLU   B CA    1 
ATOM   13022 C  C     . GLU   B 1  541  ? -6.938  30.203  79.903  1.00 15.96 ? 539  GLU   B C     1 
ATOM   13023 O  O     . GLU   B 1  541  ? -7.754  31.128  79.926  1.00 19.05 ? 539  GLU   B O     1 
ATOM   13024 C  CB    . GLU   B 1  541  ? -8.706  28.485  79.213  1.00 20.88 ? 539  GLU   B CB    1 
ATOM   13025 C  CG    . GLU   B 1  541  ? -8.953  27.278  78.290  1.00 25.70 ? 539  GLU   B CG    1 
ATOM   13026 C  CD    . GLU   B 1  541  ? -10.360 26.696  78.315  1.00 37.67 ? 539  GLU   B CD    1 
ATOM   13027 O  OE1   . GLU   B 1  541  ? -11.181 27.096  79.159  1.00 38.17 ? 539  GLU   B OE1   1 
ATOM   13028 O  OE2   . GLU   B 1  541  ? -10.636 25.814  77.472  1.00 39.68 ? 539  GLU   B OE2   1 
ATOM   13029 N  N     . LEU   B 1  542  ? -5.747  30.290  80.507  1.00 16.69 ? 540  LEU   B N     1 
ATOM   13030 C  CA    . LEU   B 1  542  ? -5.400  31.461  81.313  1.00 18.44 ? 540  LEU   B CA    1 
ATOM   13031 C  C     . LEU   B 1  542  ? -5.518  32.761  80.537  1.00 17.77 ? 540  LEU   B C     1 
ATOM   13032 O  O     . LEU   B 1  542  ? -5.788  33.812  81.130  1.00 21.43 ? 540  LEU   B O     1 
ATOM   13033 C  CB    . LEU   B 1  542  ? -3.963  31.370  81.812  1.00 19.84 ? 540  LEU   B CB    1 
ATOM   13034 C  CG    . LEU   B 1  542  ? -3.640  30.435  82.954  1.00 22.00 ? 540  LEU   B CG    1 
ATOM   13035 C  CD1   . LEU   B 1  542  ? -2.222  30.720  83.431  1.00 20.33 ? 540  LEU   B CD1   1 
ATOM   13036 C  CD2   . LEU   B 1  542  ? -4.644  30.593  84.076  1.00 21.64 ? 540  LEU   B CD2   1 
ATOM   13037 N  N     . PHE   B 1  543  ? -5.294  32.726  79.225  1.00 17.72 ? 541  PHE   B N     1 
ATOM   13038 C  CA    . PHE   B 1  543  ? -5.293  33.933  78.413  1.00 19.02 ? 541  PHE   B CA    1 
ATOM   13039 C  C     . PHE   B 1  543  ? -6.558  34.067  77.599  1.00 19.28 ? 541  PHE   B C     1 
ATOM   13040 O  O     . PHE   B 1  543  ? -6.657  34.960  76.751  1.00 21.15 ? 541  PHE   B O     1 
ATOM   13041 C  CB    . PHE   B 1  543  ? -4.030  33.985  77.557  1.00 16.91 ? 541  PHE   B CB    1 
ATOM   13042 C  CG    . PHE   B 1  543  ? -2.803  33.731  78.359  1.00 17.06 ? 541  PHE   B CG    1 
ATOM   13043 C  CD1   . PHE   B 1  543  ? -2.518  34.536  79.445  1.00 21.07 ? 541  PHE   B CD1   1 
ATOM   13044 C  CD2   . PHE   B 1  543  ? -1.966  32.662  78.083  1.00 16.98 ? 541  PHE   B CD2   1 
ATOM   13045 C  CE1   . PHE   B 1  543  ? -1.406  34.298  80.216  1.00 21.31 ? 541  PHE   B CE1   1 
ATOM   13046 C  CE2   . PHE   B 1  543  ? -0.850  32.423  78.857  1.00 17.10 ? 541  PHE   B CE2   1 
ATOM   13047 C  CZ    . PHE   B 1  543  ? -0.571  33.240  79.924  1.00 19.32 ? 541  PHE   B CZ    1 
ATOM   13048 N  N     . GLY   B 1  544  ? -7.528  33.199  77.855  1.00 18.84 ? 542  GLY   B N     1 
ATOM   13049 C  CA    . GLY   B 1  544  ? -8.814  33.315  77.196  1.00 18.56 ? 542  GLY   B CA    1 
ATOM   13050 C  C     . GLY   B 1  544  ? -8.665  33.241  75.692  1.00 20.49 ? 542  GLY   B C     1 
ATOM   13051 O  O     . GLY   B 1  544  ? -7.939  32.398  75.149  1.00 24.10 ? 542  GLY   B O     1 
ATOM   13052 N  N     . ASP   B 1  545  ? -9.346  34.157  75.004  1.00 22.85 ? 543  ASP   B N     1 
ATOM   13053 C  CA    . ASP   B 1  545  ? -9.394  34.122  73.550  1.00 24.99 ? 543  ASP   B CA    1 
ATOM   13054 C  C     . ASP   B 1  545  ? -8.097  34.574  72.895  1.00 24.69 ? 543  ASP   B C     1 
ATOM   13055 O  O     . ASP   B 1  545  ? -7.931  34.356  71.690  1.00 25.24 ? 543  ASP   B O     1 
ATOM   13056 C  CB    . ASP   B 1  545  ? -10.540 35.002  73.045  1.00 26.05 ? 543  ASP   B CB    1 
ATOM   13057 C  CG    . ASP   B 1  545  ? -11.898 34.534  73.534  1.00 44.94 ? 543  ASP   B CG    1 
ATOM   13058 O  OD1   . ASP   B 1  545  ? -12.055 33.321  73.793  1.00 42.19 ? 543  ASP   B OD1   1 
ATOM   13059 O  OD2   . ASP   B 1  545  ? -12.810 35.382  73.649  1.00 56.74 ? 543  ASP   B OD2   1 
ATOM   13060 N  N     . ALA   B 1  546  ? -7.189  35.203  73.641  1.00 22.91 ? 544  ALA   B N     1 
ATOM   13061 C  CA    . ALA   B 1  546  ? -5.975  35.736  73.029  1.00 21.23 ? 544  ALA   B CA    1 
ATOM   13062 C  C     . ALA   B 1  546  ? -5.097  34.623  72.475  1.00 21.34 ? 544  ALA   B C     1 
ATOM   13063 O  O     . ALA   B 1  546  ? -4.578  34.725  71.358  1.00 20.70 ? 544  ALA   B O     1 
ATOM   13064 C  CB    . ALA   B 1  546  ? -5.189  36.570  74.044  1.00 22.12 ? 544  ALA   B CB    1 
ATOM   13065 N  N     . ARG   B 1  547  ? -4.899  33.561  73.249  1.00 17.67 ? 545  ARG   B N     1 
ATOM   13066 C  CA    . ARG   B 1  547  ? -4.002  32.493  72.833  1.00 18.10 ? 545  ARG   B CA    1 
ATOM   13067 C  C     . ARG   B 1  547  ? -4.130  31.353  73.823  1.00 17.43 ? 545  ARG   B C     1 
ATOM   13068 O  O     . ARG   B 1  547  ? -4.658  31.516  74.927  1.00 18.32 ? 545  ARG   B O     1 
ATOM   13069 C  CB    . ARG   B 1  547  ? -2.539  32.947  72.766  1.00 21.45 ? 545  ARG   B CB    1 
ATOM   13070 C  CG    . ARG   B 1  547  ? -2.006  33.412  74.085  1.00 17.86 ? 545  ARG   B CG    1 
ATOM   13071 C  CD    . ARG   B 1  547  ? -0.573  33.910  73.921  1.00 19.57 ? 545  ARG   B CD    1 
ATOM   13072 N  NE    . ARG   B 1  547  ? -0.242  34.783  75.034  1.00 18.87 ? 545  ARG   B NE    1 
ATOM   13073 C  CZ    . ARG   B 1  547  ? 0.535   34.443  76.053  1.00 18.98 ? 545  ARG   B CZ    1 
ATOM   13074 N  NH1   . ARG   B 1  547  ? 1.132   33.264  76.106  1.00 17.65 ? 545  ARG   B NH1   1 
ATOM   13075 N  NH2   . ARG   B 1  547  ? 0.724   35.316  77.034  1.00 20.05 ? 545  ARG   B NH2   1 
ATOM   13076 N  N     . THR   B 1  548  ? -3.666  30.192  73.402  1.00 16.75 ? 546  THR   B N     1 
ATOM   13077 C  CA    . THR   B 1  548  ? -3.675  29.012  74.245  1.00 15.14 ? 546  THR   B CA    1 
ATOM   13078 C  C     . THR   B 1  548  ? -2.377  28.971  75.034  1.00 16.03 ? 546  THR   B C     1 
ATOM   13079 O  O     . THR   B 1  548  ? -1.292  29.121  74.468  1.00 16.91 ? 546  THR   B O     1 
ATOM   13080 C  CB    . THR   B 1  548  ? -3.772  27.776  73.361  1.00 18.38 ? 546  THR   B CB    1 
ATOM   13081 O  OG1   . THR   B 1  548  ? -4.980  27.839  72.587  1.00 21.80 ? 546  THR   B OG1   1 
ATOM   13082 C  CG2   . THR   B 1  548  ? -3.747  26.524  74.201  1.00 20.98 ? 546  THR   B CG2   1 
ATOM   13083 N  N     . ASN   B 1  549  ? -2.492  28.778  76.340  1.00 15.33 ? 547  ASN   B N     1 
ATOM   13084 C  CA    . ASN   B 1  549  ? -1.320  28.693  77.187  1.00 13.50 ? 547  ASN   B CA    1 
ATOM   13085 C  C     . ASN   B 1  549  ? -0.541  27.432  76.842  1.00 14.97 ? 547  ASN   B C     1 
ATOM   13086 O  O     . ASN   B 1  549  ? -1.123  26.406  76.487  1.00 17.07 ? 547  ASN   B O     1 
ATOM   13087 C  CB    . ASN   B 1  549  ? -1.789  28.633  78.639  1.00 15.96 ? 547  ASN   B CB    1 
ATOM   13088 C  CG    . ASN   B 1  549  ? -0.665  28.822  79.618  1.00 15.35 ? 547  ASN   B CG    1 
ATOM   13089 O  OD1   . ASN   B 1  549  ? 0.416   29.294  79.268  1.00 15.29 ? 547  ASN   B OD1   1 
ATOM   13090 N  ND2   . ASN   B 1  549  ? -0.922  28.479  80.879  1.00 15.89 ? 547  ASN   B ND2   1 
ATOM   13091 N  N     . SER   B 1  550  ? 0.786   27.520  76.904  1.00 14.38 ? 548  SER   B N     1 
ATOM   13092 C  CA    . SER   B 1  550  ? 1.578   26.313  76.735  1.00 14.97 ? 548  SER   B CA    1 
ATOM   13093 C  C     . SER   B 1  550  ? 1.236   25.324  77.840  1.00 16.29 ? 548  SER   B C     1 
ATOM   13094 O  O     . SER   B 1  550  ? 0.846   25.705  78.952  1.00 16.58 ? 548  SER   B O     1 
ATOM   13095 C  CB    . SER   B 1  550  ? 3.067   26.639  76.792  1.00 14.73 ? 548  SER   B CB    1 
ATOM   13096 O  OG    . SER   B 1  550  ? 3.412   27.165  78.056  1.00 14.83 ? 548  SER   B OG    1 
ATOM   13097 N  N     . ALA   B 1  551  ? 1.370   24.044  77.527  1.00 16.93 ? 549  ALA   B N     1 
ATOM   13098 C  CA    . ALA   B 1  551  ? 1.127   22.993  78.500  1.00 17.91 ? 549  ALA   B CA    1 
ATOM   13099 C  C     . ALA   B 1  551  ? 2.441   22.388  78.957  1.00 17.92 ? 549  ALA   B C     1 
ATOM   13100 O  O     . ALA   B 1  551  ? 3.370   22.232  78.166  1.00 17.69 ? 549  ALA   B O     1 
ATOM   13101 C  CB    . ALA   B 1  551  ? 0.257   21.896  77.906  1.00 18.45 ? 549  ALA   B CB    1 
ATOM   13102 N  N     . GLY   B 1  552  ? 2.515   22.059  80.237  1.00 16.39 ? 550  GLY   B N     1 
ATOM   13103 C  CA    . GLY   B 1  552  ? 3.639   21.353  80.798  1.00 17.97 ? 550  GLY   B CA    1 
ATOM   13104 C  C     . GLY   B 1  552  ? 3.388   19.864  80.882  1.00 16.59 ? 550  GLY   B C     1 
ATOM   13105 O  O     . GLY   B 1  552  ? 2.529   19.300  80.191  1.00 19.60 ? 550  GLY   B O     1 
ATOM   13106 N  N     . LEU   B 1  553  ? 4.152   19.214  81.751  1.00 18.14 ? 551  LEU   B N     1 
ATOM   13107 C  CA    . LEU   B 1  553  ? 4.050   17.784  81.975  1.00 19.40 ? 551  LEU   B CA    1 
ATOM   13108 C  C     . LEU   B 1  553  ? 4.110   17.580  83.475  1.00 17.71 ? 551  LEU   B C     1 
ATOM   13109 O  O     . LEU   B 1  553  ? 4.860   18.272  84.165  1.00 20.71 ? 551  LEU   B O     1 
ATOM   13110 C  CB    . LEU   B 1  553  ? 5.212   17.029  81.316  1.00 19.41 ? 551  LEU   B CB    1 
ATOM   13111 C  CG    . LEU   B 1  553  ? 5.230   17.031  79.787  1.00 20.51 ? 551  LEU   B CG    1 
ATOM   13112 C  CD1   . LEU   B 1  553  ? 6.548   16.498  79.280  1.00 23.03 ? 551  LEU   B CD1   1 
ATOM   13113 C  CD2   . LEU   B 1  553  ? 4.089   16.200  79.245  1.00 23.04 ? 551  LEU   B CD2   1 
ATOM   13114 N  N     . ASP   B 1  554  ? 3.288   16.662  83.975  1.00 18.48 ? 552  ASP   B N     1 
ATOM   13115 C  CA    . ASP   B 1  554  ? 3.174   16.435  85.413  1.00 17.86 ? 552  ASP   B CA    1 
ATOM   13116 C  C     . ASP   B 1  554  ? 4.187   15.367  85.804  1.00 17.32 ? 552  ASP   B C     1 
ATOM   13117 O  O     . ASP   B 1  554  ? 3.965   14.177  85.580  1.00 18.15 ? 552  ASP   B O     1 
ATOM   13118 C  CB    . ASP   B 1  554  ? 1.756   15.994  85.745  1.00 19.72 ? 552  ASP   B CB    1 
ATOM   13119 C  CG    . ASP   B 1  554  ? 1.542   15.800  87.226  1.00 19.61 ? 552  ASP   B CG    1 
ATOM   13120 O  OD1   . ASP   B 1  554  ? 2.492   16.041  88.000  1.00 20.45 ? 552  ASP   B OD1   1 
ATOM   13121 O  OD2   . ASP   B 1  554  ? 0.422   15.405  87.615  1.00 21.80 ? 552  ASP   B OD2   1 
ATOM   13122 N  N     . LEU   B 1  555  ? 5.292   15.791  86.407  1.00 17.40 ? 553  LEU   B N     1 
ATOM   13123 C  CA    . LEU   B 1  555  ? 6.337   14.861  86.808  1.00 18.55 ? 553  LEU   B CA    1 
ATOM   13124 C  C     . LEU   B 1  555  ? 6.011   14.129  88.102  1.00 20.10 ? 553  LEU   B C     1 
ATOM   13125 O  O     . LEU   B 1  555  ? 6.882   13.442  88.643  1.00 18.86 ? 553  LEU   B O     1 
ATOM   13126 C  CB    . LEU   B 1  555  ? 7.683   15.577  86.903  1.00 17.18 ? 553  LEU   B CB    1 
ATOM   13127 C  CG    . LEU   B 1  555  ? 8.104   16.291  85.621  1.00 19.26 ? 553  LEU   B CG    1 
ATOM   13128 C  CD1   . LEU   B 1  555  ? 9.492   16.887  85.818  1.00 22.73 ? 553  LEU   B CD1   1 
ATOM   13129 C  CD2   . LEU   B 1  555  ? 8.069   15.355  84.411  1.00 23.42 ? 553  LEU   B CD2   1 
ATOM   13130 N  N     . SER   B 1  556  ? 4.790   14.274  88.616  1.00 18.19 ? 554  SER   B N     1 
ATOM   13131 C  CA    . SER   B 1  556  ? 4.299   13.428  89.694  1.00 18.30 ? 554  SER   B CA    1 
ATOM   13132 C  C     . SER   B 1  556  ? 3.356   12.346  89.204  1.00 19.40 ? 554  SER   B C     1 
ATOM   13133 O  O     . SER   B 1  556  ? 2.917   11.516  89.999  1.00 21.27 ? 554  SER   B O     1 
ATOM   13134 C  CB    . SER   B 1  556  ? 3.595   14.270  90.767  1.00 19.65 ? 554  SER   B CB    1 
ATOM   13135 O  OG    . SER   B 1  556  ? 2.315   14.672  90.298  1.00 20.48 ? 554  SER   B OG    1 
ATOM   13136 N  N     . ASN   B 1  557  ? 3.055   12.317  87.912  1.00 16.94 ? 555  ASN   B N     1 
ATOM   13137 C  CA    . ASN   B 1  557  ? 2.122   11.363  87.338  1.00 19.01 ? 555  ASN   B CA    1 
ATOM   13138 C  C     . ASN   B 1  557  ? 2.913   10.173  86.806  1.00 18.69 ? 555  ASN   B C     1 
ATOM   13139 O  O     . ASN   B 1  557  ? 3.766   10.339  85.930  1.00 18.59 ? 555  ASN   B O     1 
ATOM   13140 C  CB    . ASN   B 1  557  ? 1.351   12.059  86.217  1.00 18.30 ? 555  ASN   B CB    1 
ATOM   13141 C  CG    . ASN   B 1  557  ? 0.344   11.159  85.555  1.00 19.76 ? 555  ASN   B CG    1 
ATOM   13142 O  OD1   . ASN   B 1  557  ? 0.664   10.052  85.132  1.00 20.04 ? 555  ASN   B OD1   1 
ATOM   13143 N  ND2   . ASN   B 1  557  ? -0.901  11.630  85.459  1.00 20.56 ? 555  ASN   B ND2   1 
ATOM   13144 N  N     . GLU   B 1  558  ? 2.640   8.975   87.330  1.00 19.59 ? 556  GLU   B N     1 
ATOM   13145 C  CA    . GLU   B 1  558  ? 3.434   7.817   86.919  1.00 19.95 ? 556  GLU   B CA    1 
ATOM   13146 C  C     . GLU   B 1  558  ? 3.260   7.480   85.451  1.00 20.19 ? 556  GLU   B C     1 
ATOM   13147 O  O     . GLU   B 1  558  ? 4.200   6.971   84.836  1.00 21.30 ? 556  GLU   B O     1 
ATOM   13148 C  CB    . GLU   B 1  558  ? 3.107   6.568   87.741  1.00 23.80 ? 556  GLU   B CB    1 
ATOM   13149 C  CG    . GLU   B 1  558  ? 3.534   6.625   89.173  1.00 24.82 ? 556  GLU   B CG    1 
ATOM   13150 C  CD    . GLU   B 1  558  ? 5.042   6.752   89.417  1.00 23.36 ? 556  GLU   B CD    1 
ATOM   13151 O  OE1   . GLU   B 1  558  ? 5.901   6.565   88.518  1.00 21.94 ? 556  GLU   B OE1   1 
ATOM   13152 O  OE2   . GLU   B 1  558  ? 5.362   7.036   90.575  1.00 22.99 ? 556  GLU   B OE2   1 
ATOM   13153 N  N     . GLU   B 1  559  ? 2.071   7.702   84.880  1.00 19.16 ? 557  GLU   B N     1 
ATOM   13154 C  CA    . GLU   B 1  559  ? 1.911   7.484   83.445  1.00 18.63 ? 557  GLU   B CA    1 
ATOM   13155 C  C     . GLU   B 1  559  ? 2.819   8.428   82.677  1.00 19.59 ? 557  GLU   B C     1 
ATOM   13156 O  O     . GLU   B 1  559  ? 3.494   8.028   81.721  1.00 20.80 ? 557  GLU   B O     1 
ATOM   13157 C  CB    . GLU   B 1  559  ? 0.466   7.733   83.011  1.00 24.68 ? 557  GLU   B CB    1 
ATOM   13158 C  CG    . GLU   B 1  559  ? -0.577  6.802   83.555  1.00 27.63 ? 557  GLU   B CG    1 
ATOM   13159 C  CD    . GLU   B 1  559  ? -1.938  7.075   82.926  1.00 37.65 ? 557  GLU   B CD    1 
ATOM   13160 O  OE1   . GLU   B 1  559  ? -1.972  7.549   81.766  1.00 39.08 ? 557  GLU   B OE1   1 
ATOM   13161 O  OE2   . GLU   B 1  559  ? -2.968  6.823   83.584  1.00 33.39 ? 557  GLU   B OE2   1 
ATOM   13162 N  N     . THR   B 1  560  ? 2.834   9.698   83.081  1.00 18.57 ? 558  THR   B N     1 
ATOM   13163 C  CA    . THR   B 1  560  ? 3.674   10.677  82.405  1.00 16.66 ? 558  THR   B CA    1 
ATOM   13164 C  C     . THR   B 1  560  ? 5.136   10.308  82.550  1.00 18.50 ? 558  THR   B C     1 
ATOM   13165 O  O     . THR   B 1  560  ? 5.894   10.361  81.577  1.00 19.16 ? 558  THR   B O     1 
ATOM   13166 C  CB    . THR   B 1  560  ? 3.426   12.064  82.988  1.00 17.56 ? 558  THR   B CB    1 
ATOM   13167 O  OG1   . THR   B 1  560  ? 2.037   12.386  82.863  1.00 20.11 ? 558  THR   B OG1   1 
ATOM   13168 C  CG2   . THR   B 1  560  ? 4.253   13.108  82.252  1.00 19.38 ? 558  THR   B CG2   1 
ATOM   13169 N  N     . LEU   B 1  561  ? 5.548   9.913   83.753  1.00 16.46 ? 559  LEU   B N     1 
ATOM   13170 C  CA    . LEU   B 1  561  ? 6.948   9.558   83.959  1.00 16.59 ? 559  LEU   B CA    1 
ATOM   13171 C  C     . LEU   B 1  561  ? 7.343   8.358   83.116  1.00 19.34 ? 559  LEU   B C     1 
ATOM   13172 O  O     . LEU   B 1  561  ? 8.452   8.317   82.572  1.00 17.63 ? 559  LEU   B O     1 
ATOM   13173 C  CB    . LEU   B 1  561  ? 7.218   9.292   85.438  1.00 17.90 ? 559  LEU   B CB    1 
ATOM   13174 C  CG    . LEU   B 1  561  ? 7.167   10.539  86.322  1.00 17.12 ? 559  LEU   B CG    1 
ATOM   13175 C  CD1   . LEU   B 1  561  ? 7.323   10.158  87.791  1.00 20.36 ? 559  LEU   B CD1   1 
ATOM   13176 C  CD2   . LEU   B 1  561  ? 8.241   11.519  85.900  1.00 17.59 ? 559  LEU   B CD2   1 
ATOM   13177 N  N     . ALA   B 1  562  ? 6.449   7.377   82.988  1.00 18.41 ? 560  ALA   B N     1 
ATOM   13178 C  CA    . ALA   B 1  562  ? 6.759   6.195   82.194  1.00 19.82 ? 560  ALA   B CA    1 
ATOM   13179 C  C     . ALA   B 1  562  ? 6.852   6.538   80.718  1.00 20.12 ? 560  ALA   B C     1 
ATOM   13180 O  O     . ALA   B 1  562  ? 7.756   6.063   80.022  1.00 20.26 ? 560  ALA   B O     1 
ATOM   13181 C  CB    . ALA   B 1  562  ? 5.697   5.121   82.423  1.00 21.08 ? 560  ALA   B CB    1 
ATOM   13182 N  N     . SER   B 1  563  ? 5.928   7.353   80.213  1.00 18.65 ? 561  SER   B N     1 
ATOM   13183 C  CA    . SER   B 1  563  ? 5.986   7.695   78.798  1.00 18.00 ? 561  SER   B CA    1 
ATOM   13184 C  C     . SER   B 1  563  ? 7.136   8.649   78.525  1.00 20.73 ? 561  SER   B C     1 
ATOM   13185 O  O     . SER   B 1  563  ? 7.812   8.539   77.494  1.00 20.40 ? 561  SER   B O     1 
ATOM   13186 C  CB    . SER   B 1  563  ? 4.652   8.275   78.319  1.00 21.45 ? 561  SER   B CB    1 
ATOM   13187 O  OG    . SER   B 1  563  ? 4.378   9.524   78.927  1.00 24.54 ? 561  SER   B OG    1 
ATOM   13188 N  N     . LEU   B 1  564  ? 7.396   9.567   79.457  1.00 17.47 ? 562  LEU   B N     1 
ATOM   13189 C  CA    . LEU   B 1  564  ? 8.519   10.475  79.284  1.00 18.56 ? 562  LEU   B CA    1 
ATOM   13190 C  C     . LEU   B 1  564  ? 9.830   9.711   79.290  1.00 19.60 ? 562  LEU   B C     1 
ATOM   13191 O  O     . LEU   B 1  564  ? 10.705  9.960   78.453  1.00 19.91 ? 562  LEU   B O     1 
ATOM   13192 C  CB    . LEU   B 1  564  ? 8.499   11.544  80.378  1.00 20.11 ? 562  LEU   B CB    1 
ATOM   13193 C  CG    . LEU   B 1  564  ? 9.562   12.625  80.301  1.00 23.17 ? 562  LEU   B CG    1 
ATOM   13194 C  CD1   . LEU   B 1  564  ? 9.505   13.344  78.960  1.00 24.18 ? 562  LEU   B CD1   1 
ATOM   13195 C  CD2   . LEU   B 1  564  ? 9.373   13.606  81.454  1.00 24.09 ? 562  LEU   B CD2   1 
ATOM   13196 N  N     . THR   B 1  565  ? 9.982   8.770   80.223  1.00 19.85 ? 563  THR   B N     1 
ATOM   13197 C  CA    . THR   B 1  565  ? 11.182  7.939   80.248  1.00 18.87 ? 563  THR   B CA    1 
ATOM   13198 C  C     . THR   B 1  565  ? 11.466  7.351   78.874  1.00 21.87 ? 563  THR   B C     1 
ATOM   13199 O  O     . THR   B 1  565  ? 12.591  7.432   78.373  1.00 19.67 ? 563  THR   B O     1 
ATOM   13200 C  CB    . THR   B 1  565  ? 11.021  6.819   81.281  1.00 19.62 ? 563  THR   B CB    1 
ATOM   13201 O  OG1   . THR   B 1  565  ? 10.953  7.377   82.600  1.00 21.55 ? 563  THR   B OG1   1 
ATOM   13202 C  CG2   . THR   B 1  565  ? 12.212  5.881   81.228  1.00 22.25 ? 563  THR   B CG2   1 
ATOM   13203 N  N     . GLU   B 1  566  ? 10.445  6.780   78.235  1.00 19.40 ? 564  GLU   B N     1 
ATOM   13204 C  CA    . GLU   B 1  566  ? 10.661  6.164   76.932  1.00 18.19 ? 564  GLU   B CA    1 
ATOM   13205 C  C     . GLU   B 1  566  ? 11.003  7.206   75.878  1.00 18.64 ? 564  GLU   B C     1 
ATOM   13206 O  O     . GLU   B 1  566  ? 11.892  6.982   75.050  1.00 19.69 ? 564  GLU   B O     1 
ATOM   13207 C  CB    . GLU   B 1  566  ? 9.442   5.336   76.532  1.00 24.15 ? 564  GLU   B CB    1 
ATOM   13208 C  CG    . GLU   B 1  566  ? 9.215   4.132   77.458  1.00 31.05 ? 564  GLU   B CG    1 
ATOM   13209 C  CD    . GLU   B 1  566  ? 10.509  3.420   77.845  1.00 43.21 ? 564  GLU   B CD    1 
ATOM   13210 O  OE1   . GLU   B 1  566  ? 11.314  3.082   76.946  1.00 40.39 ? 564  GLU   B OE1   1 
ATOM   13211 O  OE2   . GLU   B 1  566  ? 10.724  3.197   79.059  1.00 40.44 ? 564  GLU   B OE2   1 
ATOM   13212 N  N     . ALA   B 1  567  ? 10.314  8.347   75.891  1.00 18.88 ? 565  ALA   B N     1 
ATOM   13213 C  CA    . ALA   B 1  567  ? 10.608  9.397   74.922  1.00 19.33 ? 565  ALA   B CA    1 
ATOM   13214 C  C     . ALA   B 1  567  ? 11.998  9.973   75.134  1.00 19.17 ? 565  ALA   B C     1 
ATOM   13215 O  O     . ALA   B 1  567  ? 12.699  10.297  74.167  1.00 18.51 ? 565  ALA   B O     1 
ATOM   13216 C  CB    . ALA   B 1  567  ? 9.555   10.501  75.005  1.00 18.59 ? 565  ALA   B CB    1 
ATOM   13217 N  N     . LEU   B 1  568  ? 12.427  10.089  76.390  1.00 16.95 ? 566  LEU   B N     1 
ATOM   13218 C  CA    . LEU   B 1  568  ? 13.764  10.607  76.654  1.00 17.26 ? 566  LEU   B CA    1 
ATOM   13219 C  C     . LEU   B 1  568  ? 14.821  9.619   76.195  1.00 18.55 ? 566  LEU   B C     1 
ATOM   13220 O  O     . LEU   B 1  568  ? 15.804  10.006  75.554  1.00 18.12 ? 566  LEU   B O     1 
ATOM   13221 C  CB    . LEU   B 1  568  ? 13.928  10.903  78.145  1.00 16.86 ? 566  LEU   B CB    1 
ATOM   13222 C  CG    . LEU   B 1  568  ? 13.019  11.996  78.718  1.00 16.85 ? 566  LEU   B CG    1 
ATOM   13223 C  CD1   . LEU   B 1  568  ? 13.111  12.039  80.244  1.00 19.77 ? 566  LEU   B CD1   1 
ATOM   13224 C  CD2   . LEU   B 1  568  ? 13.332  13.345  78.102  1.00 20.63 ? 566  LEU   B CD2   1 
ATOM   13225 N  N     . ARG   B 1  569  ? 14.628  8.335   76.499  1.00 19.09 ? 567  ARG   B N     1 
ATOM   13226 C  CA    . ARG   B 1  569  ? 15.565  7.327   76.022  1.00 20.30 ? 567  ARG   B CA    1 
ATOM   13227 C  C     . ARG   B 1  569  ? 15.645  7.343   74.508  1.00 21.09 ? 567  ARG   B C     1 
ATOM   13228 O  O     . ARG   B 1  569  ? 16.743  7.298   73.935  1.00 24.21 ? 567  ARG   B O     1 
ATOM   13229 C  CB    . ARG   B 1  569  ? 15.132  5.946   76.506  1.00 21.05 ? 567  ARG   B CB    1 
ATOM   13230 C  CG    . ARG   B 1  569  ? 15.315  5.761   77.984  1.00 26.42 ? 567  ARG   B CG    1 
ATOM   13231 C  CD    . ARG   B 1  569  ? 14.840  4.400   78.459  1.00 28.56 ? 567  ARG   B CD    1 
ATOM   13232 N  NE    . ARG   B 1  569  ? 15.002  4.296   79.905  1.00 32.31 ? 567  ARG   B NE    1 
ATOM   13233 C  CZ    . ARG   B 1  569  ? 14.448  3.357   80.659  1.00 37.87 ? 567  ARG   B CZ    1 
ATOM   13234 N  NH1   . ARG   B 1  569  ? 13.678  2.417   80.136  1.00 39.16 ? 567  ARG   B NH1   1 
ATOM   13235 N  NH2   . ARG   B 1  569  ? 14.664  3.369   81.972  1.00 39.10 ? 567  ARG   B NH2   1 
ATOM   13236 N  N     . GLU   B 1  570  ? 14.494  7.434   73.845  1.00 19.29 ? 568  GLU   B N     1 
ATOM   13237 C  CA    . GLU   B 1  570  ? 14.478  7.450   72.389  1.00 19.90 ? 568  GLU   B CA    1 
ATOM   13238 C  C     . GLU   B 1  570  ? 15.164  8.687   71.846  1.00 23.06 ? 568  GLU   B C     1 
ATOM   13239 O  O     . GLU   B 1  570  ? 15.789  8.623   70.785  1.00 22.45 ? 568  GLU   B O     1 
ATOM   13240 C  CB    . GLU   B 1  570  ? 13.034  7.391   71.893  1.00 21.97 ? 568  GLU   B CB    1 
ATOM   13241 C  CG    . GLU   B 1  570  ? 12.387  6.038   72.117  1.00 23.03 ? 568  GLU   B CG    1 
ATOM   13242 C  CD    . GLU   B 1  570  ? 10.868  6.100   72.137  1.00 35.63 ? 568  GLU   B CD    1 
ATOM   13243 O  OE1   . GLU   B 1  570  ? 10.300  7.151   71.775  1.00 35.12 ? 568  GLU   B OE1   1 
ATOM   13244 O  OE2   . GLU   B 1  570  ? 10.243  5.093   72.532  1.00 37.70 ? 568  GLU   B OE2   1 
ATOM   13245 N  N     . SER   B 1  571  ? 15.062  9.817   72.552  1.00 20.06 ? 569  SER   B N     1 
ATOM   13246 C  CA    . SER   B 1  571  ? 15.704  11.032  72.070  1.00 22.16 ? 569  SER   B CA    1 
ATOM   13247 C  C     . SER   B 1  571  ? 17.206  10.874  72.072  1.00 25.85 ? 569  SER   B C     1 
ATOM   13248 O  O     . SER   B 1  571  ? 17.889  11.434  71.211  1.00 22.82 ? 569  SER   B O     1 
ATOM   13249 C  CB    . SER   B 1  571  ? 15.312  12.239  72.928  1.00 19.94 ? 569  SER   B CB    1 
ATOM   13250 O  OG    . SER   B 1  571  ? 16.009  12.244  74.172  1.00 21.15 ? 569  SER   B OG    1 
ATOM   13251 N  N     . ALA   B 1  572  ? 17.732  10.095  73.012  1.00 20.14 ? 570  ALA   B N     1 
ATOM   13252 C  CA    . ALA   B 1  572  ? 19.171  9.909   73.074  1.00 20.59 ? 570  ALA   B CA    1 
ATOM   13253 C  C     . ALA   B 1  572  ? 19.678  8.982   71.979  1.00 25.32 ? 570  ALA   B C     1 
ATOM   13254 O  O     . ALA   B 1  572  ? 20.881  8.986   71.688  1.00 27.99 ? 570  ALA   B O     1 
ATOM   13255 C  CB    . ALA   B 1  572  ? 19.574  9.420   74.464  1.00 22.50 ? 570  ALA   B CB    1 
ATOM   13256 N  N     . ALA   B 1  573  ? 18.796  8.211   71.348  1.00 21.96 ? 571  ALA   B N     1 
ATOM   13257 C  CA    . ALA   B 1  573  ? 19.189  7.350   70.242  1.00 25.06 ? 571  ALA   B CA    1 
ATOM   13258 C  C     . ALA   B 1  573  ? 19.146  8.045   68.882  1.00 25.85 ? 571  ALA   B C     1 
ATOM   13259 O  O     . ALA   B 1  573  ? 19.591  7.456   67.890  1.00 25.61 ? 571  ALA   B O     1 
ATOM   13260 C  CB    . ALA   B 1  573  ? 18.314  6.093   70.218  1.00 25.25 ? 571  ALA   B CB    1 
ATOM   13261 N  N     . MET   B 1  574  ? 18.637  9.274   68.808  1.00 21.10 ? 572  MET   B N     1 
ATOM   13262 C  CA    . MET   B 1  574  ? 18.549  9.971   67.535  1.00 20.95 ? 572  MET   B CA    1 
ATOM   13263 C  C     . MET   B 1  574  ? 19.887  10.594  67.187  1.00 22.05 ? 572  MET   B C     1 
ATOM   13264 O  O     . MET   B 1  574  ? 20.669  10.969  68.063  1.00 22.69 ? 572  MET   B O     1 
ATOM   13265 C  CB    . MET   B 1  574  ? 17.509  11.080  67.621  1.00 23.14 ? 572  MET   B CB    1 
ATOM   13266 C  CG    . MET   B 1  574  ? 16.117  10.538  67.822  1.00 25.67 ? 572  MET   B CG    1 
ATOM   13267 S  SD    . MET   B 1  574  ? 14.974  11.808  68.355  1.00 25.25 ? 572  MET   B SD    1 
ATOM   13268 C  CE    . MET   B 1  574  ? 13.461  10.840  68.431  1.00 25.68 ? 572  MET   B CE    1 
ATOM   13269 N  N     . LYS   B 1  575  ? 20.142  10.714  65.889  1.00 19.40 ? 573  LYS   B N     1 
ATOM   13270 C  CA    . LYS   B 1  575  ? 21.319  11.435  65.414  1.00 19.50 ? 573  LYS   B CA    1 
ATOM   13271 C  C     . LYS   B 1  575  ? 20.964  12.912  65.358  1.00 20.41 ? 573  LYS   B C     1 
ATOM   13272 O  O     . LYS   B 1  575  ? 20.248  13.357  64.455  1.00 20.31 ? 573  LYS   B O     1 
ATOM   13273 C  CB    . LYS   B 1  575  ? 21.721  10.924  64.037  1.00 22.11 ? 573  LYS   B CB    1 
ATOM   13274 C  CG    . LYS   B 1  575  ? 22.930  11.618  63.445  1.00 25.80 ? 573  LYS   B CG    1 
ATOM   13275 C  CD    . LYS   B 1  575  ? 23.383  10.898  62.185  1.00 30.75 ? 573  LYS   B CD    1 
ATOM   13276 C  CE    . LYS   B 1  575  ? 24.692  11.463  61.639  1.00 45.68 ? 573  LYS   B CE    1 
ATOM   13277 N  NZ    . LYS   B 1  575  ? 24.469  12.570  60.661  1.00 41.78 ? 573  LYS   B NZ    1 
ATOM   13278 N  N     . TRP   B 1  576  ? 21.446  13.669  66.338  1.00 19.80 ? 574  TRP   B N     1 
ATOM   13279 C  CA    . TRP   B 1  576  ? 21.207  15.098  66.409  1.00 17.63 ? 574  TRP   B CA    1 
ATOM   13280 C  C     . TRP   B 1  576  ? 22.350  15.834  65.745  1.00 17.00 ? 574  TRP   B C     1 
ATOM   13281 O  O     . TRP   B 1  576  ? 23.512  15.621  66.085  1.00 18.70 ? 574  TRP   B O     1 
ATOM   13282 C  CB    . TRP   B 1  576  ? 21.129  15.549  67.861  1.00 17.95 ? 574  TRP   B CB    1 
ATOM   13283 C  CG    . TRP   B 1  576  ? 19.958  15.006  68.589  1.00 16.36 ? 574  TRP   B CG    1 
ATOM   13284 C  CD1   . TRP   B 1  576  ? 19.969  14.032  69.537  1.00 20.55 ? 574  TRP   B CD1   1 
ATOM   13285 C  CD2   . TRP   B 1  576  ? 18.600  15.409  68.430  1.00 16.11 ? 574  TRP   B CD2   1 
ATOM   13286 N  NE1   . TRP   B 1  576  ? 18.693  13.810  69.994  1.00 19.48 ? 574  TRP   B NE1   1 
ATOM   13287 C  CE2   . TRP   B 1  576  ? 17.833  14.641  69.326  1.00 18.70 ? 574  TRP   B CE2   1 
ATOM   13288 C  CE3   . TRP   B 1  576  ? 17.960  16.346  67.621  1.00 17.14 ? 574  TRP   B CE3   1 
ATOM   13289 C  CZ2   . TRP   B 1  576  ? 16.454  14.780  69.438  1.00 21.17 ? 574  TRP   B CZ2   1 
ATOM   13290 C  CZ3   . TRP   B 1  576  ? 16.587  16.496  67.740  1.00 18.41 ? 574  TRP   B CZ3   1 
ATOM   13291 C  CH2   . TRP   B 1  576  ? 15.852  15.716  68.642  1.00 18.31 ? 574  TRP   B CH2   1 
ATOM   13292 N  N     . THR   B 1  577  ? 22.009  16.703  64.809  1.00 18.35 ? 575  THR   B N     1 
ATOM   13293 C  CA    . THR   B 1  577  ? 23.004  17.466  64.083  1.00 16.16 ? 575  THR   B CA    1 
ATOM   13294 C  C     . THR   B 1  577  ? 22.544  18.910  64.016  1.00 16.35 ? 575  THR   B C     1 
ATOM   13295 O  O     . THR   B 1  577  ? 21.367  19.227  64.196  1.00 17.05 ? 575  THR   B O     1 
ATOM   13296 C  CB    . THR   B 1  577  ? 23.195  16.950  62.651  1.00 19.94 ? 575  THR   B CB    1 
ATOM   13297 O  OG1   . THR   B 1  577  ? 21.985  17.152  61.907  1.00 23.97 ? 575  THR   B OG1   1 
ATOM   13298 C  CG2   . THR   B 1  577  ? 23.561  15.473  62.652  1.00 20.17 ? 575  THR   B CG2   1 
ATOM   13299 N  N     . ALA   B 1  578  ? 23.501  19.791  63.762  1.00 17.07 ? 576  ALA   B N     1 
ATOM   13300 C  CA    . ALA   B 1  578  ? 23.203  21.184  63.497  1.00 16.46 ? 576  ALA   B CA    1 
ATOM   13301 C  C     . ALA   B 1  578  ? 24.156  21.610  62.403  1.00 16.56 ? 576  ALA   B C     1 
ATOM   13302 O  O     . ALA   B 1  578  ? 25.363  21.396  62.523  1.00 18.04 ? 576  ALA   B O     1 
ATOM   13303 C  CB    . ALA   B 1  578  ? 23.407  22.047  64.745  1.00 16.44 ? 576  ALA   B CB    1 
ATOM   13304 N  N     . LEU   B 1  579  ? 23.614  22.153  61.325  1.00 17.39 ? 577  LEU   B N     1 
ATOM   13305 C  CA    . LEU   B 1  579  ? 24.383  22.462  60.132  1.00 16.76 ? 577  LEU   B CA    1 
ATOM   13306 C  C     . LEU   B 1  579  ? 24.135  23.909  59.753  1.00 16.70 ? 577  LEU   B C     1 
ATOM   13307 O  O     . LEU   B 1  579  ? 23.121  24.494  60.139  1.00 15.70 ? 577  LEU   B O     1 
ATOM   13308 C  CB    . LEU   B 1  579  ? 23.907  21.594  58.957  1.00 19.77 ? 577  LEU   B CB    1 
ATOM   13309 C  CG    . LEU   B 1  579  ? 23.738  20.101  59.189  1.00 22.32 ? 577  LEU   B CG    1 
ATOM   13310 C  CD1   . LEU   B 1  579  ? 23.196  19.412  57.940  1.00 23.95 ? 577  LEU   B CD1   1 
ATOM   13311 C  CD2   . LEU   B 1  579  ? 25.075  19.543  59.582  1.00 21.38 ? 577  LEU   B CD2   1 
ATOM   13312 N  N     . PRO   B 1  580  ? 25.022  24.508  58.963  1.00 15.67 ? 578  PRO   B N     1 
ATOM   13313 C  CA    . PRO   B 1  580  ? 24.685  25.802  58.363  1.00 15.87 ? 578  PRO   B CA    1 
ATOM   13314 C  C     . PRO   B 1  580  ? 23.592  25.581  57.340  1.00 15.25 ? 578  PRO   B C     1 
ATOM   13315 O  O     . PRO   B 1  580  ? 23.841  25.074  56.246  1.00 19.21 ? 578  PRO   B O     1 
ATOM   13316 C  CB    . PRO   B 1  580  ? 25.998  26.258  57.708  1.00 18.29 ? 578  PRO   B CB    1 
ATOM   13317 C  CG    . PRO   B 1  580  ? 27.061  25.366  58.315  1.00 18.91 ? 578  PRO   B CG    1 
ATOM   13318 C  CD    . PRO   B 1  580  ? 26.362  24.058  58.570  1.00 17.30 ? 578  PRO   B CD    1 
ATOM   13319 N  N     . GLN   B 1  581  ? 22.372  25.910  57.713  1.00 15.49 ? 579  GLN   B N     1 
ATOM   13320 C  CA    . GLN   B 1  581  ? 21.201  25.671  56.876  1.00 17.45 ? 579  GLN   B CA    1 
ATOM   13321 C  C     . GLN   B 1  581  ? 20.900  26.958  56.135  1.00 17.92 ? 579  GLN   B C     1 
ATOM   13322 O  O     . GLN   B 1  581  ? 20.190  27.835  56.630  1.00 18.25 ? 579  GLN   B O     1 
ATOM   13323 C  CB    . GLN   B 1  581  ? 20.024  25.274  57.741  1.00 18.09 ? 579  GLN   B CB    1 
ATOM   13324 C  CG    . GLN   B 1  581  ? 20.211  23.977  58.435  1.00 17.63 ? 579  GLN   B CG    1 
ATOM   13325 C  CD    . GLN   B 1  581  ? 20.161  22.783  57.493  1.00 24.95 ? 579  GLN   B CD    1 
ATOM   13326 O  OE1   . GLN   B 1  581  ? 19.954  22.920  56.276  1.00 21.44 ? 579  GLN   B OE1   1 
ATOM   13327 N  NE2   . GLN   B 1  581  ? 20.352  21.597  58.055  1.00 27.69 ? 579  GLN   B NE2   1 
ATOM   13328 N  N     . LEU   B 1  582  ? 21.459  27.073  54.940  1.00 16.49 ? 580  LEU   B N     1 
ATOM   13329 C  CA    . LEU   B 1  582  ? 21.233  28.232  54.097  1.00 15.76 ? 580  LEU   B CA    1 
ATOM   13330 C  C     . LEU   B 1  582  ? 19.986  27.991  53.249  1.00 18.01 ? 580  LEU   B C     1 
ATOM   13331 O  O     . LEU   B 1  582  ? 19.426  26.890  53.223  1.00 20.92 ? 580  LEU   B O     1 
ATOM   13332 C  CB    . LEU   B 1  582  ? 22.475  28.518  53.242  1.00 17.77 ? 580  LEU   B CB    1 
ATOM   13333 C  CG    . LEU   B 1  582  ? 23.532  29.375  53.978  1.00 23.82 ? 580  LEU   B CG    1 
ATOM   13334 C  CD1   . LEU   B 1  582  ? 24.217  28.644  55.136  1.00 21.78 ? 580  LEU   B CD1   1 
ATOM   13335 C  CD2   . LEU   B 1  582  ? 24.570  29.909  53.015  1.00 25.74 ? 580  LEU   B CD2   1 
ATOM   13336 N  N     . ALA   B 1  583  ? 19.532  29.045  52.571  1.00 18.23 ? 581  ALA   B N     1 
ATOM   13337 C  CA    . ALA   B 1  583  ? 18.318  28.926  51.770  1.00 21.42 ? 581  ALA   B CA    1 
ATOM   13338 C  C     . ALA   B 1  583  ? 18.460  27.861  50.697  1.00 25.37 ? 581  ALA   B C     1 
ATOM   13339 O  O     . ALA   B 1  583  ? 17.472  27.221  50.324  1.00 28.13 ? 581  ALA   B O     1 
ATOM   13340 C  CB    . ALA   B 1  583  ? 17.987  30.267  51.126  1.00 21.81 ? 581  ALA   B CB    1 
ATOM   13341 N  N     . THR   B 1  584  ? 19.675  27.643  50.215  1.00 20.83 ? 582  THR   B N     1 
ATOM   13342 C  CA    . THR   B 1  584  ? 19.947  26.709  49.133  1.00 22.10 ? 582  THR   B CA    1 
ATOM   13343 C  C     . THR   B 1  584  ? 20.295  25.315  49.631  1.00 18.95 ? 582  THR   B C     1 
ATOM   13344 O  O     . THR   B 1  584  ? 20.575  24.433  48.816  1.00 21.90 ? 582  THR   B O     1 
ATOM   13345 C  CB    . THR   B 1  584  ? 21.078  27.255  48.257  1.00 25.56 ? 582  THR   B CB    1 
ATOM   13346 O  OG1   . THR   B 1  584  ? 22.160  27.689  49.097  1.00 26.43 ? 582  THR   B OG1   1 
ATOM   13347 C  CG2   . THR   B 1  584  ? 20.581  28.426  47.441  1.00 33.40 ? 582  THR   B CG2   1 
ATOM   13348 N  N     . GLY   B 1  585  ? 20.274  25.096  50.942  1.00 19.95 ? 583  GLY   B N     1 
ATOM   13349 C  CA    . GLY   B 1  585  ? 20.570  23.800  51.505  1.00 19.53 ? 583  GLY   B CA    1 
ATOM   13350 C  C     . GLY   B 1  585  ? 21.688  23.909  52.518  1.00 20.18 ? 583  GLY   B C     1 
ATOM   13351 O  O     . GLY   B 1  585  ? 22.253  24.986  52.727  1.00 20.63 ? 583  GLY   B O     1 
ATOM   13352 N  N     . PRO   B 1  586  ? 22.023  22.803  53.175  1.00 18.09 ? 584  PRO   B N     1 
ATOM   13353 C  CA    . PRO   B 1  586  ? 23.088  22.852  54.180  1.00 17.58 ? 584  PRO   B CA    1 
ATOM   13354 C  C     . PRO   B 1  586  ? 24.449  23.018  53.534  1.00 19.65 ? 584  PRO   B C     1 
ATOM   13355 O  O     . PRO   B 1  586  ? 24.747  22.427  52.493  1.00 22.03 ? 584  PRO   B O     1 
ATOM   13356 C  CB    . PRO   B 1  586  ? 22.977  21.500  54.887  1.00 22.79 ? 584  PRO   B CB    1 
ATOM   13357 C  CG    . PRO   B 1  586  ? 22.390  20.600  53.857  1.00 24.89 ? 584  PRO   B CG    1 
ATOM   13358 C  CD    . PRO   B 1  586  ? 21.396  21.472  53.116  1.00 23.20 ? 584  PRO   B CD    1 
ATOM   13359 N  N     . ALA   B 1  587  ? 25.279  23.826  54.172  1.00 17.92 ? 585  ALA   B N     1 
ATOM   13360 C  CA    . ALA   B 1  587  ? 26.621  24.100  53.685  1.00 19.25 ? 585  ALA   B CA    1 
ATOM   13361 C  C     . ALA   B 1  587  ? 27.639  23.256  54.435  1.00 19.32 ? 585  ALA   B C     1 
ATOM   13362 O  O     . ALA   B 1  587  ? 27.420  22.832  55.572  1.00 20.06 ? 585  ALA   B O     1 
ATOM   13363 C  CB    . ALA   B 1  587  ? 26.954  25.585  53.859  1.00 21.08 ? 585  ALA   B CB    1 
ATOM   13364 N  N     . ALA   B 1  588  ? 28.770  23.026  53.780  1.00 19.81 ? 586  ALA   B N     1 
ATOM   13365 C  CA    . ALA   B 1  588  ? 29.875  22.353  54.434  1.00 19.03 ? 586  ALA   B CA    1 
ATOM   13366 C  C     . ALA   B 1  588  ? 30.523  23.288  55.450  1.00 19.70 ? 586  ALA   B C     1 
ATOM   13367 O  O     . ALA   B 1  588  ? 30.456  24.514  55.344  1.00 22.43 ? 586  ALA   B O     1 
ATOM   13368 C  CB    . ALA   B 1  588  ? 30.924  21.948  53.404  1.00 19.12 ? 586  ALA   B CB    1 
ATOM   13369 N  N     . GLY   B 1  589  ? 31.175  22.691  56.434  1.00 19.62 ? 587  GLY   B N     1 
ATOM   13370 C  CA    . GLY   B 1  589  ? 31.944  23.475  57.376  1.00 19.91 ? 587  GLY   B CA    1 
ATOM   13371 C  C     . GLY   B 1  589  ? 32.717  22.575  58.309  1.00 24.22 ? 587  GLY   B C     1 
ATOM   13372 O  O     . GLY   B 1  589  ? 32.758  21.357  58.132  1.00 23.46 ? 587  GLY   B O     1 
ATOM   13373 N  N     . GLU   B 1  590  ? 33.319  23.195  59.323  1.00 22.85 ? 588  GLU   B N     1 
ATOM   13374 C  CA    . GLU   B 1  590  ? 34.087  22.457  60.319  1.00 23.18 ? 588  GLU   B CA    1 
ATOM   13375 C  C     . GLU   B 1  590  ? 33.133  21.800  61.304  1.00 19.93 ? 588  GLU   B C     1 
ATOM   13376 O  O     . GLU   B 1  590  ? 32.253  22.457  61.863  1.00 20.19 ? 588  GLU   B O     1 
ATOM   13377 C  CB    . GLU   B 1  590  ? 35.011  23.410  61.072  1.00 25.93 ? 588  GLU   B CB    1 
ATOM   13378 C  CG    . GLU   B 1  590  ? 36.067  24.057  60.199  1.00 34.05 ? 588  GLU   B CG    1 
ATOM   13379 C  CD    . GLU   B 1  590  ? 37.070  23.049  59.670  1.00 42.73 ? 588  GLU   B CD    1 
ATOM   13380 O  OE1   . GLU   B 1  590  ? 37.428  22.117  60.422  1.00 47.91 ? 588  GLU   B OE1   1 
ATOM   13381 O  OE2   . GLU   B 1  590  ? 37.489  23.185  58.501  1.00 55.61 ? 588  GLU   B OE2   1 
ATOM   13382 N  N     . THR   B 1  591  ? 33.312  20.508  61.531  1.00 20.38 ? 589  THR   B N     1 
ATOM   13383 C  CA    . THR   B 1  591  ? 32.381  19.736  62.338  1.00 21.94 ? 589  THR   B CA    1 
ATOM   13384 C  C     . THR   B 1  591  ? 33.056  19.267  63.620  1.00 20.59 ? 589  THR   B C     1 
ATOM   13385 O  O     . THR   B 1  591  ? 34.243  18.911  63.624  1.00 21.42 ? 589  THR   B O     1 
ATOM   13386 C  CB    . THR   B 1  591  ? 31.865  18.546  61.530  1.00 22.53 ? 589  THR   B CB    1 
ATOM   13387 O  OG1   . THR   B 1  591  ? 31.240  19.040  60.338  1.00 24.57 ? 589  THR   B OG1   1 
ATOM   13388 C  CG2   . THR   B 1  591  ? 30.851  17.751  62.333  1.00 23.63 ? 589  THR   B CG2   1 
ATOM   13389 N  N     . ARG   B 1  592  ? 32.304  19.306  64.714  1.00 20.31 ? 590  ARG   B N     1 
ATOM   13390 C  CA    . ARG   B 1  592  ? 32.785  18.800  65.984  1.00 23.01 ? 590  ARG   B CA    1 
ATOM   13391 C  C     . ARG   B 1  592  ? 31.619  18.180  66.733  1.00 21.32 ? 590  ARG   B C     1 
ATOM   13392 O  O     . ARG   B 1  592  ? 30.451  18.422  66.419  1.00 19.53 ? 590  ARG   B O     1 
ATOM   13393 C  CB    . ARG   B 1  592  ? 33.411  19.915  66.819  1.00 22.23 ? 590  ARG   B CB    1 
ATOM   13394 C  CG    . ARG   B 1  592  ? 32.424  20.977  67.246  1.00 21.95 ? 590  ARG   B CG    1 
ATOM   13395 C  CD    . ARG   B 1  592  ? 33.027  21.825  68.332  1.00 30.78 ? 590  ARG   B CD    1 
ATOM   13396 N  NE    . ARG   B 1  592  ? 32.211  23.000  68.599  1.00 29.63 ? 590  ARG   B NE    1 
ATOM   13397 C  CZ    . ARG   B 1  592  ? 31.196  23.014  69.447  1.00 30.33 ? 590  ARG   B CZ    1 
ATOM   13398 N  NH1   . ARG   B 1  592  ? 30.837  21.927  70.112  1.00 27.14 ? 590  ARG   B NH1   1 
ATOM   13399 N  NH2   . ARG   B 1  592  ? 30.520  24.146  69.626  1.00 27.98 ? 590  ARG   B NH2   1 
ATOM   13400 N  N     . THR   B 1  593  ? 31.944  17.388  67.748  1.00 21.53 ? 591  THR   B N     1 
ATOM   13401 C  CA    . THR   B 1  593  ? 30.913  16.797  68.578  1.00 20.62 ? 591  THR   B CA    1 
ATOM   13402 C  C     . THR   B 1  593  ? 30.401  17.801  69.598  1.00 20.88 ? 591  THR   B C     1 
ATOM   13403 O  O     . THR   B 1  593  ? 31.065  18.776  69.955  1.00 21.61 ? 591  THR   B O     1 
ATOM   13404 C  CB    . THR   B 1  593  ? 31.451  15.581  69.327  1.00 25.35 ? 591  THR   B CB    1 
ATOM   13405 O  OG1   . THR   B 1  593  ? 32.599  15.972  70.089  1.00 28.52 ? 591  THR   B OG1   1 
ATOM   13406 C  CG2   . THR   B 1  593  ? 31.829  14.481  68.350  1.00 32.44 ? 591  THR   B CG2   1 
ATOM   13407 N  N     . VAL   B 1  594  ? 29.185  17.548  70.052  1.00 19.45 ? 592  VAL   B N     1 
ATOM   13408 C  CA    . VAL   B 1  594  ? 28.569  18.278  71.147  1.00 16.74 ? 592  VAL   B CA    1 
ATOM   13409 C  C     . VAL   B 1  594  ? 28.456  17.283  72.287  1.00 19.46 ? 592  VAL   B C     1 
ATOM   13410 O  O     . VAL   B 1  594  ? 27.850  16.218  72.124  1.00 20.78 ? 592  VAL   B O     1 
ATOM   13411 C  CB    . VAL   B 1  594  ? 27.191  18.813  70.728  1.00 20.23 ? 592  VAL   B CB    1 
ATOM   13412 C  CG1   . VAL   B 1  594  ? 26.501  19.515  71.893  1.00 20.63 ? 592  VAL   B CG1   1 
ATOM   13413 C  CG2   . VAL   B 1  594  ? 27.341  19.750  69.524  1.00 19.97 ? 592  VAL   B CG2   1 
ATOM   13414 N  N     . LEU   B 1  595  ? 29.066  17.606  73.426  1.00 19.66 ? 593  LEU   B N     1 
ATOM   13415 C  CA    . LEU   B 1  595  ? 29.158  16.694  74.553  1.00 18.02 ? 593  LEU   B CA    1 
ATOM   13416 C  C     . LEU   B 1  595  ? 28.261  17.187  75.675  1.00 18.94 ? 593  LEU   B C     1 
ATOM   13417 O  O     . LEU   B 1  595  ? 28.078  18.391  75.861  1.00 20.97 ? 593  LEU   B O     1 
ATOM   13418 C  CB    . LEU   B 1  595  ? 30.590  16.626  75.074  1.00 20.22 ? 593  LEU   B CB    1 
ATOM   13419 C  CG    . LEU   B 1  595  ? 31.621  16.243  74.024  1.00 21.92 ? 593  LEU   B CG    1 
ATOM   13420 C  CD1   . LEU   B 1  595  ? 32.976  16.189  74.709  1.00 23.51 ? 593  LEU   B CD1   1 
ATOM   13421 C  CD2   . LEU   B 1  595  ? 31.255  14.907  73.374  1.00 21.68 ? 593  LEU   B CD2   1 
ATOM   13422 N  N     . ASN   B 1  596  ? 27.710  16.244  76.423  1.00 18.28 ? 594  ASN   B N     1 
ATOM   13423 C  CA    . ASN   B 1  596  ? 26.875  16.583  77.566  1.00 17.24 ? 594  ASN   B CA    1 
ATOM   13424 C  C     . ASN   B 1  596  ? 27.733  17.300  78.602  1.00 18.30 ? 594  ASN   B C     1 
ATOM   13425 O  O     . ASN   B 1  596  ? 28.750  16.737  79.039  1.00 16.95 ? 594  ASN   B O     1 
ATOM   13426 C  CB    . ASN   B 1  596  ? 26.361  15.262  78.127  1.00 17.24 ? 594  ASN   B CB    1 
ATOM   13427 C  CG    . ASN   B 1  596  ? 25.332  15.430  79.206  1.00 17.21 ? 594  ASN   B CG    1 
ATOM   13428 O  OD1   . ASN   B 1  596  ? 25.363  16.384  79.979  1.00 18.57 ? 594  ASN   B OD1   1 
ATOM   13429 N  ND2   . ASN   B 1  596  ? 24.423  14.467  79.289  1.00 20.28 ? 594  ASN   B ND2   1 
ATOM   13430 N  N     . PRO   B 1  597  ? 27.399  18.531  78.999  1.00 15.91 ? 595  PRO   B N     1 
ATOM   13431 C  CA    . PRO   B 1  597  ? 28.250  19.228  79.982  1.00 17.06 ? 595  PRO   B CA    1 
ATOM   13432 C  C     . PRO   B 1  597  ? 28.341  18.512  81.310  1.00 16.67 ? 595  PRO   B C     1 
ATOM   13433 O  O     . PRO   B 1  597  ? 29.320  18.711  82.037  1.00 18.09 ? 595  PRO   B O     1 
ATOM   13434 C  CB    . PRO   B 1  597  ? 27.586  20.606  80.136  1.00 16.87 ? 595  PRO   B CB    1 
ATOM   13435 C  CG    . PRO   B 1  597  ? 26.139  20.374  79.717  1.00 17.72 ? 595  PRO   B CG    1 
ATOM   13436 C  CD    . PRO   B 1  597  ? 26.252  19.364  78.583  1.00 16.57 ? 595  PRO   B CD    1 
ATOM   13437 N  N     . GLY   B 1  598  ? 27.359  17.678  81.639  1.00 17.47 ? 596  GLY   B N     1 
ATOM   13438 C  CA    . GLY   B 1  598  ? 27.382  16.917  82.869  1.00 17.81 ? 596  GLY   B CA    1 
ATOM   13439 C  C     . GLY   B 1  598  ? 28.134  15.616  82.789  1.00 17.55 ? 596  GLY   B C     1 
ATOM   13440 O  O     . GLY   B 1  598  ? 28.377  14.982  83.820  1.00 19.56 ? 596  GLY   B O     1 
ATOM   13441 N  N     . ASP   B 1  599  ? 28.539  15.212  81.589  1.00 17.06 ? 597  ASP   B N     1 
ATOM   13442 C  CA    . ASP   B 1  599  ? 29.320  13.996  81.405  1.00 17.89 ? 597  ASP   B CA    1 
ATOM   13443 C  C     . ASP   B 1  599  ? 29.859  14.003  79.987  1.00 19.68 ? 597  ASP   B C     1 
ATOM   13444 O  O     . ASP   B 1  599  ? 29.140  13.660  79.041  1.00 19.09 ? 597  ASP   B O     1 
ATOM   13445 C  CB    . ASP   B 1  599  ? 28.435  12.769  81.609  1.00 18.84 ? 597  ASP   B CB    1 
ATOM   13446 C  CG    . ASP   B 1  599  ? 29.213  11.479  81.625  1.00 23.29 ? 597  ASP   B CG    1 
ATOM   13447 O  OD1   . ASP   B 1  599  ? 30.359  11.452  81.117  1.00 21.13 ? 597  ASP   B OD1   1 
ATOM   13448 O  OD2   . ASP   B 1  599  ? 28.662  10.485  82.145  1.00 24.44 ? 597  ASP   B OD2   1 
ATOM   13449 N  N     . HIS   B 1  600  ? 31.126  14.379  79.826  1.00 17.83 ? 598  HIS   B N     1 
ATOM   13450 C  CA    . HIS   B 1  600  ? 31.648  14.526  78.474  1.00 19.87 ? 598  HIS   B CA    1 
ATOM   13451 C  C     . HIS   B 1  600  ? 31.728  13.205  77.720  1.00 20.33 ? 598  HIS   B C     1 
ATOM   13452 O  O     . HIS   B 1  600  ? 31.942  13.223  76.506  1.00 23.62 ? 598  HIS   B O     1 
ATOM   13453 C  CB    . HIS   B 1  600  ? 33.002  15.246  78.475  1.00 22.01 ? 598  HIS   B CB    1 
ATOM   13454 C  CG    . HIS   B 1  600  ? 32.899  16.695  78.828  1.00 21.57 ? 598  HIS   B CG    1 
ATOM   13455 N  ND1   . HIS   B 1  600  ? 34.000  17.514  78.959  1.00 26.88 ? 598  HIS   B ND1   1 
ATOM   13456 C  CD2   . HIS   B 1  600  ? 31.819  17.469  79.085  1.00 21.35 ? 598  HIS   B CD2   1 
ATOM   13457 C  CE1   . HIS   B 1  600  ? 33.601  18.733  79.281  1.00 29.82 ? 598  HIS   B CE1   1 
ATOM   13458 N  NE2   . HIS   B 1  600  ? 32.282  18.733  79.362  1.00 24.88 ? 598  HIS   B NE2   1 
ATOM   13459 N  N     . ARG   B 1  601  ? 31.546  12.070  78.399  1.00 20.31 ? 599  ARG   B N     1 
ATOM   13460 C  CA    . ARG   B 1  601  ? 31.488  10.796  77.702  1.00 20.67 ? 599  ARG   B CA    1 
ATOM   13461 C  C     . ARG   B 1  601  ? 30.198  10.631  76.917  1.00 20.13 ? 599  ARG   B C     1 
ATOM   13462 O  O     . ARG   B 1  601  ? 30.141  9.791   76.011  1.00 23.33 ? 599  ARG   B O     1 
ATOM   13463 C  CB    . ARG   B 1  601  ? 31.620  9.652   78.695  1.00 25.54 ? 599  ARG   B CB    1 
ATOM   13464 C  CG    . ARG   B 1  601  ? 32.906  9.705   79.494  1.00 25.18 ? 599  ARG   B CG    1 
ATOM   13465 C  CD    . ARG   B 1  601  ? 32.850  8.726   80.631  1.00 26.71 ? 599  ARG   B CD    1 
ATOM   13466 N  NE    . ARG   B 1  601  ? 31.750  9.012   81.538  1.00 24.52 ? 599  ARG   B NE    1 
ATOM   13467 C  CZ    . ARG   B 1  601  ? 31.457  8.276   82.598  1.00 28.63 ? 599  ARG   B CZ    1 
ATOM   13468 N  NH1   . ARG   B 1  601  ? 32.193  7.224   82.931  1.00 30.02 ? 599  ARG   B NH1   1 
ATOM   13469 N  NH2   . ARG   B 1  601  ? 30.399  8.597   83.339  1.00 28.80 ? 599  ARG   B NH2   1 
ATOM   13470 N  N     . ASP   B 1  602  ? 29.167  11.410  77.245  1.00 20.88 ? 600  ASP   B N     1 
ATOM   13471 C  CA    . ASP   B 1  602  ? 27.864  11.304  76.598  1.00 20.96 ? 600  ASP   B CA    1 
ATOM   13472 C  C     . ASP   B 1  602  ? 27.877  12.254  75.406  1.00 21.11 ? 600  ASP   B C     1 
ATOM   13473 O  O     . ASP   B 1  602  ? 27.777  13.474  75.564  1.00 21.50 ? 600  ASP   B O     1 
ATOM   13474 C  CB    . ASP   B 1  602  ? 26.767  11.634  77.602  1.00 21.55 ? 600  ASP   B CB    1 
ATOM   13475 C  CG    . ASP   B 1  602  ? 25.389  11.584  76.991  1.00 23.75 ? 600  ASP   B CG    1 
ATOM   13476 O  OD1   . ASP   B 1  602  ? 25.214  10.863  75.981  1.00 23.74 ? 600  ASP   B OD1   1 
ATOM   13477 O  OD2   . ASP   B 1  602  ? 24.488  12.269  77.526  1.00 23.60 ? 600  ASP   B OD2   1 
ATOM   13478 N  N     . VAL   B 1  603  ? 28.034  11.696  74.209  1.00 21.14 ? 601  VAL   B N     1 
ATOM   13479 C  CA    . VAL   B 1  603  ? 28.032  12.482  72.982  1.00 20.50 ? 601  VAL   B CA    1 
ATOM   13480 C  C     . VAL   B 1  603  ? 26.584  12.742  72.592  1.00 20.85 ? 601  VAL   B C     1 
ATOM   13481 O  O     . VAL   B 1  603  ? 25.812  11.804  72.357  1.00 22.85 ? 601  VAL   B O     1 
ATOM   13482 C  CB    . VAL   B 1  603  ? 28.784  11.756  71.859  1.00 22.25 ? 601  VAL   B CB    1 
ATOM   13483 C  CG1   . VAL   B 1  603  ? 28.757  12.586  70.584  1.00 23.29 ? 601  VAL   B CG1   1 
ATOM   13484 C  CG2   . VAL   B 1  603  ? 30.227  11.479  72.280  1.00 23.33 ? 601  VAL   B CG2   1 
ATOM   13485 N  N     . VAL   B 1  604  ? 26.206  14.017  72.553  1.00 18.72 ? 602  VAL   B N     1 
ATOM   13486 C  CA    . VAL   B 1  604  ? 24.826  14.372  72.248  1.00 16.35 ? 602  VAL   B CA    1 
ATOM   13487 C  C     . VAL   B 1  604  ? 24.606  14.465  70.749  1.00 18.69 ? 602  VAL   B C     1 
ATOM   13488 O  O     . VAL   B 1  604  ? 23.563  14.049  70.245  1.00 19.43 ? 602  VAL   B O     1 
ATOM   13489 C  CB    . VAL   B 1  604  ? 24.449  15.679  72.961  1.00 16.30 ? 602  VAL   B CB    1 
ATOM   13490 C  CG1   . VAL   B 1  604  ? 22.972  15.957  72.779  1.00 17.22 ? 602  VAL   B CG1   1 
ATOM   13491 C  CG2   . VAL   B 1  604  ? 24.789  15.568  74.455  1.00 16.66 ? 602  VAL   B CG2   1 
ATOM   13492 N  N     . GLY   B 1  605  ? 25.572  14.993  70.015  1.00 17.82 ? 603  GLY   B N     1 
ATOM   13493 C  CA    . GLY   B 1  605  ? 25.366  15.198  68.597  1.00 20.05 ? 603  GLY   B CA    1 
ATOM   13494 C  C     . GLY   B 1  605  ? 26.577  15.846  67.988  1.00 18.30 ? 603  GLY   B C     1 
ATOM   13495 O  O     . GLY   B 1  605  ? 27.660  15.825  68.572  1.00 18.82 ? 603  GLY   B O     1 
ATOM   13496 N  N     . SER   B 1  606  ? 26.388  16.405  66.799  1.00 17.79 ? 604  SER   B N     1 
ATOM   13497 C  CA    A SER   B 1  606  ? 27.483  17.012  66.061  0.41 19.01 ? 604  SER   B CA    1 
ATOM   13498 C  CA    B SER   B 1  606  ? 27.475  16.993  66.028  0.59 18.97 ? 604  SER   B CA    1 
ATOM   13499 C  C     . SER   B 1  606  ? 27.008  18.317  65.454  1.00 18.46 ? 604  SER   B C     1 
ATOM   13500 O  O     . SER   B 1  606  ? 25.852  18.441  65.031  1.00 19.41 ? 604  SER   B O     1 
ATOM   13501 C  CB    A SER   B 1  606  ? 28.000  16.090  64.954  0.41 24.93 ? 604  SER   B CB    1 
ATOM   13502 C  CB    B SER   B 1  606  ? 27.892  16.075  64.872  0.59 24.83 ? 604  SER   B CB    1 
ATOM   13503 O  OG    A SER   B 1  606  ? 27.039  15.938  63.931  0.41 25.48 ? 604  SER   B OG    1 
ATOM   13504 O  OG    B SER   B 1  606  ? 28.529  14.903  65.351  0.59 31.32 ? 604  SER   B OG    1 
ATOM   13505 N  N     . VAL   B 1  607  ? 27.903  19.295  65.428  1.00 17.17 ? 605  VAL   B N     1 
ATOM   13506 C  CA    . VAL   B 1  607  ? 27.608  20.597  64.858  1.00 16.24 ? 605  VAL   B CA    1 
ATOM   13507 C  C     . VAL   B 1  607  ? 28.619  20.893  63.764  1.00 17.71 ? 605  VAL   B C     1 
ATOM   13508 O  O     . VAL   B 1  607  ? 29.830  20.703  63.942  1.00 17.87 ? 605  VAL   B O     1 
ATOM   13509 C  CB    . VAL   B 1  607  ? 27.576  21.709  65.924  1.00 16.21 ? 605  VAL   B CB    1 
ATOM   13510 C  CG1   . VAL   B 1  607  ? 28.892  21.760  66.730  1.00 18.47 ? 605  VAL   B CG1   1 
ATOM   13511 C  CG2   . VAL   B 1  607  ? 27.273  23.041  65.270  1.00 18.26 ? 605  VAL   B CG2   1 
ATOM   13512 N  N     . THR   B 1  608  ? 28.119  21.349  62.631  1.00 16.95 ? 606  THR   B N     1 
ATOM   13513 C  CA    . THR   B 1  608  ? 28.953  21.860  61.563  1.00 16.47 ? 606  THR   B CA    1 
ATOM   13514 C  C     . THR   B 1  608  ? 28.820  23.374  61.594  1.00 15.60 ? 606  THR   B C     1 
ATOM   13515 O  O     . THR   B 1  608  ? 27.717  23.907  61.471  1.00 17.93 ? 606  THR   B O     1 
ATOM   13516 C  CB    . THR   B 1  608  ? 28.476  21.285  60.236  1.00 19.36 ? 606  THR   B CB    1 
ATOM   13517 O  OG1   . THR   B 1  608  ? 28.664  19.868  60.269  1.00 18.73 ? 606  THR   B OG1   1 
ATOM   13518 C  CG2   . THR   B 1  608  ? 29.257  21.871  59.073  1.00 19.41 ? 606  THR   B CG2   1 
ATOM   13519 N  N     . GLU   B 1  609  ? 29.935  24.057  61.797  1.00 16.87 ? 607  GLU   B N     1 
ATOM   13520 C  CA    . GLU   B 1  609  ? 29.878  25.486  62.008  1.00 20.23 ? 607  GLU   B CA    1 
ATOM   13521 C  C     . GLU   B 1  609  ? 30.065  26.231  60.691  1.00 17.63 ? 607  GLU   B C     1 
ATOM   13522 O  O     . GLU   B 1  609  ? 30.598  25.701  59.714  1.00 18.72 ? 607  GLU   B O     1 
ATOM   13523 C  CB    . GLU   B 1  609  ? 30.854  25.894  63.112  1.00 20.41 ? 607  GLU   B CB    1 
ATOM   13524 C  CG    . GLU   B 1  609  ? 30.362  25.367  64.468  1.00 23.51 ? 607  GLU   B CG    1 
ATOM   13525 C  CD    . GLU   B 1  609  ? 31.259  25.718  65.632  1.00 30.50 ? 607  GLU   B CD    1 
ATOM   13526 O  OE1   . GLU   B 1  609  ? 32.481  25.863  65.421  1.00 37.35 ? 607  GLU   B OE1   1 
ATOM   13527 O  OE2   . GLU   B 1  609  ? 30.737  25.845  66.761  1.00 27.75 ? 607  GLU   B OE2   1 
ATOM   13528 N  N     . THR   B 1  610  ? 29.589  27.468  60.676  1.00 17.14 ? 608  THR   B N     1 
ATOM   13529 C  CA    . THR   B 1  610  ? 29.430  28.244  59.457  1.00 16.50 ? 608  THR   B CA    1 
ATOM   13530 C  C     . THR   B 1  610  ? 30.703  29.025  59.192  1.00 17.97 ? 608  THR   B C     1 
ATOM   13531 O  O     . THR   B 1  610  ? 31.239  29.674  60.092  1.00 20.43 ? 608  THR   B O     1 
ATOM   13532 C  CB    . THR   B 1  610  ? 28.279  29.238  59.642  1.00 17.53 ? 608  THR   B CB    1 
ATOM   13533 O  OG1   . THR   B 1  610  ? 27.098  28.565  60.099  1.00 17.73 ? 608  THR   B OG1   1 
ATOM   13534 C  CG2   . THR   B 1  610  ? 27.967  29.932  58.333  1.00 18.58 ? 608  THR   B CG2   1 
ATOM   13535 N  N     . SER   B 1  611  ? 31.176  28.978  57.957  1.00 16.99 ? 609  SER   B N     1 
ATOM   13536 C  CA    . SER   B 1  611  ? 32.270  29.860  57.581  1.00 17.52 ? 609  SER   B CA    1 
ATOM   13537 C  C     . SER   B 1  611  ? 31.771  31.297  57.499  1.00 21.50 ? 609  SER   B C     1 
ATOM   13538 O  O     . SER   B 1  611  ? 30.590  31.554  57.252  1.00 18.87 ? 609  SER   B O     1 
ATOM   13539 C  CB    . SER   B 1  611  ? 32.822  29.452  56.219  1.00 21.86 ? 609  SER   B CB    1 
ATOM   13540 O  OG    . SER   B 1  611  ? 31.906  29.766  55.185  1.00 21.24 ? 609  SER   B OG    1 
ATOM   13541 N  N     . GLU   B 1  612  ? 32.680  32.252  57.710  1.00 21.00 ? 610  GLU   B N     1 
ATOM   13542 C  CA    . GLU   B 1  612  ? 32.271  33.646  57.601  1.00 22.67 ? 610  GLU   B CA    1 
ATOM   13543 C  C     . GLU   B 1  612  ? 31.786  33.966  56.195  1.00 24.19 ? 610  GLU   B C     1 
ATOM   13544 O  O     . GLU   B 1  612  ? 30.856  34.768  56.023  1.00 22.08 ? 610  GLU   B O     1 
ATOM   13545 C  CB    . GLU   B 1  612  ? 33.400  34.572  58.066  1.00 25.79 ? 610  GLU   B CB    1 
ATOM   13546 C  CG    . GLU   B 1  612  ? 33.774  34.337  59.534  1.00 29.79 ? 610  GLU   B CG    1 
ATOM   13547 C  CD    . GLU   B 1  612  ? 34.929  35.209  60.011  1.00 37.01 ? 610  GLU   B CD    1 
ATOM   13548 O  OE1   . GLU   B 1  612  ? 35.087  36.335  59.493  1.00 48.01 ? 610  GLU   B OE1   1 
ATOM   13549 O  OE2   . GLU   B 1  612  ? 35.675  34.766  60.910  1.00 39.10 ? 610  GLU   B OE2   1 
ATOM   13550 N  N     . GLU   B 1  613  ? 32.364  33.317  55.184  1.00 21.01 ? 611  GLU   B N     1 
ATOM   13551 C  CA    . GLU   B 1  613  ? 31.876  33.497  53.820  1.00 22.15 ? 611  GLU   B CA    1 
ATOM   13552 C  C     . GLU   B 1  613  ? 30.433  33.021  53.687  1.00 22.77 ? 611  GLU   B C     1 
ATOM   13553 O  O     . GLU   B 1  613  ? 29.604  33.692  53.060  1.00 23.01 ? 611  GLU   B O     1 
ATOM   13554 C  CB    . GLU   B 1  613  ? 32.789  32.772  52.826  1.00 26.77 ? 611  GLU   B CB    1 
ATOM   13555 N  N     . ASP   B 1  614  ? 30.105  31.872  54.285  1.00 19.34 ? 612  ASP   B N     1 
ATOM   13556 C  CA    . ASP   B 1  614  ? 28.726  31.397  54.192  1.00 18.22 ? 612  ASP   B CA    1 
ATOM   13557 C  C     . ASP   B 1  614  ? 27.781  32.239  55.030  1.00 17.93 ? 612  ASP   B C     1 
ATOM   13558 O  O     . ASP   B 1  614  ? 26.600  32.358  54.686  1.00 18.92 ? 612  ASP   B O     1 
ATOM   13559 C  CB    . ASP   B 1  614  ? 28.635  29.920  54.549  1.00 20.15 ? 612  ASP   B CB    1 
ATOM   13560 C  CG    . ASP   B 1  614  ? 29.093  29.024  53.409  1.00 24.42 ? 612  ASP   B CG    1 
ATOM   13561 O  OD1   . ASP   B 1  614  ? 28.995  29.451  52.232  1.00 27.69 ? 612  ASP   B OD1   1 
ATOM   13562 O  OD2   . ASP   B 1  614  ? 29.556  27.902  53.693  1.00 25.47 ? 612  ASP   B OD2   1 
ATOM   13563 N  N     . ALA   B 1  615  ? 28.271  32.829  56.120  1.00 18.03 ? 613  ALA   B N     1 
ATOM   13564 C  CA    . ALA   B 1  615  ? 27.446  33.771  56.864  1.00 17.36 ? 613  ALA   B CA    1 
ATOM   13565 C  C     . ALA   B 1  615  ? 27.045  34.947  55.987  1.00 18.12 ? 613  ALA   B C     1 
ATOM   13566 O  O     . ALA   B 1  615  ? 25.874  35.333  55.938  1.00 17.96 ? 613  ALA   B O     1 
ATOM   13567 C  CB    . ALA   B 1  615  ? 28.178  34.248  58.114  1.00 20.94 ? 613  ALA   B CB    1 
ATOM   13568 N  N     . ARG   B 1  616  ? 28.008  35.523  55.269  1.00 20.72 ? 614  ARG   B N     1 
ATOM   13569 C  CA    . ARG   B 1  616  ? 27.679  36.619  54.366  1.00 18.81 ? 614  ARG   B CA    1 
ATOM   13570 C  C     . ARG   B 1  616  ? 26.768  36.153  53.241  1.00 18.17 ? 614  ARG   B C     1 
ATOM   13571 O  O     . ARG   B 1  616  ? 25.834  36.869  52.854  1.00 18.84 ? 614  ARG   B O     1 
ATOM   13572 C  CB    . ARG   B 1  616  ? 28.958  37.244  53.820  1.00 22.89 ? 614  ARG   B CB    1 
ATOM   13573 C  CG    . ARG   B 1  616  ? 29.630  38.116  54.862  1.00 24.23 ? 614  ARG   B CG    1 
ATOM   13574 C  CD    . ARG   B 1  616  ? 30.811  38.855  54.268  1.00 32.10 ? 614  ARG   B CD    1 
ATOM   13575 N  NE    . ARG   B 1  616  ? 31.927  37.947  54.071  1.00 31.87 ? 614  ARG   B NE    1 
ATOM   13576 C  CZ    . ARG   B 1  616  ? 32.745  37.566  55.040  1.00 34.69 ? 614  ARG   B CZ    1 
ATOM   13577 N  NH1   . ARG   B 1  616  ? 32.589  37.999  56.282  1.00 28.33 ? 614  ARG   B NH1   1 
ATOM   13578 N  NH2   . ARG   B 1  616  ? 33.737  36.727  54.758  1.00 31.92 ? 614  ARG   B NH2   1 
ATOM   13579 N  N     . ARG   B 1  617  ? 27.025  34.962  52.702  1.00 18.04 ? 615  ARG   B N     1 
ATOM   13580 C  CA    . ARG   B 1  617  ? 26.146  34.430  51.669  1.00 20.32 ? 615  ARG   B CA    1 
ATOM   13581 C  C     . ARG   B 1  617  ? 24.720  34.303  52.189  1.00 18.28 ? 615  ARG   B C     1 
ATOM   13582 O  O     . ARG   B 1  617  ? 23.761  34.659  51.496  1.00 19.27 ? 615  ARG   B O     1 
ATOM   13583 C  CB    . ARG   B 1  617  ? 26.672  33.081  51.169  1.00 22.40 ? 615  ARG   B CB    1 
ATOM   13584 C  CG    . ARG   B 1  617  ? 25.853  32.500  50.024  1.00 24.90 ? 615  ARG   B CG    1 
ATOM   13585 C  CD    . ARG   B 1  617  ? 26.663  31.485  49.220  1.00 30.62 ? 615  ARG   B CD    1 
ATOM   13586 N  NE    . ARG   B 1  617  ? 26.839  30.222  49.925  1.00 30.42 ? 615  ARG   B NE    1 
ATOM   13587 C  CZ    . ARG   B 1  617  ? 25.965  29.226  49.897  1.00 37.79 ? 615  ARG   B CZ    1 
ATOM   13588 N  NH1   . ARG   B 1  617  ? 24.824  29.327  49.231  1.00 34.91 ? 615  ARG   B NH1   1 
ATOM   13589 N  NH2   . ARG   B 1  617  ? 26.236  28.105  50.561  1.00 39.54 ? 615  ARG   B NH2   1 
ATOM   13590 N  N     . ALA   B 1  618  ? 24.565  33.829  53.425  1.00 17.53 ? 616  ALA   B N     1 
ATOM   13591 C  CA    . ALA   B 1  618  ? 23.229  33.689  53.991  1.00 15.09 ? 616  ALA   B CA    1 
ATOM   13592 C  C     . ALA   B 1  618  ? 22.509  35.029  54.052  1.00 16.36 ? 616  ALA   B C     1 
ATOM   13593 O  O     . ALA   B 1  618  ? 21.310  35.113  53.764  1.00 16.47 ? 616  ALA   B O     1 
ATOM   13594 C  CB    . ALA   B 1  618  ? 23.324  33.077  55.387  1.00 16.21 ? 616  ALA   B CB    1 
ATOM   13595 N  N     . VAL   B 1  619  ? 23.215  36.087  54.443  1.00 17.87 ? 617  VAL   B N     1 
ATOM   13596 C  CA    . VAL   B 1  619  ? 22.570  37.393  54.516  1.00 16.96 ? 617  VAL   B CA    1 
ATOM   13597 C  C     . VAL   B 1  619  ? 22.122  37.840  53.137  1.00 18.69 ? 617  VAL   B C     1 
ATOM   13598 O  O     . VAL   B 1  619  ? 21.031  38.397  52.972  1.00 18.35 ? 617  VAL   B O     1 
ATOM   13599 C  CB    . VAL   B 1  619  ? 23.478  38.423  55.208  1.00 16.71 ? 617  VAL   B CB    1 
ATOM   13600 C  CG1   . VAL   B 1  619  ? 22.808  39.787  55.232  1.00 21.54 ? 617  VAL   B CG1   1 
ATOM   13601 C  CG2   . VAL   B 1  619  ? 23.772  37.963  56.629  1.00 19.01 ? 617  VAL   B CG2   1 
ATOM   13602 N  N     . ARG   B 1  620  ? 22.953  37.601  52.122  1.00 19.49 ? 618  ARG   B N     1 
ATOM   13603 C  CA    . ARG   B 1  620  ? 22.551  37.943  50.762  1.00 21.90 ? 618  ARG   B CA    1 
ATOM   13604 C  C     . ARG   B 1  620  ? 21.320  37.155  50.341  1.00 18.55 ? 618  ARG   B C     1 
ATOM   13605 O  O     . ARG   B 1  620  ? 20.401  37.704  49.720  1.00 19.37 ? 618  ARG   B O     1 
ATOM   13606 C  CB    . ARG   B 1  620  ? 23.712  37.711  49.798  1.00 22.80 ? 618  ARG   B CB    1 
ATOM   13607 C  CG    . ARG   B 1  620  ? 24.580  38.940  49.634  1.00 37.86 ? 618  ARG   B CG    1 
ATOM   13608 C  CD    . ARG   B 1  620  ? 25.726  38.725  48.654  1.00 40.68 ? 618  ARG   B CD    1 
ATOM   13609 N  NE    . ARG   B 1  620  ? 26.896  38.158  49.313  1.00 49.21 ? 618  ARG   B NE    1 
ATOM   13610 C  CZ    . ARG   B 1  620  ? 27.341  36.924  49.123  1.00 42.41 ? 618  ARG   B CZ    1 
ATOM   13611 N  NH1   . ARG   B 1  620  ? 26.760  36.101  48.261  1.00 43.85 ? 618  ARG   B NH1   1 
ATOM   13612 N  NH2   . ARG   B 1  620  ? 28.397  36.506  49.812  1.00 37.74 ? 618  ARG   B NH2   1 
ATOM   13613 N  N     . LEU   B 1  621  ? 21.282  35.866  50.673  1.00 18.14 ? 619  LEU   B N     1 
ATOM   13614 C  CA    . LEU   B 1  621  ? 20.111  35.061  50.360  1.00 17.58 ? 619  LEU   B CA    1 
ATOM   13615 C  C     . LEU   B 1  621  ? 18.881  35.578  51.087  1.00 19.81 ? 619  LEU   B C     1 
ATOM   13616 O  O     . LEU   B 1  621  ? 17.775  35.571  50.532  1.00 21.16 ? 619  LEU   B O     1 
ATOM   13617 C  CB    . LEU   B 1  621  ? 20.359  33.601  50.734  1.00 19.29 ? 619  LEU   B CB    1 
ATOM   13618 C  CG    . LEU   B 1  621  ? 21.401  32.893  49.868  1.00 21.37 ? 619  LEU   B CG    1 
ATOM   13619 C  CD1   . LEU   B 1  621  ? 21.735  31.542  50.473  1.00 20.82 ? 619  LEU   B CD1   1 
ATOM   13620 C  CD2   . LEU   B 1  621  ? 20.870  32.728  48.448  1.00 26.10 ? 619  LEU   B CD2   1 
ATOM   13621 N  N     . ALA   B 1  622  ? 19.051  36.017  52.338  1.00 16.67 ? 620  ALA   B N     1 
ATOM   13622 C  CA    . ALA   B 1  622  ? 17.921  36.575  53.073  1.00 17.09 ? 620  ALA   B CA    1 
ATOM   13623 C  C     . ALA   B 1  622  ? 17.441  37.873  52.432  1.00 18.37 ? 620  ALA   B C     1 
ATOM   13624 O  O     . ALA   B 1  622  ? 16.231  38.112  52.339  1.00 18.17 ? 620  ALA   B O     1 
ATOM   13625 C  CB    . ALA   B 1  622  ? 18.299  36.800  54.538  1.00 16.87 ? 620  ALA   B CB    1 
ATOM   13626 N  N     . ALA   B 1  623  ? 18.371  38.717  51.978  1.00 16.69 ? 621  ALA   B N     1 
ATOM   13627 C  CA    . ALA   B 1  623  ? 17.969  39.962  51.334  1.00 16.92 ? 621  ALA   B CA    1 
ATOM   13628 C  C     . ALA   B 1  623  ? 17.184  39.681  50.059  1.00 19.81 ? 621  ALA   B C     1 
ATOM   13629 O  O     . ALA   B 1  623  ? 16.168  40.336  49.785  1.00 18.61 ? 621  ALA   B O     1 
ATOM   13630 C  CB    . ALA   B 1  623  ? 19.203  40.814  51.038  1.00 17.86 ? 621  ALA   B CB    1 
ATOM   13631 N  N     . ASP   B 1  624  ? 17.612  38.674  49.293  1.00 20.20 ? 622  ASP   B N     1 
ATOM   13632 C  CA    . ASP   B 1  624  ? 16.923  38.342  48.050  1.00 20.99 ? 622  ASP   B CA    1 
ATOM   13633 C  C     . ASP   B 1  624  ? 15.502  37.881  48.322  1.00 22.73 ? 622  ASP   B C     1 
ATOM   13634 O  O     . ASP   B 1  624  ? 14.581  38.186  47.554  1.00 29.00 ? 622  ASP   B O     1 
ATOM   13635 C  CB    . ASP   B 1  624  ? 17.674  37.227  47.323  1.00 27.26 ? 622  ASP   B CB    1 
ATOM   13636 C  CG    . ASP   B 1  624  ? 19.058  37.639  46.869  1.00 31.91 ? 622  ASP   B CG    1 
ATOM   13637 O  OD1   . ASP   B 1  624  ? 19.341  38.853  46.789  1.00 37.86 ? 622  ASP   B OD1   1 
ATOM   13638 O  OD2   . ASP   B 1  624  ? 19.863  36.726  46.580  1.00 35.71 ? 622  ASP   B OD2   1 
ATOM   13639 N  N     . ALA   B 1  625  ? 15.305  37.156  49.415  1.00 22.80 ? 623  ALA   B N     1 
ATOM   13640 C  CA    . ALA   B 1  625  ? 14.013  36.601  49.780  1.00 28.44 ? 623  ALA   B CA    1 
ATOM   13641 C  C     . ALA   B 1  625  ? 13.159  37.560  50.591  1.00 24.65 ? 623  ALA   B C     1 
ATOM   13642 O  O     . ALA   B 1  625  ? 11.989  37.256  50.863  1.00 23.78 ? 623  ALA   B O     1 
ATOM   13643 C  CB    . ALA   B 1  625  ? 14.230  35.344  50.611  1.00 32.18 ? 623  ALA   B CB    1 
ATOM   13644 N  N     . ALA   B 1  626  ? 13.713  38.692  51.007  1.00 20.02 ? 624  ALA   B N     1 
ATOM   13645 C  CA    . ALA   B 1  626  ? 12.979  39.577  51.907  1.00 18.32 ? 624  ALA   B CA    1 
ATOM   13646 C  C     . ALA   B 1  626  ? 11.640  40.028  51.344  1.00 19.25 ? 624  ALA   B C     1 
ATOM   13647 O  O     . ALA   B 1  626  ? 10.640  39.970  52.079  1.00 21.36 ? 624  ALA   B O     1 
ATOM   13648 C  CB    . ALA   B 1  626  ? 13.868  40.734  52.365  1.00 17.68 ? 624  ALA   B CB    1 
ATOM   13649 N  N     . PRO   B 1  627  ? 11.526  40.457  50.084  1.00 19.50 ? 625  PRO   B N     1 
ATOM   13650 C  CA    . PRO   B 1  627  ? 10.204  40.884  49.598  1.00 22.64 ? 625  PRO   B CA    1 
ATOM   13651 C  C     . PRO   B 1  627  ? 9.170   39.779  49.627  1.00 20.18 ? 625  PRO   B C     1 
ATOM   13652 O  O     . PRO   B 1  627  ? 8.006   40.044  49.956  1.00 20.58 ? 625  PRO   B O     1 
ATOM   13653 C  CB    . PRO   B 1  627  ? 10.480  41.349  48.159  1.00 23.45 ? 625  PRO   B CB    1 
ATOM   13654 C  CG    . PRO   B 1  627  ? 11.925  41.633  48.114  1.00 28.51 ? 625  PRO   B CG    1 
ATOM   13655 C  CD    . PRO   B 1  627  ? 12.578  40.682  49.078  1.00 22.27 ? 625  PRO   B CD    1 
ATOM   13656 N  N     . ASP   B 1  628  ? 9.553   38.545  49.290  1.00 19.38 ? 626  ASP   B N     1 
ATOM   13657 C  CA    . ASP   B 1  628  ? 8.570   37.465  49.249  1.00 20.86 ? 626  ASP   B CA    1 
ATOM   13658 C  C     . ASP   B 1  628  ? 8.033   37.154  50.637  1.00 21.75 ? 626  ASP   B C     1 
ATOM   13659 O  O     . ASP   B 1  628  ? 6.846   36.855  50.795  1.00 22.27 ? 626  ASP   B O     1 
ATOM   13660 C  CB    . ASP   B 1  628  ? 9.168   36.198  48.644  1.00 24.35 ? 626  ASP   B CB    1 
ATOM   13661 C  CG    . ASP   B 1  628  ? 9.455   36.334  47.165  1.00 32.39 ? 626  ASP   B CG    1 
ATOM   13662 O  OD1   . ASP   B 1  628  ? 8.829   37.193  46.507  1.00 32.52 ? 626  ASP   B OD1   1 
ATOM   13663 O  OD2   . ASP   B 1  628  ? 10.310  35.574  46.667  1.00 37.16 ? 626  ASP   B OD2   1 
ATOM   13664 N  N     . TRP   B 1  629  ? 8.897   37.192  51.647  1.00 18.65 ? 627  TRP   B N     1 
ATOM   13665 C  CA    . TRP   B 1  629  ? 8.426   36.924  52.992  1.00 17.91 ? 627  TRP   B CA    1 
ATOM   13666 C  C     . TRP   B 1  629  ? 7.596   38.087  53.511  1.00 15.76 ? 627  TRP   B C     1 
ATOM   13667 O  O     . TRP   B 1  629  ? 6.565   37.874  54.154  1.00 17.36 ? 627  TRP   B O     1 
ATOM   13668 C  CB    . TRP   B 1  629  ? 9.609   36.618  53.904  1.00 17.85 ? 627  TRP   B CB    1 
ATOM   13669 C  CG    . TRP   B 1  629  ? 9.173   36.334  55.289  1.00 15.80 ? 627  TRP   B CG    1 
ATOM   13670 C  CD1   . TRP   B 1  629  ? 9.532   37.022  56.413  1.00 17.89 ? 627  TRP   B CD1   1 
ATOM   13671 C  CD2   . TRP   B 1  629  ? 8.282   35.300  55.715  1.00 15.32 ? 627  TRP   B CD2   1 
ATOM   13672 N  NE1   . TRP   B 1  629  ? 8.921   36.479  57.512  1.00 17.86 ? 627  TRP   B NE1   1 
ATOM   13673 C  CE2   . TRP   B 1  629  ? 8.141   35.426  57.115  1.00 16.51 ? 627  TRP   B CE2   1 
ATOM   13674 C  CE3   . TRP   B 1  629  ? 7.575   34.286  55.055  1.00 17.42 ? 627  TRP   B CE3   1 
ATOM   13675 C  CZ2   . TRP   B 1  629  ? 7.333   34.569  57.861  1.00 16.99 ? 627  TRP   B CZ2   1 
ATOM   13676 C  CZ3   . TRP   B 1  629  ? 6.758   33.446  55.806  1.00 18.51 ? 627  TRP   B CZ3   1 
ATOM   13677 C  CH2   . TRP   B 1  629  ? 6.652   33.589  57.193  1.00 20.08 ? 627  TRP   B CH2   1 
ATOM   13678 N  N     . ALA   B 1  630  ? 8.010   39.318  53.208  1.00 18.50 ? 628  ALA   B N     1 
ATOM   13679 C  CA    . ALA   B 1  630  ? 7.237   40.478  53.625  1.00 17.57 ? 628  ALA   B CA    1 
ATOM   13680 C  C     . ALA   B 1  630  ? 5.840   40.434  53.033  1.00 19.76 ? 628  ALA   B C     1 
ATOM   13681 O  O     . ALA   B 1  630  ? 4.887   40.916  53.654  1.00 21.15 ? 628  ALA   B O     1 
ATOM   13682 C  CB    . ALA   B 1  630  ? 7.951   41.760  53.201  1.00 20.51 ? 628  ALA   B CB    1 
ATOM   13683 N  N     . ALA   B 1  631  ? 5.699   39.831  51.853  1.00 18.42 ? 629  ALA   B N     1 
ATOM   13684 C  CA    . ALA   B 1  631  ? 4.413   39.766  51.183  1.00 18.84 ? 629  ALA   B CA    1 
ATOM   13685 C  C     . ALA   B 1  631  ? 3.500   38.689  51.738  1.00 20.48 ? 629  ALA   B C     1 
ATOM   13686 O  O     . ALA   B 1  631  ? 2.316   38.662  51.381  1.00 21.58 ? 629  ALA   B O     1 
ATOM   13687 C  CB    . ALA   B 1  631  ? 4.622   39.557  49.679  1.00 21.37 ? 629  ALA   B CB    1 
ATOM   13688 N  N     . VAL   B 1  632  ? 4.000   37.802  52.590  1.00 19.21 ? 630  VAL   B N     1 
ATOM   13689 C  CA    . VAL   B 1  632  ? 3.093   36.857  53.246  1.00 18.32 ? 630  VAL   B CA    1 
ATOM   13690 C  C     . VAL   B 1  632  ? 2.289   37.630  54.282  1.00 19.94 ? 630  VAL   B C     1 
ATOM   13691 O  O     . VAL   B 1  632  ? 2.893   38.320  55.127  1.00 19.92 ? 630  VAL   B O     1 
ATOM   13692 C  CB    . VAL   B 1  632  ? 3.888   35.740  53.911  1.00 19.53 ? 630  VAL   B CB    1 
ATOM   13693 C  CG1   . VAL   B 1  632  ? 2.941   34.822  54.685  1.00 19.40 ? 630  VAL   B CG1   1 
ATOM   13694 C  CG2   . VAL   B 1  632  ? 4.678   34.966  52.880  1.00 19.62 ? 630  VAL   B CG2   1 
ATOM   13695 N  N     . PRO   B 1  633  ? 0.959   37.588  54.236  1.00 19.24 ? 631  PRO   B N     1 
ATOM   13696 C  CA    . PRO   B 1  633  ? 0.173   38.442  55.114  1.00 18.94 ? 631  PRO   B CA    1 
ATOM   13697 C  C     . PRO   B 1  633  ? 0.507   38.164  56.569  1.00 19.32 ? 631  PRO   B C     1 
ATOM   13698 O  O     . PRO   B 1  633  ? 0.779   37.014  56.953  1.00 18.07 ? 631  PRO   B O     1 
ATOM   13699 C  CB    . PRO   B 1  633  ? -1.268  38.035  54.795  1.00 18.06 ? 631  PRO   B CB    1 
ATOM   13700 C  CG    . PRO   B 1  633  ? -1.217  37.562  53.374  1.00 22.40 ? 631  PRO   B CG    1 
ATOM   13701 C  CD    . PRO   B 1  633  ? 0.123   36.868  53.254  1.00 17.86 ? 631  PRO   B CD    1 
ATOM   13702 N  N     . PRO   B 1  634  ? 0.477   39.193  57.410  1.00 18.15 ? 632  PRO   B N     1 
ATOM   13703 C  CA    . PRO   B 1  634  ? 0.779   38.987  58.838  1.00 19.39 ? 632  PRO   B CA    1 
ATOM   13704 C  C     . PRO   B 1  634  ? -0.003  37.860  59.477  1.00 18.22 ? 632  PRO   B C     1 
ATOM   13705 O  O     . PRO   B 1  634  ? 0.576   37.096  60.256  1.00 16.46 ? 632  PRO   B O     1 
ATOM   13706 C  CB    . PRO   B 1  634  ? 0.474   40.350  59.468  1.00 19.29 ? 632  PRO   B CB    1 
ATOM   13707 C  CG    . PRO   B 1  634  ? 0.664   41.326  58.359  1.00 20.84 ? 632  PRO   B CG    1 
ATOM   13708 C  CD    . PRO   B 1  634  ? 0.318   40.615  57.068  1.00 19.73 ? 632  PRO   B CD    1 
ATOM   13709 N  N     . SER   B 1  635  ? -1.289  37.716  59.166  1.00 19.40 ? 633  SER   B N     1 
ATOM   13710 C  CA    . SER   B 1  635  ? -2.053  36.629  59.769  1.00 20.35 ? 633  SER   B CA    1 
ATOM   13711 C  C     . SER   B 1  635  ? -1.512  35.269  59.356  1.00 17.36 ? 633  SER   B C     1 
ATOM   13712 O  O     . SER   B 1  635  ? -1.548  34.325  60.147  1.00 17.68 ? 633  SER   B O     1 
ATOM   13713 C  CB    . SER   B 1  635  ? -3.536  36.750  59.413  1.00 24.81 ? 633  SER   B CB    1 
ATOM   13714 O  OG    . SER   B 1  635  ? -3.725  36.648  58.018  1.00 32.15 ? 633  SER   B OG    1 
ATOM   13715 N  N     . GLU   B 1  636  ? -1.005  35.148  58.127  1.00 17.20 ? 634  GLU   B N     1 
ATOM   13716 C  CA    . GLU   B 1  636  ? -0.439  33.873  57.702  1.00 18.13 ? 634  GLU   B CA    1 
ATOM   13717 C  C     . GLU   B 1  636  ? 0.943   33.646  58.301  1.00 16.81 ? 634  GLU   B C     1 
ATOM   13718 O  O     . GLU   B 1  636  ? 1.286   32.509  58.644  1.00 17.51 ? 634  GLU   B O     1 
ATOM   13719 C  CB    . GLU   B 1  636  ? -0.364  33.788  56.179  1.00 18.94 ? 634  GLU   B CB    1 
ATOM   13720 C  CG    . GLU   B 1  636  ? 0.265   32.475  55.684  1.00 26.32 ? 634  GLU   B CG    1 
ATOM   13721 C  CD    . GLU   B 1  636  ? -0.348  31.223  56.336  1.00 35.01 ? 634  GLU   B CD    1 
ATOM   13722 O  OE1   . GLU   B 1  636  ? -1.595  31.149  56.477  1.00 32.62 ? 634  GLU   B OE1   1 
ATOM   13723 O  OE2   . GLU   B 1  636  ? 0.425   30.312  56.716  1.00 31.14 ? 634  GLU   B OE2   1 
ATOM   13724 N  N     . ARG   B 1  637  ? 1.737   34.708  58.454  1.00 15.59 ? 635  ARG   B N     1 
ATOM   13725 C  CA    . ARG   B 1  637  ? 2.990   34.564  59.186  1.00 16.09 ? 635  ARG   B CA    1 
ATOM   13726 C  C     . ARG   B 1  637  ? 2.716   34.133  60.616  1.00 16.04 ? 635  ARG   B C     1 
ATOM   13727 O  O     . ARG   B 1  637  ? 3.398   33.249  61.147  1.00 16.98 ? 635  ARG   B O     1 
ATOM   13728 C  CB    . ARG   B 1  637  ? 3.773   35.866  59.158  1.00 14.43 ? 635  ARG   B CB    1 
ATOM   13729 C  CG    . ARG   B 1  637  ? 4.068   36.341  57.742  1.00 15.71 ? 635  ARG   B CG    1 
ATOM   13730 C  CD    . ARG   B 1  637  ? 5.107   37.429  57.712  1.00 17.20 ? 635  ARG   B CD    1 
ATOM   13731 N  NE    . ARG   B 1  637  ? 4.724   38.596  58.498  1.00 17.27 ? 635  ARG   B NE    1 
ATOM   13732 C  CZ    . ARG   B 1  637  ? 4.485   39.799  57.993  1.00 17.58 ? 635  ARG   B CZ    1 
ATOM   13733 N  NH1   . ARG   B 1  637  ? 4.419   40.002  56.687  1.00 22.34 ? 635  ARG   B NH1   1 
ATOM   13734 N  NH2   . ARG   B 1  637  ? 4.346   40.829  58.817  1.00 18.08 ? 635  ARG   B NH2   1 
ATOM   13735 N  N     . ALA   B 1  638  ? 1.692   34.723  61.244  1.00 15.07 ? 636  ALA   B N     1 
ATOM   13736 C  CA    . ALA   B 1  638  ? 1.320   34.330  62.602  1.00 14.05 ? 636  ALA   B CA    1 
ATOM   13737 C  C     . ALA   B 1  638  ? 0.843   32.885  62.641  1.00 16.01 ? 636  ALA   B C     1 
ATOM   13738 O  O     . ALA   B 1  638  ? 1.112   32.159  63.603  1.00 15.58 ? 636  ALA   B O     1 
ATOM   13739 C  CB    . ALA   B 1  638  ? 0.243   35.278  63.149  1.00 15.25 ? 636  ALA   B CB    1 
ATOM   13740 N  N     . ALA   B 1  639  ? 0.137   32.441  61.600  1.00 15.90 ? 637  ALA   B N     1 
ATOM   13741 C  CA    . ALA   B 1  639  ? -0.313  31.052  61.573  1.00 17.04 ? 637  ALA   B CA    1 
ATOM   13742 C  C     . ALA   B 1  639  ? 0.866   30.086  61.548  1.00 15.35 ? 637  ALA   B C     1 
ATOM   13743 O  O     . ALA   B 1  639  ? 0.785   28.990  62.108  1.00 16.32 ? 637  ALA   B O     1 
ATOM   13744 C  CB    . ALA   B 1  639  ? -1.234  30.809  60.379  1.00 16.43 ? 637  ALA   B CB    1 
ATOM   13745 N  N     . CYS   B 1  640  ? 1.963   30.462  60.882  1.00 15.58 ? 638  CYS   B N     1 
ATOM   13746 C  CA    . CYS   B 1  640  ? 3.178   29.652  60.940  1.00 16.36 ? 638  CYS   B CA    1 
ATOM   13747 C  C     . CYS   B 1  640  ? 3.687   29.532  62.362  1.00 13.36 ? 638  CYS   B C     1 
ATOM   13748 O  O     . CYS   B 1  640  ? 4.073   28.446  62.800  1.00 15.59 ? 638  CYS   B O     1 
ATOM   13749 C  CB    . CYS   B 1  640  ? 4.286   30.268  60.083  1.00 14.45 ? 638  CYS   B CB    1 
ATOM   13750 S  SG    . CYS   B 1  640  ? 3.985   30.223  58.335  1.00 17.59 ? 638  CYS   B SG    1 
ATOM   13751 N  N     . LEU   B 1  641  ? 3.740   30.655  63.083  1.00 13.79 ? 639  LEU   B N     1 
ATOM   13752 C  CA    . LEU   B 1  641  ? 4.189   30.597  64.468  1.00 14.58 ? 639  LEU   B CA    1 
ATOM   13753 C  C     . LEU   B 1  641  ? 3.283   29.695  65.286  1.00 15.22 ? 639  LEU   B C     1 
ATOM   13754 O  O     . LEU   B 1  641  ? 3.766   28.876  66.079  1.00 14.72 ? 639  LEU   B O     1 
ATOM   13755 C  CB    . LEU   B 1  641  ? 4.204   31.995  65.092  1.00 15.46 ? 639  LEU   B CB    1 
ATOM   13756 C  CG    . LEU   B 1  641  ? 5.470   32.829  64.925  1.00 16.05 ? 639  LEU   B CG    1 
ATOM   13757 C  CD1   . LEU   B 1  641  ? 5.830   33.070  63.459  1.00 18.80 ? 639  LEU   B CD1   1 
ATOM   13758 C  CD2   . LEU   B 1  641  ? 5.286   34.143  65.659  1.00 14.60 ? 639  LEU   B CD2   1 
ATOM   13759 N  N     . ASP   B 1  642  ? 1.963   29.827  65.102  1.00 14.10 ? 640  ASP   B N     1 
ATOM   13760 C  CA    . ASP   B 1  642  ? 1.046   28.979  65.857  1.00 15.56 ? 640  ASP   B CA    1 
ATOM   13761 C  C     . ASP   B 1  642  ? 1.234   27.518  65.493  1.00 14.60 ? 640  ASP   B C     1 
ATOM   13762 O  O     . ASP   B 1  642  ? 1.181   26.644  66.359  1.00 15.69 ? 640  ASP   B O     1 
ATOM   13763 C  CB    . ASP   B 1  642  ? -0.396  29.399  65.621  1.00 14.84 ? 640  ASP   B CB    1 
ATOM   13764 C  CG    . ASP   B 1  642  ? -0.799  30.591  66.437  1.00 18.68 ? 640  ASP   B CG    1 
ATOM   13765 O  OD1   . ASP   B 1  642  ? -0.151  30.882  67.460  1.00 18.02 ? 640  ASP   B OD1   1 
ATOM   13766 O  OD2   . ASP   B 1  642  ? -1.797  31.226  66.045  1.00 18.55 ? 640  ASP   B OD2   1 
ATOM   13767 N  N     . ARG   B 1  643  ? 1.502   27.229  64.216  1.00 14.81 ? 641  ARG   B N     1 
ATOM   13768 C  CA    . ARG   B 1  643  ? 1.745   25.838  63.850  1.00 16.79 ? 641  ARG   B CA    1 
ATOM   13769 C  C     . ARG   B 1  643  ? 3.024   25.325  64.487  1.00 15.41 ? 641  ARG   B C     1 
ATOM   13770 O  O     . ARG   B 1  643  ? 3.081   24.181  64.951  1.00 16.02 ? 641  ARG   B O     1 
ATOM   13771 C  CB    . ARG   B 1  643  ? 1.804   25.678  62.330  1.00 16.12 ? 641  ARG   B CB    1 
ATOM   13772 C  CG    . ARG   B 1  643  ? 0.430   25.534  61.699  1.00 17.86 ? 641  ARG   B CG    1 
ATOM   13773 C  CD    . ARG   B 1  643  ? 0.542   25.180  60.220  1.00 18.99 ? 641  ARG   B CD    1 
ATOM   13774 N  NE    . ARG   B 1  643  ? 1.202   26.228  59.452  1.00 20.01 ? 641  ARG   B NE    1 
ATOM   13775 C  CZ    . ARG   B 1  643  ? 0.583   27.236  58.854  1.00 21.18 ? 641  ARG   B CZ    1 
ATOM   13776 N  NH1   . ARG   B 1  643  ? -0.730  27.384  58.932  1.00 21.49 ? 641  ARG   B NH1   1 
ATOM   13777 N  NH2   . ARG   B 1  643  ? 1.302   28.119  58.164  1.00 23.57 ? 641  ARG   B NH2   1 
ATOM   13778 N  N     . ALA   B 1  644  ? 4.059   26.163  64.530  1.00 13.51 ? 642  ALA   B N     1 
ATOM   13779 C  CA    . ALA   B 1  644  ? 5.299   25.739  65.163  1.00 14.93 ? 642  ALA   B CA    1 
ATOM   13780 C  C     . ALA   B 1  644  ? 5.088   25.477  66.645  1.00 15.02 ? 642  ALA   B C     1 
ATOM   13781 O  O     . ALA   B 1  644  ? 5.677   24.550  67.212  1.00 15.06 ? 642  ALA   B O     1 
ATOM   13782 C  CB    . ALA   B 1  644  ? 6.365   26.808  64.963  1.00 13.48 ? 642  ALA   B CB    1 
ATOM   13783 N  N     . ALA   B 1  645  ? 4.248   26.292  67.291  1.00 14.37 ? 643  ALA   B N     1 
ATOM   13784 C  CA    . ALA   B 1  645  ? 3.973   26.078  68.705  1.00 15.34 ? 643  ALA   B CA    1 
ATOM   13785 C  C     . ALA   B 1  645  ? 3.285   24.740  68.928  1.00 14.92 ? 643  ALA   B C     1 
ATOM   13786 O  O     . ALA   B 1  645  ? 3.608   24.025  69.887  1.00 15.64 ? 643  ALA   B O     1 
ATOM   13787 C  CB    . ALA   B 1  645  ? 3.126   27.228  69.242  1.00 15.31 ? 643  ALA   B CB    1 
ATOM   13788 N  N     . GLU   B 1  646  ? 2.348   24.379  68.048  1.00 15.57 ? 644  GLU   B N     1 
ATOM   13789 C  CA    . GLU   B 1  646  ? 1.684   23.083  68.167  1.00 16.19 ? 644  GLU   B CA    1 
ATOM   13790 C  C     . GLU   B 1  646  ? 2.680   21.947  68.020  1.00 16.48 ? 644  GLU   B C     1 
ATOM   13791 O  O     . GLU   B 1  646  ? 2.599   20.939  68.734  1.00 16.78 ? 644  GLU   B O     1 
ATOM   13792 C  CB    . GLU   B 1  646  ? 0.611   22.924  67.084  1.00 19.18 ? 644  GLU   B CB    1 
ATOM   13793 C  CG    . GLU   B 1  646  ? -0.573  23.843  67.215  1.00 23.95 ? 644  GLU   B CG    1 
ATOM   13794 C  CD    . GLU   B 1  646  ? -1.332  23.635  68.508  1.00 32.37 ? 644  GLU   B CD    1 
ATOM   13795 O  OE1   . GLU   B 1  646  ? -1.557  22.469  68.894  1.00 40.70 ? 644  GLU   B OE1   1 
ATOM   13796 O  OE2   . GLU   B 1  646  ? -1.691  24.646  69.144  1.00 36.53 ? 644  GLU   B OE2   1 
ATOM   13797 N  N     . LEU   B 1  647  ? 3.628   22.091  67.089  1.00 16.45 ? 645  LEU   B N     1 
ATOM   13798 C  CA    . LEU   B 1  647  ? 4.624   21.046  66.905  1.00 17.40 ? 645  LEU   B CA    1 
ATOM   13799 C  C     . LEU   B 1  647  ? 5.531   20.932  68.119  1.00 17.32 ? 645  LEU   B C     1 
ATOM   13800 O  O     . LEU   B 1  647  ? 5.846   19.822  68.558  1.00 17.65 ? 645  LEU   B O     1 
ATOM   13801 C  CB    . LEU   B 1  647  ? 5.450   21.327  65.657  1.00 16.05 ? 645  LEU   B CB    1 
ATOM   13802 C  CG    . LEU   B 1  647  ? 4.676   21.262  64.343  1.00 16.66 ? 645  LEU   B CG    1 
ATOM   13803 C  CD1   . LEU   B 1  647  ? 5.625   21.599  63.212  1.00 18.26 ? 645  LEU   B CD1   1 
ATOM   13804 C  CD2   . LEU   B 1  647  ? 4.065   19.882  64.146  1.00 20.81 ? 645  LEU   B CD2   1 
ATOM   13805 N  N     . MET   B 1  648  ? 5.975   22.064  68.667  1.00 14.62 ? 646  MET   B N     1 
ATOM   13806 C  CA    . MET   B 1  648  ? 6.820   22.005  69.857  1.00 14.53 ? 646  MET   B CA    1 
ATOM   13807 C  C     . MET   B 1  648  ? 6.060   21.415  71.033  1.00 15.34 ? 646  MET   B C     1 
ATOM   13808 O  O     . MET   B 1  648  ? 6.632   20.684  71.846  1.00 17.48 ? 646  MET   B O     1 
ATOM   13809 C  CB    . MET   B 1  648  ? 7.338   23.389  70.231  1.00 17.78 ? 646  MET   B CB    1 
ATOM   13810 C  CG    . MET   B 1  648  ? 8.370   23.905  69.284  1.00 18.39 ? 646  MET   B CG    1 
ATOM   13811 S  SD    . MET   B 1  648  ? 9.169   25.314  70.063  1.00 19.39 ? 646  MET   B SD    1 
ATOM   13812 C  CE    . MET   B 1  648  ? 10.228  25.811  68.727  1.00 20.40 ? 646  MET   B CE    1 
ATOM   13813 N  N     . GLN   B 1  649  ? 4.766   21.714  71.140  1.00 15.11 ? 647  GLN   B N     1 
ATOM   13814 C  CA    . GLN   B 1  649  ? 3.997   21.152  72.243  1.00 16.30 ? 647  GLN   B CA    1 
ATOM   13815 C  C     . GLN   B 1  649  ? 3.915   19.638  72.114  1.00 16.08 ? 647  GLN   B C     1 
ATOM   13816 O  O     . GLN   B 1  649  ? 4.112   18.907  73.094  1.00 18.35 ? 647  GLN   B O     1 
ATOM   13817 C  CB    . GLN   B 1  649  ? 2.598   21.754  72.232  1.00 16.05 ? 647  GLN   B CB    1 
ATOM   13818 C  CG    . GLN   B 1  649  ? 1.742   21.317  73.397  1.00 16.40 ? 647  GLN   B CG    1 
ATOM   13819 C  CD    . GLN   B 1  649  ? 2.194   21.952  74.693  1.00 16.49 ? 647  GLN   B CD    1 
ATOM   13820 O  OE1   . GLN   B 1  649  ? 1.906   23.122  74.950  1.00 17.48 ? 647  GLN   B OE1   1 
ATOM   13821 N  NE2   . GLN   B 1  649  ? 2.944   21.203  75.494  1.00 17.72 ? 647  GLN   B NE2   1 
ATOM   13822 N  N     . ALA   B 1  650  ? 3.633   19.157  70.900  1.00 16.54 ? 648  ALA   B N     1 
ATOM   13823 C  CA    . ALA   B 1  650  ? 3.479   17.724  70.690  1.00 17.36 ? 648  ALA   B CA    1 
ATOM   13824 C  C     . ALA   B 1  650  ? 4.803   16.995  70.841  1.00 20.28 ? 648  ALA   B C     1 
ATOM   13825 O  O     . ALA   B 1  650  ? 4.822   15.836  71.263  1.00 21.25 ? 648  ALA   B O     1 
ATOM   13826 C  CB    . ALA   B 1  650  ? 2.901   17.458  69.301  1.00 19.08 ? 648  ALA   B CB    1 
ATOM   13827 N  N     . ARG   B 1  651  ? 5.912   17.658  70.520  1.00 17.35 ? 649  ARG   B N     1 
ATOM   13828 C  CA    . ARG   B 1  651  ? 7.231   17.049  70.565  1.00 16.85 ? 649  ARG   B CA    1 
ATOM   13829 C  C     . ARG   B 1  651  ? 7.995   17.402  71.821  1.00 17.05 ? 649  ARG   B C     1 
ATOM   13830 O  O     . ARG   B 1  651  ? 9.176   17.069  71.933  1.00 18.21 ? 649  ARG   B O     1 
ATOM   13831 C  CB    . ARG   B 1  651  ? 8.013   17.458  69.327  1.00 17.95 ? 649  ARG   B CB    1 
ATOM   13832 C  CG    . ARG   B 1  651  ? 7.291   16.960  68.102  1.00 19.57 ? 649  ARG   B CG    1 
ATOM   13833 C  CD    . ARG   B 1  651  ? 7.931   17.415  66.825  1.00 20.48 ? 649  ARG   B CD    1 
ATOM   13834 N  NE    . ARG   B 1  651  ? 7.034   17.094  65.727  1.00 21.50 ? 649  ARG   B NE    1 
ATOM   13835 C  CZ    . ARG   B 1  651  ? 7.213   17.503  64.482  1.00 20.53 ? 649  ARG   B CZ    1 
ATOM   13836 N  NH1   . ARG   B 1  651  ? 8.290   18.196  64.134  1.00 21.53 ? 649  ARG   B NH1   1 
ATOM   13837 N  NH2   . ARG   B 1  651  ? 6.300   17.200  63.562  1.00 20.17 ? 649  ARG   B NH2   1 
ATOM   13838 N  N     . MET   B 1  652  ? 7.342   18.044  72.781  1.00 16.55 ? 650  MET   B N     1 
ATOM   13839 C  CA    . MET   B 1  652  ? 8.021   18.435  74.010  1.00 16.75 ? 650  MET   B CA    1 
ATOM   13840 C  C     . MET   B 1  652  ? 8.827   17.312  74.645  1.00 17.65 ? 650  MET   B C     1 
ATOM   13841 O  O     . MET   B 1  652  ? 9.967   17.578  75.047  1.00 18.59 ? 650  MET   B O     1 
ATOM   13842 C  CB    . MET   B 1  652  ? 7.015   19.035  75.005  1.00 16.76 ? 650  MET   B CB    1 
ATOM   13843 C  CG    . MET   B 1  652  ? 7.648   19.422  76.330  1.00 16.26 ? 650  MET   B CG    1 
ATOM   13844 S  SD    . MET   B 1  652  ? 6.442   20.126  77.469  1.00 19.93 ? 650  MET   B SD    1 
ATOM   13845 C  CE    . MET   B 1  652  ? 6.228   21.745  76.764  1.00 18.35 ? 650  MET   B CE    1 
ATOM   13846 N  N     . PRO   B 1  653  ? 8.333   16.075  74.768  1.00 17.43 ? 651  PRO   B N     1 
ATOM   13847 C  CA    . PRO   B 1  653  ? 9.158   15.038  75.415  1.00 19.46 ? 651  PRO   B CA    1 
ATOM   13848 C  C     . PRO   B 1  653  ? 10.505  14.832  74.745  1.00 17.87 ? 651  PRO   B C     1 
ATOM   13849 O  O     . PRO   B 1  653  ? 11.530  14.720  75.433  1.00 18.58 ? 651  PRO   B O     1 
ATOM   13850 C  CB    . PRO   B 1  653  ? 8.267   13.791  75.345  1.00 19.36 ? 651  PRO   B CB    1 
ATOM   13851 C  CG    . PRO   B 1  653  ? 6.868   14.355  75.380  1.00 19.94 ? 651  PRO   B CG    1 
ATOM   13852 C  CD    . PRO   B 1  653  ? 6.961   15.593  74.518  1.00 18.49 ? 651  PRO   B CD    1 
ATOM   13853 N  N     . THR   B 1  654  ? 10.530  14.807  73.412  1.00 18.08 ? 652  THR   B N     1 
ATOM   13854 C  CA    . THR   B 1  654  ? 11.791  14.664  72.695  1.00 18.51 ? 652  THR   B CA    1 
ATOM   13855 C  C     . THR   B 1  654  ? 12.666  15.899  72.864  1.00 18.55 ? 652  THR   B C     1 
ATOM   13856 O  O     . THR   B 1  654  ? 13.870  15.781  73.113  1.00 18.11 ? 652  THR   B O     1 
ATOM   13857 C  CB    . THR   B 1  654  ? 11.506  14.402  71.216  1.00 18.67 ? 652  THR   B CB    1 
ATOM   13858 O  OG1   . THR   B 1  654  ? 10.721  13.211  71.099  1.00 22.10 ? 652  THR   B OG1   1 
ATOM   13859 C  CG2   . THR   B 1  654  ? 12.807  14.237  70.430  1.00 17.86 ? 652  THR   B CG2   1 
ATOM   13860 N  N     . LEU   B 1  655  ? 12.084  17.092  72.744  1.00 16.30 ? 653  LEU   B N     1 
ATOM   13861 C  CA    . LEU   B 1  655  ? 12.861  18.313  72.926  1.00 16.13 ? 653  LEU   B CA    1 
ATOM   13862 C  C     . LEU   B 1  655  ? 13.463  18.376  74.318  1.00 18.14 ? 653  LEU   B C     1 
ATOM   13863 O  O     . LEU   B 1  655  ? 14.604  18.829  74.487  1.00 18.25 ? 653  LEU   B O     1 
ATOM   13864 C  CB    . LEU   B 1  655  ? 11.977  19.536  72.687  1.00 17.15 ? 653  LEU   B CB    1 
ATOM   13865 C  CG    . LEU   B 1  655  ? 11.306  19.603  71.316  1.00 19.25 ? 653  LEU   B CG    1 
ATOM   13866 C  CD1   . LEU   B 1  655  ? 10.382  20.803  71.244  1.00 19.60 ? 653  LEU   B CD1   1 
ATOM   13867 C  CD2   . LEU   B 1  655  ? 12.341  19.682  70.238  1.00 21.88 ? 653  LEU   B CD2   1 
ATOM   13868 N  N     . LEU   B 1  656  ? 12.706  17.938  75.327  1.00 19.50 ? 654  LEU   B N     1 
ATOM   13869 C  CA    . LEU   B 1  656  ? 13.223  17.914  76.695  1.00 19.81 ? 654  LEU   B CA    1 
ATOM   13870 C  C     . LEU   B 1  656  ? 14.488  17.093  76.774  1.00 19.76 ? 654  LEU   B C     1 
ATOM   13871 O  O     . LEU   B 1  656  ? 15.465  17.492  77.420  1.00 20.45 ? 654  LEU   B O     1 
ATOM   13872 C  CB    . LEU   B 1  656  ? 12.209  17.260  77.631  1.00 21.51 ? 654  LEU   B CB    1 
ATOM   13873 C  CG    . LEU   B 1  656  ? 10.857  17.897  77.824  1.00 25.84 ? 654  LEU   B CG    1 
ATOM   13874 C  CD1   . LEU   B 1  656  ? 10.172  17.210  78.975  1.00 22.94 ? 654  LEU   B CD1   1 
ATOM   13875 C  CD2   . LEU   B 1  656  ? 11.020  19.371  78.049  1.00 24.23 ? 654  LEU   B CD2   1 
ATOM   13876 N  N     . GLY   B 1  657  ? 14.453  15.901  76.190  1.00 19.01 ? 655  GLY   B N     1 
ATOM   13877 C  CA    . GLY   B 1  657  ? 15.608  15.034  76.234  1.00 21.77 ? 655  GLY   B CA    1 
ATOM   13878 C  C     . GLY   B 1  657  ? 16.831  15.705  75.660  1.00 20.39 ? 655  GLY   B C     1 
ATOM   13879 O  O     . GLY   B 1  657  ? 17.921  15.611  76.219  1.00 19.91 ? 655  GLY   B O     1 
ATOM   13880 N  N     . LEU   B 1  658  ? 16.660  16.423  74.550  1.00 17.19 ? 656  LEU   B N     1 
ATOM   13881 C  CA    . LEU   B 1  658  ? 17.801  17.099  73.964  1.00 16.31 ? 656  LEU   B CA    1 
ATOM   13882 C  C     . LEU   B 1  658  ? 18.291  18.225  74.863  1.00 18.66 ? 656  LEU   B C     1 
ATOM   13883 O  O     . LEU   B 1  658  ? 19.497  18.365  75.085  1.00 18.81 ? 656  LEU   B O     1 
ATOM   13884 C  CB    . LEU   B 1  658  ? 17.425  17.602  72.571  1.00 16.94 ? 656  LEU   B CB    1 
ATOM   13885 C  CG    . LEU   B 1  658  ? 18.560  18.279  71.815  1.00 16.12 ? 656  LEU   B CG    1 
ATOM   13886 C  CD1   . LEU   B 1  658  ? 19.788  17.369  71.676  1.00 17.11 ? 656  LEU   B CD1   1 
ATOM   13887 C  CD2   . LEU   B 1  658  ? 18.070  18.739  70.446  1.00 17.31 ? 656  LEU   B CD2   1 
ATOM   13888 N  N     . ILE   B 1  659  ? 17.374  19.024  75.408  1.00 16.33 ? 657  ILE   B N     1 
ATOM   13889 C  CA    . ILE   B 1  659  ? 17.778  20.152  76.235  1.00 14.94 ? 657  ILE   B CA    1 
ATOM   13890 C  C     . ILE   B 1  659  ? 18.461  19.666  77.500  1.00 17.38 ? 657  ILE   B C     1 
ATOM   13891 O  O     . ILE   B 1  659  ? 19.455  20.250  77.951  1.00 16.86 ? 657  ILE   B O     1 
ATOM   13892 C  CB    . ILE   B 1  659  ? 16.539  21.007  76.549  1.00 15.61 ? 657  ILE   B CB    1 
ATOM   13893 C  CG1   . ILE   B 1  659  ? 16.040  21.673  75.272  1.00 16.27 ? 657  ILE   B CG1   1 
ATOM   13894 C  CG2   . ILE   B 1  659  ? 16.845  22.025  77.643  1.00 16.84 ? 657  ILE   B CG2   1 
ATOM   13895 C  CD1   . ILE   B 1  659  ? 14.603  22.159  75.387  1.00 17.65 ? 657  ILE   B CD1   1 
ATOM   13896 N  N     . ILE   B 1  660  ? 17.930  18.602  78.099  1.00 17.04 ? 658  ILE   B N     1 
ATOM   13897 C  CA    . ILE   B 1  660  ? 18.533  18.035  79.303  1.00 16.49 ? 658  ILE   B CA    1 
ATOM   13898 C  C     . ILE   B 1  660  ? 19.993  17.681  79.052  1.00 17.75 ? 658  ILE   B C     1 
ATOM   13899 O  O     . ILE   B 1  660  ? 20.882  17.993  79.861  1.00 18.26 ? 658  ILE   B O     1 
ATOM   13900 C  CB    . ILE   B 1  660  ? 17.723  16.814  79.771  1.00 17.27 ? 658  ILE   B CB    1 
ATOM   13901 C  CG1   . ILE   B 1  660  ? 16.401  17.259  80.417  1.00 18.22 ? 658  ILE   B CG1   1 
ATOM   13902 C  CG2   . ILE   B 1  660  ? 18.559  15.942  80.713  1.00 18.96 ? 658  ILE   B CG2   1 
ATOM   13903 C  CD1   . ILE   B 1  660  ? 15.478  16.090  80.709  1.00 19.98 ? 658  ILE   B CD1   1 
ATOM   13904 N  N     . ARG   B 1  661  ? 20.268  17.033  77.924  1.00 16.19 ? 659  ARG   B N     1 
ATOM   13905 C  CA    . ARG   B 1  661  ? 21.611  16.520  77.684  1.00 15.74 ? 659  ARG   B CA    1 
ATOM   13906 C  C     . ARG   B 1  661  ? 22.536  17.563  77.086  1.00 17.62 ? 659  ARG   B C     1 
ATOM   13907 O  O     . ARG   B 1  661  ? 23.743  17.528  77.348  1.00 19.40 ? 659  ARG   B O     1 
ATOM   13908 C  CB    . ARG   B 1  661  ? 21.557  15.255  76.825  1.00 17.48 ? 659  ARG   B CB    1 
ATOM   13909 C  CG    . ARG   B 1  661  ? 21.009  14.078  77.609  1.00 18.87 ? 659  ARG   B CG    1 
ATOM   13910 C  CD    . ARG   B 1  661  ? 20.826  12.841  76.745  1.00 20.02 ? 659  ARG   B CD    1 
ATOM   13911 N  NE    . ARG   B 1  661  ? 22.053  12.409  76.077  1.00 20.55 ? 659  ARG   B NE    1 
ATOM   13912 C  CZ    . ARG   B 1  661  ? 22.187  12.286  74.763  1.00 21.52 ? 659  ARG   B CZ    1 
ATOM   13913 N  NH1   . ARG   B 1  661  ? 21.202  12.588  73.933  1.00 22.74 ? 659  ARG   B NH1   1 
ATOM   13914 N  NH2   . ARG   B 1  661  ? 23.336  11.829  74.264  1.00 22.40 ? 659  ARG   B NH2   1 
ATOM   13915 N  N     . GLU   B 1  662  ? 22.005  18.497  76.299  1.00 16.39 ? 660  GLU   B N     1 
ATOM   13916 C  CA    . GLU   B 1  662  ? 22.885  19.461  75.654  1.00 18.13 ? 660  GLU   B CA    1 
ATOM   13917 C  C     . GLU   B 1  662  ? 23.194  20.647  76.559  1.00 18.63 ? 660  GLU   B C     1 
ATOM   13918 O  O     . GLU   B 1  662  ? 24.308  21.173  76.535  1.00 19.11 ? 660  GLU   B O     1 
ATOM   13919 C  CB    . GLU   B 1  662  ? 22.257  19.965  74.344  1.00 19.57 ? 660  GLU   B CB    1 
ATOM   13920 C  CG    . GLU   B 1  662  ? 23.162  20.955  73.598  1.00 19.32 ? 660  GLU   B CG    1 
ATOM   13921 C  CD    . GLU   B 1  662  ? 22.588  21.469  72.277  1.00 18.56 ? 660  GLU   B CD    1 
ATOM   13922 O  OE1   . GLU   B 1  662  ? 21.354  21.623  72.147  1.00 20.09 ? 660  GLU   B OE1   1 
ATOM   13923 O  OE2   . GLU   B 1  662  ? 23.402  21.730  71.380  1.00 19.74 ? 660  GLU   B OE2   1 
ATOM   13924 N  N     . ALA   B 1  663  ? 22.228  21.092  77.357  1.00 16.21 ? 661  ALA   B N     1 
ATOM   13925 C  CA    . ALA   B 1  663  ? 22.385  22.343  78.079  1.00 16.82 ? 661  ALA   B CA    1 
ATOM   13926 C  C     . ALA   B 1  663  ? 22.443  22.166  79.588  1.00 18.55 ? 661  ALA   B C     1 
ATOM   13927 O  O     . ALA   B 1  663  ? 22.389  23.162  80.313  1.00 23.77 ? 661  ALA   B O     1 
ATOM   13928 C  CB    . ALA   B 1  663  ? 21.280  23.326  77.697  1.00 17.36 ? 661  ALA   B CB    1 
ATOM   13929 N  N     . GLY   B 1  664  ? 22.512  20.929  80.076  1.00 19.67 ? 662  GLY   B N     1 
ATOM   13930 C  CA    . GLY   B 1  664  ? 22.629  20.735  81.510  1.00 21.77 ? 662  GLY   B CA    1 
ATOM   13931 C  C     . GLY   B 1  664  ? 21.383  21.059  82.299  1.00 20.19 ? 662  GLY   B C     1 
ATOM   13932 O  O     . GLY   B 1  664  ? 21.478  21.371  83.486  1.00 20.59 ? 662  GLY   B O     1 
ATOM   13933 N  N     . LYS   B 1  665  ? 20.215  20.995  81.678  1.00 18.02 ? 663  LYS   B N     1 
ATOM   13934 C  CA    . LYS   B 1  665  ? 18.988  21.370  82.361  1.00 17.94 ? 663  LYS   B CA    1 
ATOM   13935 C  C     . LYS   B 1  665  ? 18.358  20.152  83.007  1.00 16.19 ? 663  LYS   B C     1 
ATOM   13936 O  O     . LYS   B 1  665  ? 18.430  19.040  82.487  1.00 17.90 ? 663  LYS   B O     1 
ATOM   13937 C  CB    . LYS   B 1  665  ? 17.971  21.934  81.372  1.00 17.97 ? 663  LYS   B CB    1 
ATOM   13938 C  CG    . LYS   B 1  665  ? 18.449  23.142  80.605  1.00 19.84 ? 663  LYS   B CG    1 
ATOM   13939 C  CD    . LYS   B 1  665  ? 18.824  24.280  81.524  1.00 22.58 ? 663  LYS   B CD    1 
ATOM   13940 C  CE    . LYS   B 1  665  ? 19.267  25.500  80.715  1.00 27.78 ? 663  LYS   B CE    1 
ATOM   13941 N  NZ    . LYS   B 1  665  ? 19.788  26.584  81.609  1.00 27.05 ? 663  LYS   B NZ    1 
ATOM   13942 N  N     . SER   B 1  666  ? 17.704  20.382  84.139  1.00 18.96 ? 664  SER   B N     1 
ATOM   13943 C  CA    . SER   B 1  666  ? 16.848  19.355  84.697  1.00 18.30 ? 664  SER   B CA    1 
ATOM   13944 C  C     . SER   B 1  666  ? 15.564  19.247  83.880  1.00 19.42 ? 664  SER   B C     1 
ATOM   13945 O  O     . SER   B 1  666  ? 15.232  20.114  83.066  1.00 19.67 ? 664  SER   B O     1 
ATOM   13946 C  CB    . SER   B 1  666  ? 16.455  19.724  86.119  1.00 22.08 ? 664  SER   B CB    1 
ATOM   13947 O  OG    . SER   B 1  666  ? 15.586  20.843  86.077  1.00 23.04 ? 664  SER   B OG    1 
ATOM   13948 N  N     . ALA   B 1  667  ? 14.825  18.166  84.116  1.00 19.34 ? 665  ALA   B N     1 
ATOM   13949 C  CA    . ALA   B 1  667  ? 13.567  17.971  83.405  1.00 18.62 ? 665  ALA   B CA    1 
ATOM   13950 C  C     . ALA   B 1  667  ? 12.613  19.136  83.633  1.00 17.69 ? 665  ALA   B C     1 
ATOM   13951 O  O     . ALA   B 1  667  ? 11.997  19.627  82.683  1.00 18.03 ? 665  ALA   B O     1 
ATOM   13952 C  CB    . ALA   B 1  667  ? 12.919  16.658  83.836  1.00 19.91 ? 665  ALA   B CB    1 
ATOM   13953 N  N     . LEU   B 1  668  ? 12.455  19.582  84.886  1.00 17.91 ? 666  LEU   B N     1 
ATOM   13954 C  CA    . LEU   B 1  668  ? 11.533  20.689  85.129  1.00 19.22 ? 666  LEU   B CA    1 
ATOM   13955 C  C     . LEU   B 1  668  ? 11.948  21.928  84.354  1.00 18.28 ? 666  LEU   B C     1 
ATOM   13956 O  O     . LEU   B 1  668  ? 11.102  22.629  83.782  1.00 19.33 ? 666  LEU   B O     1 
ATOM   13957 C  CB    . LEU   B 1  668  ? 11.433  21.012  86.622  1.00 21.71 ? 666  LEU   B CB    1 
ATOM   13958 C  CG    . LEU   B 1  668  ? 10.448  20.156  87.410  1.00 28.12 ? 666  LEU   B CG    1 
ATOM   13959 C  CD1   . LEU   B 1  668  ? 10.503  20.515  88.888  1.00 34.19 ? 666  LEU   B CD1   1 
ATOM   13960 C  CD2   . LEU   B 1  668  ? 9.030   20.315  86.868  1.00 29.67 ? 666  LEU   B CD2   1 
ATOM   13961 N  N     . ASN   B 1  669  ? 13.244  22.220  84.327  1.00 18.82 ? 667  ASN   B N     1 
ATOM   13962 C  CA    . ASN   B 1  669  ? 13.677  23.427  83.643  1.00 19.00 ? 667  ASN   B CA    1 
ATOM   13963 C  C     . ASN   B 1  669  ? 13.645  23.269  82.136  1.00 18.39 ? 667  ASN   B C     1 
ATOM   13964 O  O     . ASN   B 1  669  ? 13.454  24.260  81.422  1.00 19.40 ? 667  ASN   B O     1 
ATOM   13965 C  CB    . ASN   B 1  669  ? 15.037  23.858  84.174  1.00 24.00 ? 667  ASN   B CB    1 
ATOM   13966 C  CG    . ASN   B 1  669  ? 14.934  24.375  85.591  1.00 25.19 ? 667  ASN   B CG    1 
ATOM   13967 O  OD1   . ASN   B 1  669  ? 13.940  25.024  85.948  1.00 31.49 ? 667  ASN   B OD1   1 
ATOM   13968 N  ND2   . ASN   B 1  669  ? 15.920  24.068  86.409  1.00 32.23 ? 667  ASN   B ND2   1 
ATOM   13969 N  N     . ALA   B 1  670  ? 13.799  22.042  81.642  1.00 16.51 ? 668  ALA   B N     1 
ATOM   13970 C  CA    . ALA   B 1  670  ? 13.642  21.801  80.218  1.00 16.88 ? 668  ALA   B CA    1 
ATOM   13971 C  C     . ALA   B 1  670  ? 12.187  21.966  79.807  1.00 17.00 ? 668  ALA   B C     1 
ATOM   13972 O  O     . ALA   B 1  670  ? 11.898  22.490  78.726  1.00 16.34 ? 668  ALA   B O     1 
ATOM   13973 C  CB    . ALA   B 1  670  ? 14.166  20.411  79.845  1.00 17.14 ? 668  ALA   B CB    1 
ATOM   13974 N  N     . ILE   B 1  671  ? 11.251  21.511  80.650  1.00 15.99 ? 669  ILE   B N     1 
ATOM   13975 C  CA    . ILE   B 1  671  ? 9.839   21.754  80.372  1.00 15.76 ? 669  ILE   B CA    1 
ATOM   13976 C  C     . ILE   B 1  671  ? 9.570   23.248  80.301  1.00 15.30 ? 669  ILE   B C     1 
ATOM   13977 O  O     . ILE   B 1  671  ? 8.913   23.731  79.374  1.00 17.05 ? 669  ILE   B O     1 
ATOM   13978 C  CB    . ILE   B 1  671  ? 8.952   21.077  81.432  1.00 15.04 ? 669  ILE   B CB    1 
ATOM   13979 C  CG1   . ILE   B 1  671  ? 8.944   19.574  81.235  1.00 17.85 ? 669  ILE   B CG1   1 
ATOM   13980 C  CG2   . ILE   B 1  671  ? 7.544   21.624  81.330  1.00 18.49 ? 669  ILE   B CG2   1 
ATOM   13981 C  CD1   . ILE   B 1  671  ? 8.478   18.815  82.465  1.00 19.77 ? 669  ILE   B CD1   1 
ATOM   13982 N  N     . ALA   B 1  672  ? 10.087  24.001  81.274  1.00 16.14 ? 670  ALA   B N     1 
ATOM   13983 C  CA    . ALA   B 1  672  ? 9.874   25.442  81.277  1.00 16.02 ? 670  ALA   B CA    1 
ATOM   13984 C  C     . ALA   B 1  672  ? 10.444  26.073  80.017  1.00 15.97 ? 670  ALA   B C     1 
ATOM   13985 O  O     . ALA   B 1  672  ? 9.849   27.004  79.458  1.00 17.57 ? 670  ALA   B O     1 
ATOM   13986 C  CB    . ALA   B 1  672  ? 10.519  26.059  82.518  1.00 19.93 ? 670  ALA   B CB    1 
ATOM   13987 N  N     . GLU   B 1  673  ? 11.599  25.582  79.568  1.00 15.86 ? 671  GLU   B N     1 
ATOM   13988 C  CA    . GLU   B 1  673  ? 12.234  26.090  78.361  1.00 16.98 ? 671  GLU   B CA    1 
ATOM   13989 C  C     . GLU   B 1  673  ? 11.340  25.889  77.146  1.00 16.24 ? 671  GLU   B C     1 
ATOM   13990 O  O     . GLU   B 1  673  ? 11.143  26.812  76.341  1.00 15.85 ? 671  GLU   B O     1 
ATOM   13991 C  CB    . GLU   B 1  673  ? 13.551  25.348  78.165  1.00 18.34 ? 671  GLU   B CB    1 
ATOM   13992 C  CG    . GLU   B 1  673  ? 14.369  25.832  77.004  1.00 18.91 ? 671  GLU   B CG    1 
ATOM   13993 C  CD    . GLU   B 1  673  ? 15.146  27.087  77.305  1.00 21.51 ? 671  GLU   B CD    1 
ATOM   13994 O  OE1   . GLU   B 1  673  ? 15.358  27.430  78.495  1.00 22.29 ? 671  GLU   B OE1   1 
ATOM   13995 O  OE2   . GLU   B 1  673  ? 15.553  27.737  76.332  1.00 17.80 ? 671  GLU   B OE2   1 
ATOM   13996 N  N     . VAL   B 1  674  ? 10.808  24.677  76.978  1.00 14.32 ? 672  VAL   B N     1 
ATOM   13997 C  CA    . VAL   B 1  674  ? 9.960   24.420  75.820  1.00 14.68 ? 672  VAL   B CA    1 
ATOM   13998 C  C     . VAL   B 1  674  ? 8.662   25.203  75.923  1.00 14.23 ? 672  VAL   B C     1 
ATOM   13999 O  O     . VAL   B 1  674  ? 8.192   25.782  74.940  1.00 14.86 ? 672  VAL   B O     1 
ATOM   14000 C  CB    . VAL   B 1  674  ? 9.716   22.915  75.633  1.00 14.39 ? 672  VAL   B CB    1 
ATOM   14001 C  CG1   . VAL   B 1  674  ? 8.865   22.673  74.402  1.00 15.24 ? 672  VAL   B CG1   1 
ATOM   14002 C  CG2   . VAL   B 1  674  ? 11.050  22.202  75.493  1.00 14.68 ? 672  VAL   B CG2   1 
ATOM   14003 N  N     . ARG   B 1  675  ? 8.082   25.261  77.119  1.00 14.13 ? 673  ARG   B N     1 
ATOM   14004 C  CA    . ARG   B 1  675  ? 6.862   26.039  77.299  1.00 13.96 ? 673  ARG   B CA    1 
ATOM   14005 C  C     . ARG   B 1  675  ? 7.083   27.489  76.922  1.00 14.71 ? 673  ARG   B C     1 
ATOM   14006 O  O     . ARG   B 1  675  ? 6.248   28.099  76.248  1.00 14.45 ? 673  ARG   B O     1 
ATOM   14007 C  CB    . ARG   B 1  675  ? 6.408   25.954  78.747  1.00 14.61 ? 673  ARG   B CB    1 
ATOM   14008 C  CG    . ARG   B 1  675  ? 5.820   24.618  79.131  1.00 16.34 ? 673  ARG   B CG    1 
ATOM   14009 C  CD    . ARG   B 1  675  ? 5.148   24.728  80.499  1.00 14.74 ? 673  ARG   B CD    1 
ATOM   14010 N  NE    . ARG   B 1  675  ? 3.999   25.620  80.412  1.00 14.83 ? 673  ARG   B NE    1 
ATOM   14011 C  CZ    . ARG   B 1  675  ? 3.415   26.181  81.461  1.00 15.93 ? 673  ARG   B CZ    1 
ATOM   14012 N  NH1   . ARG   B 1  675  ? 3.889   26.016  82.681  1.00 17.68 ? 673  ARG   B NH1   1 
ATOM   14013 N  NH2   . ARG   B 1  675  ? 2.334   26.930  81.271  1.00 15.64 ? 673  ARG   B NH2   1 
ATOM   14014 N  N     . GLU   B 1  676  ? 8.220   28.049  77.311  1.00 14.44 ? 674  GLU   B N     1 
ATOM   14015 C  CA    A GLU   B 1  676  ? 8.486   29.449  77.007  0.50 14.42 ? 674  GLU   B CA    1 
ATOM   14016 C  CA    B GLU   B 1  676  ? 8.468   29.451  77.005  0.50 14.41 ? 674  GLU   B CA    1 
ATOM   14017 C  C     . GLU   B 1  676  ? 8.594   29.675  75.504  1.00 13.23 ? 674  GLU   B C     1 
ATOM   14018 O  O     . GLU   B 1  676  ? 8.093   30.672  74.982  1.00 14.68 ? 674  GLU   B O     1 
ATOM   14019 C  CB    A GLU   B 1  676  ? 9.766   29.886  77.714  0.50 16.64 ? 674  GLU   B CB    1 
ATOM   14020 C  CB    B GLU   B 1  676  ? 9.702   29.949  77.757  0.50 16.65 ? 674  GLU   B CB    1 
ATOM   14021 C  CG    A GLU   B 1  676  ? 10.077  31.356  77.562  0.50 17.93 ? 674  GLU   B CG    1 
ATOM   14022 C  CG    B GLU   B 1  676  ? 9.902   31.449  77.650  0.50 17.73 ? 674  GLU   B CG    1 
ATOM   14023 C  CD    A GLU   B 1  676  ? 9.474   32.201  78.658  0.50 20.52 ? 674  GLU   B CD    1 
ATOM   14024 C  CD    B GLU   B 1  676  ? 10.966  31.972  78.595  0.50 22.65 ? 674  GLU   B CD    1 
ATOM   14025 O  OE1   A GLU   B 1  676  ? 8.609   31.697  79.405  0.50 26.57 ? 674  GLU   B OE1   1 
ATOM   14026 O  OE1   B GLU   B 1  676  ? 10.984  31.544  79.771  0.50 26.71 ? 674  GLU   B OE1   1 
ATOM   14027 O  OE2   A GLU   B 1  676  ? 9.881   33.375  78.771  0.50 20.47 ? 674  GLU   B OE2   1 
ATOM   14028 O  OE2   B GLU   B 1  676  ? 11.780  32.811  78.164  0.50 25.84 ? 674  GLU   B OE2   1 
ATOM   14029 N  N     . ALA   B 1  677  ? 9.253   28.760  74.794  1.00 13.43 ? 675  ALA   B N     1 
ATOM   14030 C  CA    . ALA   B 1  677  ? 9.307   28.871  73.340  1.00 13.01 ? 675  ALA   B CA    1 
ATOM   14031 C  C     . ALA   B 1  677  ? 7.910   28.840  72.733  1.00 14.28 ? 675  ALA   B C     1 
ATOM   14032 O  O     . ALA   B 1  677  ? 7.592   29.644  71.851  1.00 14.08 ? 675  ALA   B O     1 
ATOM   14033 C  CB    . ALA   B 1  677  ? 10.171  27.749  72.762  1.00 15.54 ? 675  ALA   B CB    1 
ATOM   14034 N  N     . ILE   B 1  678  ? 7.066   27.911  73.197  1.00 14.19 ? 676  ILE   B N     1 
ATOM   14035 C  CA    . ILE   B 1  678  ? 5.686   27.826  72.733  1.00 12.98 ? 676  ILE   B CA    1 
ATOM   14036 C  C     . ILE   B 1  678  ? 4.960   29.128  73.005  1.00 12.93 ? 676  ILE   B C     1 
ATOM   14037 O  O     . ILE   B 1  678  ? 4.249   29.653  72.139  1.00 14.77 ? 676  ILE   B O     1 
ATOM   14038 C  CB    . ILE   B 1  678  ? 4.974   26.638  73.402  1.00 13.57 ? 676  ILE   B CB    1 
ATOM   14039 C  CG1   . ILE   B 1  678  ? 5.548   25.317  72.886  1.00 15.20 ? 676  ILE   B CG1   1 
ATOM   14040 C  CG2   . ILE   B 1  678  ? 3.443   26.706  73.215  1.00 14.64 ? 676  ILE   B CG2   1 
ATOM   14041 C  CD1   . ILE   B 1  678  ? 5.339   24.154  73.859  1.00 15.00 ? 676  ILE   B CD1   1 
ATOM   14042 N  N     . ASP   B 1  679  ? 5.151   29.674  74.202  1.00 13.22 ? 677  ASP   B N     1 
ATOM   14043 C  CA    . ASP   B 1  679  ? 4.462   30.902  74.565  1.00 14.04 ? 677  ASP   B CA    1 
ATOM   14044 C  C     . ASP   B 1  679  ? 4.941   32.083  73.733  1.00 13.93 ? 677  ASP   B C     1 
ATOM   14045 O  O     . ASP   B 1  679  ? 4.134   32.925  73.343  1.00 14.34 ? 677  ASP   B O     1 
ATOM   14046 C  CB    . ASP   B 1  679  ? 4.615   31.186  76.056  1.00 13.57 ? 677  ASP   B CB    1 
ATOM   14047 C  CG    . ASP   B 1  679  ? 3.870   30.194  76.926  1.00 16.36 ? 677  ASP   B CG    1 
ATOM   14048 O  OD1   . ASP   B 1  679  ? 2.802   29.697  76.515  1.00 17.36 ? 677  ASP   B OD1   1 
ATOM   14049 O  OD2   . ASP   B 1  679  ? 4.350   29.942  78.051  1.00 18.65 ? 677  ASP   B OD2   1 
ATOM   14050 N  N     . PHE   B 1  680  ? 6.246   32.178  73.468  1.00 13.51 ? 678  PHE   B N     1 
ATOM   14051 C  CA    . PHE   B 1  680  ? 6.718   33.239  72.573  1.00 13.78 ? 678  PHE   B CA    1 
ATOM   14052 C  C     . PHE   B 1  680  ? 6.045   33.135  71.216  1.00 13.42 ? 678  PHE   B C     1 
ATOM   14053 O  O     . PHE   B 1  680  ? 5.575   34.133  70.654  1.00 13.32 ? 678  PHE   B O     1 
ATOM   14054 C  CB    . PHE   B 1  680  ? 8.224   33.131  72.361  1.00 12.89 ? 678  PHE   B CB    1 
ATOM   14055 C  CG    . PHE   B 1  680  ? 9.058   33.796  73.426  1.00 13.61 ? 678  PHE   B CG    1 
ATOM   14056 C  CD1   . PHE   B 1  680  ? 8.831   35.102  73.817  1.00 13.67 ? 678  PHE   B CD1   1 
ATOM   14057 C  CD2   . PHE   B 1  680  ? 10.113  33.099  74.005  1.00 13.98 ? 678  PHE   B CD2   1 
ATOM   14058 C  CE1   . PHE   B 1  680  ? 9.645   35.699  74.790  1.00 15.02 ? 678  PHE   B CE1   1 
ATOM   14059 C  CE2   . PHE   B 1  680  ? 10.909  33.689  74.976  1.00 14.72 ? 678  PHE   B CE2   1 
ATOM   14060 C  CZ    . PHE   B 1  680  ? 10.680  34.979  75.359  1.00 16.04 ? 678  PHE   B CZ    1 
ATOM   14061 N  N     . LEU   B 1  681  ? 6.038   31.931  70.651  1.00 12.34 ? 679  LEU   B N     1 
ATOM   14062 C  CA    . LEU   B 1  681  ? 5.419   31.734  69.350  1.00 12.88 ? 679  LEU   B CA    1 
ATOM   14063 C  C     . LEU   B 1  681  ? 3.978   32.211  69.366  1.00 13.20 ? 679  LEU   B C     1 
ATOM   14064 O  O     . LEU   B 1  681  ? 3.549   32.980  68.495  1.00 13.74 ? 679  LEU   B O     1 
ATOM   14065 C  CB    . LEU   B 1  681  ? 5.477   30.252  68.995  1.00 13.27 ? 679  LEU   B CB    1 
ATOM   14066 C  CG    . LEU   B 1  681  ? 6.891   29.789  68.629  1.00 13.09 ? 679  LEU   B CG    1 
ATOM   14067 C  CD1   . LEU   B 1  681  ? 6.976   28.284  68.701  1.00 13.80 ? 679  LEU   B CD1   1 
ATOM   14068 C  CD2   . LEU   B 1  681  ? 7.268   30.276  67.227  1.00 14.21 ? 679  LEU   B CD2   1 
ATOM   14069 N  N     . ARG   B 1  682  ? 3.204   31.762  70.355  1.00 12.52 ? 680  ARG   B N     1 
ATOM   14070 C  CA    . ARG   B 1  682  ? 1.792   32.094  70.361  1.00 12.84 ? 680  ARG   B CA    1 
ATOM   14071 C  C     . ARG   B 1  682  ? 1.559   33.545  70.724  1.00 12.60 ? 680  ARG   B C     1 
ATOM   14072 O  O     . ARG   B 1  682  ? 0.611   34.158  70.225  1.00 13.92 ? 680  ARG   B O     1 
ATOM   14073 C  CB    . ARG   B 1  682  ? 1.058   31.165  71.313  1.00 13.10 ? 680  ARG   B CB    1 
ATOM   14074 C  CG    . ARG   B 1  682  ? 1.006   29.757  70.785  1.00 14.20 ? 680  ARG   B CG    1 
ATOM   14075 C  CD    . ARG   B 1  682  ? 0.344   28.880  71.800  1.00 15.33 ? 680  ARG   B CD    1 
ATOM   14076 N  NE    . ARG   B 1  682  ? 0.121   27.540  71.286  1.00 16.09 ? 680  ARG   B NE    1 
ATOM   14077 C  CZ    . ARG   B 1  682  ? -0.095  26.490  72.061  1.00 16.07 ? 680  ARG   B CZ    1 
ATOM   14078 N  NH1   . ARG   B 1  682  ? -0.134  26.604  73.378  1.00 16.59 ? 680  ARG   B NH1   1 
ATOM   14079 N  NH2   . ARG   B 1  682  ? -0.247  25.297  71.502  1.00 19.42 ? 680  ARG   B NH2   1 
ATOM   14080 N  N     . TYR   B 1  683  ? 2.396   34.099  71.591  1.00 12.48 ? 681  TYR   B N     1 
ATOM   14081 C  CA    . TYR   B 1  683  ? 2.240   35.497  71.974  1.00 14.30 ? 681  TYR   B CA    1 
ATOM   14082 C  C     . TYR   B 1  683  ? 2.546   36.416  70.803  1.00 14.87 ? 681  TYR   B C     1 
ATOM   14083 O  O     . TYR   B 1  683  ? 1.776   37.331  70.510  1.00 14.92 ? 681  TYR   B O     1 
ATOM   14084 C  CB    . TYR   B 1  683  ? 3.121   35.814  73.180  1.00 13.63 ? 681  TYR   B CB    1 
ATOM   14085 C  CG    . TYR   B 1  683  ? 3.074   37.260  73.592  1.00 12.76 ? 681  TYR   B CG    1 
ATOM   14086 C  CD1   . TYR   B 1  683  ? 2.002   37.757  74.330  1.00 14.45 ? 681  TYR   B CD1   1 
ATOM   14087 C  CD2   . TYR   B 1  683  ? 4.096   38.123  73.236  1.00 15.32 ? 681  TYR   B CD2   1 
ATOM   14088 C  CE1   . TYR   B 1  683  ? 1.962   39.089  74.701  1.00 15.08 ? 681  TYR   B CE1   1 
ATOM   14089 C  CE2   . TYR   B 1  683  ? 4.064   39.450  73.591  1.00 14.04 ? 681  TYR   B CE2   1 
ATOM   14090 C  CZ    . TYR   B 1  683  ? 2.996   39.923  74.325  1.00 14.33 ? 681  TYR   B CZ    1 
ATOM   14091 O  OH    . TYR   B 1  683  ? 2.971   41.242  74.676  1.00 16.53 ? 681  TYR   B OH    1 
ATOM   14092 N  N     . TYR   B 1  684  ? 3.671   36.199  70.120  1.00 13.34 ? 682  TYR   B N     1 
ATOM   14093 C  CA    . TYR   B 1  684  ? 3.972   37.078  68.992  1.00 13.92 ? 682  TYR   B CA    1 
ATOM   14094 C  C     . TYR   B 1  684  ? 2.990   36.875  67.853  1.00 14.61 ? 682  TYR   B C     1 
ATOM   14095 O  O     . TYR   B 1  684  ? 2.684   37.831  67.139  1.00 14.76 ? 682  TYR   B O     1 
ATOM   14096 C  CB    . TYR   B 1  684  ? 5.420   36.908  68.528  1.00 13.50 ? 682  TYR   B CB    1 
ATOM   14097 C  CG    . TYR   B 1  684  ? 6.421   37.290  69.587  1.00 12.86 ? 682  TYR   B CG    1 
ATOM   14098 C  CD1   . TYR   B 1  684  ? 6.252   38.434  70.350  1.00 15.48 ? 682  TYR   B CD1   1 
ATOM   14099 C  CD2   . TYR   B 1  684  ? 7.547   36.499  69.819  1.00 12.90 ? 682  TYR   B CD2   1 
ATOM   14100 C  CE1   . TYR   B 1  684  ? 7.169   38.781  71.320  1.00 14.78 ? 682  TYR   B CE1   1 
ATOM   14101 C  CE2   . TYR   B 1  684  ? 8.468   36.831  70.794  1.00 12.91 ? 682  TYR   B CE2   1 
ATOM   14102 C  CZ    . TYR   B 1  684  ? 8.274   37.971  71.537  1.00 14.74 ? 682  TYR   B CZ    1 
ATOM   14103 O  OH    . TYR   B 1  684  ? 9.183   38.286  72.508  1.00 14.48 ? 682  TYR   B OH    1 
ATOM   14104 N  N     . ALA   B 1  685  ? 2.450   35.664  67.696  1.00 13.54 ? 683  ALA   B N     1 
ATOM   14105 C  CA    . ALA   B 1  685  ? 1.392   35.458  66.713  1.00 14.48 ? 683  ALA   B CA    1 
ATOM   14106 C  C     . ALA   B 1  685  ? 0.177   36.303  67.050  1.00 14.52 ? 683  ALA   B C     1 
ATOM   14107 O  O     . ALA   B 1  685  ? -0.356  37.015  66.191  1.00 14.73 ? 683  ALA   B O     1 
ATOM   14108 C  CB    . ALA   B 1  685  ? 1.020   33.977  66.648  1.00 15.14 ? 683  ALA   B CB    1 
ATOM   14109 N  N     . GLU   B 1  686  ? -0.263  36.256  68.308  1.00 14.08 ? 684  GLU   B N     1 
ATOM   14110 C  CA    . GLU   B 1  686  ? -1.437  37.040  68.667  1.00 15.43 ? 684  GLU   B CA    1 
ATOM   14111 C  C     . GLU   B 1  686  ? -1.152  38.535  68.595  1.00 16.56 ? 684  GLU   B C     1 
ATOM   14112 O  O     . GLU   B 1  686  ? -1.981  39.303  68.093  1.00 15.84 ? 684  GLU   B O     1 
ATOM   14113 C  CB    . GLU   B 1  686  ? -1.925  36.648  70.051  1.00 17.42 ? 684  GLU   B CB    1 
ATOM   14114 C  CG    . GLU   B 1  686  ? -3.064  37.552  70.563  1.00 18.89 ? 684  GLU   B CG    1 
ATOM   14115 C  CD    . GLU   B 1  686  ? -4.360  37.465  69.750  1.00 24.26 ? 684  GLU   B CD    1 
ATOM   14116 O  OE1   . GLU   B 1  686  ? -4.522  36.584  68.867  1.00 22.56 ? 684  GLU   B OE1   1 
ATOM   14117 O  OE2   . GLU   B 1  686  ? -5.252  38.292  70.024  1.00 25.78 ? 684  GLU   B OE2   1 
ATOM   14118 N  N     . GLN   B 1  687  ? 0.022   38.970  69.063  1.00 14.96 ? 685  GLN   B N     1 
ATOM   14119 C  CA    . GLN   B 1  687  ? 0.325   40.391  68.981  1.00 14.49 ? 685  GLN   B CA    1 
ATOM   14120 C  C     . GLN   B 1  687  ? 0.336   40.857  67.534  1.00 15.07 ? 685  GLN   B C     1 
ATOM   14121 O  O     . GLN   B 1  687  ? -0.109  41.973  67.224  1.00 16.11 ? 685  GLN   B O     1 
ATOM   14122 C  CB    . GLN   B 1  687  ? 1.659   40.698  69.657  1.00 15.13 ? 685  GLN   B CB    1 
ATOM   14123 C  CG    . GLN   B 1  687  ? 1.613   40.507  71.168  1.00 17.81 ? 685  GLN   B CG    1 
ATOM   14124 C  CD    . GLN   B 1  687  ? 0.587   41.406  71.813  1.00 19.25 ? 685  GLN   B CD    1 
ATOM   14125 O  OE1   . GLN   B 1  687  ? 0.640   42.624  71.660  1.00 18.16 ? 685  GLN   B OE1   1 
ATOM   14126 N  NE2   . GLN   B 1  687  ? -0.369  40.807  72.527  1.00 20.88 ? 685  GLN   B NE2   1 
ATOM   14127 N  N     . THR   B 1  688  ? 0.818   40.003  66.628  1.00 14.18 ? 686  THR   B N     1 
ATOM   14128 C  CA    . THR   B 1  688  ? 0.766   40.331  65.209  1.00 15.29 ? 686  THR   B CA    1 
ATOM   14129 C  C     . THR   B 1  688  ? -0.672  40.493  64.743  1.00 15.46 ? 686  THR   B C     1 
ATOM   14130 O  O     . THR   B 1  688  ? -1.006  41.464  64.055  1.00 16.42 ? 686  THR   B O     1 
ATOM   14131 C  CB    . THR   B 1  688  ? 1.450   39.227  64.414  1.00 14.98 ? 686  THR   B CB    1 
ATOM   14132 O  OG1   . THR   B 1  688  ? 2.840   39.261  64.723  1.00 15.93 ? 686  THR   B OG1   1 
ATOM   14133 C  CG2   . THR   B 1  688  ? 1.266   39.451  62.926  1.00 15.27 ? 686  THR   B CG2   1 
ATOM   14134 N  N     . ARG   B 1  689  ? -1.535  39.539  65.098  1.00 15.21 ? 687  ARG   B N     1 
ATOM   14135 C  CA    . ARG   B 1  689  ? -2.937  39.623  64.693  1.00 14.25 ? 687  ARG   B CA    1 
ATOM   14136 C  C     . ARG   B 1  689  ? -3.620  40.864  65.246  1.00 16.57 ? 687  ARG   B C     1 
ATOM   14137 O  O     . ARG   B 1  689  ? -4.578  41.353  64.646  1.00 18.11 ? 687  ARG   B O     1 
ATOM   14138 C  CB    . ARG   B 1  689  ? -3.666  38.363  65.138  1.00 15.31 ? 687  ARG   B CB    1 
ATOM   14139 C  CG    . ARG   B 1  689  ? -3.301  37.141  64.302  1.00 19.74 ? 687  ARG   B CG    1 
ATOM   14140 C  CD    . ARG   B 1  689  ? -4.202  35.988  64.658  1.00 18.99 ? 687  ARG   B CD    1 
ATOM   14141 N  NE    . ARG   B 1  689  ? -4.024  35.581  66.043  1.00 20.24 ? 687  ARG   B NE    1 
ATOM   14142 C  CZ    . ARG   B 1  689  ? -3.263  34.571  66.437  1.00 19.77 ? 687  ARG   B CZ    1 
ATOM   14143 N  NH1   . ARG   B 1  689  ? -2.587  33.840  65.568  1.00 19.00 ? 687  ARG   B NH1   1 
ATOM   14144 N  NH2   . ARG   B 1  689  ? -3.195  34.280  67.734  1.00 19.40 ? 687  ARG   B NH2   1 
ATOM   14145 N  N     . ARG   B 1  690  ? -3.148  41.386  66.375  1.00 15.02 ? 688  ARG   B N     1 
ATOM   14146 C  CA    . ARG   B 1  690  ? -3.719  42.595  66.948  1.00 16.03 ? 688  ARG   B CA    1 
ATOM   14147 C  C     . ARG   B 1  690  ? -3.187  43.876  66.324  1.00 15.87 ? 688  ARG   B C     1 
ATOM   14148 O  O     . ARG   B 1  690  ? -3.813  44.928  66.498  1.00 16.27 ? 688  ARG   B O     1 
ATOM   14149 C  CB    . ARG   B 1  690  ? -3.397  42.646  68.444  1.00 18.87 ? 688  ARG   B CB    1 
ATOM   14150 C  CG    . ARG   B 1  690  ? -4.067  41.559  69.270  1.00 17.42 ? 688  ARG   B CG    1 
ATOM   14151 C  CD    . ARG   B 1  690  ? -5.568  41.831  69.464  1.00 21.07 ? 688  ARG   B CD    1 
ATOM   14152 N  NE    . ARG   B 1  690  ? -5.804  43.090  70.169  1.00 22.59 ? 688  ARG   B NE    1 
ATOM   14153 C  CZ    . ARG   B 1  690  ? -6.375  44.155  69.630  1.00 23.84 ? 688  ARG   B CZ    1 
ATOM   14154 N  NH1   . ARG   B 1  690  ? -6.831  44.140  68.389  1.00 24.84 ? 688  ARG   B NH1   1 
ATOM   14155 N  NH2   . ARG   B 1  690  ? -6.516  45.257  70.364  1.00 21.02 ? 688  ARG   B NH2   1 
ATOM   14156 N  N     . THR   B 1  691  ? -2.037  43.837  65.646  1.00 15.76 ? 689  THR   B N     1 
ATOM   14157 C  CA    . THR   B 1  691  ? -1.404  45.105  65.296  1.00 17.21 ? 689  THR   B CA    1 
ATOM   14158 C  C     . THR   B 1  691  ? -1.004  45.277  63.837  1.00 17.09 ? 689  THR   B C     1 
ATOM   14159 O  O     . THR   B 1  691  ? -1.172  46.369  63.301  1.00 20.05 ? 689  THR   B O     1 
ATOM   14160 C  CB    . THR   B 1  691  ? -0.161  45.341  66.154  1.00 16.08 ? 689  THR   B CB    1 
ATOM   14161 O  OG1   . THR   B 1  691  ? 0.753   44.247  65.987  1.00 17.52 ? 689  THR   B OG1   1 
ATOM   14162 C  CG2   . THR   B 1  691  ? -0.535  45.476  67.620  1.00 19.11 ? 689  THR   B CG2   1 
ATOM   14163 N  N     . LEU   B 1  692  ? -0.408  44.271  63.203  1.00 15.74 ? 690  LEU   B N     1 
ATOM   14164 C  CA    . LEU   B 1  692  ? 0.352   44.554  61.992  1.00 15.88 ? 690  LEU   B CA    1 
ATOM   14165 C  C     . LEU   B 1  692  ? -0.535  44.698  60.760  1.00 16.18 ? 690  LEU   B C     1 
ATOM   14166 O  O     . LEU   B 1  692  ? -1.364  43.834  60.459  1.00 19.58 ? 690  LEU   B O     1 
ATOM   14167 C  CB    . LEU   B 1  692  ? 1.430   43.501  61.756  1.00 16.76 ? 690  LEU   B CB    1 
ATOM   14168 C  CG    . LEU   B 1  692  ? 2.490   43.463  62.853  1.00 18.21 ? 690  LEU   B CG    1 
ATOM   14169 C  CD1   . LEU   B 1  692  ? 3.610   42.527  62.426  1.00 20.06 ? 690  LEU   B CD1   1 
ATOM   14170 C  CD2   . LEU   B 1  692  ? 3.038   44.835  63.161  1.00 18.84 ? 690  LEU   B CD2   1 
ATOM   14171 N  N     . GLY   B 1  693  ? -0.330  45.800  60.050  1.00 18.60 ? 691  GLY   B N     1 
ATOM   14172 C  CA    . GLY   B 1  693  ? -1.032  46.090  58.831  1.00 18.58 ? 691  GLY   B CA    1 
ATOM   14173 C  C     . GLY   B 1  693  ? -0.066  46.491  57.741  1.00 19.83 ? 691  GLY   B C     1 
ATOM   14174 O  O     . GLY   B 1  693  ? 1.155   46.448  57.908  1.00 20.43 ? 691  GLY   B O     1 
ATOM   14175 N  N     . PRO   B 1  694  ? -0.605  46.917  56.604  1.00 23.68 ? 692  PRO   B N     1 
ATOM   14176 C  CA    . PRO   B 1  694  ? 0.255   47.136  55.429  1.00 22.16 ? 692  PRO   B CA    1 
ATOM   14177 C  C     . PRO   B 1  694  ? 1.311   48.208  55.618  1.00 23.30 ? 692  PRO   B C     1 
ATOM   14178 O  O     . PRO   B 1  694  ? 2.382   48.118  55.005  1.00 27.73 ? 692  PRO   B O     1 
ATOM   14179 C  CB    . PRO   B 1  694  ? -0.741  47.469  54.306  1.00 25.31 ? 692  PRO   B CB    1 
ATOM   14180 C  CG    . PRO   B 1  694  ? -2.042  47.784  54.998  1.00 28.55 ? 692  PRO   B CG    1 
ATOM   14181 C  CD    . PRO   B 1  694  ? -2.040  47.040  56.301  1.00 24.03 ? 692  PRO   B CD    1 
ATOM   14182 N  N     . GLY   B 1  695  ? 1.064   49.210  56.456  1.00 21.80 ? 693  GLY   B N     1 
ATOM   14183 C  CA    . GLY   B 1  695  ? 2.017   50.270  56.683  1.00 23.04 ? 693  GLY   B CA    1 
ATOM   14184 C  C     . GLY   B 1  695  ? 3.101   49.969  57.690  1.00 23.18 ? 693  GLY   B C     1 
ATOM   14185 O  O     . GLY   B 1  695  ? 3.937   50.836  57.962  1.00 27.01 ? 693  GLY   B O     1 
ATOM   14186 N  N     . HIS   B 1  696  ? 3.105   48.772  58.278  1.00 22.55 ? 694  HIS   B N     1 
ATOM   14187 C  CA    . HIS   B 1  696  ? 4.155   48.378  59.220  1.00 19.18 ? 694  HIS   B CA    1 
ATOM   14188 C  C     . HIS   B 1  696  ? 5.132   47.472  58.479  1.00 20.02 ? 694  HIS   B C     1 
ATOM   14189 O  O     . HIS   B 1  696  ? 5.134   46.252  58.624  1.00 25.51 ? 694  HIS   B O     1 
ATOM   14190 C  CB    . HIS   B 1  696  ? 3.543   47.691  60.425  1.00 19.20 ? 694  HIS   B CB    1 
ATOM   14191 C  CG    . HIS   B 1  696  ? 2.432   48.475  61.034  1.00 18.00 ? 694  HIS   B CG    1 
ATOM   14192 N  ND1   . HIS   B 1  696  ? 1.158   47.974  61.158  1.00 18.96 ? 694  HIS   B ND1   1 
ATOM   14193 C  CD2   . HIS   B 1  696  ? 2.393   49.739  61.516  1.00 19.79 ? 694  HIS   B CD2   1 
ATOM   14194 C  CE1   . HIS   B 1  696  ? 0.382   48.889  61.711  1.00 20.24 ? 694  HIS   B CE1   1 
ATOM   14195 N  NE2   . HIS   B 1  696  ? 1.105   49.971  61.932  1.00 19.76 ? 694  HIS   B NE2   1 
ATOM   14196 N  N     . GLY   B 1  697  ? 5.973   48.095  57.665  1.00 22.60 ? 695  GLY   B N     1 
ATOM   14197 C  CA    . GLY   B 1  697  ? 6.872   47.350  56.814  1.00 21.17 ? 695  GLY   B CA    1 
ATOM   14198 C  C     . GLY   B 1  697  ? 8.025   46.751  57.588  1.00 17.92 ? 695  GLY   B C     1 
ATOM   14199 O  O     . GLY   B 1  697  ? 8.493   47.311  58.573  1.00 20.37 ? 695  GLY   B O     1 
ATOM   14200 N  N     . PRO   B 1  698  ? 8.534   45.615  57.130  1.00 21.11 ? 696  PRO   B N     1 
ATOM   14201 C  CA    . PRO   B 1  698  ? 9.660   44.984  57.827  1.00 20.00 ? 696  PRO   B CA    1 
ATOM   14202 C  C     . PRO   B 1  698  ? 10.947  45.772  57.643  1.00 17.60 ? 696  PRO   B C     1 
ATOM   14203 O  O     . PRO   B 1  698  ? 11.094  46.592  56.735  1.00 19.36 ? 696  PRO   B O     1 
ATOM   14204 C  CB    . PRO   B 1  698  ? 9.773   43.619  57.147  1.00 21.69 ? 696  PRO   B CB    1 
ATOM   14205 C  CG    . PRO   B 1  698  ? 9.244   43.863  55.782  1.00 27.86 ? 696  PRO   B CG    1 
ATOM   14206 C  CD    . PRO   B 1  698  ? 8.107   44.839  55.956  1.00 23.95 ? 696  PRO   B CD    1 
ATOM   14207 N  N     . LEU   B 1  699  ? 11.887  45.519  58.553  1.00 16.42 ? 697  LEU   B N     1 
ATOM   14208 C  CA    . LEU   B 1  699  ? 13.222  46.094  58.407  1.00 15.85 ? 697  LEU   B CA    1 
ATOM   14209 C  C     . LEU   B 1  699  ? 13.968  45.464  57.239  1.00 16.40 ? 697  LEU   B C     1 
ATOM   14210 O  O     . LEU   B 1  699  ? 14.677  46.157  56.502  1.00 19.50 ? 697  LEU   B O     1 
ATOM   14211 C  CB    . LEU   B 1  699  ? 14.024  45.869  59.684  1.00 16.51 ? 697  LEU   B CB    1 
ATOM   14212 C  CG    . LEU   B 1  699  ? 13.451  46.452  60.978  1.00 19.03 ? 697  LEU   B CG    1 
ATOM   14213 C  CD1   . LEU   B 1  699  ? 14.321  46.089  62.176  1.00 19.84 ? 697  LEU   B CD1   1 
ATOM   14214 C  CD2   . LEU   B 1  699  ? 13.304  47.957  60.853  1.00 24.21 ? 697  LEU   B CD2   1 
ATOM   14215 N  N     . GLY   B 1  700  ? 13.837  44.152  57.068  1.00 16.01 ? 698  GLY   B N     1 
ATOM   14216 C  CA    . GLY   B 1  700  ? 14.702  43.400  56.193  1.00 16.25 ? 698  GLY   B CA    1 
ATOM   14217 C  C     . GLY   B 1  700  ? 15.365  42.275  56.964  1.00 15.52 ? 698  GLY   B C     1 
ATOM   14218 O  O     . GLY   B 1  700  ? 14.904  41.893  58.038  1.00 15.64 ? 698  GLY   B O     1 
ATOM   14219 N  N     . PRO   B 1  701  ? 16.472  41.744  56.457  1.00 15.89 ? 699  PRO   B N     1 
ATOM   14220 C  CA    . PRO   B 1  701  ? 17.128  40.621  57.143  1.00 14.99 ? 699  PRO   B CA    1 
ATOM   14221 C  C     . PRO   B 1  701  ? 17.527  41.002  58.560  1.00 14.74 ? 699  PRO   B C     1 
ATOM   14222 O  O     . PRO   B 1  701  ? 18.175  42.023  58.787  1.00 16.49 ? 699  PRO   B O     1 
ATOM   14223 C  CB    . PRO   B 1  701  ? 18.362  40.347  56.278  1.00 15.81 ? 699  PRO   B CB    1 
ATOM   14224 C  CG    . PRO   B 1  701  ? 17.985  40.882  54.925  1.00 18.05 ? 699  PRO   B CG    1 
ATOM   14225 C  CD    . PRO   B 1  701  ? 17.176  42.109  55.215  1.00 16.46 ? 699  PRO   B CD    1 
ATOM   14226 N  N     . ILE   B 1  702  ? 17.110  40.184  59.518  1.00 14.85 ? 700  ILE   B N     1 
ATOM   14227 C  CA    A ILE   B 1  702  ? 17.434  40.400  60.920  0.71 14.65 ? 700  ILE   B CA    1 
ATOM   14228 C  CA    B ILE   B 1  702  ? 17.416  40.392  60.928  0.29 14.64 ? 700  ILE   B CA    1 
ATOM   14229 C  C     . ILE   B 1  702  ? 18.345  39.279  61.374  1.00 15.18 ? 700  ILE   B C     1 
ATOM   14230 O  O     . ILE   B 1  702  ? 18.073  38.099  61.124  1.00 14.79 ? 700  ILE   B O     1 
ATOM   14231 C  CB    A ILE   B 1  702  ? 16.171  40.481  61.786  0.71 13.73 ? 700  ILE   B CB    1 
ATOM   14232 C  CB    B ILE   B 1  702  ? 16.142  40.400  61.787  0.29 13.77 ? 700  ILE   B CB    1 
ATOM   14233 C  CG1   A ILE   B 1  702  ? 15.479  41.812  61.521  0.71 15.28 ? 700  ILE   B CG1   1 
ATOM   14234 C  CG1   B ILE   B 1  702  ? 15.191  41.489  61.303  0.29 14.76 ? 700  ILE   B CG1   1 
ATOM   14235 C  CG2   A ILE   B 1  702  ? 16.536  40.316  63.266  0.71 15.19 ? 700  ILE   B CG2   1 
ATOM   14236 C  CG2   B ILE   B 1  702  ? 16.496  40.605  63.257  0.29 15.10 ? 700  ILE   B CG2   1 
ATOM   14237 C  CD1   A ILE   B 1  702  ? 14.204  41.988  62.295  0.71 15.20 ? 700  ILE   B CD1   1 
ATOM   14238 C  CD1   B ILE   B 1  702  ? 15.769  42.865  61.361  0.29 15.55 ? 700  ILE   B CD1   1 
ATOM   14239 N  N     . VAL   B 1  703  ? 19.430  39.652  62.021  1.00 13.95 ? 701  VAL   B N     1 
ATOM   14240 C  CA    . VAL   B 1  703  ? 20.350  38.692  62.598  1.00 13.33 ? 701  VAL   B CA    1 
ATOM   14241 C  C     . VAL   B 1  703  ? 19.928  38.480  64.041  1.00 14.67 ? 701  VAL   B C     1 
ATOM   14242 O  O     . VAL   B 1  703  ? 19.849  39.437  64.814  1.00 14.74 ? 701  VAL   B O     1 
ATOM   14243 C  CB    . VAL   B 1  703  ? 21.781  39.231  62.510  1.00 13.78 ? 701  VAL   B CB    1 
ATOM   14244 C  CG1   . VAL   B 1  703  ? 22.728  38.376  63.309  1.00 15.75 ? 701  VAL   B CG1   1 
ATOM   14245 C  CG2   . VAL   B 1  703  ? 22.220  39.273  61.052  1.00 15.89 ? 701  VAL   B CG2   1 
ATOM   14246 N  N     . CYS   B 1  704  ? 19.656  37.232  64.403  1.00 13.56 ? 702  CYS   B N     1 
ATOM   14247 C  CA    . CYS   B 1  704  ? 19.228  36.898  65.751  1.00 13.37 ? 702  CYS   B CA    1 
ATOM   14248 C  C     . CYS   B 1  704  ? 20.341  36.101  66.396  1.00 14.13 ? 702  CYS   B C     1 
ATOM   14249 O  O     . CYS   B 1  704  ? 20.667  35.003  65.937  1.00 14.16 ? 702  CYS   B O     1 
ATOM   14250 C  CB    . CYS   B 1  704  ? 17.944  36.077  65.728  1.00 13.80 ? 702  CYS   B CB    1 
ATOM   14251 S  SG    . CYS   B 1  704  ? 16.560  36.962  65.025  1.00 14.95 ? 702  CYS   B SG    1 
ATOM   14252 N  N     . ILE   B 1  705  ? 20.927  36.664  67.450  1.00 13.10 ? 703  ILE   B N     1 
ATOM   14253 C  CA    . ILE   B 1  705  ? 22.057  36.061  68.131  1.00 14.63 ? 703  ILE   B CA    1 
ATOM   14254 C  C     . ILE   B 1  705  ? 21.610  35.787  69.553  1.00 13.93 ? 703  ILE   B C     1 
ATOM   14255 O  O     . ILE   B 1  705  ? 21.113  36.692  70.230  1.00 14.22 ? 703  ILE   B O     1 
ATOM   14256 C  CB    . ILE   B 1  705  ? 23.273  36.998  68.101  1.00 13.80 ? 703  ILE   B CB    1 
ATOM   14257 C  CG1   . ILE   B 1  705  ? 23.816  37.094  66.675  1.00 14.43 ? 703  ILE   B CG1   1 
ATOM   14258 C  CG2   . ILE   B 1  705  ? 24.316  36.501  69.068  1.00 14.23 ? 703  ILE   B CG2   1 
ATOM   14259 C  CD1   . ILE   B 1  705  ? 24.793  38.243  66.473  1.00 16.59 ? 703  ILE   B CD1   1 
ATOM   14260 N  N     . SER   B 1  706  ? 21.751  34.544  69.987  1.00 14.19 ? 704  SER   B N     1 
ATOM   14261 C  CA    . SER   B 1  706  ? 21.116  34.088  71.209  1.00 16.05 ? 704  SER   B CA    1 
ATOM   14262 C  C     . SER   B 1  706  ? 22.126  33.454  72.149  1.00 13.78 ? 704  SER   B C     1 
ATOM   14263 O  O     . SER   B 1  706  ? 23.215  33.036  71.733  1.00 15.25 ? 704  SER   B O     1 
ATOM   14264 C  CB    . SER   B 1  706  ? 19.997  33.097  70.859  1.00 15.28 ? 704  SER   B CB    1 
ATOM   14265 O  OG    . SER   B 1  706  ? 20.497  32.052  70.041  1.00 14.72 ? 704  SER   B OG    1 
ATOM   14266 N  N     . PRO   B 1  707  ? 21.804  33.406  73.430  1.00 14.12 ? 705  PRO   B N     1 
ATOM   14267 C  CA    . PRO   B 1  707  ? 22.719  32.878  74.439  1.00 15.32 ? 705  PRO   B CA    1 
ATOM   14268 C  C     . PRO   B 1  707  ? 22.503  31.379  74.592  1.00 15.17 ? 705  PRO   B C     1 
ATOM   14269 O  O     . PRO   B 1  707  ? 21.507  30.815  74.136  1.00 16.53 ? 705  PRO   B O     1 
ATOM   14270 C  CB    . PRO   B 1  707  ? 22.244  33.609  75.704  1.00 16.70 ? 705  PRO   B CB    1 
ATOM   14271 C  CG    . PRO   B 1  707  ? 20.763  33.708  75.511  1.00 16.69 ? 705  PRO   B CG    1 
ATOM   14272 C  CD    . PRO   B 1  707  ? 20.585  33.981  74.032  1.00 15.89 ? 705  PRO   B CD    1 
ATOM   14273 N  N     . TRP   B 1  708  ? 23.455  30.739  75.258  1.00 14.22 ? 706  TRP   B N     1 
ATOM   14274 C  CA    . TRP   B 1  708  ? 23.340  29.297  75.413  1.00 14.63 ? 706  TRP   B CA    1 
ATOM   14275 C  C     . TRP   B 1  708  ? 22.331  28.902  76.476  1.00 15.19 ? 706  TRP   B C     1 
ATOM   14276 O  O     . TRP   B 1  708  ? 21.823  27.785  76.433  1.00 15.83 ? 706  TRP   B O     1 
ATOM   14277 C  CB    . TRP   B 1  708  ? 24.696  28.648  75.745  1.00 14.67 ? 706  TRP   B CB    1 
ATOM   14278 C  CG    . TRP   B 1  708  ? 25.092  28.895  77.161  1.00 14.81 ? 706  TRP   B CG    1 
ATOM   14279 C  CD1   . TRP   B 1  708  ? 25.870  29.907  77.626  1.00 18.37 ? 706  TRP   B CD1   1 
ATOM   14280 C  CD2   . TRP   B 1  708  ? 24.668  28.144  78.309  1.00 16.17 ? 706  TRP   B CD2   1 
ATOM   14281 N  NE1   . TRP   B 1  708  ? 25.950  29.843  78.997  1.00 16.79 ? 706  TRP   B NE1   1 
ATOM   14282 C  CE2   . TRP   B 1  708  ? 25.222  28.765  79.436  1.00 15.95 ? 706  TRP   B CE2   1 
ATOM   14283 C  CE3   . TRP   B 1  708  ? 23.880  27.000  78.485  1.00 17.55 ? 706  TRP   B CE3   1 
ATOM   14284 C  CZ2   . TRP   B 1  708  ? 25.020  28.282  80.724  1.00 15.73 ? 706  TRP   B CZ2   1 
ATOM   14285 C  CZ3   . TRP   B 1  708  ? 23.660  26.527  79.766  1.00 16.36 ? 706  TRP   B CZ3   1 
ATOM   14286 C  CH2   . TRP   B 1  708  ? 24.234  27.164  80.871  1.00 17.46 ? 706  TRP   B CH2   1 
ATOM   14287 N  N     . ASN   B 1  709  ? 22.043  29.781  77.438  1.00 14.75 ? 707  ASN   B N     1 
ATOM   14288 C  CA    . ASN   B 1  709  ? 21.480  29.308  78.697  1.00 14.98 ? 707  ASN   B CA    1 
ATOM   14289 C  C     . ASN   B 1  709  ? 19.984  29.099  78.644  1.00 16.18 ? 707  ASN   B C     1 
ATOM   14290 O  O     . ASN   B 1  709  ? 19.453  28.342  79.462  1.00 18.28 ? 707  ASN   B O     1 
ATOM   14291 C  CB    . ASN   B 1  709  ? 21.842  30.253  79.835  1.00 16.40 ? 707  ASN   B CB    1 
ATOM   14292 C  CG    . ASN   B 1  709  ? 21.101  31.559  79.743  1.00 17.29 ? 707  ASN   B CG    1 
ATOM   14293 O  OD1   . ASN   B 1  709  ? 21.344  32.353  78.842  1.00 19.45 ? 707  ASN   B OD1   1 
ATOM   14294 N  ND2   . ASN   B 1  709  ? 20.170  31.781  80.661  1.00 18.20 ? 707  ASN   B ND2   1 
ATOM   14295 N  N     . PHE   B 1  710  ? 19.296  29.753  77.711  1.00 15.27 ? 708  PHE   B N     1 
ATOM   14296 C  CA    . PHE   B 1  710  ? 17.904  29.464  77.388  1.00 15.88 ? 708  PHE   B CA    1 
ATOM   14297 C  C     . PHE   B 1  710  ? 17.952  29.100  75.912  1.00 16.53 ? 708  PHE   B C     1 
ATOM   14298 O  O     . PHE   B 1  710  ? 17.561  29.893  75.042  1.00 16.05 ? 708  PHE   B O     1 
ATOM   14299 C  CB    . PHE   B 1  710  ? 17.003  30.670  77.643  1.00 16.05 ? 708  PHE   B CB    1 
ATOM   14300 C  CG    . PHE   B 1  710  ? 16.940  31.099  79.093  1.00 18.22 ? 708  PHE   B CG    1 
ATOM   14301 C  CD1   . PHE   B 1  710  ? 16.884  30.162  80.112  1.00 18.79 ? 708  PHE   B CD1   1 
ATOM   14302 C  CD2   . PHE   B 1  710  ? 16.929  32.441  79.429  1.00 17.80 ? 708  PHE   B CD2   1 
ATOM   14303 C  CE1   . PHE   B 1  710  ? 16.814  30.554  81.439  1.00 22.35 ? 708  PHE   B CE1   1 
ATOM   14304 C  CE2   . PHE   B 1  710  ? 16.858  32.843  80.753  1.00 19.31 ? 708  PHE   B CE2   1 
ATOM   14305 C  CZ    . PHE   B 1  710  ? 16.797  31.894  81.761  1.00 21.76 ? 708  PHE   B CZ    1 
ATOM   14306 N  N     . PRO   B 1  711  ? 18.445  27.902  75.594  1.00 16.83 ? 709  PRO   B N     1 
ATOM   14307 C  CA    . PRO   B 1  711  ? 18.883  27.606  74.227  1.00 17.41 ? 709  PRO   B CA    1 
ATOM   14308 C  C     . PRO   B 1  711  ? 17.758  27.380  73.235  1.00 14.93 ? 709  PRO   B C     1 
ATOM   14309 O  O     . PRO   B 1  711  ? 18.021  27.369  72.026  1.00 15.43 ? 709  PRO   B O     1 
ATOM   14310 C  CB    . PRO   B 1  711  ? 19.706  26.327  74.412  1.00 16.28 ? 709  PRO   B CB    1 
ATOM   14311 C  CG    . PRO   B 1  711  ? 19.035  25.643  75.583  1.00 17.79 ? 709  PRO   B CG    1 
ATOM   14312 C  CD    . PRO   B 1  711  ? 18.717  26.783  76.519  1.00 17.07 ? 709  PRO   B CD    1 
ATOM   14313 N  N     . LEU   B 1  712  ? 16.538  27.156  73.696  1.00 15.09 ? 710  LEU   B N     1 
ATOM   14314 C  CA    . LEU   B 1  712  ? 15.387  27.112  72.813  1.00 14.68 ? 710  LEU   B CA    1 
ATOM   14315 C  C     . LEU   B 1  712  ? 14.473  28.304  72.997  1.00 14.99 ? 710  LEU   B C     1 
ATOM   14316 O  O     . LEU   B 1  712  ? 13.962  28.836  72.012  1.00 16.30 ? 710  LEU   B O     1 
ATOM   14317 C  CB    . LEU   B 1  712  ? 14.587  25.819  73.017  1.00 15.41 ? 710  LEU   B CB    1 
ATOM   14318 C  CG    . LEU   B 1  712  ? 13.408  25.650  72.051  1.00 13.50 ? 710  LEU   B CG    1 
ATOM   14319 C  CD1   . LEU   B 1  712  ? 13.879  25.549  70.603  1.00 14.88 ? 710  LEU   B CD1   1 
ATOM   14320 C  CD2   . LEU   B 1  712  ? 12.574  24.433  72.418  1.00 17.85 ? 710  LEU   B CD2   1 
ATOM   14321 N  N     . ALA   B 1  713  ? 14.273  28.766  74.231  1.00 14.60 ? 711  ALA   B N     1 
ATOM   14322 C  CA    . ALA   B 1  713  ? 13.251  29.780  74.466  1.00 14.49 ? 711  ALA   B CA    1 
ATOM   14323 C  C     . ALA   B 1  713  ? 13.641  31.133  73.888  1.00 15.88 ? 711  ALA   B C     1 
ATOM   14324 O  O     . ALA   B 1  713  ? 12.894  31.716  73.096  1.00 15.76 ? 711  ALA   B O     1 
ATOM   14325 C  CB    . ALA   B 1  713  ? 12.946  29.886  75.960  1.00 17.16 ? 711  ALA   B CB    1 
ATOM   14326 N  N     . ILE   B 1  714  ? 14.790  31.673  74.289  1.00 15.52 ? 712  ILE   B N     1 
ATOM   14327 C  CA    . ILE   B 1  714  ? 15.186  32.971  73.748  1.00 16.42 ? 712  ILE   B CA    1 
ATOM   14328 C  C     . ILE   B 1  714  ? 15.499  32.855  72.269  1.00 16.12 ? 712  ILE   B C     1 
ATOM   14329 O  O     . ILE   B 1  714  ? 15.156  33.737  71.473  1.00 14.93 ? 712  ILE   B O     1 
ATOM   14330 C  CB    . ILE   B 1  714  ? 16.341  33.562  74.568  1.00 15.26 ? 712  ILE   B CB    1 
ATOM   14331 C  CG1   . ILE   B 1  714  ? 15.743  33.985  75.908  1.00 18.22 ? 712  ILE   B CG1   1 
ATOM   14332 C  CG2   . ILE   B 1  714  ? 16.975  34.739  73.842  1.00 15.90 ? 712  ILE   B CG2   1 
ATOM   14333 C  CD1   . ILE   B 1  714  ? 16.662  34.746  76.778  1.00 24.85 ? 712  ILE   B CD1   1 
ATOM   14334 N  N     . PHE   B 1  715  ? 16.130  31.753  71.881  1.00 14.26 ? 713  PHE   B N     1 
ATOM   14335 C  CA    . PHE   B 1  715  ? 16.392  31.488  70.475  1.00 14.39 ? 713  PHE   B CA    1 
ATOM   14336 C  C     . PHE   B 1  715  ? 15.113  31.617  69.668  1.00 14.84 ? 713  PHE   B C     1 
ATOM   14337 O  O     . PHE   B 1  715  ? 15.053  32.367  68.683  1.00 14.46 ? 713  PHE   B O     1 
ATOM   14338 C  CB    . PHE   B 1  715  ? 16.958  30.077  70.339  1.00 16.07 ? 713  PHE   B CB    1 
ATOM   14339 C  CG    . PHE   B 1  715  ? 17.197  29.670  68.925  1.00 14.58 ? 713  PHE   B CG    1 
ATOM   14340 C  CD1   . PHE   B 1  715  ? 18.319  30.111  68.265  1.00 14.18 ? 713  PHE   B CD1   1 
ATOM   14341 C  CD2   . PHE   B 1  715  ? 16.293  28.854  68.249  1.00 15.03 ? 713  PHE   B CD2   1 
ATOM   14342 C  CE1   . PHE   B 1  715  ? 18.550  29.746  66.954  1.00 15.24 ? 713  PHE   B CE1   1 
ATOM   14343 C  CE2   . PHE   B 1  715  ? 16.511  28.492  66.936  1.00 14.68 ? 713  PHE   B CE2   1 
ATOM   14344 C  CZ    . PHE   B 1  715  ? 17.650  28.929  66.292  1.00 14.69 ? 713  PHE   B CZ    1 
ATOM   14345 N  N     . THR   B 1  716  ? 14.065  30.905  70.095  1.00 13.98 ? 714  THR   B N     1 
ATOM   14346 C  CA    . THR   B 1  716  ? 12.806  30.906  69.358  1.00 14.29 ? 714  THR   B CA    1 
ATOM   14347 C  C     . THR   B 1  716  ? 12.114  32.255  69.449  1.00 13.58 ? 714  THR   B C     1 
ATOM   14348 O  O     . THR   B 1  716  ? 11.539  32.729  68.465  1.00 14.36 ? 714  THR   B O     1 
ATOM   14349 C  CB    . THR   B 1  716  ? 11.886  29.827  69.925  1.00 13.73 ? 714  THR   B CB    1 
ATOM   14350 O  OG1   . THR   B 1  716  ? 12.481  28.543  69.743  1.00 16.47 ? 714  THR   B OG1   1 
ATOM   14351 C  CG2   . THR   B 1  716  ? 10.527  29.857  69.218  1.00 16.02 ? 714  THR   B CG2   1 
ATOM   14352 N  N     . GLY   B 1  717  ? 12.152  32.885  70.622  1.00 14.11 ? 715  GLY   B N     1 
ATOM   14353 C  CA    . GLY   B 1  717  ? 11.459  34.157  70.786  1.00 13.47 ? 715  GLY   B CA    1 
ATOM   14354 C  C     . GLY   B 1  717  ? 11.957  35.226  69.830  1.00 13.40 ? 715  GLY   B C     1 
ATOM   14355 O  O     . GLY   B 1  717  ? 11.164  35.891  69.154  1.00 13.58 ? 715  GLY   B O     1 
ATOM   14356 N  N     . GLN   B 1  718  ? 13.279  35.393  69.737  1.00 13.58 ? 716  GLN   B N     1 
ATOM   14357 C  CA    . GLN   B 1  718  ? 13.798  36.438  68.859  1.00 13.29 ? 716  GLN   B CA    1 
ATOM   14358 C  C     . GLN   B 1  718  ? 13.446  36.137  67.411  1.00 13.04 ? 716  GLN   B C     1 
ATOM   14359 O  O     . GLN   B 1  718  ? 12.978  37.007  66.676  1.00 13.34 ? 716  GLN   B O     1 
ATOM   14360 C  CB    . GLN   B 1  718  ? 15.313  36.568  69.001  1.00 13.87 ? 716  GLN   B CB    1 
ATOM   14361 C  CG    . GLN   B 1  718  ? 15.746  36.974  70.405  1.00 13.32 ? 716  GLN   B CG    1 
ATOM   14362 C  CD    . GLN   B 1  718  ? 17.226  37.244  70.518  1.00 15.11 ? 716  GLN   B CD    1 
ATOM   14363 O  OE1   . GLN   B 1  718  ? 17.632  38.233  71.135  1.00 16.01 ? 716  GLN   B OE1   1 
ATOM   14364 N  NE2   . GLN   B 1  718  ? 18.052  36.373  69.924  1.00 15.28 ? 716  GLN   B NE2   1 
ATOM   14365 N  N     . ILE   B 1  719  ? 13.646  34.891  67.005  1.00 13.69 ? 717  ILE   B N     1 
ATOM   14366 C  CA    . ILE   B 1  719  ? 13.398  34.513  65.620  1.00 13.98 ? 717  ILE   B CA    1 
ATOM   14367 C  C     . ILE   B 1  719  ? 11.927  34.673  65.284  1.00 14.17 ? 717  ILE   B C     1 
ATOM   14368 O  O     . ILE   B 1  719  ? 11.563  35.187  64.221  1.00 14.32 ? 717  ILE   B O     1 
ATOM   14369 C  CB    . ILE   B 1  719  ? 13.865  33.072  65.396  1.00 15.14 ? 717  ILE   B CB    1 
ATOM   14370 C  CG1   . ILE   B 1  719  ? 15.379  33.024  65.457  1.00 15.00 ? 717  ILE   B CG1   1 
ATOM   14371 C  CG2   . ILE   B 1  719  ? 13.381  32.549  64.066  1.00 21.10 ? 717  ILE   B CG2   1 
ATOM   14372 C  CD1   . ILE   B 1  719  ? 15.843  31.611  65.593  1.00 21.45 ? 717  ILE   B CD1   1 
ATOM   14373 N  N     . ALA   B 1  720  ? 11.065  34.204  66.178  1.00 13.64 ? 718  ALA   B N     1 
ATOM   14374 C  CA    . ALA   B 1  720  ? 9.640   34.230  65.913  1.00 13.24 ? 718  ALA   B CA    1 
ATOM   14375 C  C     . ALA   B 1  720  ? 9.160   35.656  65.743  1.00 14.22 ? 718  ALA   B C     1 
ATOM   14376 O  O     . ALA   B 1  720  ? 8.368   35.955  64.837  1.00 14.08 ? 718  ALA   B O     1 
ATOM   14377 C  CB    . ALA   B 1  720  ? 8.899   33.559  67.067  1.00 15.82 ? 718  ALA   B CB    1 
ATOM   14378 N  N     . ALA   B 1  721  ? 9.636   36.555  66.606  1.00 13.95 ? 719  ALA   B N     1 
ATOM   14379 C  CA    . ALA   B 1  721  ? 9.223   37.947  66.511  1.00 14.30 ? 719  ALA   B CA    1 
ATOM   14380 C  C     . ALA   B 1  721  ? 9.695   38.555  65.206  1.00 13.24 ? 719  ALA   B C     1 
ATOM   14381 O  O     . ALA   B 1  721  ? 8.939   39.245  64.517  1.00 13.83 ? 719  ALA   B O     1 
ATOM   14382 C  CB    . ALA   B 1  721  ? 9.779   38.724  67.706  1.00 13.99 ? 719  ALA   B CB    1 
ATOM   14383 N  N     . ALA   B 1  722  ? 10.956  38.322  64.857  1.00 12.76 ? 720  ALA   B N     1 
ATOM   14384 C  CA    . ALA   B 1  722  ? 11.474  38.897  63.621  1.00 12.58 ? 720  ALA   B CA    1 
ATOM   14385 C  C     . ALA   B 1  722  ? 10.704  38.370  62.420  1.00 13.81 ? 720  ALA   B C     1 
ATOM   14386 O  O     . ALA   B 1  722  ? 10.289  39.145  61.552  1.00 13.80 ? 720  ALA   B O     1 
ATOM   14387 C  CB    . ALA   B 1  722  ? 12.966  38.604  63.511  1.00 13.45 ? 720  ALA   B CB    1 
ATOM   14388 N  N     . LEU   B 1  723  ? 10.458  37.058  62.392  1.00 13.74 ? 721  LEU   B N     1 
ATOM   14389 C  CA    . LEU   B 1  723  ? 9.750   36.451  61.267  1.00 13.38 ? 721  LEU   B CA    1 
ATOM   14390 C  C     . LEU   B 1  723  ? 8.344   36.987  61.158  1.00 14.65 ? 721  LEU   B C     1 
ATOM   14391 O  O     . LEU   B 1  723  ? 7.878   37.329  60.066  1.00 15.12 ? 721  LEU   B O     1 
ATOM   14392 C  CB    . LEU   B 1  723  ? 9.673   34.943  61.454  1.00 14.38 ? 721  LEU   B CB    1 
ATOM   14393 C  CG    . LEU   B 1  723  ? 10.966  34.178  61.226  1.00 13.94 ? 721  LEU   B CG    1 
ATOM   14394 C  CD1   . LEU   B 1  723  ? 10.761  32.746  61.646  1.00 14.65 ? 721  LEU   B CD1   1 
ATOM   14395 C  CD2   . LEU   B 1  723  ? 11.409  34.261  59.768  1.00 15.19 ? 721  LEU   B CD2   1 
ATOM   14396 N  N     . VAL   B 1  724  ? 7.634   37.040  62.280  1.00 13.91 ? 722  VAL   B N     1 
ATOM   14397 C  CA    . VAL   B 1  724  ? 6.231   37.398  62.182  1.00 13.42 ? 722  VAL   B CA    1 
ATOM   14398 C  C     . VAL   B 1  724  ? 6.074   38.870  61.840  1.00 13.84 ? 722  VAL   B C     1 
ATOM   14399 O  O     . VAL   B 1  724  ? 5.087   39.266  61.209  1.00 14.59 ? 722  VAL   B O     1 
ATOM   14400 C  CB    . VAL   B 1  724  ? 5.472   36.964  63.450  1.00 13.47 ? 722  VAL   B CB    1 
ATOM   14401 C  CG1   . VAL   B 1  724  ? 5.655   37.961  64.593  1.00 15.10 ? 722  VAL   B CG1   1 
ATOM   14402 C  CG2   . VAL   B 1  724  ? 4.006   36.737  63.115  1.00 14.26 ? 722  VAL   B CG2   1 
ATOM   14403 N  N     . ALA   B 1  725  ? 7.064   39.689  62.187  1.00 14.88 ? 723  ALA   B N     1 
ATOM   14404 C  CA    . ALA   B 1  725  ? 7.089   41.074  61.739  1.00 13.78 ? 723  ALA   B CA    1 
ATOM   14405 C  C     . ALA   B 1  725  ? 7.436   41.202  60.262  1.00 15.80 ? 723  ALA   B C     1 
ATOM   14406 O  O     . ALA   B 1  725  ? 7.444   42.325  59.750  1.00 18.17 ? 723  ALA   B O     1 
ATOM   14407 C  CB    . ALA   B 1  725  ? 8.064   41.891  62.596  1.00 15.83 ? 723  ALA   B CB    1 
ATOM   14408 N  N     . GLY   B 1  726  ? 7.703   40.100  59.566  1.00 14.52 ? 724  GLY   B N     1 
ATOM   14409 C  CA    . GLY   B 1  726  ? 7.915   40.147  58.137  1.00 15.69 ? 724  GLY   B CA    1 
ATOM   14410 C  C     . GLY   B 1  726  ? 9.359   40.159  57.706  1.00 15.94 ? 724  GLY   B C     1 
ATOM   14411 O  O     . GLY   B 1  726  ? 9.631   40.450  56.535  1.00 17.59 ? 724  GLY   B O     1 
ATOM   14412 N  N     . ASN   B 1  727  ? 10.288  39.855  58.601  1.00 15.16 ? 725  ASN   B N     1 
ATOM   14413 C  CA    . ASN   B 1  727  ? 11.706  39.909  58.305  1.00 14.85 ? 725  ASN   B CA    1 
ATOM   14414 C  C     . ASN   B 1  727  ? 12.253  38.508  58.133  1.00 14.22 ? 725  ASN   B C     1 
ATOM   14415 O  O     . ASN   B 1  727  ? 11.976  37.645  58.973  1.00 16.09 ? 725  ASN   B O     1 
ATOM   14416 C  CB    . ASN   B 1  727  ? 12.443  40.559  59.469  1.00 15.09 ? 725  ASN   B CB    1 
ATOM   14417 C  CG    . ASN   B 1  727  ? 11.883  41.909  59.841  1.00 16.71 ? 725  ASN   B CG    1 
ATOM   14418 O  OD1   . ASN   B 1  727  ? 12.158  42.908  59.183  1.00 16.42 ? 725  ASN   B OD1   1 
ATOM   14419 N  ND2   . ASN   B 1  727  ? 11.114  41.953  60.918  1.00 14.81 ? 725  ASN   B ND2   1 
ATOM   14420 N  N     . PRO   B 1  728  ? 13.055  38.243  57.108  1.00 13.88 ? 726  PRO   B N     1 
ATOM   14421 C  CA    . PRO   B 1  728  ? 13.790  36.984  57.080  1.00 14.66 ? 726  PRO   B CA    1 
ATOM   14422 C  C     . PRO   B 1  728  ? 14.865  37.037  58.140  1.00 15.90 ? 726  PRO   B C     1 
ATOM   14423 O  O     . PRO   B 1  728  ? 15.347  38.111  58.508  1.00 15.45 ? 726  PRO   B O     1 
ATOM   14424 C  CB    . PRO   B 1  728  ? 14.400  36.966  55.676  1.00 16.71 ? 726  PRO   B CB    1 
ATOM   14425 C  CG    . PRO   B 1  728  ? 14.600  38.425  55.356  1.00 16.85 ? 726  PRO   B CG    1 
ATOM   14426 C  CD    . PRO   B 1  728  ? 13.464  39.167  56.039  1.00 16.54 ? 726  PRO   B CD    1 
ATOM   14427 N  N     . VAL   B 1  729  ? 15.218  35.865  58.648  1.00 13.77 ? 727  VAL   B N     1 
ATOM   14428 C  CA    . VAL   B 1  729  ? 16.054  35.766  59.836  1.00 13.79 ? 727  VAL   B CA    1 
ATOM   14429 C  C     . VAL   B 1  729  ? 17.296  34.944  59.549  1.00 15.74 ? 727  VAL   B C     1 
ATOM   14430 O  O     . VAL   B 1  729  ? 17.234  33.890  58.899  1.00 15.03 ? 727  VAL   B O     1 
ATOM   14431 C  CB    . VAL   B 1  729  ? 15.269  35.130  60.993  1.00 15.03 ? 727  VAL   B CB    1 
ATOM   14432 C  CG1   . VAL   B 1  729  ? 16.236  34.670  62.098  1.00 15.64 ? 727  VAL   B CG1   1 
ATOM   14433 C  CG2   . VAL   B 1  729  ? 14.255  36.112  61.537  1.00 14.36 ? 727  VAL   B CG2   1 
ATOM   14434 N  N     . LEU   B 1  730  ? 18.428  35.432  60.053  1.00 14.07 ? 728  LEU   B N     1 
ATOM   14435 C  CA    . LEU   B 1  730  ? 19.661  34.674  60.146  1.00 14.12 ? 728  LEU   B CA    1 
ATOM   14436 C  C     . LEU   B 1  730  ? 19.823  34.321  61.615  1.00 13.36 ? 728  LEU   B C     1 
ATOM   14437 O  O     . LEU   B 1  730  ? 20.054  35.206  62.444  1.00 14.88 ? 728  LEU   B O     1 
ATOM   14438 C  CB    . LEU   B 1  730  ? 20.837  35.528  59.689  1.00 15.57 ? 728  LEU   B CB    1 
ATOM   14439 C  CG    . LEU   B 1  730  ? 20.881  36.017  58.242  1.00 15.78 ? 728  LEU   B CG    1 
ATOM   14440 C  CD1   . LEU   B 1  730  ? 20.526  34.895  57.273  1.00 17.25 ? 728  LEU   B CD1   1 
ATOM   14441 C  CD2   . LEU   B 1  730  ? 19.989  37.231  58.006  1.00 16.61 ? 728  LEU   B CD2   1 
ATOM   14442 N  N     . ALA   B 1  731  ? 19.701  33.044  61.939  1.00 13.49 ? 729  ALA   B N     1 
ATOM   14443 C  CA    . ALA   B 1  731  ? 19.684  32.608  63.329  1.00 12.70 ? 729  ALA   B CA    1 
ATOM   14444 C  C     . ALA   B 1  731  ? 21.062  32.070  63.683  1.00 15.43 ? 729  ALA   B C     1 
ATOM   14445 O  O     . ALA   B 1  731  ? 21.511  31.079  63.103  1.00 15.07 ? 729  ALA   B O     1 
ATOM   14446 C  CB    . ALA   B 1  731  ? 18.608  31.543  63.528  1.00 16.48 ? 729  ALA   B CB    1 
ATOM   14447 N  N     . LYS   B 1  732  ? 21.728  32.728  64.632  1.00 14.27 ? 730  LYS   B N     1 
ATOM   14448 C  CA    . LYS   B 1  732  ? 23.072  32.364  65.061  1.00 14.53 ? 730  LYS   B CA    1 
ATOM   14449 C  C     . LYS   B 1  732  ? 22.977  31.941  66.519  1.00 13.57 ? 730  LYS   B C     1 
ATOM   14450 O  O     . LYS   B 1  732  ? 23.020  32.788  67.430  1.00 14.86 ? 730  LYS   B O     1 
ATOM   14451 C  CB    . LYS   B 1  732  ? 24.039  33.533  64.875  1.00 14.96 ? 730  LYS   B CB    1 
ATOM   14452 C  CG    . LYS   B 1  732  ? 25.476  33.112  64.550  1.00 15.00 ? 730  LYS   B CG    1 
ATOM   14453 C  CD    . LYS   B 1  732  ? 26.079  32.211  65.625  1.00 15.27 ? 730  LYS   B CD    1 
ATOM   14454 C  CE    . LYS   B 1  732  ? 26.444  32.997  66.857  1.00 14.99 ? 730  LYS   B CE    1 
ATOM   14455 N  NZ    . LYS   B 1  732  ? 26.984  32.062  67.872  1.00 15.56 ? 730  LYS   B NZ    1 
ATOM   14456 N  N     . PRO   B 1  733  ? 22.836  30.653  66.783  1.00 13.05 ? 731  PRO   B N     1 
ATOM   14457 C  CA    . PRO   B 1  733  ? 22.714  30.186  68.165  1.00 14.69 ? 731  PRO   B CA    1 
ATOM   14458 C  C     . PRO   B 1  733  ? 24.079  30.145  68.819  1.00 13.52 ? 731  PRO   B C     1 
ATOM   14459 O  O     . PRO   B 1  733  ? 25.121  30.112  68.164  1.00 14.98 ? 731  PRO   B O     1 
ATOM   14460 C  CB    . PRO   B 1  733  ? 22.189  28.761  67.998  1.00 16.20 ? 731  PRO   B CB    1 
ATOM   14461 C  CG    . PRO   B 1  733  ? 22.810  28.311  66.698  1.00 15.74 ? 731  PRO   B CG    1 
ATOM   14462 C  CD    . PRO   B 1  733  ? 22.775  29.549  65.809  1.00 15.78 ? 731  PRO   B CD    1 
ATOM   14463 N  N     . ALA   B 1  734  ? 24.052  30.146  70.141  1.00 14.35 ? 732  ALA   B N     1 
ATOM   14464 C  CA    . ALA   B 1  734  ? 25.289  30.081  70.902  1.00 14.84 ? 732  ALA   B CA    1 
ATOM   14465 C  C     . ALA   B 1  734  ? 26.065  28.820  70.542  1.00 15.35 ? 732  ALA   B C     1 
ATOM   14466 O  O     . ALA   B 1  734  ? 25.493  27.770  70.239  1.00 16.08 ? 732  ALA   B O     1 
ATOM   14467 C  CB    . ALA   B 1  734  ? 24.965  30.084  72.395  1.00 15.59 ? 732  ALA   B CB    1 
ATOM   14468 N  N     . GLU   B 1  735  ? 27.387  28.932  70.570  1.00 15.44 ? 733  GLU   B N     1 
ATOM   14469 C  CA    . GLU   B 1  735  ? 28.207  27.804  70.154  1.00 16.42 ? 733  GLU   B CA    1 
ATOM   14470 C  C     . GLU   B 1  735  ? 28.026  26.602  71.069  1.00 16.62 ? 733  GLU   B C     1 
ATOM   14471 O  O     . GLU   B 1  735  ? 28.214  25.465  70.638  1.00 16.90 ? 733  GLU   B O     1 
ATOM   14472 C  CB    . GLU   B 1  735  ? 29.681  28.203  70.054  1.00 16.96 ? 733  GLU   B CB    1 
ATOM   14473 C  CG    . GLU   B 1  735  ? 30.275  28.810  71.312  1.00 22.09 ? 733  GLU   B CG    1 
ATOM   14474 C  CD    . GLU   B 1  735  ? 30.156  30.329  71.360  1.00 22.47 ? 733  GLU   B CD    1 
ATOM   14475 O  OE1   . GLU   B 1  735  ? 29.194  30.902  70.795  1.00 20.84 ? 733  GLU   B OE1   1 
ATOM   14476 O  OE2   . GLU   B 1  735  ? 31.042  30.969  71.974  1.00 23.54 ? 733  GLU   B OE2   1 
ATOM   14477 N  N     . GLU   B 1  736  ? 27.628  26.832  72.321  1.00 15.48 ? 734  GLU   B N     1 
ATOM   14478 C  CA    . GLU   B 1  736  ? 27.488  25.721  73.251  1.00 16.17 ? 734  GLU   B CA    1 
ATOM   14479 C  C     . GLU   B 1  736  ? 26.262  24.863  72.957  1.00 15.23 ? 734  GLU   B C     1 
ATOM   14480 O  O     . GLU   B 1  736  ? 26.252  23.672  73.293  1.00 18.75 ? 734  GLU   B O     1 
ATOM   14481 C  CB    . GLU   B 1  736  ? 27.401  26.250  74.677  1.00 16.48 ? 734  GLU   B CB    1 
ATOM   14482 C  CG    . GLU   B 1  736  ? 28.639  26.974  75.169  1.00 18.95 ? 734  GLU   B CG    1 
ATOM   14483 C  CD    . GLU   B 1  736  ? 28.628  28.479  74.931  1.00 21.49 ? 734  GLU   B CD    1 
ATOM   14484 O  OE1   . GLU   B 1  736  ? 27.862  28.981  74.085  1.00 17.44 ? 734  GLU   B OE1   1 
ATOM   14485 O  OE2   . GLU   B 1  736  ? 29.395  29.182  75.617  1.00 24.12 ? 734  GLU   B OE2   1 
ATOM   14486 N  N     . THR   B 1  737  ? 25.213  25.437  72.365  1.00 15.45 ? 735  THR   B N     1 
ATOM   14487 C  CA    . THR   B 1  737  ? 23.903  24.775  72.299  1.00 15.44 ? 735  THR   B CA    1 
ATOM   14488 C  C     . THR   B 1  737  ? 23.300  24.836  70.902  1.00 15.93 ? 735  THR   B C     1 
ATOM   14489 O  O     . THR   B 1  737  ? 22.166  25.279  70.718  1.00 16.90 ? 735  THR   B O     1 
ATOM   14490 C  CB    . THR   B 1  737  ? 22.945  25.366  73.334  1.00 16.05 ? 735  THR   B CB    1 
ATOM   14491 O  OG1   . THR   B 1  737  ? 22.892  26.788  73.168  1.00 16.22 ? 735  THR   B OG1   1 
ATOM   14492 C  CG2   . THR   B 1  737  ? 23.421  25.032  74.748  1.00 17.59 ? 735  THR   B CG2   1 
ATOM   14493 N  N     . PRO   B 1  738  ? 24.023  24.362  69.889  1.00 15.12 ? 736  PRO   B N     1 
ATOM   14494 C  CA    . PRO   B 1  738  ? 23.487  24.422  68.520  1.00 14.36 ? 736  PRO   B CA    1 
ATOM   14495 C  C     . PRO   B 1  738  ? 22.422  23.389  68.218  1.00 16.63 ? 736  PRO   B C     1 
ATOM   14496 O  O     . PRO   B 1  738  ? 21.646  23.606  67.281  1.00 15.81 ? 736  PRO   B O     1 
ATOM   14497 C  CB    . PRO   B 1  738  ? 24.721  24.146  67.659  1.00 14.90 ? 736  PRO   B CB    1 
ATOM   14498 C  CG    . PRO   B 1  738  ? 25.506  23.179  68.515  1.00 16.38 ? 736  PRO   B CG    1 
ATOM   14499 C  CD    . PRO   B 1  738  ? 25.353  23.728  69.927  1.00 14.96 ? 736  PRO   B CD    1 
ATOM   14500 N  N     . LEU   B 1  739  ? 22.372  22.270  68.940  1.00 14.28 ? 737  LEU   B N     1 
ATOM   14501 C  CA    . LEU   B 1  739  ? 21.487  21.184  68.520  1.00 14.11 ? 737  LEU   B CA    1 
ATOM   14502 C  C     . LEU   B 1  739  ? 20.024  21.538  68.728  1.00 14.86 ? 737  LEU   B C     1 
ATOM   14503 O  O     . LEU   B 1  739  ? 19.191  21.323  67.838  1.00 15.45 ? 737  LEU   B O     1 
ATOM   14504 C  CB    . LEU   B 1  739  ? 21.839  19.892  69.244  1.00 15.76 ? 737  LEU   B CB    1 
ATOM   14505 C  CG    . LEU   B 1  739  ? 23.272  19.415  69.033  1.00 16.37 ? 737  LEU   B CG    1 
ATOM   14506 C  CD1   . LEU   B 1  739  ? 23.496  18.195  69.911  1.00 17.61 ? 737  LEU   B CD1   1 
ATOM   14507 C  CD2   . LEU   B 1  739  ? 23.555  19.123  67.558  1.00 16.54 ? 737  LEU   B CD2   1 
ATOM   14508 N  N     . ILE   B 1  740  ? 19.683  22.062  69.905  1.00 15.64 ? 738  ILE   B N     1 
ATOM   14509 C  CA    . ILE   B 1  740  ? 18.281  22.398  70.126  1.00 13.79 ? 738  ILE   B CA    1 
ATOM   14510 C  C     . ILE   B 1  740  ? 17.872  23.553  69.224  1.00 14.06 ? 738  ILE   B C     1 
ATOM   14511 O  O     . ILE   B 1  740  ? 16.710  23.635  68.801  1.00 16.03 ? 738  ILE   B O     1 
ATOM   14512 C  CB    . ILE   B 1  740  ? 17.979  22.636  71.620  1.00 17.68 ? 738  ILE   B CB    1 
ATOM   14513 C  CG1   . ILE   B 1  740  ? 16.475  22.781  71.852  1.00 16.41 ? 738  ILE   B CG1   1 
ATOM   14514 C  CG2   . ILE   B 1  740  ? 18.698  23.863  72.096  1.00 18.60 ? 738  ILE   B CG2   1 
ATOM   14515 C  CD1   . ILE   B 1  740  ? 15.683  21.538  71.534  1.00 17.77 ? 738  ILE   B CD1   1 
ATOM   14516 N  N     . ALA   B 1  741  ? 18.814  24.446  68.896  1.00 13.96 ? 739  ALA   B N     1 
ATOM   14517 C  CA    . ALA   B 1  741  ? 18.501  25.540  67.981  1.00 13.35 ? 739  ALA   B CA    1 
ATOM   14518 C  C     . ALA   B 1  741  ? 18.194  24.998  66.598  1.00 14.84 ? 739  ALA   B C     1 
ATOM   14519 O  O     . ALA   B 1  741  ? 17.236  25.436  65.951  1.00 15.06 ? 739  ALA   B O     1 
ATOM   14520 C  CB    . ALA   B 1  741  ? 19.673  26.515  67.914  1.00 17.13 ? 739  ALA   B CB    1 
ATOM   14521 N  N     . ALA   B 1  742  ? 18.986  24.029  66.142  1.00 14.35 ? 740  ALA   B N     1 
ATOM   14522 C  CA    . ALA   B 1  742  ? 18.720  23.413  64.852  1.00 14.54 ? 740  ALA   B CA    1 
ATOM   14523 C  C     . ALA   B 1  742  ? 17.345  22.775  64.845  1.00 15.84 ? 740  ALA   B C     1 
ATOM   14524 O  O     . ALA   B 1  742  ? 16.614  22.857  63.850  1.00 16.14 ? 740  ALA   B O     1 
ATOM   14525 C  CB    . ALA   B 1  742  ? 19.784  22.361  64.549  1.00 15.49 ? 740  ALA   B CB    1 
ATOM   14526 N  N     . GLU   B 1  743  ? 16.959  22.165  65.965  1.00 15.69 ? 741  GLU   B N     1 
ATOM   14527 C  CA    . GLU   B 1  743  ? 15.644  21.540  66.036  1.00 14.34 ? 741  GLU   B CA    1 
ATOM   14528 C  C     . GLU   B 1  743  ? 14.546  22.588  66.010  1.00 15.60 ? 741  GLU   B C     1 
ATOM   14529 O  O     . GLU   B 1  743  ? 13.513  22.398  65.352  1.00 16.50 ? 741  GLU   B O     1 
ATOM   14530 C  CB    . GLU   B 1  743  ? 15.568  20.684  67.293  1.00 16.54 ? 741  GLU   B CB    1 
ATOM   14531 C  CG    . GLU   B 1  743  ? 14.248  20.003  67.473  1.00 17.99 ? 741  GLU   B CG    1 
ATOM   14532 C  CD    . GLU   B 1  743  ? 13.939  18.952  66.419  1.00 19.35 ? 741  GLU   B CD    1 
ATOM   14533 O  OE1   . GLU   B 1  743  ? 14.809  18.592  65.589  1.00 19.07 ? 741  GLU   B OE1   1 
ATOM   14534 O  OE2   . GLU   B 1  743  ? 12.781  18.477  66.425  1.00 21.51 ? 741  GLU   B OE2   1 
ATOM   14535 N  N     . GLY   B 1  744  ? 14.764  23.719  66.691  1.00 15.66 ? 742  GLY   B N     1 
ATOM   14536 C  CA    . GLY   B 1  744  ? 13.825  24.823  66.587  1.00 15.59 ? 742  GLY   B CA    1 
ATOM   14537 C  C     . GLY   B 1  744  ? 13.647  25.284  65.152  1.00 15.43 ? 742  GLY   B C     1 
ATOM   14538 O  O     . GLY   B 1  744  ? 12.529  25.549  64.711  1.00 15.13 ? 742  GLY   B O     1 
ATOM   14539 N  N     . VAL   B 1  745  ? 14.747  25.390  64.404  1.00 14.60 ? 743  VAL   B N     1 
ATOM   14540 C  CA    . VAL   B 1  745  ? 14.637  25.813  63.010  1.00 14.09 ? 743  VAL   B CA    1 
ATOM   14541 C  C     . VAL   B 1  745  ? 13.921  24.755  62.187  1.00 16.55 ? 743  VAL   B C     1 
ATOM   14542 O  O     . VAL   B 1  745  ? 13.077  25.085  61.345  1.00 15.97 ? 743  VAL   B O     1 
ATOM   14543 C  CB    . VAL   B 1  745  ? 16.012  26.199  62.437  1.00 15.28 ? 743  VAL   B CB    1 
ATOM   14544 C  CG1   . VAL   B 1  745  ? 15.945  26.343  60.908  1.00 15.96 ? 743  VAL   B CG1   1 
ATOM   14545 C  CG2   . VAL   B 1  745  ? 16.460  27.503  63.058  1.00 15.85 ? 743  VAL   B CG2   1 
ATOM   14546 N  N     . ARG   B 1  746  ? 14.215  23.471  62.431  1.00 14.69 ? 744  ARG   B N     1 
ATOM   14547 C  CA    . ARG   B 1  746  ? 13.472  22.415  61.739  1.00 15.27 ? 744  ARG   B CA    1 
ATOM   14548 C  C     . ARG   B 1  746  ? 11.976  22.568  61.960  1.00 14.55 ? 744  ARG   B C     1 
ATOM   14549 O  O     . ARG   B 1  746  ? 11.180  22.414  61.029  1.00 15.97 ? 744  ARG   B O     1 
ATOM   14550 C  CB    . ARG   B 1  746  ? 13.876  21.043  62.271  1.00 16.79 ? 744  ARG   B CB    1 
ATOM   14551 C  CG    . ARG   B 1  746  ? 15.251  20.573  61.872  1.00 18.07 ? 744  ARG   B CG    1 
ATOM   14552 C  CD    . ARG   B 1  746  ? 15.454  19.151  62.379  1.00 16.49 ? 744  ARG   B CD    1 
ATOM   14553 N  NE    . ARG   B 1  746  ? 16.848  18.769  62.245  1.00 20.03 ? 744  ARG   B NE    1 
ATOM   14554 C  CZ    . ARG   B 1  746  ? 17.763  18.869  63.197  1.00 17.63 ? 744  ARG   B CZ    1 
ATOM   14555 N  NH1   . ARG   B 1  746  ? 17.432  19.082  64.462  1.00 18.26 ? 744  ARG   B NH1   1 
ATOM   14556 N  NH2   . ARG   B 1  746  ? 19.048  18.782  62.864  1.00 18.97 ? 744  ARG   B NH2   1 
ATOM   14557 N  N     . ILE   B 1  747  ? 11.578  22.862  63.193  1.00 14.16 ? 745  ILE   B N     1 
ATOM   14558 C  CA    . ILE   B 1  747  ? 10.160  22.944  63.508  1.00 14.80 ? 745  ILE   B CA    1 
ATOM   14559 C  C     . ILE   B 1  747  ? 9.531   24.168  62.859  1.00 15.31 ? 745  ILE   B C     1 
ATOM   14560 O  O     . ILE   B 1  747  ? 8.435   24.088  62.288  1.00 13.85 ? 745  ILE   B O     1 
ATOM   14561 C  CB    . ILE   B 1  747  ? 9.961   22.921  65.029  1.00 14.71 ? 745  ILE   B CB    1 
ATOM   14562 C  CG1   . ILE   B 1  747  ? 10.187  21.506  65.538  1.00 15.69 ? 745  ILE   B CG1   1 
ATOM   14563 C  CG2   . ILE   B 1  747  ? 8.564   23.375  65.374  1.00 15.00 ? 745  ILE   B CG2   1 
ATOM   14564 C  CD1   . ILE   B 1  747  ? 10.357  21.431  67.027  1.00 17.75 ? 745  ILE   B CD1   1 
ATOM   14565 N  N     . LEU   B 1  748  ? 10.212  25.315  62.913  1.00 13.95 ? 746  LEU   B N     1 
ATOM   14566 C  CA    . LEU   B 1  748  ? 9.668   26.504  62.263  1.00 14.50 ? 746  LEU   B CA    1 
ATOM   14567 C  C     . LEU   B 1  748  ? 9.541   26.302  60.765  1.00 14.28 ? 746  LEU   B C     1 
ATOM   14568 O  O     . LEU   B 1  748  ? 8.565   26.741  60.160  1.00 15.24 ? 746  LEU   B O     1 
ATOM   14569 C  CB    . LEU   B 1  748  ? 10.522  27.730  62.565  1.00 14.87 ? 746  LEU   B CB    1 
ATOM   14570 C  CG    . LEU   B 1  748  ? 10.177  28.352  63.916  1.00 18.81 ? 746  LEU   B CG    1 
ATOM   14571 C  CD1   . LEU   B 1  748  ? 11.346  29.208  64.408  1.00 19.51 ? 746  LEU   B CD1   1 
ATOM   14572 C  CD2   . LEU   B 1  748  ? 8.927   29.173  63.764  1.00 20.72 ? 746  LEU   B CD2   1 
ATOM   14573 N  N     . ARG   B 1  749  ? 10.530  25.664  60.142  1.00 14.86 ? 747  ARG   B N     1 
ATOM   14574 C  CA    . ARG   B 1  749  ? 10.408  25.392  58.715  1.00 14.65 ? 747  ARG   B CA    1 
ATOM   14575 C  C     . ARG   B 1  749  ? 9.269   24.420  58.440  1.00 14.31 ? 747  ARG   B C     1 
ATOM   14576 O  O     . ARG   B 1  749  ? 8.506   24.603  57.478  1.00 14.90 ? 747  ARG   B O     1 
ATOM   14577 C  CB    . ARG   B 1  749  ? 11.730  24.853  58.180  1.00 15.32 ? 747  ARG   B CB    1 
ATOM   14578 C  CG    . ARG   B 1  749  ? 12.804  25.912  58.051  1.00 16.39 ? 747  ARG   B CG    1 
ATOM   14579 C  CD    . ARG   B 1  749  ? 14.011  25.328  57.368  1.00 18.50 ? 747  ARG   B CD    1 
ATOM   14580 N  NE    . ARG   B 1  749  ? 15.002  26.340  57.037  1.00 17.17 ? 747  ARG   B NE    1 
ATOM   14581 C  CZ    . ARG   B 1  749  ? 16.069  26.086  56.294  1.00 23.89 ? 747  ARG   B CZ    1 
ATOM   14582 N  NH1   . ARG   B 1  749  ? 16.250  24.897  55.736  1.00 25.05 ? 747  ARG   B NH1   1 
ATOM   14583 N  NH2   . ARG   B 1  749  ? 16.972  27.043  56.105  1.00 24.35 ? 747  ARG   B NH2   1 
ATOM   14584 N  N     . GLU   B 1  750  ? 9.142   23.375  59.266  1.00 14.32 ? 748  GLU   B N     1 
ATOM   14585 C  CA    . GLU   B 1  750  ? 8.048   22.433  59.071  1.00 15.02 ? 748  GLU   B CA    1 
ATOM   14586 C  C     . GLU   B 1  750  ? 6.704   23.129  59.202  1.00 13.85 ? 748  GLU   B C     1 
ATOM   14587 O  O     . GLU   B 1  750  ? 5.752   22.796  58.485  1.00 16.38 ? 748  GLU   B O     1 
ATOM   14588 C  CB    . GLU   B 1  750  ? 8.164   21.300  60.089  1.00 16.73 ? 748  GLU   B CB    1 
ATOM   14589 C  CG    . GLU   B 1  750  ? 7.104   20.242  59.914  1.00 17.21 ? 748  GLU   B CG    1 
ATOM   14590 C  CD    . GLU   B 1  750  ? 7.300   19.075  60.860  1.00 19.36 ? 748  GLU   B CD    1 
ATOM   14591 O  OE1   . GLU   B 1  750  ? 8.384   18.985  61.471  1.00 20.38 ? 748  GLU   B OE1   1 
ATOM   14592 O  OE2   . GLU   B 1  750  ? 6.371   18.246  60.968  1.00 25.17 ? 748  GLU   B OE2   1 
ATOM   14593 N  N     . ALA   B 1  751  ? 6.629   24.135  60.064  1.00 15.05 ? 749  ALA   B N     1 
ATOM   14594 C  CA    . ALA   B 1  751  ? 5.404   24.879  60.287  1.00 15.00 ? 749  ALA   B CA    1 
ATOM   14595 C  C     . ALA   B 1  751  ? 5.094   25.876  59.186  1.00 15.44 ? 749  ALA   B C     1 
ATOM   14596 O  O     . ALA   B 1  751  ? 4.036   26.509  59.233  1.00 17.46 ? 749  ALA   B O     1 
ATOM   14597 C  CB    . ALA   B 1  751  ? 5.532   25.639  61.600  1.00 14.83 ? 749  ALA   B CB    1 
ATOM   14598 N  N     . GLY   B 1  752  ? 5.981   26.053  58.214  1.00 15.20 ? 750  GLY   B N     1 
ATOM   14599 C  CA    . GLY   B 1  752  ? 5.690   26.901  57.074  1.00 15.85 ? 750  GLY   B CA    1 
ATOM   14600 C  C     . GLY   B 1  752  ? 6.657   28.040  56.851  1.00 16.49 ? 750  GLY   B C     1 
ATOM   14601 O  O     . GLY   B 1  752  ? 6.482   28.784  55.881  1.00 18.02 ? 750  GLY   B O     1 
ATOM   14602 N  N     . ILE   B 1  753  ? 7.664   28.253  57.694  1.00 16.09 ? 751  ILE   B N     1 
ATOM   14603 C  CA    . ILE   B 1  753  ? 8.611   29.330  57.435  1.00 16.89 ? 751  ILE   B CA    1 
ATOM   14604 C  C     . ILE   B 1  753  ? 9.514   28.884  56.293  1.00 17.33 ? 751  ILE   B C     1 
ATOM   14605 O  O     . ILE   B 1  753  ? 10.164  27.840  56.399  1.00 17.97 ? 751  ILE   B O     1 
ATOM   14606 C  CB    . ILE   B 1  753  ? 9.445   29.638  58.685  1.00 14.13 ? 751  ILE   B CB    1 
ATOM   14607 C  CG1   . ILE   B 1  753  ? 8.548   29.982  59.879  1.00 17.59 ? 751  ILE   B CG1   1 
ATOM   14608 C  CG2   . ILE   B 1  753  ? 10.404  30.780  58.378  1.00 16.77 ? 751  ILE   B CG2   1 
ATOM   14609 C  CD1   . ILE   B 1  753  ? 7.708   31.256  59.665  1.00 17.34 ? 751  ILE   B CD1   1 
ATOM   14610 N  N     . PRO   B 1  754  ? 9.572   29.624  55.189  1.00 16.65 ? 752  PRO   B N     1 
ATOM   14611 C  CA    . PRO   B 1  754  ? 10.393  29.189  54.055  1.00 17.13 ? 752  PRO   B CA    1 
ATOM   14612 C  C     . PRO   B 1  754  ? 11.864  29.149  54.420  1.00 18.05 ? 752  PRO   B C     1 
ATOM   14613 O  O     . PRO   B 1  754  ? 12.342  29.904  55.267  1.00 17.06 ? 752  PRO   B O     1 
ATOM   14614 C  CB    . PRO   B 1  754  ? 10.132  30.257  52.986  1.00 19.34 ? 752  PRO   B CB    1 
ATOM   14615 C  CG    . PRO   B 1  754  ? 8.895   30.971  53.420  1.00 22.61 ? 752  PRO   B CG    1 
ATOM   14616 C  CD    . PRO   B 1  754  ? 8.781   30.828  54.900  1.00 16.62 ? 752  PRO   B CD    1 
ATOM   14617 N  N     . ALA   B 1  755  ? 12.593  28.255  53.755  1.00 19.98 ? 753  ALA   B N     1 
ATOM   14618 C  CA    . ALA   B 1  755  ? 14.014  28.143  54.043  1.00 20.73 ? 753  ALA   B CA    1 
ATOM   14619 C  C     . ALA   B 1  755  ? 14.735  29.461  53.809  1.00 17.24 ? 753  ALA   B C     1 
ATOM   14620 O  O     . ALA   B 1  755  ? 15.675  29.793  54.534  1.00 20.57 ? 753  ALA   B O     1 
ATOM   14621 C  CB    . ALA   B 1  755  ? 14.640  27.020  53.216  1.00 23.93 ? 753  ALA   B CB    1 
ATOM   14622 N  N     . SER   B 1  756  ? 14.285  30.254  52.838  1.00 17.16 ? 754  SER   B N     1 
ATOM   14623 C  CA    . SER   B 1  756  ? 14.962  31.519  52.599  1.00 18.02 ? 754  SER   B CA    1 
ATOM   14624 C  C     . SER   B 1  756  ? 14.646  32.540  53.677  1.00 16.89 ? 754  SER   B C     1 
ATOM   14625 O  O     . SER   B 1  756  ? 15.383  33.520  53.824  1.00 18.64 ? 754  SER   B O     1 
ATOM   14626 C  CB    . SER   B 1  756  ? 14.566  32.068  51.237  1.00 22.22 ? 754  SER   B CB    1 
ATOM   14627 O  OG    . SER   B 1  756  ? 13.168  32.269  51.198  1.00 23.81 ? 754  SER   B OG    1 
ATOM   14628 N  N     . ALA   B 1  757  ? 13.560  32.341  54.420  1.00 14.77 ? 755  ALA   B N     1 
ATOM   14629 C  CA    . ALA   B 1  757  ? 13.207  33.246  55.492  1.00 15.10 ? 755  ALA   B CA    1 
ATOM   14630 C  C     . ALA   B 1  757  ? 13.853  32.878  56.815  1.00 15.04 ? 755  ALA   B C     1 
ATOM   14631 O  O     . ALA   B 1  757  ? 13.833  33.693  57.737  1.00 16.13 ? 755  ALA   B O     1 
ATOM   14632 C  CB    . ALA   B 1  757  ? 11.687  33.286  55.660  1.00 15.74 ? 755  ALA   B CB    1 
ATOM   14633 N  N     . LEU   B 1  758  ? 14.404  31.679  56.947  1.00 15.23 ? 756  LEU   B N     1 
ATOM   14634 C  CA    . LEU   B 1  758  ? 14.963  31.279  58.235  1.00 15.20 ? 756  LEU   B CA    1 
ATOM   14635 C  C     . LEU   B 1  758  ? 16.149  30.372  57.965  1.00 13.95 ? 756  LEU   B C     1 
ATOM   14636 O  O     . LEU   B 1  758  ? 15.979  29.200  57.614  1.00 17.23 ? 756  LEU   B O     1 
ATOM   14637 C  CB    . LEU   B 1  758  ? 13.934  30.572  59.099  1.00 14.25 ? 756  LEU   B CB    1 
ATOM   14638 C  CG    . LEU   B 1  758  ? 14.511  30.044  60.412  1.00 14.49 ? 756  LEU   B CG    1 
ATOM   14639 C  CD1   . LEU   B 1  758  ? 15.086  31.172  61.263  1.00 16.10 ? 756  LEU   B CD1   1 
ATOM   14640 C  CD2   . LEU   B 1  758  ? 13.407  29.323  61.164  1.00 16.25 ? 756  LEU   B CD2   1 
ATOM   14641 N  N     . GLN   B 1  759  ? 17.335  30.921  58.146  1.00 13.97 ? 757  GLN   B N     1 
ATOM   14642 C  CA    . GLN   B 1  759  ? 18.575  30.197  57.940  1.00 14.29 ? 757  GLN   B CA    1 
ATOM   14643 C  C     . GLN   B 1  759  ? 19.277  30.071  59.278  1.00 15.14 ? 757  GLN   B C     1 
ATOM   14644 O  O     . GLN   B 1  759  ? 19.269  31.009  60.082  1.00 16.51 ? 757  GLN   B O     1 
ATOM   14645 C  CB    . GLN   B 1  759  ? 19.455  30.942  56.944  1.00 14.56 ? 757  GLN   B CB    1 
ATOM   14646 C  CG    . GLN   B 1  759  ? 18.851  30.945  55.542  1.00 14.96 ? 757  GLN   B CG    1 
ATOM   14647 C  CD    . GLN   B 1  759  ? 19.634  31.801  54.602  1.00 16.01 ? 757  GLN   B CD    1 
ATOM   14648 O  OE1   . GLN   B 1  759  ? 20.479  31.310  53.852  1.00 18.47 ? 757  GLN   B OE1   1 
ATOM   14649 N  NE2   . GLN   B 1  759  ? 19.378  33.099  54.639  1.00 15.83 ? 757  GLN   B NE2   1 
ATOM   14650 N  N     . LEU   B 1  760  ? 19.861  28.908  59.519  1.00 14.06 ? 758  LEU   B N     1 
ATOM   14651 C  CA    . LEU   B 1  760  ? 20.574  28.625  60.756  1.00 14.05 ? 758  LEU   B CA    1 
ATOM   14652 C  C     . LEU   B 1  760  ? 22.067  28.657  60.480  1.00 16.13 ? 758  LEU   B C     1 
ATOM   14653 O  O     . LEU   B 1  760  ? 22.548  27.957  59.586  1.00 15.73 ? 758  LEU   B O     1 
ATOM   14654 C  CB    . LEU   B 1  760  ? 20.221  27.228  61.253  1.00 15.92 ? 758  LEU   B CB    1 
ATOM   14655 C  CG    . LEU   B 1  760  ? 20.918  26.854  62.564  1.00 15.14 ? 758  LEU   B CG    1 
ATOM   14656 C  CD1   . LEU   B 1  760  ? 20.231  27.531  63.750  1.00 17.22 ? 758  LEU   B CD1   1 
ATOM   14657 C  CD2   . LEU   B 1  760  ? 20.955  25.337  62.724  1.00 19.03 ? 758  LEU   B CD2   1 
ATOM   14658 N  N     . LEU   B 1  761  ? 22.805  29.449  61.253  1.00 16.51 ? 759  LEU   B N     1 
ATOM   14659 C  CA    . LEU   B 1  761  ? 24.247  29.587  61.076  1.00 14.83 ? 759  LEU   B CA    1 
ATOM   14660 C  C     . LEU   B 1  761  ? 24.924  29.246  62.396  1.00 15.08 ? 759  LEU   B C     1 
ATOM   14661 O  O     . LEU   B 1  761  ? 25.219  30.145  63.202  1.00 16.81 ? 759  LEU   B O     1 
ATOM   14662 C  CB    . LEU   B 1  761  ? 24.638  30.996  60.635  1.00 16.81 ? 759  LEU   B CB    1 
ATOM   14663 C  CG    . LEU   B 1  761  ? 24.113  31.544  59.299  1.00 18.19 ? 759  LEU   B CG    1 
ATOM   14664 C  CD1   . LEU   B 1  761  ? 24.170  30.498  58.184  1.00 20.08 ? 759  LEU   B CD1   1 
ATOM   14665 C  CD2   . LEU   B 1  761  ? 22.722  32.112  59.432  1.00 21.25 ? 759  LEU   B CD2   1 
ATOM   14666 N  N     . PRO   B 1  762  ? 25.182  27.971  62.660  1.00 15.26 ? 760  PRO   B N     1 
ATOM   14667 C  CA    . PRO   B 1  762  ? 25.882  27.621  63.900  1.00 15.02 ? 760  PRO   B CA    1 
ATOM   14668 C  C     . PRO   B 1  762  ? 27.300  28.139  63.862  1.00 15.46 ? 760  PRO   B C     1 
ATOM   14669 O  O     . PRO   B 1  762  ? 27.906  28.300  62.796  1.00 16.45 ? 760  PRO   B O     1 
ATOM   14670 C  CB    . PRO   B 1  762  ? 25.884  26.089  63.897  1.00 15.02 ? 760  PRO   B CB    1 
ATOM   14671 C  CG    . PRO   B 1  762  ? 24.803  25.700  62.915  1.00 16.73 ? 760  PRO   B CG    1 
ATOM   14672 C  CD    . PRO   B 1  762  ? 24.825  26.782  61.872  1.00 15.87 ? 760  PRO   B CD    1 
ATOM   14673 N  N     . GLY   B 1  763  ? 27.843  28.351  65.044  1.00 15.91 ? 761  GLY   B N     1 
ATOM   14674 C  CA    . GLY   B 1  763  ? 29.234  28.728  65.167  1.00 16.45 ? 761  GLY   B CA    1 
ATOM   14675 C  C     . GLY   B 1  763  ? 29.417  29.657  66.344  1.00 14.54 ? 761  GLY   B C     1 
ATOM   14676 O  O     . GLY   B 1  763  ? 28.499  29.887  67.132  1.00 16.44 ? 761  GLY   B O     1 
ATOM   14677 N  N     . ASP   B 1  764  ? 30.632  30.176  66.455  1.00 17.46 ? 762  ASP   B N     1 
ATOM   14678 C  CA    . ASP   B 1  764  ? 30.982  30.972  67.622  1.00 17.96 ? 762  ASP   B CA    1 
ATOM   14679 C  C     . ASP   B 1  764  ? 30.731  32.454  67.340  1.00 19.12 ? 762  ASP   B C     1 
ATOM   14680 O  O     . ASP   B 1  764  ? 30.007  32.818  66.405  1.00 17.93 ? 762  ASP   B O     1 
ATOM   14681 C  CB    . ASP   B 1  764  ? 32.388  30.602  68.110  1.00 21.55 ? 762  ASP   B CB    1 
ATOM   14682 C  CG    . ASP   B 1  764  ? 33.487  31.046  67.159  1.00 25.72 ? 762  ASP   B CG    1 
ATOM   14683 O  OD1   . ASP   B 1  764  ? 33.243  31.849  66.236  1.00 21.37 ? 762  ASP   B OD1   1 
ATOM   14684 O  OD2   . ASP   B 1  764  ? 34.631  30.581  67.344  1.00 32.00 ? 762  ASP   B OD2   1 
ATOM   14685 N  N     . GLY   B 1  765  ? 31.317  33.332  68.159  1.00 18.33 ? 763  GLY   B N     1 
ATOM   14686 C  CA    . GLY   B 1  765  ? 31.058  34.751  68.017  1.00 18.30 ? 763  GLY   B CA    1 
ATOM   14687 C  C     . GLY   B 1  765  ? 31.535  35.334  66.710  1.00 19.25 ? 763  GLY   B C     1 
ATOM   14688 O  O     . GLY   B 1  765  ? 31.024  36.378  66.297  1.00 19.60 ? 763  GLY   B O     1 
ATOM   14689 N  N     . ARG   B 1  766  ? 32.514  34.696  66.059  1.00 18.50 ? 764  ARG   B N     1 
ATOM   14690 C  CA    . ARG   B 1  766  ? 32.962  35.178  64.756  1.00 20.73 ? 764  ARG   B CA    1 
ATOM   14691 C  C     . ARG   B 1  766  ? 31.852  35.061  63.724  1.00 16.33 ? 764  ARG   B C     1 
ATOM   14692 O  O     . ARG   B 1  766  ? 31.748  35.898  62.820  1.00 17.98 ? 764  ARG   B O     1 
ATOM   14693 C  CB    . ARG   B 1  766  ? 34.195  34.406  64.291  1.00 20.50 ? 764  ARG   B CB    1 
ATOM   14694 C  CG    . ARG   B 1  766  ? 35.402  34.557  65.198  1.00 24.81 ? 764  ARG   B CG    1 
ATOM   14695 C  CD    . ARG   B 1  766  ? 36.462  33.529  64.835  1.00 31.46 ? 764  ARG   B CD    1 
ATOM   14696 N  NE    . ARG   B 1  766  ? 35.945  32.172  64.970  1.00 36.61 ? 764  ARG   B NE    1 
ATOM   14697 C  CZ    . ARG   B 1  766  ? 36.616  31.077  64.639  1.00 42.94 ? 764  ARG   B CZ    1 
ATOM   14698 N  NH1   . ARG   B 1  766  ? 37.843  31.140  64.149  1.00 41.93 ? 764  ARG   B NH1   1 
ATOM   14699 N  NH2   . ARG   B 1  766  ? 36.040  29.889  64.802  1.00 42.62 ? 764  ARG   B NH2   1 
ATOM   14700 N  N     . VAL   B 1  767  ? 31.026  34.018  63.834  1.00 15.78 ? 765  VAL   B N     1 
ATOM   14701 C  CA    . VAL   B 1  767  ? 29.890  33.892  62.934  1.00 16.27 ? 765  VAL   B CA    1 
ATOM   14702 C  C     . VAL   B 1  767  ? 28.878  34.982  63.227  1.00 16.29 ? 765  VAL   B C     1 
ATOM   14703 O  O     . VAL   B 1  767  ? 28.355  35.624  62.309  1.00 17.91 ? 765  VAL   B O     1 
ATOM   14704 C  CB    . VAL   B 1  767  ? 29.279  32.488  63.042  1.00 15.40 ? 765  VAL   B CB    1 
ATOM   14705 C  CG1   . VAL   B 1  767  ? 28.101  32.364  62.104  1.00 16.93 ? 765  VAL   B CG1   1 
ATOM   14706 C  CG2   . VAL   B 1  767  ? 30.319  31.443  62.717  1.00 18.29 ? 765  VAL   B CG2   1 
ATOM   14707 N  N     . GLY   B 1  768  ? 28.609  35.234  64.510  1.00 15.22 ? 766  GLY   B N     1 
ATOM   14708 C  CA    . GLY   B 1  768  ? 27.728  36.336  64.852  1.00 16.59 ? 766  GLY   B CA    1 
ATOM   14709 C  C     . GLY   B 1  768  ? 28.245  37.660  64.321  1.00 16.95 ? 766  GLY   B C     1 
ATOM   14710 O  O     . GLY   B 1  768  ? 27.499  38.449  63.733  1.00 16.54 ? 766  GLY   B O     1 
ATOM   14711 N  N     . ALA   B 1  769  ? 29.545  37.915  64.506  1.00 17.66 ? 767  ALA   B N     1 
ATOM   14712 C  CA    . ALA   B 1  769  ? 30.104  39.184  64.047  1.00 17.47 ? 767  ALA   B CA    1 
ATOM   14713 C  C     . ALA   B 1  769  ? 30.010  39.313  62.531  1.00 17.62 ? 767  ALA   B C     1 
ATOM   14714 O  O     . ALA   B 1  769  ? 29.715  40.395  62.008  1.00 17.40 ? 767  ALA   B O     1 
ATOM   14715 C  CB    . ALA   B 1  769  ? 31.554  39.324  64.519  1.00 17.06 ? 767  ALA   B CB    1 
ATOM   14716 N  N     . ALA   B 1  770  ? 30.256  38.215  61.810  1.00 16.73 ? 768  ALA   B N     1 
ATOM   14717 C  CA    . ALA   B 1  770  ? 30.184  38.268  60.355  1.00 16.44 ? 768  ALA   B CA    1 
ATOM   14718 C  C     . ALA   B 1  770  ? 28.760  38.571  59.894  1.00 17.26 ? 768  ALA   B C     1 
ATOM   14719 O  O     . ALA   B 1  770  ? 28.554  39.309  58.925  1.00 18.76 ? 768  ALA   B O     1 
ATOM   14720 C  CB    . ALA   B 1  770  ? 30.672  36.951  59.759  1.00 17.30 ? 768  ALA   B CB    1 
ATOM   14721 N  N     . LEU   B 1  771  ? 27.763  38.010  60.580  1.00 16.30 ? 769  LEU   B N     1 
ATOM   14722 C  CA    . LEU   B 1  771  ? 26.385  38.310  60.222  1.00 17.25 ? 769  LEU   B CA    1 
ATOM   14723 C  C     . LEU   B 1  771  ? 26.052  39.768  60.499  1.00 16.28 ? 769  LEU   B C     1 
ATOM   14724 O  O     . LEU   B 1  771  ? 25.408  40.431  59.681  1.00 18.11 ? 769  LEU   B O     1 
ATOM   14725 C  CB    . LEU   B 1  771  ? 25.449  37.405  61.015  1.00 16.88 ? 769  LEU   B CB    1 
ATOM   14726 C  CG    . LEU   B 1  771  ? 25.511  35.933  60.610  1.00 16.03 ? 769  LEU   B CG    1 
ATOM   14727 C  CD1   . LEU   B 1  771  ? 24.696  35.103  61.588  1.00 17.15 ? 769  LEU   B CD1   1 
ATOM   14728 C  CD2   . LEU   B 1  771  ? 25.011  35.747  59.165  1.00 17.01 ? 769  LEU   B CD2   1 
ATOM   14729 N  N     . VAL   B 1  772  ? 26.466  40.276  61.660  1.00 16.20 ? 770  VAL   B N     1 
ATOM   14730 C  CA    . VAL   B 1  772  ? 26.173  41.657  62.038  1.00 16.49 ? 770  VAL   B CA    1 
ATOM   14731 C  C     . VAL   B 1  772  ? 26.772  42.633  61.039  1.00 19.90 ? 770  VAL   B C     1 
ATOM   14732 O  O     . VAL   B 1  772  ? 26.149  43.643  60.684  1.00 20.66 ? 770  VAL   B O     1 
ATOM   14733 C  CB    . VAL   B 1  772  ? 26.687  41.926  63.465  1.00 17.20 ? 770  VAL   B CB    1 
ATOM   14734 C  CG1   . VAL   B 1  772  ? 26.710  43.421  63.774  1.00 18.93 ? 770  VAL   B CG1   1 
ATOM   14735 C  CG2   . VAL   B 1  772  ? 25.863  41.161  64.475  1.00 17.09 ? 770  VAL   B CG2   1 
ATOM   14736 N  N     . ALA   B 1  773  ? 27.993  42.350  60.575  1.00 18.58 ? 771  ALA   B N     1 
ATOM   14737 C  CA    . ALA   B 1  773  ? 28.697  43.255  59.674  1.00 19.65 ? 771  ALA   B CA    1 
ATOM   14738 C  C     . ALA   B 1  773  ? 28.221  43.162  58.232  1.00 22.15 ? 771  ALA   B C     1 
ATOM   14739 O  O     . ALA   B 1  773  ? 28.580  44.026  57.424  1.00 23.42 ? 771  ALA   B O     1 
ATOM   14740 C  CB    . ALA   B 1  773  ? 30.188  42.954  59.726  1.00 20.51 ? 771  ALA   B CB    1 
ATOM   14741 N  N     . ALA   B 1  774  ? 27.431  42.147  57.893  1.00 19.19 ? 772  ALA   B N     1 
ATOM   14742 C  CA    . ALA   B 1  774  ? 27.030  41.942  56.508  1.00 18.13 ? 772  ALA   B CA    1 
ATOM   14743 C  C     . ALA   B 1  774  ? 26.217  43.125  56.001  1.00 20.66 ? 772  ALA   B C     1 
ATOM   14744 O  O     . ALA   B 1  774  ? 25.405  43.704  56.729  1.00 21.08 ? 772  ALA   B O     1 
ATOM   14745 C  CB    . ALA   B 1  774  ? 26.224  40.653  56.374  1.00 21.20 ? 772  ALA   B CB    1 
ATOM   14746 N  N     . ALA   B 1  775  ? 26.419  43.446  54.720  1.00 24.24 ? 773  ALA   B N     1 
ATOM   14747 C  CA    . ALA   B 1  775  ? 25.902  44.690  54.159  1.00 25.49 ? 773  ALA   B CA    1 
ATOM   14748 C  C     . ALA   B 1  775  ? 24.383  44.782  54.257  1.00 21.60 ? 773  ALA   B C     1 
ATOM   14749 O  O     . ALA   B 1  775  ? 23.835  45.868  54.474  1.00 23.99 ? 773  ALA   B O     1 
ATOM   14750 C  CB    . ALA   B 1  775  ? 26.350  44.811  52.703  1.00 28.87 ? 773  ALA   B CB    1 
ATOM   14751 N  N     . GLU   B 1  776  ? 23.686  43.663  54.089  1.00 21.51 ? 774  GLU   B N     1 
ATOM   14752 C  CA    . GLU   B 1  776  ? 22.234  43.676  54.003  1.00 19.60 ? 774  GLU   B CA    1 
ATOM   14753 C  C     . GLU   B 1  776  ? 21.544  43.471  55.345  1.00 16.75 ? 774  GLU   B C     1 
ATOM   14754 O  O     . GLU   B 1  776  ? 20.313  43.482  55.392  1.00 17.96 ? 774  GLU   B O     1 
ATOM   14755 C  CB    . GLU   B 1  776  ? 21.743  42.628  52.995  1.00 19.30 ? 774  GLU   B CB    1 
ATOM   14756 C  CG    . GLU   B 1  776  ? 22.322  42.775  51.587  1.00 26.79 ? 774  GLU   B CG    1 
ATOM   14757 C  CD    . GLU   B 1  776  ? 23.670  42.078  51.413  1.00 35.04 ? 774  GLU   B CD    1 
ATOM   14758 O  OE1   . GLU   B 1  776  ? 24.166  41.434  52.373  1.00 26.94 ? 774  GLU   B OE1   1 
ATOM   14759 O  OE2   . GLU   B 1  776  ? 24.245  42.184  50.307  1.00 35.37 ? 774  GLU   B OE2   1 
ATOM   14760 N  N     . THR   B 1  777  ? 22.294  43.276  56.424  1.00 16.98 ? 775  THR   B N     1 
ATOM   14761 C  CA    . THR   B 1  777  ? 21.679  43.149  57.735  1.00 15.98 ? 775  THR   B CA    1 
ATOM   14762 C  C     . THR   B 1  777  ? 20.956  44.435  58.095  1.00 16.87 ? 775  THR   B C     1 
ATOM   14763 O  O     . THR   B 1  777  ? 21.538  45.522  58.061  1.00 18.24 ? 775  THR   B O     1 
ATOM   14764 C  CB    . THR   B 1  777  ? 22.765  42.830  58.751  1.00 17.54 ? 775  THR   B CB    1 
ATOM   14765 O  OG1   . THR   B 1  777  ? 23.280  41.534  58.444  1.00 19.65 ? 775  THR   B OG1   1 
ATOM   14766 C  CG2   . THR   B 1  777  ? 22.199  42.835  60.165  1.00 17.01 ? 775  THR   B CG2   1 
ATOM   14767 N  N     . ALA   B 1  778  ? 19.664  44.308  58.410  1.00 14.35 ? 776  ALA   B N     1 
ATOM   14768 C  CA    . ALA   B 1  778  ? 18.800  45.455  58.634  1.00 15.59 ? 776  ALA   B CA    1 
ATOM   14769 C  C     . ALA   B 1  778  ? 18.400  45.612  60.089  1.00 15.13 ? 776  ALA   B C     1 
ATOM   14770 O  O     . ALA   B 1  778  ? 17.752  46.606  60.444  1.00 16.56 ? 776  ALA   B O     1 
ATOM   14771 C  CB    . ALA   B 1  778  ? 17.543  45.332  57.768  1.00 17.08 ? 776  ALA   B CB    1 
ATOM   14772 N  N     . GLY   B 1  779  ? 18.768  44.665  60.932  1.00 14.90 ? 777  GLY   B N     1 
ATOM   14773 C  CA    . GLY   B 1  779  ? 18.492  44.779  62.349  1.00 15.57 ? 777  GLY   B CA    1 
ATOM   14774 C  C     . GLY   B 1  779  ? 19.142  43.599  63.029  1.00 16.12 ? 777  GLY   B C     1 
ATOM   14775 O  O     . GLY   B 1  779  ? 19.415  42.567  62.404  1.00 15.22 ? 777  GLY   B O     1 
ATOM   14776 N  N     . VAL   B 1  780  ? 19.409  43.774  64.320  1.00 14.76 ? 778  VAL   B N     1 
ATOM   14777 C  CA    . VAL   B 1  780  ? 20.047  42.736  65.119  1.00 14.44 ? 778  VAL   B CA    1 
ATOM   14778 C  C     . VAL   B 1  780  ? 19.272  42.578  66.410  1.00 15.07 ? 778  VAL   B C     1 
ATOM   14779 O  O     . VAL   B 1  780  ? 18.947  43.574  67.074  1.00 14.99 ? 778  VAL   B O     1 
ATOM   14780 C  CB    . VAL   B 1  780  ? 21.531  43.041  65.411  1.00 14.19 ? 778  VAL   B CB    1 
ATOM   14781 C  CG1   . VAL   B 1  780  ? 22.131  41.931  66.258  1.00 16.53 ? 778  VAL   B CG1   1 
ATOM   14782 C  CG2   . VAL   B 1  780  ? 22.301  43.178  64.121  1.00 16.51 ? 778  VAL   B CG2   1 
ATOM   14783 N  N     . MET   B 1  781  ? 18.963  41.333  66.747  1.00 13.05 ? 779  MET   B N     1 
ATOM   14784 C  CA    . MET   B 1  781  ? 18.358  40.979  68.026  1.00 12.80 ? 779  MET   B CA    1 
ATOM   14785 C  C     . MET   B 1  781  ? 19.394  40.156  68.757  1.00 14.09 ? 779  MET   B C     1 
ATOM   14786 O  O     . MET   B 1  781  ? 19.789  39.083  68.290  1.00 14.72 ? 779  MET   B O     1 
ATOM   14787 C  CB    . MET   B 1  781  ? 17.072  40.183  67.824  1.00 13.27 ? 779  MET   B CB    1 
ATOM   14788 C  CG    . MET   B 1  781  ? 16.100  40.935  66.964  1.00 15.50 ? 779  MET   B CG    1 
ATOM   14789 S  SD    . MET   B 1  781  ? 14.627  40.001  66.598  1.00 15.21 ? 779  MET   B SD    1 
ATOM   14790 C  CE    . MET   B 1  781  ? 13.787  40.069  68.174  1.00 14.19 ? 779  MET   B CE    1 
ATOM   14791 N  N     . PHE   B 1  782  ? 19.906  40.702  69.845  1.00 13.81 ? 780  PHE   B N     1 
ATOM   14792 C  CA    . PHE   B 1  782  ? 20.974  40.073  70.593  1.00 14.69 ? 780  PHE   B CA    1 
ATOM   14793 C  C     . PHE   B 1  782  ? 20.528  39.857  72.024  1.00 13.49 ? 780  PHE   B C     1 
ATOM   14794 O  O     . PHE   B 1  782  ? 19.994  40.766  72.664  1.00 14.76 ? 780  PHE   B O     1 
ATOM   14795 C  CB    . PHE   B 1  782  ? 22.209  40.962  70.627  1.00 13.96 ? 780  PHE   B CB    1 
ATOM   14796 C  CG    . PHE   B 1  782  ? 23.269  40.437  71.522  1.00 13.68 ? 780  PHE   B CG    1 
ATOM   14797 C  CD1   . PHE   B 1  782  ? 24.063  39.380  71.100  1.00 15.11 ? 780  PHE   B CD1   1 
ATOM   14798 C  CD2   . PHE   B 1  782  ? 23.453  40.959  72.802  1.00 14.22 ? 780  PHE   B CD2   1 
ATOM   14799 C  CE1   . PHE   B 1  782  ? 25.041  38.865  71.907  1.00 15.15 ? 780  PHE   B CE1   1 
ATOM   14800 C  CE2   . PHE   B 1  782  ? 24.438  40.436  73.624  1.00 16.49 ? 780  PHE   B CE2   1 
ATOM   14801 C  CZ    . PHE   B 1  782  ? 25.237  39.402  73.165  1.00 15.05 ? 780  PHE   B CZ    1 
ATOM   14802 N  N     . THR   B 1  783  ? 20.766  38.659  72.524  1.00 13.36 ? 781  THR   B N     1 
ATOM   14803 C  CA    . THR   B 1  783  ? 20.636  38.397  73.945  1.00 14.34 ? 781  THR   B CA    1 
ATOM   14804 C  C     . THR   B 1  783  ? 21.904  37.681  74.368  1.00 14.66 ? 781  THR   B C     1 
ATOM   14805 O  O     . THR   B 1  783  ? 22.330  36.721  73.719  1.00 15.09 ? 781  THR   B O     1 
ATOM   14806 C  CB    . THR   B 1  783  ? 19.395  37.559  74.263  1.00 15.42 ? 781  THR   B CB    1 
ATOM   14807 O  OG1   . THR   B 1  783  ? 18.225  38.244  73.812  1.00 14.99 ? 781  THR   B OG1   1 
ATOM   14808 C  CG2   . THR   B 1  783  ? 19.276  37.373  75.777  1.00 15.01 ? 781  THR   B CG2   1 
ATOM   14809 N  N     . GLY   B 1  784  ? 22.535  38.180  75.420  1.00 14.26 ? 782  GLY   B N     1 
ATOM   14810 C  CA    . GLY   B 1  784  ? 23.842  37.681  75.788  1.00 14.42 ? 782  GLY   B CA    1 
ATOM   14811 C  C     . GLY   B 1  784  ? 24.513  38.651  76.741  1.00 15.41 ? 782  GLY   B C     1 
ATOM   14812 O  O     . GLY   B 1  784  ? 23.857  39.485  77.359  1.00 15.86 ? 782  GLY   B O     1 
ATOM   14813 N  N     . SER   B 1  785  ? 25.822  38.520  76.840  1.00 17.44 ? 783  SER   B N     1 
ATOM   14814 C  CA    . SER   B 1  785  ? 26.548  39.349  77.788  1.00 18.12 ? 783  SER   B CA    1 
ATOM   14815 C  C     . SER   B 1  785  ? 26.603  40.799  77.324  1.00 20.70 ? 783  SER   B C     1 
ATOM   14816 O  O     . SER   B 1  785  ? 26.605  41.103  76.128  1.00 18.44 ? 783  SER   B O     1 
ATOM   14817 C  CB    . SER   B 1  785  ? 27.960  38.804  77.977  1.00 18.44 ? 783  SER   B CB    1 
ATOM   14818 O  OG    . SER   B 1  785  ? 28.712  38.896  76.782  1.00 18.73 ? 783  SER   B OG    1 
ATOM   14819 N  N     . THR   B 1  786  ? 26.665  41.709  78.297  1.00 18.72 ? 784  THR   B N     1 
ATOM   14820 C  CA    . THR   B 1  786  ? 26.792  43.123  77.967  1.00 19.02 ? 784  THR   B CA    1 
ATOM   14821 C  C     . THR   B 1  786  ? 28.057  43.386  77.151  1.00 18.03 ? 784  THR   B C     1 
ATOM   14822 O  O     . THR   B 1  786  ? 28.050  44.196  76.215  1.00 20.41 ? 784  THR   B O     1 
ATOM   14823 C  CB    . THR   B 1  786  ? 26.750  43.963  79.256  1.00 18.68 ? 784  THR   B CB    1 
ATOM   14824 O  OG1   . THR   B 1  786  ? 25.597  43.596  80.025  1.00 21.65 ? 784  THR   B OG1   1 
ATOM   14825 C  CG2   . THR   B 1  786  ? 26.651  45.427  78.921  1.00 23.78 ? 784  THR   B CG2   1 
ATOM   14826 N  N     . GLU   B 1  787  ? 29.152  42.689  77.476  1.00 21.11 ? 785  GLU   B N     1 
ATOM   14827 C  CA    . GLU   B 1  787  ? 30.415  42.892  76.772  1.00 19.38 ? 785  GLU   B CA    1 
ATOM   14828 C  C     . GLU   B 1  787  ? 30.281  42.587  75.285  1.00 21.49 ? 785  GLU   B C     1 
ATOM   14829 O  O     . GLU   B 1  787  ? 30.775  43.343  74.438  1.00 20.20 ? 785  GLU   B O     1 
ATOM   14830 C  CB    . GLU   B 1  787  ? 31.499  42.009  77.398  1.00 25.64 ? 785  GLU   B CB    1 
ATOM   14831 N  N     . VAL   B 1  788  ? 29.601  41.489  74.948  1.00 17.85 ? 786  VAL   B N     1 
ATOM   14832 C  CA    . VAL   B 1  788  ? 29.420  41.149  73.541  1.00 18.19 ? 786  VAL   B CA    1 
ATOM   14833 C  C     . VAL   B 1  788  ? 28.485  42.142  72.870  1.00 16.14 ? 786  VAL   B C     1 
ATOM   14834 O  O     . VAL   B 1  788  ? 28.703  42.548  71.729  1.00 17.74 ? 786  VAL   B O     1 
ATOM   14835 C  CB    . VAL   B 1  788  ? 28.930  39.697  73.402  1.00 16.59 ? 786  VAL   B CB    1 
ATOM   14836 C  CG1   . VAL   B 1  788  ? 28.487  39.415  71.964  1.00 18.11 ? 786  VAL   B CG1   1 
ATOM   14837 C  CG2   . VAL   B 1  788  ? 30.054  38.731  73.809  1.00 19.38 ? 786  VAL   B CG2   1 
ATOM   14838 N  N     . ALA   B 1  789  ? 27.432  42.559  73.573  1.00 15.85 ? 787  ALA   B N     1 
ATOM   14839 C  CA    . ALA   B 1  789  ? 26.504  43.521  72.994  1.00 15.24 ? 787  ALA   B CA    1 
ATOM   14840 C  C     . ALA   B 1  789  ? 27.225  44.791  72.581  1.00 15.81 ? 787  ALA   B C     1 
ATOM   14841 O  O     . ALA   B 1  789  ? 26.912  45.380  71.547  1.00 17.66 ? 787  ALA   B O     1 
ATOM   14842 C  CB    . ALA   B 1  789  ? 25.384  43.856  73.975  1.00 15.77 ? 787  ALA   B CB    1 
ATOM   14843 N  N     . ARG   B 1  790  ? 28.198  45.232  73.387  1.00 16.76 ? 788  ARG   B N     1 
ATOM   14844 C  CA    . ARG   B 1  790  ? 28.929  46.446  73.031  1.00 18.42 ? 788  ARG   B CA    1 
ATOM   14845 C  C     . ARG   B 1  790  ? 29.693  46.272  71.733  1.00 19.75 ? 788  ARG   B C     1 
ATOM   14846 O  O     . ARG   B 1  790  ? 29.800  47.212  70.935  1.00 20.39 ? 788  ARG   B O     1 
ATOM   14847 C  CB    . ARG   B 1  790  ? 29.938  46.789  74.118  1.00 22.99 ? 788  ARG   B CB    1 
ATOM   14848 C  CG    . ARG   B 1  790  ? 29.351  47.328  75.355  1.00 24.59 ? 788  ARG   B CG    1 
ATOM   14849 C  CD    . ARG   B 1  790  ? 30.464  47.868  76.243  1.00 29.20 ? 788  ARG   B CD    1 
ATOM   14850 N  NE    . ARG   B 1  790  ? 29.929  48.087  77.569  1.00 38.31 ? 788  ARG   B NE    1 
ATOM   14851 C  CZ    . ARG   B 1  790  ? 29.167  49.120  77.884  1.00 37.03 ? 788  ARG   B CZ    1 
ATOM   14852 N  NH1   . ARG   B 1  790  ? 28.912  50.081  77.005  1.00 33.02 ? 788  ARG   B NH1   1 
ATOM   14853 N  NH2   . ARG   B 1  790  ? 28.647  49.190  79.105  1.00 42.16 ? 788  ARG   B NH2   1 
ATOM   14854 N  N     . LEU   B 1  791  ? 30.251  45.082  71.513  1.00 18.40 ? 789  LEU   B N     1 
ATOM   14855 C  CA    . LEU   B 1  791  ? 30.969  44.845  70.268  1.00 20.54 ? 789  LEU   B CA    1 
ATOM   14856 C  C     . LEU   B 1  791  ? 30.026  44.930  69.082  1.00 20.65 ? 789  LEU   B C     1 
ATOM   14857 O  O     . LEU   B 1  791  ? 30.359  45.519  68.051  1.00 20.95 ? 789  LEU   B O     1 
ATOM   14858 C  CB    . LEU   B 1  791  ? 31.643  43.479  70.311  1.00 21.97 ? 789  LEU   B CB    1 
ATOM   14859 C  CG    . LEU   B 1  791  ? 32.683  43.299  71.414  1.00 22.75 ? 789  LEU   B CG    1 
ATOM   14860 C  CD1   . LEU   B 1  791  ? 33.260  41.897  71.343  1.00 23.16 ? 789  LEU   B CD1   1 
ATOM   14861 C  CD2   . LEU   B 1  791  ? 33.784  44.362  71.290  1.00 23.94 ? 789  LEU   B CD2   1 
ATOM   14862 N  N     . ILE   B 1  792  ? 28.827  44.362  69.227  1.00 19.82 ? 790  ILE   B N     1 
ATOM   14863 C  CA    . ILE   B 1  792  ? 27.844  44.402  68.155  1.00 18.36 ? 790  ILE   B CA    1 
ATOM   14864 C  C     . ILE   B 1  792  ? 27.383  45.828  67.908  1.00 16.66 ? 790  ILE   B C     1 
ATOM   14865 O  O     . ILE   B 1  792  ? 27.255  46.265  66.759  1.00 19.55 ? 790  ILE   B O     1 
ATOM   14866 C  CB    . ILE   B 1  792  ? 26.674  43.484  68.530  1.00 17.17 ? 790  ILE   B CB    1 
ATOM   14867 C  CG1   . ILE   B 1  792  ? 27.135  42.030  68.509  1.00 16.54 ? 790  ILE   B CG1   1 
ATOM   14868 C  CG2   . ILE   B 1  792  ? 25.461  43.746  67.629  1.00 16.73 ? 790  ILE   B CG2   1 
ATOM   14869 C  CD1   . ILE   B 1  792  ? 26.163  41.093  69.138  1.00 18.54 ? 790  ILE   B CD1   1 
ATOM   14870 N  N     . GLN   B 1  793  ? 27.100  46.557  68.986  1.00 17.88 ? 791  GLN   B N     1 
ATOM   14871 C  CA    . GLN   B 1  793  ? 26.703  47.953  68.866  1.00 18.46 ? 791  GLN   B CA    1 
ATOM   14872 C  C     . GLN   B 1  793  ? 27.746  48.760  68.103  1.00 16.35 ? 791  GLN   B C     1 
ATOM   14873 O  O     . GLN   B 1  793  ? 27.402  49.594  67.254  1.00 19.54 ? 791  GLN   B O     1 
ATOM   14874 C  CB    . GLN   B 1  793  ? 26.513  48.529  70.262  1.00 18.73 ? 791  GLN   B CB    1 
ATOM   14875 C  CG    . GLN   B 1  793  ? 26.145  49.986  70.289  1.00 20.70 ? 791  GLN   B CG    1 
ATOM   14876 C  CD    . GLN   B 1  793  ? 26.417  50.595  71.637  1.00 23.95 ? 791  GLN   B CD    1 
ATOM   14877 O  OE1   . GLN   B 1  793  ? 27.440  50.313  72.268  1.00 25.00 ? 791  GLN   B OE1   1 
ATOM   14878 N  NE2   . GLN   B 1  793  ? 25.497  51.420  72.101  1.00 27.94 ? 791  GLN   B NE2   1 
ATOM   14879 N  N     . ALA   B 1  794  ? 29.026  48.515  68.384  1.00 18.85 ? 792  ALA   B N     1 
ATOM   14880 C  CA    . ALA   B 1  794  ? 30.081  49.226  67.670  1.00 19.97 ? 792  ALA   B CA    1 
ATOM   14881 C  C     . ALA   B 1  794  ? 30.091  48.875  66.188  1.00 21.42 ? 792  ALA   B C     1 
ATOM   14882 O  O     . ALA   B 1  794  ? 30.266  49.762  65.343  1.00 22.93 ? 792  ALA   B O     1 
ATOM   14883 C  CB    . ALA   B 1  794  ? 31.438  48.938  68.317  1.00 22.37 ? 792  ALA   B CB    1 
ATOM   14884 N  N     . GLN   B 1  795  ? 29.926  47.588  65.854  1.00 20.54 ? 793  GLN   B N     1 
ATOM   14885 C  CA    . GLN   B 1  795  ? 29.854  47.197  64.446  1.00 21.22 ? 793  GLN   B CA    1 
ATOM   14886 C  C     . GLN   B 1  795  ? 28.726  47.931  63.736  1.00 19.47 ? 793  GLN   B C     1 
ATOM   14887 O  O     . GLN   B 1  795  ? 28.898  48.424  62.614  1.00 20.32 ? 793  GLN   B O     1 
ATOM   14888 C  CB    . GLN   B 1  795  ? 29.601  45.692  64.319  1.00 23.73 ? 793  GLN   B CB    1 
ATOM   14889 C  CG    . GLN   B 1  795  ? 30.731  44.743  64.657  1.00 27.19 ? 793  GLN   B CG    1 
ATOM   14890 C  CD    . GLN   B 1  795  ? 30.327  43.285  64.421  1.00 26.44 ? 793  GLN   B CD    1 
ATOM   14891 O  OE1   . GLN   B 1  795  ? 29.675  42.664  65.264  1.00 28.26 ? 793  GLN   B OE1   1 
ATOM   14892 N  NE2   . GLN   B 1  795  ? 30.703  42.743  63.274  1.00 25.79 ? 793  GLN   B NE2   1 
ATOM   14893 N  N     . LEU   B 1  796  ? 27.550  47.998  64.370  1.00 18.55 ? 794  LEU   B N     1 
ATOM   14894 C  CA    . LEU   B 1  796  ? 26.379  48.541  63.695  1.00 20.10 ? 794  LEU   B CA    1 
ATOM   14895 C  C     . LEU   B 1  796  ? 26.470  50.044  63.534  1.00 21.57 ? 794  LEU   B C     1 
ATOM   14896 O  O     . LEU   B 1  796  ? 25.923  50.594  62.575  1.00 22.88 ? 794  LEU   B O     1 
ATOM   14897 C  CB    . LEU   B 1  796  ? 25.122  48.209  64.487  1.00 19.40 ? 794  LEU   B CB    1 
ATOM   14898 C  CG    . LEU   B 1  796  ? 24.715  46.742  64.460  1.00 19.45 ? 794  LEU   B CG    1 
ATOM   14899 C  CD1   . LEU   B 1  796  ? 23.479  46.591  65.310  1.00 18.91 ? 794  LEU   B CD1   1 
ATOM   14900 C  CD2   . LEU   B 1  796  ? 24.434  46.312  63.024  1.00 18.94 ? 794  LEU   B CD2   1 
ATOM   14901 N  N     . ALA   B 1  797  ? 27.143  50.716  64.466  1.00 22.52 ? 795  ALA   B N     1 
ATOM   14902 C  CA    . ALA   B 1  797  ? 27.240  52.167  64.426  1.00 25.40 ? 795  ALA   B CA    1 
ATOM   14903 C  C     . ALA   B 1  797  ? 28.063  52.652  63.246  1.00 22.59 ? 795  ALA   B C     1 
ATOM   14904 O  O     . ALA   B 1  797  ? 27.968  53.824  62.884  1.00 28.11 ? 795  ALA   B O     1 
ATOM   14905 C  CB    . ALA   B 1  797  ? 27.839  52.685  65.729  1.00 26.09 ? 795  ALA   B CB    1 
ATOM   14906 N  N     . ASP   B 1  798  ? 28.850  51.776  62.631  1.00 23.47 ? 796  ASP   B N     1 
ATOM   14907 C  CA    . ASP   B 1  798  ? 29.553  52.156  61.416  1.00 30.90 ? 796  ASP   B CA    1 
ATOM   14908 C  C     . ASP   B 1  798  ? 28.642  52.141  60.202  1.00 30.72 ? 796  ASP   B C     1 
ATOM   14909 O  O     . ASP   B 1  798  ? 29.050  52.602  59.132  1.00 31.54 ? 796  ASP   B O     1 
ATOM   14910 C  CB    . ASP   B 1  798  ? 30.716  51.192  61.165  1.00 28.22 ? 796  ASP   B CB    1 
ATOM   14911 C  CG    . ASP   B 1  798  ? 31.831  51.325  62.203  1.00 42.63 ? 796  ASP   B CG    1 
ATOM   14912 O  OD1   . ASP   B 1  798  ? 32.059  52.450  62.704  1.00 46.60 ? 796  ASP   B OD1   1 
ATOM   14913 O  OD2   . ASP   B 1  798  ? 32.487  50.304  62.513  1.00 47.75 ? 796  ASP   B OD2   1 
ATOM   14914 N  N     . ARG   B 1  799  ? 27.414  51.657  60.353  1.00 26.90 ? 797  ARG   B N     1 
ATOM   14915 C  CA    A ARG   B 1  799  ? 26.537  51.347  59.237  0.43 28.85 ? 797  ARG   B CA    1 
ATOM   14916 C  CA    B ARG   B 1  799  ? 26.554  51.379  59.221  0.57 28.86 ? 797  ARG   B CA    1 
ATOM   14917 C  C     . ARG   B 1  799  ? 25.260  52.174  59.321  1.00 26.11 ? 797  ARG   B C     1 
ATOM   14918 O  O     . ARG   B 1  799  ? 24.871  52.652  60.389  1.00 24.44 ? 797  ARG   B O     1 
ATOM   14919 C  CB    A ARG   B 1  799  ? 26.163  49.853  59.244  0.43 30.53 ? 797  ARG   B CB    1 
ATOM   14920 C  CB    B ARG   B 1  799  ? 26.243  49.880  59.151  0.57 30.64 ? 797  ARG   B CB    1 
ATOM   14921 C  CG    A ARG   B 1  799  ? 27.341  48.899  59.475  0.43 31.60 ? 797  ARG   B CG    1 
ATOM   14922 C  CG    B ARG   B 1  799  ? 27.470  48.993  59.377  0.57 31.64 ? 797  ARG   B CG    1 
ATOM   14923 C  CD    A ARG   B 1  799  ? 26.899  47.434  59.432  0.43 29.48 ? 797  ARG   B CD    1 
ATOM   14924 C  CD    B ARG   B 1  799  ? 27.569  47.963  58.278  0.57 30.46 ? 797  ARG   B CD    1 
ATOM   14925 N  NE    A ARG   B 1  799  ? 25.935  47.214  58.361  0.43 33.93 ? 797  ARG   B NE    1 
ATOM   14926 N  NE    B ARG   B 1  799  ? 26.233  47.603  57.833  0.57 34.12 ? 797  ARG   B NE    1 
ATOM   14927 C  CZ    A ARG   B 1  799  ? 24.764  46.603  58.500  0.43 29.39 ? 797  ARG   B CZ    1 
ATOM   14928 C  CZ    B ARG   B 1  799  ? 25.550  46.560  58.282  0.57 32.99 ? 797  ARG   B CZ    1 
ATOM   14929 N  NH1   A ARG   B 1  799  ? 24.428  45.993  59.625  0.43 24.64 ? 797  ARG   B NH1   1 
ATOM   14930 N  NH1   B ARG   B 1  799  ? 26.101  45.672  59.093  0.57 28.14 ? 797  ARG   B NH1   1 
ATOM   14931 N  NH2   A ARG   B 1  799  ? 23.914  46.594  57.479  0.43 28.05 ? 797  ARG   B NH2   1 
ATOM   14932 N  NH2   B ARG   B 1  799  ? 24.278  46.415  57.918  0.57 30.07 ? 797  ARG   B NH2   1 
ATOM   14933 N  N     . LEU   B 1  800  ? 24.604  52.321  58.178  1.00 23.46 ? 798  LEU   B N     1 
ATOM   14934 C  CA    . LEU   B 1  800  ? 23.288  52.923  58.084  1.00 24.91 ? 798  LEU   B CA    1 
ATOM   14935 C  C     . LEU   B 1  800  ? 22.457  52.066  57.147  1.00 23.71 ? 798  LEU   B C     1 
ATOM   14936 O  O     . LEU   B 1  800  ? 22.995  51.379  56.274  1.00 26.99 ? 798  LEU   B O     1 
ATOM   14937 C  CB    . LEU   B 1  800  ? 23.338  54.337  57.493  1.00 27.64 ? 798  LEU   B CB    1 
ATOM   14938 C  CG    . LEU   B 1  800  ? 23.945  55.440  58.354  1.00 27.89 ? 798  LEU   B CG    1 
ATOM   14939 C  CD1   . LEU   B 1  800  ? 23.953  56.734  57.566  1.00 32.52 ? 798  LEU   B CD1   1 
ATOM   14940 C  CD2   . LEU   B 1  800  ? 23.146  55.587  59.626  1.00 23.93 ? 798  LEU   B CD2   1 
ATOM   14941 N  N     . SER   B 1  801  ? 21.145  52.106  57.341  1.00 23.86 ? 799  SER   B N     1 
ATOM   14942 C  CA    . SER   B 1  801  ? 20.237  51.464  56.418  1.00 26.11 ? 799  SER   B CA    1 
ATOM   14943 C  C     . SER   B 1  801  ? 20.301  52.183  55.075  1.00 29.42 ? 799  SER   B C     1 
ATOM   14944 O  O     . SER   B 1  801  ? 20.833  53.292  54.981  1.00 28.75 ? 799  SER   B O     1 
ATOM   14945 C  CB    . SER   B 1  801  ? 18.820  51.566  56.959  1.00 27.81 ? 799  SER   B CB    1 
ATOM   14946 O  OG    . SER   B 1  801  ? 18.362  52.897  56.832  1.00 27.65 ? 799  SER   B OG    1 
ATOM   14947 N  N     . PRO   B 1  802  ? 19.784  51.564  54.010  1.00 32.04 ? 800  PRO   B N     1 
ATOM   14948 C  CA    . PRO   B 1  802  ? 19.710  52.286  52.729  1.00 33.86 ? 800  PRO   B CA    1 
ATOM   14949 C  C     . PRO   B 1  802  ? 18.915  53.576  52.826  1.00 35.28 ? 800  PRO   B C     1 
ATOM   14950 O  O     . PRO   B 1  802  ? 19.155  54.508  52.049  1.00 38.55 ? 800  PRO   B O     1 
ATOM   14951 C  CB    . PRO   B 1  802  ? 19.058  51.267  51.786  1.00 30.06 ? 800  PRO   B CB    1 
ATOM   14952 C  CG    . PRO   B 1  802  ? 19.405  49.938  52.378  1.00 34.71 ? 800  PRO   B CG    1 
ATOM   14953 C  CD    . PRO   B 1  802  ? 19.397  50.147  53.870  1.00 29.35 ? 800  PRO   B CD    1 
ATOM   14954 N  N     . ALA   B 1  803  ? 17.981  53.658  53.771  1.00 34.56 ? 801  ALA   B N     1 
ATOM   14955 C  CA    . ALA   B 1  803  ? 17.266  54.892  54.063  1.00 32.63 ? 801  ALA   B CA    1 
ATOM   14956 C  C     . ALA   B 1  803  ? 18.100  55.884  54.866  1.00 34.69 ? 801  ALA   B C     1 
ATOM   14957 O  O     . ALA   B 1  803  ? 17.627  56.992  55.133  1.00 37.57 ? 801  ALA   B O     1 
ATOM   14958 C  CB    . ALA   B 1  803  ? 15.967  54.580  54.809  1.00 35.46 ? 801  ALA   B CB    1 
ATOM   14959 N  N     . GLY   B 1  804  ? 19.319  55.521  55.256  1.00 32.36 ? 802  GLY   B N     1 
ATOM   14960 C  CA    . GLY   B 1  804  ? 20.169  56.439  55.988  1.00 29.38 ? 802  GLY   B CA    1 
ATOM   14961 C  C     . GLY   B 1  804  ? 19.866  56.550  57.464  1.00 28.87 ? 802  GLY   B C     1 
ATOM   14962 O  O     . GLY   B 1  804  ? 20.051  57.622  58.048  1.00 30.45 ? 802  GLY   B O     1 
ATOM   14963 N  N     . ARG   B 1  805  ? 19.421  55.474  58.093  1.00 28.14 ? 803  ARG   B N     1 
ATOM   14964 C  CA    . ARG   B 1  805  ? 19.041  55.499  59.496  1.00 24.36 ? 803  ARG   B CA    1 
ATOM   14965 C  C     . ARG   B 1  805  ? 19.771  54.398  60.248  1.00 23.36 ? 803  ARG   B C     1 
ATOM   14966 O  O     . ARG   B 1  805  ? 20.240  53.427  59.644  1.00 23.61 ? 803  ARG   B O     1 
ATOM   14967 C  CB    . ARG   B 1  805  ? 17.525  55.320  59.638  1.00 28.74 ? 803  ARG   B CB    1 
ATOM   14968 C  CG    . ARG   B 1  805  ? 16.733  56.423  58.960  1.00 29.32 ? 803  ARG   B CG    1 
ATOM   14969 C  CD    . ARG   B 1  805  ? 17.040  57.775  59.596  1.00 35.05 ? 803  ARG   B CD    1 
ATOM   14970 N  NE    . ARG   B 1  805  ? 16.267  58.847  58.977  1.00 39.97 ? 803  ARG   B NE    1 
ATOM   14971 C  CZ    . ARG   B 1  805  ? 16.743  59.680  58.063  1.00 33.41 ? 803  ARG   B CZ    1 
ATOM   14972 N  NH1   . ARG   B 1  805  ? 18.004  59.625  57.666  1.00 34.13 ? 803  ARG   B NH1   1 
ATOM   14973 N  NH2   . ARG   B 1  805  ? 15.930  60.589  57.527  1.00 38.55 ? 803  ARG   B NH2   1 
ATOM   14974 N  N     . PRO   B 1  806  ? 19.908  54.531  61.567  1.00 20.72 ? 804  PRO   B N     1 
ATOM   14975 C  CA    . PRO   B 1  806  ? 20.608  53.496  62.331  1.00 20.82 ? 804  PRO   B CA    1 
ATOM   14976 C  C     . PRO   B 1  806  ? 19.929  52.144  62.195  1.00 18.29 ? 804  PRO   B C     1 
ATOM   14977 O  O     . PRO   B 1  806  ? 18.701  52.042  62.105  1.00 20.25 ? 804  PRO   B O     1 
ATOM   14978 C  CB    . PRO   B 1  806  ? 20.537  54.010  63.773  1.00 21.11 ? 804  PRO   B CB    1 
ATOM   14979 C  CG    . PRO   B 1  806  ? 20.403  55.485  63.620  1.00 24.42 ? 804  PRO   B CG    1 
ATOM   14980 C  CD    . PRO   B 1  806  ? 19.506  55.654  62.430  1.00 23.75 ? 804  PRO   B CD    1 
ATOM   14981 N  N     . ILE   B 1  807  ? 20.756  51.107  62.175  1.00 18.34 ? 805  ILE   B N     1 
ATOM   14982 C  CA    . ILE   B 1  807  ? 20.293  49.723  62.168  1.00 17.30 ? 805  ILE   B CA    1 
ATOM   14983 C  C     . ILE   B 1  807  ? 19.802  49.408  63.576  1.00 18.14 ? 805  ILE   B C     1 
ATOM   14984 O  O     . ILE   B 1  807  ? 20.578  49.538  64.534  1.00 18.25 ? 805  ILE   B O     1 
ATOM   14985 C  CB    . ILE   B 1  807  ? 21.435  48.770  61.798  1.00 16.14 ? 805  ILE   B CB    1 
ATOM   14986 C  CG1   . ILE   B 1  807  ? 22.043  49.137  60.436  1.00 22.27 ? 805  ILE   B CG1   1 
ATOM   14987 C  CG2   . ILE   B 1  807  ? 20.940  47.331  61.847  1.00 18.03 ? 805  ILE   B CG2   1 
ATOM   14988 C  CD1   . ILE   B 1  807  ? 21.095  48.972  59.300  1.00 25.40 ? 805  ILE   B CD1   1 
ATOM   14989 N  N     . PRO   B 1  808  ? 18.552  48.991  63.751  1.00 15.26 ? 806  PRO   B N     1 
ATOM   14990 C  CA    . PRO   B 1  808  ? 18.045  48.736  65.105  1.00 16.96 ? 806  PRO   B CA    1 
ATOM   14991 C  C     . PRO   B 1  808  ? 18.750  47.562  65.752  1.00 17.80 ? 806  PRO   B C     1 
ATOM   14992 O  O     . PRO   B 1  808  ? 19.010  46.533  65.121  1.00 16.10 ? 806  PRO   B O     1 
ATOM   14993 C  CB    . PRO   B 1  808  ? 16.568  48.405  64.874  1.00 17.63 ? 806  PRO   B CB    1 
ATOM   14994 C  CG    . PRO   B 1  808  ? 16.227  49.092  63.575  1.00 21.81 ? 806  PRO   B CG    1 
ATOM   14995 C  CD    . PRO   B 1  808  ? 17.484  48.942  62.742  1.00 17.06 ? 806  PRO   B CD    1 
ATOM   14996 N  N     . LEU   B 1  809  ? 19.049  47.728  67.036  1.00 15.01 ? 807  LEU   B N     1 
ATOM   14997 C  CA    . LEU   B 1  809  ? 19.625  46.674  67.857  1.00 15.87 ? 807  LEU   B CA    1 
ATOM   14998 C  C     . LEU   B 1  809  ? 18.763  46.530  69.101  1.00 14.25 ? 807  LEU   B C     1 
ATOM   14999 O  O     . LEU   B 1  809  ? 18.558  47.509  69.826  1.00 17.28 ? 807  LEU   B O     1 
ATOM   15000 C  CB    . LEU   B 1  809  ? 21.046  47.049  68.267  1.00 16.00 ? 807  LEU   B CB    1 
ATOM   15001 C  CG    . LEU   B 1  809  ? 21.719  46.153  69.303  1.00 16.54 ? 807  LEU   B CG    1 
ATOM   15002 C  CD1   . LEU   B 1  809  ? 21.884  44.730  68.778  1.00 17.57 ? 807  LEU   B CD1   1 
ATOM   15003 C  CD2   . LEU   B 1  809  ? 23.085  46.748  69.684  1.00 18.50 ? 807  LEU   B CD2   1 
ATOM   15004 N  N     . ILE   B 1  810  ? 18.259  45.321  69.341  1.00 13.99 ? 808  ILE   B N     1 
ATOM   15005 C  CA    . ILE   B 1  810  ? 17.723  44.958  70.644  1.00 15.09 ? 808  ILE   B CA    1 
ATOM   15006 C  C     . ILE   B 1  810  ? 18.829  44.177  71.316  1.00 15.14 ? 808  ILE   B C     1 
ATOM   15007 O  O     . ILE   B 1  810  ? 19.311  43.180  70.768  1.00 16.44 ? 808  ILE   B O     1 
ATOM   15008 C  CB    . ILE   B 1  810  ? 16.441  44.118  70.534  1.00 15.38 ? 808  ILE   B CB    1 
ATOM   15009 C  CG1   . ILE   B 1  810  ? 15.396  44.835  69.696  1.00 15.18 ? 808  ILE   B CG1   1 
ATOM   15010 C  CG2   . ILE   B 1  810  ? 15.864  43.862  71.940  1.00 18.17 ? 808  ILE   B CG2   1 
ATOM   15011 C  CD1   . ILE   B 1  810  ? 14.061  44.080  69.631  1.00 18.54 ? 808  ILE   B CD1   1 
ATOM   15012 N  N     . ALA   B 1  811  ? 19.295  44.662  72.458  1.00 14.60 ? 809  ALA   B N     1 
ATOM   15013 C  CA    . ALA   B 1  811  ? 20.406  44.023  73.152  1.00 15.27 ? 809  ALA   B CA    1 
ATOM   15014 C  C     . ALA   B 1  811  ? 19.969  43.818  74.593  1.00 17.21 ? 809  ALA   B C     1 
ATOM   15015 O  O     . ALA   B 1  811  ? 19.918  44.769  75.379  1.00 17.30 ? 809  ALA   B O     1 
ATOM   15016 C  CB    . ALA   B 1  811  ? 21.675  44.859  73.064  1.00 16.45 ? 809  ALA   B CB    1 
ATOM   15017 N  N     . GLU   B 1  812  ? 19.649  42.579  74.917  1.00 14.52 ? 810  GLU   B N     1 
ATOM   15018 C  CA    . GLU   B 1  812  ? 19.151  42.205  76.230  1.00 14.38 ? 810  GLU   B CA    1 
ATOM   15019 C  C     . GLU   B 1  812  ? 20.275  41.455  76.916  1.00 16.04 ? 810  GLU   B C     1 
ATOM   15020 O  O     . GLU   B 1  812  ? 20.714  40.402  76.442  1.00 16.96 ? 810  GLU   B O     1 
ATOM   15021 C  CB    . GLU   B 1  812  ? 17.891  41.361  76.063  1.00 16.78 ? 810  GLU   B CB    1 
ATOM   15022 C  CG    . GLU   B 1  812  ? 16.806  42.161  75.329  1.00 18.04 ? 810  GLU   B CG    1 
ATOM   15023 C  CD    . GLU   B 1  812  ? 16.434  43.440  76.096  1.00 21.29 ? 810  GLU   B CD    1 
ATOM   15024 O  OE1   . GLU   B 1  812  ? 15.715  43.329  77.109  1.00 19.17 ? 810  GLU   B OE1   1 
ATOM   15025 O  OE2   . GLU   B 1  812  ? 16.868  44.547  75.709  1.00 19.49 ? 810  GLU   B OE2   1 
ATOM   15026 N  N     . THR   B 1  813  ? 20.777  42.031  78.001  1.00 15.48 ? 811  THR   B N     1 
ATOM   15027 C  CA    . THR   B 1  813  ? 22.089  41.661  78.486  1.00 14.40 ? 811  THR   B CA    1 
ATOM   15028 C  C     . THR   B 1  813  ? 22.052  41.203  79.944  1.00 15.29 ? 811  THR   B C     1 
ATOM   15029 O  O     . THR   B 1  813  ? 21.032  40.697  80.410  1.00 16.55 ? 811  THR   B O     1 
ATOM   15030 C  CB    . THR   B 1  813  ? 23.069  42.800  78.173  1.00 16.93 ? 811  THR   B CB    1 
ATOM   15031 O  OG1   . THR   B 1  813  ? 22.522  44.059  78.595  1.00 17.64 ? 811  THR   B OG1   1 
ATOM   15032 C  CG2   . THR   B 1  813  ? 23.287  42.885  76.649  1.00 17.57 ? 811  THR   B CG2   1 
ATOM   15033 N  N     . GLY   B 1  814  ? 23.153  41.340  80.666  1.00 16.83 ? 812  GLY   B N     1 
ATOM   15034 C  CA    . GLY   B 1  814  ? 23.286  40.651  81.931  1.00 17.58 ? 812  GLY   B CA    1 
ATOM   15035 C  C     . GLY   B 1  814  ? 22.574  41.329  83.082  1.00 17.37 ? 812  GLY   B C     1 
ATOM   15036 O  O     . GLY   B 1  814  ? 21.926  42.363  82.948  1.00 18.94 ? 812  GLY   B O     1 
ATOM   15037 N  N     . GLY   B 1  815  ? 22.685  40.702  84.248  1.00 17.31 ? 813  GLY   B N     1 
ATOM   15038 C  CA    . GLY   B 1  815  ? 22.093  41.249  85.449  1.00 18.07 ? 813  GLY   B CA    1 
ATOM   15039 C  C     . GLY   B 1  815  ? 23.045  41.083  86.612  1.00 16.95 ? 813  GLY   B C     1 
ATOM   15040 O  O     . GLY   B 1  815  ? 24.009  40.317  86.556  1.00 18.54 ? 813  GLY   B O     1 
ATOM   15041 N  N     . GLN   B 1  816  ? 22.772  41.835  87.660  1.00 15.51 ? 814  GLN   B N     1 
ATOM   15042 C  CA    . GLN   B 1  816  ? 23.427  41.657  88.959  1.00 15.73 ? 814  GLN   B CA    1 
ATOM   15043 C  C     . GLN   B 1  816  ? 22.312  41.699  89.997  1.00 15.17 ? 814  GLN   B C     1 
ATOM   15044 O  O     . GLN   B 1  816  ? 22.143  42.669  90.740  1.00 17.44 ? 814  GLN   B O     1 
ATOM   15045 C  CB    . GLN   B 1  816  ? 24.476  42.731  89.208  1.00 17.97 ? 814  GLN   B CB    1 
ATOM   15046 C  CG    . GLN   B 1  816  ? 25.379  42.422  90.393  1.00 17.28 ? 814  GLN   B CG    1 
ATOM   15047 C  CD    . GLN   B 1  816  ? 26.259  41.218  90.135  1.00 17.56 ? 814  GLN   B CD    1 
ATOM   15048 O  OE1   . GLN   B 1  816  ? 25.821  40.072  90.266  1.00 19.23 ? 814  GLN   B OE1   1 
ATOM   15049 N  NE2   . GLN   B 1  816  ? 27.517  41.472  89.761  1.00 17.19 ? 814  GLN   B NE2   1 
ATOM   15050 N  N     . ASN   B 1  817  ? 21.526  40.639  90.031  1.00 13.90 ? 815  ASN   B N     1 
ATOM   15051 C  CA    . ASN   B 1  817  ? 20.180  40.713  90.574  1.00 13.87 ? 815  ASN   B CA    1 
ATOM   15052 C  C     . ASN   B 1  817  ? 20.180  40.482  92.071  1.00 15.76 ? 815  ASN   B C     1 
ATOM   15053 O  O     . ASN   B 1  817  ? 20.781  39.517  92.561  1.00 16.33 ? 815  ASN   B O     1 
ATOM   15054 C  CB    . ASN   B 1  817  ? 19.313  39.663  89.896  1.00 14.85 ? 815  ASN   B CB    1 
ATOM   15055 C  CG    . ASN   B 1  817  ? 19.429  39.713  88.397  1.00 15.02 ? 815  ASN   B CG    1 
ATOM   15056 O  OD1   . ASN   B 1  817  ? 19.222  40.763  87.786  1.00 14.59 ? 815  ASN   B OD1   1 
ATOM   15057 N  ND2   . ASN   B 1  817  ? 19.790  38.589  87.799  1.00 15.01 ? 815  ASN   B ND2   1 
ATOM   15058 N  N     . ALA   B 1  818  ? 19.447  41.330  92.779  1.00 14.68 ? 816  ALA   B N     1 
ATOM   15059 C  CA    . ALA   B 1  818  ? 19.371  41.280  94.228  1.00 14.60 ? 816  ALA   B CA    1 
ATOM   15060 C  C     . ALA   B 1  818  ? 17.988  40.848  94.674  1.00 15.11 ? 816  ALA   B C     1 
ATOM   15061 O  O     . ALA   B 1  818  ? 16.994  41.003  93.961  1.00 15.45 ? 816  ALA   B O     1 
ATOM   15062 C  CB    . ALA   B 1  818  ? 19.672  42.656  94.827  1.00 15.38 ? 816  ALA   B CB    1 
ATOM   15063 N  N     . MET   B 1  819  ? 17.947  40.297  95.882  1.00 14.20 ? 817  MET   B N     1 
ATOM   15064 C  CA    . MET   B 1  819  ? 16.713  40.071  96.606  1.00 14.70 ? 817  MET   B CA    1 
ATOM   15065 C  C     . MET   B 1  819  ? 16.917  40.653  97.989  1.00 15.13 ? 817  MET   B C     1 
ATOM   15066 O  O     . MET   B 1  819  ? 17.915  40.342  98.651  1.00 16.06 ? 817  MET   B O     1 
ATOM   15067 C  CB    . MET   B 1  819  ? 16.370  38.587  96.717  1.00 16.44 ? 817  MET   B CB    1 
ATOM   15068 C  CG    . MET   B 1  819  ? 15.118  38.342  97.559  1.00 17.67 ? 817  MET   B CG    1 
ATOM   15069 S  SD    . MET   B 1  819  ? 14.837  36.593  97.894  1.00 18.76 ? 817  MET   B SD    1 
ATOM   15070 C  CE    . MET   B 1  819  ? 14.262  36.027  96.303  1.00 20.33 ? 817  MET   B CE    1 
ATOM   15071 N  N     . ILE   B 1  820  ? 16.004  41.524  98.395  1.00 15.62 ? 818  ILE   B N     1 
ATOM   15072 C  CA    . ILE   B 1  820  ? 16.028  42.106  99.729  1.00 14.56 ? 818  ILE   B CA    1 
ATOM   15073 C  C     . ILE   B 1  820  ? 14.994  41.397  100.575 1.00 15.94 ? 818  ILE   B C     1 
ATOM   15074 O  O     . ILE   B 1  820  ? 13.839  41.238  100.160 1.00 15.99 ? 818  ILE   B O     1 
ATOM   15075 C  CB    . ILE   B 1  820  ? 15.755  43.612  99.678  1.00 15.54 ? 818  ILE   B CB    1 
ATOM   15076 C  CG1   . ILE   B 1  820  ? 16.869  44.299  98.896  1.00 16.16 ? 818  ILE   B CG1   1 
ATOM   15077 C  CG2   . ILE   B 1  820  ? 15.643  44.178  101.107 1.00 16.38 ? 818  ILE   B CG2   1 
ATOM   15078 C  CD1   . ILE   B 1  820  ? 16.673  45.788  98.768  1.00 19.34 ? 818  ILE   B CD1   1 
ATOM   15079 N  N     . VAL   B 1  821  ? 15.406  40.980  101.767 1.00 16.24 ? 819  VAL   B N     1 
ATOM   15080 C  CA    . VAL   B 1  821  ? 14.579  40.209  102.676 1.00 15.38 ? 819  VAL   B CA    1 
ATOM   15081 C  C     . VAL   B 1  821  ? 14.591  40.960  103.994 1.00 17.86 ? 819  VAL   B C     1 
ATOM   15082 O  O     . VAL   B 1  821  ? 15.664  41.181  104.566 1.00 18.13 ? 819  VAL   B O     1 
ATOM   15083 C  CB    . VAL   B 1  821  ? 15.169  38.807  102.886 1.00 15.16 ? 819  VAL   B CB    1 
ATOM   15084 C  CG1   . VAL   B 1  821  ? 14.322  38.026  103.886 1.00 17.02 ? 819  VAL   B CG1   1 
ATOM   15085 C  CG2   . VAL   B 1  821  ? 15.281  38.061  101.558 1.00 16.78 ? 819  VAL   B CG2   1 
ATOM   15086 N  N     . ASP   B 1  822  ? 13.424  41.345  104.481 1.00 16.97 ? 820  ASP   B N     1 
ATOM   15087 C  CA    . ASP   B 1  822  ? 13.388  41.991  105.784 1.00 18.27 ? 820  ASP   B CA    1 
ATOM   15088 C  C     . ASP   B 1  822  ? 12.977  40.994  106.866 1.00 18.73 ? 820  ASP   B C     1 
ATOM   15089 O  O     . ASP   B 1  822  ? 12.734  39.811  106.612 1.00 18.51 ? 820  ASP   B O     1 
ATOM   15090 C  CB    . ASP   B 1  822  ? 12.574  43.291  105.759 1.00 19.22 ? 820  ASP   B CB    1 
ATOM   15091 C  CG    . ASP   B 1  822  ? 11.079  43.069  105.705 1.00 20.17 ? 820  ASP   B CG    1 
ATOM   15092 O  OD1   . ASP   B 1  822  ? 10.595  41.940  105.909 1.00 18.43 ? 820  ASP   B OD1   1 
ATOM   15093 O  OD2   . ASP   B 1  822  ? 10.375  44.066  105.445 1.00 22.47 ? 820  ASP   B OD2   1 
ATOM   15094 N  N     . SER   B 1  823  ? 12.892  41.493  108.098 1.00 18.27 ? 821  SER   B N     1 
ATOM   15095 C  CA    . SER   B 1  823  ? 12.607  40.609  109.218 1.00 20.29 ? 821  SER   B CA    1 
ATOM   15096 C  C     . SER   B 1  823  ? 11.160  40.134  109.268 1.00 20.66 ? 821  SER   B C     1 
ATOM   15097 O  O     . SER   B 1  823  ? 10.840  39.276  110.102 1.00 22.74 ? 821  SER   B O     1 
ATOM   15098 C  CB    . SER   B 1  823  ? 13.006  41.281  110.528 1.00 20.32 ? 821  SER   B CB    1 
ATOM   15099 O  OG    . SER   B 1  823  ? 12.265  42.472  110.721 1.00 22.18 ? 821  SER   B OG    1 
ATOM   15100 N  N     . SER   B 1  824  ? 10.275  40.657  108.424 1.00 17.58 ? 822  SER   B N     1 
ATOM   15101 C  CA    . SER   B 1  824  ? 8.909   40.161  108.398 1.00 19.16 ? 822  SER   B CA    1 
ATOM   15102 C  C     . SER   B 1  824  ? 8.732   38.982  107.456 1.00 19.58 ? 822  SER   B C     1 
ATOM   15103 O  O     . SER   B 1  824  ? 7.669   38.348  107.461 1.00 21.77 ? 822  SER   B O     1 
ATOM   15104 C  CB    . SER   B 1  824  ? 7.941   41.279  108.002 1.00 19.52 ? 822  SER   B CB    1 
ATOM   15105 O  OG    . SER   B 1  824  ? 8.057   41.572  106.622 1.00 18.20 ? 822  SER   B OG    1 
ATOM   15106 N  N     . ALA   B 1  825  ? 9.739   38.682  106.645 1.00 18.92 ? 823  ALA   B N     1 
ATOM   15107 C  CA    . ALA   B 1  825  ? 9.602   37.636  105.648 1.00 19.09 ? 823  ALA   B CA    1 
ATOM   15108 C  C     . ALA   B 1  825  ? 9.574   36.267  106.315 1.00 19.90 ? 823  ALA   B C     1 
ATOM   15109 O  O     . ALA   B 1  825  ? 10.094  36.074  107.415 1.00 22.26 ? 823  ALA   B O     1 
ATOM   15110 C  CB    . ALA   B 1  825  ? 10.778  37.715  104.678 1.00 20.44 ? 823  ALA   B CB    1 
ATOM   15111 N  N     . LEU   B 1  826  ? 8.946   35.311  105.645 1.00 20.74 ? 824  LEU   B N     1 
ATOM   15112 C  CA    . LEU   B 1  826  ? 8.850   33.949  106.157 1.00 21.76 ? 824  LEU   B CA    1 
ATOM   15113 C  C     . LEU   B 1  826  ? 10.074  33.172  105.687 1.00 22.52 ? 824  LEU   B C     1 
ATOM   15114 O  O     . LEU   B 1  826  ? 10.252  32.956  104.485 1.00 20.50 ? 824  LEU   B O     1 
ATOM   15115 C  CB    . LEU   B 1  826  ? 7.573   33.286  105.652 1.00 24.02 ? 824  LEU   B CB    1 
ATOM   15116 C  CG    . LEU   B 1  826  ? 7.333   31.846  106.112 1.00 29.87 ? 824  LEU   B CG    1 
ATOM   15117 C  CD1   . LEU   B 1  826  ? 7.286   31.754  107.629 1.00 30.93 ? 824  LEU   B CD1   1 
ATOM   15118 C  CD2   . LEU   B 1  826  ? 6.042   31.320  105.503 1.00 37.05 ? 824  LEU   B CD2   1 
ATOM   15119 N  N     . ALA   B 1  827  ? 10.913  32.751  106.634 1.00 20.94 ? 825  ALA   B N     1 
ATOM   15120 C  CA    . ALA   B 1  827  ? 12.215  32.186  106.282 1.00 19.63 ? 825  ALA   B CA    1 
ATOM   15121 C  C     . ALA   B 1  827  ? 12.090  31.022  105.305 1.00 20.03 ? 825  ALA   B C     1 
ATOM   15122 O  O     . ALA   B 1  827  ? 12.844  30.949  104.325 1.00 20.40 ? 825  ALA   B O     1 
ATOM   15123 C  CB    . ALA   B 1  827  ? 12.953  31.754  107.546 1.00 19.85 ? 825  ALA   B CB    1 
ATOM   15124 N  N     . GLU   B 1  828  ? 11.159  30.097  105.555 1.00 19.49 ? 826  GLU   B N     1 
ATOM   15125 C  CA    . GLU   B 1  828  ? 11.012  28.942  104.670 1.00 20.76 ? 826  GLU   B CA    1 
ATOM   15126 C  C     . GLU   B 1  828  ? 10.699  29.373  103.244 1.00 22.50 ? 826  GLU   B C     1 
ATOM   15127 O  O     . GLU   B 1  828  ? 11.207  28.782  102.280 1.00 20.62 ? 826  GLU   B O     1 
ATOM   15128 C  CB    . GLU   B 1  828  ? 9.910   28.018  105.186 1.00 24.60 ? 826  GLU   B CB    1 
ATOM   15129 C  CG    . GLU   B 1  828  ? 10.282  27.205  106.415 1.00 27.25 ? 826  GLU   B CG    1 
ATOM   15130 C  CD    . GLU   B 1  828  ? 10.172  27.980  107.722 1.00 29.74 ? 826  GLU   B CD    1 
ATOM   15131 O  OE1   . GLU   B 1  828  ? 9.788   29.176  107.706 1.00 28.01 ? 826  GLU   B OE1   1 
ATOM   15132 O  OE2   . GLU   B 1  828  ? 10.479  27.380  108.777 1.00 31.97 ? 826  GLU   B OE2   1 
ATOM   15133 N  N     . GLN   B 1  829  ? 9.860   30.401  103.089 1.00 18.61 ? 827  GLN   B N     1 
ATOM   15134 C  CA    . GLN   B 1  829  ? 9.522   30.879  101.751 1.00 20.01 ? 827  GLN   B CA    1 
ATOM   15135 C  C     . GLN   B 1  829  ? 10.726  31.531  101.096 1.00 19.65 ? 827  GLN   B C     1 
ATOM   15136 O  O     . GLN   B 1  829  ? 11.015  31.286  99.919  1.00 18.94 ? 827  GLN   B O     1 
ATOM   15137 C  CB    . GLN   B 1  829  ? 8.359   31.869  101.841 1.00 24.70 ? 827  GLN   B CB    1 
ATOM   15138 N  N     . VAL   B 1  830  ? 11.449  32.350  101.855 1.00 18.58 ? 828  VAL   B N     1 
ATOM   15139 C  CA    . VAL   B 1  830  ? 12.680  32.952  101.362 1.00 17.42 ? 828  VAL   B CA    1 
ATOM   15140 C  C     . VAL   B 1  830  ? 13.642  31.877  100.892 1.00 19.32 ? 828  VAL   B C     1 
ATOM   15141 O  O     . VAL   B 1  830  ? 14.212  31.959  99.800  1.00 17.72 ? 828  VAL   B O     1 
ATOM   15142 C  CB    . VAL   B 1  830  ? 13.325  33.806  102.466 1.00 16.51 ? 828  VAL   B CB    1 
ATOM   15143 C  CG1   . VAL   B 1  830  ? 14.709  34.285  102.019 1.00 19.22 ? 828  VAL   B CG1   1 
ATOM   15144 C  CG2   . VAL   B 1  830  ? 12.419  34.965  102.831 1.00 18.32 ? 828  VAL   B CG2   1 
ATOM   15145 N  N     . VAL   B 1  831  ? 13.869  30.868  101.732 1.00 17.22 ? 829  VAL   B N     1 
ATOM   15146 C  CA    . VAL   B 1  831  ? 14.874  29.871  101.395 1.00 15.31 ? 829  VAL   B CA    1 
ATOM   15147 C  C     . VAL   B 1  831  ? 14.493  29.132  100.121 1.00 18.04 ? 829  VAL   B C     1 
ATOM   15148 O  O     . VAL   B 1  831  ? 15.331  28.935  99.232  1.00 18.08 ? 829  VAL   B O     1 
ATOM   15149 C  CB    . VAL   B 1  831  ? 15.109  28.927  102.583 1.00 17.16 ? 829  VAL   B CB    1 
ATOM   15150 C  CG1   . VAL   B 1  831  ? 15.870  27.692  102.123 1.00 18.58 ? 829  VAL   B CG1   1 
ATOM   15151 C  CG2   . VAL   B 1  831  ? 15.864  29.676  103.675 1.00 18.61 ? 829  VAL   B CG2   1 
ATOM   15152 N  N     . GLY   B 1  832  ? 13.227  28.738  99.992  1.00 16.65 ? 830  GLY   B N     1 
ATOM   15153 C  CA    . GLY   B 1  832  ? 12.806  28.085  98.767  1.00 18.11 ? 830  GLY   B CA    1 
ATOM   15154 C  C     . GLY   B 1  832  ? 13.014  28.969  97.556  1.00 17.29 ? 830  GLY   B C     1 
ATOM   15155 O  O     . GLY   B 1  832  ? 13.498  28.515  96.519  1.00 18.15 ? 830  GLY   B O     1 
ATOM   15156 N  N     . ASP   B 1  833  ? 12.682  30.251  97.681  1.00 16.26 ? 831  ASP   B N     1 
ATOM   15157 C  CA    . ASP   B 1  833  ? 12.821  31.136  96.533  1.00 16.57 ? 831  ASP   B CA    1 
ATOM   15158 C  C     . ASP   B 1  833  ? 14.273  31.472  96.242  1.00 17.74 ? 831  ASP   B C     1 
ATOM   15159 O  O     . ASP   B 1  833  ? 14.632  31.725  95.092  1.00 17.09 ? 831  ASP   B O     1 
ATOM   15160 C  CB    . ASP   B 1  833  ? 12.013  32.406  96.767  1.00 16.88 ? 831  ASP   B CB    1 
ATOM   15161 C  CG    . ASP   B 1  833  ? 10.538  32.139  96.781  1.00 18.17 ? 831  ASP   B CG    1 
ATOM   15162 O  OD1   . ASP   B 1  833  ? 10.124  31.064  96.289  1.00 20.21 ? 831  ASP   B OD1   1 
ATOM   15163 O  OD2   . ASP   B 1  833  ? 9.785   32.997  97.270  1.00 20.24 ? 831  ASP   B OD2   1 
ATOM   15164 N  N     . VAL   B 1  834  ? 15.126  31.481  97.264  1.00 16.31 ? 832  VAL   B N     1 
ATOM   15165 C  CA    . VAL   B 1  834  ? 16.544  31.709  97.039  1.00 15.51 ? 832  VAL   B CA    1 
ATOM   15166 C  C     . VAL   B 1  834  ? 17.164  30.517  96.333  1.00 17.33 ? 832  VAL   B C     1 
ATOM   15167 O  O     . VAL   B 1  834  ? 17.963  30.671  95.397  1.00 18.13 ? 832  VAL   B O     1 
ATOM   15168 C  CB    . VAL   B 1  834  ? 17.244  32.011  98.377  1.00 16.93 ? 832  VAL   B CB    1 
ATOM   15169 C  CG1   . VAL   B 1  834  ? 18.745  31.848  98.235  1.00 17.85 ? 832  VAL   B CG1   1 
ATOM   15170 C  CG2   . VAL   B 1  834  ? 16.898  33.423  98.851  1.00 18.72 ? 832  VAL   B CG2   1 
ATOM   15171 N  N     . ILE   B 1  835  ? 16.827  29.309  96.771  1.00 17.21 ? 833  ILE   B N     1 
ATOM   15172 C  CA    . ILE   B 1  835  ? 17.385  28.130  96.121  1.00 20.51 ? 833  ILE   B CA    1 
ATOM   15173 C  C     . ILE   B 1  835  ? 16.981  28.093  94.658  1.00 20.17 ? 833  ILE   B C     1 
ATOM   15174 O  O     . ILE   B 1  835  ? 17.820  27.893  93.767  1.00 21.91 ? 833  ILE   B O     1 
ATOM   15175 C  CB    . ILE   B 1  835  ? 16.985  26.854  96.870  1.00 21.70 ? 833  ILE   B CB    1 
ATOM   15176 C  CG1   . ILE   B 1  835  ? 17.644  26.860  98.241  1.00 25.40 ? 833  ILE   B CG1   1 
ATOM   15177 C  CG2   . ILE   B 1  835  ? 17.390  25.615  96.062  1.00 25.88 ? 833  ILE   B CG2   1 
ATOM   15178 C  CD1   . ILE   B 1  835  ? 17.495  25.569  98.951  1.00 27.31 ? 833  ILE   B CD1   1 
ATOM   15179 N  N     . THR   B 1  836  ? 15.698  28.323  94.385  1.00 17.40 ? 834  THR   B N     1 
ATOM   15180 C  CA    . THR   B 1  836  ? 15.231  28.381  93.005  1.00 19.30 ? 834  THR   B CA    1 
ATOM   15181 C  C     . THR   B 1  836  ? 15.967  29.466  92.231  1.00 21.61 ? 834  THR   B C     1 
ATOM   15182 O  O     . THR   B 1  836  ? 16.499  29.225  91.141  1.00 24.66 ? 834  THR   B O     1 
ATOM   15183 C  CB    . THR   B 1  836  ? 13.734  28.672  93.011  1.00 19.46 ? 834  THR   B CB    1 
ATOM   15184 O  OG1   . THR   B 1  836  ? 13.035  27.561  93.590  1.00 26.07 ? 834  THR   B OG1   1 
ATOM   15185 C  CG2   . THR   B 1  836  ? 13.220  28.901  91.599  1.00 23.29 ? 834  THR   B CG2   1 
ATOM   15186 N  N     . SER   B 1  837  ? 16.024  30.669  92.787  1.00 17.46 ? 835  SER   B N     1 
ATOM   15187 C  CA    . SER   B 1  837  ? 16.519  31.798  92.013  1.00 17.35 ? 835  SER   B CA    1 
ATOM   15188 C  C     . SER   B 1  837  ? 18.028  31.758  91.850  1.00 16.55 ? 835  SER   B C     1 
ATOM   15189 O  O     . SER   B 1  837  ? 18.550  32.176  90.815  1.00 16.43 ? 835  SER   B O     1 
ATOM   15190 C  CB    . SER   B 1  837  ? 16.111  33.111  92.670  1.00 16.32 ? 835  SER   B CB    1 
ATOM   15191 O  OG    . SER   B 1  837  ? 14.706  33.161  92.843  1.00 16.24 ? 835  SER   B OG    1 
ATOM   15192 N  N     . ALA   B 1  838  ? 18.751  31.306  92.871  1.00 16.31 ? 836  ALA   B N     1 
ATOM   15193 C  CA    . ALA   B 1  838  ? 20.201  31.392  92.828  1.00 15.10 ? 836  ALA   B CA    1 
ATOM   15194 C  C     . ALA   B 1  838  ? 20.853  30.144  92.265  1.00 16.37 ? 836  ALA   B C     1 
ATOM   15195 O  O     . ALA   B 1  838  ? 21.895  30.249  91.616  1.00 18.58 ? 836  ALA   B O     1 
ATOM   15196 C  CB    . ALA   B 1  838  ? 20.771  31.650  94.231  1.00 15.03 ? 836  ALA   B CB    1 
ATOM   15197 N  N     . PHE   B 1  839  ? 20.284  28.963  92.500  1.00 18.94 ? 837  PHE   B N     1 
ATOM   15198 C  CA    . PHE   B 1  839  ? 21.018  27.738  92.234  1.00 19.04 ? 837  PHE   B CA    1 
ATOM   15199 C  C     . PHE   B 1  839  ? 20.368  26.815  91.223  1.00 20.35 ? 837  PHE   B C     1 
ATOM   15200 O  O     . PHE   B 1  839  ? 21.064  25.955  90.673  1.00 22.16 ? 837  PHE   B O     1 
ATOM   15201 C  CB    . PHE   B 1  839  ? 21.283  26.978  93.537  1.00 18.88 ? 837  PHE   B CB    1 
ATOM   15202 C  CG    . PHE   B 1  839  ? 21.992  27.804  94.570  1.00 19.69 ? 837  PHE   B CG    1 
ATOM   15203 C  CD1   . PHE   B 1  839  ? 23.260  28.322  94.317  1.00 17.84 ? 837  PHE   B CD1   1 
ATOM   15204 C  CD2   . PHE   B 1  839  ? 21.399  28.077  95.786  1.00 20.06 ? 837  PHE   B CD2   1 
ATOM   15205 C  CE1   . PHE   B 1  839  ? 23.906  29.093  95.258  1.00 17.42 ? 837  PHE   B CE1   1 
ATOM   15206 C  CE2   . PHE   B 1  839  ? 22.053  28.844  96.743  1.00 21.47 ? 837  PHE   B CE2   1 
ATOM   15207 C  CZ    . PHE   B 1  839  ? 23.312  29.346  96.479  1.00 20.37 ? 837  PHE   B CZ    1 
ATOM   15208 N  N     . ASP   B 1  840  ? 19.078  26.954  90.966  1.00 21.23 ? 838  ASP   B N     1 
ATOM   15209 C  CA    . ASP   B 1  840  ? 18.465  26.247  89.855  1.00 22.87 ? 838  ASP   B CA    1 
ATOM   15210 C  C     . ASP   B 1  840  ? 19.218  26.589  88.574  1.00 24.97 ? 838  ASP   B C     1 
ATOM   15211 O  O     . ASP   B 1  840  ? 19.676  27.720  88.381  1.00 20.43 ? 838  ASP   B O     1 
ATOM   15212 C  CB    . ASP   B 1  840  ? 16.994  26.664  89.768  1.00 27.13 ? 838  ASP   B CB    1 
ATOM   15213 C  CG    . ASP   B 1  840  ? 16.288  26.153  88.536  1.00 38.89 ? 838  ASP   B CG    1 
ATOM   15214 O  OD1   . ASP   B 1  840  ? 16.462  26.747  87.447  1.00 38.57 ? 838  ASP   B OD1   1 
ATOM   15215 O  OD2   . ASP   B 1  840  ? 15.532  25.168  88.666  1.00 44.12 ? 838  ASP   B OD2   1 
ATOM   15216 N  N     . SER   B 1  841  ? 19.398  25.583  87.721  1.00 19.51 ? 839  SER   B N     1 
ATOM   15217 C  CA    . SER   B 1  841  ? 20.206  25.717  86.508  1.00 19.13 ? 839  SER   B CA    1 
ATOM   15218 C  C     . SER   B 1  841  ? 21.628  26.138  86.824  1.00 17.93 ? 839  SER   B C     1 
ATOM   15219 O  O     . SER   B 1  841  ? 22.314  26.739  85.989  1.00 17.70 ? 839  SER   B O     1 
ATOM   15220 C  CB    . SER   B 1  841  ? 19.578  26.665  85.484  1.00 24.59 ? 839  SER   B CB    1 
ATOM   15221 O  OG    . SER   B 1  841  ? 18.254  26.257  85.207  1.00 25.91 ? 839  SER   B OG    1 
ATOM   15222 N  N     . ALA   B 1  842  ? 22.090  25.791  88.027  1.00 17.21 ? 840  ALA   B N     1 
ATOM   15223 C  CA    . ALA   B 1  842  ? 23.409  26.198  88.497  1.00 16.15 ? 840  ALA   B CA    1 
ATOM   15224 C  C     . ALA   B 1  842  ? 23.608  27.705  88.335  1.00 16.17 ? 840  ALA   B C     1 
ATOM   15225 O  O     . ALA   B 1  842  ? 24.693  28.184  88.009  1.00 16.75 ? 840  ALA   B O     1 
ATOM   15226 C  CB    . ALA   B 1  842  ? 24.531  25.379  87.848  1.00 17.28 ? 840  ALA   B CB    1 
ATOM   15227 N  N     . GLY   B 1  843  ? 22.540  28.463  88.578  1.00 16.31 ? 841  GLY   B N     1 
ATOM   15228 C  CA    . GLY   B 1  843  ? 22.659  29.908  88.493  1.00 16.28 ? 841  GLY   B CA    1 
ATOM   15229 C  C     . GLY   B 1  843  ? 22.829  30.432  87.089  1.00 15.66 ? 841  GLY   B C     1 
ATOM   15230 O  O     . GLY   B 1  843  ? 23.159  31.607  86.915  1.00 16.78 ? 841  GLY   B O     1 
ATOM   15231 N  N     . GLN   B 1  844  ? 22.608  29.595  86.090  1.00 14.90 ? 842  GLN   B N     1 
ATOM   15232 C  CA    . GLN   B 1  844  ? 22.860  29.993  84.711  1.00 16.18 ? 842  GLN   B CA    1 
ATOM   15233 C  C     . GLN   B 1  844  ? 21.599  30.524  84.058  1.00 16.20 ? 842  GLN   B C     1 
ATOM   15234 O  O     . GLN   B 1  844  ? 21.136  30.045  83.034  1.00 16.88 ? 842  GLN   B O     1 
ATOM   15235 C  CB    . GLN   B 1  844  ? 23.478  28.839  83.938  1.00 14.65 ? 842  GLN   B CB    1 
ATOM   15236 C  CG    . GLN   B 1  844  ? 24.847  28.538  84.492  1.00 15.12 ? 842  GLN   B CG    1 
ATOM   15237 C  CD    . GLN   B 1  844  ? 25.415  27.229  84.000  1.00 16.18 ? 842  GLN   B CD    1 
ATOM   15238 O  OE1   . GLN   B 1  844  ? 26.499  27.194  83.430  1.00 16.92 ? 842  GLN   B OE1   1 
ATOM   15239 N  NE2   . GLN   B 1  844  ? 24.707  26.143  84.259  1.00 17.61 ? 842  GLN   B NE2   1 
ATOM   15240 N  N     . ARG   B 1  845  ? 21.010  31.512  84.719  1.00 16.24 ? 843  ARG   B N     1 
ATOM   15241 C  CA    . ARG   B 1  845  ? 19.909  32.293  84.187  1.00 13.32 ? 843  ARG   B CA    1 
ATOM   15242 C  C     . ARG   B 1  845  ? 20.307  33.753  84.308  1.00 13.99 ? 843  ARG   B C     1 
ATOM   15243 O  O     . ARG   B 1  845  ? 20.873  34.168  85.318  1.00 15.01 ? 843  ARG   B O     1 
ATOM   15244 C  CB    . ARG   B 1  845  ? 18.635  32.094  85.000  1.00 16.60 ? 843  ARG   B CB    1 
ATOM   15245 C  CG    . ARG   B 1  845  ? 18.080  30.694  84.993  1.00 18.73 ? 843  ARG   B CG    1 
ATOM   15246 C  CD    . ARG   B 1  845  ? 16.770  30.718  85.770  1.00 24.27 ? 843  ARG   B CD    1 
ATOM   15247 N  NE    . ARG   B 1  845  ? 16.222  29.393  86.016  1.00 27.06 ? 843  ARG   B NE    1 
ATOM   15248 C  CZ    . ARG   B 1  845  ? 15.278  28.822  85.287  1.00 37.60 ? 843  ARG   B CZ    1 
ATOM   15249 N  NH1   . ARG   B 1  845  ? 14.762  29.425  84.227  1.00 39.22 ? 843  ARG   B NH1   1 
ATOM   15250 N  NH2   . ARG   B 1  845  ? 14.834  27.618  85.635  1.00 44.09 ? 843  ARG   B NH2   1 
ATOM   15251 N  N     . CYS   B 1  846  ? 19.973  34.554  83.300  1.00 16.01 ? 844  CYS   B N     1 
ATOM   15252 C  CA    . CYS   B 1  846  ? 20.253  35.977  83.424  1.00 16.69 ? 844  CYS   B CA    1 
ATOM   15253 C  C     . CYS   B 1  846  ? 19.528  36.585  84.616  1.00 13.09 ? 844  CYS   B C     1 
ATOM   15254 O  O     . CYS   B 1  846  ? 19.993  37.572  85.189  1.00 15.71 ? 844  CYS   B O     1 
ATOM   15255 C  CB    . CYS   B 1  846  ? 19.838  36.686  82.140  1.00 16.83 ? 844  CYS   B CB    1 
ATOM   15256 S  SG    . CYS   B 1  846  ? 18.179  36.322  81.605  1.00 16.27 ? 844  CYS   B SG    1 
ATOM   15257 N  N     . SER   B 1  847  ? 18.369  36.037  84.952  1.00 14.26 ? 845  SER   B N     1 
ATOM   15258 C  CA    . SER   B 1  847  ? 17.514  36.470  86.046  1.00 14.49 ? 845  SER   B CA    1 
ATOM   15259 C  C     . SER   B 1  847  ? 17.951  35.941  87.399  1.00 15.39 ? 845  SER   B C     1 
ATOM   15260 O  O     . SER   B 1  847  ? 17.317  36.284  88.402  1.00 14.56 ? 845  SER   B O     1 
ATOM   15261 C  CB    . SER   B 1  847  ? 16.125  35.919  85.780  1.00 15.18 ? 845  SER   B CB    1 
ATOM   15262 O  OG    . SER   B 1  847  ? 16.239  34.532  85.520  1.00 17.07 ? 845  SER   B OG    1 
ATOM   15263 N  N     . ALA   B 1  848  ? 19.009  35.140  87.458  1.00 14.15 ? 846  ALA   B N     1 
ATOM   15264 C  CA    . ALA   B 1  848  ? 19.334  34.437  88.688  1.00 13.99 ? 846  ALA   B CA    1 
ATOM   15265 C  C     . ALA   B 1  848  ? 19.674  35.411  89.805  1.00 14.78 ? 846  ALA   B C     1 
ATOM   15266 O  O     . ALA   B 1  848  ? 20.236  36.485  89.588  1.00 15.39 ? 846  ALA   B O     1 
ATOM   15267 C  CB    . ALA   B 1  848  ? 20.547  33.533  88.460  1.00 14.75 ? 846  ALA   B CB    1 
ATOM   15268 N  N     . LEU   B 1  849  ? 19.360  34.987  91.025  1.00 14.95 ? 847  LEU   B N     1 
ATOM   15269 C  CA    . LEU   B 1  849  ? 19.698  35.762  92.207  1.00 14.16 ? 847  LEU   B CA    1 
ATOM   15270 C  C     . LEU   B 1  849  ? 21.201  35.746  92.445  1.00 14.57 ? 847  LEU   B C     1 
ATOM   15271 O  O     . LEU   B 1  849  ? 21.790  34.677  92.623  1.00 15.91 ? 847  LEU   B O     1 
ATOM   15272 C  CB    . LEU   B 1  849  ? 18.958  35.162  93.390  1.00 15.26 ? 847  LEU   B CB    1 
ATOM   15273 C  CG    . LEU   B 1  849  ? 19.313  35.791  94.727  1.00 15.80 ? 847  LEU   B CG    1 
ATOM   15274 C  CD1   . LEU   B 1  849  ? 19.029  37.269  94.721  1.00 17.88 ? 847  LEU   B CD1   1 
ATOM   15275 C  CD2   . LEU   B 1  849  ? 18.556  35.079  95.831  1.00 16.33 ? 847  LEU   B CD2   1 
ATOM   15276 N  N     . ARG   B 1  850  ? 21.815  36.929  92.440  1.00 13.67 ? 848  ARG   B N     1 
ATOM   15277 C  CA    . ARG   B 1  850  ? 23.243  37.063  92.675  1.00 14.70 ? 848  ARG   B CA    1 
ATOM   15278 C  C     . ARG   B 1  850  ? 23.567  37.607  94.051  1.00 15.75 ? 848  ARG   B C     1 
ATOM   15279 O  O     . ARG   B 1  850  ? 24.632  37.299  94.592  1.00 16.49 ? 848  ARG   B O     1 
ATOM   15280 C  CB    . ARG   B 1  850  ? 23.880  38.001  91.639  1.00 15.80 ? 848  ARG   B CB    1 
ATOM   15281 C  CG    . ARG   B 1  850  ? 23.550  37.653  90.206  1.00 17.26 ? 848  ARG   B CG    1 
ATOM   15282 C  CD    . ARG   B 1  850  ? 23.925  36.220  89.930  1.00 15.58 ? 848  ARG   B CD    1 
ATOM   15283 N  NE    . ARG   B 1  850  ? 23.711  35.901  88.524  1.00 16.79 ? 848  ARG   B NE    1 
ATOM   15284 C  CZ    . ARG   B 1  850  ? 23.803  34.682  88.021  1.00 16.12 ? 848  ARG   B CZ    1 
ATOM   15285 N  NH1   . ARG   B 1  850  ? 24.067  33.641  88.788  1.00 16.92 ? 848  ARG   B NH1   1 
ATOM   15286 N  NH2   . ARG   B 1  850  ? 23.596  34.501  86.713  1.00 16.03 ? 848  ARG   B NH2   1 
ATOM   15287 N  N     . VAL   B 1  851  ? 22.701  38.451  94.606  1.00 15.79 ? 849  VAL   B N     1 
ATOM   15288 C  CA    . VAL   B 1  851  ? 22.983  39.121  95.871  1.00 15.43 ? 849  VAL   B CA    1 
ATOM   15289 C  C     . VAL   B 1  851  ? 21.758  39.013  96.759  1.00 16.36 ? 849  VAL   B C     1 
ATOM   15290 O  O     . VAL   B 1  851  ? 20.730  39.640  96.485  1.00 16.57 ? 849  VAL   B O     1 
ATOM   15291 C  CB    . VAL   B 1  851  ? 23.376  40.593  95.682  1.00 17.04 ? 849  VAL   B CB    1 
ATOM   15292 C  CG1   . VAL   B 1  851  ? 23.744  41.196  97.034  1.00 20.09 ? 849  VAL   B CG1   1 
ATOM   15293 C  CG2   . VAL   B 1  851  ? 24.529  40.743  94.683  1.00 20.11 ? 849  VAL   B CG2   1 
ATOM   15294 N  N     . LEU   B 1  852  ? 21.875  38.240  97.831  1.00 17.36 ? 850  LEU   B N     1 
ATOM   15295 C  CA    . LEU   B 1  852  ? 20.818  38.102  98.816  1.00 15.82 ? 850  LEU   B CA    1 
ATOM   15296 C  C     . LEU   B 1  852  ? 21.112  39.080  99.945  1.00 15.44 ? 850  LEU   B C     1 
ATOM   15297 O  O     . LEU   B 1  852  ? 22.167  38.996  100.579 1.00 16.38 ? 850  LEU   B O     1 
ATOM   15298 C  CB    . LEU   B 1  852  ? 20.798  36.670  99.331  1.00 16.43 ? 850  LEU   B CB    1 
ATOM   15299 C  CG    . LEU   B 1  852  ? 19.781  36.392  100.427 1.00 16.03 ? 850  LEU   B CG    1 
ATOM   15300 C  CD1   . LEU   B 1  852  ? 18.366  36.694  99.934  1.00 17.35 ? 850  LEU   B CD1   1 
ATOM   15301 C  CD2   . LEU   B 1  852  ? 19.898  34.947  100.857 1.00 18.75 ? 850  LEU   B CD2   1 
ATOM   15302 N  N     . CYS   B 1  853  ? 20.197  40.016  100.174 1.00 15.86 ? 851  CYS   B N     1 
ATOM   15303 C  CA    . CYS   B 1  853  ? 20.362  41.058  101.180 1.00 16.37 ? 851  CYS   B CA    1 
ATOM   15304 C  C     . CYS   B 1  853  ? 19.417  40.751  102.326 1.00 15.63 ? 851  CYS   B C     1 
ATOM   15305 O  O     . CYS   B 1  853  ? 18.195  40.806  102.166 1.00 16.85 ? 851  CYS   B O     1 
ATOM   15306 C  CB    . CYS   B 1  853  ? 20.055  42.435  100.609 1.00 16.59 ? 851  CYS   B CB    1 
ATOM   15307 S  SG    . CYS   B 1  853  ? 20.997  42.775  99.123  1.00 19.41 ? 851  CYS   B SG    1 
ATOM   15308 N  N     . LEU   B 1  854  ? 19.983  40.413  103.475 1.00 16.60 ? 852  LEU   B N     1 
ATOM   15309 C  CA    . LEU   B 1  854  ? 19.201  39.945  104.605 1.00 16.33 ? 852  LEU   B CA    1 
ATOM   15310 C  C     . LEU   B 1  854  ? 19.262  40.983  105.709 1.00 18.19 ? 852  LEU   B C     1 
ATOM   15311 O  O     . LEU   B 1  854  ? 20.350  41.414  106.097 1.00 17.86 ? 852  LEU   B O     1 
ATOM   15312 C  CB    . LEU   B 1  854  ? 19.809  38.652  105.139 1.00 16.37 ? 852  LEU   B CB    1 
ATOM   15313 C  CG    . LEU   B 1  854  ? 19.816  37.510  104.132 1.00 16.52 ? 852  LEU   B CG    1 
ATOM   15314 C  CD1   . LEU   B 1  854  ? 20.518  36.302  104.770 1.00 17.66 ? 852  LEU   B CD1   1 
ATOM   15315 C  CD2   . LEU   B 1  854  ? 18.398  37.165  103.715 1.00 19.26 ? 852  LEU   B CD2   1 
ATOM   15316 N  N     . GLN   B 1  855  ? 18.105  41.363  106.234 1.00 16.98 ? 853  GLN   B N     1 
ATOM   15317 C  CA    . GLN   B 1  855  ? 18.110  42.222  107.406 1.00 16.25 ? 853  GLN   B CA    1 
ATOM   15318 C  C     . GLN   B 1  855  ? 18.887  41.535  108.525 1.00 19.42 ? 853  GLN   B C     1 
ATOM   15319 O  O     . GLN   B 1  855  ? 18.764  40.327  108.733 1.00 18.69 ? 853  GLN   B O     1 
ATOM   15320 C  CB    . GLN   B 1  855  ? 16.687  42.524  107.846 1.00 16.39 ? 853  GLN   B CB    1 
ATOM   15321 C  CG    . GLN   B 1  855  ? 16.635  43.694  108.817 1.00 19.74 ? 853  GLN   B CG    1 
ATOM   15322 C  CD    . GLN   B 1  855  ? 15.237  44.011  109.267 1.00 24.12 ? 853  GLN   B CD    1 
ATOM   15323 O  OE1   . GLN   B 1  855  ? 14.294  43.978  108.479 1.00 27.30 ? 853  GLN   B OE1   1 
ATOM   15324 N  NE2   . GLN   B 1  855  ? 15.090  44.325  110.545 1.00 25.95 ? 853  GLN   B NE2   1 
ATOM   15325 N  N     . GLU   B 1  856  ? 19.711  42.319  109.230 1.00 19.40 ? 854  GLU   B N     1 
ATOM   15326 C  CA    . GLU   B 1  856  ? 20.706  41.746  110.135 1.00 19.30 ? 854  GLU   B CA    1 
ATOM   15327 C  C     . GLU   B 1  856  ? 20.077  40.837  111.185 1.00 21.12 ? 854  GLU   B C     1 
ATOM   15328 O  O     . GLU   B 1  856  ? 20.661  39.809  111.551 1.00 23.07 ? 854  GLU   B O     1 
ATOM   15329 C  CB    . GLU   B 1  856  ? 21.500  42.873  110.804 1.00 26.52 ? 854  GLU   B CB    1 
ATOM   15330 N  N     . ASP   B 1  857  ? 18.892  41.195  111.683 1.00 21.47 ? 855  ASP   B N     1 
ATOM   15331 C  CA    . ASP   B 1  857  ? 18.280  40.449  112.781 1.00 23.52 ? 855  ASP   B CA    1 
ATOM   15332 C  C     . ASP   B 1  857  ? 17.811  39.056  112.379 1.00 21.85 ? 855  ASP   B C     1 
ATOM   15333 O  O     . ASP   B 1  857  ? 17.623  38.204  113.252 1.00 26.20 ? 855  ASP   B O     1 
ATOM   15334 C  CB    . ASP   B 1  857  ? 17.088  41.220  113.347 1.00 27.67 ? 855  ASP   B CB    1 
ATOM   15335 N  N     . VAL   B 1  858  ? 17.595  38.799  111.092 1.00 18.30 ? 856  VAL   B N     1 
ATOM   15336 C  CA    . VAL   B 1  858  ? 17.151  37.488  110.649 1.00 20.13 ? 856  VAL   B CA    1 
ATOM   15337 C  C     . VAL   B 1  858  ? 18.192  36.767  109.826 1.00 16.62 ? 856  VAL   B C     1 
ATOM   15338 O  O     . VAL   B 1  858  ? 17.967  35.614  109.448 1.00 19.36 ? 856  VAL   B O     1 
ATOM   15339 C  CB    . VAL   B 1  858  ? 15.812  37.550  109.895 1.00 20.51 ? 856  VAL   B CB    1 
ATOM   15340 C  CG1   . VAL   B 1  858  ? 14.714  38.043  110.818 1.00 23.14 ? 856  VAL   B CG1   1 
ATOM   15341 C  CG2   . VAL   B 1  858  ? 15.945  38.444  108.679 1.00 20.13 ? 856  VAL   B CG2   1 
ATOM   15342 N  N     . ALA   B 1  859  ? 19.332  37.398  109.555 1.00 18.83 ? 857  ALA   B N     1 
ATOM   15343 C  CA    . ALA   B 1  859  ? 20.279  36.840  108.593 1.00 17.59 ? 857  ALA   B CA    1 
ATOM   15344 C  C     . ALA   B 1  859  ? 20.798  35.471  109.029 1.00 18.67 ? 857  ALA   B C     1 
ATOM   15345 O  O     . ALA   B 1  859  ? 20.828  34.528  108.233 1.00 18.96 ? 857  ALA   B O     1 
ATOM   15346 C  CB    . ALA   B 1  859  ? 21.429  37.820  108.356 1.00 17.53 ? 857  ALA   B CB    1 
ATOM   15347 N  N     . ASP   B 1  860  ? 21.200  35.335  110.294 1.00 19.28 ? 858  ASP   B N     1 
ATOM   15348 C  CA    . ASP   B 1  860  ? 21.781  34.074  110.744 1.00 19.30 ? 858  ASP   B CA    1 
ATOM   15349 C  C     . ASP   B 1  860  ? 20.785  32.933  110.620 1.00 19.45 ? 858  ASP   B C     1 
ATOM   15350 O  O     . ASP   B 1  860  ? 21.130  31.841  110.151 1.00 20.22 ? 858  ASP   B O     1 
ATOM   15351 C  CB    . ASP   B 1  860  ? 22.252  34.191  112.194 1.00 19.62 ? 858  ASP   B CB    1 
ATOM   15352 C  CG    . ASP   B 1  860  ? 23.464  35.072  112.344 1.00 29.01 ? 858  ASP   B CG    1 
ATOM   15353 O  OD1   . ASP   B 1  860  ? 24.286  35.118  111.410 1.00 31.03 ? 858  ASP   B OD1   1 
ATOM   15354 O  OD2   . ASP   B 1  860  ? 23.598  35.719  113.401 1.00 30.76 ? 858  ASP   B OD2   1 
ATOM   15355 N  N     . ARG   B 1  861  ? 19.541  33.162  111.051 1.00 18.49 ? 859  ARG   B N     1 
ATOM   15356 C  CA    . ARG   B 1  861  ? 18.548  32.097  110.991 1.00 20.97 ? 859  ARG   B CA    1 
ATOM   15357 C  C     . ARG   B 1  861  ? 18.234  31.722  109.552 1.00 18.78 ? 859  ARG   B C     1 
ATOM   15358 O  O     . ARG   B 1  861  ? 18.114  30.539  109.226 1.00 19.56 ? 859  ARG   B O     1 
ATOM   15359 C  CB    . ARG   B 1  861  ? 17.279  32.499  111.740 1.00 24.03 ? 859  ARG   B CB    1 
ATOM   15360 C  CG    . ARG   B 1  861  ? 16.195  31.449  111.663 1.00 33.02 ? 859  ARG   B CG    1 
ATOM   15361 C  CD    . ARG   B 1  861  ? 15.046  31.714  112.614 1.00 37.44 ? 859  ARG   B CD    1 
ATOM   15362 N  NE    . ARG   B 1  861  ? 14.000  30.719  112.407 1.00 47.68 ? 859  ARG   B NE    1 
ATOM   15363 C  CZ    . ARG   B 1  861  ? 12.953  30.892  111.612 1.00 42.61 ? 859  ARG   B CZ    1 
ATOM   15364 N  NH1   . ARG   B 1  861  ? 12.741  32.042  110.992 1.00 45.47 ? 859  ARG   B NH1   1 
ATOM   15365 N  NH2   . ARG   B 1  861  ? 12.099  29.888  111.435 1.00 45.99 ? 859  ARG   B NH2   1 
ATOM   15366 N  N     . ILE   B 1  862  ? 18.114  32.716  108.671 1.00 17.53 ? 860  ILE   B N     1 
ATOM   15367 C  CA    . ILE   B 1  862  ? 17.866  32.398  107.270 1.00 17.37 ? 860  ILE   B CA    1 
ATOM   15368 C  C     . ILE   B 1  862  ? 19.047  31.660  106.655 1.00 16.95 ? 860  ILE   B C     1 
ATOM   15369 O  O     . ILE   B 1  862  ? 18.864  30.692  105.908 1.00 18.36 ? 860  ILE   B O     1 
ATOM   15370 C  CB    . ILE   B 1  862  ? 17.493  33.669  106.498 1.00 18.04 ? 860  ILE   B CB    1 
ATOM   15371 C  CG1   . ILE   B 1  862  ? 16.124  34.155  106.984 1.00 20.70 ? 860  ILE   B CG1   1 
ATOM   15372 C  CG2   . ILE   B 1  862  ? 17.506  33.404  104.995 1.00 18.92 ? 860  ILE   B CG2   1 
ATOM   15373 C  CD1   . ILE   B 1  862  ? 15.713  35.521  106.452 1.00 23.81 ? 860  ILE   B CD1   1 
ATOM   15374 N  N     . LEU   B 1  863  ? 20.270  32.094  106.954 1.00 18.34 ? 861  LEU   B N     1 
ATOM   15375 C  CA    . LEU   B 1  863  ? 21.429  31.431  106.365 1.00 18.98 ? 861  LEU   B CA    1 
ATOM   15376 C  C     . LEU   B 1  863  ? 21.569  30.004  106.868 1.00 21.84 ? 861  LEU   B C     1 
ATOM   15377 O  O     . LEU   B 1  863  ? 21.940  29.105  106.104 1.00 19.99 ? 861  LEU   B O     1 
ATOM   15378 C  CB    . LEU   B 1  863  ? 22.696  32.231  106.638 1.00 18.98 ? 861  LEU   B CB    1 
ATOM   15379 C  CG    . LEU   B 1  863  ? 22.760  33.541  105.863 1.00 19.04 ? 861  LEU   B CG    1 
ATOM   15380 C  CD1   . LEU   B 1  863  ? 23.909  34.370  106.420 1.00 23.50 ? 861  LEU   B CD1   1 
ATOM   15381 C  CD2   . LEU   B 1  863  ? 22.940  33.276  104.378 1.00 22.00 ? 861  LEU   B CD2   1 
ATOM   15382 N  N     . THR   B 1  864  ? 21.288  29.772  108.149 1.00 18.14 ? 862  THR   B N     1 
ATOM   15383 C  CA    . THR   B 1  864  ? 21.319  28.403  108.649 1.00 19.01 ? 862  THR   B CA    1 
ATOM   15384 C  C     . THR   B 1  864  ? 20.319  27.542  107.901 1.00 20.32 ? 862  THR   B C     1 
ATOM   15385 O  O     . THR   B 1  864  ? 20.627  26.414  107.506 1.00 20.75 ? 862  THR   B O     1 
ATOM   15386 C  CB    . THR   B 1  864  ? 21.018  28.384  110.145 1.00 23.72 ? 862  THR   B CB    1 
ATOM   15387 O  OG1   . THR   B 1  864  ? 22.079  29.046  110.835 1.00 24.72 ? 862  THR   B OG1   1 
ATOM   15388 C  CG2   . THR   B 1  864  ? 20.893  26.948  110.651 1.00 25.57 ? 862  THR   B CG2   1 
ATOM   15389 N  N     . MET   B 1  865  ? 19.121  28.072  107.672 1.00 17.33 ? 863  MET   B N     1 
ATOM   15390 C  CA    . MET   B 1  865  ? 18.101  27.296  106.995 1.00 18.65 ? 863  MET   B CA    1 
ATOM   15391 C  C     . MET   B 1  865  ? 18.473  27.085  105.535 1.00 19.57 ? 863  MET   B C     1 
ATOM   15392 O  O     . MET   B 1  865  ? 18.278  25.995  104.986 1.00 17.18 ? 863  MET   B O     1 
ATOM   15393 C  CB    . MET   B 1  865  ? 16.767  28.025  107.112 1.00 17.63 ? 863  MET   B CB    1 
ATOM   15394 C  CG    . MET   B 1  865  ? 15.625  27.248  106.540 1.00 19.09 ? 863  MET   B CG    1 
ATOM   15395 S  SD    . MET   B 1  865  ? 14.076  28.136  106.674 1.00 22.38 ? 863  MET   B SD    1 
ATOM   15396 C  CE    . MET   B 1  865  ? 13.949  28.315  108.452 1.00 24.98 ? 863  MET   B CE    1 
ATOM   15397 N  N     . LEU   B 1  866  ? 19.012  28.126  104.901 1.00 17.66 ? 864  LEU   B N     1 
ATOM   15398 C  CA    . LEU   B 1  866  ? 19.434  28.018  103.510 1.00 17.34 ? 864  LEU   B CA    1 
ATOM   15399 C  C     . LEU   B 1  866  ? 20.499  26.947  103.354 1.00 18.14 ? 864  LEU   B C     1 
ATOM   15400 O  O     . LEU   B 1  866  ? 20.406  26.089  102.468 1.00 17.84 ? 864  LEU   B O     1 
ATOM   15401 C  CB    . LEU   B 1  866  ? 19.968  29.371  103.047 1.00 17.13 ? 864  LEU   B CB    1 
ATOM   15402 C  CG    . LEU   B 1  866  ? 20.588  29.351  101.651 1.00 16.36 ? 864  LEU   B CG    1 
ATOM   15403 C  CD1   . LEU   B 1  866  ? 19.555  28.955  100.619 1.00 19.02 ? 864  LEU   B CD1   1 
ATOM   15404 C  CD2   . LEU   B 1  866  ? 21.178  30.734  101.340 1.00 20.23 ? 864  LEU   B CD2   1 
ATOM   15405 N  N     . LYS   B 1  867  ? 21.506  26.966  104.234 1.00 18.16 ? 865  LYS   B N     1 
ATOM   15406 C  CA    . LYS   B 1  867  ? 22.570  25.974  104.146 1.00 18.79 ? 865  LYS   B CA    1 
ATOM   15407 C  C     . LYS   B 1  867  ? 22.037  24.572  104.399 1.00 20.50 ? 865  LYS   B C     1 
ATOM   15408 O  O     . LYS   B 1  867  ? 22.438  23.619  103.720 1.00 19.47 ? 865  LYS   B O     1 
ATOM   15409 C  CB    . LYS   B 1  867  ? 23.715  26.356  105.085 1.00 20.40 ? 865  LYS   B CB    1 
ATOM   15410 C  CG    . LYS   B 1  867  ? 24.411  27.626  104.604 1.00 23.84 ? 865  LYS   B CG    1 
ATOM   15411 C  CD    . LYS   B 1  867  ? 25.346  28.200  105.642 1.00 23.09 ? 865  LYS   B CD    1 
ATOM   15412 C  CE    . LYS   B 1  867  ? 25.836  29.578  105.213 1.00 32.26 ? 865  LYS   B CE    1 
ATOM   15413 N  NZ    . LYS   B 1  867  ? 26.612  30.258  106.292 1.00 34.59 ? 865  LYS   B NZ    1 
ATOM   15414 N  N     . GLY   B 1  868  ? 21.096  24.431  105.337 1.00 18.58 ? 866  GLY   B N     1 
ATOM   15415 C  CA    . GLY   B 1  868  ? 20.493  23.127  105.561 1.00 18.46 ? 866  GLY   B CA    1 
ATOM   15416 C  C     . GLY   B 1  868  ? 19.719  22.644  104.352 1.00 19.19 ? 866  GLY   B C     1 
ATOM   15417 O  O     . GLY   B 1  868  ? 19.771  21.465  103.992 1.00 20.24 ? 866  GLY   B O     1 
ATOM   15418 N  N     . ALA   B 1  869  ? 18.987  23.550  103.705 1.00 18.16 ? 867  ALA   B N     1 
ATOM   15419 C  CA    . ALA   B 1  869  ? 18.263  23.186  102.494 1.00 19.69 ? 867  ALA   B CA    1 
ATOM   15420 C  C     . ALA   B 1  869  ? 19.224  22.845  101.358 1.00 16.36 ? 867  ALA   B C     1 
ATOM   15421 O  O     . ALA   B 1  869  ? 18.964  21.926  100.569 1.00 17.84 ? 867  ALA   B O     1 
ATOM   15422 C  CB    . ALA   B 1  869  ? 17.323  24.319  102.093 1.00 18.33 ? 867  ALA   B CB    1 
ATOM   15423 N  N     . LEU   B 1  870  ? 20.348  23.565  101.267 1.00 17.06 ? 868  LEU   B N     1 
ATOM   15424 C  CA    . LEU   B 1  870  ? 21.312  23.276  100.207 1.00 17.57 ? 868  LEU   B CA    1 
ATOM   15425 C  C     . LEU   B 1  870  ? 21.926  21.898  100.373 1.00 17.58 ? 868  LEU   B C     1 
ATOM   15426 O  O     . LEU   B 1  870  ? 22.268  21.251  99.383  1.00 19.62 ? 868  LEU   B O     1 
ATOM   15427 C  CB    . LEU   B 1  870  ? 22.423  24.325  100.175 1.00 19.39 ? 868  LEU   B CB    1 
ATOM   15428 C  CG    . LEU   B 1  870  ? 22.039  25.672  99.575  1.00 22.47 ? 868  LEU   B CG    1 
ATOM   15429 C  CD1   . LEU   B 1  870  ? 23.175  26.657  99.703  1.00 22.09 ? 868  LEU   B CD1   1 
ATOM   15430 C  CD2   . LEU   B 1  870  ? 21.682  25.481  98.104  1.00 22.54 ? 868  LEU   B CD2   1 
ATOM   15431 N  N     . HIS   B 1  871  ? 22.054  21.428  101.609 1.00 17.19 ? 869  HIS   B N     1 
ATOM   15432 C  CA    A HIS   B 1  871  ? 22.636  20.111  101.819 0.53 18.98 ? 869  HIS   B CA    1 
ATOM   15433 C  CA    B HIS   B 1  871  ? 22.620  20.108  101.859 0.47 18.98 ? 869  HIS   B CA    1 
ATOM   15434 C  C     . HIS   B 1  871  ? 21.750  18.999  101.288 1.00 20.44 ? 869  HIS   B C     1 
ATOM   15435 O  O     . HIS   B 1  871  ? 22.229  17.877  101.105 1.00 22.65 ? 869  HIS   B O     1 
ATOM   15436 C  CB    A HIS   B 1  871  ? 22.970  19.891  103.294 0.53 19.73 ? 869  HIS   B CB    1 
ATOM   15437 C  CB    B HIS   B 1  871  ? 22.813  19.912  103.367 0.47 19.77 ? 869  HIS   B CB    1 
ATOM   15438 C  CG    A HIS   B 1  871  ? 24.299  20.449  103.696 0.53 22.87 ? 869  HIS   B CG    1 
ATOM   15439 C  CG    B HIS   B 1  871  ? 23.368  18.572  103.741 0.47 23.46 ? 869  HIS   B CG    1 
ATOM   15440 N  ND1   A HIS   B 1  871  ? 24.437  21.672  104.315 0.53 23.77 ? 869  HIS   B ND1   1 
ATOM   15441 N  ND1   B HIS   B 1  871  ? 24.716  18.288  103.710 0.47 27.34 ? 869  HIS   B ND1   1 
ATOM   15442 C  CD2   A HIS   B 1  871  ? 25.552  19.953  103.556 0.53 26.80 ? 869  HIS   B CD2   1 
ATOM   15443 C  CD2   B HIS   B 1  871  ? 22.753  17.436  104.148 0.47 25.04 ? 869  HIS   B CD2   1 
ATOM   15444 C  CE1   A HIS   B 1  871  ? 25.716  21.903  104.545 0.53 27.07 ? 869  HIS   B CE1   1 
ATOM   15445 C  CE1   B HIS   B 1  871  ? 24.909  17.037  104.088 0.47 23.53 ? 869  HIS   B CE1   1 
ATOM   15446 N  NE2   A HIS   B 1  871  ? 26.414  20.878  104.088 0.53 24.07 ? 869  HIS   B NE2   1 
ATOM   15447 N  NE2   B HIS   B 1  871  ? 23.734  16.497  104.356 0.47 25.69 ? 869  HIS   B NE2   1 
ATOM   15448 N  N     . GLU   B 1  872  ? 20.490  19.288  101.005 1.00 17.20 ? 870  GLU   B N     1 
ATOM   15449 C  CA    . GLU   B 1  872  ? 19.572  18.283  100.492 1.00 18.40 ? 870  GLU   B CA    1 
ATOM   15450 C  C     . GLU   B 1  872  ? 19.504  18.244  98.977  1.00 18.01 ? 870  GLU   B C     1 
ATOM   15451 O  O     . GLU   B 1  872  ? 18.744  17.438  98.427  1.00 19.95 ? 870  GLU   B O     1 
ATOM   15452 C  CB    . GLU   B 1  872  ? 18.175  18.519  101.063 1.00 18.08 ? 870  GLU   B CB    1 
ATOM   15453 C  CG    . GLU   B 1  872  ? 18.173  18.547  102.569 1.00 19.10 ? 870  GLU   B CG    1 
ATOM   15454 C  CD    . GLU   B 1  872  ? 18.578  17.216  103.159 1.00 21.70 ? 870  GLU   B CD    1 
ATOM   15455 O  OE1   . GLU   B 1  872  ? 18.376  16.183  102.482 1.00 23.91 ? 870  GLU   B OE1   1 
ATOM   15456 O  OE2   . GLU   B 1  872  ? 19.090  17.186  104.299 1.00 22.88 ? 870  GLU   B OE2   1 
ATOM   15457 N  N     . LEU   B 1  873  ? 20.267  19.089  98.293  1.00 18.88 ? 871  LEU   B N     1 
ATOM   15458 C  CA    . LEU   B 1  873  ? 20.221  19.117  96.841  1.00 18.55 ? 871  LEU   B CA    1 
ATOM   15459 C  C     . LEU   B 1  873  ? 21.117  18.040  96.256  1.00 19.94 ? 871  LEU   B C     1 
ATOM   15460 O  O     . LEU   B 1  873  ? 22.184  17.726  96.788  1.00 21.12 ? 871  LEU   B O     1 
ATOM   15461 C  CB    . LEU   B 1  873  ? 20.685  20.469  96.322  1.00 19.35 ? 871  LEU   B CB    1 
ATOM   15462 C  CG    . LEU   B 1  873  ? 19.784  21.636  96.703  1.00 21.74 ? 871  LEU   B CG    1 
ATOM   15463 C  CD1   . LEU   B 1  873  ? 20.214  22.842  95.891  1.00 23.18 ? 871  LEU   B CD1   1 
ATOM   15464 C  CD2   . LEU   B 1  873  ? 18.305  21.324  96.495  1.00 20.76 ? 871  LEU   B CD2   1 
ATOM   15465 N  N     . HIS   B 1  874  ? 20.678  17.490  95.137  1.00 18.65 ? 872  HIS   B N     1 
ATOM   15466 C  CA    . HIS   B 1  874  ? 21.439  16.505  94.391  1.00 20.44 ? 872  HIS   B CA    1 
ATOM   15467 C  C     . HIS   B 1  874  ? 22.010  17.206  93.159  1.00 18.64 ? 872  HIS   B C     1 
ATOM   15468 O  O     . HIS   B 1  874  ? 21.253  17.744  92.339  1.00 17.99 ? 872  HIS   B O     1 
ATOM   15469 C  CB    . HIS   B 1  874  ? 20.499  15.360  94.014  1.00 21.71 ? 872  HIS   B CB    1 
ATOM   15470 C  CG    . HIS   B 1  874  ? 21.146  14.255  93.246  1.00 20.58 ? 872  HIS   B CG    1 
ATOM   15471 N  ND1   . HIS   B 1  874  ? 20.451  13.135  92.844  1.00 27.71 ? 872  HIS   B ND1   1 
ATOM   15472 C  CD2   . HIS   B 1  874  ? 22.409  14.105  92.782  1.00 25.71 ? 872  HIS   B CD2   1 
ATOM   15473 C  CE1   . HIS   B 1  874  ? 21.263  12.336  92.173  1.00 27.88 ? 872  HIS   B CE1   1 
ATOM   15474 N  NE2   . HIS   B 1  874  ? 22.456  12.902  92.120  1.00 27.54 ? 872  HIS   B NE2   1 
ATOM   15475 N  N     . ILE   B 1  875  ? 23.337  17.242  93.068  1.00 18.66 ? 873  ILE   B N     1 
ATOM   15476 C  CA    . ILE   B 1  875  ? 24.056  17.839  91.948  1.00 18.78 ? 873  ILE   B CA    1 
ATOM   15477 C  C     . ILE   B 1  875  ? 24.550  16.697  91.084  1.00 20.14 ? 873  ILE   B C     1 
ATOM   15478 O  O     . ILE   B 1  875  ? 25.203  15.779  91.589  1.00 19.66 ? 873  ILE   B O     1 
ATOM   15479 C  CB    . ILE   B 1  875  ? 25.257  18.657  92.445  1.00 21.89 ? 873  ILE   B CB    1 
ATOM   15480 C  CG1   . ILE   B 1  875  ? 24.817  19.719  93.449  1.00 27.00 ? 873  ILE   B CG1   1 
ATOM   15481 C  CG2   . ILE   B 1  875  ? 26.004  19.271  91.259  1.00 21.55 ? 873  ILE   B CG2   1 
ATOM   15482 C  CD1   . ILE   B 1  875  ? 25.946  20.187  94.345  1.00 30.31 ? 873  ILE   B CD1   1 
ATOM   15483 N  N     . GLY   B 1  876  ? 24.268  16.748  89.789  1.00 17.07 ? 874  GLY   B N     1 
ATOM   15484 C  CA    . GLY   B 1  876  ? 24.782  15.702  88.930  1.00 19.28 ? 874  GLY   B CA    1 
ATOM   15485 C  C     . GLY   B 1  876  ? 24.289  15.841  87.510  1.00 17.36 ? 874  GLY   B C     1 
ATOM   15486 O  O     . GLY   B 1  876  ? 23.688  16.846  87.130  1.00 17.41 ? 874  GLY   B O     1 
ATOM   15487 N  N     . ARG   B 1  877  ? 24.559  14.800  86.732  1.00 19.18 ? 875  ARG   B N     1 
ATOM   15488 C  CA    . ARG   B 1  877  ? 24.076  14.752  85.367  1.00 18.61 ? 875  ARG   B CA    1 
ATOM   15489 C  C     . ARG   B 1  877  ? 22.555  14.734  85.394  1.00 18.84 ? 875  ARG   B C     1 
ATOM   15490 O  O     . ARG   B 1  877  ? 21.945  14.035  86.203  1.00 19.95 ? 875  ARG   B O     1 
ATOM   15491 C  CB    . ARG   B 1  877  ? 24.618  13.493  84.700  1.00 20.75 ? 875  ARG   B CB    1 
ATOM   15492 C  CG    . ARG   B 1  877  ? 24.548  13.546  83.207  1.00 22.44 ? 875  ARG   B CG    1 
ATOM   15493 C  CD    . ARG   B 1  877  ? 25.196  12.315  82.619  1.00 27.17 ? 875  ARG   B CD    1 
ATOM   15494 N  NE    . ARG   B 1  877  ? 24.298  11.174  82.557  1.00 24.24 ? 875  ARG   B NE    1 
ATOM   15495 C  CZ    . ARG   B 1  877  ? 24.609  10.035  81.957  1.00 32.58 ? 875  ARG   B CZ    1 
ATOM   15496 N  NH1   . ARG   B 1  877  ? 25.816  9.832   81.451  1.00 29.18 ? 875  ARG   B NH1   1 
ATOM   15497 N  NH2   . ARG   B 1  877  ? 23.686  9.082   81.851  1.00 32.62 ? 875  ARG   B NH2   1 
ATOM   15498 N  N     . THR   B 1  878  ? 21.937  15.516  84.509  1.00 16.27 ? 876  THR   B N     1 
ATOM   15499 C  CA    . THR   B 1  878  ? 20.542  15.904  84.696  1.00 18.18 ? 876  THR   B CA    1 
ATOM   15500 C  C     . THR   B 1  878  ? 19.532  14.927  84.105  1.00 15.90 ? 876  THR   B C     1 
ATOM   15501 O  O     . THR   B 1  878  ? 18.332  15.216  84.118  1.00 17.58 ? 876  THR   B O     1 
ATOM   15502 C  CB    . THR   B 1  878  ? 20.311  17.297  84.130  1.00 18.60 ? 876  THR   B CB    1 
ATOM   15503 O  OG1   . THR   B 1  878  ? 20.854  17.359  82.809  1.00 19.86 ? 876  THR   B OG1   1 
ATOM   15504 C  CG2   . THR   B 1  878  ? 20.988  18.324  84.996  1.00 20.99 ? 876  THR   B CG2   1 
ATOM   15505 N  N     . ASP   B 1  879  ? 19.970  13.770  83.628  1.00 16.93 ? 877  ASP   B N     1 
ATOM   15506 C  CA    . ASP   B 1  879  ? 19.059  12.780  83.072  1.00 17.22 ? 877  ASP   B CA    1 
ATOM   15507 C  C     . ASP   B 1  879  ? 18.459  11.875  84.136  1.00 18.36 ? 877  ASP   B C     1 
ATOM   15508 O  O     . ASP   B 1  879  ? 18.078  10.739  83.840  1.00 19.66 ? 877  ASP   B O     1 
ATOM   15509 C  CB    . ASP   B 1  879  ? 19.734  11.977  81.959  1.00 20.92 ? 877  ASP   B CB    1 
ATOM   15510 C  CG    . ASP   B 1  879  ? 20.896  11.143  82.460  1.00 24.84 ? 877  ASP   B CG    1 
ATOM   15511 O  OD1   . ASP   B 1  879  ? 21.589  11.570  83.409  1.00 26.53 ? 877  ASP   B OD1   1 
ATOM   15512 O  OD2   . ASP   B 1  879  ? 21.106  10.049  81.904  1.00 24.87 ? 877  ASP   B OD2   1 
ATOM   15513 N  N     . ARG   B 1  880  ? 18.376  12.356  85.373  1.00 18.84 ? 878  ARG   B N     1 
ATOM   15514 C  CA    . ARG   B 1  880  ? 17.670  11.682  86.455  1.00 18.94 ? 878  ARG   B CA    1 
ATOM   15515 C  C     . ARG   B 1  880  ? 16.751  12.704  87.098  1.00 17.83 ? 878  ARG   B C     1 
ATOM   15516 O  O     . ARG   B 1  880  ? 17.169  13.836  87.363  1.00 18.45 ? 878  ARG   B O     1 
ATOM   15517 C  CB    . ARG   B 1  880  ? 18.636  11.151  87.520  1.00 21.78 ? 878  ARG   B CB    1 
ATOM   15518 C  CG    . ARG   B 1  880  ? 19.466  9.946   87.118  1.00 29.12 ? 878  ARG   B CG    1 
ATOM   15519 C  CD    . ARG   B 1  880  ? 20.421  9.562   88.248  1.00 33.87 ? 878  ARG   B CD    1 
ATOM   15520 N  NE    . ARG   B 1  880  ? 21.368  8.531   87.843  1.00 51.46 ? 878  ARG   B NE    1 
ATOM   15521 C  CZ    . ARG   B 1  880  ? 21.304  7.263   88.225  1.00 55.98 ? 878  ARG   B CZ    1 
ATOM   15522 N  NH1   . ARG   B 1  880  ? 20.365  6.838   89.057  1.00 56.58 ? 878  ARG   B NH1   1 
ATOM   15523 N  NH2   . ARG   B 1  880  ? 22.205  6.400   87.762  1.00 54.47 ? 878  ARG   B NH2   1 
ATOM   15524 N  N     . LEU   B 1  881  ? 15.504  12.300  87.349  1.00 17.68 ? 879  LEU   B N     1 
ATOM   15525 C  CA    . LEU   B 1  881  ? 14.537  13.202  87.960  1.00 17.73 ? 879  LEU   B CA    1 
ATOM   15526 C  C     . LEU   B 1  881  ? 15.000  13.680  89.330  1.00 16.90 ? 879  LEU   B C     1 
ATOM   15527 O  O     . LEU   B 1  881  ? 14.675  14.799  89.741  1.00 18.49 ? 879  LEU   B O     1 
ATOM   15528 C  CB    . LEU   B 1  881  ? 13.201  12.478  88.073  1.00 18.89 ? 879  LEU   B CB    1 
ATOM   15529 C  CG    . LEU   B 1  881  ? 12.039  13.265  88.675  1.00 21.45 ? 879  LEU   B CG    1 
ATOM   15530 C  CD1   . LEU   B 1  881  ? 11.654  14.411  87.767  1.00 21.35 ? 879  LEU   B CD1   1 
ATOM   15531 C  CD2   . LEU   B 1  881  ? 10.860  12.329  88.903  1.00 21.08 ? 879  LEU   B CD2   1 
ATOM   15532 N  N     . SER   B 1  882  ? 15.772  12.864  90.036  1.00 15.61 ? 880  SER   B N     1 
ATOM   15533 C  CA    . SER   B 1  882  ? 16.243  13.234  91.360  1.00 16.67 ? 880  SER   B CA    1 
ATOM   15534 C  C     . SER   B 1  882  ? 17.327  14.306  91.340  1.00 19.20 ? 880  SER   B C     1 
ATOM   15535 O  O     . SER   B 1  882  ? 17.741  14.743  92.414  1.00 18.81 ? 880  SER   B O     1 
ATOM   15536 C  CB    . SER   B 1  882  ? 16.787  11.996  92.073  1.00 19.12 ? 880  SER   B CB    1 
ATOM   15537 O  OG    . SER   B 1  882  ? 17.988  11.568  91.452  1.00 23.04 ? 880  SER   B OG    1 
ATOM   15538 N  N     . VAL   B 1  883  ? 17.818  14.738  90.184  1.00 18.32 ? 881  VAL   B N     1 
ATOM   15539 C  CA    . VAL   B 1  883  ? 18.874  15.744  90.158  1.00 17.23 ? 881  VAL   B CA    1 
ATOM   15540 C  C     . VAL   B 1  883  ? 18.265  17.136  90.237  1.00 18.57 ? 881  VAL   B C     1 
ATOM   15541 O  O     . VAL   B 1  883  ? 17.338  17.466  89.490  1.00 20.83 ? 881  VAL   B O     1 
ATOM   15542 C  CB    . VAL   B 1  883  ? 19.769  15.585  88.921  1.00 17.31 ? 881  VAL   B CB    1 
ATOM   15543 C  CG1   . VAL   B 1  883  ? 20.709  16.784  88.791  1.00 20.53 ? 881  VAL   B CG1   1 
ATOM   15544 C  CG2   . VAL   B 1  883  ? 20.566  14.315  89.058  1.00 20.20 ? 881  VAL   B CG2   1 
ATOM   15545 N  N     . ASP   B 1  884  ? 18.786  17.949  91.149  1.00 16.83 ? 882  ASP   B N     1 
ATOM   15546 C  CA    . ASP   B 1  884  ? 18.318  19.309  91.371  1.00 17.15 ? 882  ASP   B CA    1 
ATOM   15547 C  C     . ASP   B 1  884  ? 19.164  20.356  90.668  1.00 21.52 ? 882  ASP   B C     1 
ATOM   15548 O  O     . ASP   B 1  884  ? 18.616  21.320  90.129  1.00 24.42 ? 882  ASP   B O     1 
ATOM   15549 C  CB    . ASP   B 1  884  ? 18.329  19.602  92.867  1.00 18.57 ? 882  ASP   B CB    1 
ATOM   15550 C  CG    . ASP   B 1  884  ? 17.464  18.645  93.629  1.00 20.02 ? 882  ASP   B CG    1 
ATOM   15551 O  OD1   . ASP   B 1  884  ? 16.266  18.539  93.283  1.00 19.88 ? 882  ASP   B OD1   1 
ATOM   15552 O  OD2   . ASP   B 1  884  ? 17.976  17.971  94.537  1.00 19.38 ? 882  ASP   B OD2   1 
ATOM   15553 N  N     . VAL   B 1  885  ? 20.484  20.188  90.678  1.00 18.81 ? 883  VAL   B N     1 
ATOM   15554 C  CA    . VAL   B 1  885  ? 21.422  21.162  90.133  1.00 19.74 ? 883  VAL   B CA    1 
ATOM   15555 C  C     . VAL   B 1  885  ? 22.289  20.438  89.116  1.00 16.93 ? 883  VAL   B C     1 
ATOM   15556 O  O     . VAL   B 1  885  ? 22.952  19.447  89.451  1.00 18.03 ? 883  VAL   B O     1 
ATOM   15557 C  CB    . VAL   B 1  885  ? 22.287  21.787  91.238  1.00 19.31 ? 883  VAL   B CB    1 
ATOM   15558 C  CG1   . VAL   B 1  885  ? 23.246  22.820  90.651  1.00 21.25 ? 883  VAL   B CG1   1 
ATOM   15559 C  CG2   . VAL   B 1  885  ? 21.402  22.421  92.315  1.00 24.48 ? 883  VAL   B CG2   1 
ATOM   15560 N  N     . GLY   B 1  886  ? 22.297  20.946  87.885  1.00 18.08 ? 884  GLY   B N     1 
ATOM   15561 C  CA    . GLY   B 1  886  ? 23.107  20.389  86.831  1.00 17.49 ? 884  GLY   B CA    1 
ATOM   15562 C  C     . GLY   B 1  886  ? 24.459  21.050  86.711  1.00 16.38 ? 884  GLY   B C     1 
ATOM   15563 O  O     . GLY   B 1  886  ? 24.895  21.805  87.579  1.00 17.69 ? 884  GLY   B O     1 
ATOM   15564 N  N     . PRO   B 1  887  ? 25.142  20.773  85.607  1.00 15.53 ? 885  PRO   B N     1 
ATOM   15565 C  CA    . PRO   B 1  887  ? 26.506  21.264  85.408  1.00 15.09 ? 885  PRO   B CA    1 
ATOM   15566 C  C     . PRO   B 1  887  ? 26.518  22.710  84.937  1.00 14.73 ? 885  PRO   B C     1 
ATOM   15567 O  O     . PRO   B 1  887  ? 25.519  23.264  84.484  1.00 15.42 ? 885  PRO   B O     1 
ATOM   15568 C  CB    . PRO   B 1  887  ? 27.011  20.362  84.278  1.00 15.12 ? 885  PRO   B CB    1 
ATOM   15569 C  CG    . PRO   B 1  887  ? 25.769  20.039  83.500  1.00 15.98 ? 885  PRO   B CG    1 
ATOM   15570 C  CD    . PRO   B 1  887  ? 24.711  19.852  84.545  1.00 16.04 ? 885  PRO   B CD    1 
ATOM   15571 N  N     . VAL   B 1  888  ? 27.694  23.300  85.015  1.00 15.65 ? 886  VAL   B N     1 
ATOM   15572 C  CA    . VAL   B 1  888  ? 27.947  24.521  84.269  1.00 16.21 ? 886  VAL   B CA    1 
ATOM   15573 C  C     . VAL   B 1  888  ? 28.317  24.146  82.837  1.00 17.71 ? 886  VAL   B C     1 
ATOM   15574 O  O     . VAL   B 1  888  ? 28.739  23.022  82.552  1.00 16.89 ? 886  VAL   B O     1 
ATOM   15575 C  CB    . VAL   B 1  888  ? 29.010  25.409  84.939  1.00 19.10 ? 886  VAL   B CB    1 
ATOM   15576 C  CG1   . VAL   B 1  888  ? 28.535  25.806  86.344  1.00 18.66 ? 886  VAL   B CG1   1 
ATOM   15577 C  CG2   . VAL   B 1  888  ? 30.343  24.716  85.005  1.00 25.69 ? 886  VAL   B CG2   1 
ATOM   15578 N  N     . ILE   B 1  889  ? 28.094  25.078  81.915  1.00 16.79 ? 887  ILE   B N     1 
ATOM   15579 C  CA    . ILE   B 1  889  ? 27.997  24.684  80.510  1.00 16.02 ? 887  ILE   B CA    1 
ATOM   15580 C  C     . ILE   B 1  889  ? 29.338  24.215  79.944  1.00 16.54 ? 887  ILE   B C     1 
ATOM   15581 O  O     . ILE   B 1  889  ? 29.375  23.319  79.094  1.00 16.51 ? 887  ILE   B O     1 
ATOM   15582 C  CB    . ILE   B 1  889  ? 27.353  25.805  79.676  1.00 16.77 ? 887  ILE   B CB    1 
ATOM   15583 C  CG1   . ILE   B 1  889  ? 27.095  25.339  78.236  1.00 16.94 ? 887  ILE   B CG1   1 
ATOM   15584 C  CG2   . ILE   B 1  889  ? 28.209  27.074  79.710  1.00 17.94 ? 887  ILE   B CG2   1 
ATOM   15585 C  CD1   . ILE   B 1  889  ? 26.140  24.186  78.129  1.00 16.02 ? 887  ILE   B CD1   1 
ATOM   15586 N  N     . THR   B 1  890  ? 30.447  24.819  80.364  1.00 16.09 ? 888  THR   B N     1 
ATOM   15587 C  CA    . THR   B 1  890  ? 31.741  24.488  79.784  1.00 16.91 ? 888  THR   B CA    1 
ATOM   15588 C  C     . THR   B 1  890  ? 32.810  24.605  80.848  1.00 17.45 ? 888  THR   B C     1 
ATOM   15589 O  O     . THR   B 1  890  ? 32.609  25.206  81.907  1.00 17.74 ? 888  THR   B O     1 
ATOM   15590 C  CB    . THR   B 1  890  ? 32.167  25.467  78.677  1.00 20.08 ? 888  THR   B CB    1 
ATOM   15591 O  OG1   . THR   B 1  890  ? 32.195  26.801  79.198  1.00 19.82 ? 888  THR   B OG1   1 
ATOM   15592 C  CG2   . THR   B 1  890  ? 31.238  25.398  77.466  1.00 18.73 ? 888  THR   B CG2   1 
ATOM   15593 N  N     . SER   B 1  891  ? 33.971  24.042  80.529  1.00 19.22 ? 889  SER   B N     1 
ATOM   15594 C  CA    A SER   B 1  891  ? 35.127  24.197  81.405  0.34 18.16 ? 889  SER   B CA    1 
ATOM   15595 C  CA    B SER   B 1  891  ? 35.118  24.197  81.415  0.41 18.15 ? 889  SER   B CA    1 
ATOM   15596 C  CA    C SER   B 1  891  ? 35.120  24.197  81.412  0.25 18.18 ? 889  SER   B CA    1 
ATOM   15597 C  C     . SER   B 1  891  ? 35.533  25.659  81.514  1.00 18.91 ? 889  SER   B C     1 
ATOM   15598 O  O     . SER   B 1  891  ? 35.944  26.120  82.583  1.00 19.29 ? 889  SER   B O     1 
ATOM   15599 C  CB    A SER   B 1  891  ? 36.294  23.365  80.877  0.34 19.66 ? 889  SER   B CB    1 
ATOM   15600 C  CB    B SER   B 1  891  ? 36.280  23.328  80.933  0.41 19.66 ? 889  SER   B CB    1 
ATOM   15601 C  CB    C SER   B 1  891  ? 36.281  23.334  80.918  0.25 19.67 ? 889  SER   B CB    1 
ATOM   15602 O  OG    A SER   B 1  891  ? 35.974  21.989  80.871  0.34 21.10 ? 889  SER   B OG    1 
ATOM   15603 O  OG    B SER   B 1  891  ? 36.823  23.830  79.726  0.41 20.10 ? 889  SER   B OG    1 
ATOM   15604 O  OG    C SER   B 1  891  ? 37.353  23.343  81.845  0.25 21.52 ? 889  SER   B OG    1 
ATOM   15605 N  N     . GLU   B 1  892  ? 35.422  26.404  80.411  1.00 17.77 ? 890  GLU   B N     1 
ATOM   15606 C  CA    . GLU   B 1  892  ? 35.751  27.825  80.448  1.00 19.06 ? 890  GLU   B CA    1 
ATOM   15607 C  C     . GLU   B 1  892  ? 34.838  28.562  81.413  1.00 18.95 ? 890  GLU   B C     1 
ATOM   15608 O  O     . GLU   B 1  892  ? 35.300  29.401  82.195  1.00 20.54 ? 890  GLU   B O     1 
ATOM   15609 C  CB    . GLU   B 1  892  ? 35.627  28.439  79.051  1.00 22.17 ? 890  GLU   B CB    1 
ATOM   15610 N  N     . ALA   B 1  893  ? 33.541  28.258  81.380  1.00 18.14 ? 891  ALA   B N     1 
ATOM   15611 C  CA    . ALA   B 1  893  ? 32.626  28.899  82.314  1.00 18.20 ? 891  ALA   B CA    1 
ATOM   15612 C  C     . ALA   B 1  893  ? 32.973  28.514  83.741  1.00 17.59 ? 891  ALA   B C     1 
ATOM   15613 O  O     . ALA   B 1  893  ? 32.988  29.368  84.634  1.00 19.04 ? 891  ALA   B O     1 
ATOM   15614 C  CB    . ALA   B 1  893  ? 31.184  28.512  81.987  1.00 20.57 ? 891  ALA   B CB    1 
ATOM   15615 N  N     . LYS   B 1  894  ? 33.275  27.235  83.965  1.00 17.21 ? 892  LYS   B N     1 
ATOM   15616 C  CA    . LYS   B 1  894  ? 33.667  26.781  85.294  1.00 18.90 ? 892  LYS   B CA    1 
ATOM   15617 C  C     . LYS   B 1  894  ? 34.898  27.529  85.793  1.00 18.30 ? 892  LYS   B C     1 
ATOM   15618 O  O     . LYS   B 1  894  ? 34.929  28.013  86.930  1.00 19.43 ? 892  LYS   B O     1 
ATOM   15619 C  CB    . LYS   B 1  894  ? 33.930  25.283  85.253  1.00 19.43 ? 892  LYS   B CB    1 
ATOM   15620 C  CG    . LYS   B 1  894  ? 34.395  24.704  86.561  1.00 19.01 ? 892  LYS   B CG    1 
ATOM   15621 C  CD    . LYS   B 1  894  ? 34.592  23.208  86.404  1.00 24.64 ? 892  LYS   B CD    1 
ATOM   15622 C  CE    . LYS   B 1  894  ? 35.493  22.648  87.490  1.00 32.21 ? 892  LYS   B CE    1 
ATOM   15623 N  NZ    . LYS   B 1  894  ? 34.723  22.134  88.639  1.00 36.28 ? 892  LYS   B NZ    1 
ATOM   15624 N  N     . ASP   B 1  895  ? 35.920  27.647  84.944  1.00 18.90 ? 893  ASP   B N     1 
ATOM   15625 C  CA    . ASP   B 1  895  ? 37.116  28.392  85.326  1.00 19.51 ? 893  ASP   B CA    1 
ATOM   15626 C  C     . ASP   B 1  895  ? 36.793  29.846  85.660  1.00 20.16 ? 893  ASP   B C     1 
ATOM   15627 O  O     . ASP   B 1  895  ? 37.385  30.427  86.578  1.00 21.29 ? 893  ASP   B O     1 
ATOM   15628 C  CB    . ASP   B 1  895  ? 38.130  28.354  84.186  1.00 21.51 ? 893  ASP   B CB    1 
ATOM   15629 C  CG    . ASP   B 1  895  ? 38.720  26.986  83.979  1.00 24.83 ? 893  ASP   B CG    1 
ATOM   15630 O  OD1   . ASP   B 1  895  ? 38.610  26.141  84.890  1.00 27.80 ? 893  ASP   B OD1   1 
ATOM   15631 O  OD2   . ASP   B 1  895  ? 39.309  26.771  82.899  1.00 27.34 ? 893  ASP   B OD2   1 
ATOM   15632 N  N     . ASN   B 1  896  ? 35.899  30.464  84.888  1.00 18.43 ? 894  ASN   B N     1 
ATOM   15633 C  CA    . ASN   B 1  896  ? 35.555  31.859  85.112  1.00 18.96 ? 894  ASN   B CA    1 
ATOM   15634 C  C     . ASN   B 1  896  ? 34.871  32.023  86.464  1.00 20.61 ? 894  ASN   B C     1 
ATOM   15635 O  O     . ASN   B 1  896  ? 35.200  32.931  87.239  1.00 19.90 ? 894  ASN   B O     1 
ATOM   15636 C  CB    . ASN   B 1  896  ? 34.637  32.302  83.973  1.00 20.22 ? 894  ASN   B CB    1 
ATOM   15637 C  CG    . ASN   B 1  896  ? 34.191  33.743  84.092  1.00 30.48 ? 894  ASN   B CG    1 
ATOM   15638 O  OD1   . ASN   B 1  896  ? 33.510  34.118  85.041  1.00 32.72 ? 894  ASN   B OD1   1 
ATOM   15639 N  ND2   . ASN   B 1  896  ? 34.538  34.551  83.099  1.00 41.86 ? 894  ASN   B ND2   1 
ATOM   15640 N  N     . ILE   B 1  897  ? 33.934  31.130  86.768  1.00 18.38 ? 895  ILE   B N     1 
ATOM   15641 C  CA    . ILE   B 1  897  ? 33.251  31.160  88.055  1.00 18.56 ? 895  ILE   B CA    1 
ATOM   15642 C  C     . ILE   B 1  897  ? 34.243  30.909  89.178  1.00 18.26 ? 895  ILE   B C     1 
ATOM   15643 O  O     . ILE   B 1  897  ? 34.258  31.617  90.193  1.00 19.12 ? 895  ILE   B O     1 
ATOM   15644 C  CB    . ILE   B 1  897  ? 32.133  30.107  88.062  1.00 18.23 ? 895  ILE   B CB    1 
ATOM   15645 C  CG1   . ILE   B 1  897  ? 31.067  30.454  87.024  1.00 17.20 ? 895  ILE   B CG1   1 
ATOM   15646 C  CG2   . ILE   B 1  897  ? 31.552  29.959  89.463  1.00 19.13 ? 895  ILE   B CG2   1 
ATOM   15647 C  CD1   . ILE   B 1  897  ? 30.254  29.248  86.596  1.00 17.61 ? 895  ILE   B CD1   1 
ATOM   15648 N  N     . GLU   B 1  898  ? 35.095  29.899  89.008  1.00 18.44 ? 896  GLU   B N     1 
ATOM   15649 C  CA    . GLU   B 1  898  ? 36.037  29.572  90.069  1.00 17.55 ? 896  GLU   B CA    1 
ATOM   15650 C  C     . GLU   B 1  898  ? 37.050  30.686  90.284  1.00 17.89 ? 896  GLU   B C     1 
ATOM   15651 O  O     . GLU   B 1  898  ? 37.496  30.903  91.418  1.00 19.82 ? 896  GLU   B O     1 
ATOM   15652 C  CB    . GLU   B 1  898  ? 36.705  28.227  89.795  1.00 21.36 ? 896  GLU   B CB    1 
ATOM   15653 C  CG    . GLU   B 1  898  ? 35.705  27.094  89.961  1.00 21.90 ? 896  GLU   B CG    1 
ATOM   15654 C  CD    . GLU   B 1  898  ? 36.280  25.733  89.648  1.00 30.75 ? 896  GLU   B CD    1 
ATOM   15655 O  OE1   . GLU   B 1  898  ? 37.366  25.673  89.042  1.00 32.68 ? 896  GLU   B OE1   1 
ATOM   15656 O  OE2   . GLU   B 1  898  ? 35.639  24.725  90.015  1.00 36.33 ? 896  GLU   B OE2   1 
ATOM   15657 N  N     . LYS   B 1  899  ? 37.418  31.408  89.223  1.00 18.23 ? 897  LYS   B N     1 
ATOM   15658 C  CA    . LYS   B 1  899  ? 38.325  32.535  89.394  1.00 20.76 ? 897  LYS   B CA    1 
ATOM   15659 C  C     . LYS   B 1  899  ? 37.710  33.575  90.310  1.00 18.54 ? 897  LYS   B C     1 
ATOM   15660 O  O     . LYS   B 1  899  ? 38.389  34.121  91.189  1.00 19.11 ? 897  LYS   B O     1 
ATOM   15661 C  CB    . LYS   B 1  899  ? 38.666  33.157  88.042  1.00 22.21 ? 897  LYS   B CB    1 
ATOM   15662 C  CG    . LYS   B 1  899  ? 39.617  34.332  88.171  1.00 23.84 ? 897  LYS   B CG    1 
ATOM   15663 C  CD    . LYS   B 1  899  ? 40.196  34.751  86.830  1.00 32.97 ? 897  LYS   B CD    1 
ATOM   15664 C  CE    . LYS   B 1  899  ? 39.296  35.731  86.106  1.00 36.66 ? 897  LYS   B CE    1 
ATOM   15665 N  NZ    . LYS   B 1  899  ? 40.047  36.454  85.033  1.00 34.17 ? 897  LYS   B NZ    1 
ATOM   15666 N  N     . HIS   B 1  900  ? 36.411  33.816  90.158  1.00 18.68 ? 898  HIS   B N     1 
ATOM   15667 C  CA    . HIS   B 1  900  ? 35.737  34.767  91.025  1.00 18.46 ? 898  HIS   B CA    1 
ATOM   15668 C  C     . HIS   B 1  900  ? 35.700  34.259  92.459  1.00 18.20 ? 898  HIS   B C     1 
ATOM   15669 O  O     . HIS   B 1  900  ? 35.975  35.010  93.402  1.00 18.88 ? 898  HIS   B O     1 
ATOM   15670 C  CB    . HIS   B 1  900  ? 34.325  35.006  90.516  1.00 18.15 ? 898  HIS   B CB    1 
ATOM   15671 C  CG    . HIS   B 1  900  ? 33.482  35.741  91.495  1.00 17.73 ? 898  HIS   B CG    1 
ATOM   15672 N  ND1   . HIS   B 1  900  ? 33.672  37.075  91.776  1.00 21.78 ? 898  HIS   B ND1   1 
ATOM   15673 C  CD2   . HIS   B 1  900  ? 32.470  35.322  92.289  1.00 19.78 ? 898  HIS   B CD2   1 
ATOM   15674 C  CE1   . HIS   B 1  900  ? 32.791  37.455  92.686  1.00 19.65 ? 898  HIS   B CE1   1 
ATOM   15675 N  NE2   . HIS   B 1  900  ? 32.050  36.411  93.011  1.00 19.36 ? 898  HIS   B NE2   1 
ATOM   15676 N  N     . ILE   B 1  901  ? 35.348  32.987  92.640  1.00 18.54 ? 899  ILE   B N     1 
ATOM   15677 C  CA    . ILE   B 1  901  ? 35.270  32.418  93.984  1.00 18.46 ? 899  ILE   B CA    1 
ATOM   15678 C  C     . ILE   B 1  901  ? 36.620  32.520  94.675  1.00 18.93 ? 899  ILE   B C     1 
ATOM   15679 O  O     . ILE   B 1  901  ? 36.718  32.929  95.840  1.00 20.30 ? 899  ILE   B O     1 
ATOM   15680 C  CB    . ILE   B 1  901  ? 34.781  30.964  93.915  1.00 18.51 ? 899  ILE   B CB    1 
ATOM   15681 C  CG1   . ILE   B 1  901  ? 33.337  30.915  93.430  1.00 17.60 ? 899  ILE   B CG1   1 
ATOM   15682 C  CG2   . ILE   B 1  901  ? 34.892  30.308  95.275  1.00 19.35 ? 899  ILE   B CG2   1 
ATOM   15683 C  CD1   . ILE   B 1  901  ? 32.874  29.497  93.080  1.00 20.53 ? 899  ILE   B CD1   1 
ATOM   15684 N  N     . GLU   B 1  902  ? 37.689  32.183  93.952  1.00 21.27 ? 900  GLU   B N     1 
ATOM   15685 C  CA    . GLU   B 1  902  ? 39.017  32.231  94.549  1.00 21.81 ? 900  GLU   B CA    1 
ATOM   15686 C  C     . GLU   B 1  902  ? 39.468  33.665  94.769  1.00 19.56 ? 900  GLU   B C     1 
ATOM   15687 O  O     . GLU   B 1  902  ? 40.229  33.934  95.703  1.00 23.20 ? 900  GLU   B O     1 
ATOM   15688 C  CB    . GLU   B 1  902  ? 40.012  31.443  93.694  1.00 22.99 ? 900  GLU   B CB    1 
ATOM   15689 C  CG    . GLU   B 1  902  ? 39.734  29.933  93.657  1.00 30.05 ? 900  GLU   B CG    1 
ATOM   15690 C  CD    . GLU   B 1  902  ? 39.517  29.323  95.046  1.00 37.10 ? 900  GLU   B CD    1 
ATOM   15691 O  OE1   . GLU   B 1  902  ? 40.379  29.525  95.931  1.00 34.68 ? 900  GLU   B OE1   1 
ATOM   15692 O  OE2   . GLU   B 1  902  ? 38.480  28.647  95.249  1.00 35.89 ? 900  GLU   B OE2   1 
ATOM   15693 N  N     . ARG   B 1  903  ? 39.000  34.603  93.948  1.00 20.90 ? 901  ARG   B N     1 
ATOM   15694 C  CA    . ARG   B 1  903  ? 39.330  35.997  94.215  1.00 23.34 ? 901  ARG   B CA    1 
ATOM   15695 C  C     . ARG   B 1  903  ? 38.673  36.466  95.507  1.00 23.65 ? 901  ARG   B C     1 
ATOM   15696 O  O     . ARG   B 1  903  ? 39.311  37.133  96.333  1.00 24.51 ? 901  ARG   B O     1 
ATOM   15697 C  CB    . ARG   B 1  903  ? 38.913  36.880  93.039  1.00 24.91 ? 901  ARG   B CB    1 
ATOM   15698 C  CG    . ARG   B 1  903  ? 39.333  38.334  93.211  1.00 34.12 ? 901  ARG   B CG    1 
ATOM   15699 C  CD    . ARG   B 1  903  ? 38.968  39.181  92.000  1.00 37.53 ? 901  ARG   B CD    1 
ATOM   15700 N  NE    . ARG   B 1  903  ? 37.567  39.589  91.993  1.00 43.67 ? 901  ARG   B NE    1 
ATOM   15701 C  CZ    . ARG   B 1  903  ? 37.111  40.707  92.542  1.00 45.14 ? 901  ARG   B CZ    1 
ATOM   15702 N  NH1   . ARG   B 1  903  ? 37.911  41.531  93.195  1.00 44.03 ? 901  ARG   B NH1   1 
ATOM   15703 N  NH2   . ARG   B 1  903  ? 35.817  41.001  92.440  1.00 43.58 ? 901  ARG   B NH2   1 
ATOM   15704 N  N     . MET   B 1  904  ? 37.405  36.102  95.708  1.00 21.52 ? 902  MET   B N     1 
ATOM   15705 C  CA    . MET   B 1  904  ? 36.720  36.442  96.951  1.00 19.58 ? 902  MET   B CA    1 
ATOM   15706 C  C     . MET   B 1  904  ? 37.390  35.775  98.142  1.00 24.11 ? 902  MET   B C     1 
ATOM   15707 O  O     . MET   B 1  904  ? 37.586  36.403  99.190  1.00 24.23 ? 902  MET   B O     1 
ATOM   15708 C  CB    . MET   B 1  904  ? 35.252  36.031  96.859  1.00 22.19 ? 902  MET   B CB    1 
ATOM   15709 C  CG    . MET   B 1  904  ? 34.485  36.717  95.738  1.00 21.77 ? 902  MET   B CG    1 
ATOM   15710 S  SD    . MET   B 1  904  ? 34.303  38.475  96.079  1.00 31.78 ? 902  MET   B SD    1 
ATOM   15711 C  CE    . MET   B 1  904  ? 35.539  39.156  95.001  1.00 31.07 ? 902  MET   B CE    1 
ATOM   15712 N  N     . ARG   B 1  905  ? 37.741  34.501  98.002  1.00 22.28 ? 903  ARG   B N     1 
ATOM   15713 C  CA    . ARG   B 1  905  ? 38.411  33.810  99.094  1.00 24.45 ? 903  ARG   B CA    1 
ATOM   15714 C  C     . ARG   B 1  905  ? 39.730  34.487  99.436  1.00 26.31 ? 903  ARG   B C     1 
ATOM   15715 O  O     . ARG   B 1  905  ? 40.050  34.687  100.615 1.00 25.73 ? 903  ARG   B O     1 
ATOM   15716 C  CB    . ARG   B 1  905  ? 38.634  32.347  98.717  1.00 26.29 ? 903  ARG   B CB    1 
ATOM   15717 C  CG    . ARG   B 1  905  ? 38.746  31.422  99.902  1.00 33.33 ? 903  ARG   B CG    1 
ATOM   15718 C  CD    . ARG   B 1  905  ? 39.230  30.053  99.477  1.00 34.47 ? 903  ARG   B CD    1 
ATOM   15719 N  NE    . ARG   B 1  905  ? 38.404  29.455  98.435  1.00 32.55 ? 903  ARG   B NE    1 
ATOM   15720 C  CZ    . ARG   B 1  905  ? 37.325  28.715  98.657  1.00 28.50 ? 903  ARG   B CZ    1 
ATOM   15721 N  NH1   . ARG   B 1  905  ? 36.846  28.536  99.877  1.00 32.53 ? 903  ARG   B NH1   1 
ATOM   15722 N  NH2   . ARG   B 1  905  ? 36.720  28.128  97.628  1.00 31.32 ? 903  ARG   B NH2   1 
ATOM   15723 N  N     . GLY   B 1  906  ? 40.494  34.885  98.416  1.00 23.41 ? 904  GLY   B N     1 
ATOM   15724 C  CA    . GLY   B 1  906  ? 41.790  35.496  98.663  1.00 24.84 ? 904  GLY   B CA    1 
ATOM   15725 C  C     . GLY   B 1  906  ? 41.706  36.876  99.277  1.00 27.90 ? 904  GLY   B C     1 
ATOM   15726 O  O     . GLY   B 1  906  ? 42.656  37.303  99.944  1.00 30.84 ? 904  GLY   B O     1 
ATOM   15727 N  N     . LEU   B 1  907  ? 40.592  37.579  99.070  1.00 27.81 ? 905  LEU   B N     1 
ATOM   15728 C  CA    . LEU   B 1  907  ? 40.330  38.857  99.718  1.00 30.15 ? 905  LEU   B CA    1 
ATOM   15729 C  C     . LEU   B 1  907  ? 39.814  38.696  101.138 1.00 27.56 ? 905  LEU   B C     1 
ATOM   15730 O  O     . LEU   B 1  907  ? 39.575  39.705  101.810 1.00 29.01 ? 905  LEU   B O     1 
ATOM   15731 C  CB    . LEU   B 1  907  ? 39.336  39.675  98.894  1.00 31.75 ? 905  LEU   B CB    1 
ATOM   15732 C  CG    . LEU   B 1  907  ? 39.864  40.128  97.532  1.00 36.44 ? 905  LEU   B CG    1 
ATOM   15733 C  CD1   . LEU   B 1  907  ? 38.805  40.903  96.767  1.00 41.06 ? 905  LEU   B CD1   1 
ATOM   15734 C  CD2   . LEU   B 1  907  ? 41.124  40.952  97.699  1.00 36.50 ? 905  LEU   B CD2   1 
ATOM   15735 N  N     . GLY   B 1  908  ? 39.641  37.464  101.601 1.00 25.26 ? 906  GLY   B N     1 
ATOM   15736 C  CA    . GLY   B 1  908  ? 39.241  37.204  102.964 1.00 27.55 ? 906  GLY   B CA    1 
ATOM   15737 C  C     . GLY   B 1  908  ? 37.757  37.049  103.184 1.00 31.66 ? 906  GLY   B C     1 
ATOM   15738 O  O     . GLY   B 1  908  ? 37.331  36.933  104.339 1.00 26.57 ? 906  GLY   B O     1 
ATOM   15739 N  N     . ARG   B 1  909  ? 36.954  37.040  102.123 1.00 23.52 ? 907  ARG   B N     1 
ATOM   15740 C  CA    . ARG   B 1  909  ? 35.520  36.878  102.288 1.00 22.05 ? 907  ARG   B CA    1 
ATOM   15741 C  C     . ARG   B 1  909  ? 35.195  35.450  102.693 1.00 23.02 ? 907  ARG   B C     1 
ATOM   15742 O  O     . ARG   B 1  909  ? 35.856  34.492  102.284 1.00 26.71 ? 907  ARG   B O     1 
ATOM   15743 C  CB    . ARG   B 1  909  ? 34.792  37.158  100.980 1.00 23.31 ? 907  ARG   B CB    1 
ATOM   15744 C  CG    . ARG   B 1  909  ? 35.193  38.429  100.278 1.00 28.38 ? 907  ARG   B CG    1 
ATOM   15745 C  CD    . ARG   B 1  909  ? 34.736  39.668  100.999 1.00 39.64 ? 907  ARG   B CD    1 
ATOM   15746 N  NE    . ARG   B 1  909  ? 35.380  40.841  100.420 1.00 45.96 ? 907  ARG   B NE    1 
ATOM   15747 C  CZ    . ARG   B 1  909  ? 35.206  42.082  100.850 1.00 53.03 ? 907  ARG   B CZ    1 
ATOM   15748 N  NH1   . ARG   B 1  909  ? 34.380  42.357  101.846 1.00 59.38 ? 907  ARG   B NH1   1 
ATOM   15749 N  NH2   . ARG   B 1  909  ? 35.876  43.071  100.265 1.00 54.69 ? 907  ARG   B NH2   1 
ATOM   15750 N  N     . LYS   B 1  910  ? 34.137  35.305  103.472 1.00 22.53 ? 908  LYS   B N     1 
ATOM   15751 C  CA    . LYS   B 1  910  ? 33.687  33.975  103.843 1.00 23.41 ? 908  LYS   B CA    1 
ATOM   15752 C  C     . LYS   B 1  910  ? 33.063  33.302  102.625 1.00 21.99 ? 908  LYS   B C     1 
ATOM   15753 O  O     . LYS   B 1  910  ? 32.105  33.818  102.039 1.00 22.11 ? 908  LYS   B O     1 
ATOM   15754 C  CB    . LYS   B 1  910  ? 32.684  34.057  104.987 1.00 25.31 ? 908  LYS   B CB    1 
ATOM   15755 C  CG    . LYS   B 1  910  ? 32.349  32.702  105.580 1.00 30.50 ? 908  LYS   B CG    1 
ATOM   15756 C  CD    . LYS   B 1  910  ? 31.261  32.802  106.633 1.00 37.04 ? 908  LYS   B CD    1 
ATOM   15757 C  CE    . LYS   B 1  910  ? 31.037  31.454  107.300 1.00 46.71 ? 908  LYS   B CE    1 
ATOM   15758 N  NZ    . LYS   B 1  910  ? 29.737  31.391  108.024 1.00 45.43 ? 908  LYS   B NZ    1 
ATOM   15759 N  N     . VAL   B 1  911  ? 33.615  32.159  102.239 1.00 22.27 ? 909  VAL   B N     1 
ATOM   15760 C  CA    . VAL   B 1  911  ? 33.144  31.384  101.102 1.00 21.22 ? 909  VAL   B CA    1 
ATOM   15761 C  C     . VAL   B 1  911  ? 32.773  30.004  101.611 1.00 21.79 ? 909  VAL   B C     1 
ATOM   15762 O  O     . VAL   B 1  911  ? 33.588  29.337  102.264 1.00 22.89 ? 909  VAL   B O     1 
ATOM   15763 C  CB    . VAL   B 1  911  ? 34.231  31.284  100.020 1.00 19.65 ? 909  VAL   B CB    1 
ATOM   15764 C  CG1   . VAL   B 1  911  ? 33.780  30.372  98.879  1.00 21.21 ? 909  VAL   B CG1   1 
ATOM   15765 C  CG2   . VAL   B 1  911  ? 34.607  32.688  99.525  1.00 22.05 ? 909  VAL   B CG2   1 
ATOM   15766 N  N     . GLU   B 1  912  ? 31.549  29.585  101.332 1.00 19.64 ? 910  GLU   B N     1 
ATOM   15767 C  CA    . GLU   B 1  912  ? 31.089  28.252  101.682 1.00 19.31 ? 910  GLU   B CA    1 
ATOM   15768 C  C     . GLU   B 1  912  ? 30.539  27.568  100.446 1.00 21.68 ? 910  GLU   B C     1 
ATOM   15769 O  O     . GLU   B 1  912  ? 29.815  28.182  99.660  1.00 21.14 ? 910  GLU   B O     1 
ATOM   15770 C  CB    . GLU   B 1  912  ? 30.009  28.304  102.758 1.00 24.80 ? 910  GLU   B CB    1 
ATOM   15771 C  CG    . GLU   B 1  912  ? 30.499  28.910  104.068 1.00 30.61 ? 910  GLU   B CG    1 
ATOM   15772 C  CD    . GLU   B 1  912  ? 29.369  29.166  105.041 1.00 41.27 ? 910  GLU   B CD    1 
ATOM   15773 O  OE1   . GLU   B 1  912  ? 28.829  28.187  105.601 1.00 46.57 ? 910  GLU   B OE1   1 
ATOM   15774 O  OE2   . GLU   B 1  912  ? 29.010  30.347  105.231 1.00 46.60 ? 910  GLU   B OE2   1 
ATOM   15775 N  N     . GLN   B 1  913  ? 30.891  26.299  100.271 1.00 20.56 ? 911  GLN   B N     1 
ATOM   15776 C  CA    . GLN   B 1  913  ? 30.371  25.509  99.169  1.00 21.70 ? 911  GLN   B CA    1 
ATOM   15777 C  C     . GLN   B 1  913  ? 29.761  24.244  99.730  1.00 22.70 ? 911  GLN   B C     1 
ATOM   15778 O  O     . GLN   B 1  913  ? 30.321  23.618  100.634 1.00 26.42 ? 911  GLN   B O     1 
ATOM   15779 C  CB    . GLN   B 1  913  ? 31.467  25.166  98.155  1.00 22.47 ? 911  GLN   B CB    1 
ATOM   15780 C  CG    . GLN   B 1  913  ? 32.044  26.403  97.493  1.00 23.73 ? 911  GLN   B CG    1 
ATOM   15781 C  CD    . GLN   B 1  913  ? 33.015  26.064  96.389  1.00 26.78 ? 911  GLN   B CD    1 
ATOM   15782 O  OE1   . GLN   B 1  913  ? 34.024  25.407  96.624  1.00 32.39 ? 911  GLN   B OE1   1 
ATOM   15783 N  NE2   . GLN   B 1  913  ? 32.710  26.499  95.175  1.00 24.34 ? 911  GLN   B NE2   1 
ATOM   15784 N  N     . ILE   B 1  914  ? 28.598  23.886  99.216  1.00 23.47 ? 912  ILE   B N     1 
ATOM   15785 C  CA    . ILE   B 1  914  ? 27.865  22.728  99.701  1.00 30.69 ? 912  ILE   B CA    1 
ATOM   15786 C  C     . ILE   B 1  914  ? 27.778  21.793  98.506  1.00 31.69 ? 912  ILE   B C     1 
ATOM   15787 O  O     . ILE   B 1  914  ? 26.935  21.987  97.620  1.00 30.98 ? 912  ILE   B O     1 
ATOM   15788 C  CB    . ILE   B 1  914  ? 26.502  23.120  100.282 1.00 29.51 ? 912  ILE   B CB    1 
ATOM   15789 C  CG1   . ILE   B 1  914  ? 26.742  24.056  101.481 1.00 32.41 ? 912  ILE   B CG1   1 
ATOM   15790 C  CG2   . ILE   B 1  914  ? 25.724  21.890  100.706 1.00 30.75 ? 912  ILE   B CG2   1 
ATOM   15791 C  CD1   . ILE   B 1  914  ? 25.501  24.725  102.061 1.00 33.33 ? 912  ILE   B CD1   1 
ATOM   15792 N  N     . GLY   B 1  915  ? 28.667  20.791  98.485  1.00 45.39 ? 913  GLY   B N     1 
ATOM   15793 C  CA    . GLY   B 1  915  ? 29.312  20.301  97.276  1.00 49.46 ? 913  GLY   B CA    1 
ATOM   15794 C  C     . GLY   B 1  915  ? 28.751  19.006  96.719  1.00 48.21 ? 913  GLY   B C     1 
ATOM   15795 O  O     . GLY   B 1  915  ? 27.628  18.595  97.027  1.00 59.65 ? 913  GLY   B O     1 
ATOM   15796 N  N     . LEU   B 1  916  ? 29.561  18.347  95.883  1.00 58.86 ? 914  LEU   B N     1 
ATOM   15797 C  CA    . LEU   B 1  916  ? 29.078  17.316  94.971  1.00 54.51 ? 914  LEU   B CA    1 
ATOM   15798 C  C     . LEU   B 1  916  ? 29.890  16.030  95.084  1.00 62.65 ? 914  LEU   B C     1 
ATOM   15799 O  O     . LEU   B 1  916  ? 30.936  15.973  95.737  1.00 59.23 ? 914  LEU   B O     1 
ATOM   15800 C  CB    . LEU   B 1  916  ? 29.089  17.805  93.516  1.00 56.21 ? 914  LEU   B CB    1 
ATOM   15801 N  N     . ALA   B 1  917  ? 29.395  15.000  94.397  1.00 53.00 ? 915  ALA   B N     1 
ATOM   15802 C  CA    . ALA   B 1  917  ? 29.894  13.635  94.490  1.00 49.72 ? 915  ALA   B CA    1 
ATOM   15803 C  C     . ALA   B 1  917  ? 30.901  13.331  93.383  1.00 51.54 ? 915  ALA   B C     1 
ATOM   15804 O  O     . ALA   B 1  917  ? 31.140  14.134  92.477  1.00 44.60 ? 915  ALA   B O     1 
ATOM   15805 C  CB    . ALA   B 1  917  ? 28.728  12.641  94.422  1.00 55.21 ? 915  ALA   B CB    1 
ATOM   15806 N  N     . SER   B 1  918  ? 31.475  12.126  93.463  1.00 45.54 ? 916  SER   B N     1 
ATOM   15807 C  CA    . SER   B 1  918  ? 32.552  11.738  92.557  1.00 45.11 ? 916  SER   B CA    1 
ATOM   15808 C  C     . SER   B 1  918  ? 32.092  11.697  91.105  1.00 45.31 ? 916  SER   B C     1 
ATOM   15809 O  O     . SER   B 1  918  ? 32.872  12.013  90.198  1.00 41.22 ? 916  SER   B O     1 
ATOM   15810 C  CB    . SER   B 1  918  ? 33.122  10.381  92.976  1.00 39.73 ? 916  SER   B CB    1 
ATOM   15811 N  N     . GLU   B 1  919  ? 30.831  11.324  90.867  1.00 41.23 ? 917  GLU   B N     1 
ATOM   15812 C  CA    . GLU   B 1  919  ? 30.307  11.216  89.510  1.00 41.96 ? 917  GLU   B CA    1 
ATOM   15813 C  C     . GLU   B 1  919  ? 30.357  12.533  88.746  1.00 43.57 ? 917  GLU   B C     1 
ATOM   15814 O  O     . GLU   B 1  919  ? 30.215  12.521  87.518  1.00 36.26 ? 917  GLU   B O     1 
ATOM   15815 C  CB    . GLU   B 1  919  ? 28.875  10.680  89.540  1.00 37.54 ? 917  GLU   B CB    1 
ATOM   15816 N  N     . THR   B 1  920  ? 30.559  13.661  89.430  1.00 36.53 ? 918  THR   B N     1 
ATOM   15817 C  CA    . THR   B 1  920  ? 30.620  14.940  88.735  1.00 33.72 ? 918  THR   B CA    1 
ATOM   15818 C  C     . THR   B 1  920  ? 31.919  15.122  87.955  1.00 34.84 ? 918  THR   B C     1 
ATOM   15819 O  O     . THR   B 1  920  ? 31.941  15.912  87.008  1.00 32.14 ? 918  THR   B O     1 
ATOM   15820 C  CB    . THR   B 1  920  ? 30.417  16.103  89.714  1.00 40.34 ? 918  THR   B CB    1 
ATOM   15821 O  OG1   . THR   B 1  920  ? 31.421  16.063  90.738  1.00 35.82 ? 918  THR   B OG1   1 
ATOM   15822 C  CG2   . THR   B 1  920  ? 29.036  16.045  90.350  1.00 29.94 ? 918  THR   B CG2   1 
ATOM   15823 N  N     . GLY   B 1  921  ? 32.986  14.398  88.317  1.00 35.27 ? 919  GLY   B N     1 
ATOM   15824 C  CA    . GLY   B 1  921  ? 34.299  14.604  87.718  1.00 35.78 ? 919  GLY   B CA    1 
ATOM   15825 C  C     . GLY   B 1  921  ? 34.354  14.395  86.215  1.00 35.40 ? 919  GLY   B C     1 
ATOM   15826 O  O     . GLY   B 1  921  ? 35.308  14.843  85.568  1.00 39.06 ? 919  GLY   B O     1 
ATOM   15827 N  N     . VAL   B 1  922  ? 33.359  13.716  85.644  1.00 23.68 ? 920  VAL   B N     1 
ATOM   15828 C  CA    . VAL   B 1  922  ? 33.295  13.528  84.195  1.00 21.43 ? 920  VAL   B CA    1 
ATOM   15829 C  C     . VAL   B 1  922  ? 32.645  14.699  83.472  1.00 22.58 ? 920  VAL   B C     1 
ATOM   15830 O  O     . VAL   B 1  922  ? 32.699  14.756  82.232  1.00 22.55 ? 920  VAL   B O     1 
ATOM   15831 C  CB    . VAL   B 1  922  ? 32.562  12.222  83.831  1.00 23.89 ? 920  VAL   B CB    1 
ATOM   15832 C  CG1   . VAL   B 1  922  ? 33.379  11.025  84.302  1.00 25.60 ? 920  VAL   B CG1   1 
ATOM   15833 C  CG2   . VAL   B 1  922  ? 31.177  12.201  84.457  1.00 24.83 ? 920  VAL   B CG2   1 
ATOM   15834 N  N     . GLY   B 1  923  ? 32.032  15.622  84.199  1.00 21.23 ? 921  GLY   B N     1 
ATOM   15835 C  CA    . GLY   B 1  923  ? 31.459  16.814  83.610  1.00 20.61 ? 921  GLY   B CA    1 
ATOM   15836 C  C     . GLY   B 1  923  ? 32.024  18.056  84.258  1.00 21.19 ? 921  GLY   B C     1 
ATOM   15837 O  O     . GLY   B 1  923  ? 33.014  17.975  84.994  1.00 22.36 ? 921  GLY   B O     1 
ATOM   15838 N  N     . THR   B 1  924  ? 31.416  19.204  84.013  1.00 16.57 ? 922  THR   B N     1 
ATOM   15839 C  CA    . THR   B 1  924  ? 31.905  20.477  84.536  1.00 17.47 ? 922  THR   B CA    1 
ATOM   15840 C  C     . THR   B 1  924  ? 30.865  21.005  85.514  1.00 17.92 ? 922  THR   B C     1 
ATOM   15841 O  O     . THR   B 1  924  ? 29.836  21.538  85.101  1.00 19.76 ? 922  THR   B O     1 
ATOM   15842 C  CB    . THR   B 1  924  ? 32.162  21.478  83.413  1.00 17.31 ? 922  THR   B CB    1 
ATOM   15843 O  OG1   . THR   B 1  924  ? 31.034  21.533  82.538  1.00 18.69 ? 922  THR   B OG1   1 
ATOM   15844 C  CG2   . THR   B 1  924  ? 33.381  21.070  82.594  1.00 19.00 ? 922  THR   B CG2   1 
ATOM   15845 N  N     . PHE   B 1  925  ? 31.133  20.849  86.804  1.00 17.78 ? 923  PHE   B N     1 
ATOM   15846 C  CA    . PHE   B 1  925  ? 30.206  21.255  87.846  1.00 18.97 ? 923  PHE   B CA    1 
ATOM   15847 C  C     . PHE   B 1  925  ? 30.864  22.252  88.783  1.00 17.68 ? 923  PHE   B C     1 
ATOM   15848 O  O     . PHE   B 1  925  ? 32.063  22.181  89.061  1.00 19.32 ? 923  PHE   B O     1 
ATOM   15849 C  CB    . PHE   B 1  925  ? 29.754  20.054  88.687  1.00 17.17 ? 923  PHE   B CB    1 
ATOM   15850 C  CG    . PHE   B 1  925  ? 28.884  19.091  87.946  1.00 16.94 ? 923  PHE   B CG    1 
ATOM   15851 C  CD1   . PHE   B 1  925  ? 29.441  18.116  87.137  1.00 16.72 ? 923  PHE   B CD1   1 
ATOM   15852 C  CD2   . PHE   B 1  925  ? 27.503  19.159  88.061  1.00 15.63 ? 923  PHE   B CD2   1 
ATOM   15853 C  CE1   . PHE   B 1  925  ? 28.638  17.218  86.447  1.00 18.84 ? 923  PHE   B CE1   1 
ATOM   15854 C  CE2   . PHE   B 1  925  ? 26.696  18.274  87.367  1.00 17.41 ? 923  PHE   B CE2   1 
ATOM   15855 C  CZ    . PHE   B 1  925  ? 27.267  17.293  86.571  1.00 18.12 ? 923  PHE   B CZ    1 
ATOM   15856 N  N     . VAL   B 1  926  ? 30.055  23.170  89.286  1.00 17.39 ? 924  VAL   B N     1 
ATOM   15857 C  CA    . VAL   B 1  926  ? 30.428  24.056  90.384  1.00 18.13 ? 924  VAL   B CA    1 
ATOM   15858 C  C     . VAL   B 1  926  ? 29.316  23.890  91.410  1.00 16.68 ? 924  VAL   B C     1 
ATOM   15859 O  O     . VAL   B 1  926  ? 28.139  24.006  91.056  1.00 17.41 ? 924  VAL   B O     1 
ATOM   15860 C  CB    . VAL   B 1  926  ? 30.526  25.516  89.915  1.00 18.00 ? 924  VAL   B CB    1 
ATOM   15861 C  CG1   . VAL   B 1  926  ? 30.747  26.461  91.106  1.00 19.69 ? 924  VAL   B CG1   1 
ATOM   15862 C  CG2   . VAL   B 1  926  ? 31.646  25.673  88.881  1.00 21.22 ? 924  VAL   B CG2   1 
ATOM   15863 N  N     . PRO   B 1  927  ? 29.623  23.614  92.672  1.00 19.63 ? 925  PRO   B N     1 
ATOM   15864 C  CA    . PRO   B 1  927  ? 28.562  23.443  93.651  1.00 19.42 ? 925  PRO   B CA    1 
ATOM   15865 C  C     . PRO   B 1  927  ? 28.000  24.789  94.060  1.00 21.30 ? 925  PRO   B C     1 
ATOM   15866 O  O     . PRO   B 1  927  ? 28.675  25.821  93.919  1.00 20.49 ? 925  PRO   B O     1 
ATOM   15867 C  CB    . PRO   B 1  927  ? 29.287  22.780  94.826  1.00 24.73 ? 925  PRO   B CB    1 
ATOM   15868 C  CG    . PRO   B 1  927  ? 30.663  23.355  94.759  1.00 21.49 ? 925  PRO   B CG    1 
ATOM   15869 C  CD    . PRO   B 1  927  ? 30.962  23.515  93.274  1.00 21.44 ? 925  PRO   B CD    1 
ATOM   15870 N  N     . PRO   B 1  928  ? 26.761  24.818  94.538  1.00 19.06 ? 926  PRO   B N     1 
ATOM   15871 C  CA    . PRO   B 1  928  ? 26.221  26.039  95.138  1.00 17.52 ? 926  PRO   B CA    1 
ATOM   15872 C  C     . PRO   B 1  928  ? 27.203  26.654  96.119  1.00 18.59 ? 926  PRO   B C     1 
ATOM   15873 O  O     . PRO   B 1  928  ? 27.744  25.981  97.004  1.00 20.27 ? 926  PRO   B O     1 
ATOM   15874 C  CB    . PRO   B 1  928  ? 24.967  25.540  95.857  1.00 19.28 ? 926  PRO   B CB    1 
ATOM   15875 C  CG    . PRO   B 1  928  ? 24.509  24.399  95.011  1.00 24.58 ? 926  PRO   B CG    1 
ATOM   15876 C  CD    . PRO   B 1  928  ? 25.768  23.732  94.512  1.00 19.66 ? 926  PRO   B CD    1 
ATOM   15877 N  N     . THR   B 1  929  ? 27.426  27.943  95.953  1.00 18.75 ? 927  THR   B N     1 
ATOM   15878 C  CA    . THR   B 1  929  ? 28.460  28.654  96.674  1.00 16.10 ? 927  THR   B CA    1 
ATOM   15879 C  C     . THR   B 1  929  ? 27.839  29.899  97.271  1.00 17.72 ? 927  THR   B C     1 
ATOM   15880 O  O     . THR   B 1  929  ? 27.058  30.587  96.616  1.00 18.65 ? 927  THR   B O     1 
ATOM   15881 C  CB    . THR   B 1  929  ? 29.592  29.028  95.703  1.00 18.60 ? 927  THR   B CB    1 
ATOM   15882 O  OG1   . THR   B 1  929  ? 30.137  27.828  95.139  1.00 19.54 ? 927  THR   B OG1   1 
ATOM   15883 C  CG2   . THR   B 1  929  ? 30.702  29.807  96.406  1.00 19.32 ? 927  THR   B CG2   1 
ATOM   15884 N  N     . ILE   B 1  930  ? 28.159  30.164  98.534  1.00 17.54 ? 928  ILE   B N     1 
ATOM   15885 C  CA    . ILE   B 1  930  ? 27.672  31.334  99.249  1.00 19.04 ? 928  ILE   B CA    1 
ATOM   15886 C  C     . ILE   B 1  930  ? 28.880  32.137  99.687  1.00 18.94 ? 928  ILE   B C     1 
ATOM   15887 O  O     . ILE   B 1  930  ? 29.782  31.605  100.348 1.00 19.28 ? 928  ILE   B O     1 
ATOM   15888 C  CB    . ILE   B 1  930  ? 26.830  30.945  100.474 1.00 18.74 ? 928  ILE   B CB    1 
ATOM   15889 C  CG1   . ILE   B 1  930  ? 25.626  30.110  100.050 1.00 18.55 ? 928  ILE   B CG1   1 
ATOM   15890 C  CG2   . ILE   B 1  930  ? 26.407  32.202  101.233 1.00 19.56 ? 928  ILE   B CG2   1 
ATOM   15891 C  CD1   . ILE   B 1  930  ? 24.807  29.595  101.220 1.00 24.69 ? 928  ILE   B CD1   1 
ATOM   15892 N  N     . ILE   B 1  931  ? 28.897  33.415  99.327  1.00 18.24 ? 929  ILE   B N     1 
ATOM   15893 C  CA    . ILE   B 1  931  ? 30.007  34.304  99.631  1.00 17.13 ? 929  ILE   B CA    1 
ATOM   15894 C  C     . ILE   B 1  931  ? 29.448  35.494  100.383 1.00 19.88 ? 929  ILE   B C     1 
ATOM   15895 O  O     . ILE   B 1  931  ? 28.535  36.161  99.894  1.00 18.63 ? 929  ILE   B O     1 
ATOM   15896 C  CB    . ILE   B 1  931  ? 30.704  34.779  98.349  1.00 17.63 ? 929  ILE   B CB    1 
ATOM   15897 C  CG1   . ILE   B 1  931  ? 31.187  33.572  97.546  1.00 20.17 ? 929  ILE   B CG1   1 
ATOM   15898 C  CG2   . ILE   B 1  931  ? 31.871  35.714  98.696  1.00 19.30 ? 929  ILE   B CG2   1 
ATOM   15899 C  CD1   . ILE   B 1  931  ? 31.985  33.970  96.315  1.00 20.61 ? 929  ILE   B CD1   1 
ATOM   15900 N  N     . GLU   B 1  932  ? 29.997  35.773  101.561 1.00 18.99 ? 930  GLU   B N     1 
ATOM   15901 C  CA    . GLU   B 1  932  ? 29.536  36.914  102.332 1.00 18.91 ? 930  GLU   B CA    1 
ATOM   15902 C  C     . GLU   B 1  932  ? 30.337  38.136  101.925 1.00 20.09 ? 930  GLU   B C     1 
ATOM   15903 O  O     . GLU   B 1  932  ? 31.573  38.109  101.936 1.00 20.89 ? 930  GLU   B O     1 
ATOM   15904 C  CB    . GLU   B 1  932  ? 29.668  36.652  103.831 1.00 23.97 ? 930  GLU   B CB    1 
ATOM   15905 C  CG    . GLU   B 1  932  ? 28.757  35.554  104.310 1.00 27.20 ? 930  GLU   B CG    1 
ATOM   15906 C  CD    . GLU   B 1  932  ? 28.566  35.566  105.807 1.00 42.88 ? 930  GLU   B CD    1 
ATOM   15907 O  OE1   . GLU   B 1  932  ? 29.274  36.336  106.494 1.00 43.85 ? 930  GLU   B OE1   1 
ATOM   15908 O  OE2   . GLU   B 1  932  ? 27.708  34.802  106.293 1.00 35.71 ? 930  GLU   B OE2   1 
ATOM   15909 N  N     . LEU   B 1  933  ? 29.636  39.192  101.539 1.00 20.72 ? 931  LEU   B N     1 
ATOM   15910 C  CA    . LEU   B 1  933  ? 30.270  40.433  101.142 1.00 19.72 ? 931  LEU   B CA    1 
ATOM   15911 C  C     . LEU   B 1  933  ? 30.107  41.470  102.239 1.00 23.86 ? 931  LEU   B C     1 
ATOM   15912 O  O     . LEU   B 1  933  ? 29.124  41.459  102.981 1.00 27.77 ? 931  LEU   B O     1 
ATOM   15913 C  CB    . LEU   B 1  933  ? 29.628  40.971  99.868  1.00 22.78 ? 931  LEU   B CB    1 
ATOM   15914 C  CG    . LEU   B 1  933  ? 29.659  40.074  98.632  1.00 23.87 ? 931  LEU   B CG    1 
ATOM   15915 C  CD1   . LEU   B 1  933  ? 29.009  40.826  97.488  1.00 27.45 ? 931  LEU   B CD1   1 
ATOM   15916 C  CD2   . LEU   B 1  933  ? 31.090  39.671  98.295  1.00 30.14 ? 931  LEU   B CD2   1 
ATOM   15917 N  N     . GLU   B 1  934  ? 31.077  42.379  102.328 1.00 27.20 ? 932  GLU   B N     1 
ATOM   15918 C  CA    . GLU   B 1  934  ? 30.903  43.537  103.197 1.00 31.26 ? 932  GLU   B CA    1 
ATOM   15919 C  C     . GLU   B 1  934  ? 30.042  44.599  102.526 1.00 30.65 ? 932  GLU   B C     1 
ATOM   15920 O  O     . GLU   B 1  934  ? 29.204  45.230  103.178 1.00 35.53 ? 932  GLU   B O     1 
ATOM   15921 C  CB    . GLU   B 1  934  ? 32.265  44.113  103.592 1.00 34.20 ? 932  GLU   B CB    1 
ATOM   15922 N  N     . LYS   B 1  935  ? 30.217  44.786  101.222 1.00 26.96 ? 933  LYS   B N     1 
ATOM   15923 C  CA    . LYS   B 1  935  ? 29.485  45.790  100.473 1.00 26.42 ? 933  LYS   B CA    1 
ATOM   15924 C  C     . LYS   B 1  935  ? 29.194  45.225  99.094  1.00 24.11 ? 933  LYS   B C     1 
ATOM   15925 O  O     . LYS   B 1  935  ? 29.941  44.387  98.583  1.00 27.02 ? 933  LYS   B O     1 
ATOM   15926 C  CB    . LYS   B 1  935  ? 30.301  47.085  100.343 1.00 31.96 ? 933  LYS   B CB    1 
ATOM   15927 N  N     . LEU   B 1  936  ? 28.083  45.674  98.505  1.00 23.24 ? 934  LEU   B N     1 
ATOM   15928 C  CA    . LEU   B 1  936  ? 27.746  45.221  97.163  1.00 23.26 ? 934  LEU   B CA    1 
ATOM   15929 C  C     . LEU   B 1  936  ? 28.833  45.589  96.163  1.00 24.44 ? 934  LEU   B C     1 
ATOM   15930 O  O     . LEU   B 1  936  ? 29.054  44.856  95.196  1.00 25.14 ? 934  LEU   B O     1 
ATOM   15931 C  CB    . LEU   B 1  936  ? 26.398  45.797  96.746  1.00 27.04 ? 934  LEU   B CB    1 
ATOM   15932 C  CG    . LEU   B 1  936  ? 25.487  44.810  96.022  1.00 27.39 ? 934  LEU   B CG    1 
ATOM   15933 C  CD1   . LEU   B 1  936  ? 24.035  45.186  96.233  1.00 30.93 ? 934  LEU   B CD1   1 
ATOM   15934 C  CD2   . LEU   B 1  936  ? 25.833  44.791  94.563  1.00 30.77 ? 934  LEU   B CD2   1 
ATOM   15935 N  N     . SER   B 1  937  ? 29.536  46.698  96.386  1.00 23.91 ? 935  SER   B N     1 
ATOM   15936 C  CA    . SER   B 1  937  ? 30.597  47.102  95.472  1.00 26.40 ? 935  SER   B CA    1 
ATOM   15937 C  C     . SER   B 1  937  ? 31.774  46.135  95.458  1.00 27.93 ? 935  SER   B C     1 
ATOM   15938 O  O     . SER   B 1  937  ? 32.651  46.280  94.599  1.00 26.57 ? 935  SER   B O     1 
ATOM   15939 C  CB    . SER   B 1  937  ? 31.068  48.523  95.790  1.00 30.23 ? 935  SER   B CB    1 
ATOM   15940 O  OG    . SER   B 1  937  ? 31.431  48.637  97.151  1.00 31.69 ? 935  SER   B OG    1 
ATOM   15941 N  N     . ASP   B 1  938  ? 31.820  45.161  96.378  1.00 26.67 ? 936  ASP   B N     1 
ATOM   15942 C  CA    . ASP   B 1  938  ? 32.816  44.098  96.272  1.00 24.46 ? 936  ASP   B CA    1 
ATOM   15943 C  C     . ASP   B 1  938  ? 32.628  43.300  94.995  1.00 25.54 ? 936  ASP   B C     1 
ATOM   15944 O  O     . ASP   B 1  938  ? 33.576  42.679  94.506  1.00 26.53 ? 936  ASP   B O     1 
ATOM   15945 C  CB    . ASP   B 1  938  ? 32.703  43.120  97.442  1.00 30.98 ? 936  ASP   B CB    1 
ATOM   15946 C  CG    . ASP   B 1  938  ? 33.015  43.749  98.779  1.00 39.68 ? 936  ASP   B CG    1 
ATOM   15947 O  OD1   . ASP   B 1  938  ? 33.630  44.834  98.814  1.00 34.73 ? 936  ASP   B OD1   1 
ATOM   15948 O  OD2   . ASP   B 1  938  ? 32.631  43.143  99.803  1.00 41.96 ? 936  ASP   B OD2   1 
ATOM   15949 N  N     . LEU   B 1  939  ? 31.410  43.276  94.465  1.00 23.36 ? 937  LEU   B N     1 
ATOM   15950 C  CA    . LEU   B 1  939  ? 31.084  42.547  93.250  1.00 26.32 ? 937  LEU   B CA    1 
ATOM   15951 C  C     . LEU   B 1  939  ? 31.250  43.497  92.073  1.00 27.91 ? 937  LEU   B C     1 
ATOM   15952 O  O     . LEU   B 1  939  ? 30.603  44.551  92.030  1.00 35.68 ? 937  LEU   B O     1 
ATOM   15953 C  CB    . LEU   B 1  939  ? 29.622  42.120  93.331  1.00 26.41 ? 937  LEU   B CB    1 
ATOM   15954 C  CG    . LEU   B 1  939  ? 29.246  40.649  93.410  1.00 36.73 ? 937  LEU   B CG    1 
ATOM   15955 C  CD1   . LEU   B 1  939  ? 27.753  40.551  93.316  1.00 26.20 ? 937  LEU   B CD1   1 
ATOM   15956 C  CD2   . LEU   B 1  939  ? 29.886  39.858  92.288  1.00 33.70 ? 937  LEU   B CD2   1 
ATOM   15957 N  N     . GLN   B 1  940  ? 32.077  43.114  91.102  1.00 24.93 ? 938  GLN   B N     1 
ATOM   15958 C  CA    . GLN   B 1  940  ? 32.389  43.990  89.981  1.00 31.75 ? 938  GLN   B CA    1 
ATOM   15959 C  C     . GLN   B 1  940  ? 31.851  43.499  88.647  1.00 26.62 ? 938  GLN   B C     1 
ATOM   15960 O  O     . GLN   B 1  940  ? 31.889  44.252  87.667  1.00 27.43 ? 938  GLN   B O     1 
ATOM   15961 C  CB    . GLN   B 1  940  ? 33.909  44.187  89.861  1.00 38.67 ? 938  GLN   B CB    1 
ATOM   15962 N  N     . ARG   B 1  941  ? 31.350  42.271  88.578  1.00 21.62 ? 939  ARG   B N     1 
ATOM   15963 C  CA    . ARG   B 1  941  ? 30.973  41.702  87.297  1.00 23.24 ? 939  ARG   B CA    1 
ATOM   15964 C  C     . ARG   B 1  941  ? 29.917  40.638  87.534  1.00 19.63 ? 939  ARG   B C     1 
ATOM   15965 O  O     . ARG   B 1  941  ? 29.813  40.071  88.622  1.00 20.25 ? 939  ARG   B O     1 
ATOM   15966 C  CB    . ARG   B 1  941  ? 32.184  41.108  86.554  1.00 24.79 ? 939  ARG   B CB    1 
ATOM   15967 C  CG    . ARG   B 1  941  ? 32.833  39.899  87.226  1.00 27.93 ? 939  ARG   B CG    1 
ATOM   15968 C  CD    . ARG   B 1  941  ? 34.104  39.480  86.485  1.00 26.69 ? 939  ARG   B CD    1 
ATOM   15969 N  NE    . ARG   B 1  941  ? 34.730  38.288  87.051  1.00 26.94 ? 939  ARG   B NE    1 
ATOM   15970 C  CZ    . ARG   B 1  941  ? 34.475  37.046  86.656  1.00 28.32 ? 939  ARG   B CZ    1 
ATOM   15971 N  NH1   . ARG   B 1  941  ? 33.553  36.787  85.744  1.00 28.68 ? 939  ARG   B NH1   1 
ATOM   15972 N  NH2   . ARG   B 1  941  ? 35.177  36.040  87.177  1.00 27.06 ? 939  ARG   B NH2   1 
ATOM   15973 N  N     . GLU   B 1  942  ? 29.126  40.383  86.500  1.00 20.98 ? 940  GLU   B N     1 
ATOM   15974 C  CA    . GLU   B 1  942  ? 28.144  39.309  86.553  1.00 17.71 ? 940  GLU   B CA    1 
ATOM   15975 C  C     . GLU   B 1  942  ? 28.885  37.987  86.520  1.00 19.80 ? 940  GLU   B C     1 
ATOM   15976 O  O     . GLU   B 1  942  ? 29.642  37.720  85.585  1.00 23.68 ? 940  GLU   B O     1 
ATOM   15977 C  CB    . GLU   B 1  942  ? 27.214  39.407  85.348  1.00 19.18 ? 940  GLU   B CB    1 
ATOM   15978 C  CG    . GLU   B 1  942  ? 26.217  38.255  85.260  1.00 19.55 ? 940  GLU   B CG    1 
ATOM   15979 C  CD    . GLU   B 1  942  ? 25.508  38.188  83.914  1.00 20.25 ? 940  GLU   B CD    1 
ATOM   15980 O  OE1   . GLU   B 1  942  ? 26.183  38.363  82.875  1.00 22.15 ? 940  GLU   B OE1   1 
ATOM   15981 O  OE2   . GLU   B 1  942  ? 24.282  37.956  83.882  1.00 17.66 ? 940  GLU   B OE2   1 
ATOM   15982 N  N     . VAL   B 1  943  ? 28.685  37.166  87.539  1.00 17.38 ? 941  VAL   B N     1 
ATOM   15983 C  CA    . VAL   B 1  943  ? 29.311  35.856  87.627  1.00 16.60 ? 941  VAL   B CA    1 
ATOM   15984 C  C     . VAL   B 1  943  ? 28.215  34.843  87.351  1.00 18.03 ? 941  VAL   B C     1 
ATOM   15985 O  O     . VAL   B 1  943  ? 27.294  34.658  88.157  1.00 17.56 ? 941  VAL   B O     1 
ATOM   15986 C  CB    . VAL   B 1  943  ? 29.976  35.637  88.990  1.00 18.34 ? 941  VAL   B CB    1 
ATOM   15987 C  CG1   . VAL   B 1  943  ? 30.609  34.254  89.046  1.00 20.31 ? 941  VAL   B CG1   1 
ATOM   15988 C  CG2   . VAL   B 1  943  ? 31.023  36.711  89.220  1.00 23.59 ? 941  VAL   B CG2   1 
ATOM   15989 N  N     . PHE   B 1  944  ? 28.289  34.217  86.182  1.00 16.97 ? 942  PHE   B N     1 
ATOM   15990 C  CA    . PHE   B 1  944  ? 27.168  33.466  85.638  1.00 17.02 ? 942  PHE   B CA    1 
ATOM   15991 C  C     . PHE   B 1  944  ? 27.300  32.008  86.066  1.00 17.49 ? 942  PHE   B C     1 
ATOM   15992 O  O     . PHE   B 1  944  ? 27.626  31.110  85.293  1.00 18.68 ? 942  PHE   B O     1 
ATOM   15993 C  CB    . PHE   B 1  944  ? 27.158  33.603  84.123  1.00 16.91 ? 942  PHE   B CB    1 
ATOM   15994 C  CG    . PHE   B 1  944  ? 25.829  33.336  83.499  1.00 16.93 ? 942  PHE   B CG    1 
ATOM   15995 C  CD1   . PHE   B 1  944  ? 24.778  34.225  83.671  1.00 16.94 ? 942  PHE   B CD1   1 
ATOM   15996 C  CD2   . PHE   B 1  944  ? 25.625  32.201  82.727  1.00 16.27 ? 942  PHE   B CD2   1 
ATOM   15997 C  CE1   . PHE   B 1  944  ? 23.551  34.001  83.091  1.00 17.01 ? 942  PHE   B CE1   1 
ATOM   15998 C  CE2   . PHE   B 1  944  ? 24.379  31.963  82.143  1.00 17.13 ? 942  PHE   B CE2   1 
ATOM   15999 C  CZ    . PHE   B 1  944  ? 23.339  32.872  82.336  1.00 17.28 ? 942  PHE   B CZ    1 
ATOM   16000 N  N     . GLY   B 1  945  ? 27.027  31.785  87.339  1.00 16.94 ? 943  GLY   B N     1 
ATOM   16001 C  CA    . GLY   B 1  945  ? 27.154  30.472  87.909  1.00 17.56 ? 943  GLY   B CA    1 
ATOM   16002 C  C     . GLY   B 1  945  ? 26.444  30.425  89.240  1.00 17.31 ? 943  GLY   B C     1 
ATOM   16003 O  O     . GLY   B 1  945  ? 25.768  31.374  89.639  1.00 17.69 ? 943  GLY   B O     1 
ATOM   16004 N  N     . PRO   B 1  946  ? 26.598  29.330  89.962  1.00 16.75 ? 944  PRO   B N     1 
ATOM   16005 C  CA    . PRO   B 1  946  ? 25.798  29.116  91.186  1.00 16.82 ? 944  PRO   B CA    1 
ATOM   16006 C  C     . PRO   B 1  946  ? 26.465  29.757  92.399  1.00 16.63 ? 944  PRO   B C     1 
ATOM   16007 O  O     . PRO   B 1  946  ? 26.852  29.087  93.360  1.00 18.18 ? 944  PRO   B O     1 
ATOM   16008 C  CB    . PRO   B 1  946  ? 25.760  27.588  91.282  1.00 16.20 ? 944  PRO   B CB    1 
ATOM   16009 C  CG    . PRO   B 1  946  ? 27.120  27.173  90.729  1.00 16.95 ? 944  PRO   B CG    1 
ATOM   16010 C  CD    . PRO   B 1  946  ? 27.417  28.157  89.605  1.00 16.81 ? 944  PRO   B CD    1 
ATOM   16011 N  N     . VAL   B 1  947  ? 26.627  31.071  92.343  1.00 16.32 ? 945  VAL   B N     1 
ATOM   16012 C  CA    . VAL   B 1  947  ? 27.393  31.798  93.344  1.00 17.19 ? 945  VAL   B CA    1 
ATOM   16013 C  C     . VAL   B 1  947  ? 26.498  32.884  93.907  1.00 19.30 ? 945  VAL   B C     1 
ATOM   16014 O  O     . VAL   B 1  947  ? 26.213  33.881  93.229  1.00 17.70 ? 945  VAL   B O     1 
ATOM   16015 C  CB    . VAL   B 1  947  ? 28.694  32.381  92.778  1.00 17.99 ? 945  VAL   B CB    1 
ATOM   16016 C  CG1   . VAL   B 1  947  ? 29.493  33.052  93.883  1.00 19.35 ? 945  VAL   B CG1   1 
ATOM   16017 C  CG2   . VAL   B 1  947  ? 29.526  31.287  92.120  1.00 17.76 ? 945  VAL   B CG2   1 
ATOM   16018 N  N     . LEU   B 1  948  ? 26.043  32.687  95.138  1.00 16.06 ? 946  LEU   B N     1 
ATOM   16019 C  CA    . LEU   B 1  948  ? 25.161  33.622  95.811  1.00 17.56 ? 946  LEU   B CA    1 
ATOM   16020 C  C     . LEU   B 1  948  ? 25.996  34.465  96.758  1.00 17.32 ? 946  LEU   B C     1 
ATOM   16021 O  O     . LEU   B 1  948  ? 26.739  33.928  97.586  1.00 17.76 ? 946  LEU   B O     1 
ATOM   16022 C  CB    . LEU   B 1  948  ? 24.117  32.858  96.612  1.00 16.92 ? 946  LEU   B CB    1 
ATOM   16023 C  CG    . LEU   B 1  948  ? 23.164  33.761  97.374  1.00 16.48 ? 946  LEU   B CG    1 
ATOM   16024 C  CD1   . LEU   B 1  948  ? 22.346  34.569  96.373  1.00 15.36 ? 946  LEU   B CD1   1 
ATOM   16025 C  CD2   . LEU   B 1  948  ? 22.267  32.880  98.237  1.00 21.01 ? 946  LEU   B CD2   1 
ATOM   16026 N  N     . HIS   B 1  949  ? 25.877  35.772  96.637  1.00 15.82 ? 947  HIS   B N     1 
ATOM   16027 C  CA    . HIS   B 1  949  ? 26.555  36.696  97.530  1.00 16.07 ? 947  HIS   B CA    1 
ATOM   16028 C  C     . HIS   B 1  949  ? 25.555  37.174  98.557  1.00 17.46 ? 947  HIS   B C     1 
ATOM   16029 O  O     . HIS   B 1  949  ? 24.368  37.324  98.260  1.00 19.26 ? 947  HIS   B O     1 
ATOM   16030 C  CB    . HIS   B 1  949  ? 27.124  37.863  96.732  1.00 17.95 ? 947  HIS   B CB    1 
ATOM   16031 C  CG    . HIS   B 1  949  ? 28.019  37.411  95.628  1.00 16.04 ? 947  HIS   B CG    1 
ATOM   16032 N  ND1   . HIS   B 1  949  ? 27.529  37.023  94.399  1.00 18.49 ? 947  HIS   B ND1   1 
ATOM   16033 C  CD2   . HIS   B 1  949  ? 29.355  37.200  95.587  1.00 18.06 ? 947  HIS   B CD2   1 
ATOM   16034 C  CE1   . HIS   B 1  949  ? 28.531  36.627  93.636  1.00 17.50 ? 947  HIS   B CE1   1 
ATOM   16035 N  NE2   . HIS   B 1  949  ? 29.647  36.717  94.333  1.00 18.74 ? 947  HIS   B NE2   1 
ATOM   16036 N  N     . VAL   B 1  950  ? 26.018  37.347  99.787  1.00 18.56 ? 948  VAL   B N     1 
ATOM   16037 C  CA    . VAL   B 1  950  ? 25.128  37.668  100.889 1.00 18.61 ? 948  VAL   B CA    1 
ATOM   16038 C  C     . VAL   B 1  950  ? 25.583  38.969  101.510 1.00 18.21 ? 948  VAL   B C     1 
ATOM   16039 O  O     . VAL   B 1  950  ? 26.770  39.140  101.812 1.00 18.88 ? 948  VAL   B O     1 
ATOM   16040 C  CB    . VAL   B 1  950  ? 25.090  36.546  101.938 1.00 17.72 ? 948  VAL   B CB    1 
ATOM   16041 C  CG1   . VAL   B 1  950  ? 24.267  36.994  103.154 1.00 20.31 ? 948  VAL   B CG1   1 
ATOM   16042 C  CG2   . VAL   B 1  950  ? 24.512  35.281  101.336 1.00 20.14 ? 948  VAL   B CG2   1 
ATOM   16043 N  N     . ILE   B 1  951  ? 24.641  39.881  101.695 1.00 17.58 ? 949  ILE   B N     1 
ATOM   16044 C  CA    . ILE   B 1  951  ? 24.874  41.156  102.354 1.00 17.83 ? 949  ILE   B CA    1 
ATOM   16045 C  C     . ILE   B 1  951  ? 23.917  41.208  103.530 1.00 17.13 ? 949  ILE   B C     1 
ATOM   16046 O  O     . ILE   B 1  951  ? 22.763  40.789  103.401 1.00 18.99 ? 949  ILE   B O     1 
ATOM   16047 C  CB    . ILE   B 1  951  ? 24.562  42.303  101.372 1.00 20.42 ? 949  ILE   B CB    1 
ATOM   16048 C  CG1   . ILE   B 1  951  ? 25.677  42.418  100.337 1.00 28.28 ? 949  ILE   B CG1   1 
ATOM   16049 C  CG2   . ILE   B 1  951  ? 24.336  43.630  102.109 1.00 29.28 ? 949  ILE   B CG2   1 
ATOM   16050 C  CD1   . ILE   B 1  951  ? 25.430  43.497  99.338  1.00 37.93 ? 949  ILE   B CD1   1 
ATOM   16051 N  N     . ARG   B 1  952  ? 24.388  41.694  104.669 1.00 17.22 ? 950  ARG   B N     1 
ATOM   16052 C  CA    . ARG   B 1  952  ? 23.522  41.946  105.814 1.00 18.11 ? 950  ARG   B CA    1 
ATOM   16053 C  C     . ARG   B 1  952  ? 23.306  43.449  105.917 1.00 18.71 ? 950  ARG   B C     1 
ATOM   16054 O  O     . ARG   B 1  952  ? 24.227  44.235  105.681 1.00 24.25 ? 950  ARG   B O     1 
ATOM   16055 C  CB    . ARG   B 1  952  ? 24.181  41.431  107.099 1.00 19.94 ? 950  ARG   B CB    1 
ATOM   16056 C  CG    . ARG   B 1  952  ? 24.434  39.944  107.058 1.00 21.13 ? 950  ARG   B CG    1 
ATOM   16057 C  CD    . ARG   B 1  952  ? 25.458  39.523  108.087 1.00 29.09 ? 950  ARG   B CD    1 
ATOM   16058 N  NE    . ARG   B 1  952  ? 25.834  38.125  107.911 1.00 32.87 ? 950  ARG   B NE    1 
ATOM   16059 C  CZ    . ARG   B 1  952  ? 25.463  37.142  108.720 1.00 27.47 ? 950  ARG   B CZ    1 
ATOM   16060 N  NH1   . ARG   B 1  952  ? 24.687  37.365  109.766 1.00 28.40 ? 950  ARG   B NH1   1 
ATOM   16061 N  NH2   . ARG   B 1  952  ? 25.898  35.908  108.482 1.00 31.64 ? 950  ARG   B NH2   1 
ATOM   16062 N  N     . TYR   B 1  953  ? 22.087  43.860  106.265 1.00 17.77 ? 951  TYR   B N     1 
ATOM   16063 C  CA    . TYR   B 1  953  ? 21.832  45.288  106.360 1.00 18.31 ? 951  TYR   B CA    1 
ATOM   16064 C  C     . TYR   B 1  953  ? 20.969  45.595  107.575 1.00 18.49 ? 951  TYR   B C     1 
ATOM   16065 O  O     . TYR   B 1  953  ? 20.175  44.763  108.025 1.00 20.12 ? 951  TYR   B O     1 
ATOM   16066 C  CB    . TYR   B 1  953  ? 21.165  45.833  105.077 1.00 18.64 ? 951  TYR   B CB    1 
ATOM   16067 C  CG    . TYR   B 1  953  ? 19.726  45.418  104.923 1.00 17.06 ? 951  TYR   B CG    1 
ATOM   16068 C  CD1   . TYR   B 1  953  ? 19.386  44.187  104.361 1.00 17.23 ? 951  TYR   B CD1   1 
ATOM   16069 C  CD2   . TYR   B 1  953  ? 18.696  46.256  105.334 1.00 17.09 ? 951  TYR   B CD2   1 
ATOM   16070 C  CE1   . TYR   B 1  953  ? 18.071  43.805  104.229 1.00 17.87 ? 951  TYR   B CE1   1 
ATOM   16071 C  CE2   . TYR   B 1  953  ? 17.389  45.881  105.206 1.00 19.31 ? 951  TYR   B CE2   1 
ATOM   16072 C  CZ    . TYR   B 1  953  ? 17.077  44.656  104.641 1.00 18.29 ? 951  TYR   B CZ    1 
ATOM   16073 O  OH    . TYR   B 1  953  ? 15.763  44.279  104.528 1.00 19.08 ? 951  TYR   B OH    1 
ATOM   16074 N  N     . ARG   B 1  954  ? 21.137  46.808  108.097 1.00 22.19 ? 952  ARG   B N     1 
ATOM   16075 C  CA    . ARG   B 1  954  ? 20.261  47.337  109.131 1.00 26.85 ? 952  ARG   B CA    1 
ATOM   16076 C  C     . ARG   B 1  954  ? 19.064  47.983  108.452 1.00 24.42 ? 952  ARG   B C     1 
ATOM   16077 O  O     . ARG   B 1  954  ? 19.211  48.635  107.416 1.00 21.00 ? 952  ARG   B O     1 
ATOM   16078 C  CB    . ARG   B 1  954  ? 21.001  48.385  109.968 1.00 26.89 ? 952  ARG   B CB    1 
ATOM   16079 N  N     . ARG   B 1  955  ? 17.877  47.808  109.046 1.00 25.12 ? 953  ARG   B N     1 
ATOM   16080 C  CA    . ARG   B 1  955  ? 16.657  48.299  108.412 1.00 26.84 ? 953  ARG   B CA    1 
ATOM   16081 C  C     . ARG   B 1  955  ? 16.725  49.797  108.129 1.00 23.88 ? 953  ARG   B C     1 
ATOM   16082 O  O     . ARG   B 1  955  ? 16.216  50.263  107.103 1.00 25.03 ? 953  ARG   B O     1 
ATOM   16083 C  CB    . ARG   B 1  955  ? 15.428  47.950  109.254 1.00 30.29 ? 953  ARG   B CB    1 
ATOM   16084 C  CG    . ARG   B 1  955  ? 14.097  48.422  108.663 1.00 33.84 ? 953  ARG   B CG    1 
ATOM   16085 C  CD    . ARG   B 1  955  ? 13.902  47.958  107.215 1.00 34.47 ? 953  ARG   B CD    1 
ATOM   16086 N  NE    . ARG   B 1  955  ? 12.610  48.366  106.673 1.00 35.79 ? 953  ARG   B NE    1 
ATOM   16087 C  CZ    . ARG   B 1  955  ? 12.309  49.600  106.288 1.00 36.38 ? 953  ARG   B CZ    1 
ATOM   16088 N  NH1   . ARG   B 1  955  ? 13.186  50.588  106.383 1.00 36.98 ? 953  ARG   B NH1   1 
ATOM   16089 N  NH2   . ARG   B 1  955  ? 11.097  49.849  105.796 1.00 31.19 ? 953  ARG   B NH2   1 
ATOM   16090 N  N     . ASP   B 1  956  ? 17.350  50.572  109.020 1.00 24.02 ? 954  ASP   B N     1 
ATOM   16091 C  CA    A ASP   B 1  956  ? 17.479  52.011  108.798 0.51 27.18 ? 954  ASP   B CA    1 
ATOM   16092 C  CA    B ASP   B 1  956  ? 17.436  52.006  108.766 0.49 27.19 ? 954  ASP   B CA    1 
ATOM   16093 C  C     . ASP   B 1  956  ? 18.324  52.340  107.577 1.00 27.03 ? 954  ASP   B C     1 
ATOM   16094 O  O     . ASP   B 1  956  ? 18.293  53.481  107.102 1.00 29.75 ? 954  ASP   B O     1 
ATOM   16095 C  CB    A ASP   B 1  956  ? 18.081  52.689  110.029 0.51 27.86 ? 954  ASP   B CB    1 
ATOM   16096 C  CB    B ASP   B 1  956  ? 17.821  52.800  110.025 0.49 28.01 ? 954  ASP   B CB    1 
ATOM   16097 C  CG    A ASP   B 1  956  ? 17.145  52.673  111.217 0.51 31.76 ? 954  ASP   B CG    1 
ATOM   16098 C  CG    B ASP   B 1  956  ? 19.221  52.484  110.539 0.49 23.72 ? 954  ASP   B CG    1 
ATOM   16099 O  OD1   A ASP   B 1  956  ? 15.924  52.511  111.006 0.51 35.26 ? 954  ASP   B OD1   1 
ATOM   16100 O  OD1   B ASP   B 1  956  ? 19.945  51.675  109.927 0.49 30.51 ? 954  ASP   B OD1   1 
ATOM   16101 O  OD2   A ASP   B 1  956  ? 17.631  52.830  112.357 0.51 35.99 ? 954  ASP   B OD2   1 
ATOM   16102 O  OD2   B ASP   B 1  956  ? 19.596  53.059  111.587 0.49 33.72 ? 954  ASP   B OD2   1 
ATOM   16103 N  N     . ASP   B 1  957  ? 19.082  51.375  107.069 1.00 22.39 ? 955  ASP   B N     1 
ATOM   16104 C  CA    . ASP   B 1  957  ? 19.909  51.576  105.894 1.00 25.09 ? 955  ASP   B CA    1 
ATOM   16105 C  C     . ASP   B 1  957  ? 19.255  51.044  104.627 1.00 22.19 ? 955  ASP   B C     1 
ATOM   16106 O  O     . ASP   B 1  957  ? 19.935  50.913  103.613 1.00 22.16 ? 955  ASP   B O     1 
ATOM   16107 C  CB    . ASP   B 1  957  ? 21.271  50.905  106.074 1.00 26.86 ? 955  ASP   B CB    1 
ATOM   16108 C  CG    . ASP   B 1  957  ? 22.129  51.594  107.110 1.00 36.69 ? 955  ASP   B CG    1 
ATOM   16109 O  OD1   . ASP   B 1  957  ? 21.975  52.822  107.287 1.00 34.50 ? 955  ASP   B OD1   1 
ATOM   16110 O  OD2   . ASP   B 1  957  ? 22.958  50.903  107.742 1.00 40.44 ? 955  ASP   B OD2   1 
ATOM   16111 N  N     . LEU   B 1  958  ? 17.962  50.715  104.672 1.00 20.27 ? 956  LEU   B N     1 
ATOM   16112 C  CA    . LEU   B 1  958  ? 17.314  50.113  103.507 1.00 19.75 ? 956  LEU   B CA    1 
ATOM   16113 C  C     . LEU   B 1  958  ? 17.427  51.004  102.277 1.00 19.81 ? 956  LEU   B C     1 
ATOM   16114 O  O     . LEU   B 1  958  ? 17.724  50.522  101.178 1.00 18.60 ? 956  LEU   B O     1 
ATOM   16115 C  CB    . LEU   B 1  958  ? 15.848  49.836  103.816 1.00 20.47 ? 956  LEU   B CB    1 
ATOM   16116 C  CG    . LEU   B 1  958  ? 15.042  49.228  102.672 1.00 20.66 ? 956  LEU   B CG    1 
ATOM   16117 C  CD1   . LEU   B 1  958  ? 15.657  47.921  102.201 1.00 20.75 ? 956  LEU   B CD1   1 
ATOM   16118 C  CD2   . LEU   B 1  958  ? 13.617  49.026  103.136 1.00 23.98 ? 956  LEU   B CD2   1 
ATOM   16119 N  N     . ASP   B 1  959  ? 17.202  52.307  102.431 1.00 18.92 ? 957  ASP   B N     1 
ATOM   16120 C  CA    . ASP   B 1  959  ? 17.238  53.171  101.257 1.00 18.73 ? 957  ASP   B CA    1 
ATOM   16121 C  C     . ASP   B 1  959  ? 18.627  53.175  100.628 1.00 19.10 ? 957  ASP   B C     1 
ATOM   16122 O  O     . ASP   B 1  959  ? 18.765  53.107  99.401  1.00 18.79 ? 957  ASP   B O     1 
ATOM   16123 C  CB    . ASP   B 1  959  ? 16.774  54.579  101.619 1.00 19.20 ? 957  ASP   B CB    1 
ATOM   16124 C  CG    . ASP   B 1  959  ? 16.335  55.362  100.413 1.00 19.63 ? 957  ASP   B CG    1 
ATOM   16125 O  OD1   . ASP   B 1  959  ? 15.565  54.814  99.602  1.00 20.69 ? 957  ASP   B OD1   1 
ATOM   16126 O  OD2   . ASP   B 1  959  ? 16.735  56.531  100.285 1.00 22.20 ? 957  ASP   B OD2   1 
ATOM   16127 N  N     . ARG   B 1  960  ? 19.666  53.239  101.458 1.00 19.92 ? 958  ARG   B N     1 
ATOM   16128 C  CA    . ARG   B 1  960  ? 21.028  53.183  100.950 1.00 18.26 ? 958  ARG   B CA    1 
ATOM   16129 C  C     . ARG   B 1  960  ? 21.310  51.837  100.297 1.00 20.07 ? 958  ARG   B C     1 
ATOM   16130 O  O     . ARG   B 1  960  ? 22.022  51.763  99.290  1.00 18.93 ? 958  ARG   B O     1 
ATOM   16131 C  CB    . ARG   B 1  960  ? 22.003  53.435  102.100 1.00 24.69 ? 958  ARG   B CB    1 
ATOM   16132 N  N     . LEU   B 1  961  ? 20.753  50.759  100.847 1.00 16.85 ? 959  LEU   B N     1 
ATOM   16133 C  CA    . LEU   B 1  961  ? 20.939  49.449  100.238 1.00 16.77 ? 959  LEU   B CA    1 
ATOM   16134 C  C     . LEU   B 1  961  ? 20.343  49.412  98.843  1.00 17.11 ? 959  LEU   B C     1 
ATOM   16135 O  O     . LEU   B 1  961  ? 20.959  48.879  97.913  1.00 17.57 ? 959  LEU   B O     1 
ATOM   16136 C  CB    . LEU   B 1  961  ? 20.311  48.366  101.108 1.00 18.69 ? 959  LEU   B CB    1 
ATOM   16137 C  CG    . LEU   B 1  961  ? 20.287  46.975  100.483 1.00 17.75 ? 959  LEU   B CG    1 
ATOM   16138 C  CD1   . LEU   B 1  961  ? 21.711  46.441  100.294 1.00 23.64 ? 959  LEU   B CD1   1 
ATOM   16139 C  CD2   . LEU   B 1  961  ? 19.445  46.003  101.290 1.00 19.70 ? 959  LEU   B CD2   1 
ATOM   16140 N  N     . VAL   B 1  962  ? 19.152  49.985  98.672  1.00 15.58 ? 960  VAL   B N     1 
ATOM   16141 C  CA    . VAL   B 1  962  ? 18.575  50.067  97.338  1.00 17.55 ? 960  VAL   B CA    1 
ATOM   16142 C  C     . VAL   B 1  962  ? 19.505  50.828  96.401  1.00 17.90 ? 960  VAL   B C     1 
ATOM   16143 O  O     . VAL   B 1  962  ? 19.724  50.411  95.261  1.00 17.48 ? 960  VAL   B O     1 
ATOM   16144 C  CB    . VAL   B 1  962  ? 17.168  50.682  97.403  1.00 18.14 ? 960  VAL   B CB    1 
ATOM   16145 C  CG1   . VAL   B 1  962  ? 16.678  50.982  96.006  1.00 20.66 ? 960  VAL   B CG1   1 
ATOM   16146 C  CG2   . VAL   B 1  962  ? 16.212  49.720  98.101  1.00 19.35 ? 960  VAL   B CG2   1 
ATOM   16147 N  N     . ASP   B 1  963  ? 20.096  51.934  96.875  1.00 17.08 ? 961  ASP   B N     1 
ATOM   16148 C  CA    . ASP   B 1  963  ? 21.085  52.648  96.065  1.00 19.37 ? 961  ASP   B CA    1 
ATOM   16149 C  C     . ASP   B 1  963  ? 22.231  51.738  95.672  1.00 19.27 ? 961  ASP   B C     1 
ATOM   16150 O  O     . ASP   B 1  963  ? 22.700  51.779  94.530  1.00 19.74 ? 961  ASP   B O     1 
ATOM   16151 C  CB    . ASP   B 1  963  ? 21.683  53.813  96.846  1.00 19.46 ? 961  ASP   B CB    1 
ATOM   16152 C  CG    . ASP   B 1  963  ? 20.743  54.955  97.005  1.00 25.81 ? 961  ASP   B CG    1 
ATOM   16153 O  OD1   . ASP   B 1  963  ? 19.773  55.033  96.229  1.00 25.88 ? 961  ASP   B OD1   1 
ATOM   16154 O  OD2   . ASP   B 1  963  ? 21.004  55.790  97.904  1.00 26.29 ? 961  ASP   B OD2   1 
ATOM   16155 N  N     . ASP   B 1  964  ? 22.714  50.931  96.621  1.00 18.78 ? 962  ASP   B N     1 
ATOM   16156 C  CA    . ASP   B 1  964  ? 23.808  50.008  96.341  1.00 18.46 ? 962  ASP   B CA    1 
ATOM   16157 C  C     . ASP   B 1  964  ? 23.419  49.013  95.257  1.00 19.69 ? 962  ASP   B C     1 
ATOM   16158 O  O     . ASP   B 1  964  ? 24.221  48.705  94.371  1.00 18.53 ? 962  ASP   B O     1 
ATOM   16159 C  CB    . ASP   B 1  964  ? 24.192  49.258  97.617  1.00 19.73 ? 962  ASP   B CB    1 
ATOM   16160 C  CG    . ASP   B 1  964  ? 24.883  50.142  98.637  1.00 27.25 ? 962  ASP   B CG    1 
ATOM   16161 O  OD1   . ASP   B 1  964  ? 25.213  51.306  98.318  1.00 24.33 ? 962  ASP   B OD1   1 
ATOM   16162 O  OD2   . ASP   B 1  964  ? 25.097  49.662  99.773  1.00 30.71 ? 962  ASP   B OD2   1 
ATOM   16163 N  N     . VAL   B 1  965  ? 22.192  48.492  95.314  1.00 16.81 ? 963  VAL   B N     1 
ATOM   16164 C  CA    . VAL   B 1  965  ? 21.729  47.587  94.265  1.00 15.32 ? 963  VAL   B CA    1 
ATOM   16165 C  C     . VAL   B 1  965  ? 21.715  48.301  92.921  1.00 16.79 ? 963  VAL   B C     1 
ATOM   16166 O  O     . VAL   B 1  965  ? 22.230  47.784  91.920  1.00 17.70 ? 963  VAL   B O     1 
ATOM   16167 C  CB    . VAL   B 1  965  ? 20.355  46.997  94.620  1.00 16.63 ? 963  VAL   B CB    1 
ATOM   16168 C  CG1   . VAL   B 1  965  ? 19.833  46.182  93.457  1.00 16.23 ? 963  VAL   B CG1   1 
ATOM   16169 C  CG2   . VAL   B 1  965  ? 20.450  46.146  95.887  1.00 18.13 ? 963  VAL   B CG2   1 
ATOM   16170 N  N     . ASN   B 1  966  ? 21.170  49.519  92.883  1.00 16.61 ? 964  ASN   B N     1 
ATOM   16171 C  CA    . ASN   B 1  966  ? 21.111  50.249  91.616  1.00 16.82 ? 964  ASN   B CA    1 
ATOM   16172 C  C     . ASN   B 1  966  ? 22.497  50.640  91.122  1.00 18.02 ? 964  ASN   B C     1 
ATOM   16173 O  O     . ASN   B 1  966  ? 22.694  50.809  89.914  1.00 20.75 ? 964  ASN   B O     1 
ATOM   16174 C  CB    . ASN   B 1  966  ? 20.283  51.521  91.770  1.00 17.59 ? 964  ASN   B CB    1 
ATOM   16175 C  CG    . ASN   B 1  966  ? 18.811  51.245  91.979  1.00 16.79 ? 964  ASN   B CG    1 
ATOM   16176 O  OD1   . ASN   B 1  966  ? 18.293  50.225  91.548  1.00 18.00 ? 964  ASN   B OD1   1 
ATOM   16177 N  ND2   . ASN   B 1  966  ? 18.125  52.178  92.625  1.00 18.55 ? 964  ASN   B ND2   1 
ATOM   16178 N  N     . ALA   B 1  967  ? 23.464  50.788  92.030  1.00 16.45 ? 965  ALA   B N     1 
ATOM   16179 C  CA    . ALA   B 1  967  ? 24.757  51.341  91.668  1.00 18.17 ? 965  ALA   B CA    1 
ATOM   16180 C  C     . ALA   B 1  967  ? 25.595  50.396  90.830  1.00 19.21 ? 965  ALA   B C     1 
ATOM   16181 O  O     . ALA   B 1  967  ? 26.617  50.833  90.292  1.00 20.29 ? 965  ALA   B O     1 
ATOM   16182 C  CB    . ALA   B 1  967  ? 25.535  51.708  92.932  1.00 18.56 ? 965  ALA   B CB    1 
ATOM   16183 N  N     . THR   B 1  968  ? 25.208  49.126  90.708  1.00 17.01 ? 966  THR   B N     1 
ATOM   16184 C  CA    . THR   B 1  968  ? 25.960  48.237  89.836  1.00 17.96 ? 966  THR   B CA    1 
ATOM   16185 C  C     . THR   B 1  968  ? 25.817  48.642  88.381  1.00 18.89 ? 966  THR   B C     1 
ATOM   16186 O  O     . THR   B 1  968  ? 26.645  48.249  87.554  1.00 19.25 ? 966  THR   B O     1 
ATOM   16187 C  CB    . THR   B 1  968  ? 25.462  46.801  89.964  1.00 18.14 ? 966  THR   B CB    1 
ATOM   16188 O  OG1   . THR   B 1  968  ? 24.153  46.706  89.378  1.00 18.22 ? 966  THR   B OG1   1 
ATOM   16189 C  CG2   . THR   B 1  968  ? 25.410  46.369  91.421  1.00 19.82 ? 966  THR   B CG2   1 
ATOM   16190 N  N     . GLY   B 1  969  ? 24.782  49.416  88.058  1.00 17.36 ? 967  GLY   B N     1 
ATOM   16191 C  CA    . GLY   B 1  969  ? 24.472  49.773  86.698  1.00 17.55 ? 967  GLY   B CA    1 
ATOM   16192 C  C     . GLY   B 1  969  ? 23.563  48.795  85.997  1.00 18.12 ? 967  GLY   B C     1 
ATOM   16193 O  O     . GLY   B 1  969  ? 23.034  49.126  84.929  1.00 17.42 ? 967  GLY   B O     1 
ATOM   16194 N  N     . TYR   B 1  970  ? 23.370  47.609  86.566  1.00 18.42 ? 968  TYR   B N     1 
ATOM   16195 C  CA    . TYR   B 1  970  ? 22.440  46.634  86.026  1.00 16.48 ? 968  TYR   B CA    1 
ATOM   16196 C  C     . TYR   B 1  970  ? 21.027  46.944  86.502  1.00 15.59 ? 968  TYR   B C     1 
ATOM   16197 O  O     . TYR   B 1  970  ? 20.811  47.747  87.409  1.00 17.70 ? 968  TYR   B O     1 
ATOM   16198 C  CB    . TYR   B 1  970  ? 22.860  45.240  86.478  1.00 16.17 ? 968  TYR   B CB    1 
ATOM   16199 C  CG    . TYR   B 1  970  ? 24.082  44.734  85.759  1.00 17.61 ? 968  TYR   B CG    1 
ATOM   16200 C  CD1   . TYR   B 1  970  ? 23.975  44.238  84.467  1.00 20.52 ? 968  TYR   B CD1   1 
ATOM   16201 C  CD2   . TYR   B 1  970  ? 25.338  44.748  86.363  1.00 20.35 ? 968  TYR   B CD2   1 
ATOM   16202 C  CE1   . TYR   B 1  970  ? 25.079  43.763  83.782  1.00 25.06 ? 968  TYR   B CE1   1 
ATOM   16203 C  CE2   . TYR   B 1  970  ? 26.457  44.262  85.674  1.00 22.58 ? 968  TYR   B CE2   1 
ATOM   16204 C  CZ    . TYR   B 1  970  ? 26.305  43.779  84.386  1.00 25.75 ? 968  TYR   B CZ    1 
ATOM   16205 O  OH    . TYR   B 1  970  ? 27.389  43.294  83.678  1.00 36.19 ? 968  TYR   B OH    1 
ATOM   16206 N  N     . GLY   B 1  971  ? 20.055  46.274  85.900  1.00 14.79 ? 969  GLY   B N     1 
ATOM   16207 C  CA    . GLY   B 1  971  ? 18.680  46.504  86.281  1.00 14.55 ? 969  GLY   B CA    1 
ATOM   16208 C  C     . GLY   B 1  971  ? 17.767  45.487  85.640  1.00 14.82 ? 969  GLY   B C     1 
ATOM   16209 O  O     . GLY   B 1  971  ? 16.827  45.854  84.931  1.00 14.95 ? 969  GLY   B O     1 
ATOM   16210 N  N     . LEU   B 1  972  ? 18.028  44.209  85.895  1.00 13.54 ? 970  LEU   B N     1 
ATOM   16211 C  CA    . LEU   B 1  972  ? 17.255  43.144  85.274  1.00 13.87 ? 970  LEU   B CA    1 
ATOM   16212 C  C     . LEU   B 1  972  ? 16.168  42.646  86.221  1.00 13.26 ? 970  LEU   B C     1 
ATOM   16213 O  O     . LEU   B 1  972  ? 15.037  43.140  86.160  1.00 14.63 ? 970  LEU   B O     1 
ATOM   16214 C  CB    . LEU   B 1  972  ? 18.186  42.038  84.765  1.00 15.13 ? 970  LEU   B CB    1 
ATOM   16215 C  CG    . LEU   B 1  972  ? 17.543  40.967  83.902  1.00 14.08 ? 970  LEU   B CG    1 
ATOM   16216 C  CD1   . LEU   B 1  972  ? 16.815  41.602  82.735  1.00 17.59 ? 970  LEU   B CD1   1 
ATOM   16217 C  CD2   . LEU   B 1  972  ? 18.620  40.010  83.406  1.00 16.70 ? 970  LEU   B CD2   1 
ATOM   16218 N  N     . THR   B 1  973  ? 16.473  41.680  87.089  1.00 14.37 ? 971  THR   B N     1 
ATOM   16219 C  CA    . THR   B 1  973  ? 15.470  41.206  88.028  1.00 14.33 ? 971  THR   B CA    1 
ATOM   16220 C  C     . THR   B 1  973  ? 15.797  41.672  89.436  1.00 12.55 ? 971  THR   B C     1 
ATOM   16221 O  O     . THR   B 1  973  ? 16.946  41.966  89.771  1.00 14.40 ? 971  THR   B O     1 
ATOM   16222 C  CB    . THR   B 1  973  ? 15.350  39.683  88.017  1.00 14.08 ? 971  THR   B CB    1 
ATOM   16223 O  OG1   . THR   B 1  973  ? 16.606  39.090  88.363  1.00 13.25 ? 971  THR   B OG1   1 
ATOM   16224 C  CG2   . THR   B 1  973  ? 14.888  39.189  86.646  1.00 15.40 ? 971  THR   B CG2   1 
ATOM   16225 N  N     . PHE   B 1  974  ? 14.748  41.747  90.250  1.00 13.41 ? 972  PHE   B N     1 
ATOM   16226 C  CA    . PHE   B 1  974  ? 14.892  42.182  91.626  1.00 13.04 ? 972  PHE   B CA    1 
ATOM   16227 C  C     . PHE   B 1  974  ? 13.765  41.582  92.443  1.00 12.61 ? 972  PHE   B C     1 
ATOM   16228 O  O     . PHE   B 1  974  ? 12.608  41.605  92.026  1.00 13.74 ? 972  PHE   B O     1 
ATOM   16229 C  CB    . PHE   B 1  974  ? 14.811  43.704  91.732  1.00 13.47 ? 972  PHE   B CB    1 
ATOM   16230 C  CG    . PHE   B 1  974  ? 14.746  44.173  93.150  1.00 13.61 ? 972  PHE   B CG    1 
ATOM   16231 C  CD1   . PHE   B 1  974  ? 15.900  44.234  93.901  1.00 16.04 ? 972  PHE   B CD1   1 
ATOM   16232 C  CD2   . PHE   B 1  974  ? 13.531  44.495  93.740  1.00 15.41 ? 972  PHE   B CD2   1 
ATOM   16233 C  CE1   . PHE   B 1  974  ? 15.865  44.636  95.223  1.00 15.78 ? 972  PHE   B CE1   1 
ATOM   16234 C  CE2   . PHE   B 1  974  ? 13.476  44.888  95.067  1.00 15.65 ? 972  PHE   B CE2   1 
ATOM   16235 C  CZ    . PHE   B 1  974  ? 14.643  44.951  95.810  1.00 16.76 ? 972  PHE   B CZ    1 
ATOM   16236 N  N     . GLY   B 1  975  ? 14.107  41.069  93.621  1.00 13.78 ? 973  GLY   B N     1 
ATOM   16237 C  CA    . GLY   B 1  975  ? 13.129  40.464  94.505  1.00 15.32 ? 973  GLY   B CA    1 
ATOM   16238 C  C     . GLY   B 1  975  ? 13.054  41.155  95.849  1.00 15.16 ? 973  GLY   B C     1 
ATOM   16239 O  O     . GLY   B 1  975  ? 14.039  41.686  96.349  1.00 15.32 ? 973  GLY   B O     1 
ATOM   16240 N  N     . LEU   B 1  976  ? 11.865  41.144  96.423  1.00 14.65 ? 974  LEU   B N     1 
ATOM   16241 C  CA    . LEU   B 1  976  ? 11.658  41.690  97.753  1.00 14.73 ? 974  LEU   B CA    1 
ATOM   16242 C  C     . LEU   B 1  976  ? 10.767  40.714  98.490  1.00 15.92 ? 974  LEU   B C     1 
ATOM   16243 O  O     . LEU   B 1  976  ? 9.690   40.362  98.002  1.00 15.99 ? 974  LEU   B O     1 
ATOM   16244 C  CB    . LEU   B 1  976  ? 10.971  43.056  97.670  1.00 15.81 ? 974  LEU   B CB    1 
ATOM   16245 C  CG    . LEU   B 1  976  ? 10.577  43.696  99.005  1.00 17.84 ? 974  LEU   B CG    1 
ATOM   16246 C  CD1   . LEU   B 1  976  ? 11.813  44.032  99.834  1.00 20.10 ? 974  LEU   B CD1   1 
ATOM   16247 C  CD2   . LEU   B 1  976  ? 9.751   44.945  98.762  1.00 18.89 ? 974  LEU   B CD2   1 
ATOM   16248 N  N     . HIS   B 1  977  ? 11.219  40.268  99.656  1.00 14.21 ? 975  HIS   B N     1 
ATOM   16249 C  CA    . HIS   B 1  977  ? 10.404  39.450  100.549 1.00 15.45 ? 975  HIS   B CA    1 
ATOM   16250 C  C     . HIS   B 1  977  ? 10.102  40.265  101.796 1.00 16.27 ? 975  HIS   B C     1 
ATOM   16251 O  O     . HIS   B 1  977  ? 11.008  40.592  102.567 1.00 16.23 ? 975  HIS   B O     1 
ATOM   16252 C  CB    . HIS   B 1  977  ? 11.120  38.157  100.926 1.00 16.18 ? 975  HIS   B CB    1 
ATOM   16253 C  CG    . HIS   B 1  977  ? 10.777  37.002  100.044 1.00 18.36 ? 975  HIS   B CG    1 
ATOM   16254 N  ND1   . HIS   B 1  977  ? 9.890   36.017  100.423 1.00 24.30 ? 975  HIS   B ND1   1 
ATOM   16255 C  CD2   . HIS   B 1  977  ? 11.189  36.683  98.797  1.00 24.38 ? 975  HIS   B CD2   1 
ATOM   16256 C  CE1   . HIS   B 1  977  ? 9.785   35.130  99.450  1.00 22.68 ? 975  HIS   B CE1   1 
ATOM   16257 N  NE2   . HIS   B 1  977  ? 10.563  35.510  98.455  1.00 23.98 ? 975  HIS   B NE2   1 
ATOM   16258 N  N     . THR   B 1  978  ? 8.835   40.621  101.961 1.00 16.00 ? 976  THR   B N     1 
ATOM   16259 C  CA    . THR   B 1  978  ? 8.384   41.377  103.118 1.00 16.03 ? 976  THR   B CA    1 
ATOM   16260 C  C     . THR   B 1  978  ? 6.884   41.222  103.200 1.00 17.53 ? 976  THR   B C     1 
ATOM   16261 O  O     . THR   B 1  978  ? 6.214   41.007  102.191 1.00 19.46 ? 976  THR   B O     1 
ATOM   16262 C  CB    . THR   B 1  978  ? 8.741   42.859  103.009 1.00 18.53 ? 976  THR   B CB    1 
ATOM   16263 O  OG1   . THR   B 1  978  ? 8.217   43.554  104.143 1.00 17.03 ? 976  THR   B OG1   1 
ATOM   16264 C  CG2   . THR   B 1  978  ? 8.151   43.467  101.759 1.00 20.87 ? 976  THR   B CG2   1 
ATOM   16265 N  N     . ARG   B 1  979  ? 6.365   41.328  104.407 1.00 18.25 ? 977  ARG   B N     1 
ATOM   16266 C  CA    . ARG   B 1  979  ? 4.926   41.369  104.567 1.00 18.85 ? 977  ARG   B CA    1 
ATOM   16267 C  C     . ARG   B 1  979  ? 4.383   42.787  104.654 1.00 20.56 ? 977  ARG   B C     1 
ATOM   16268 O  O     . ARG   B 1  979  ? 3.167   42.956  104.750 1.00 19.89 ? 977  ARG   B O     1 
ATOM   16269 C  CB    . ARG   B 1  979  ? 4.511   40.555  105.788 1.00 22.50 ? 977  ARG   B CB    1 
ATOM   16270 C  CG    . ARG   B 1  979  ? 4.676   39.081  105.551 1.00 28.87 ? 977  ARG   B CG    1 
ATOM   16271 C  CD    . ARG   B 1  979  ? 4.469   38.313  106.816 1.00 36.46 ? 977  ARG   B CD    1 
ATOM   16272 N  NE    . ARG   B 1  979  ? 4.443   36.878  106.575 1.00 41.16 ? 977  ARG   B NE    1 
ATOM   16273 C  CZ    . ARG   B 1  979  ? 4.218   35.976  107.519 1.00 50.78 ? 977  ARG   B CZ    1 
ATOM   16274 N  NH1   . ARG   B 1  979  ? 3.997   36.333  108.775 1.00 38.43 ? 977  ARG   B NH1   1 
ATOM   16275 N  NH2   . ARG   B 1  979  ? 4.212   34.685  107.196 1.00 49.39 ? 977  ARG   B NH2   1 
ATOM   16276 N  N     . LEU   B 1  980  ? 5.243   43.804  104.598 1.00 17.38 ? 978  LEU   B N     1 
ATOM   16277 C  CA    . LEU   B 1  980  ? 4.895   45.159  105.008 1.00 16.75 ? 978  LEU   B CA    1 
ATOM   16278 C  C     . LEU   B 1  980  ? 4.683   46.050  103.794 1.00 17.89 ? 978  LEU   B C     1 
ATOM   16279 O  O     . LEU   B 1  980  ? 5.617   46.278  103.019 1.00 18.52 ? 978  LEU   B O     1 
ATOM   16280 C  CB    . LEU   B 1  980  ? 6.022   45.727  105.863 1.00 18.74 ? 978  LEU   B CB    1 
ATOM   16281 C  CG    . LEU   B 1  980  ? 6.365   44.830  107.053 1.00 20.65 ? 978  LEU   B CG    1 
ATOM   16282 C  CD1   . LEU   B 1  980  ? 7.498   45.447  107.872 1.00 20.86 ? 978  LEU   B CD1   1 
ATOM   16283 C  CD2   . LEU   B 1  980  ? 5.138   44.551  107.923 1.00 19.16 ? 978  LEU   B CD2   1 
ATOM   16284 N  N     . ASP   B 1  981  ? 3.471   46.592  103.658 1.00 18.16 ? 979  ASP   B N     1 
ATOM   16285 C  CA    . ASP   B 1  981  ? 3.159   47.409  102.489 1.00 17.28 ? 979  ASP   B CA    1 
ATOM   16286 C  C     . ASP   B 1  981  ? 4.060   48.632  102.387 1.00 17.72 ? 979  ASP   B C     1 
ATOM   16287 O  O     . ASP   B 1  981  ? 4.388   49.066  101.280 1.00 18.07 ? 979  ASP   B O     1 
ATOM   16288 C  CB    . ASP   B 1  981  ? 1.702   47.860  102.517 1.00 18.57 ? 979  ASP   B CB    1 
ATOM   16289 C  CG    . ASP   B 1  981  ? 0.734   46.751  102.226 1.00 20.49 ? 979  ASP   B CG    1 
ATOM   16290 O  OD1   . ASP   B 1  981  ? 1.133   45.705  101.673 1.00 23.32 ? 979  ASP   B OD1   1 
ATOM   16291 O  OD2   . ASP   B 1  981  ? -0.457  46.964  102.541 1.00 23.39 ? 979  ASP   B OD2   1 
ATOM   16292 N  N     . GLU   B 1  982  ? 4.441   49.232  103.517 1.00 16.64 ? 980  GLU   B N     1 
ATOM   16293 C  CA    . GLU   B 1  982  ? 5.295   50.417  103.443 1.00 17.63 ? 980  GLU   B CA    1 
ATOM   16294 C  C     . GLU   B 1  982  ? 6.651   50.066  102.852 1.00 17.78 ? 980  GLU   B C     1 
ATOM   16295 O  O     . GLU   B 1  982  ? 7.225   50.843  102.079 1.00 18.34 ? 980  GLU   B O     1 
ATOM   16296 C  CB    . GLU   B 1  982  ? 5.479   51.050  104.823 1.00 19.46 ? 980  GLU   B CB    1 
ATOM   16297 C  CG    . GLU   B 1  982  ? 6.352   52.295  104.780 1.00 22.97 ? 980  GLU   B CG    1 
ATOM   16298 C  CD    . GLU   B 1  982  ? 6.868   52.703  106.142 1.00 28.51 ? 980  GLU   B CD    1 
ATOM   16299 O  OE1   . GLU   B 1  982  ? 7.163   51.810  106.970 1.00 34.21 ? 980  GLU   B OE1   1 
ATOM   16300 O  OE2   . GLU   B 1  982  ? 6.987   53.916  106.381 1.00 27.11 ? 980  GLU   B OE2   1 
ATOM   16301 N  N     . THR   B 1  983  ? 7.186   48.910  103.231 1.00 17.57 ? 981  THR   B N     1 
ATOM   16302 C  CA    . THR   B 1  983  ? 8.460   48.475  102.685 1.00 16.33 ? 981  THR   B CA    1 
ATOM   16303 C  C     . THR   B 1  983  ? 8.336   48.163  101.203 1.00 16.79 ? 981  THR   B C     1 
ATOM   16304 O  O     . THR   B 1  983  ? 9.237   48.490  100.417 1.00 17.45 ? 981  THR   B O     1 
ATOM   16305 C  CB    . THR   B 1  983  ? 8.956   47.268  103.473 1.00 17.72 ? 981  THR   B CB    1 
ATOM   16306 O  OG1   . THR   B 1  983  ? 9.179   47.668  104.829 1.00 19.66 ? 981  THR   B OG1   1 
ATOM   16307 C  CG2   . THR   B 1  983  ? 10.254  46.750  102.880 1.00 18.33 ? 981  THR   B CG2   1 
ATOM   16308 N  N     . ILE   B 1  984  ? 7.222   47.548  100.798 1.00 16.02 ? 982  ILE   B N     1 
ATOM   16309 C  CA    . ILE   B 1  984  ? 6.995   47.285  99.382  1.00 16.07 ? 982  ILE   B CA    1 
ATOM   16310 C  C     . ILE   B 1  984  ? 6.945   48.588  98.604  1.00 16.49 ? 982  ILE   B C     1 
ATOM   16311 O  O     . ILE   B 1  984  ? 7.604   48.734  97.567  1.00 17.47 ? 982  ILE   B O     1 
ATOM   16312 C  CB    . ILE   B 1  984  ? 5.720   46.451  99.185  1.00 16.05 ? 982  ILE   B CB    1 
ATOM   16313 C  CG1   . ILE   B 1  984  ? 5.924   45.057  99.752  1.00 21.06 ? 982  ILE   B CG1   1 
ATOM   16314 C  CG2   . ILE   B 1  984  ? 5.376   46.332  97.713  1.00 18.08 ? 982  ILE   B CG2   1 
ATOM   16315 C  CD1   . ILE   B 1  984  ? 4.642   44.252  99.850  1.00 19.79 ? 982  ILE   B CD1   1 
ATOM   16316 N  N     . ALA   B 1  985  ? 6.187   49.567  99.103  1.00 16.71 ? 983  ALA   B N     1 
ATOM   16317 C  CA    . ALA   B 1  985  ? 6.067   50.829  98.377  1.00 17.69 ? 983  ALA   B CA    1 
ATOM   16318 C  C     . ALA   B 1  985  ? 7.410   51.533  98.292  1.00 17.30 ? 983  ALA   B C     1 
ATOM   16319 O  O     . ALA   B 1  985  ? 7.792   52.025  97.224  1.00 18.06 ? 983  ALA   B O     1 
ATOM   16320 C  CB    . ALA   B 1  985  ? 5.021   51.735  99.029  1.00 17.20 ? 983  ALA   B CB    1 
ATOM   16321 N  N     . HIS   B 1  986  ? 8.151   51.563  99.400  1.00 17.68 ? 984  HIS   B N     1 
ATOM   16322 C  CA    . HIS   B 1  986  ? 9.448   52.227  99.411  1.00 18.60 ? 984  HIS   B CA    1 
ATOM   16323 C  C     . HIS   B 1  986  ? 10.378  51.570  98.408  1.00 18.25 ? 984  HIS   B C     1 
ATOM   16324 O  O     . HIS   B 1  986  ? 10.904  52.222  97.502  1.00 17.72 ? 984  HIS   B O     1 
ATOM   16325 C  CB    . HIS   B 1  986  ? 10.036  52.147  100.825 1.00 19.55 ? 984  HIS   B CB    1 
ATOM   16326 C  CG    . HIS   B 1  986  ? 11.425  52.695  100.958 1.00 21.03 ? 984  HIS   B CG    1 
ATOM   16327 N  ND1   . HIS   B 1  986  ? 12.044  52.827  102.181 1.00 26.04 ? 984  HIS   B ND1   1 
ATOM   16328 C  CD2   . HIS   B 1  986  ? 12.319  53.133  100.038 1.00 21.26 ? 984  HIS   B CD2   1 
ATOM   16329 C  CE1   . HIS   B 1  986  ? 13.254  53.330  102.012 1.00 24.07 ? 984  HIS   B CE1   1 
ATOM   16330 N  NE2   . HIS   B 1  986  ? 13.449  53.516  100.720 1.00 22.70 ? 984  HIS   B NE2   1 
ATOM   16331 N  N     . VAL   B 1  987  ? 10.564  50.264  98.543  1.00 16.07 ? 985  VAL   B N     1 
ATOM   16332 C  CA    . VAL   B 1  987  ? 11.576  49.589  97.747  1.00 16.84 ? 985  VAL   B CA    1 
ATOM   16333 C  C     . VAL   B 1  987  ? 11.208  49.611  96.278  1.00 17.49 ? 985  VAL   B C     1 
ATOM   16334 O  O     . VAL   B 1  987  ? 12.057  49.886  95.426  1.00 18.27 ? 985  VAL   B O     1 
ATOM   16335 C  CB    . VAL   B 1  987  ? 11.791  48.165  98.271  1.00 16.96 ? 985  VAL   B CB    1 
ATOM   16336 C  CG1   . VAL   B 1  987  ? 12.656  47.383  97.303  1.00 18.65 ? 985  VAL   B CG1   1 
ATOM   16337 C  CG2   . VAL   B 1  987  ? 12.440  48.227  99.647  1.00 16.46 ? 985  VAL   B CG2   1 
ATOM   16338 N  N     . THR   B 1  988  ? 9.947   49.321  95.949  1.00 17.49 ? 986  THR   B N     1 
ATOM   16339 C  CA    . THR   B 1  988  ? 9.573   49.310  94.536  1.00 17.87 ? 986  THR   B CA    1 
ATOM   16340 C  C     . THR   B 1  988  ? 9.613   50.704  93.922  1.00 18.77 ? 986  THR   B C     1 
ATOM   16341 O  O     . THR   B 1  988  ? 9.825   50.816  92.710  1.00 23.52 ? 986  THR   B O     1 
ATOM   16342 C  CB    . THR   B 1  988  ? 8.217   48.625  94.306  1.00 20.62 ? 986  THR   B CB    1 
ATOM   16343 O  OG1   . THR   B 1  988  ? 7.184   49.349  94.969  1.00 22.89 ? 986  THR   B OG1   1 
ATOM   16344 C  CG2   . THR   B 1  988  ? 8.244   47.191  94.812  1.00 22.95 ? 986  THR   B CG2   1 
ATOM   16345 N  N     . SER   B 1  989  ? 9.453   51.758  94.723  1.00 18.77 ? 987  SER   B N     1 
ATOM   16346 C  CA    . SER   B 1  989  ? 9.555   53.112  94.193  1.00 21.30 ? 987  SER   B CA    1 
ATOM   16347 C  C     . SER   B 1  989  ? 10.994  53.515  93.907  1.00 22.16 ? 987  SER   B C     1 
ATOM   16348 O  O     . SER   B 1  989  ? 11.217  54.421  93.096  1.00 28.86 ? 987  SER   B O     1 
ATOM   16349 C  CB    . SER   B 1  989  ? 8.893   54.140  95.122  1.00 23.41 ? 987  SER   B CB    1 
ATOM   16350 O  OG    . SER   B 1  989  ? 9.606   54.321  96.336  1.00 30.78 ? 987  SER   B OG    1 
ATOM   16351 N  N     . ARG   B 1  990  ? 11.972  52.863  94.536  1.00 18.39 ? 988  ARG   B N     1 
ATOM   16352 C  CA    . ARG   B 1  990  ? 13.359  53.297  94.450  1.00 18.10 ? 988  ARG   B CA    1 
ATOM   16353 C  C     . ARG   B 1  990  ? 14.240  52.356  93.646  1.00 17.77 ? 988  ARG   B C     1 
ATOM   16354 O  O     . ARG   B 1  990  ? 15.272  52.794  93.129  1.00 18.23 ? 988  ARG   B O     1 
ATOM   16355 C  CB    . ARG   B 1  990  ? 13.966  53.442  95.855  1.00 19.93 ? 988  ARG   B CB    1 
ATOM   16356 C  CG    . ARG   B 1  990  ? 13.129  54.265  96.823  1.00 25.66 ? 988  ARG   B CG    1 
ATOM   16357 C  CD    . ARG   B 1  990  ? 13.280  55.741  96.577  1.00 27.48 ? 988  ARG   B CD    1 
ATOM   16358 N  NE    . ARG   B 1  990  ? 14.408  56.300  97.314  1.00 21.71 ? 988  ARG   B NE    1 
ATOM   16359 C  CZ    . ARG   B 1  990  ? 14.773  57.572  97.243  1.00 21.69 ? 988  ARG   B CZ    1 
ATOM   16360 N  NH1   . ARG   B 1  990  ? 14.167  58.418  96.425  1.00 26.12 ? 988  ARG   B NH1   1 
ATOM   16361 N  NH2   . ARG   B 1  990  ? 15.758  58.008  98.019  1.00 22.08 ? 988  ARG   B NH2   1 
ATOM   16362 N  N     . ILE   B 1  991  ? 13.876  51.078  93.544  1.00 15.97 ? 989  ILE   B N     1 
ATOM   16363 C  CA    . ILE   B 1  991  ? 14.674  50.145  92.761  1.00 17.52 ? 989  ILE   B CA    1 
ATOM   16364 C  C     . ILE   B 1  991  ? 14.522  50.480  91.283  1.00 17.55 ? 989  ILE   B C     1 
ATOM   16365 O  O     . ILE   B 1  991  ? 13.479  50.972  90.840  1.00 19.49 ? 989  ILE   B O     1 
ATOM   16366 C  CB    . ILE   B 1  991  ? 14.219  48.706  93.064  1.00 17.87 ? 989  ILE   B CB    1 
ATOM   16367 C  CG1   . ILE   B 1  991  ? 15.228  47.689  92.541  1.00 20.65 ? 989  ILE   B CG1   1 
ATOM   16368 C  CG2   . ILE   B 1  991  ? 12.845  48.437  92.474  1.00 19.70 ? 989  ILE   B CG2   1 
ATOM   16369 C  CD1   . ILE   B 1  991  ? 16.544  47.747  93.275  1.00 23.74 ? 989  ILE   B CD1   1 
ATOM   16370 N  N     . LYS   B 1  992  ? 15.576  50.244  90.514  1.00 15.66 ? 990  LYS   B N     1 
ATOM   16371 C  CA    . LYS   B 1  992  ? 15.562  50.533  89.081  1.00 17.38 ? 990  LYS   B CA    1 
ATOM   16372 C  C     . LYS   B 1  992  ? 15.859  49.229  88.357  1.00 18.57 ? 990  LYS   B C     1 
ATOM   16373 O  O     . LYS   B 1  992  ? 16.978  48.984  87.919  1.00 22.00 ? 990  LYS   B O     1 
ATOM   16374 C  CB    . LYS   B 1  992  ? 16.598  51.614  88.754  1.00 17.92 ? 990  LYS   B CB    1 
ATOM   16375 C  CG    . LYS   B 1  992  ? 16.276  52.953  89.392  1.00 22.42 ? 990  LYS   B CG    1 
ATOM   16376 C  CD    . LYS   B 1  992  ? 17.381  53.968  89.120  1.00 28.67 ? 990  LYS   B CD    1 
ATOM   16377 C  CE    . LYS   B 1  992  ? 17.614  54.162  87.625  1.00 33.78 ? 990  LYS   B CE    1 
ATOM   16378 N  NZ    . LYS   B 1  992  ? 18.887  54.899  87.342  1.00 41.30 ? 990  LYS   B NZ    1 
ATOM   16379 N  N     . ALA   B 1  993  ? 14.851  48.379  88.244  1.00 16.88 ? 991  ALA   B N     1 
ATOM   16380 C  CA    . ALA   B 1  993  ? 15.008  47.104  87.566  1.00 15.40 ? 991  ALA   B CA    1 
ATOM   16381 C  C     . ALA   B 1  993  ? 13.763  46.858  86.735  1.00 15.30 ? 991  ALA   B C     1 
ATOM   16382 O  O     . ALA   B 1  993  ? 12.676  47.351  87.054  1.00 16.86 ? 991  ALA   B O     1 
ATOM   16383 C  CB    . ALA   B 1  993  ? 15.233  45.949  88.549  1.00 18.42 ? 991  ALA   B CB    1 
ATOM   16384 N  N     . GLY   B 1  994  ? 13.938  46.116  85.643  1.00 14.47 ? 992  GLY   B N     1 
ATOM   16385 C  CA    . GLY   B 1  994  ? 12.824  45.901  84.735  1.00 15.09 ? 992  GLY   B CA    1 
ATOM   16386 C  C     . GLY   B 1  994  ? 11.830  44.846  85.161  1.00 15.03 ? 992  GLY   B C     1 
ATOM   16387 O  O     . GLY   B 1  994  ? 10.691  44.881  84.702  1.00 13.60 ? 992  GLY   B O     1 
ATOM   16388 N  N     . ASN   B 1  995  ? 12.226  43.903  86.008  1.00 14.33 ? 993  ASN   B N     1 
ATOM   16389 C  CA    . ASN   B 1  995  ? 11.351  42.823  86.445  1.00 13.67 ? 993  ASN   B CA    1 
ATOM   16390 C  C     . ASN   B 1  995  ? 11.471  42.735  87.952  1.00 13.69 ? 993  ASN   B C     1 
ATOM   16391 O  O     . ASN   B 1  995  ? 12.541  42.407  88.471  1.00 14.06 ? 993  ASN   B O     1 
ATOM   16392 C  CB    . ASN   B 1  995  ? 11.730  41.497  85.790  1.00 14.27 ? 993  ASN   B CB    1 
ATOM   16393 C  CG    . ASN   B 1  995  ? 11.199  41.404  84.395  1.00 15.83 ? 993  ASN   B CG    1 
ATOM   16394 O  OD1   . ASN   B 1  995  ? 11.808  41.908  83.452  1.00 14.32 ? 993  ASN   B OD1   1 
ATOM   16395 N  ND2   . ASN   B 1  995  ? 10.022  40.807  84.258  1.00 15.39 ? 993  ASN   B ND2   1 
ATOM   16396 N  N     . LEU   B 1  996  ? 10.375  43.035  88.629  1.00 13.68 ? 994  LEU   B N     1 
ATOM   16397 C  CA    . LEU   B 1  996  ? 10.304  43.013  90.078  1.00 12.96 ? 994  LEU   B CA    1 
ATOM   16398 C  C     . LEU   B 1  996  ? 9.452   41.833  90.492  1.00 13.11 ? 994  LEU   B C     1 
ATOM   16399 O  O     . LEU   B 1  996  ? 8.497   41.465  89.799  1.00 13.88 ? 994  LEU   B O     1 
ATOM   16400 C  CB    . LEU   B 1  996  ? 9.666   44.300  90.599  1.00 14.55 ? 994  LEU   B CB    1 
ATOM   16401 C  CG    . LEU   B 1  996  ? 10.245  45.595  90.023  1.00 15.65 ? 994  LEU   B CG    1 
ATOM   16402 C  CD1   . LEU   B 1  996  ? 9.511   46.806  90.622  1.00 20.02 ? 994  LEU   B CD1   1 
ATOM   16403 C  CD2   . LEU   B 1  996  ? 11.749  45.694  90.210  1.00 16.68 ? 994  LEU   B CD2   1 
ATOM   16404 N  N     . TYR   B 1  997  ? 9.774   41.268  91.654  1.00 13.53 ? 995  TYR   B N     1 
ATOM   16405 C  CA    . TYR   B 1  997  ? 9.080   40.090  92.163  1.00 14.32 ? 995  TYR   B CA    1 
ATOM   16406 C  C     . TYR   B 1  997  ? 8.922   40.261  93.656  1.00 13.76 ? 995  TYR   B C     1 
ATOM   16407 O  O     . TYR   B 1  997  ? 9.903   40.509  94.361  1.00 15.96 ? 995  TYR   B O     1 
ATOM   16408 C  CB    . TYR   B 1  997  ? 9.862   38.803  91.897  1.00 15.73 ? 995  TYR   B CB    1 
ATOM   16409 C  CG    . TYR   B 1  997  ? 10.223  38.643  90.436  1.00 14.62 ? 995  TYR   B CG    1 
ATOM   16410 C  CD1   . TYR   B 1  997  ? 11.363  39.233  89.924  1.00 13.73 ? 995  TYR   B CD1   1 
ATOM   16411 C  CD2   . TYR   B 1  997  ? 9.427   37.908  89.579  1.00 15.83 ? 995  TYR   B CD2   1 
ATOM   16412 C  CE1   . TYR   B 1  997  ? 11.697  39.113  88.608  1.00 16.10 ? 995  TYR   B CE1   1 
ATOM   16413 C  CE2   . TYR   B 1  997  ? 9.763   37.767  88.239  1.00 15.89 ? 995  TYR   B CE2   1 
ATOM   16414 C  CZ    . TYR   B 1  997  ? 10.909  38.376  87.775  1.00 16.53 ? 995  TYR   B CZ    1 
ATOM   16415 O  OH    . TYR   B 1  997  ? 11.273  38.268  86.441  1.00 19.35 ? 995  TYR   B OH    1 
ATOM   16416 N  N     . ILE   B 1  998  ? 7.691   40.150  94.128  1.00 14.52 ? 996  ILE   B N     1 
ATOM   16417 C  CA    . ILE   B 1  998  ? 7.385   40.363  95.534  1.00 13.80 ? 996  ILE   B CA    1 
ATOM   16418 C  C     . ILE   B 1  998  ? 6.948   39.036  96.135  1.00 16.44 ? 996  ILE   B C     1 
ATOM   16419 O  O     . ILE   B 1  998  ? 5.940   38.454  95.717  1.00 15.53 ? 996  ILE   B O     1 
ATOM   16420 C  CB    . ILE   B 1  998  ? 6.302   41.439  95.711  1.00 16.86 ? 996  ILE   B CB    1 
ATOM   16421 C  CG1   . ILE   B 1  998  ? 6.700   42.742  95.002  1.00 20.33 ? 996  ILE   B CG1   1 
ATOM   16422 C  CG2   . ILE   B 1  998  ? 6.018   41.674  97.193  1.00 17.37 ? 996  ILE   B CG2   1 
ATOM   16423 C  CD1   . ILE   B 1  998  ? 7.970   43.360  95.490  1.00 23.59 ? 996  ILE   B CD1   1 
ATOM   16424 N  N     . ASN   B 1  999  ? 7.713   38.560  97.121  1.00 14.22 ? 997  ASN   B N     1 
ATOM   16425 C  CA    . ASN   B 1  999  ? 7.351   37.375  97.904  1.00 15.75 ? 997  ASN   B CA    1 
ATOM   16426 C  C     . ASN   B 1  999  ? 7.294   36.118  97.043  1.00 14.42 ? 997  ASN   B C     1 
ATOM   16427 O  O     . ASN   B 1  999  ? 6.475   35.226  97.261  1.00 16.07 ? 997  ASN   B O     1 
ATOM   16428 C  CB    . ASN   B 1  999  ? 6.061   37.588  98.691  1.00 15.55 ? 997  ASN   B CB    1 
ATOM   16429 C  CG    . ASN   B 1  999  ? 6.225   38.631  99.742  1.00 16.23 ? 997  ASN   B CG    1 
ATOM   16430 O  OD1   . ASN   B 1  999  ? 7.302   38.762  100.305 1.00 16.50 ? 997  ASN   B OD1   1 
ATOM   16431 N  ND2   . ASN   B 1  999  ? 5.173   39.400  100.008 1.00 17.23 ? 997  ASN   B ND2   1 
ATOM   16432 N  N     . ARG   B 1  1000 ? 8.198   36.036  96.075  1.00 15.79 ? 998  ARG   B N     1 
ATOM   16433 C  CA    . ARG   B 1  1000 ? 8.307   34.871  95.211  1.00 15.34 ? 998  ARG   B CA    1 
ATOM   16434 C  C     . ARG   B 1  1000 ? 9.725   34.838  94.665  1.00 16.71 ? 998  ARG   B C     1 
ATOM   16435 O  O     . ARG   B 1  1000 ? 10.549  35.704  94.967  1.00 17.24 ? 998  ARG   B O     1 
ATOM   16436 C  CB    . ARG   B 1  1000 ? 7.283   34.929  94.078  1.00 15.44 ? 998  ARG   B CB    1 
ATOM   16437 C  CG    . ARG   B 1  1000 ? 7.286   36.271  93.342  1.00 16.48 ? 998  ARG   B CG    1 
ATOM   16438 C  CD    . ARG   B 1  1000 ? 6.791   36.115  91.904  1.00 15.65 ? 998  ARG   B CD    1 
ATOM   16439 N  NE    . ARG   B 1  1000 ? 7.706   35.294  91.130  1.00 13.16 ? 998  ARG   B NE    1 
ATOM   16440 C  CZ    . ARG   B 1  1000 ? 7.414   34.827  89.927  1.00 14.08 ? 998  ARG   B CZ    1 
ATOM   16441 N  NH1   . ARG   B 1  1000 ? 6.268   35.136  89.331  1.00 16.57 ? 998  ARG   B NH1   1 
ATOM   16442 N  NH2   . ARG   B 1  1000 ? 8.284   34.030  89.316  1.00 15.94 ? 998  ARG   B NH2   1 
ATOM   16443 N  N     . ASN   B 1  1001 ? 10.007  33.830  93.847  1.00 13.90 ? 999  ASN   B N     1 
ATOM   16444 C  CA    . ASN   B 1  1001 ? 11.328  33.776  93.243  1.00 14.79 ? 999  ASN   B CA    1 
ATOM   16445 C  C     . ASN   B 1  1001 ? 11.456  34.881  92.192  1.00 14.50 ? 999  ASN   B C     1 
ATOM   16446 O  O     . ASN   B 1  1001 ? 10.479  35.536  91.823  1.00 16.10 ? 999  ASN   B O     1 
ATOM   16447 C  CB    . ASN   B 1  1001 ? 11.601  32.384  92.665  1.00 16.26 ? 999  ASN   B CB    1 
ATOM   16448 C  CG    . ASN   B 1  1001 ? 10.756  32.064  91.446  1.00 18.33 ? 999  ASN   B CG    1 
ATOM   16449 O  OD1   . ASN   B 1  1001 ? 10.642  32.853  90.514  1.00 17.67 ? 999  ASN   B OD1   1 
ATOM   16450 N  ND2   . ASN   B 1  1001 ? 10.154  30.885  91.456  1.00 27.23 ? 999  ASN   B ND2   1 
ATOM   16451 N  N     . ILE   B 1  1002 ? 12.673  35.102  91.714  1.00 15.27 ? 1000 ILE   B N     1 
ATOM   16452 C  CA    . ILE   B 1  1002 ? 12.918  36.205  90.795  1.00 15.41 ? 1000 ILE   B CA    1 
ATOM   16453 C  C     . ILE   B 1  1002 ? 13.218  35.719  89.383  1.00 15.94 ? 1000 ILE   B C     1 
ATOM   16454 O  O     . ILE   B 1  1002 ? 13.818  36.442  88.605  1.00 16.27 ? 1000 ILE   B O     1 
ATOM   16455 C  CB    . ILE   B 1  1002 ? 14.001  37.173  91.305  1.00 15.89 ? 1000 ILE   B CB    1 
ATOM   16456 C  CG1   . ILE   B 1  1002 ? 15.390  36.515  91.321  1.00 15.07 ? 1000 ILE   B CG1   1 
ATOM   16457 C  CG2   . ILE   B 1  1002 ? 13.613  37.711  92.663  1.00 16.27 ? 1000 ILE   B CG2   1 
ATOM   16458 C  CD1   . ILE   B 1  1002 ? 16.502  37.516  91.540  1.00 15.14 ? 1000 ILE   B CD1   1 
ATOM   16459 N  N     . ILE   B 1  1003 ? 12.806  34.510  89.031  1.00 16.04 ? 1001 ILE   B N     1 
ATOM   16460 C  CA    . ILE   B 1  1003 ? 13.170  33.992  87.721  1.00 17.29 ? 1001 ILE   B CA    1 
ATOM   16461 C  C     . ILE   B 1  1003 ? 11.977  33.914  86.777  1.00 24.90 ? 1001 ILE   B C     1 
ATOM   16462 O  O     . ILE   B 1  1003 ? 12.082  33.319  85.703  1.00 23.42 ? 1001 ILE   B O     1 
ATOM   16463 C  CB    . ILE   B 1  1003 ? 13.980  32.693  87.813  1.00 20.32 ? 1001 ILE   B CB    1 
ATOM   16464 C  CG1   . ILE   B 1  1003 ? 13.223  31.610  88.569  1.00 24.34 ? 1001 ILE   B CG1   1 
ATOM   16465 C  CG2   . ILE   B 1  1003 ? 15.304  32.978  88.534  1.00 19.80 ? 1001 ILE   B CG2   1 
ATOM   16466 C  CD1   . ILE   B 1  1003 ? 13.945  30.282  88.517  1.00 31.17 ? 1001 ILE   B CD1   1 
ATOM   16467 N  N     . GLY   B 1  1004 ? 10.869  34.572  87.120  1.00 20.81 ? 1002 GLY   B N     1 
ATOM   16468 C  CA    . GLY   B 1  1004 ? 9.677   34.525  86.285  1.00 19.52 ? 1002 GLY   B CA    1 
ATOM   16469 C  C     . GLY   B 1  1004 ? 9.812   35.361  85.025  1.00 19.98 ? 1002 GLY   B C     1 
ATOM   16470 O  O     . GLY   B 1  1004 ? 10.104  36.563  85.073  1.00 22.11 ? 1002 GLY   B O     1 
ATOM   16471 N  N     . ALA   B 1  1005 ? 9.581   34.725  83.889  1.00 19.11 ? 1003 ALA   B N     1 
ATOM   16472 C  CA    . ALA   B 1  1005 ? 9.610   35.397  82.610  1.00 21.09 ? 1003 ALA   B CA    1 
ATOM   16473 C  C     . ALA   B 1  1005 ? 8.463   34.894  81.774  1.00 20.30 ? 1003 ALA   B C     1 
ATOM   16474 O  O     . ALA   B 1  1005 ? 8.591   34.705  80.558  1.00 20.93 ? 1003 ALA   B O     1 
ATOM   16475 C  CB    . ALA   B 1  1005 ? 10.939  35.172  81.888  1.00 19.57 ? 1003 ALA   B CB    1 
ATOM   16476 N  N     . VAL   B 1  1006 ? 7.317   34.668  82.416  1.00 15.87 ? 1004 VAL   B N     1 
ATOM   16477 C  CA    . VAL   B 1  1006 ? 6.184   34.113  81.687  1.00 16.90 ? 1004 VAL   B CA    1 
ATOM   16478 C  C     . VAL   B 1  1006 ? 5.763   35.106  80.619  1.00 16.56 ? 1004 VAL   B C     1 
ATOM   16479 O  O     . VAL   B 1  1006 ? 5.453   36.266  80.911  1.00 15.74 ? 1004 VAL   B O     1 
ATOM   16480 C  CB    . VAL   B 1  1006 ? 5.040   33.751  82.637  1.00 17.53 ? 1004 VAL   B CB    1 
ATOM   16481 C  CG1   . VAL   B 1  1006 ? 3.845   33.254  81.823  1.00 18.05 ? 1004 VAL   B CG1   1 
ATOM   16482 C  CG2   . VAL   B 1  1006 ? 5.488   32.673  83.624  1.00 18.47 ? 1004 VAL   B CG2   1 
ATOM   16483 N  N     . VAL   B 1  1007 ? 5.793   34.652  79.363  1.00 16.69 ? 1005 VAL   B N     1 
ATOM   16484 C  CA    . VAL   B 1  1007 ? 5.534   35.524  78.226  1.00 16.23 ? 1005 VAL   B CA    1 
ATOM   16485 C  C     . VAL   B 1  1007 ? 4.170   36.181  78.379  1.00 15.84 ? 1005 VAL   B C     1 
ATOM   16486 O  O     . VAL   B 1  1007 ? 3.173   35.519  78.688  1.00 16.10 ? 1005 VAL   B O     1 
ATOM   16487 C  CB    . VAL   B 1  1007 ? 5.611   34.691  76.944  1.00 16.17 ? 1005 VAL   B CB    1 
ATOM   16488 C  CG1   . VAL   B 1  1007 ? 5.238   35.542  75.769  1.00 16.10 ? 1005 VAL   B CG1   1 
ATOM   16489 C  CG2   . VAL   B 1  1007 ? 7.010   34.121  76.773  1.00 17.89 ? 1005 VAL   B CG2   1 
ATOM   16490 N  N     . GLY   B 1  1008 ? 4.117   37.494  78.154  1.00 15.50 ? 1006 GLY   B N     1 
ATOM   16491 C  CA    . GLY   B 1  1008 ? 2.864   38.218  78.254  1.00 15.01 ? 1006 GLY   B CA    1 
ATOM   16492 C  C     . GLY   B 1  1008 ? 2.300   38.343  79.652  1.00 16.46 ? 1006 GLY   B C     1 
ATOM   16493 O  O     . GLY   B 1  1008 ? 1.203   38.895  79.810  1.00 19.04 ? 1006 GLY   B O     1 
ATOM   16494 N  N     . VAL   B 1  1009 ? 2.997   37.825  80.659  1.00 15.39 ? 1007 VAL   B N     1 
ATOM   16495 C  CA    . VAL   B 1  1009 ? 2.584   37.905  82.053  1.00 15.98 ? 1007 VAL   B CA    1 
ATOM   16496 C  C     . VAL   B 1  1009 ? 3.625   38.640  82.887  1.00 16.59 ? 1007 VAL   B C     1 
ATOM   16497 O  O     . VAL   B 1  1009 ? 3.301   39.588  83.610  1.00 16.81 ? 1007 VAL   B O     1 
ATOM   16498 C  CB    . VAL   B 1  1009 ? 2.294   36.502  82.638  1.00 16.54 ? 1007 VAL   B CB    1 
ATOM   16499 C  CG1   . VAL   B 1  1009 ? 1.827   36.612  84.079  1.00 16.58 ? 1007 VAL   B CG1   1 
ATOM   16500 C  CG2   . VAL   B 1  1009 ? 1.230   35.785  81.810  1.00 15.95 ? 1007 VAL   B CG2   1 
ATOM   16501 N  N     . GLN   B 1  1010 ? 4.886   38.216  82.788  1.00 15.38 ? 1008 GLN   B N     1 
ATOM   16502 C  CA    . GLN   B 1  1010 ? 6.048   39.024  83.166  1.00 14.92 ? 1008 GLN   B CA    1 
ATOM   16503 C  C     . GLN   B 1  1010 ? 6.867   39.313  81.912  1.00 15.56 ? 1008 GLN   B C     1 
ATOM   16504 O  O     . GLN   B 1  1010 ? 7.899   38.671  81.687  1.00 17.01 ? 1008 GLN   B O     1 
ATOM   16505 C  CB    . GLN   B 1  1010 ? 6.923   38.319  84.200  1.00 16.73 ? 1008 GLN   B CB    1 
ATOM   16506 C  CG    . GLN   B 1  1010 ? 6.210   37.969  85.491  1.00 18.01 ? 1008 GLN   B CG    1 
ATOM   16507 C  CD    . GLN   B 1  1010 ? 5.795   36.524  85.545  1.00 17.92 ? 1008 GLN   B CD    1 
ATOM   16508 O  OE1   . GLN   B 1  1010 ? 6.497   35.644  85.058  1.00 18.44 ? 1008 GLN   B OE1   1 
ATOM   16509 N  NE2   . GLN   B 1  1010 ? 4.653   36.264  86.167  1.00 17.01 ? 1008 GLN   B NE2   1 
ATOM   16510 N  N     . PRO   B 1  1011 ? 6.427   40.252  81.065  1.00 14.22 ? 1009 PRO   B N     1 
ATOM   16511 C  CA    . PRO   B 1  1011 ? 7.293   40.718  79.975  1.00 15.26 ? 1009 PRO   B CA    1 
ATOM   16512 C  C     . PRO   B 1  1011 ? 8.664   41.000  80.553  1.00 13.61 ? 1009 PRO   B C     1 
ATOM   16513 O  O     . PRO   B 1  1011 ? 8.792   41.623  81.610  1.00 14.23 ? 1009 PRO   B O     1 
ATOM   16514 C  CB    . PRO   B 1  1011 ? 6.609   42.006  79.509  1.00 15.35 ? 1009 PRO   B CB    1 
ATOM   16515 C  CG    . PRO   B 1  1011 ? 5.165   41.769  79.820  1.00 16.86 ? 1009 PRO   B CG    1 
ATOM   16516 C  CD    . PRO   B 1  1011 ? 5.178   41.027  81.139  1.00 16.88 ? 1009 PRO   B CD    1 
ATOM   16517 N  N     . PHE   B 1  1012 ? 9.685   40.472  79.905  1.00 13.82 ? 1010 PHE   B N     1 
ATOM   16518 C  CA    . PHE   B 1  1012 ? 10.967  40.306  80.549  1.00 13.79 ? 1010 PHE   B CA    1 
ATOM   16519 C  C     . PHE   B 1  1012 ? 12.020  41.173  79.885  1.00 14.33 ? 1010 PHE   B C     1 
ATOM   16520 O  O     . PHE   B 1  1012 ? 12.177  41.149  78.663  1.00 15.14 ? 1010 PHE   B O     1 
ATOM   16521 C  CB    . PHE   B 1  1012 ? 11.403  38.846  80.537  1.00 14.64 ? 1010 PHE   B CB    1 
ATOM   16522 C  CG    . PHE   B 1  1012 ? 12.623  38.622  81.339  1.00 13.64 ? 1010 PHE   B CG    1 
ATOM   16523 C  CD1   . PHE   B 1  1012 ? 12.533  38.452  82.705  1.00 15.00 ? 1010 PHE   B CD1   1 
ATOM   16524 C  CD2   . PHE   B 1  1012 ? 13.868  38.651  80.740  1.00 15.22 ? 1010 PHE   B CD2   1 
ATOM   16525 C  CE1   . PHE   B 1  1012 ? 13.681  38.273  83.463  1.00 15.61 ? 1010 PHE   B CE1   1 
ATOM   16526 C  CE2   . PHE   B 1  1012 ? 15.027  38.483  81.495  1.00 15.63 ? 1010 PHE   B CE2   1 
ATOM   16527 C  CZ    . PHE   B 1  1012 ? 14.925  38.292  82.855  1.00 16.82 ? 1010 PHE   B CZ    1 
ATOM   16528 N  N     . GLY   B 1  1013 ? 12.744  41.919  80.699  1.00 14.66 ? 1011 GLY   B N     1 
ATOM   16529 C  CA    . GLY   B 1  1013 ? 13.856  42.692  80.184  1.00 13.33 ? 1011 GLY   B CA    1 
ATOM   16530 C  C     . GLY   B 1  1013 ? 14.144  43.853  81.092  1.00 14.84 ? 1011 GLY   B C     1 
ATOM   16531 O  O     . GLY   B 1  1013 ? 13.246  44.371  81.754  1.00 15.70 ? 1011 GLY   B O     1 
ATOM   16532 N  N     . GLY   B 1  1014 ? 15.405  44.261  81.117  1.00 15.65 ? 1012 GLY   B N     1 
ATOM   16533 C  CA    . GLY   B 1  1014 ? 15.805  45.289  82.037  1.00 17.84 ? 1012 GLY   B CA    1 
ATOM   16534 C  C     . GLY   B 1  1014 ? 16.375  46.519  81.386  1.00 15.85 ? 1012 GLY   B C     1 
ATOM   16535 O  O     . GLY   B 1  1014 ? 16.277  46.704  80.167  1.00 18.77 ? 1012 GLY   B O     1 
ATOM   16536 N  N     . ARG   B 1  1015 ? 16.995  47.356  82.207  1.00 16.26 ? 1013 ARG   B N     1 
ATOM   16537 C  CA    . ARG   B 1  1015 ? 17.480  48.667  81.829  1.00 17.72 ? 1013 ARG   B CA    1 
ATOM   16538 C  C     . ARG   B 1  1015 ? 18.941  48.770  82.228  1.00 16.65 ? 1013 ARG   B C     1 
ATOM   16539 O  O     . ARG   B 1  1015 ? 19.515  47.848  82.812  1.00 15.86 ? 1013 ARG   B O     1 
ATOM   16540 C  CB    . ARG   B 1  1015 ? 16.661  49.757  82.541  1.00 16.26 ? 1013 ARG   B CB    1 
ATOM   16541 C  CG    . ARG   B 1  1015 ? 16.675  49.618  84.083  1.00 18.45 ? 1013 ARG   B CG    1 
ATOM   16542 C  CD    . ARG   B 1  1015 ? 16.614  50.979  84.794  1.00 22.13 ? 1013 ARG   B CD    1 
ATOM   16543 N  NE    . ARG   B 1  1015 ? 17.920  51.635  84.784  1.00 23.94 ? 1013 ARG   B NE    1 
ATOM   16544 C  CZ    . ARG   B 1  1015 ? 18.937  51.281  85.558  1.00 23.55 ? 1013 ARG   B CZ    1 
ATOM   16545 N  NH1   . ARG   B 1  1015 ? 18.830  50.300  86.444  1.00 21.62 ? 1013 ARG   B NH1   1 
ATOM   16546 N  NH2   . ARG   B 1  1015 ? 20.101  51.915  85.432  1.00 27.38 ? 1013 ARG   B NH2   1 
ATOM   16547 N  N     . GLY   B 1  1016 ? 19.534  49.927  81.952  1.00 17.72 ? 1014 GLY   B N     1 
ATOM   16548 C  CA    . GLY   B 1  1016 ? 20.944  50.101  82.265  1.00 17.19 ? 1014 GLY   B CA    1 
ATOM   16549 C  C     . GLY   B 1  1016 ? 21.796  49.116  81.499  1.00 16.62 ? 1014 GLY   B C     1 
ATOM   16550 O  O     . GLY   B 1  1016 ? 21.594  48.885  80.302  1.00 18.64 ? 1014 GLY   B O     1 
ATOM   16551 N  N     . LEU   B 1  1017 ? 22.742  48.503  82.201  1.00 15.81 ? 1015 LEU   B N     1 
ATOM   16552 C  CA    . LEU   B 1  1017 ? 23.593  47.490  81.605  1.00 17.88 ? 1015 LEU   B CA    1 
ATOM   16553 C  C     . LEU   B 1  1017 ? 22.837  46.224  81.255  1.00 17.27 ? 1015 LEU   B C     1 
ATOM   16554 O  O     . LEU   B 1  1017 ? 23.432  45.322  80.660  1.00 17.19 ? 1015 LEU   B O     1 
ATOM   16555 C  CB    . LEU   B 1  1017 ? 24.740  47.130  82.551  1.00 17.02 ? 1015 LEU   B CB    1 
ATOM   16556 C  CG    . LEU   B 1  1017 ? 25.667  48.295  82.881  1.00 19.85 ? 1015 LEU   B CG    1 
ATOM   16557 C  CD1   . LEU   B 1  1017 ? 26.725  47.841  83.876  1.00 21.30 ? 1015 LEU   B CD1   1 
ATOM   16558 C  CD2   . LEU   B 1  1017 ? 26.314  48.839  81.609  1.00 21.60 ? 1015 LEU   B CD2   1 
ATOM   16559 N  N     . SER   B 1  1018 ? 21.562  46.126  81.623  1.00 14.25 ? 1016 SER   B N     1 
ATOM   16560 C  CA    . SER   B 1  1018 ? 20.794  44.915  81.399  1.00 13.83 ? 1016 SER   B CA    1 
ATOM   16561 C  C     . SER   B 1  1018 ? 19.984  44.922  80.115  1.00 13.61 ? 1016 SER   B C     1 
ATOM   16562 O  O     . SER   B 1  1018 ? 19.465  43.872  79.738  1.00 15.94 ? 1016 SER   B O     1 
ATOM   16563 C  CB    . SER   B 1  1018 ? 19.833  44.677  82.558  1.00 15.09 ? 1016 SER   B CB    1 
ATOM   16564 O  OG    . SER   B 1  1018 ? 20.579  44.457  83.749  1.00 15.82 ? 1016 SER   B OG    1 
ATOM   16565 N  N     . GLY   B 1  1019 ? 19.822  46.047  79.441  1.00 13.82 ? 1017 GLY   B N     1 
ATOM   16566 C  CA    . GLY   B 1  1019 ? 19.038  45.970  78.222  1.00 15.05 ? 1017 GLY   B CA    1 
ATOM   16567 C  C     . GLY   B 1  1019 ? 18.818  47.315  77.583  1.00 14.92 ? 1017 GLY   B C     1 
ATOM   16568 O  O     . GLY   B 1  1019 ? 18.850  48.356  78.239  1.00 17.39 ? 1017 GLY   B O     1 
ATOM   16569 N  N     . THR   B 1  1020 ? 18.557  47.264  76.277  1.00 16.72 ? 1018 THR   B N     1 
ATOM   16570 C  CA    . THR   B 1  1020 ? 18.024  48.406  75.562  1.00 15.83 ? 1018 THR   B CA    1 
ATOM   16571 C  C     . THR   B 1  1020 ? 16.509  48.439  75.595  1.00 17.04 ? 1018 THR   B C     1 
ATOM   16572 O  O     . THR   B 1  1020 ? 15.913  49.505  75.399  1.00 17.41 ? 1018 THR   B O     1 
ATOM   16573 C  CB    . THR   B 1  1020 ? 18.418  48.318  74.081  1.00 15.34 ? 1018 THR   B CB    1 
ATOM   16574 O  OG1   . THR   B 1  1020 ? 17.954  47.072  73.544  1.00 15.42 ? 1018 THR   B OG1   1 
ATOM   16575 C  CG2   . THR   B 1  1020 ? 19.925  48.378  73.919  1.00 16.61 ? 1018 THR   B CG2   1 
ATOM   16576 N  N     . GLY   B 1  1021 ? 15.884  47.295  75.812  1.00 15.42 ? 1019 GLY   B N     1 
ATOM   16577 C  CA    . GLY   B 1  1021 ? 14.485  47.148  75.524  1.00 16.45 ? 1019 GLY   B CA    1 
ATOM   16578 C  C     . GLY   B 1  1021 ? 14.245  47.196  74.031  1.00 15.71 ? 1019 GLY   B C     1 
ATOM   16579 O  O     . GLY   B 1  1021 ? 15.177  47.339  73.233  1.00 16.18 ? 1019 GLY   B O     1 
ATOM   16580 N  N     . PRO   B 1  1022 ? 13.001  47.043  73.620  1.00 14.29 ? 1020 PRO   B N     1 
ATOM   16581 C  CA    . PRO   B 1  1022 ? 11.828  46.766  74.448  1.00 15.41 ? 1020 PRO   B CA    1 
ATOM   16582 C  C     . PRO   B 1  1022 ? 11.862  45.338  74.987  1.00 17.26 ? 1020 PRO   B C     1 
ATOM   16583 O  O     . PRO   B 1  1022 ? 12.647  44.497  74.539  1.00 16.80 ? 1020 PRO   B O     1 
ATOM   16584 C  CB    . PRO   B 1  1022 ? 10.675  46.957  73.462  1.00 17.78 ? 1020 PRO   B CB    1 
ATOM   16585 C  CG    . PRO   B 1  1022 ? 11.252  46.508  72.156  1.00 16.58 ? 1020 PRO   B CG    1 
ATOM   16586 C  CD    . PRO   B 1  1022 ? 12.678  47.015  72.181  1.00 15.34 ? 1020 PRO   B CD    1 
ATOM   16587 N  N     . LYS   B 1  1023 ? 11.002  45.048  75.960  1.00 14.57 ? 1021 LYS   B N     1 
ATOM   16588 C  CA    . LYS   B 1  1023 ? 11.011  43.743  76.599  1.00 15.51 ? 1021 LYS   B CA    1 
ATOM   16589 C  C     . LYS   B 1  1023 ? 10.532  42.664  75.646  1.00 14.11 ? 1021 LYS   B C     1 
ATOM   16590 O  O     . LYS   B 1  1023 ? 9.483   42.796  75.007  1.00 15.19 ? 1021 LYS   B O     1 
ATOM   16591 C  CB    . LYS   B 1  1023 ? 10.051  43.754  77.775  1.00 15.12 ? 1021 LYS   B CB    1 
ATOM   16592 C  CG    . LYS   B 1  1023 ? 10.488  44.566  78.972  1.00 14.72 ? 1021 LYS   B CG    1 
ATOM   16593 C  CD    . LYS   B 1  1023 ? 9.348   44.528  79.977  1.00 14.12 ? 1021 LYS   B CD    1 
ATOM   16594 C  CE    . LYS   B 1  1023 ? 9.738   45.030  81.365  1.00 15.59 ? 1021 LYS   B CE    1 
ATOM   16595 N  NZ    . LYS   B 1  1023 ? 10.520  43.988  82.096  1.00 15.53 ? 1021 LYS   B NZ    1 
ATOM   16596 N  N     . ALA   B 1  1024 ? 11.275  41.566  75.605  1.00 14.88 ? 1022 ALA   B N     1 
ATOM   16597 C  CA    . ALA   B 1  1024 ? 10.770  40.339  75.015  1.00 15.56 ? 1022 ALA   B CA    1 
ATOM   16598 C  C     . ALA   B 1  1024 ? 9.526   39.877  75.765  1.00 15.41 ? 1022 ALA   B C     1 
ATOM   16599 O  O     . ALA   B 1  1024 ? 9.379   40.082  76.973  1.00 16.78 ? 1022 ALA   B O     1 
ATOM   16600 C  CB    . ALA   B 1  1024 ? 11.862  39.264  75.061  1.00 15.87 ? 1022 ALA   B CB    1 
ATOM   16601 N  N     . GLY   B 1  1025 ? 8.601   39.275  75.030  1.00 13.93 ? 1023 GLY   B N     1 
ATOM   16602 C  CA    . GLY   B 1  1025 ? 7.388   38.798  75.664  1.00 15.69 ? 1023 GLY   B CA    1 
ATOM   16603 C  C     . GLY   B 1  1025 ? 6.487   39.907  76.138  1.00 14.42 ? 1023 GLY   B C     1 
ATOM   16604 O  O     . GLY   B 1  1025 ? 5.606   39.673  76.971  1.00 15.65 ? 1023 GLY   B O     1 
ATOM   16605 N  N     . GLY   B 1  1026 ? 6.665   41.107  75.600  1.00 15.15 ? 1024 GLY   B N     1 
ATOM   16606 C  CA    . GLY   B 1  1026 ? 5.828   42.235  75.920  1.00 14.42 ? 1024 GLY   B CA    1 
ATOM   16607 C  C     . GLY   B 1  1026 ? 5.339   42.903  74.656  1.00 14.60 ? 1024 GLY   B C     1 
ATOM   16608 O  O     . GLY   B 1  1026 ? 5.752   42.572  73.539  1.00 14.75 ? 1024 GLY   B O     1 
ATOM   16609 N  N     . PRO   B 1  1027 ? 4.442   43.870  74.821  1.00 15.31 ? 1025 PRO   B N     1 
ATOM   16610 C  CA    . PRO   B 1  1027 ? 3.675   44.385  73.683  1.00 13.88 ? 1025 PRO   B CA    1 
ATOM   16611 C  C     . PRO   B 1  1027 ? 4.420   45.401  72.848  1.00 14.38 ? 1025 PRO   B C     1 
ATOM   16612 O  O     . PRO   B 1  1027 ? 3.919   45.761  71.783  1.00 14.78 ? 1025 PRO   B O     1 
ATOM   16613 C  CB    . PRO   B 1  1027 ? 2.452   45.021  74.356  1.00 15.73 ? 1025 PRO   B CB    1 
ATOM   16614 C  CG    . PRO   B 1  1027 ? 2.965   45.429  75.713  1.00 17.32 ? 1025 PRO   B CG    1 
ATOM   16615 C  CD    . PRO   B 1  1027 ? 3.932   44.349  76.112  1.00 16.53 ? 1025 PRO   B CD    1 
ATOM   16616 N  N     . LEU   B 1  1028 ? 5.579   45.885  73.284  1.00 14.65 ? 1026 LEU   B N     1 
ATOM   16617 C  CA    . LEU   B 1  1028 ? 6.323   46.840  72.474  1.00 14.44 ? 1026 LEU   B CA    1 
ATOM   16618 C  C     . LEU   B 1  1028 ? 7.315   46.166  71.550  1.00 15.56 ? 1026 LEU   B C     1 
ATOM   16619 O  O     . LEU   B 1  1028 ? 7.907   46.848  70.711  1.00 16.87 ? 1026 LEU   B O     1 
ATOM   16620 C  CB    . LEU   B 1  1028 ? 7.114   47.813  73.356  1.00 14.62 ? 1026 LEU   B CB    1 
ATOM   16621 C  CG    . LEU   B 1  1028 ? 6.269   48.568  74.364  1.00 17.48 ? 1026 LEU   B CG    1 
ATOM   16622 C  CD1   . LEU   B 1  1028 ? 7.139   49.574  75.089  1.00 19.33 ? 1026 LEU   B CD1   1 
ATOM   16623 C  CD2   . LEU   B 1  1028 ? 5.152   49.257  73.653  1.00 21.09 ? 1026 LEU   B CD2   1 
ATOM   16624 N  N     . TYR   B 1  1029 ? 7.519   44.857  71.706  1.00 14.48 ? 1027 TYR   B N     1 
ATOM   16625 C  CA    . TYR   B 1  1029 ? 8.640   44.176  71.071  1.00 14.54 ? 1027 TYR   B CA    1 
ATOM   16626 C  C     . TYR   B 1  1029 ? 8.516   44.179  69.558  1.00 14.32 ? 1027 TYR   B C     1 
ATOM   16627 O  O     . TYR   B 1  1029 ? 9.466   44.527  68.855  1.00 13.81 ? 1027 TYR   B O     1 
ATOM   16628 C  CB    . TYR   B 1  1029 ? 8.643   42.747  71.562  1.00 14.84 ? 1027 TYR   B CB    1 
ATOM   16629 C  CG    . TYR   B 1  1029 ? 9.907   41.956  71.416  1.00 14.70 ? 1027 TYR   B CG    1 
ATOM   16630 C  CD1   . TYR   B 1  1029 ? 11.057  42.287  72.126  1.00 13.95 ? 1027 TYR   B CD1   1 
ATOM   16631 C  CD2   . TYR   B 1  1029 ? 9.918   40.801  70.657  1.00 14.11 ? 1027 TYR   B CD2   1 
ATOM   16632 C  CE1   . TYR   B 1  1029 ? 12.210  41.494  72.035  1.00 14.90 ? 1027 TYR   B CE1   1 
ATOM   16633 C  CE2   . TYR   B 1  1029 ? 11.049  39.999  70.582  1.00 15.23 ? 1027 TYR   B CE2   1 
ATOM   16634 C  CZ    . TYR   B 1  1029 ? 12.184  40.353  71.265  1.00 14.66 ? 1027 TYR   B CZ    1 
ATOM   16635 O  OH    . TYR   B 1  1029 ? 13.277  39.533  71.191  1.00 15.96 ? 1027 TYR   B OH    1 
ATOM   16636 N  N     . LEU   B 1  1030 ? 7.366   43.752  69.029  1.00 14.59 ? 1028 LEU   B N     1 
ATOM   16637 C  CA    . LEU   B 1  1030 ? 7.271   43.613  67.579  1.00 13.27 ? 1028 LEU   B CA    1 
ATOM   16638 C  C     . LEU   B 1  1030 ? 7.459   44.947  66.890  1.00 14.67 ? 1028 LEU   B C     1 
ATOM   16639 O  O     . LEU   B 1  1030 ? 7.977   44.995  65.767  1.00 14.22 ? 1028 LEU   B O     1 
ATOM   16640 C  CB    . LEU   B 1  1030 ? 5.926   43.004  67.187  1.00 14.46 ? 1028 LEU   B CB    1 
ATOM   16641 C  CG    . LEU   B 1  1030 ? 5.716   41.553  67.609  1.00 15.31 ? 1028 LEU   B CG    1 
ATOM   16642 C  CD1   . LEU   B 1  1030 ? 4.379   41.040  67.118  1.00 17.66 ? 1028 LEU   B CD1   1 
ATOM   16643 C  CD2   . LEU   B 1  1030 ? 6.855   40.675  67.072  1.00 18.46 ? 1028 LEU   B CD2   1 
ATOM   16644 N  N     . GLY   B 1  1031 ? 7.064   46.040  67.546  1.00 14.56 ? 1029 GLY   B N     1 
ATOM   16645 C  CA    . GLY   B 1  1031 ? 7.143   47.354  66.930  1.00 16.67 ? 1029 GLY   B CA    1 
ATOM   16646 C  C     . GLY   B 1  1031 ? 8.553   47.807  66.645  1.00 13.79 ? 1029 GLY   B C     1 
ATOM   16647 O  O     . GLY   B 1  1031 ? 8.750   48.712  65.826  1.00 16.60 ? 1029 GLY   B O     1 
ATOM   16648 N  N     . ARG   B 1  1032 ? 9.539   47.183  67.280  1.00 13.71 ? 1030 ARG   B N     1 
ATOM   16649 C  CA    . ARG   B 1  1032 ? 10.927  47.504  67.014  1.00 14.38 ? 1030 ARG   B CA    1 
ATOM   16650 C  C     . ARG   B 1  1032 ? 11.422  46.857  65.735  1.00 15.76 ? 1030 ARG   B C     1 
ATOM   16651 O  O     . ARG   B 1  1032 ? 12.493  47.227  65.238  1.00 16.56 ? 1030 ARG   B O     1 
ATOM   16652 C  CB    . ARG   B 1  1032 ? 11.761  47.035  68.213  1.00 14.19 ? 1030 ARG   B CB    1 
ATOM   16653 C  CG    . ARG   B 1  1032 ? 13.198  47.523  68.221  1.00 16.77 ? 1030 ARG   B CG    1 
ATOM   16654 C  CD    . ARG   B 1  1032 ? 13.266  49.025  68.434  1.00 16.98 ? 1030 ARG   B CD    1 
ATOM   16655 N  NE    . ARG   B 1  1032 ? 14.637  49.464  68.661  1.00 17.71 ? 1030 ARG   B NE    1 
ATOM   16656 C  CZ    . ARG   B 1  1032 ? 15.244  50.440  67.999  1.00 20.92 ? 1030 ARG   B CZ    1 
ATOM   16657 N  NH1   . ARG   B 1  1032 ? 14.627  51.117  67.036  1.00 21.52 ? 1030 ARG   B NH1   1 
ATOM   16658 N  NH2   . ARG   B 1  1032 ? 16.502  50.740  68.307  1.00 20.88 ? 1030 ARG   B NH2   1 
ATOM   16659 N  N     . LEU   B 1  1033 ? 10.664  45.904  65.195  1.00 14.24 ? 1031 LEU   B N     1 
ATOM   16660 C  CA    . LEU   B 1  1033 ? 11.129  45.069  64.096  1.00 14.64 ? 1031 LEU   B CA    1 
ATOM   16661 C  C     . LEU   B 1  1033 ? 10.442  45.418  62.788  1.00 15.68 ? 1031 LEU   B C     1 
ATOM   16662 O  O     . LEU   B 1  1033 ? 10.483  44.628  61.838  1.00 16.20 ? 1031 LEU   B O     1 
ATOM   16663 C  CB    . LEU   B 1  1033 ? 10.906  43.598  64.440  1.00 14.63 ? 1031 LEU   B CB    1 
ATOM   16664 C  CG    . LEU   B 1  1033 ? 11.399  43.202  65.834  1.00 15.51 ? 1031 LEU   B CG    1 
ATOM   16665 C  CD1   . LEU   B 1  1033 ? 11.048  41.758  66.137  1.00 16.35 ? 1031 LEU   B CD1   1 
ATOM   16666 C  CD2   . LEU   B 1  1033 ? 12.904  43.426  65.957  1.00 17.30 ? 1031 LEU   B CD2   1 
ATOM   16667 N  N     . VAL   B 1  1034 ? 9.772   46.568  62.747  1.00 16.16 ? 1032 VAL   B N     1 
ATOM   16668 C  CA    . VAL   B 1  1034 ? 9.161   47.136  61.560  1.00 17.96 ? 1032 VAL   B CA    1 
ATOM   16669 C  C     . VAL   B 1  1034 ? 9.599   48.592  61.484  1.00 16.39 ? 1032 VAL   B C     1 
ATOM   16670 O  O     . VAL   B 1  1034 ? 10.086  49.166  62.459  1.00 19.17 ? 1032 VAL   B O     1 
ATOM   16671 C  CB    . VAL   B 1  1034 ? 7.629   47.022  61.604  1.00 16.50 ? 1032 VAL   B CB    1 
ATOM   16672 C  CG1   . VAL   B 1  1034 ? 7.197   45.573  61.448  1.00 18.60 ? 1032 VAL   B CG1   1 
ATOM   16673 C  CG2   . VAL   B 1  1034 ? 7.105   47.588  62.929  1.00 16.72 ? 1032 VAL   B CG2   1 
ATOM   16674 N  N     . THR   B 1  1035 ? 9.450   49.193  60.297  1.00 18.96 ? 1033 THR   B N     1 
ATOM   16675 C  CA    . THR   B 1  1035 ? 9.966   50.547  60.135  1.00 21.30 ? 1033 THR   B CA    1 
ATOM   16676 C  C     . THR   B 1  1035 ? 9.035   51.604  60.699  1.00 23.09 ? 1033 THR   B C     1 
ATOM   16677 O  O     . THR   B 1  1035 ? 9.484   52.722  60.974  1.00 27.78 ? 1033 THR   B O     1 
ATOM   16678 C  CB    . THR   B 1  1035 ? 10.301  50.842  58.674  1.00 27.18 ? 1033 THR   B CB    1 
ATOM   16679 O  OG1   . THR   B 1  1035 ? 9.238   50.379  57.844  1.00 29.95 ? 1033 THR   B OG1   1 
ATOM   16680 C  CG2   . THR   B 1  1035 ? 11.594  50.142  58.280  1.00 31.51 ? 1033 THR   B CG2   1 
ATOM   16681 N  N     . THR   B 1  1036 ? 7.761   51.275  60.888  1.00 20.34 ? 1034 THR   B N     1 
ATOM   16682 C  CA    . THR   B 1  1036 ? 6.807   52.154  61.543  1.00 23.42 ? 1034 THR   B CA    1 
ATOM   16683 C  C     . THR   B 1  1036 ? 6.128   51.324  62.615  1.00 20.37 ? 1034 THR   B C     1 
ATOM   16684 O  O     . THR   B 1  1036 ? 5.513   50.303  62.301  1.00 20.30 ? 1034 THR   B O     1 
ATOM   16685 C  CB    . THR   B 1  1036 ? 5.761   52.638  60.544  1.00 25.63 ? 1034 THR   B CB    1 
ATOM   16686 O  OG1   . THR   B 1  1036 ? 6.410   53.339  59.476  1.00 32.58 ? 1034 THR   B OG1   1 
ATOM   16687 C  CG2   . THR   B 1  1036 ? 4.764   53.556  61.234  1.00 28.81 ? 1034 THR   B CG2   1 
ATOM   16688 N  N     . ALA   B 1  1037 ? 6.261   51.741  63.869  1.00 21.28 ? 1035 ALA   B N     1 
ATOM   16689 C  CA    . ALA   B 1  1037 ? 5.729   50.942  64.962  1.00 21.11 ? 1035 ALA   B CA    1 
ATOM   16690 C  C     . ALA   B 1  1037 ? 4.208   51.051  64.997  1.00 18.04 ? 1035 ALA   B C     1 
ATOM   16691 O  O     . ALA   B 1  1037 ? 3.660   52.145  64.835  1.00 19.52 ? 1035 ALA   B O     1 
ATOM   16692 C  CB    . ALA   B 1  1037 ? 6.298   51.418  66.299  1.00 22.22 ? 1035 ALA   B CB    1 
ATOM   16693 N  N     . PRO   B 1  1038 ? 3.508   49.944  65.200  1.00 16.71 ? 1036 PRO   B N     1 
ATOM   16694 C  CA    . PRO   B 1  1038 ? 2.066   50.004  65.437  1.00 17.56 ? 1036 PRO   B CA    1 
ATOM   16695 C  C     . PRO   B 1  1038 ? 1.784   50.474  66.855  1.00 16.92 ? 1036 PRO   B C     1 
ATOM   16696 O  O     . PRO   B 1  1038 ? 2.667   50.576  67.698  1.00 17.59 ? 1036 PRO   B O     1 
ATOM   16697 C  CB    . PRO   B 1  1038 ? 1.631   48.549  65.287  1.00 19.73 ? 1036 PRO   B CB    1 
ATOM   16698 C  CG    . PRO   B 1  1038 ? 2.832   47.772  65.779  1.00 19.59 ? 1036 PRO   B CG    1 
ATOM   16699 C  CD    . PRO   B 1  1038 ? 4.036   48.568  65.275  1.00 17.39 ? 1036 PRO   B CD    1 
ATOM   16700 N  N     . VAL   B 1  1039 ? 0.508   50.744  67.109  1.00 17.97 ? 1037 VAL   B N     1 
ATOM   16701 C  CA    . VAL   B 1  1039 ? 0.025   51.034  68.455  1.00 17.46 ? 1037 VAL   B CA    1 
ATOM   16702 C  C     . VAL   B 1  1039 ? -0.261  49.694  69.127  1.00 15.84 ? 1037 VAL   B C     1 
ATOM   16703 O  O     . VAL   B 1  1039 ? -1.170  48.976  68.683  1.00 17.84 ? 1037 VAL   B O     1 
ATOM   16704 C  CB    . VAL   B 1  1039 ? -1.231  51.910  68.410  1.00 16.85 ? 1037 VAL   B CB    1 
ATOM   16705 C  CG1   . VAL   B 1  1039 ? -1.700  52.174  69.832  1.00 21.06 ? 1037 VAL   B CG1   1 
ATOM   16706 C  CG2   . VAL   B 1  1039 ? -0.904  53.205  67.699  1.00 20.41 ? 1037 VAL   B CG2   1 
ATOM   16707 N  N     . PRO   B 1  1040 ? 0.487   49.308  70.155  1.00 16.64 ? 1038 PRO   B N     1 
ATOM   16708 C  CA    . PRO   B 1  1040 ? 0.278   48.003  70.758  1.00 17.48 ? 1038 PRO   B CA    1 
ATOM   16709 C  C     . PRO   B 1  1040 ? -1.065  47.925  71.461  1.00 17.22 ? 1038 PRO   B C     1 
ATOM   16710 O  O     . PRO   B 1  1040 ? -1.636  48.955  71.849  1.00 17.91 ? 1038 PRO   B O     1 
ATOM   16711 C  CB    . PRO   B 1  1040 ? 1.435   47.897  71.764  1.00 20.30 ? 1038 PRO   B CB    1 
ATOM   16712 C  CG    . PRO   B 1  1040 ? 2.447   48.904  71.301  1.00 22.00 ? 1038 PRO   B CG    1 
ATOM   16713 C  CD    . PRO   B 1  1040 ? 1.647   50.015  70.721  1.00 19.02 ? 1038 PRO   B CD    1 
ATOM   16714 N  N     . PRO   B 1  1041 ? -1.590  46.715  71.662  1.00 18.16 ? 1039 PRO   B N     1 
ATOM   16715 C  CA    . PRO   B 1  1041 ? -2.808  46.554  72.457  1.00 17.67 ? 1039 PRO   B CA    1 
ATOM   16716 C  C     . PRO   B 1  1041 ? -2.638  47.209  73.818  1.00 17.29 ? 1039 PRO   B C     1 
ATOM   16717 O  O     . PRO   B 1  1041 ? -1.576  47.111  74.440  1.00 18.34 ? 1039 PRO   B O     1 
ATOM   16718 C  CB    . PRO   B 1  1041 ? -2.940  45.032  72.595  1.00 20.24 ? 1039 PRO   B CB    1 
ATOM   16719 C  CG    . PRO   B 1  1041 ? -2.132  44.468  71.466  1.00 22.02 ? 1039 PRO   B CG    1 
ATOM   16720 C  CD    . PRO   B 1  1041 ? -1.002  45.420  71.272  1.00 22.28 ? 1039 PRO   B CD    1 
ATOM   16721 N  N     . GLN   B 1  1042 ? -3.684  47.913  74.252  1.00 17.39 ? 1040 GLN   B N     1 
ATOM   16722 C  CA    . GLN   B 1  1042 ? -3.781  48.524  75.576  1.00 18.00 ? 1040 GLN   B CA    1 
ATOM   16723 C  C     . GLN   B 1  1042 ? -2.767  49.634  75.800  1.00 18.45 ? 1040 GLN   B C     1 
ATOM   16724 O  O     . GLN   B 1  1042 ? -2.582  50.086  76.936  1.00 18.29 ? 1040 GLN   B O     1 
ATOM   16725 C  CB    . GLN   B 1  1042 ? -3.674  47.479  76.695  1.00 20.98 ? 1040 GLN   B CB    1 
ATOM   16726 C  CG    . GLN   B 1  1042 ? -4.741  46.400  76.640  1.00 24.54 ? 1040 GLN   B CG    1 
ATOM   16727 C  CD    . GLN   B 1  1042 ? -4.534  45.376  77.739  1.00 30.97 ? 1040 GLN   B CD    1 
ATOM   16728 O  OE1   . GLN   B 1  1042 ? -3.547  44.639  77.736  1.00 46.11 ? 1040 GLN   B OE1   1 
ATOM   16729 N  NE2   . GLN   B 1  1042 ? -5.435  45.361  78.705  1.00 39.98 ? 1040 GLN   B NE2   1 
ATOM   16730 N  N     . HIS   B 1  1043 ? -2.103  50.104  74.757  1.00 17.64 ? 1041 HIS   B N     1 
ATOM   16731 C  CA    . HIS   B 1  1043 ? -0.985  51.026  74.923  1.00 16.41 ? 1041 HIS   B CA    1 
ATOM   16732 C  C     . HIS   B 1  1043 ? -1.512  52.450  74.833  1.00 17.33 ? 1041 HIS   B C     1 
ATOM   16733 O  O     . HIS   B 1  1043 ? -1.620  53.031  73.754  1.00 19.41 ? 1041 HIS   B O     1 
ATOM   16734 C  CB    . HIS   B 1  1043 ? 0.070   50.740  73.867  1.00 16.57 ? 1041 HIS   B CB    1 
ATOM   16735 C  CG    . HIS   B 1  1043 ? 1.276   51.624  73.942  1.00 17.29 ? 1041 HIS   B CG    1 
ATOM   16736 N  ND1   . HIS   B 1  1043 ? 2.373   51.331  74.726  1.00 17.35 ? 1041 HIS   B ND1   1 
ATOM   16737 C  CD2   . HIS   B 1  1043 ? 1.570   52.780  73.299  1.00 18.51 ? 1041 HIS   B CD2   1 
ATOM   16738 C  CE1   . HIS   B 1  1043 ? 3.286   52.276  74.571  1.00 18.04 ? 1041 HIS   B CE1   1 
ATOM   16739 N  NE2   . HIS   B 1  1043 ? 2.832   53.155  73.694  1.00 17.58 ? 1041 HIS   B NE2   1 
ATOM   16740 N  N     . SER   B 1  1044 ? -1.838  53.020  75.988  1.00 15.55 ? 1042 SER   B N     1 
ATOM   16741 C  CA    . SER   B 1  1044 ? -2.281  54.403  76.064  1.00 17.08 ? 1042 SER   B CA    1 
ATOM   16742 C  C     . SER   B 1  1044 ? -2.211  54.806  77.523  1.00 16.79 ? 1042 SER   B C     1 
ATOM   16743 O  O     . SER   B 1  1044 ? -2.055  53.967  78.413  1.00 17.03 ? 1042 SER   B O     1 
ATOM   16744 C  CB    . SER   B 1  1044 ? -3.713  54.566  75.555  1.00 17.06 ? 1042 SER   B CB    1 
ATOM   16745 O  OG    . SER   B 1  1044 ? -4.615  53.932  76.443  1.00 18.10 ? 1042 SER   B OG    1 
ATOM   16746 N  N     . SER   B 1  1045 ? -2.366  56.098  77.759  1.00 15.07 ? 1043 SER   B N     1 
ATOM   16747 C  CA    . SER   B 1  1045 ? -2.420  56.600  79.119  1.00 13.98 ? 1043 SER   B CA    1 
ATOM   16748 C  C     . SER   B 1  1045 ? -3.271  57.852  79.127  1.00 16.25 ? 1043 SER   B C     1 
ATOM   16749 O  O     . SER   B 1  1045 ? -3.207  58.658  78.195  1.00 18.01 ? 1043 SER   B O     1 
ATOM   16750 C  CB    . SER   B 1  1045 ? -1.008  56.969  79.566  1.00 17.44 ? 1043 SER   B CB    1 
ATOM   16751 O  OG    . SER   B 1  1045 ? -1.042  57.570  80.840  1.00 17.62 ? 1043 SER   B OG    1 
ATOM   16752 N  N     . VAL   B 1  1046 ? -4.057  58.022  80.194  1.00 16.87 ? 1044 VAL   B N     1 
ATOM   16753 C  CA    . VAL   B 1  1046 ? -4.832  59.252  80.337  1.00 18.23 ? 1044 VAL   B CA    1 
ATOM   16754 C  C     . VAL   B 1  1046 ? -4.024  60.383  80.937  1.00 17.44 ? 1044 VAL   B C     1 
ATOM   16755 O  O     . VAL   B 1  1046 ? -4.510  61.521  80.994  1.00 19.23 ? 1044 VAL   B O     1 
ATOM   16756 C  CB    . VAL   B 1  1046 ? -6.115  59.042  81.162  1.00 20.29 ? 1044 VAL   B CB    1 
ATOM   16757 C  CG1   . VAL   B 1  1046 ? -6.988  58.014  80.466  1.00 23.22 ? 1044 VAL   B CG1   1 
ATOM   16758 C  CG2   . VAL   B 1  1046 ? -5.777  58.605  82.578  1.00 19.93 ? 1044 VAL   B CG2   1 
ATOM   16759 N  N     . HIS   B 1  1047 ? -2.803  60.100  81.366  1.00 18.69 ? 1045 HIS   B N     1 
ATOM   16760 C  CA    A HIS   B 1  1047 ? -1.997  61.102  82.028  0.61 19.04 ? 1045 HIS   B CA    1 
ATOM   16761 C  CA    B HIS   B 1  1047 ? -1.942  61.061  82.045  0.39 19.03 ? 1045 HIS   B CA    1 
ATOM   16762 C  C     . HIS   B 1  1047 ? -1.173  61.883  81.023  1.00 17.26 ? 1045 HIS   B C     1 
ATOM   16763 O  O     . HIS   B 1  1047 ? -0.696  61.345  80.022  1.00 20.06 ? 1045 HIS   B O     1 
ATOM   16764 C  CB    A HIS   B 1  1047 ? -1.120  60.416  83.059  0.61 19.62 ? 1045 HIS   B CB    1 
ATOM   16765 C  CB    B HIS   B 1  1047 ? -0.939  60.299  82.917  0.39 19.38 ? 1045 HIS   B CB    1 
ATOM   16766 C  CG    A HIS   B 1  1047 ? -1.910  59.549  83.983  0.61 19.54 ? 1045 HIS   B CG    1 
ATOM   16767 C  CG    B HIS   B 1  1047 ? 0.270   61.095  83.309  0.39 19.43 ? 1045 HIS   B CG    1 
ATOM   16768 N  ND1   A HIS   B 1  1047 ? -2.725  60.067  84.964  0.61 23.18 ? 1045 HIS   B ND1   1 
ATOM   16769 N  ND1   B HIS   B 1  1047 ? 0.244   62.052  84.301  0.39 22.55 ? 1045 HIS   B ND1   1 
ATOM   16770 C  CD2   A HIS   B 1  1047 ? -2.055  58.203  84.043  0.61 19.43 ? 1045 HIS   B CD2   1 
ATOM   16771 C  CD2   B HIS   B 1  1047 ? 1.546   61.058  82.856  0.39 19.92 ? 1045 HIS   B CD2   1 
ATOM   16772 C  CE1   A HIS   B 1  1047 ? -3.320  59.078  85.606  0.61 25.71 ? 1045 HIS   B CE1   1 
ATOM   16773 C  CE1   B HIS   B 1  1047 ? 1.448   62.579  84.434  0.39 22.31 ? 1045 HIS   B CE1   1 
ATOM   16774 N  NE2   A HIS   B 1  1047 ? -2.935  57.937  85.063  0.61 22.28 ? 1045 HIS   B NE2   1 
ATOM   16775 N  NE2   B HIS   B 1  1047 ? 2.256   61.994  83.568  0.39 23.95 ? 1045 HIS   B NE2   1 
ATOM   16776 N  N     . THR   B 1  1048 ? -1.036  63.172  81.291  1.00 16.52 ? 1046 THR   B N     1 
ATOM   16777 C  CA    . THR   B 1  1048 ? -0.227  64.049  80.465  1.00 18.60 ? 1046 THR   B CA    1 
ATOM   16778 C  C     . THR   B 1  1048 ? 0.887   64.603  81.334  1.00 17.71 ? 1046 THR   B C     1 
ATOM   16779 O  O     . THR   B 1  1048 ? 0.632   65.144  82.415  1.00 18.54 ? 1046 THR   B O     1 
ATOM   16780 C  CB    . THR   B 1  1048 ? -1.051  65.198  79.902  1.00 22.44 ? 1046 THR   B CB    1 
ATOM   16781 O  OG1   . THR   B 1  1048 ? -2.254  64.682  79.310  1.00 20.82 ? 1046 THR   B OG1   1 
ATOM   16782 C  CG2   . THR   B 1  1048 ? -0.233  65.934  78.841  1.00 20.99 ? 1046 THR   B CG2   1 
ATOM   16783 N  N     . ASP   B 1  1049 ? 2.112   64.449  80.868  1.00 18.32 ? 1047 ASP   B N     1 
ATOM   16784 C  CA    . ASP   B 1  1049 ? 3.230   64.955  81.628  1.00 17.46 ? 1047 ASP   B CA    1 
ATOM   16785 C  C     . ASP   B 1  1049 ? 3.073   66.458  81.840  1.00 16.37 ? 1047 ASP   B C     1 
ATOM   16786 O  O     . ASP   B 1  1049 ? 2.810   67.191  80.883  1.00 18.84 ? 1047 ASP   B O     1 
ATOM   16787 C  CB    . ASP   B 1  1049 ? 4.516   64.648  80.880  1.00 16.22 ? 1047 ASP   B CB    1 
ATOM   16788 C  CG    . ASP   B 1  1049 ? 5.730   65.108  81.641  1.00 18.34 ? 1047 ASP   B CG    1 
ATOM   16789 O  OD1   . ASP   B 1  1049 ? 6.052   66.306  81.552  1.00 19.94 ? 1047 ASP   B OD1   1 
ATOM   16790 O  OD2   . ASP   B 1  1049 ? 6.310   64.278  82.363  1.00 19.07 ? 1047 ASP   B OD2   1 
ATOM   16791 N  N     . PRO   B 1  1050 ? 3.197   66.949  83.074  1.00 19.41 ? 1048 PRO   B N     1 
ATOM   16792 C  CA    . PRO   B 1  1050 ? 2.936   68.371  83.318  1.00 19.80 ? 1048 PRO   B CA    1 
ATOM   16793 C  C     . PRO   B 1  1050 ? 4.010   69.269  82.749  1.00 19.67 ? 1048 PRO   B C     1 
ATOM   16794 O  O     . PRO   B 1  1050 ? 3.718   70.417  82.398  1.00 21.06 ? 1048 PRO   B O     1 
ATOM   16795 C  CB    . PRO   B 1  1050 ? 2.880   68.460  84.849  1.00 23.98 ? 1048 PRO   B CB    1 
ATOM   16796 C  CG    . PRO   B 1  1050 ? 3.703   67.315  85.314  1.00 24.07 ? 1048 PRO   B CG    1 
ATOM   16797 C  CD    . PRO   B 1  1050 ? 3.471   66.211  84.315  1.00 21.81 ? 1048 PRO   B CD    1 
ATOM   16798 N  N     . VAL   B 1  1051 ? 5.248   68.782  82.660  1.00 20.50 ? 1049 VAL   B N     1 
ATOM   16799 C  CA    . VAL   B 1  1051 ? 6.313   69.594  82.078  1.00 17.78 ? 1049 VAL   B CA    1 
ATOM   16800 C  C     . VAL   B 1  1051 ? 6.112   69.727  80.577  1.00 17.94 ? 1049 VAL   B C     1 
ATOM   16801 O  O     . VAL   B 1  1051 ? 6.316   70.800  80.001  1.00 20.04 ? 1049 VAL   B O     1 
ATOM   16802 C  CB    . VAL   B 1  1051 ? 7.692   69.019  82.442  1.00 21.82 ? 1049 VAL   B CB    1 
ATOM   16803 C  CG1   . VAL   B 1  1051 ? 8.784   69.845  81.792  1.00 23.00 ? 1049 VAL   B CG1   1 
ATOM   16804 C  CG2   . VAL   B 1  1051 ? 7.862   69.008  83.956  1.00 24.57 ? 1049 VAL   B CG2   1 
ATOM   16805 N  N     . LEU   B 1  1052 ? 5.685   68.645  79.926  1.00 16.69 ? 1050 LEU   B N     1 
ATOM   16806 C  CA    . LEU   B 1  1052 ? 5.235   68.739  78.542  1.00 17.65 ? 1050 LEU   B CA    1 
ATOM   16807 C  C     . LEU   B 1  1052 ? 4.195   69.838  78.380  1.00 20.69 ? 1050 LEU   B C     1 
ATOM   16808 O  O     . LEU   B 1  1052 ? 4.272   70.649  77.452  1.00 19.70 ? 1050 LEU   B O     1 
ATOM   16809 C  CB    . LEU   B 1  1052 ? 4.675   67.391  78.082  1.00 17.99 ? 1050 LEU   B CB    1 
ATOM   16810 C  CG    . LEU   B 1  1052 ? 4.176   67.225  76.637  1.00 17.94 ? 1050 LEU   B CG    1 
ATOM   16811 C  CD1   . LEU   B 1  1052 ? 2.773   67.790  76.419  1.00 18.13 ? 1050 LEU   B CD1   1 
ATOM   16812 C  CD2   . LEU   B 1  1052 ? 5.177   67.817  75.627  1.00 18.25 ? 1050 LEU   B CD2   1 
ATOM   16813 N  N     . LEU   B 1  1053 ? 3.200   69.872  79.273  1.00 18.89 ? 1051 LEU   B N     1 
ATOM   16814 C  CA    . LEU   B 1  1053 ? 2.156   70.883  79.169  1.00 21.22 ? 1051 LEU   B CA    1 
ATOM   16815 C  C     . LEU   B 1  1053 ? 2.746   72.286  79.247  1.00 20.69 ? 1051 LEU   B C     1 
ATOM   16816 O  O     . LEU   B 1  1053 ? 2.386   73.168  78.462  1.00 21.97 ? 1051 LEU   B O     1 
ATOM   16817 C  CB    . LEU   B 1  1053 ? 1.116   70.675  80.274  1.00 23.39 ? 1051 LEU   B CB    1 
ATOM   16818 C  CG    . LEU   B 1  1053 ? 0.184   69.476  80.069  1.00 26.31 ? 1051 LEU   B CG    1 
ATOM   16819 C  CD1   . LEU   B 1  1053 ? -0.656  69.249  81.316  1.00 24.09 ? 1051 LEU   B CD1   1 
ATOM   16820 C  CD2   . LEU   B 1  1053 ? -0.696  69.697  78.861  1.00 26.34 ? 1051 LEU   B CD2   1 
ATOM   16821 N  N     . ASP   B 1  1054 ? 3.658   72.507  80.194  1.00 20.20 ? 1052 ASP   B N     1 
ATOM   16822 C  CA    . ASP   B 1  1054 ? 4.291   73.817  80.317  1.00 23.51 ? 1052 ASP   B CA    1 
ATOM   16823 C  C     . ASP   B 1  1054 ? 5.125   74.145  79.088  1.00 19.26 ? 1052 ASP   B C     1 
ATOM   16824 O  O     . ASP   B 1  1054 ? 5.201   75.309  78.678  1.00 22.23 ? 1052 ASP   B O     1 
ATOM   16825 C  CB    . ASP   B 1  1054 ? 5.169   73.843  81.564  1.00 23.79 ? 1052 ASP   B CB    1 
ATOM   16826 C  CG    . ASP   B 1  1054 ? 4.363   73.847  82.843  1.00 32.30 ? 1052 ASP   B CG    1 
ATOM   16827 O  OD1   . ASP   B 1  1054 ? 3.135   74.063  82.772  1.00 29.92 ? 1052 ASP   B OD1   1 
ATOM   16828 O  OD2   . ASP   B 1  1054 ? 4.961   73.639  83.919  1.00 33.28 ? 1052 ASP   B OD2   1 
ATOM   16829 N  N     . PHE   B 1  1055 ? 5.748   73.131  78.487  1.00 20.28 ? 1053 PHE   B N     1 
ATOM   16830 C  CA    . PHE   B 1  1055 ? 6.529   73.347  77.279  1.00 19.96 ? 1053 PHE   B CA    1 
ATOM   16831 C  C     . PHE   B 1  1055 ? 5.634   73.770  76.125  1.00 21.77 ? 1053 PHE   B C     1 
ATOM   16832 O  O     . PHE   B 1  1055 ? 5.970   74.699  75.382  1.00 21.68 ? 1053 PHE   B O     1 
ATOM   16833 C  CB    . PHE   B 1  1055 ? 7.305   72.075  76.940  1.00 21.10 ? 1053 PHE   B CB    1 
ATOM   16834 C  CG    . PHE   B 1  1055 ? 8.233   72.216  75.764  1.00 18.84 ? 1053 PHE   B CG    1 
ATOM   16835 C  CD1   . PHE   B 1  1055 ? 9.218   73.193  75.754  1.00 22.07 ? 1053 PHE   B CD1   1 
ATOM   16836 C  CD2   . PHE   B 1  1055 ? 8.132   71.354  74.676  1.00 18.82 ? 1053 PHE   B CD2   1 
ATOM   16837 C  CE1   . PHE   B 1  1055 ? 10.081  73.317  74.667  1.00 21.53 ? 1053 PHE   B CE1   1 
ATOM   16838 C  CE2   . PHE   B 1  1055 ? 8.982   71.484  73.586  1.00 20.98 ? 1053 PHE   B CE2   1 
ATOM   16839 C  CZ    . PHE   B 1  1055 ? 9.953   72.470  73.589  1.00 20.52 ? 1053 PHE   B CZ    1 
ATOM   16840 N  N     . ALA   B 1  1056 ? 4.474   73.120  75.977  1.00 19.84 ? 1054 ALA   B N     1 
ATOM   16841 C  CA    . ALA   B 1  1056 ? 3.560   73.491  74.902  1.00 22.45 ? 1054 ALA   B CA    1 
ATOM   16842 C  C     . ALA   B 1  1056 ? 3.089   74.933  75.049  1.00 20.66 ? 1054 ALA   B C     1 
ATOM   16843 O  O     . ALA   B 1  1056 ? 2.994   75.663  74.056  1.00 22.96 ? 1054 ALA   B O     1 
ATOM   16844 C  CB    . ALA   B 1  1056 ? 2.362   72.541  74.864  1.00 23.47 ? 1054 ALA   B CB    1 
ATOM   16845 N  N     . LYS   B 1  1057 ? 2.787   75.358  76.280  1.00 22.69 ? 1055 LYS   B N     1 
ATOM   16846 C  CA    . LYS   B 1  1057 ? 2.365   76.739  76.494  1.00 23.04 ? 1055 LYS   B CA    1 
ATOM   16847 C  C     . LYS   B 1  1057 ? 3.486   77.709  76.158  1.00 26.03 ? 1055 LYS   B C     1 
ATOM   16848 O  O     . LYS   B 1  1057 ? 3.240   78.784  75.597  1.00 28.02 ? 1055 LYS   B O     1 
ATOM   16849 C  CB    . LYS   B 1  1057 ? 1.912   76.943  77.937  1.00 28.05 ? 1055 LYS   B CB    1 
ATOM   16850 C  CG    . LYS   B 1  1057 ? 0.540   76.378  78.242  1.00 32.16 ? 1055 LYS   B CG    1 
ATOM   16851 C  CD    . LYS   B 1  1057 ? 0.134   76.689  79.668  1.00 27.25 ? 1055 LYS   B CD    1 
ATOM   16852 C  CE    . LYS   B 1  1057 ? 1.153   76.158  80.659  1.00 30.72 ? 1055 LYS   B CE    1 
ATOM   16853 N  NZ    . LYS   B 1  1057 ? 0.634   76.231  82.052  1.00 34.09 ? 1055 LYS   B NZ    1 
ATOM   16854 N  N     . TRP   B 1  1058 ? 4.725   77.349  76.500  1.00 24.92 ? 1056 TRP   B N     1 
ATOM   16855 C  CA    . TRP   B 1  1058 ? 5.859   78.196  76.148  1.00 26.38 ? 1056 TRP   B CA    1 
ATOM   16856 C  C     . TRP   B 1  1058 ? 6.000   78.310  74.637  1.00 25.83 ? 1056 TRP   B C     1 
ATOM   16857 O  O     . TRP   B 1  1058 ? 6.180   79.408  74.101  1.00 27.99 ? 1056 TRP   B O     1 
ATOM   16858 C  CB    . TRP   B 1  1058 ? 7.126   77.635  76.791  1.00 26.31 ? 1056 TRP   B CB    1 
ATOM   16859 C  CG    . TRP   B 1  1058 ? 8.385   78.368  76.444  1.00 26.08 ? 1056 TRP   B CG    1 
ATOM   16860 C  CD1   . TRP   B 1  1058 ? 8.823   79.546  76.973  1.00 32.33 ? 1056 TRP   B CD1   1 
ATOM   16861 C  CD2   . TRP   B 1  1058 ? 9.376   77.956  75.500  1.00 24.81 ? 1056 TRP   B CD2   1 
ATOM   16862 N  NE1   . TRP   B 1  1058 ? 10.024  79.897  76.413  1.00 32.37 ? 1056 TRP   B NE1   1 
ATOM   16863 C  CE2   . TRP   B 1  1058 ? 10.387  78.940  75.504  1.00 30.57 ? 1056 TRP   B CE2   1 
ATOM   16864 C  CE3   . TRP   B 1  1058 ? 9.507   76.854  74.651  1.00 26.97 ? 1056 TRP   B CE3   1 
ATOM   16865 C  CZ2   . TRP   B 1  1058 ? 11.520  78.848  74.694  1.00 27.66 ? 1056 TRP   B CZ2   1 
ATOM   16866 C  CZ3   . TRP   B 1  1058 ? 10.633  76.769  73.838  1.00 30.65 ? 1056 TRP   B CZ3   1 
ATOM   16867 C  CH2   . TRP   B 1  1058 ? 11.622  77.762  73.869  1.00 29.59 ? 1056 TRP   B CH2   1 
ATOM   16868 N  N     . LEU   B 1  1059 ? 5.896   77.180  73.930  1.00 21.82 ? 1057 LEU   B N     1 
ATOM   16869 C  CA    . LEU   B 1  1059 ? 5.980   77.196  72.472  1.00 25.75 ? 1057 LEU   B CA    1 
ATOM   16870 C  C     . LEU   B 1  1059 ? 4.904   78.085  71.863  1.00 30.47 ? 1057 LEU   B C     1 
ATOM   16871 O  O     . LEU   B 1  1059 ? 5.173   78.860  70.938  1.00 30.77 ? 1057 LEU   B O     1 
ATOM   16872 C  CB    . LEU   B 1  1059 ? 5.862   75.779  71.925  1.00 22.60 ? 1057 LEU   B CB    1 
ATOM   16873 C  CG    . LEU   B 1  1059 ? 7.068   74.877  72.182  1.00 22.37 ? 1057 LEU   B CG    1 
ATOM   16874 C  CD1   . LEU   B 1  1059 ? 6.763   73.460  71.760  1.00 23.27 ? 1057 LEU   B CD1   1 
ATOM   16875 C  CD2   . LEU   B 1  1059 ? 8.294   75.413  71.440  1.00 28.26 ? 1057 LEU   B CD2   1 
ATOM   16876 N  N     . ASP   B 1  1060 ? 3.668   77.977  72.352  1.00 27.32 ? 1058 ASP   B N     1 
ATOM   16877 C  CA    . ASP   B 1  1060 ? 2.625   78.840  71.804  1.00 28.34 ? 1058 ASP   B CA    1 
ATOM   16878 C  C     . ASP   B 1  1060 ? 2.878   80.299  72.145  1.00 31.52 ? 1058 ASP   B C     1 
ATOM   16879 O  O     . ASP   B 1  1060 ? 2.569   81.188  71.341  1.00 35.44 ? 1058 ASP   B O     1 
ATOM   16880 C  CB    . ASP   B 1  1060 ? 1.253   78.410  72.298  1.00 34.96 ? 1058 ASP   B CB    1 
ATOM   16881 C  CG    . ASP   B 1  1060 ? 0.589   77.426  71.369  1.00 41.79 ? 1058 ASP   B CG    1 
ATOM   16882 O  OD1   . ASP   B 1  1060 ? 0.635   77.632  70.128  1.00 41.64 ? 1058 ASP   B OD1   1 
ATOM   16883 O  OD2   . ASP   B 1  1060 ? 0.036   76.438  71.883  1.00 34.34 ? 1058 ASP   B OD2   1 
ATOM   16884 N  N     . GLY   B 1  1061 ? 3.435   80.562  73.328  1.00 32.16 ? 1059 GLY   B N     1 
ATOM   16885 C  CA    . GLY   B 1  1061 ? 3.785   81.925  73.684  1.00 33.16 ? 1059 GLY   B CA    1 
ATOM   16886 C  C     . GLY   B 1  1061 ? 4.696   82.581  72.665  1.00 38.77 ? 1059 GLY   B C     1 
ATOM   16887 O  O     . GLY   B 1  1061 ? 4.501   83.743  72.301  1.00 36.86 ? 1059 GLY   B O     1 
ATOM   16888 N  N     . LYS   B 1  1062 ? 5.691   81.843  72.175  1.00 33.36 ? 1060 LYS   B N     1 
ATOM   16889 C  CA    . LYS   B 1  1062 ? 6.626   82.377  71.194  1.00 36.54 ? 1060 LYS   B CA    1 
ATOM   16890 C  C     . LYS   B 1  1062 ? 6.193   82.123  69.753  1.00 38.87 ? 1060 LYS   B C     1 
ATOM   16891 O  O     . LYS   B 1  1062 ? 6.985   82.347  68.832  1.00 42.64 ? 1060 LYS   B O     1 
ATOM   16892 C  CB    . LYS   B 1  1062 ? 8.044   81.856  71.452  1.00 40.43 ? 1060 LYS   B CB    1 
ATOM   16893 C  CG    . LYS   B 1  1062 ? 8.173   80.353  71.492  1.00 41.13 ? 1060 LYS   B CG    1 
ATOM   16894 C  CD    . LYS   B 1  1062 ? 9.586   79.949  71.901  1.00 36.05 ? 1060 LYS   B CD    1 
ATOM   16895 C  CE    . LYS   B 1  1062 ? 10.625  80.547  70.956  1.00 33.05 ? 1060 LYS   B CE    1 
ATOM   16896 N  NZ    . LYS   B 1  1062 ? 12.007  80.424  71.480  1.00 42.17 ? 1060 LYS   B NZ    1 
ATOM   16897 N  N     . GLY   B 1  1063 ? 4.961   81.668  69.536  1.00 36.75 ? 1061 GLY   B N     1 
ATOM   16898 C  CA    . GLY   B 1  1063 ? 4.431   81.524  68.198  1.00 35.77 ? 1061 GLY   B CA    1 
ATOM   16899 C  C     . GLY   B 1  1063 ? 4.884   80.302  67.437  1.00 42.54 ? 1061 GLY   B C     1 
ATOM   16900 O  O     . GLY   B 1  1063 ? 4.634   80.220  66.228  1.00 37.98 ? 1061 GLY   B O     1 
ATOM   16901 N  N     . ALA   B 1  1064 ? 5.540   79.345  68.097  1.00 32.99 ? 1062 ALA   B N     1 
ATOM   16902 C  CA    . ALA   B 1  1064 ? 5.970   78.110  67.443  1.00 33.64 ? 1062 ALA   B CA    1 
ATOM   16903 C  C     . ALA   B 1  1064 ? 4.771   77.166  67.350  1.00 32.91 ? 1062 ALA   B C     1 
ATOM   16904 O  O     . ALA   B 1  1064 ? 4.653   76.172  68.069  1.00 28.94 ? 1062 ALA   B O     1 
ATOM   16905 C  CB    . ALA   B 1  1064 ? 7.138   77.482  68.193  1.00 32.02 ? 1062 ALA   B CB    1 
ATOM   16906 N  N     . ARG   B 1  1065 ? 3.867   77.500  66.425  1.00 33.03 ? 1063 ARG   B N     1 
ATOM   16907 C  CA    . ARG   B 1  1065 ? 2.549   76.868  66.397  1.00 31.23 ? 1063 ARG   B CA    1 
ATOM   16908 C  C     . ARG   B 1  1065 ? 2.636   75.391  66.028  1.00 30.12 ? 1063 ARG   B C     1 
ATOM   16909 O  O     . ARG   B 1  1065 ? 2.020   74.540  66.681  1.00 29.41 ? 1063 ARG   B O     1 
ATOM   16910 C  CB    . ARG   B 1  1065 ? 1.623   77.623  65.439  1.00 36.47 ? 1063 ARG   B CB    1 
ATOM   16911 N  N     . ALA   B 1  1066 ? 3.388   75.062  64.977  1.00 26.26 ? 1064 ALA   B N     1 
ATOM   16912 C  CA    . ALA   B 1  1066 ? 3.534   73.658  64.613  1.00 28.04 ? 1064 ALA   B CA    1 
ATOM   16913 C  C     . ALA   B 1  1066 ? 4.185   72.867  65.740  1.00 27.38 ? 1064 ALA   B C     1 
ATOM   16914 O  O     . ALA   B 1  1066 ? 3.801   71.724  66.013  1.00 27.68 ? 1064 ALA   B O     1 
ATOM   16915 C  CB    . ALA   B 1  1066 ? 4.350   73.526  63.329  1.00 31.27 ? 1064 ALA   B CB    1 
ATOM   16916 N  N     . GLU   B 1  1067 ? 5.174   73.462  66.409  1.00 25.58 ? 1065 GLU   B N     1 
ATOM   16917 C  CA    . GLU   B 1  1067 ? 5.860   72.745  67.476  1.00 28.31 ? 1065 GLU   B CA    1 
ATOM   16918 C  C     . GLU   B 1  1067 ? 4.962   72.567  68.693  1.00 23.37 ? 1065 GLU   B C     1 
ATOM   16919 O  O     . GLU   B 1  1067 ? 4.972   71.505  69.327  1.00 22.17 ? 1065 GLU   B O     1 
ATOM   16920 C  CB    . GLU   B 1  1067 ? 7.160   73.462  67.833  1.00 24.95 ? 1065 GLU   B CB    1 
ATOM   16921 C  CG    . GLU   B 1  1067 ? 8.227   73.339  66.747  1.00 25.85 ? 1065 GLU   B CG    1 
ATOM   16922 C  CD    . GLU   B 1  1067 ? 8.050   74.337  65.626  1.00 31.66 ? 1065 GLU   B CD    1 
ATOM   16923 O  OE1   . GLU   B 1  1067 ? 7.176   75.225  65.734  1.00 29.72 ? 1065 GLU   B OE1   1 
ATOM   16924 O  OE2   . GLU   B 1  1067 ? 8.794   74.231  64.628  1.00 31.41 ? 1065 GLU   B OE2   1 
ATOM   16925 N  N     . ALA   B 1  1068 ? 4.191   73.598  69.043  1.00 24.37 ? 1066 ALA   B N     1 
ATOM   16926 C  CA    . ALA   B 1  1068 ? 3.247   73.465  70.146  1.00 26.30 ? 1066 ALA   B CA    1 
ATOM   16927 C  C     . ALA   B 1  1068 ? 2.233   72.367  69.857  1.00 25.00 ? 1066 ALA   B C     1 
ATOM   16928 O  O     . ALA   B 1  1068 ? 1.889   71.582  70.746  1.00 21.78 ? 1066 ALA   B O     1 
ATOM   16929 C  CB    . ALA   B 1  1068 ? 2.544   74.796  70.387  1.00 24.37 ? 1066 ALA   B CB    1 
ATOM   16930 N  N     . GLU   B 1  1069 ? 1.767   72.281  68.609  1.00 21.10 ? 1067 GLU   B N     1 
ATOM   16931 C  CA    . GLU   B 1  1069 ? 0.846   71.216  68.232  1.00 27.78 ? 1067 GLU   B CA    1 
ATOM   16932 C  C     . GLU   B 1  1069 ? 1.510   69.850  68.335  1.00 28.23 ? 1067 GLU   B C     1 
ATOM   16933 O  O     . GLU   B 1  1069 ? 0.906   68.895  68.840  1.00 23.90 ? 1067 GLU   B O     1 
ATOM   16934 C  CB    . GLU   B 1  1069 ? 0.321   71.462  66.817  1.00 28.68 ? 1067 GLU   B CB    1 
ATOM   16935 C  CG    . GLU   B 1  1069 ? -0.598  70.374  66.282  1.00 29.06 ? 1067 GLU   B CG    1 
ATOM   16936 C  CD    . GLU   B 1  1069 ? -1.960  70.334  66.970  1.00 37.92 ? 1067 GLU   B CD    1 
ATOM   16937 O  OE1   . GLU   B 1  1069 ? -2.240  71.197  67.829  1.00 38.97 ? 1067 GLU   B OE1   1 
ATOM   16938 O  OE2   . GLU   B 1  1069 ? -2.756  69.427  66.647  1.00 45.05 ? 1067 GLU   B OE2   1 
ATOM   16939 N  N     . ALA   B 1  1070 ? 2.753   69.735  67.867  1.00 23.31 ? 1068 ALA   B N     1 
ATOM   16940 C  CA    . ALA   B 1  1070 ? 3.470   68.476  68.025  1.00 24.36 ? 1068 ALA   B CA    1 
ATOM   16941 C  C     . ALA   B 1  1070 ? 3.646   68.136  69.499  1.00 21.10 ? 1068 ALA   B C     1 
ATOM   16942 O  O     . ALA   B 1  1070 ? 3.542   66.968  69.889  1.00 22.85 ? 1068 ALA   B O     1 
ATOM   16943 C  CB    . ALA   B 1  1070 ? 4.829   68.551  67.326  1.00 28.03 ? 1068 ALA   B CB    1 
ATOM   16944 N  N     . ALA   B 1  1071 ? 3.900   69.146  70.331  1.00 20.78 ? 1069 ALA   B N     1 
ATOM   16945 C  CA    . ALA   B 1  1071 ? 4.045   68.903  71.762  1.00 20.56 ? 1069 ALA   B CA    1 
ATOM   16946 C  C     . ALA   B 1  1071 ? 2.749   68.368  72.360  1.00 19.36 ? 1069 ALA   B C     1 
ATOM   16947 O  O     . ALA   B 1  1071 ? 2.759   67.372  73.092  1.00 20.27 ? 1069 ALA   B O     1 
ATOM   16948 C  CB    . ALA   B 1  1071 ? 4.506   70.168  72.487  1.00 18.58 ? 1069 ALA   B CB    1 
ATOM   16949 N  N     . ARG   B 1  1072 ? 1.617   69.010  72.052  1.00 20.06 ? 1070 ARG   B N     1 
ATOM   16950 C  CA    A ARG   B 1  1072 ? 0.338   68.531  72.574  0.59 21.44 ? 1070 ARG   B CA    1 
ATOM   16951 C  CA    B ARG   B 1  1072 ? 0.350   68.525  72.589  0.41 21.46 ? 1070 ARG   B CA    1 
ATOM   16952 C  C     . ARG   B 1  1072 ? 0.045   67.117  72.095  1.00 21.83 ? 1070 ARG   B C     1 
ATOM   16953 O  O     . ARG   B 1  1072 ? -0.426  66.272  72.865  1.00 20.72 ? 1070 ARG   B O     1 
ATOM   16954 C  CB    A ARG   B 1  1072 ? -0.791  69.477  72.162  0.59 22.21 ? 1070 ARG   B CB    1 
ATOM   16955 C  CB    B ARG   B 1  1072 ? -0.781  69.503  72.266  0.41 22.27 ? 1070 ARG   B CB    1 
ATOM   16956 C  CG    A ARG   B 1  1072 ? -0.827  70.775  72.942  0.59 24.72 ? 1070 ARG   B CG    1 
ATOM   16957 C  CG    B ARG   B 1  1072 ? -0.528  70.882  72.846  0.41 24.29 ? 1070 ARG   B CG    1 
ATOM   16958 C  CD    A ARG   B 1  1072 ? -2.045  71.603  72.555  0.59 25.04 ? 1070 ARG   B CD    1 
ATOM   16959 C  CD    B ARG   B 1  1072 ? -1.782  71.737  72.939  0.41 24.69 ? 1070 ARG   B CD    1 
ATOM   16960 N  NE    A ARG   B 1  1072 ? -1.991  72.031  71.163  0.59 26.62 ? 1070 ARG   B NE    1 
ATOM   16961 N  NE    B ARG   B 1  1072 ? -1.445  73.061  73.444  0.41 24.80 ? 1070 ARG   B NE    1 
ATOM   16962 C  CZ    A ARG   B 1  1072 ? -1.488  73.189  70.757  0.59 27.13 ? 1070 ARG   B CZ    1 
ATOM   16963 C  CZ    B ARG   B 1  1072 ? -1.271  73.351  74.726  0.41 21.35 ? 1070 ARG   B CZ    1 
ATOM   16964 N  NH1   A ARG   B 1  1072 ? -1.007  74.072  71.617  0.59 26.74 ? 1070 ARG   B NH1   1 
ATOM   16965 N  NH1   B ARG   B 1  1072 ? -1.477  72.449  75.674  0.41 27.09 ? 1070 ARG   B NH1   1 
ATOM   16966 N  NH2   A ARG   B 1  1072 ? -1.465  73.467  69.456  0.59 23.65 ? 1070 ARG   B NH2   1 
ATOM   16967 N  NH2   B ARG   B 1  1072 ? -0.871  74.571  75.065  0.41 21.92 ? 1070 ARG   B NH2   1 
ATOM   16968 N  N     . ASN   B 1  1073 ? 0.327   66.836  70.824  1.00 20.81 ? 1071 ASN   B N     1 
ATOM   16969 C  CA    . ASN   B 1  1073 ? 0.074   65.503  70.297  1.00 21.45 ? 1071 ASN   B CA    1 
ATOM   16970 C  C     . ASN   B 1  1073 ? 0.941   64.464  70.990  1.00 21.10 ? 1071 ASN   B C     1 
ATOM   16971 O  O     . ASN   B 1  1073 ? 0.472   63.362  71.301  1.00 22.74 ? 1071 ASN   B O     1 
ATOM   16972 C  CB    . ASN   B 1  1073 ? 0.304   65.491  68.790  1.00 23.23 ? 1071 ASN   B CB    1 
ATOM   16973 C  CG    . ASN   B 1  1073 ? -0.765  66.259  68.045  1.00 29.93 ? 1071 ASN   B CG    1 
ATOM   16974 O  OD1   . ASN   B 1  1073 ? -1.865  66.471  68.562  1.00 32.08 ? 1071 ASN   B OD1   1 
ATOM   16975 N  ND2   . ASN   B 1  1073 ? -0.453  66.683  66.829  1.00 32.32 ? 1071 ASN   B ND2   1 
ATOM   16976 N  N     . ALA   B 1  1074 ? 2.210   64.795  71.235  1.00 19.59 ? 1072 ALA   B N     1 
ATOM   16977 C  CA    . ALA   B 1  1074 ? 3.070   63.881  71.976  1.00 19.37 ? 1072 ALA   B CA    1 
ATOM   16978 C  C     . ALA   B 1  1074 ? 2.543   63.663  73.384  1.00 18.19 ? 1072 ALA   B C     1 
ATOM   16979 O  O     . ALA   B 1  1074 ? 2.568   62.539  73.898  1.00 18.09 ? 1072 ALA   B O     1 
ATOM   16980 C  CB    . ALA   B 1  1074 ? 4.492   64.438  72.029  1.00 19.28 ? 1072 ALA   B CB    1 
ATOM   16981 N  N     . GLY   B 1  1075 ? 2.082   64.732  74.032  1.00 17.97 ? 1073 GLY   B N     1 
ATOM   16982 C  CA    . GLY   B 1  1075 ? 1.559   64.594  75.380  1.00 19.08 ? 1073 GLY   B CA    1 
ATOM   16983 C  C     . GLY   B 1  1075 ? 0.407   63.613  75.442  1.00 20.37 ? 1073 GLY   B C     1 
ATOM   16984 O  O     . GLY   B 1  1075 ? 0.308   62.815  76.376  1.00 22.25 ? 1073 GLY   B O     1 
ATOM   16985 N  N     . SER   B 1  1076 ? -0.460  63.642  74.430  1.00 21.15 ? 1074 SER   B N     1 
ATOM   16986 C  CA    . SER   B 1  1076 ? -1.614  62.752  74.412  1.00 20.57 ? 1074 SER   B CA    1 
ATOM   16987 C  C     . SER   B 1  1076 ? -1.227  61.337  74.008  1.00 21.72 ? 1074 SER   B C     1 
ATOM   16988 O  O     . SER   B 1  1076 ? -1.682  60.369  74.626  1.00 24.54 ? 1074 SER   B O     1 
ATOM   16989 C  CB    . SER   B 1  1076 ? -2.678  63.299  73.462  1.00 23.79 ? 1074 SER   B CB    1 
ATOM   16990 O  OG    . SER   B 1  1076 ? -3.233  64.493  73.983  1.00 26.86 ? 1074 SER   B OG    1 
ATOM   16991 N  N     . SER   B 1  1077 ? -0.375  61.185  72.994  1.00 18.92 ? 1075 SER   B N     1 
ATOM   16992 C  CA    . SER   B 1  1077 ? -0.090  59.842  72.507  1.00 21.86 ? 1075 SER   B CA    1 
ATOM   16993 C  C     . SER   B 1  1077 ? 0.921   59.093  73.369  1.00 21.16 ? 1075 SER   B C     1 
ATOM   16994 O  O     . SER   B 1  1077 ? 0.972   57.860  73.305  1.00 25.61 ? 1075 SER   B O     1 
ATOM   16995 C  CB    . SER   B 1  1077 ? 0.344   59.876  71.044  1.00 26.52 ? 1075 SER   B CB    1 
ATOM   16996 O  OG    . SER   B 1  1077 ? 1.691   60.279  70.931  1.00 27.14 ? 1075 SER   B OG    1 
ATOM   16997 N  N     . SER   B 1  1078 ? 1.699   59.804  74.182  1.00 17.02 ? 1076 SER   B N     1 
ATOM   16998 C  CA    . SER   B 1  1078 ? 2.582   59.152  75.137  1.00 16.26 ? 1076 SER   B CA    1 
ATOM   16999 C  C     . SER   B 1  1078 ? 1.797   58.197  76.015  1.00 17.61 ? 1076 SER   B C     1 
ATOM   17000 O  O     . SER   B 1  1078 ? 0.695   58.516  76.475  1.00 17.90 ? 1076 SER   B O     1 
ATOM   17001 C  CB    . SER   B 1  1078 ? 3.211   60.208  76.039  1.00 17.89 ? 1076 SER   B CB    1 
ATOM   17002 O  OG    . SER   B 1  1078 ? 3.884   59.577  77.122  1.00 16.39 ? 1076 SER   B OG    1 
ATOM   17003 N  N     . ALA   B 1  1079 ? 2.375   57.027  76.269  1.00 15.33 ? 1077 ALA   B N     1 
ATOM   17004 C  CA    . ALA   B 1  1079 ? 1.738   56.063  77.154  1.00 16.23 ? 1077 ALA   B CA    1 
ATOM   17005 C  C     . ALA   B 1  1079 ? 2.361   56.073  78.533  1.00 15.65 ? 1077 ALA   B C     1 
ATOM   17006 O  O     . ALA   B 1  1079 ? 2.110   55.165  79.323  1.00 15.64 ? 1077 ALA   B O     1 
ATOM   17007 C  CB    . ALA   B 1  1079 ? 1.759   54.654  76.557  1.00 18.55 ? 1077 ALA   B CB    1 
ATOM   17008 N  N     . LEU   B 1  1080 ? 3.198   57.064  78.819  1.00 15.42 ? 1078 LEU   B N     1 
ATOM   17009 C  CA    . LEU   B 1  1080 ? 3.730   57.239  80.161  1.00 14.88 ? 1078 LEU   B CA    1 
ATOM   17010 C  C     . LEU   B 1  1080 ? 2.596   57.207  81.169  1.00 14.77 ? 1078 LEU   B C     1 
ATOM   17011 O  O     . LEU   B 1  1080 ? 1.597   57.919  81.030  1.00 16.23 ? 1078 LEU   B O     1 
ATOM   17012 C  CB    . LEU   B 1  1080 ? 4.436   58.588  80.241  1.00 15.44 ? 1078 LEU   B CB    1 
ATOM   17013 C  CG    . LEU   B 1  1080 ? 4.872   59.028  81.636  1.00 15.86 ? 1078 LEU   B CG    1 
ATOM   17014 C  CD1   . LEU   B 1  1080 ? 6.029   58.169  82.125  1.00 17.51 ? 1078 LEU   B CD1   1 
ATOM   17015 C  CD2   . LEU   B 1  1080 ? 5.229   60.508  81.631  1.00 18.28 ? 1078 LEU   B CD2   1 
ATOM   17016 N  N     . GLY   B 1  1081 ? 2.762   56.389  82.196  1.00 14.67 ? 1079 GLY   B N     1 
ATOM   17017 C  CA    . GLY   B 1  1081 ? 1.749   56.252  83.218  1.00 16.64 ? 1079 GLY   B CA    1 
ATOM   17018 C  C     . GLY   B 1  1081 ? 0.807   55.085  83.015  1.00 18.15 ? 1079 GLY   B C     1 
ATOM   17019 O  O     . GLY   B 1  1081 ? -0.051  54.844  83.879  1.00 19.35 ? 1079 GLY   B O     1 
ATOM   17020 N  N     . LEU   B 1  1082 ? 0.909   54.383  81.895  1.00 16.75 ? 1080 LEU   B N     1 
ATOM   17021 C  CA    A LEU   B 1  1082 ? 0.158   53.148  81.726  0.48 16.55 ? 1080 LEU   B CA    1 
ATOM   17022 C  CA    B LEU   B 1  1082 ? 0.164   53.144  81.723  0.52 16.55 ? 1080 LEU   B CA    1 
ATOM   17023 C  C     . LEU   B 1  1082 ? 0.438   52.231  82.906  1.00 16.60 ? 1080 LEU   B C     1 
ATOM   17024 O  O     . LEU   B 1  1082 ? 1.575   52.106  83.357  1.00 17.69 ? 1080 LEU   B O     1 
ATOM   17025 C  CB    A LEU   B 1  1082 ? 0.582   52.467  80.426  0.48 16.62 ? 1080 LEU   B CB    1 
ATOM   17026 C  CB    B LEU   B 1  1082 ? 0.612   52.464  80.428  0.52 16.62 ? 1080 LEU   B CB    1 
ATOM   17027 C  CG    A LEU   B 1  1082 ? -0.097  51.135  80.097  0.48 15.95 ? 1080 LEU   B CG    1 
ATOM   17028 C  CG    B LEU   B 1  1082 ? 0.038   51.096  80.042  0.52 16.01 ? 1080 LEU   B CG    1 
ATOM   17029 C  CD1   A LEU   B 1  1082 ? -1.597  51.307  80.050  0.48 19.27 ? 1080 LEU   B CD1   1 
ATOM   17030 C  CD1   B LEU   B 1  1082 ? 0.086   50.946  78.536  0.52 18.31 ? 1080 LEU   B CD1   1 
ATOM   17031 C  CD2   A LEU   B 1  1082 ? 0.415   50.569  78.776  0.48 17.27 ? 1080 LEU   B CD2   1 
ATOM   17032 C  CD2   B LEU   B 1  1082 ? 0.801   49.942  80.695  0.52 14.81 ? 1080 LEU   B CD2   1 
ATOM   17033 N  N     . ASP   B 1  1083 ? -0.610  51.593  83.412  1.00 18.01 ? 1081 ASP   B N     1 
ATOM   17034 C  CA    . ASP   B 1  1083 ? -0.475  50.794  84.624  1.00 21.45 ? 1081 ASP   B CA    1 
ATOM   17035 C  C     . ASP   B 1  1083 ? -1.554  49.720  84.544  1.00 21.86 ? 1081 ASP   B C     1 
ATOM   17036 O  O     . ASP   B 1  1083 ? -2.722  49.982  84.853  1.00 24.12 ? 1081 ASP   B O     1 
ATOM   17037 C  CB    . ASP   B 1  1083 ? -0.653  51.697  85.832  1.00 22.54 ? 1081 ASP   B CB    1 
ATOM   17038 C  CG    . ASP   B 1  1083 ? -0.516  50.965  87.147  1.00 35.42 ? 1081 ASP   B CG    1 
ATOM   17039 O  OD1   . ASP   B 1  1083 ? 0.002   49.831  87.164  1.00 36.74 ? 1081 ASP   B OD1   1 
ATOM   17040 O  OD2   . ASP   B 1  1083 ? -0.931  51.540  88.175  1.00 40.30 ? 1081 ASP   B OD2   1 
ATOM   17041 N  N     . LEU   B 1  1084 ? -1.159  48.533  84.110  1.00 19.03 ? 1082 LEU   B N     1 
ATOM   17042 C  CA    . LEU   B 1  1084 ? -2.084  47.468  83.769  1.00 19.18 ? 1082 LEU   B CA    1 
ATOM   17043 C  C     . LEU   B 1  1084 ? -1.809  46.260  84.646  1.00 19.67 ? 1082 LEU   B C     1 
ATOM   17044 O  O     . LEU   B 1  1084 ? -0.676  46.026  85.071  1.00 18.68 ? 1082 LEU   B O     1 
ATOM   17045 C  CB    . LEU   B 1  1084 ? -1.879  47.029  82.322  1.00 22.67 ? 1082 LEU   B CB    1 
ATOM   17046 C  CG    . LEU   B 1  1084 ? -2.246  48.012  81.215  1.00 26.64 ? 1082 LEU   B CG    1 
ATOM   17047 C  CD1   . LEU   B 1  1084 ? -1.817  47.449  79.882  1.00 25.32 ? 1082 LEU   B CD1   1 
ATOM   17048 C  CD2   . LEU   B 1  1084 ? -3.741  48.318  81.240  1.00 29.02 ? 1082 LEU   B CD2   1 
ATOM   17049 N  N     . GLU   B 1  1085 ? -2.854  45.487  84.904  1.00 17.75 ? 1083 GLU   B N     1 
ATOM   17050 C  CA    . GLU   B 1  1085 ? -2.698  44.139  85.411  1.00 16.29 ? 1083 GLU   B CA    1 
ATOM   17051 C  C     . GLU   B 1  1085 ? -2.891  43.166  84.258  1.00 18.45 ? 1083 GLU   B C     1 
ATOM   17052 O  O     . GLU   B 1  1085 ? -3.885  43.249  83.525  1.00 20.31 ? 1083 GLU   B O     1 
ATOM   17053 C  CB    . GLU   B 1  1085 ? -3.679  43.834  86.549  1.00 18.58 ? 1083 GLU   B CB    1 
ATOM   17054 C  CG    . GLU   B 1  1085 ? -3.415  42.442  87.089  1.00 21.14 ? 1083 GLU   B CG    1 
ATOM   17055 C  CD    . GLU   B 1  1085 ? -4.205  42.077  88.318  1.00 27.67 ? 1083 GLU   B CD    1 
ATOM   17056 O  OE1   . GLU   B 1  1085 ? -4.772  42.981  88.973  1.00 30.40 ? 1083 GLU   B OE1   1 
ATOM   17057 O  OE2   . GLU   B 1  1085 ? -4.248  40.863  88.622  1.00 27.34 ? 1083 GLU   B OE2   1 
ATOM   17058 N  N     . LEU   B 1  1086 ? -1.940  42.283  84.078  1.00 17.21 ? 1084 LEU   B N     1 
ATOM   17059 C  CA    . LEU   B 1  1086 ? -1.951  41.325  82.981  1.00 16.96 ? 1084 LEU   B CA    1 
ATOM   17060 C  C     . LEU   B 1  1086 ? -2.594  40.019  83.437  1.00 21.47 ? 1084 LEU   B C     1 
ATOM   17061 O  O     . LEU   B 1  1086 ? -2.385  39.590  84.572  1.00 21.68 ? 1084 LEU   B O     1 
ATOM   17062 C  CB    . LEU   B 1  1086 ? -0.531  41.042  82.511  1.00 18.39 ? 1084 LEU   B CB    1 
ATOM   17063 C  CG    . LEU   B 1  1086 ? 0.222   42.285  82.041  1.00 18.90 ? 1084 LEU   B CG    1 
ATOM   17064 C  CD1   . LEU   B 1  1086 ? 1.609   41.920  81.555  1.00 19.56 ? 1084 LEU   B CD1   1 
ATOM   17065 C  CD2   . LEU   B 1  1086 ? -0.558  42.969  80.931  1.00 22.55 ? 1084 LEU   B CD2   1 
ATOM   17066 N  N     . PRO   B 1  1087 ? -3.376  39.390  82.568  1.00 19.26 ? 1085 PRO   B N     1 
ATOM   17067 C  CA    . PRO   B 1  1087 ? -3.989  38.105  82.924  1.00 19.95 ? 1085 PRO   B CA    1 
ATOM   17068 C  C     . PRO   B 1  1087 ? -2.927  37.057  83.210  1.00 19.34 ? 1085 PRO   B C     1 
ATOM   17069 O  O     . PRO   B 1  1087 ? -1.914  36.960  82.518  1.00 20.28 ? 1085 PRO   B O     1 
ATOM   17070 C  CB    . PRO   B 1  1087 ? -4.783  37.734  81.668  1.00 23.07 ? 1085 PRO   B CB    1 
ATOM   17071 C  CG    . PRO   B 1  1087 ? -5.031  39.020  80.977  1.00 22.60 ? 1085 PRO   B CG    1 
ATOM   17072 C  CD    . PRO   B 1  1087 ? -3.860  39.905  81.270  1.00 19.94 ? 1085 PRO   B CD    1 
ATOM   17073 N  N     . GLY   B 1  1088 ? -3.155  36.276  84.253  1.00 20.15 ? 1086 GLY   B N     1 
ATOM   17074 C  CA    . GLY   B 1  1088 ? -2.229  35.236  84.617  1.00 20.36 ? 1086 GLY   B CA    1 
ATOM   17075 C  C     . GLY   B 1  1088 ? -2.867  34.288  85.603  1.00 18.20 ? 1086 GLY   B C     1 
ATOM   17076 O  O     . GLY   B 1  1088 ? -4.089  34.236  85.749  1.00 19.10 ? 1086 GLY   B O     1 
ATOM   17077 N  N     . PRO   B 1  1089 ? -2.041  33.537  86.320  1.00 18.02 ? 1087 PRO   B N     1 
ATOM   17078 C  CA    . PRO   B 1  1089 ? -2.571  32.571  87.284  1.00 18.50 ? 1087 PRO   B CA    1 
ATOM   17079 C  C     . PRO   B 1  1089 ? -3.187  33.248  88.492  1.00 18.50 ? 1087 PRO   B C     1 
ATOM   17080 O  O     . PRO   B 1  1089 ? -2.858  34.380  88.854  1.00 18.92 ? 1087 PRO   B O     1 
ATOM   17081 C  CB    . PRO   B 1  1089 ? -1.329  31.783  87.706  1.00 19.76 ? 1087 PRO   B CB    1 
ATOM   17082 C  CG    . PRO   B 1  1089 ? -0.187  32.771  87.517  1.00 21.97 ? 1087 PRO   B CG    1 
ATOM   17083 C  CD    . PRO   B 1  1089 ? -0.565  33.586  86.315  1.00 19.21 ? 1087 PRO   B CD    1 
ATOM   17084 N  N     . VAL   B 1  1090 ? -4.090  32.508  89.140  1.00 16.41 ? 1088 VAL   B N     1 
ATOM   17085 C  CA    . VAL   B 1  1090 ? -4.601  32.949  90.423  1.00 17.31 ? 1088 VAL   B CA    1 
ATOM   17086 C  C     . VAL   B 1  1090 ? -3.468  33.009  91.438  1.00 17.31 ? 1088 VAL   B C     1 
ATOM   17087 O  O     . VAL   B 1  1090 ? -2.419  32.372  91.287  1.00 18.24 ? 1088 VAL   B O     1 
ATOM   17088 C  CB    . VAL   B 1  1090 ? -5.732  32.054  90.945  1.00 18.85 ? 1088 VAL   B CB    1 
ATOM   17089 C  CG1   . VAL   B 1  1090 ? -6.894  32.023  89.953  1.00 19.51 ? 1088 VAL   B CG1   1 
ATOM   17090 C  CG2   . VAL   B 1  1090 ? -5.211  30.646  91.266  1.00 18.58 ? 1088 VAL   B CG2   1 
ATOM   17091 N  N     . GLY   B 1  1091 ? -3.694  33.794  92.489  1.00 18.08 ? 1089 GLY   B N     1 
ATOM   17092 C  CA    . GLY   B 1  1091 ? -2.709  33.907  93.555  1.00 17.74 ? 1089 GLY   B CA    1 
ATOM   17093 C  C     . GLY   B 1  1091 ? -1.486  34.699  93.183  1.00 18.38 ? 1089 GLY   B C     1 
ATOM   17094 O  O     . GLY   B 1  1091 ? -0.471  34.623  93.878  1.00 17.84 ? 1089 GLY   B O     1 
ATOM   17095 N  N     . GLU   B 1  1092 ? -1.555  35.458  92.095  1.00 17.97 ? 1090 GLU   B N     1 
ATOM   17096 C  CA    . GLU   B 1  1092 ? -0.483  36.332  91.679  1.00 17.77 ? 1090 GLU   B CA    1 
ATOM   17097 C  C     . GLU   B 1  1092 ? -1.130  37.551  91.059  1.00 18.21 ? 1090 GLU   B C     1 
ATOM   17098 O  O     . GLU   B 1  1092 ? -2.198  37.456  90.447  1.00 20.01 ? 1090 GLU   B O     1 
ATOM   17099 C  CB    . GLU   B 1  1092 ? 0.350   35.646  90.596  1.00 20.31 ? 1090 GLU   B CB    1 
ATOM   17100 C  CG    . GLU   B 1  1092 ? 1.815   35.573  90.879  1.00 28.50 ? 1090 GLU   B CG    1 
ATOM   17101 C  CD    . GLU   B 1  1092 ? 2.548   34.741  89.845  1.00 27.68 ? 1090 GLU   B CD    1 
ATOM   17102 O  OE1   . GLU   B 1  1092 ? 2.383   35.006  88.631  1.00 23.85 ? 1090 GLU   B OE1   1 
ATOM   17103 O  OE2   . GLU   B 1  1092 ? 3.285   33.816  90.249  1.00 27.67 ? 1090 GLU   B OE2   1 
ATOM   17104 N  N     . ARG   B 1  1093 ? -0.492  38.698  91.239  1.00 16.54 ? 1091 ARG   B N     1 
ATOM   17105 C  CA    . ARG   B 1  1093 ? -0.851  39.903  90.509  1.00 17.33 ? 1091 ARG   B CA    1 
ATOM   17106 C  C     . ARG   B 1  1093 ? 0.352   40.280  89.672  1.00 17.71 ? 1091 ARG   B C     1 
ATOM   17107 O  O     . ARG   B 1  1093 ? 1.453   40.457  90.201  1.00 16.71 ? 1091 ARG   B O     1 
ATOM   17108 C  CB    . ARG   B 1  1093 ? -1.229  41.050  91.447  1.00 18.99 ? 1091 ARG   B CB    1 
ATOM   17109 C  CG    . ARG   B 1  1093 ? -2.674  41.024  91.874  1.00 30.31 ? 1091 ARG   B CG    1 
ATOM   17110 C  CD    . ARG   B 1  1093 ? -3.132  42.414  92.306  1.00 39.57 ? 1091 ARG   B CD    1 
ATOM   17111 N  NE    . ARG   B 1  1093 ? -2.271  42.947  93.352  1.00 42.37 ? 1091 ARG   B NE    1 
ATOM   17112 C  CZ    . ARG   B 1  1093 ? -2.426  42.695  94.644  1.00 52.79 ? 1091 ARG   B CZ    1 
ATOM   17113 N  NH1   . ARG   B 1  1093 ? -3.427  41.949  95.088  1.00 50.08 ? 1091 ARG   B NH1   1 
ATOM   17114 N  NH2   . ARG   B 1  1093 ? -1.551  43.196  95.514  1.00 49.59 ? 1091 ARG   B NH2   1 
ATOM   17115 N  N     . ASN   B 1  1094 ? 0.143   40.382  88.372  1.00 15.59 ? 1092 ASN   B N     1 
ATOM   17116 C  CA    . ASN   B 1  1094 ? 1.224   40.629  87.436  1.00 14.74 ? 1092 ASN   B CA    1 
ATOM   17117 C  C     . ASN   B 1  1094 ? 0.933   41.963  86.787  1.00 16.66 ? 1092 ASN   B C     1 
ATOM   17118 O  O     . ASN   B 1  1094 ? -0.087  42.123  86.103  1.00 18.07 ? 1092 ASN   B O     1 
ATOM   17119 C  CB    . ASN   B 1  1094 ? 1.322   39.488  86.435  1.00 16.11 ? 1092 ASN   B CB    1 
ATOM   17120 C  CG    . ASN   B 1  1094 ? 1.910   38.260  87.073  1.00 16.47 ? 1092 ASN   B CG    1 
ATOM   17121 O  OD1   . ASN   B 1  1094 ? 3.094   38.239  87.361  1.00 16.88 ? 1092 ASN   B OD1   1 
ATOM   17122 N  ND2   . ASN   B 1  1094 ? 1.089   37.259  87.348  1.00 17.20 ? 1092 ASN   B ND2   1 
ATOM   17123 N  N     . LEU   B 1  1095 ? 1.790   42.926  87.063  1.00 15.63 ? 1093 LEU   B N     1 
ATOM   17124 C  CA    . LEU   B 1  1095 ? 1.555   44.316  86.736  1.00 15.84 ? 1093 LEU   B CA    1 
ATOM   17125 C  C     . LEU   B 1  1095 ? 2.558   44.755  85.687  1.00 13.55 ? 1093 LEU   B C     1 
ATOM   17126 O  O     . LEU   B 1  1095 ? 3.687   44.267  85.635  1.00 15.62 ? 1093 LEU   B O     1 
ATOM   17127 C  CB    . LEU   B 1  1095 ? 1.712   45.197  87.968  1.00 17.64 ? 1093 LEU   B CB    1 
ATOM   17128 C  CG    . LEU   B 1  1095 ? 0.871   44.712  89.149  1.00 19.58 ? 1093 LEU   B CG    1 
ATOM   17129 C  CD1   . LEU   B 1  1095 ? 1.111   45.621  90.358  1.00 23.79 ? 1093 LEU   B CD1   1 
ATOM   17130 C  CD2   . LEU   B 1  1095 ? -0.612  44.645  88.786  1.00 20.32 ? 1093 LEU   B CD2   1 
ATOM   17131 N  N     . TYR   B 1  1096 ? 2.131   45.688  84.853  1.00 14.50 ? 1094 TYR   B N     1 
ATOM   17132 C  CA    . TYR   B 1  1096 ? 2.969   46.175  83.772  1.00 14.14 ? 1094 TYR   B CA    1 
ATOM   17133 C  C     . TYR   B 1  1096 ? 2.754   47.674  83.707  1.00 14.34 ? 1094 TYR   B C     1 
ATOM   17134 O  O     . TYR   B 1  1096 ? 1.615   48.138  83.617  1.00 15.34 ? 1094 TYR   B O     1 
ATOM   17135 C  CB    . TYR   B 1  1096 ? 2.586   45.491  82.462  1.00 14.95 ? 1094 TYR   B CB    1 
ATOM   17136 C  CG    . TYR   B 1  1096 ? 3.234   46.030  81.207  1.00 14.91 ? 1094 TYR   B CG    1 
ATOM   17137 C  CD1   . TYR   B 1  1096 ? 4.465   45.558  80.767  1.00 15.40 ? 1094 TYR   B CD1   1 
ATOM   17138 C  CD2   . TYR   B 1  1096 ? 2.578   46.969  80.437  1.00 18.55 ? 1094 TYR   B CD2   1 
ATOM   17139 C  CE1   . TYR   B 1  1096 ? 5.031   46.041  79.593  1.00 15.21 ? 1094 TYR   B CE1   1 
ATOM   17140 C  CE2   . TYR   B 1  1096 ? 3.132   47.448  79.256  1.00 17.43 ? 1094 TYR   B CE2   1 
ATOM   17141 C  CZ    . TYR   B 1  1096 ? 4.357   46.987  78.857  1.00 16.91 ? 1094 TYR   B CZ    1 
ATOM   17142 O  OH    . TYR   B 1  1096 ? 4.922   47.461  77.704  1.00 16.94 ? 1094 TYR   B OH    1 
ATOM   17143 N  N     . THR   B 1  1097 ? 3.838   48.432  83.803  1.00 14.80 ? 1095 THR   B N     1 
ATOM   17144 C  CA    . THR   B 1  1097 ? 3.749   49.871  83.942  1.00 15.67 ? 1095 THR   B CA    1 
ATOM   17145 C  C     . THR   B 1  1097 ? 4.777   50.519  83.035  1.00 14.50 ? 1095 THR   B C     1 
ATOM   17146 O  O     . THR   B 1  1097 ? 5.841   49.949  82.777  1.00 16.56 ? 1095 THR   B O     1 
ATOM   17147 C  CB    . THR   B 1  1097 ? 4.000   50.300  85.383  1.00 19.46 ? 1095 THR   B CB    1 
ATOM   17148 O  OG1   . THR   B 1  1097 ? 5.294   49.857  85.795  1.00 23.34 ? 1095 THR   B OG1   1 
ATOM   17149 C  CG2   . THR   B 1  1097 ? 3.003   49.665  86.291  1.00 18.95 ? 1095 THR   B CG2   1 
ATOM   17150 N  N     . LEU   B 1  1098 ? 4.441   51.702  82.532  1.00 15.13 ? 1096 LEU   B N     1 
ATOM   17151 C  CA    . LEU   B 1  1098 ? 5.357   52.469  81.696  1.00 13.82 ? 1096 LEU   B CA    1 
ATOM   17152 C  C     . LEU   B 1  1098 ? 5.789   53.713  82.447  1.00 14.75 ? 1096 LEU   B C     1 
ATOM   17153 O  O     . LEU   B 1  1098 ? 4.955   54.534  82.845  1.00 16.43 ? 1096 LEU   B O     1 
ATOM   17154 C  CB    . LEU   B 1  1098 ? 4.737   52.859  80.358  1.00 13.93 ? 1096 LEU   B CB    1 
ATOM   17155 C  CG    . LEU   B 1  1098 ? 4.371   51.663  79.486  1.00 14.47 ? 1096 LEU   B CG    1 
ATOM   17156 C  CD1   . LEU   B 1  1098 ? 3.794   52.170  78.179  1.00 15.48 ? 1096 LEU   B CD1   1 
ATOM   17157 C  CD2   . LEU   B 1  1098 ? 5.574   50.777  79.221  1.00 15.69 ? 1096 LEU   B CD2   1 
ATOM   17158 N  N     . HIS   B 1  1099 ? 7.094   53.857  82.605  1.00 15.74 ? 1097 HIS   B N     1 
ATOM   17159 C  CA    . HIS   B 1  1099 ? 7.710   54.956  83.318  1.00 16.40 ? 1097 HIS   B CA    1 
ATOM   17160 C  C     . HIS   B 1  1099 ? 8.586   55.709  82.340  1.00 15.74 ? 1097 HIS   B C     1 
ATOM   17161 O  O     . HIS   B 1  1099 ? 8.820   55.251  81.221  1.00 15.39 ? 1097 HIS   B O     1 
ATOM   17162 C  CB    . HIS   B 1  1099 ? 8.616   54.414  84.419  1.00 17.20 ? 1097 HIS   B CB    1 
ATOM   17163 C  CG    . HIS   B 1  1099 ? 7.895   53.571  85.410  1.00 19.00 ? 1097 HIS   B CG    1 
ATOM   17164 N  ND1   . HIS   B 1  1099 ? 7.519   54.041  86.649  1.00 23.30 ? 1097 HIS   B ND1   1 
ATOM   17165 C  CD2   . HIS   B 1  1099 ? 7.458   52.291  85.340  1.00 23.19 ? 1097 HIS   B CD2   1 
ATOM   17166 C  CE1   . HIS   B 1  1099 ? 6.899   53.078  87.309  1.00 25.17 ? 1097 HIS   B CE1   1 
ATOM   17167 N  NE2   . HIS   B 1  1099 ? 6.849   52.007  86.538  1.00 24.54 ? 1097 HIS   B NE2   1 
ATOM   17168 N  N     . ALA   B 1  1100 ? 9.082   56.863  82.775  1.00 16.45 ? 1098 ALA   B N     1 
ATOM   17169 C  CA    . ALA   B 1  1100 ? 10.088  57.554  81.983  1.00 17.87 ? 1098 ALA   B CA    1 
ATOM   17170 C  C     . ALA   B 1  1100 ? 11.329  56.686  81.851  1.00 16.87 ? 1098 ALA   B C     1 
ATOM   17171 O  O     . ALA   B 1  1100 ? 11.646  55.884  82.737  1.00 18.89 ? 1098 ALA   B O     1 
ATOM   17172 C  CB    . ALA   B 1  1100 ? 10.476  58.864  82.661  1.00 19.01 ? 1098 ALA   B CB    1 
ATOM   17173 N  N     . ARG   B 1  1101 ? 12.018  56.825  80.710  1.00 16.55 ? 1099 ARG   B N     1 
ATOM   17174 C  CA    . ARG   B 1  1101 ? 13.325  56.188  80.556  1.00 16.25 ? 1099 ARG   B CA    1 
ATOM   17175 C  C     . ARG   B 1  1101 ? 14.364  56.775  81.505  1.00 17.08 ? 1099 ARG   B C     1 
ATOM   17176 O  O     . ARG   B 1  1101 ? 15.186  56.038  82.061  1.00 17.98 ? 1099 ARG   B O     1 
ATOM   17177 C  CB    . ARG   B 1  1101 ? 13.812  56.297  79.108  1.00 19.73 ? 1099 ARG   B CB    1 
ATOM   17178 C  CG    . ARG   B 1  1101 ? 13.216  55.265  78.162  1.00 19.75 ? 1099 ARG   B CG    1 
ATOM   17179 C  CD    . ARG   B 1  1101 ? 14.015  53.971  78.170  1.00 20.75 ? 1099 ARG   B CD    1 
ATOM   17180 N  NE    . ARG   B 1  1101 ? 13.471  52.988  77.234  1.00 22.43 ? 1099 ARG   B NE    1 
ATOM   17181 C  CZ    . ARG   B 1  1101 ? 14.194  52.093  76.576  1.00 20.41 ? 1099 ARG   B CZ    1 
ATOM   17182 N  NH1   . ARG   B 1  1101 ? 15.509  52.009  76.730  1.00 19.74 ? 1099 ARG   B NH1   1 
ATOM   17183 N  NH2   . ARG   B 1  1101 ? 13.587  51.251  75.747  1.00 23.57 ? 1099 ARG   B NH2   1 
ATOM   17184 N  N     . GLY   B 1  1102 ? 14.347  58.087  81.702  1.00 16.98 ? 1100 GLY   B N     1 
ATOM   17185 C  CA    . GLY   B 1  1102 ? 15.388  58.743  82.465  1.00 18.85 ? 1100 GLY   B CA    1 
ATOM   17186 C  C     . GLY   B 1  1102 ? 15.842  60.016  81.780  1.00 18.63 ? 1100 GLY   B C     1 
ATOM   17187 O  O     . GLY   B 1  1102 ? 15.032  60.896  81.472  1.00 19.82 ? 1100 GLY   B O     1 
ATOM   17188 N  N     . ARG   B 1  1103 ? 17.143  60.142  81.557  1.00 18.11 ? 1101 ARG   B N     1 
ATOM   17189 C  CA    . ARG   B 1  1103 ? 17.682  61.300  80.868  1.00 19.34 ? 1101 ARG   B CA    1 
ATOM   17190 C  C     . ARG   B 1  1103 ? 18.012  60.904  79.437  1.00 16.92 ? 1101 ARG   B C     1 
ATOM   17191 O  O     . ARG   B 1  1103 ? 18.741  59.935  79.206  1.00 19.29 ? 1101 ARG   B O     1 
ATOM   17192 C  CB    . ARG   B 1  1103 ? 18.929  61.844  81.561  1.00 20.45 ? 1101 ARG   B CB    1 
ATOM   17193 C  CG    . ARG   B 1  1103 ? 19.391  63.144  80.907  1.00 22.14 ? 1101 ARG   B CG    1 
ATOM   17194 C  CD    . ARG   B 1  1103 ? 20.382  63.912  81.758  1.00 26.43 ? 1101 ARG   B CD    1 
ATOM   17195 N  NE    . ARG   B 1  1103 ? 19.706  64.656  82.813  1.00 31.78 ? 1101 ARG   B NE    1 
ATOM   17196 C  CZ    . ARG   B 1  1103 ? 19.830  64.409  84.107  1.00 37.76 ? 1101 ARG   B CZ    1 
ATOM   17197 N  NH1   . ARG   B 1  1103 ? 20.630  63.453  84.554  1.00 45.10 ? 1101 ARG   B NH1   1 
ATOM   17198 N  NH2   . ARG   B 1  1103 ? 19.141  65.147  84.974  1.00 37.19 ? 1101 ARG   B NH2   1 
ATOM   17199 N  N     . ILE   B 1  1104 ? 17.462  61.637  78.486  1.00 16.30 ? 1102 ILE   B N     1 
ATOM   17200 C  CA    . ILE   B 1  1104 ? 17.643  61.335  77.076  1.00 17.06 ? 1102 ILE   B CA    1 
ATOM   17201 C  C     . ILE   B 1  1104 ? 18.657  62.318  76.523  1.00 17.48 ? 1102 ILE   B C     1 
ATOM   17202 O  O     . ILE   B 1  1104 ? 18.545  63.527  76.749  1.00 18.48 ? 1102 ILE   B O     1 
ATOM   17203 C  CB    . ILE   B 1  1104 ? 16.312  61.453  76.315  1.00 16.77 ? 1102 ILE   B CB    1 
ATOM   17204 C  CG1   . ILE   B 1  1104 ? 15.219  60.602  76.990  1.00 18.01 ? 1102 ILE   B CG1   1 
ATOM   17205 C  CG2   . ILE   B 1  1104 ? 16.483  61.069  74.834  1.00 17.25 ? 1102 ILE   B CG2   1 
ATOM   17206 C  CD1   . ILE   B 1  1104 ? 15.532  59.125  77.040  1.00 17.47 ? 1102 ILE   B CD1   1 
ATOM   17207 N  N     . LEU   B 1  1105 ? 19.633  61.803  75.785  1.00 15.93 ? 1103 LEU   B N     1 
ATOM   17208 C  CA    . LEU   B 1  1105 ? 20.580  62.660  75.083  1.00 16.80 ? 1103 LEU   B CA    1 
ATOM   17209 C  C     . LEU   B 1  1105 ? 19.912  63.197  73.823  1.00 17.43 ? 1103 LEU   B C     1 
ATOM   17210 O  O     . LEU   B 1  1105 ? 19.418  62.422  73.000  1.00 16.93 ? 1103 LEU   B O     1 
ATOM   17211 C  CB    . LEU   B 1  1105 ? 21.807  61.832  74.716  1.00 17.94 ? 1103 LEU   B CB    1 
ATOM   17212 C  CG    . LEU   B 1  1105 ? 22.842  62.524  73.840  1.00 17.19 ? 1103 LEU   B CG    1 
ATOM   17213 C  CD1   . LEU   B 1  1105 ? 23.466  63.704  74.579  1.00 17.97 ? 1103 LEU   B CD1   1 
ATOM   17214 C  CD2   . LEU   B 1  1105 ? 23.888  61.496  73.435  1.00 18.09 ? 1103 LEU   B CD2   1 
ATOM   17215 N  N     . LEU   B 1  1106 ? 19.865  64.512  73.678  1.00 16.69 ? 1104 LEU   B N     1 
ATOM   17216 C  CA    . LEU   B 1  1106 ? 19.283  65.140  72.505  1.00 16.55 ? 1104 LEU   B CA    1 
ATOM   17217 C  C     . LEU   B 1  1106 ? 20.419  65.691  71.660  1.00 17.55 ? 1104 LEU   B C     1 
ATOM   17218 O  O     . LEU   B 1  1106 ? 21.256  66.452  72.157  1.00 19.03 ? 1104 LEU   B O     1 
ATOM   17219 C  CB    . LEU   B 1  1106 ? 18.336  66.275  72.898  1.00 18.02 ? 1104 LEU   B CB    1 
ATOM   17220 C  CG    . LEU   B 1  1106 ? 16.861  65.925  73.029  1.00 25.39 ? 1104 LEU   B CG    1 
ATOM   17221 C  CD1   . LEU   B 1  1106 ? 16.644  64.601  73.739  1.00 24.27 ? 1104 LEU   B CD1   1 
ATOM   17222 C  CD2   . LEU   B 1  1106 ? 16.103  67.069  73.705  1.00 17.53 ? 1104 LEU   B CD2   1 
ATOM   17223 N  N     . VAL   B 1  1107 ? 20.431  65.314  70.390  1.00 16.63 ? 1105 VAL   B N     1 
ATOM   17224 C  CA    . VAL   B 1  1107 ? 21.443  65.800  69.461  1.00 15.99 ? 1105 VAL   B CA    1 
ATOM   17225 C  C     . VAL   B 1  1107 ? 20.692  66.481  68.327  1.00 17.57 ? 1105 VAL   B C     1 
ATOM   17226 O  O     . VAL   B 1  1107 ? 20.473  65.873  67.271  1.00 18.61 ? 1105 VAL   B O     1 
ATOM   17227 C  CB    . VAL   B 1  1107 ? 22.346  64.664  68.964  1.00 17.54 ? 1105 VAL   B CB    1 
ATOM   17228 C  CG1   . VAL   B 1  1107 ? 23.513  65.245  68.164  1.00 18.96 ? 1105 VAL   B CG1   1 
ATOM   17229 C  CG2   . VAL   B 1  1107 ? 22.864  63.845  70.133  1.00 17.85 ? 1105 VAL   B CG2   1 
ATOM   17230 N  N     . PRO   B 1  1108 ? 20.243  67.714  68.516  1.00 17.30 ? 1106 PRO   B N     1 
ATOM   17231 C  CA    . PRO   B 1  1108 ? 19.492  68.398  67.469  1.00 18.43 ? 1106 PRO   B CA    1 
ATOM   17232 C  C     . PRO   B 1  1108 ? 20.430  69.035  66.463  1.00 20.15 ? 1106 PRO   B C     1 
ATOM   17233 O  O     . PRO   B 1  1108 ? 21.629  69.222  66.703  1.00 24.64 ? 1106 PRO   B O     1 
ATOM   17234 C  CB    . PRO   B 1  1108 ? 18.762  69.497  68.248  1.00 19.64 ? 1106 PRO   B CB    1 
ATOM   17235 C  CG    . PRO   B 1  1108 ? 19.734  69.837  69.335  1.00 19.31 ? 1106 PRO   B CG    1 
ATOM   17236 C  CD    . PRO   B 1  1108 ? 20.319  68.513  69.751  1.00 18.84 ? 1106 PRO   B CD    1 
ATOM   17237 N  N     . ALA   B 1  1109 ? 19.851  69.383  65.326  1.00 19.92 ? 1107 ALA   B N     1 
ATOM   17238 C  CA    . ALA   B 1  1109 ? 20.520  70.211  64.334  1.00 20.71 ? 1107 ALA   B CA    1 
ATOM   17239 C  C     . ALA   B 1  1109 ? 19.882  71.581  64.197  1.00 25.09 ? 1107 ALA   B C     1 
ATOM   17240 O  O     . ALA   B 1  1109 ? 20.589  72.571  64.006  1.00 24.83 ? 1107 ALA   B O     1 
ATOM   17241 C  CB    . ALA   B 1  1109 ? 20.502  69.518  62.970  1.00 21.72 ? 1107 ALA   B CB    1 
ATOM   17242 N  N     . THR   B 1  1110 ? 18.559  71.660  64.302  1.00 20.61 ? 1108 THR   B N     1 
ATOM   17243 C  CA    . THR   B 1  1110 ? 17.827  72.897  64.093  1.00 21.75 ? 1108 THR   B CA    1 
ATOM   17244 C  C     . THR   B 1  1110 ? 16.975  73.205  65.314  1.00 21.54 ? 1108 THR   B C     1 
ATOM   17245 O  O     . THR   B 1  1110 ? 16.681  72.329  66.131  1.00 20.77 ? 1108 THR   B O     1 
ATOM   17246 C  CB    . THR   B 1  1110 ? 16.897  72.802  62.876  1.00 22.30 ? 1108 THR   B CB    1 
ATOM   17247 O  OG1   . THR   B 1  1110 ? 15.903  71.792  63.099  1.00 21.88 ? 1108 THR   B OG1   1 
ATOM   17248 C  CG2   . THR   B 1  1110 ? 17.684  72.459  61.615  1.00 24.49 ? 1108 THR   B CG2   1 
ATOM   17249 N  N     . GLU   B 1  1111 ? 16.569  74.468  65.416  1.00 22.03 ? 1109 GLU   B N     1 
ATOM   17250 C  CA    . GLU   B 1  1111 ? 15.688  74.870  66.505  1.00 21.79 ? 1109 GLU   B CA    1 
ATOM   17251 C  C     . GLU   B 1  1111 ? 14.405  74.047  66.503  1.00 21.79 ? 1109 GLU   B C     1 
ATOM   17252 O  O     . GLU   B 1  1111 ? 14.004  73.504  67.537  1.00 21.16 ? 1109 GLU   B O     1 
ATOM   17253 C  CB    . GLU   B 1  1111 ? 15.366  76.355  66.380  1.00 22.54 ? 1109 GLU   B CB    1 
ATOM   17254 C  CG    . GLU   B 1  1111 ? 14.356  76.827  67.397  1.00 25.51 ? 1109 GLU   B CG    1 
ATOM   17255 C  CD    . GLU   B 1  1111 ? 14.174  78.326  67.354  1.00 27.82 ? 1109 GLU   B CD    1 
ATOM   17256 O  OE1   . GLU   B 1  1111 ? 14.996  79.036  67.965  1.00 29.05 ? 1109 GLU   B OE1   1 
ATOM   17257 O  OE2   . GLU   B 1  1111 ? 13.214  78.785  66.703  1.00 32.12 ? 1109 GLU   B OE2   1 
ATOM   17258 N  N     . SER   B 1  1112 ? 13.748  73.942  65.346  1.00 21.58 ? 1110 SER   B N     1 
ATOM   17259 C  CA    . SER   B 1  1112 ? 12.514  73.164  65.281  1.00 22.41 ? 1110 SER   B CA    1 
ATOM   17260 C  C     . SER   B 1  1112 ? 12.767  71.709  65.645  1.00 22.32 ? 1110 SER   B C     1 
ATOM   17261 O  O     . SER   B 1  1112 ? 11.980  71.095  66.379  1.00 21.32 ? 1110 SER   B O     1 
ATOM   17262 C  CB    . SER   B 1  1112 ? 11.888  73.264  63.890  1.00 23.45 ? 1110 SER   B CB    1 
ATOM   17263 O  OG    . SER   B 1  1112 ? 10.673  72.523  63.833  1.00 25.31 ? 1110 SER   B OG    1 
ATOM   17264 N  N     . GLY   B 1  1113 ? 13.876  71.144  65.164  1.00 20.85 ? 1111 GLY   B N     1 
ATOM   17265 C  CA    . GLY   B 1  1113 ? 14.208  69.780  65.536  1.00 18.44 ? 1111 GLY   B CA    1 
ATOM   17266 C  C     . GLY   B 1  1113 ? 14.358  69.620  67.034  1.00 18.91 ? 1111 GLY   B C     1 
ATOM   17267 O  O     . GLY   B 1  1113 ? 13.863  68.653  67.620  1.00 19.04 ? 1111 GLY   B O     1 
ATOM   17268 N  N     . LEU   B 1  1114 ? 15.045  70.569  67.675  1.00 18.09 ? 1112 LEU   B N     1 
ATOM   17269 C  CA    . LEU   B 1  1114 ? 15.188  70.522  69.128  1.00 16.70 ? 1112 LEU   B CA    1 
ATOM   17270 C  C     . LEU   B 1  1114 ? 13.834  70.587  69.818  1.00 19.46 ? 1112 LEU   B C     1 
ATOM   17271 O  O     . LEU   B 1  1114 ? 13.590  69.840  70.768  1.00 17.80 ? 1112 LEU   B O     1 
ATOM   17272 C  CB    . LEU   B 1  1114 ? 16.079  71.659  69.622  1.00 20.44 ? 1112 LEU   B CB    1 
ATOM   17273 C  CG    . LEU   B 1  1114 ? 16.180  71.838  71.136  1.00 21.44 ? 1112 LEU   B CG    1 
ATOM   17274 C  CD1   . LEU   B 1  1114 ? 16.699  70.569  71.806  1.00 19.22 ? 1112 LEU   B CD1   1 
ATOM   17275 C  CD2   . LEU   B 1  1114 ? 17.062  73.038  71.462  1.00 22.35 ? 1112 LEU   B CD2   1 
ATOM   17276 N  N     . TYR   B 1  1115 ? 12.946  71.474  69.358  1.00 19.54 ? 1113 TYR   B N     1 
ATOM   17277 C  CA    . TYR   B 1  1115 ? 11.622  71.565  69.975  1.00 18.47 ? 1113 TYR   B CA    1 
ATOM   17278 C  C     . TYR   B 1  1115 ? 10.864  70.254  69.836  1.00 19.38 ? 1113 TYR   B C     1 
ATOM   17279 O  O     . TYR   B 1  1115 ? 10.189  69.820  70.775  1.00 19.32 ? 1113 TYR   B O     1 
ATOM   17280 C  CB    . TYR   B 1  1115 ? 10.814  72.694  69.338  1.00 19.94 ? 1113 TYR   B CB    1 
ATOM   17281 C  CG    . TYR   B 1  1115 ? 11.333  74.082  69.617  1.00 20.43 ? 1113 TYR   B CG    1 
ATOM   17282 C  CD1   . TYR   B 1  1115 ? 12.284  74.307  70.590  1.00 20.67 ? 1113 TYR   B CD1   1 
ATOM   17283 C  CD2   . TYR   B 1  1115 ? 10.861  75.168  68.893  1.00 23.65 ? 1113 TYR   B CD2   1 
ATOM   17284 C  CE1   . TYR   B 1  1115 ? 12.756  75.584  70.845  1.00 24.87 ? 1113 TYR   B CE1   1 
ATOM   17285 C  CE2   . TYR   B 1  1115 ? 11.323  76.444  69.140  1.00 25.03 ? 1113 TYR   B CE2   1 
ATOM   17286 C  CZ    . TYR   B 1  1115 ? 12.271  76.644  70.118  1.00 26.23 ? 1113 TYR   B CZ    1 
ATOM   17287 O  OH    . TYR   B 1  1115 ? 12.740  77.915  70.359  1.00 30.04 ? 1113 TYR   B OH    1 
ATOM   17288 N  N     . HIS   B 1  1116 ? 10.956  69.613  68.673  1.00 18.04 ? 1114 HIS   B N     1 
ATOM   17289 C  CA    . HIS   B 1  1116 ? 10.300  68.322  68.487  1.00 18.01 ? 1114 HIS   B CA    1 
ATOM   17290 C  C     . HIS   B 1  1116 ? 10.937  67.252  69.359  1.00 19.44 ? 1114 HIS   B C     1 
ATOM   17291 O  O     . HIS   B 1  1116 ? 10.233  66.407  69.925  1.00 20.12 ? 1114 HIS   B O     1 
ATOM   17292 C  CB    . HIS   B 1  1116 ? 10.352  67.904  67.017  1.00 18.60 ? 1114 HIS   B CB    1 
ATOM   17293 C  CG    . HIS   B 1  1116 ? 9.313   68.558  66.162  1.00 22.38 ? 1114 HIS   B CG    1 
ATOM   17294 N  ND1   . HIS   B 1  1116 ? 9.504   69.786  65.565  1.00 24.32 ? 1114 HIS   B ND1   1 
ATOM   17295 C  CD2   . HIS   B 1  1116 ? 8.073   68.150  65.798  1.00 23.49 ? 1114 HIS   B CD2   1 
ATOM   17296 C  CE1   . HIS   B 1  1116 ? 8.426   70.109  64.874  1.00 26.11 ? 1114 HIS   B CE1   1 
ATOM   17297 N  NE2   . HIS   B 1  1116 ? 7.545   69.134  64.996  1.00 26.48 ? 1114 HIS   B NE2   1 
ATOM   17298 N  N     . GLN   B 1  1117 ? 12.270  67.258  69.478  1.00 17.31 ? 1115 GLN   B N     1 
ATOM   17299 C  CA    . GLN   B 1  1117 ? 12.916  66.280  70.347  1.00 15.99 ? 1115 GLN   B CA    1 
ATOM   17300 C  C     . GLN   B 1  1117 ? 12.502  66.490  71.791  1.00 17.55 ? 1115 GLN   B C     1 
ATOM   17301 O  O     . GLN   B 1  1117 ? 12.226  65.525  72.519  1.00 16.88 ? 1115 GLN   B O     1 
ATOM   17302 C  CB    . GLN   B 1  1117 ? 14.436  66.389  70.227  1.00 16.56 ? 1115 GLN   B CB    1 
ATOM   17303 C  CG    . GLN   B 1  1117 ? 14.974  65.924  68.895  1.00 16.22 ? 1115 GLN   B CG    1 
ATOM   17304 C  CD    . GLN   B 1  1117 ? 16.473  66.118  68.797  1.00 17.35 ? 1115 GLN   B CD    1 
ATOM   17305 O  OE1   . GLN   B 1  1117 ? 17.073  66.798  69.623  1.00 19.10 ? 1115 GLN   B OE1   1 
ATOM   17306 N  NE2   . GLN   B 1  1117 ? 17.086  65.502  67.791  1.00 18.19 ? 1115 GLN   B NE2   1 
ATOM   17307 N  N     . LEU   B 1  1118 ? 12.510  67.747  72.235  1.00 17.61 ? 1116 LEU   B N     1 
ATOM   17308 C  CA    . LEU   B 1  1118 ? 12.073  68.062  73.588  1.00 17.19 ? 1116 LEU   B CA    1 
ATOM   17309 C  C     . LEU   B 1  1118 ? 10.641  67.615  73.810  1.00 17.59 ? 1116 LEU   B C     1 
ATOM   17310 O  O     . LEU   B 1  1118 ? 10.326  67.039  74.852  1.00 18.67 ? 1116 LEU   B O     1 
ATOM   17311 C  CB    . LEU   B 1  1118 ? 12.177  69.559  73.839  1.00 19.12 ? 1116 LEU   B CB    1 
ATOM   17312 C  CG    . LEU   B 1  1118 ? 13.580  70.064  74.109  1.00 24.69 ? 1116 LEU   B CG    1 
ATOM   17313 C  CD1   . LEU   B 1  1118 ? 13.577  71.575  74.075  1.00 23.96 ? 1116 LEU   B CD1   1 
ATOM   17314 C  CD2   . LEU   B 1  1118 ? 14.032  69.568  75.463  1.00 23.75 ? 1116 LEU   B CD2   1 
ATOM   17315 N  N     . ALA   B 1  1119 ? 9.761   67.869  72.842  1.00 19.01 ? 1117 ALA   B N     1 
ATOM   17316 C  CA    . ALA   B 1  1119 ? 8.373   67.450  72.998  1.00 18.20 ? 1117 ALA   B CA    1 
ATOM   17317 C  C     . ALA   B 1  1119 ? 8.285   65.950  73.226  1.00 17.51 ? 1117 ALA   B C     1 
ATOM   17318 O  O     . ALA   B 1  1119 ? 7.615   65.492  74.161  1.00 19.05 ? 1117 ALA   B O     1 
ATOM   17319 C  CB    . ALA   B 1  1119 ? 7.552   67.868  71.779  1.00 19.65 ? 1117 ALA   B CB    1 
ATOM   17320 N  N     . ALA   B 1  1120 ? 8.992   65.171  72.408  1.00 15.87 ? 1118 ALA   B N     1 
ATOM   17321 C  CA    . ALA   B 1  1120 ? 8.926   63.721  72.542  1.00 15.38 ? 1118 ALA   B CA    1 
ATOM   17322 C  C     . ALA   B 1  1120 ? 9.481   63.274  73.886  1.00 16.98 ? 1118 ALA   B C     1 
ATOM   17323 O  O     . ALA   B 1  1120 ? 8.874   62.438  74.574  1.00 17.41 ? 1118 ALA   B O     1 
ATOM   17324 C  CB    . ALA   B 1  1120 ? 9.690   63.053  71.398  1.00 17.35 ? 1118 ALA   B CB    1 
ATOM   17325 N  N     . ALA   B 1  1121 ? 10.620  63.840  74.300  1.00 15.66 ? 1119 ALA   B N     1 
ATOM   17326 C  CA    . ALA   B 1  1121 ? 11.228  63.411  75.552  1.00 15.74 ? 1119 ALA   B CA    1 
ATOM   17327 C  C     . ALA   B 1  1121 ? 10.412  63.852  76.759  1.00 15.05 ? 1119 ALA   B C     1 
ATOM   17328 O  O     . ALA   B 1  1121 ? 10.248  63.080  77.712  1.00 15.54 ? 1119 ALA   B O     1 
ATOM   17329 C  CB    . ALA   B 1  1121 ? 12.656  63.945  75.653  1.00 17.14 ? 1119 ALA   B CB    1 
ATOM   17330 N  N     . LEU   B 1  1122 ? 9.921   65.096  76.755  1.00 16.07 ? 1120 LEU   B N     1 
ATOM   17331 C  CA    . LEU   B 1  1122 ? 9.161   65.572  77.907  1.00 15.50 ? 1120 LEU   B CA    1 
ATOM   17332 C  C     . LEU   B 1  1122 ? 7.840   64.833  78.026  1.00 16.48 ? 1120 LEU   B C     1 
ATOM   17333 O  O     . LEU   B 1  1122 ? 7.408   64.508  79.136  1.00 17.06 ? 1120 LEU   B O     1 
ATOM   17334 C  CB    . LEU   B 1  1122 ? 8.905   67.073  77.822  1.00 16.82 ? 1120 LEU   B CB    1 
ATOM   17335 C  CG    . LEU   B 1  1122 ? 10.166  67.932  77.880  1.00 20.69 ? 1120 LEU   B CG    1 
ATOM   17336 C  CD1   . LEU   B 1  1122 ? 9.813   69.381  77.587  1.00 19.89 ? 1120 LEU   B CD1   1 
ATOM   17337 C  CD2   . LEU   B 1  1122 ? 10.872  67.798  79.235  1.00 20.59 ? 1120 LEU   B CD2   1 
ATOM   17338 N  N     . ALA   B 1  1123 ? 7.194   64.556  76.895  1.00 15.03 ? 1121 ALA   B N     1 
ATOM   17339 C  CA    . ALA   B 1  1123 ? 5.891   63.901  76.938  1.00 16.21 ? 1121 ALA   B CA    1 
ATOM   17340 C  C     . ALA   B 1  1123 ? 5.983   62.521  77.548  1.00 19.51 ? 1121 ALA   B C     1 
ATOM   17341 O  O     . ALA   B 1  1123 ? 4.981   62.004  78.052  1.00 17.58 ? 1121 ALA   B O     1 
ATOM   17342 C  CB    . ALA   B 1  1123 ? 5.349   63.750  75.524  1.00 16.05 ? 1121 ALA   B CB    1 
ATOM   17343 N  N     . THR   B 1  1124 ? 7.156   61.910  77.488  1.00 15.33 ? 1122 THR   B N     1 
ATOM   17344 C  CA    . THR   B 1  1124 ? 7.387   60.595  78.047  1.00 14.09 ? 1122 THR   B CA    1 
ATOM   17345 C  C     . THR   B 1  1124 ? 8.078   60.664  79.406  1.00 13.40 ? 1122 THR   B C     1 
ATOM   17346 O  O     . THR   B 1  1124 ? 8.594   59.654  79.882  1.00 16.14 ? 1122 THR   B O     1 
ATOM   17347 C  CB    . THR   B 1  1124 ? 8.148   59.728  77.042  1.00 16.60 ? 1122 THR   B CB    1 
ATOM   17348 O  OG1   . THR   B 1  1124 ? 9.243   60.478  76.510  1.00 15.83 ? 1122 THR   B OG1   1 
ATOM   17349 C  CG2   . THR   B 1  1124 ? 7.200   59.330  75.890  1.00 15.48 ? 1122 THR   B CG2   1 
ATOM   17350 N  N     . GLY   B 1  1125 ? 8.086   61.832  80.035  1.00 15.55 ? 1123 GLY   B N     1 
ATOM   17351 C  CA    . GLY   B 1  1125 ? 8.502   61.971  81.417  1.00 15.69 ? 1123 GLY   B CA    1 
ATOM   17352 C  C     . GLY   B 1  1125 ? 9.984   62.137  81.623  1.00 15.43 ? 1123 GLY   B C     1 
ATOM   17353 O  O     . GLY   B 1  1125 ? 10.437  62.150  82.771  1.00 16.34 ? 1123 GLY   B O     1 
ATOM   17354 N  N     . ASN   B 1  1126 ? 10.744  62.290  80.559  1.00 16.33 ? 1124 ASN   B N     1 
ATOM   17355 C  CA    . ASN   B 1  1126 ? 12.188  62.265  80.661  1.00 14.99 ? 1124 ASN   B CA    1 
ATOM   17356 C  C     . ASN   B 1  1126 ? 12.751  63.648  80.911  1.00 15.71 ? 1124 ASN   B C     1 
ATOM   17357 O  O     . ASN   B 1  1126 ? 12.137  64.672  80.621  1.00 16.96 ? 1124 ASN   B O     1 
ATOM   17358 C  CB    . ASN   B 1  1126 ? 12.787  61.709  79.376  1.00 14.28 ? 1124 ASN   B CB    1 
ATOM   17359 C  CG    . ASN   B 1  1126 ? 12.310  60.314  79.100  1.00 15.30 ? 1124 ASN   B CG    1 
ATOM   17360 O  OD1   . ASN   B 1  1126 ? 12.663  59.383  79.815  1.00 16.96 ? 1124 ASN   B OD1   1 
ATOM   17361 N  ND2   . ASN   B 1  1126 ? 11.505  60.153  78.061  1.00 15.87 ? 1124 ASN   B ND2   1 
ATOM   17362 N  N     . SER   B 1  1127 ? 13.954  63.648  81.461  1.00 17.26 ? 1125 SER   B N     1 
ATOM   17363 C  CA    . SER   B 1  1127 ? 14.809  64.815  81.402  1.00 17.44 ? 1125 SER   B CA    1 
ATOM   17364 C  C     . SER   B 1  1127 ? 15.698  64.673  80.174  1.00 17.57 ? 1125 SER   B C     1 
ATOM   17365 O  O     . SER   B 1  1127 ? 15.716  63.633  79.518  1.00 16.74 ? 1125 SER   B O     1 
ATOM   17366 C  CB    . SER   B 1  1127 ? 15.648  64.921  82.670  1.00 17.73 ? 1125 SER   B CB    1 
ATOM   17367 O  OG    . SER   B 1  1127 ? 16.457  63.772  82.854  1.00 22.82 ? 1125 SER   B OG    1 
ATOM   17368 N  N     . VAL   B 1  1128 ? 16.423  65.737  79.846  1.00 18.13 ? 1126 VAL   B N     1 
ATOM   17369 C  CA    . VAL   B 1  1128 ? 17.240  65.726  78.642  1.00 16.42 ? 1126 VAL   B CA    1 
ATOM   17370 C  C     . VAL   B 1  1128 ? 18.592  66.350  78.920  1.00 19.14 ? 1126 VAL   B C     1 
ATOM   17371 O  O     . VAL   B 1  1128 ? 18.730  67.239  79.764  1.00 21.02 ? 1126 VAL   B O     1 
ATOM   17372 C  CB    . VAL   B 1  1128 ? 16.574  66.439  77.448  1.00 18.25 ? 1126 VAL   B CB    1 
ATOM   17373 C  CG1   . VAL   B 1  1128 ? 15.255  65.754  77.085  1.00 17.04 ? 1126 VAL   B CG1   1 
ATOM   17374 C  CG2   . VAL   B 1  1128 ? 16.345  67.914  77.771  1.00 19.25 ? 1126 VAL   B CG2   1 
ATOM   17375 N  N     . ALA   B 1  1129 ? 19.588  65.882  78.177  1.00 17.47 ? 1127 ALA   B N     1 
ATOM   17376 C  CA    . ALA   B 1  1129 ? 20.859  66.577  78.032  1.00 18.90 ? 1127 ALA   B CA    1 
ATOM   17377 C  C     . ALA   B 1  1129 ? 20.986  66.913  76.558  1.00 16.67 ? 1127 ALA   B C     1 
ATOM   17378 O  O     . ALA   B 1  1129 ? 20.966  66.013  75.716  1.00 17.42 ? 1127 ALA   B O     1 
ATOM   17379 C  CB    . ALA   B 1  1129 ? 22.015  65.684  78.469  1.00 21.26 ? 1127 ALA   B CB    1 
ATOM   17380 N  N     . ILE   B 1  1130 ? 21.062  68.199  76.238  1.00 17.22 ? 1128 ILE   B N     1 
ATOM   17381 C  CA    . ILE   B 1  1130 ? 21.102  68.653  74.855  1.00 16.50 ? 1128 ILE   B CA    1 
ATOM   17382 C  C     . ILE   B 1  1130 ? 22.550  68.896  74.474  1.00 18.46 ? 1128 ILE   B C     1 
ATOM   17383 O  O     . ILE   B 1  1130 ? 23.304  69.520  75.231  1.00 18.00 ? 1128 ILE   B O     1 
ATOM   17384 C  CB    . ILE   B 1  1130 ? 20.285  69.935  74.656  1.00 17.77 ? 1128 ILE   B CB    1 
ATOM   17385 C  CG1   . ILE   B 1  1130 ? 18.876  69.771  75.244  1.00 21.23 ? 1128 ILE   B CG1   1 
ATOM   17386 C  CG2   . ILE   B 1  1130 ? 20.208  70.273  73.179  1.00 19.32 ? 1128 ILE   B CG2   1 
ATOM   17387 C  CD1   . ILE   B 1  1130 ? 18.154  71.088  75.361  1.00 20.30 ? 1128 ILE   B CD1   1 
ATOM   17388 N  N     . ASP   B 1  1131 ? 22.927  68.411  73.301  1.00 18.16 ? 1129 ASP   B N     1 
ATOM   17389 C  CA    . ASP   B 1  1131 ? 24.291  68.575  72.822  1.00 17.97 ? 1129 ASP   B CA    1 
ATOM   17390 C  C     . ASP   B 1  1131 ? 24.608  70.056  72.677  1.00 19.02 ? 1129 ASP   B C     1 
ATOM   17391 O  O     . ASP   B 1  1131 ? 24.007  70.744  71.852  1.00 18.75 ? 1129 ASP   B O     1 
ATOM   17392 C  CB    . ASP   B 1  1131 ? 24.392  67.889  71.466  1.00 18.09 ? 1129 ASP   B CB    1 
ATOM   17393 C  CG    . ASP   B 1  1131 ? 25.738  68.092  70.823  1.00 19.90 ? 1129 ASP   B CG    1 
ATOM   17394 O  OD1   . ASP   B 1  1131 ? 26.722  68.216  71.576  1.00 21.62 ? 1129 ASP   B OD1   1 
ATOM   17395 O  OD2   . ASP   B 1  1131 ? 25.788  68.152  69.585  1.00 20.90 ? 1129 ASP   B OD2   1 
ATOM   17396 N  N     . ALA   B 1  1132 ? 25.570  70.542  73.468  1.00 20.31 ? 1130 ALA   B N     1 
ATOM   17397 C  CA    . ALA   B 1  1132 ? 25.936  71.957  73.404  1.00 20.28 ? 1130 ALA   B CA    1 
ATOM   17398 C  C     . ALA   B 1  1132 ? 26.537  72.323  72.055  1.00 22.05 ? 1130 ALA   B C     1 
ATOM   17399 O  O     . ALA   B 1  1132 ? 26.433  73.479  71.622  1.00 22.31 ? 1130 ALA   B O     1 
ATOM   17400 C  CB    . ALA   B 1  1132 ? 26.889  72.310  74.548  1.00 20.76 ? 1130 ALA   B CB    1 
ATOM   17401 N  N     . ALA   B 1  1133 ? 27.159  71.361  71.372  1.00 20.62 ? 1131 ALA   B N     1 
ATOM   17402 C  CA    . ALA   B 1  1133 ? 27.752  71.652  70.075  1.00 24.53 ? 1131 ALA   B CA    1 
ATOM   17403 C  C     . ALA   B 1  1133 ? 26.714  71.997  69.020  1.00 26.22 ? 1131 ALA   B C     1 
ATOM   17404 O  O     . ALA   B 1  1133 ? 27.087  72.460  67.938  1.00 26.32 ? 1131 ALA   B O     1 
ATOM   17405 C  CB    . ALA   B 1  1133 ? 28.630  70.488  69.606  1.00 23.40 ? 1131 ALA   B CB    1 
ATOM   17406 N  N     . SER   B 1  1134 ? 25.424  71.782  69.303  1.00 20.67 ? 1132 SER   B N     1 
ATOM   17407 C  CA    . SER   B 1  1134 ? 24.392  72.213  68.373  1.00 21.21 ? 1132 SER   B CA    1 
ATOM   17408 C  C     . SER   B 1  1134 ? 24.337  73.729  68.240  1.00 18.88 ? 1132 SER   B C     1 
ATOM   17409 O  O     . SER   B 1  1134 ? 23.850  74.223  67.221  1.00 22.81 ? 1132 SER   B O     1 
ATOM   17410 C  CB    . SER   B 1  1134 ? 23.024  71.718  68.853  1.00 20.68 ? 1132 SER   B CB    1 
ATOM   17411 O  OG    . SER   B 1  1134 ? 22.677  72.356  70.071  1.00 21.88 ? 1132 SER   B OG    1 
ATOM   17412 N  N     . GLY   B 1  1135 ? 24.808  74.472  69.240  1.00 21.23 ? 1133 GLY   B N     1 
ATOM   17413 C  CA    . GLY   B 1  1135 ? 24.749  75.918  69.161  1.00 24.43 ? 1133 GLY   B CA    1 
ATOM   17414 C  C     . GLY   B 1  1135 ? 23.363  76.503  69.325  1.00 26.12 ? 1133 GLY   B C     1 
ATOM   17415 O  O     . GLY   B 1  1135 ? 23.152  77.674  68.997  1.00 26.76 ? 1133 GLY   B O     1 
ATOM   17416 N  N     . LEU   B 1  1136 ? 22.411  75.726  69.846  1.00 23.14 ? 1134 LEU   B N     1 
ATOM   17417 C  CA    . LEU   B 1  1136 ? 21.010  76.126  69.896  1.00 22.12 ? 1134 LEU   B CA    1 
ATOM   17418 C  C     . LEU   B 1  1136 ? 20.587  76.680  71.254  1.00 26.53 ? 1134 LEU   B C     1 
ATOM   17419 O  O     . LEU   B 1  1136 ? 19.386  76.751  71.533  1.00 24.34 ? 1134 LEU   B O     1 
ATOM   17420 C  CB    . LEU   B 1  1136 ? 20.121  74.947  69.504  1.00 20.20 ? 1134 LEU   B CB    1 
ATOM   17421 C  CG    . LEU   B 1  1136 ? 20.319  74.422  68.085  1.00 22.85 ? 1134 LEU   B CG    1 
ATOM   17422 C  CD1   . LEU   B 1  1136 ? 19.542  73.142  67.887  1.00 23.41 ? 1134 LEU   B CD1   1 
ATOM   17423 C  CD2   . LEU   B 1  1136 ? 19.881  75.467  67.062  1.00 24.41 ? 1134 LEU   B CD2   1 
ATOM   17424 N  N     . GLN   B 1  1137 ? 21.539  77.087  72.096  1.00 23.33 ? 1135 GLN   B N     1 
ATOM   17425 C  CA    . GLN   B 1  1137 ? 21.201  77.510  73.450  1.00 22.79 ? 1135 GLN   B CA    1 
ATOM   17426 C  C     . GLN   B 1  1137 ? 20.209  78.671  73.453  1.00 26.96 ? 1135 GLN   B C     1 
ATOM   17427 O  O     . GLN   B 1  1137 ? 19.312  78.723  74.303  1.00 27.17 ? 1135 GLN   B O     1 
ATOM   17428 C  CB    . GLN   B 1  1137 ? 22.468  77.881  74.215  1.00 27.64 ? 1135 GLN   B CB    1 
ATOM   17429 C  CG    . GLN   B 1  1137 ? 23.331  76.691  74.585  1.00 26.49 ? 1135 GLN   B CG    1 
ATOM   17430 C  CD    . GLN   B 1  1137 ? 24.309  76.297  73.491  1.00 22.55 ? 1135 GLN   B CD    1 
ATOM   17431 O  OE1   . GLN   B 1  1137 ? 24.203  76.736  72.349  1.00 24.43 ? 1135 GLN   B OE1   1 
ATOM   17432 N  NE2   . GLN   B 1  1137 ? 25.275  75.464  73.848  1.00 26.87 ? 1135 GLN   B NE2   1 
ATOM   17433 N  N     . ALA   B 1  1138 ? 20.341  79.600  72.501  1.00 23.86 ? 1136 ALA   B N     1 
ATOM   17434 C  CA    . ALA   B 1  1138 ? 19.443  80.751  72.464  1.00 27.57 ? 1136 ALA   B CA    1 
ATOM   17435 C  C     . ALA   B 1  1138 ? 18.006  80.347  72.174  1.00 29.90 ? 1136 ALA   B C     1 
ATOM   17436 O  O     . ALA   B 1  1138 ? 17.086  81.116  72.467  1.00 31.16 ? 1136 ALA   B O     1 
ATOM   17437 C  CB    . ALA   B 1  1138 ? 19.907  81.763  71.417  1.00 28.93 ? 1136 ALA   B CB    1 
ATOM   17438 N  N     . SER   B 1  1139 ? 17.799  79.161  71.607  1.00 28.42 ? 1137 SER   B N     1 
ATOM   17439 C  CA    . SER   B 1  1139 ? 16.459  78.686  71.292  1.00 25.98 ? 1137 SER   B CA    1 
ATOM   17440 C  C     . SER   B 1  1139 ? 15.631  78.410  72.538  1.00 30.10 ? 1137 SER   B C     1 
ATOM   17441 O  O     . SER   B 1  1139 ? 14.398  78.379  72.450  1.00 28.48 ? 1137 SER   B O     1 
ATOM   17442 C  CB    . SER   B 1  1139 ? 16.557  77.416  70.455  1.00 24.27 ? 1137 SER   B CB    1 
ATOM   17443 O  OG    . SER   B 1  1139 ? 17.034  77.703  69.155  1.00 27.51 ? 1137 SER   B OG    1 
ATOM   17444 N  N     . LEU   B 1  1140 ? 16.274  78.194  73.685  1.00 26.66 ? 1138 LEU   B N     1 
ATOM   17445 C  CA    . LEU   B 1  1140 ? 15.578  77.960  74.942  1.00 27.90 ? 1138 LEU   B CA    1 
ATOM   17446 C  C     . LEU   B 1  1140 ? 15.590  79.178  75.856  1.00 32.75 ? 1138 LEU   B C     1 
ATOM   17447 O  O     . LEU   B 1  1140 ? 15.424  79.033  77.071  1.00 32.32 ? 1138 LEU   B O     1 
ATOM   17448 C  CB    . LEU   B 1  1140 ? 16.136  76.726  75.655  1.00 27.41 ? 1138 LEU   B CB    1 
ATOM   17449 C  CG    . LEU   B 1  1140 ? 15.987  75.415  74.883  1.00 28.17 ? 1138 LEU   B CG    1 
ATOM   17450 C  CD1   . LEU   B 1  1140 ? 16.421  74.219  75.722  1.00 26.41 ? 1138 LEU   B CD1   1 
ATOM   17451 C  CD2   . LEU   B 1  1140 ? 14.549  75.259  74.401  1.00 33.64 ? 1138 LEU   B CD2   1 
ATOM   17452 N  N     . LYS   B 1  1141 ? 15.781  80.374  75.300  1.00 35.67 ? 1139 LYS   B N     1 
ATOM   17453 C  CA    . LYS   B 1  1141 ? 15.716  81.585  76.109  1.00 37.29 ? 1139 LYS   B CA    1 
ATOM   17454 C  C     . LYS   B 1  1141 ? 14.324  81.727  76.716  1.00 37.18 ? 1139 LYS   B C     1 
ATOM   17455 O  O     . LYS   B 1  1141 ? 13.314  81.516  76.038  1.00 36.19 ? 1139 LYS   B O     1 
ATOM   17456 C  CB    . LYS   B 1  1141 ? 16.036  82.808  75.246  1.00 35.30 ? 1139 LYS   B CB    1 
ATOM   17457 N  N     . ASN   B 1  1142 ? 14.279  82.067  78.005  1.00 34.61 ? 1140 ASN   B N     1 
ATOM   17458 C  CA    . ASN   B 1  1142 ? 13.044  82.315  78.745  1.00 34.89 ? 1140 ASN   B CA    1 
ATOM   17459 C  C     . ASN   B 1  1142 ? 12.198  81.061  78.943  1.00 35.14 ? 1140 ASN   B C     1 
ATOM   17460 O  O     . ASN   B 1  1142 ? 10.977  81.153  79.114  1.00 34.32 ? 1140 ASN   B O     1 
ATOM   17461 C  CB    . ASN   B 1  1142 ? 12.214  83.455  78.140  1.00 39.56 ? 1140 ASN   B CB    1 
ATOM   17462 C  CG    . ASN   B 1  1142 ? 13.036  84.707  77.888  1.00 48.90 ? 1140 ASN   B CG    1 
ATOM   17463 O  OD1   . ASN   B 1  1142 ? 13.805  85.142  78.746  1.00 48.36 ? 1140 ASN   B OD1   1 
ATOM   17464 N  ND2   . ASN   B 1  1142 ? 12.884  85.285  76.704  1.00 51.58 ? 1140 ASN   B ND2   1 
ATOM   17465 N  N     . LEU   B 1  1143 ? 12.819  79.888  78.921  1.00 33.57 ? 1141 LEU   B N     1 
ATOM   17466 C  CA    . LEU   B 1  1143 ? 12.083  78.659  79.157  1.00 31.16 ? 1141 LEU   B CA    1 
ATOM   17467 C  C     . LEU   B 1  1143 ? 11.516  78.674  80.574  1.00 32.48 ? 1141 LEU   B C     1 
ATOM   17468 O  O     . LEU   B 1  1143 ? 12.194  79.120  81.505  1.00 36.96 ? 1141 LEU   B O     1 
ATOM   17469 C  CB    . LEU   B 1  1143 ? 13.036  77.472  79.002  1.00 28.23 ? 1141 LEU   B CB    1 
ATOM   17470 C  CG    . LEU   B 1  1143 ? 12.489  76.056  78.875  1.00 30.23 ? 1141 LEU   B CG    1 
ATOM   17471 C  CD1   . LEU   B 1  1143 ? 11.762  75.862  77.553  1.00 27.00 ? 1141 LEU   B CD1   1 
ATOM   17472 C  CD2   . LEU   B 1  1143 ? 13.625  75.062  79.018  1.00 27.19 ? 1141 LEU   B CD2   1 
ATOM   17473 N  N     . PRO   B 1  1144 ? 10.285  78.207  80.774  1.00 32.73 ? 1142 PRO   B N     1 
ATOM   17474 C  CA    . PRO   B 1  1144 ? 9.754   78.102  82.139  1.00 34.96 ? 1142 PRO   B CA    1 
ATOM   17475 C  C     . PRO   B 1  1144 ? 10.649  77.223  83.001  1.00 31.01 ? 1142 PRO   B C     1 
ATOM   17476 O  O     . PRO   B 1  1144 ? 11.204  76.227  82.535  1.00 26.90 ? 1142 PRO   B O     1 
ATOM   17477 C  CB    . PRO   B 1  1144 ? 8.379   77.451  81.935  1.00 35.20 ? 1142 PRO   B CB    1 
ATOM   17478 C  CG    . PRO   B 1  1144 ? 8.043   77.676  80.494  1.00 34.31 ? 1142 PRO   B CG    1 
ATOM   17479 C  CD    . PRO   B 1  1144 ? 9.352   77.673  79.768  1.00 30.64 ? 1142 PRO   B CD    1 
ATOM   17480 N  N     . GLN   B 1  1145 ? 10.778  77.600  84.278  1.00 31.05 ? 1143 GLN   B N     1 
ATOM   17481 C  CA    . GLN   B 1  1145 ? 11.626  76.850  85.201  1.00 28.98 ? 1143 GLN   B CA    1 
ATOM   17482 C  C     . GLN   B 1  1145 ? 11.170  75.404  85.343  1.00 27.70 ? 1143 GLN   B C     1 
ATOM   17483 O  O     . GLN   B 1  1145 ? 11.994  74.515  85.583  1.00 27.35 ? 1143 GLN   B O     1 
ATOM   17484 C  CB    . GLN   B 1  1145 ? 11.653  77.531  86.572  1.00 32.63 ? 1143 GLN   B CB    1 
ATOM   17485 N  N     . THR   B 1  1146 ? 9.868   75.142  85.213  1.00 29.08 ? 1144 THR   B N     1 
ATOM   17486 C  CA    . THR   B 1  1146 ? 9.415   73.757  85.246  1.00 29.11 ? 1144 THR   B CA    1 
ATOM   17487 C  C     . THR   B 1  1146 ? 10.069  72.954  84.134  1.00 28.72 ? 1144 THR   B C     1 
ATOM   17488 O  O     . THR   B 1  1146 ? 10.495  71.810  84.345  1.00 30.88 ? 1144 THR   B O     1 
ATOM   17489 C  CB    . THR   B 1  1146 ? 7.895   73.690  85.126  1.00 30.29 ? 1144 THR   B CB    1 
ATOM   17490 O  OG1   . THR   B 1  1146 ? 7.459   74.577  84.088  1.00 37.99 ? 1144 THR   B OG1   1 
ATOM   17491 C  CG2   . THR   B 1  1146 ? 7.243   74.087  86.443  1.00 39.36 ? 1144 THR   B CG2   1 
ATOM   17492 N  N     . VAL   B 1  1147 ? 10.185  73.547  82.950  1.00 25.63 ? 1145 VAL   B N     1 
ATOM   17493 C  CA    . VAL   B 1  1147 ? 10.847  72.843  81.861  1.00 22.15 ? 1145 VAL   B CA    1 
ATOM   17494 C  C     . VAL   B 1  1147 ? 12.354  72.887  82.039  1.00 24.36 ? 1145 VAL   B C     1 
ATOM   17495 O  O     . VAL   B 1  1147 ? 13.049  71.899  81.785  1.00 25.40 ? 1145 VAL   B O     1 
ATOM   17496 C  CB    . VAL   B 1  1147 ? 10.412  73.403  80.497  1.00 21.65 ? 1145 VAL   B CB    1 
ATOM   17497 C  CG1   . VAL   B 1  1147 ? 10.949  72.514  79.380  1.00 24.61 ? 1145 VAL   B CG1   1 
ATOM   17498 C  CG2   . VAL   B 1  1147 ? 8.894   73.532  80.427  1.00 22.51 ? 1145 VAL   B CG2   1 
ATOM   17499 N  N     . GLY   B 1  1148 ? 12.880  74.029  82.484  1.00 24.28 ? 1146 GLY   B N     1 
ATOM   17500 C  CA    . GLY   B 1  1148 ? 14.319  74.157  82.642  1.00 26.81 ? 1146 GLY   B CA    1 
ATOM   17501 C  C     . GLY   B 1  1148 ? 14.912  73.142  83.595  1.00 25.22 ? 1146 GLY   B C     1 
ATOM   17502 O  O     . GLY   B 1  1148 ? 16.037  72.675  83.386  1.00 25.75 ? 1146 GLY   B O     1 
ATOM   17503 N  N     . LEU   B 1  1149 ? 14.174  72.780  84.649  1.00 25.16 ? 1147 LEU   B N     1 
ATOM   17504 C  CA    . LEU   B 1  1149 ? 14.662  71.799  85.609  1.00 28.42 ? 1147 LEU   B CA    1 
ATOM   17505 C  C     . LEU   B 1  1149 ? 14.894  70.439  84.969  1.00 27.45 ? 1147 LEU   B C     1 
ATOM   17506 O  O     . LEU   B 1  1149 ? 15.639  69.625  85.526  1.00 28.52 ? 1147 LEU   B O     1 
ATOM   17507 C  CB    . LEU   B 1  1149 ? 13.678  71.662  86.776  1.00 35.03 ? 1147 LEU   B CB    1 
ATOM   17508 N  N     . ARG   B 1  1150 ? 14.270  70.173  83.824  1.00 23.88 ? 1148 ARG   B N     1 
ATOM   17509 C  CA    . ARG   B 1  1150 ? 14.452  68.917  83.106  1.00 23.42 ? 1148 ARG   B CA    1 
ATOM   17510 C  C     . ARG   B 1  1150 ? 15.511  69.011  82.026  1.00 20.97 ? 1148 ARG   B C     1 
ATOM   17511 O  O     . ARG   B 1  1150 ? 15.788  68.008  81.361  1.00 21.28 ? 1148 ARG   B O     1 
ATOM   17512 C  CB    . ARG   B 1  1150 ? 13.150  68.508  82.430  1.00 22.96 ? 1148 ARG   B CB    1 
ATOM   17513 C  CG    . ARG   B 1  1150 ? 12.069  68.031  83.370  1.00 25.66 ? 1148 ARG   B CG    1 
ATOM   17514 C  CD    . ARG   B 1  1150 ? 11.727  66.596  83.070  1.00 26.03 ? 1148 ARG   B CD    1 
ATOM   17515 N  NE    . ARG   B 1  1150 ? 10.485  66.208  83.716  1.00 25.72 ? 1148 ARG   B NE    1 
ATOM   17516 C  CZ    . ARG   B 1  1150 ? 9.411   65.769  83.078  1.00 24.68 ? 1148 ARG   B CZ    1 
ATOM   17517 N  NH1   . ARG   B 1  1150 ? 9.418   65.555  81.769  1.00 19.80 ? 1148 ARG   B NH1   1 
ATOM   17518 N  NH2   . ARG   B 1  1150 ? 8.307   65.520  83.775  1.00 21.81 ? 1148 ARG   B NH2   1 
ATOM   17519 N  N     . VAL   B 1  1151 ? 16.089  70.185  81.817  1.00 22.07 ? 1149 VAL   B N     1 
ATOM   17520 C  CA    . VAL   B 1  1151 ? 16.960  70.437  80.677  1.00 20.01 ? 1149 VAL   B CA    1 
ATOM   17521 C  C     . VAL   B 1  1151 ? 18.361  70.710  81.186  1.00 23.48 ? 1149 VAL   B C     1 
ATOM   17522 O  O     . VAL   B 1  1151 ? 18.553  71.549  82.069  1.00 23.48 ? 1149 VAL   B O     1 
ATOM   17523 C  CB    . VAL   B 1  1151 ? 16.471  71.627  79.840  1.00 21.89 ? 1149 VAL   B CB    1 
ATOM   17524 C  CG1   . VAL   B 1  1151 ? 17.530  72.010  78.798  1.00 25.60 ? 1149 VAL   B CG1   1 
ATOM   17525 C  CG2   . VAL   B 1  1151 ? 15.156  71.295  79.168  1.00 25.13 ? 1149 VAL   B CG2   1 
ATOM   17526 N  N     . SER   B 1  1152 ? 19.332  70.005  80.631  1.00 21.95 ? 1150 SER   B N     1 
ATOM   17527 C  CA    . SER   B 1  1152 ? 20.722  70.371  80.806  1.00 22.80 ? 1150 SER   B CA    1 
ATOM   17528 C  C     . SER   B 1  1152 ? 21.358  70.409  79.428  1.00 22.82 ? 1150 SER   B C     1 
ATOM   17529 O  O     . SER   B 1  1152 ? 20.820  69.864  78.458  1.00 21.43 ? 1150 SER   B O     1 
ATOM   17530 C  CB    . SER   B 1  1152 ? 21.454  69.402  81.742  1.00 22.49 ? 1150 SER   B CB    1 
ATOM   17531 O  OG    . SER   B 1  1152 ? 21.482  68.098  81.196  1.00 28.01 ? 1150 SER   B OG    1 
ATOM   17532 N  N     . TRP   B 1  1153 ? 22.488  71.094  79.342  1.00 22.46 ? 1151 TRP   B N     1 
ATOM   17533 C  CA    . TRP   B 1  1153 ? 23.278  71.147  78.129  1.00 20.85 ? 1151 TRP   B CA    1 
ATOM   17534 C  C     . TRP   B 1  1153 ? 24.572  70.398  78.381  1.00 22.70 ? 1151 TRP   B C     1 
ATOM   17535 O  O     . TRP   B 1  1153 ? 25.181  70.538  79.445  1.00 25.40 ? 1151 TRP   B O     1 
ATOM   17536 C  CB    . TRP   B 1  1153 ? 23.578  72.592  77.757  1.00 23.18 ? 1151 TRP   B CB    1 
ATOM   17537 C  CG    . TRP   B 1  1153 ? 22.349  73.287  77.288  1.00 22.27 ? 1151 TRP   B CG    1 
ATOM   17538 C  CD1   . TRP   B 1  1153 ? 21.408  73.907  78.062  1.00 26.59 ? 1151 TRP   B CD1   1 
ATOM   17539 C  CD2   . TRP   B 1  1153 ? 21.913  73.417  75.939  1.00 21.59 ? 1151 TRP   B CD2   1 
ATOM   17540 N  NE1   . TRP   B 1  1153 ? 20.414  74.425  77.268  1.00 23.75 ? 1151 TRP   B NE1   1 
ATOM   17541 C  CE2   . TRP   B 1  1153 ? 20.695  74.134  75.959  1.00 21.69 ? 1151 TRP   B CE2   1 
ATOM   17542 C  CE3   . TRP   B 1  1153 ? 22.427  72.996  74.708  1.00 22.38 ? 1151 TRP   B CE3   1 
ATOM   17543 C  CZ2   . TRP   B 1  1153 ? 20.000  74.447  74.799  1.00 22.60 ? 1151 TRP   B CZ2   1 
ATOM   17544 C  CZ3   . TRP   B 1  1153 ? 21.738  73.310  73.566  1.00 21.31 ? 1151 TRP   B CZ3   1 
ATOM   17545 C  CH2   . TRP   B 1  1153 ? 20.530  74.027  73.615  1.00 22.54 ? 1151 TRP   B CH2   1 
ATOM   17546 N  N     . SER   B 1  1154 ? 24.971  69.574  77.422  1.00 18.10 ? 1152 SER   B N     1 
ATOM   17547 C  CA    . SER   B 1  1154 ? 26.150  68.740  77.607  1.00 20.59 ? 1152 SER   B CA    1 
ATOM   17548 C  C     . SER   B 1  1154 ? 27.201  69.107  76.577  1.00 19.07 ? 1152 SER   B C     1 
ATOM   17549 O  O     . SER   B 1  1154 ? 26.935  69.089  75.371  1.00 20.23 ? 1152 SER   B O     1 
ATOM   17550 C  CB    . SER   B 1  1154 ? 25.814  67.254  77.503  1.00 22.19 ? 1152 SER   B CB    1 
ATOM   17551 O  OG    . SER   B 1  1154 ? 27.019  66.511  77.575  1.00 20.29 ? 1152 SER   B OG    1 
ATOM   17552 N  N     . LYS   B 1  1155 ? 28.394  69.444  77.064  1.00 18.65 ? 1153 LYS   B N     1 
ATOM   17553 C  CA    . LYS   B 1  1155 ? 29.580  69.578  76.234  1.00 24.31 ? 1153 LYS   B CA    1 
ATOM   17554 C  C     . LYS   B 1  1155 ? 30.463  68.342  76.315  1.00 22.94 ? 1153 LYS   B C     1 
ATOM   17555 O  O     . LYS   B 1  1155 ? 31.593  68.358  75.815  1.00 25.10 ? 1153 LYS   B O     1 
ATOM   17556 C  CB    . LYS   B 1  1155 ? 30.377  70.817  76.651  1.00 26.45 ? 1153 LYS   B CB    1 
ATOM   17557 N  N     . ASP   B 1  1156 ? 29.975  67.276  76.940  1.00 18.55 ? 1154 ASP   B N     1 
ATOM   17558 C  CA    . ASP   B 1  1156 ? 30.794  66.090  77.170  1.00 17.26 ? 1154 ASP   B CA    1 
ATOM   17559 C  C     . ASP   B 1  1156 ? 29.806  64.950  77.430  1.00 17.47 ? 1154 ASP   B C     1 
ATOM   17560 O  O     . ASP   B 1  1156 ? 29.445  64.685  78.574  1.00 18.63 ? 1154 ASP   B O     1 
ATOM   17561 C  CB    . ASP   B 1  1156 ? 31.700  66.311  78.359  1.00 18.70 ? 1154 ASP   B CB    1 
ATOM   17562 C  CG    . ASP   B 1  1156 ? 32.728  65.215  78.516  1.00 18.92 ? 1154 ASP   B CG    1 
ATOM   17563 O  OD1   . ASP   B 1  1156 ? 32.462  64.074  78.098  1.00 18.30 ? 1154 ASP   B OD1   1 
ATOM   17564 O  OD2   . ASP   B 1  1156 ? 33.798  65.515  79.064  1.00 21.34 ? 1154 ASP   B OD2   1 
ATOM   17565 N  N     . TRP   B 1  1157 ? 29.381  64.291  76.354  1.00 15.54 ? 1155 TRP   B N     1 
ATOM   17566 C  CA    . TRP   B 1  1157 ? 28.307  63.310  76.495  1.00 16.35 ? 1155 TRP   B CA    1 
ATOM   17567 C  C     . TRP   B 1  1157 ? 28.721  62.172  77.406  1.00 18.44 ? 1155 TRP   B C     1 
ATOM   17568 O  O     . TRP   B 1  1157 ? 27.922  61.686  78.210  1.00 19.60 ? 1155 TRP   B O     1 
ATOM   17569 C  CB    . TRP   B 1  1157 ? 27.911  62.734  75.145  1.00 18.29 ? 1155 TRP   B CB    1 
ATOM   17570 C  CG    . TRP   B 1  1157 ? 27.478  63.719  74.131  1.00 16.72 ? 1155 TRP   B CG    1 
ATOM   17571 C  CD1   . TRP   B 1  1157 ? 27.240  65.050  74.307  1.00 17.20 ? 1155 TRP   B CD1   1 
ATOM   17572 C  CD2   . TRP   B 1  1157 ? 27.234  63.440  72.753  1.00 17.17 ? 1155 TRP   B CD2   1 
ATOM   17573 N  NE1   . TRP   B 1  1157 ? 26.868  65.620  73.113  1.00 18.70 ? 1155 TRP   B NE1   1 
ATOM   17574 C  CE2   . TRP   B 1  1157 ? 26.857  64.649  72.141  1.00 18.03 ? 1155 TRP   B CE2   1 
ATOM   17575 C  CE3   . TRP   B 1  1157 ? 27.313  62.277  71.970  1.00 18.71 ? 1155 TRP   B CE3   1 
ATOM   17576 C  CZ2   . TRP   B 1  1157 ? 26.557  64.733  70.785  1.00 20.82 ? 1155 TRP   B CZ2   1 
ATOM   17577 C  CZ3   . TRP   B 1  1157 ? 27.007  62.356  70.634  1.00 19.34 ? 1155 TRP   B CZ3   1 
ATOM   17578 C  CH2   . TRP   B 1  1157 ? 26.637  63.579  70.047  1.00 19.77 ? 1155 TRP   B CH2   1 
ATOM   17579 N  N     . ALA   B 1  1158 ? 29.966  61.724  77.289  1.00 17.68 ? 1156 ALA   B N     1 
ATOM   17580 C  CA    . ALA   B 1  1158 ? 30.386  60.571  78.066  1.00 18.11 ? 1156 ALA   B CA    1 
ATOM   17581 C  C     . ALA   B 1  1158 ? 30.482  60.893  79.545  1.00 20.90 ? 1156 ALA   B C     1 
ATOM   17582 O  O     . ALA   B 1  1158 ? 30.255  60.014  80.378  1.00 25.11 ? 1156 ALA   B O     1 
ATOM   17583 C  CB    . ALA   B 1  1158 ? 31.721  60.039  77.546  1.00 17.57 ? 1156 ALA   B CB    1 
ATOM   17584 N  N     . ALA   B 1  1159 ? 30.839  62.130  79.894  1.00 18.39 ? 1157 ALA   B N     1 
ATOM   17585 C  CA    . ALA   B 1  1159 ? 30.916  62.495  81.300  1.00 18.58 ? 1157 ALA   B CA    1 
ATOM   17586 C  C     . ALA   B 1  1159 ? 29.542  62.749  81.904  1.00 22.33 ? 1157 ALA   B C     1 
ATOM   17587 O  O     . ALA   B 1  1159 ? 29.369  62.582  83.114  1.00 22.41 ? 1157 ALA   B O     1 
ATOM   17588 C  CB    . ALA   B 1  1159 ? 31.807  63.721  81.486  1.00 21.26 ? 1157 ALA   B CB    1 
ATOM   17589 N  N     . ASP   B 1  1160 ? 28.563  63.135  81.088  1.00 21.95 ? 1158 ASP   B N     1 
ATOM   17590 C  CA    . ASP   B 1  1160 ? 27.273  63.604  81.579  1.00 21.76 ? 1158 ASP   B CA    1 
ATOM   17591 C  C     . ASP   B 1  1160 ? 26.196  62.529  81.585  1.00 22.62 ? 1158 ASP   B C     1 
ATOM   17592 O  O     . ASP   B 1  1160 ? 25.052  62.820  81.959  1.00 24.55 ? 1158 ASP   B O     1 
ATOM   17593 C  CB    . ASP   B 1  1160 ? 26.818  64.810  80.758  1.00 22.13 ? 1158 ASP   B CB    1 
ATOM   17594 C  CG    . ASP   B 1  1160 ? 27.727  66.002  80.944  1.00 23.35 ? 1158 ASP   B CG    1 
ATOM   17595 O  OD1   . ASP   B 1  1160 ? 28.480  66.021  81.947  1.00 28.09 ? 1158 ASP   B OD1   1 
ATOM   17596 O  OD2   . ASP   B 1  1160 ? 27.700  66.917  80.095  1.00 24.68 ? 1158 ASP   B OD2   1 
ATOM   17597 N  N     . GLY   B 1  1161 ? 26.525  61.307  81.183  1.00 20.77 ? 1159 GLY   B N     1 
ATOM   17598 C  CA    . GLY   B 1  1161 ? 25.615  60.194  81.285  1.00 21.90 ? 1159 GLY   B CA    1 
ATOM   17599 C  C     . GLY   B 1  1161 ? 25.600  59.610  82.684  1.00 26.14 ? 1159 GLY   B C     1 
ATOM   17600 O  O     . GLY   B 1  1161 ? 26.138  60.192  83.631  1.00 28.70 ? 1159 GLY   B O     1 
ATOM   17601 N  N     . PRO   B 1  1162 ? 25.008  58.427  82.840  1.00 25.48 ? 1160 PRO   B N     1 
ATOM   17602 C  CA    . PRO   B 1  1162 ? 24.411  57.598  81.792  1.00 23.62 ? 1160 PRO   B CA    1 
ATOM   17603 C  C     . PRO   B 1  1162 ? 23.076  58.144  81.339  1.00 21.65 ? 1160 PRO   B C     1 
ATOM   17604 O  O     . PRO   B 1  1162 ? 22.273  58.695  82.090  1.00 23.45 ? 1160 PRO   B O     1 
ATOM   17605 C  CB    . PRO   B 1  1162 ? 24.269  56.228  82.472  1.00 25.47 ? 1160 PRO   B CB    1 
ATOM   17606 C  CG    . PRO   B 1  1162 ? 24.062  56.563  83.919  1.00 29.16 ? 1160 PRO   B CG    1 
ATOM   17607 C  CD    . PRO   B 1  1162 ? 24.963  57.760  84.156  1.00 28.75 ? 1160 PRO   B CD    1 
ATOM   17608 N  N     . PHE   B 1  1163 ? 22.849  58.008  80.048  1.00 17.00 ? 1161 PHE   B N     1 
ATOM   17609 C  CA    . PHE   B 1  1163 ? 21.567  58.318  79.447  1.00 17.57 ? 1161 PHE   B CA    1 
ATOM   17610 C  C     . PHE   B 1  1163 ? 20.761  57.038  79.294  1.00 17.16 ? 1161 PHE   B C     1 
ATOM   17611 O  O     . PHE   B 1  1163 ? 21.248  55.934  79.527  1.00 18.39 ? 1161 PHE   B O     1 
ATOM   17612 C  CB    . PHE   B 1  1163 ? 21.787  59.031  78.111  1.00 17.14 ? 1161 PHE   B CB    1 
ATOM   17613 C  CG    . PHE   B 1  1163 ? 22.632  60.256  78.241  1.00 17.97 ? 1161 PHE   B CG    1 
ATOM   17614 C  CD1   . PHE   B 1  1163 ? 22.193  61.331  78.989  1.00 24.53 ? 1161 PHE   B CD1   1 
ATOM   17615 C  CD2   . PHE   B 1  1163 ? 23.880  60.323  77.653  1.00 20.04 ? 1161 PHE   B CD2   1 
ATOM   17616 C  CE1   . PHE   B 1  1163 ? 22.971  62.461  79.135  1.00 24.48 ? 1161 PHE   B CE1   1 
ATOM   17617 C  CE2   . PHE   B 1  1163 ? 24.657  61.463  77.786  1.00 21.76 ? 1161 PHE   B CE2   1 
ATOM   17618 C  CZ    . PHE   B 1  1163 ? 24.204  62.527  78.525  1.00 20.56 ? 1161 PHE   B CZ    1 
ATOM   17619 N  N     . ALA   B 1  1164 ? 19.493  57.203  78.934  1.00 17.63 ? 1162 ALA   B N     1 
ATOM   17620 C  CA    . ALA   B 1  1164 ? 18.606  56.069  78.717  1.00 17.51 ? 1162 ALA   B CA    1 
ATOM   17621 C  C     . ALA   B 1  1164 ? 18.055  56.033  77.303  1.00 20.38 ? 1162 ALA   B C     1 
ATOM   17622 O  O     . ALA   B 1  1164 ? 17.125  55.267  77.031  1.00 20.85 ? 1162 ALA   B O     1 
ATOM   17623 C  CB    . ALA   B 1  1164 ? 17.465  56.077  79.736  1.00 18.53 ? 1162 ALA   B CB    1 
ATOM   17624 N  N     . GLY   B 1  1165 ? 18.609  56.832  76.408  1.00 16.48 ? 1163 GLY   B N     1 
ATOM   17625 C  CA    . GLY   B 1  1165 ? 18.184  56.868  75.027  1.00 17.25 ? 1163 GLY   B CA    1 
ATOM   17626 C  C     . GLY   B 1  1165 ? 18.733  58.129  74.398  1.00 16.20 ? 1163 GLY   B C     1 
ATOM   17627 O  O     . GLY   B 1  1165 ? 19.322  58.972  75.068  1.00 16.55 ? 1163 GLY   B O     1 
ATOM   17628 N  N     . ALA   B 1  1166 ? 18.531  58.243  73.090  1.00 16.87 ? 1164 ALA   B N     1 
ATOM   17629 C  CA    . ALA   B 1  1166 ? 19.025  59.424  72.402  1.00 14.57 ? 1164 ALA   B CA    1 
ATOM   17630 C  C     . ALA   B 1  1166 ? 18.138  59.722  71.216  1.00 16.75 ? 1164 ALA   B C     1 
ATOM   17631 O  O     . ALA   B 1  1166 ? 17.654  58.805  70.551  1.00 19.04 ? 1164 ALA   B O     1 
ATOM   17632 C  CB    . ALA   B 1  1166 ? 20.462  59.219  71.919  1.00 16.69 ? 1164 ALA   B CB    1 
ATOM   17633 N  N     . LEU   B 1  1167 ? 17.933  61.007  70.960  1.00 15.83 ? 1165 LEU   B N     1 
ATOM   17634 C  CA    . LEU   B 1  1167 ? 17.240  61.472  69.772  1.00 16.17 ? 1165 LEU   B CA    1 
ATOM   17635 C  C     . LEU   B 1  1167 ? 18.225  62.308  68.975  1.00 18.27 ? 1165 LEU   B C     1 
ATOM   17636 O  O     . LEU   B 1  1167 ? 18.871  63.201  69.530  1.00 17.96 ? 1165 LEU   B O     1 
ATOM   17637 C  CB    . LEU   B 1  1167 ? 16.034  62.328  70.150  1.00 17.24 ? 1165 LEU   B CB    1 
ATOM   17638 C  CG    . LEU   B 1  1167 ? 15.025  61.643  71.068  1.00 16.67 ? 1165 LEU   B CG    1 
ATOM   17639 C  CD1   . LEU   B 1  1167 ? 13.912  62.625  71.382  1.00 19.52 ? 1165 LEU   B CD1   1 
ATOM   17640 C  CD2   . LEU   B 1  1167 ? 14.457  60.412  70.371  1.00 18.59 ? 1165 LEU   B CD2   1 
ATOM   17641 N  N     . VAL   B 1  1168 ? 18.337  62.014  67.688  1.00 17.86 ? 1166 VAL   B N     1 
ATOM   17642 C  CA    . VAL   B 1  1168 ? 19.343  62.628  66.838  1.00 17.46 ? 1166 VAL   B CA    1 
ATOM   17643 C  C     . VAL   B 1  1168 ? 18.643  63.215  65.628  1.00 19.15 ? 1166 VAL   B C     1 
ATOM   17644 O  O     . VAL   B 1  1168 ? 17.742  62.595  65.054  1.00 18.02 ? 1166 VAL   B O     1 
ATOM   17645 C  CB    . VAL   B 1  1168 ? 20.387  61.583  66.406  1.00 17.50 ? 1166 VAL   B CB    1 
ATOM   17646 C  CG1   . VAL   B 1  1168 ? 21.451  62.214  65.488  1.00 18.96 ? 1166 VAL   B CG1   1 
ATOM   17647 C  CG2   . VAL   B 1  1168 ? 21.005  60.911  67.640  1.00 17.72 ? 1166 VAL   B CG2   1 
ATOM   17648 N  N     . GLU   B 1  1169 ? 19.048  64.415  65.251  1.00 17.00 ? 1167 GLU   B N     1 
ATOM   17649 C  CA    . GLU   B 1  1169 ? 18.578  65.064  64.039  1.00 18.07 ? 1167 GLU   B CA    1 
ATOM   17650 C  C     . GLU   B 1  1169 ? 19.784  65.356  63.159  1.00 18.18 ? 1167 GLU   B C     1 
ATOM   17651 O  O     . GLU   B 1  1169 ? 20.809  65.833  63.646  1.00 22.24 ? 1167 GLU   B O     1 
ATOM   17652 C  CB    . GLU   B 1  1169 ? 17.896  66.386  64.373  1.00 18.38 ? 1167 GLU   B CB    1 
ATOM   17653 C  CG    . GLU   B 1  1169 ? 17.437  67.167  63.157  1.00 19.57 ? 1167 GLU   B CG    1 
ATOM   17654 C  CD    . GLU   B 1  1169 ? 17.053  68.592  63.490  1.00 19.79 ? 1167 GLU   B CD    1 
ATOM   17655 O  OE1   . GLU   B 1  1169 ? 17.301  69.043  64.631  1.00 19.76 ? 1167 GLU   B OE1   1 
ATOM   17656 O  OE2   . GLU   B 1  1169 ? 16.487  69.264  62.609  1.00 23.48 ? 1167 GLU   B OE2   1 
ATOM   17657 N  N     . GLY   B 1  1170 ? 19.666  65.062  61.876  1.00 19.25 ? 1168 GLY   B N     1 
ATOM   17658 C  CA    . GLY   B 1  1170 ? 20.742  65.387  60.961  1.00 20.54 ? 1168 GLY   B CA    1 
ATOM   17659 C  C     . GLY   B 1  1170 ? 20.607  64.623  59.671  1.00 24.58 ? 1168 GLY   B C     1 
ATOM   17660 O  O     . GLY   B 1  1170 ? 19.726  63.779  59.504  1.00 21.97 ? 1168 GLY   B O     1 
ATOM   17661 N  N     . ASP   B 1  1171 ? 21.504  64.943  58.745  1.00 24.32 ? 1169 ASP   B N     1 
ATOM   17662 C  CA    . ASP   B 1  1171 ? 21.557  64.173  57.516  1.00 23.59 ? 1169 ASP   B CA    1 
ATOM   17663 C  C     . ASP   B 1  1171 ? 22.251  62.838  57.776  1.00 22.06 ? 1169 ASP   B C     1 
ATOM   17664 O  O     . ASP   B 1  1171 ? 22.725  62.557  58.880  1.00 22.02 ? 1169 ASP   B O     1 
ATOM   17665 C  CB    . ASP   B 1  1171 ? 22.160  64.989  56.369  1.00 23.53 ? 1169 ASP   B CB    1 
ATOM   17666 C  CG    . ASP   B 1  1171 ? 23.624  65.342  56.582  1.00 28.84 ? 1169 ASP   B CG    1 
ATOM   17667 O  OD1   . ASP   B 1  1171 ? 24.256  64.880  57.556  1.00 24.46 ? 1169 ASP   B OD1   1 
ATOM   17668 O  OD2   . ASP   B 1  1171 ? 24.155  66.107  55.748  1.00 33.92 ? 1169 ASP   B OD2   1 
ATOM   17669 N  N     . ALA   B 1  1172 ? 22.311  62.002  56.739  1.00 24.14 ? 1170 ALA   B N     1 
ATOM   17670 C  CA    . ALA   B 1  1172 ? 22.787  60.635  56.916  1.00 25.57 ? 1170 ALA   B CA    1 
ATOM   17671 C  C     . ALA   B 1  1172 ? 24.174  60.601  57.546  1.00 23.31 ? 1170 ALA   B C     1 
ATOM   17672 O  O     . ALA   B 1  1172 ? 24.422  59.838  58.487  1.00 23.35 ? 1170 ALA   B O     1 
ATOM   17673 C  CB    . ALA   B 1  1172 ? 22.779  59.899  55.576  1.00 26.16 ? 1170 ALA   B CB    1 
ATOM   17674 N  N     . GLU   B 1  1173 ? 25.099  61.425  57.048  1.00 25.14 ? 1171 GLU   B N     1 
ATOM   17675 C  CA    . GLU   B 1  1173 ? 26.448  61.337  57.590  1.00 23.57 ? 1171 GLU   B CA    1 
ATOM   17676 C  C     . GLU   B 1  1173 ? 26.535  61.899  59.004  1.00 22.02 ? 1171 GLU   B C     1 
ATOM   17677 O  O     . GLU   B 1  1173 ? 27.331  61.408  59.811  1.00 22.41 ? 1171 GLU   B O     1 
ATOM   17678 C  CB    . GLU   B 1  1173 ? 27.466  61.945  56.627  1.00 34.82 ? 1171 GLU   B CB    1 
ATOM   17679 C  CG    . GLU   B 1  1173 ? 27.631  61.107  55.351  1.00 38.50 ? 1171 GLU   B CG    1 
ATOM   17680 C  CD    . GLU   B 1  1173 ? 28.011  59.646  55.629  1.00 39.45 ? 1171 GLU   B CD    1 
ATOM   17681 O  OE1   . GLU   B 1  1173 ? 28.890  59.397  56.482  1.00 37.20 ? 1171 GLU   B OE1   1 
ATOM   17682 O  OE2   . GLU   B 1  1173 ? 27.428  58.741  54.990  1.00 41.79 ? 1171 GLU   B OE2   1 
ATOM   17683 N  N     . ARG   B 1  1174 ? 25.716  62.906  59.327  1.00 22.43 ? 1172 ARG   B N     1 
ATOM   17684 C  CA    . ARG   B 1  1174 ? 25.618  63.367  60.710  1.00 21.24 ? 1172 ARG   B CA    1 
ATOM   17685 C  C     . ARG   B 1  1174 ? 25.091  62.252  61.604  1.00 19.58 ? 1172 ARG   B C     1 
ATOM   17686 O  O     . ARG   B 1  1174 ? 25.654  61.973  62.667  1.00 20.59 ? 1172 ARG   B O     1 
ATOM   17687 C  CB    . ARG   B 1  1174 ? 24.709  64.596  60.787  1.00 22.28 ? 1172 ARG   B CB    1 
ATOM   17688 C  CG    . ARG   B 1  1174 ? 24.463  65.122  62.200  1.00 21.84 ? 1172 ARG   B CG    1 
ATOM   17689 C  CD    . ARG   B 1  1174 ? 25.759  65.539  62.872  1.00 26.35 ? 1172 ARG   B CD    1 
ATOM   17690 N  NE    . ARG   B 1  1174 ? 25.519  66.066  64.210  1.00 24.51 ? 1172 ARG   B NE    1 
ATOM   17691 C  CZ    . ARG   B 1  1174 ? 26.439  66.138  65.161  1.00 23.09 ? 1172 ARG   B CZ    1 
ATOM   17692 N  NH1   . ARG   B 1  1174 ? 27.683  65.735  64.952  1.00 24.31 ? 1172 ARG   B NH1   1 
ATOM   17693 N  NH2   . ARG   B 1  1174 ? 26.101  66.603  66.359  1.00 22.80 ? 1172 ARG   B NH2   1 
ATOM   17694 N  N     . ILE   B 1  1175 ? 24.019  61.590  61.169  1.00 19.65 ? 1173 ILE   B N     1 
ATOM   17695 C  CA    . ILE   B 1  1175 ? 23.469  60.474  61.938  1.00 18.49 ? 1173 ILE   B CA    1 
ATOM   17696 C  C     . ILE   B 1  1175 ? 24.529  59.408  62.181  1.00 19.23 ? 1173 ILE   B C     1 
ATOM   17697 O  O     . ILE   B 1  1175 ? 24.701  58.924  63.306  1.00 19.72 ? 1173 ILE   B O     1 
ATOM   17698 C  CB    . ILE   B 1  1175 ? 22.228  59.905  61.236  1.00 18.52 ? 1173 ILE   B CB    1 
ATOM   17699 C  CG1   . ILE   B 1  1175 ? 21.080  60.917  61.324  1.00 20.86 ? 1173 ILE   B CG1   1 
ATOM   17700 C  CG2   . ILE   B 1  1175 ? 21.844  58.556  61.837  1.00 20.12 ? 1173 ILE   B CG2   1 
ATOM   17701 C  CD1   . ILE   B 1  1175 ? 19.914  60.603  60.422  1.00 20.99 ? 1173 ILE   B CD1   1 
ATOM   17702 N  N     . ARG   B 1  1176 ? 25.269  59.032  61.131  1.00 20.98 ? 1174 ARG   B N     1 
ATOM   17703 C  CA    . ARG   B 1  1176 ? 26.302  58.014  61.295  1.00 20.06 ? 1174 ARG   B CA    1 
ATOM   17704 C  C     . ARG   B 1  1176 ? 27.360  58.457  62.295  1.00 19.62 ? 1174 ARG   B C     1 
ATOM   17705 O  O     . ARG   B 1  1176 ? 27.774  57.685  63.165  1.00 19.56 ? 1174 ARG   B O     1 
ATOM   17706 C  CB    . ARG   B 1  1176 ? 26.948  57.690  59.948  1.00 21.17 ? 1174 ARG   B CB    1 
ATOM   17707 C  CG    . ARG   B 1  1176 ? 27.869  56.480  60.015  1.00 25.59 ? 1174 ARG   B CG    1 
ATOM   17708 C  CD    . ARG   B 1  1176 ? 28.834  56.399  58.826  1.00 28.06 ? 1174 ARG   B CD    1 
ATOM   17709 N  NE    . ARG   B 1  1176 ? 28.174  56.598  57.541  1.00 32.25 ? 1174 ARG   B NE    1 
ATOM   17710 C  CZ    . ARG   B 1  1176 ? 27.668  55.628  56.791  1.00 34.36 ? 1174 ARG   B CZ    1 
ATOM   17711 N  NH1   . ARG   B 1  1176 ? 27.698  54.364  57.181  1.00 31.82 ? 1174 ARG   B NH1   1 
ATOM   17712 N  NH2   . ARG   B 1  1176 ? 27.126  55.932  55.614  1.00 35.33 ? 1174 ARG   B NH2   1 
ATOM   17713 N  N     . ALA   B 1  1177 ? 27.813  59.707  62.182  1.00 20.37 ? 1175 ALA   B N     1 
ATOM   17714 C  CA    . ALA   B 1  1177 ? 28.843  60.197  63.085  1.00 21.42 ? 1175 ALA   B CA    1 
ATOM   17715 C  C     . ALA   B 1  1177 ? 28.348  60.215  64.522  1.00 19.56 ? 1175 ALA   B C     1 
ATOM   17716 O  O     . ALA   B 1  1177 ? 29.068  59.820  65.444  1.00 20.33 ? 1175 ALA   B O     1 
ATOM   17717 C  CB    . ALA   B 1  1177 ? 29.267  61.601  62.663  1.00 22.94 ? 1175 ALA   B CB    1 
ATOM   17718 N  N     . VAL   B 1  1178 ? 27.116  60.669  64.729  1.00 19.09 ? 1176 VAL   B N     1 
ATOM   17719 C  CA    . VAL   B 1  1178 ? 26.574  60.711  66.081  1.00 17.85 ? 1176 VAL   B CA    1 
ATOM   17720 C  C     . VAL   B 1  1178 ? 26.366  59.301  66.610  1.00 18.58 ? 1176 VAL   B C     1 
ATOM   17721 O  O     . VAL   B 1  1178 ? 26.649  59.005  67.773  1.00 18.65 ? 1176 VAL   B O     1 
ATOM   17722 C  CB    . VAL   B 1  1178 ? 25.272  61.523  66.082  1.00 19.19 ? 1176 VAL   B CB    1 
ATOM   17723 C  CG1   . VAL   B 1  1178 ? 24.567  61.397  67.439  1.00 20.21 ? 1176 VAL   B CG1   1 
ATOM   17724 C  CG2   . VAL   B 1  1178 ? 25.563  62.975  65.766  1.00 22.88 ? 1176 VAL   B CG2   1 
ATOM   17725 N  N     . ASN   B 1  1179 ? 25.868  58.408  65.760  1.00 17.90 ? 1177 ASN   B N     1 
ATOM   17726 C  CA    . ASN   B 1  1179 ? 25.631  57.039  66.193  1.00 19.37 ? 1177 ASN   B CA    1 
ATOM   17727 C  C     . ASN   B 1  1179 ? 26.932  56.371  66.615  1.00 19.43 ? 1177 ASN   B C     1 
ATOM   17728 O  O     . ASN   B 1  1179 ? 26.980  55.655  67.622  1.00 19.98 ? 1177 ASN   B O     1 
ATOM   17729 C  CB    . ASN   B 1  1179 ? 24.955  56.277  65.054  1.00 19.19 ? 1177 ASN   B CB    1 
ATOM   17730 C  CG    . ASN   B 1  1179 ? 24.227  55.035  65.526  1.00 22.68 ? 1177 ASN   B CG    1 
ATOM   17731 O  OD1   . ASN   B 1  1179 ? 23.793  54.936  66.684  1.00 23.39 ? 1177 ASN   B OD1   1 
ATOM   17732 N  ND2   . ASN   B 1  1179 ? 24.077  54.075  64.617  1.00 23.14 ? 1177 ASN   B ND2   1 
ATOM   17733 N  N     . LYS   B 1  1180 ? 28.012  56.619  65.873  1.00 19.74 ? 1178 LYS   B N     1 
ATOM   17734 C  CA    . LYS   B 1  1180 ? 29.313  56.093  66.273  1.00 20.09 ? 1178 LYS   B CA    1 
ATOM   17735 C  C     . LYS   B 1  1180 ? 29.744  56.659  67.617  1.00 17.56 ? 1178 LYS   B C     1 
ATOM   17736 O  O     . LYS   B 1  1180 ? 30.249  55.930  68.476  1.00 21.36 ? 1178 LYS   B O     1 
ATOM   17737 C  CB    . LYS   B 1  1180 ? 30.356  56.408  65.201  1.00 22.20 ? 1178 LYS   B CB    1 
ATOM   17738 C  CG    . LYS   B 1  1180 ? 30.344  55.447  64.031  1.00 26.67 ? 1178 LYS   B CG    1 
ATOM   17739 C  CD    . LYS   B 1  1180 ? 31.366  55.869  62.968  1.00 30.57 ? 1178 LYS   B CD    1 
ATOM   17740 C  CE    . LYS   B 1  1180 ? 32.744  56.097  63.571  1.00 42.70 ? 1178 LYS   B CE    1 
ATOM   17741 N  NZ    . LYS   B 1  1180 ? 33.518  54.834  63.763  1.00 51.48 ? 1178 LYS   B NZ    1 
ATOM   17742 N  N     . ALA   B 1  1181 ? 29.550  57.964  67.816  1.00 19.19 ? 1179 ALA   B N     1 
ATOM   17743 C  CA    . ALA   B 1  1181 ? 29.928  58.569  69.090  1.00 18.61 ? 1179 ALA   B CA    1 
ATOM   17744 C  C     . ALA   B 1  1181 ? 29.108  57.993  70.237  1.00 18.26 ? 1179 ALA   B C     1 
ATOM   17745 O  O     . ALA   B 1  1181 ? 29.643  57.722  71.315  1.00 19.79 ? 1179 ALA   B O     1 
ATOM   17746 C  CB    . ALA   B 1  1181 ? 29.749  60.081  69.020  1.00 18.89 ? 1179 ALA   B CB    1 
ATOM   17747 N  N     . ILE   B 1  1182 ? 27.813  57.767  70.008  1.00 18.06 ? 1180 ILE   B N     1 
ATOM   17748 C  CA    . ILE   B 1  1182 ? 26.970  57.194  71.051  1.00 20.21 ? 1180 ILE   B CA    1 
ATOM   17749 C  C     . ILE   B 1  1182 ? 27.383  55.764  71.368  1.00 19.03 ? 1180 ILE   B C     1 
ATOM   17750 O  O     . ILE   B 1  1182 ? 27.398  55.353  72.531  1.00 19.88 ? 1180 ILE   B O     1 
ATOM   17751 C  CB    . ILE   B 1  1182 ? 25.491  57.287  70.649  1.00 20.15 ? 1180 ILE   B CB    1 
ATOM   17752 C  CG1   . ILE   B 1  1182 ? 25.044  58.744  70.711  1.00 19.72 ? 1180 ILE   B CG1   1 
ATOM   17753 C  CG2   . ILE   B 1  1182 ? 24.635  56.390  71.545  1.00 22.10 ? 1180 ILE   B CG2   1 
ATOM   17754 C  CD1   . ILE   B 1  1182 ? 23.689  59.001  70.070  1.00 19.23 ? 1180 ILE   B CD1   1 
ATOM   17755 N  N     . ALA   B 1  1183 ? 27.728  54.981  70.340  1.00 20.37 ? 1181 ALA   B N     1 
ATOM   17756 C  CA    . ALA   B 1  1183 ? 28.149  53.608  70.582  1.00 22.32 ? 1181 ALA   B CA    1 
ATOM   17757 C  C     . ALA   B 1  1183 ? 29.408  53.544  71.428  1.00 22.26 ? 1181 ALA   B C     1 
ATOM   17758 O  O     . ALA   B 1  1183 ? 29.637  52.548  72.122  1.00 25.94 ? 1181 ALA   B O     1 
ATOM   17759 C  CB    . ALA   B 1  1183 ? 28.365  52.874  69.256  1.00 20.70 ? 1181 ALA   B CB    1 
ATOM   17760 N  N     . ALA   B 1  1184 ? 30.225  54.595  71.403  1.00 20.64 ? 1182 ALA   B N     1 
ATOM   17761 C  CA    . ALA   B 1  1184 ? 31.431  54.641  72.213  1.00 22.52 ? 1182 ALA   B CA    1 
ATOM   17762 C  C     . ALA   B 1  1184 ? 31.207  55.211  73.608  1.00 21.68 ? 1182 ALA   B C     1 
ATOM   17763 O  O     . ALA   B 1  1184 ? 32.166  55.315  74.373  1.00 22.96 ? 1182 ALA   B O     1 
ATOM   17764 C  CB    . ALA   B 1  1184 ? 32.528  55.440  71.494  1.00 22.96 ? 1182 ALA   B CB    1 
ATOM   17765 N  N     . LEU   B 1  1185 ? 29.985  55.592  73.967  1.00 19.53 ? 1183 LEU   B N     1 
ATOM   17766 C  CA    . LEU   B 1  1185 ? 29.772  56.080  75.324  1.00 19.85 ? 1183 LEU   B CA    1 
ATOM   17767 C  C     . LEU   B 1  1185 ? 29.872  54.923  76.314  1.00 22.60 ? 1183 LEU   B C     1 
ATOM   17768 O  O     . LEU   B 1  1185 ? 29.445  53.800  76.016  1.00 22.91 ? 1183 LEU   B O     1 
ATOM   17769 C  CB    . LEU   B 1  1185 ? 28.407  56.742  75.464  1.00 19.29 ? 1183 LEU   B CB    1 
ATOM   17770 C  CG    . LEU   B 1  1185 ? 28.222  57.958  74.561  1.00 19.27 ? 1183 LEU   B CG    1 
ATOM   17771 C  CD1   . LEU   B 1  1185 ? 26.777  58.436  74.631  1.00 19.93 ? 1183 LEU   B CD1   1 
ATOM   17772 C  CD2   . LEU   B 1  1185 ? 29.203  59.062  74.933  1.00 19.08 ? 1183 LEU   B CD2   1 
ATOM   17773 N  N     . PRO   B 1  1186 ? 30.431  55.156  77.491  1.00 21.56 ? 1184 PRO   B N     1 
ATOM   17774 C  CA    . PRO   B 1  1186 ? 30.470  54.103  78.504  1.00 23.50 ? 1184 PRO   B CA    1 
ATOM   17775 C  C     . PRO   B 1  1186 ? 29.081  53.885  79.073  1.00 20.45 ? 1184 PRO   B C     1 
ATOM   17776 O  O     . PRO   B 1  1186 ? 28.188  54.725  78.949  1.00 22.63 ? 1184 PRO   B O     1 
ATOM   17777 C  CB    . PRO   B 1  1186 ? 31.405  54.678  79.571  1.00 29.05 ? 1184 PRO   B CB    1 
ATOM   17778 C  CG    . PRO   B 1  1186 ? 31.249  56.168  79.431  1.00 31.09 ? 1184 PRO   B CG    1 
ATOM   17779 C  CD    . PRO   B 1  1186 ? 31.008  56.427  77.973  1.00 24.77 ? 1184 PRO   B CD    1 
ATOM   17780 N  N     . GLY   B 1  1187 ? 28.914  52.734  79.713  1.00 22.35 ? 1185 GLY   B N     1 
ATOM   17781 C  CA    . GLY   B 1  1187 ? 27.679  52.445  80.404  1.00 21.96 ? 1185 GLY   B CA    1 
ATOM   17782 C  C     . GLY   B 1  1187 ? 26.664  51.771  79.511  1.00 20.35 ? 1185 GLY   B C     1 
ATOM   17783 O  O     . GLY   B 1  1187 ? 26.995  50.934  78.669  1.00 24.15 ? 1185 GLY   B O     1 
ATOM   17784 N  N     . PRO   B 1  1188 ? 25.398  52.112  79.694  1.00 18.18 ? 1186 PRO   B N     1 
ATOM   17785 C  CA    . PRO   B 1  1188 ? 24.342  51.389  78.980  1.00 20.55 ? 1186 PRO   B CA    1 
ATOM   17786 C  C     . PRO   B 1  1188 ? 24.405  51.616  77.482  1.00 18.91 ? 1186 PRO   B C     1 
ATOM   17787 O  O     . PRO   B 1  1188 ? 24.846  52.660  76.997  1.00 21.55 ? 1186 PRO   B O     1 
ATOM   17788 C  CB    . PRO   B 1  1188 ? 23.051  51.971  79.565  1.00 20.56 ? 1186 PRO   B CB    1 
ATOM   17789 C  CG    . PRO   B 1  1188 ? 23.445  53.297  80.117  1.00 25.89 ? 1186 PRO   B CG    1 
ATOM   17790 C  CD    . PRO   B 1  1188 ? 24.861  53.141  80.598  1.00 20.35 ? 1186 PRO   B CD    1 
ATOM   17791 N  N     . LEU   B 1  1189 ? 23.954  50.611  76.744  1.00 17.95 ? 1187 LEU   B N     1 
ATOM   17792 C  CA    . LEU   B 1  1189 ? 23.776  50.762  75.311  1.00 17.73 ? 1187 LEU   B CA    1 
ATOM   17793 C  C     . LEU   B 1  1189 ? 22.525  51.584  75.081  1.00 19.63 ? 1187 LEU   B C     1 
ATOM   17794 O  O     . LEU   B 1  1189 ? 21.445  51.214  75.557  1.00 20.53 ? 1187 LEU   B O     1 
ATOM   17795 C  CB    . LEU   B 1  1189 ? 23.607  49.399  74.652  1.00 17.58 ? 1187 LEU   B CB    1 
ATOM   17796 C  CG    . LEU   B 1  1189 ? 24.853  48.563  74.387  1.00 20.01 ? 1187 LEU   B CG    1 
ATOM   17797 C  CD1   . LEU   B 1  1189 ? 25.369  47.953  75.685  1.00 25.17 ? 1187 LEU   B CD1   1 
ATOM   17798 C  CD2   . LEU   B 1  1189 ? 24.515  47.476  73.372  1.00 21.48 ? 1187 LEU   B CD2   1 
ATOM   17799 N  N     . LEU   B 1  1190 ? 22.651  52.684  74.355  1.00 18.70 ? 1188 LEU   B N     1 
ATOM   17800 C  CA    . LEU   B 1  1190 ? 21.530  53.598  74.207  1.00 17.33 ? 1188 LEU   B CA    1 
ATOM   17801 C  C     . LEU   B 1  1190 ? 20.685  53.217  73.007  1.00 19.48 ? 1188 LEU   B C     1 
ATOM   17802 O  O     . LEU   B 1  1190 ? 21.202  52.946  71.919  1.00 18.38 ? 1188 LEU   B O     1 
ATOM   17803 C  CB    . LEU   B 1  1190 ? 21.995  55.040  74.038  1.00 17.57 ? 1188 LEU   B CB    1 
ATOM   17804 C  CG    . LEU   B 1  1190 ? 22.832  55.624  75.164  1.00 18.11 ? 1188 LEU   B CG    1 
ATOM   17805 C  CD1   . LEU   B 1  1190 ? 22.945  57.120  74.919  1.00 19.57 ? 1188 LEU   B CD1   1 
ATOM   17806 C  CD2   . LEU   B 1  1190 ? 22.225  55.321  76.541  1.00 20.04 ? 1188 LEU   B CD2   1 
ATOM   17807 N  N     . LEU   B 1  1191 ? 19.376  53.233  73.211  1.00 17.63 ? 1189 LEU   B N     1 
ATOM   17808 C  CA    . LEU   B 1  1191 ? 18.433  53.119  72.109  1.00 16.65 ? 1189 LEU   B CA    1 
ATOM   17809 C  C     . LEU   B 1  1191 ? 18.353  54.474  71.417  1.00 18.41 ? 1189 LEU   B C     1 
ATOM   17810 O  O     . LEU   B 1  1191 ? 17.821  55.441  71.979  1.00 19.22 ? 1189 LEU   B O     1 
ATOM   17811 C  CB    . LEU   B 1  1191 ? 17.075  52.680  72.640  1.00 17.37 ? 1189 LEU   B CB    1 
ATOM   17812 C  CG    . LEU   B 1  1191 ? 16.082  52.108  71.625  1.00 17.26 ? 1189 LEU   B CG    1 
ATOM   17813 C  CD1   . LEU   B 1  1191 ? 14.942  51.417  72.363  1.00 18.17 ? 1189 LEU   B CD1   1 
ATOM   17814 C  CD2   . LEU   B 1  1191 ? 15.534  53.173  70.673  1.00 17.12 ? 1189 LEU   B CD2   1 
ATOM   17815 N  N     . VAL   B 1  1192 ? 18.884  54.532  70.198  1.00 16.67 ? 1190 VAL   B N     1 
ATOM   17816 C  CA    . VAL   B 1  1192 ? 19.040  55.761  69.430  1.00 18.41 ? 1190 VAL   B CA    1 
ATOM   17817 C  C     . VAL   B 1  1192 ? 17.925  55.841  68.403  1.00 17.93 ? 1190 VAL   B C     1 
ATOM   17818 O  O     . VAL   B 1  1192 ? 17.661  54.869  67.681  1.00 19.48 ? 1190 VAL   B O     1 
ATOM   17819 C  CB    . VAL   B 1  1192 ? 20.401  55.789  68.718  1.00 18.34 ? 1190 VAL   B CB    1 
ATOM   17820 C  CG1   . VAL   B 1  1192 ? 20.539  57.046  67.866  1.00 19.71 ? 1190 VAL   B CG1   1 
ATOM   17821 C  CG2   . VAL   B 1  1192 ? 21.536  55.693  69.725  1.00 17.69 ? 1190 VAL   B CG2   1 
ATOM   17822 N  N     . GLN   B 1  1193 ? 17.298  57.005  68.313  1.00 17.21 ? 1191 GLN   B N     1 
ATOM   17823 C  CA    . GLN   B 1  1193 ? 16.355  57.307  67.250  1.00 15.09 ? 1191 GLN   B CA    1 
ATOM   17824 C  C     . GLN   B 1  1193 ? 16.880  58.501  66.481  1.00 16.53 ? 1191 GLN   B C     1 
ATOM   17825 O  O     . GLN   B 1  1193 ? 17.239  59.517  67.081  1.00 18.99 ? 1191 GLN   B O     1 
ATOM   17826 C  CB    . GLN   B 1  1193 ? 14.997  57.655  67.827  1.00 18.13 ? 1191 GLN   B CB    1 
ATOM   17827 C  CG    . GLN   B 1  1193 ? 14.448  56.568  68.691  1.00 17.86 ? 1191 GLN   B CG    1 
ATOM   17828 C  CD    . GLN   B 1  1193 ? 12.985  56.774  68.919  1.00 20.55 ? 1191 GLN   B CD    1 
ATOM   17829 O  OE1   . GLN   B 1  1193 ? 12.191  56.683  67.989  1.00 19.79 ? 1191 GLN   B OE1   1 
ATOM   17830 N  NE2   . GLN   B 1  1193 ? 12.614  57.081  70.149  1.00 19.67 ? 1191 GLN   B NE2   1 
ATOM   17831 N  N     . ALA   B 1  1194 ? 16.913  58.380  65.158  1.00 17.18 ? 1192 ALA   B N     1 
ATOM   17832 C  CA    . ALA   B 1  1194 ? 17.438  59.435  64.312  1.00 17.80 ? 1192 ALA   B CA    1 
ATOM   17833 C  C     . ALA   B 1  1194 ? 16.426  59.809  63.243  1.00 19.55 ? 1192 ALA   B C     1 
ATOM   17834 O  O     . ALA   B 1  1194 ? 15.636  58.981  62.786  1.00 22.26 ? 1192 ALA   B O     1 
ATOM   17835 C  CB    . ALA   B 1  1194 ? 18.731  58.989  63.640  1.00 20.11 ? 1192 ALA   B CB    1 
ATOM   17836 N  N     . ALA   B 1  1195 ? 16.461  61.074  62.850  1.00 18.78 ? 1193 ALA   B N     1 
ATOM   17837 C  CA    . ALA   B 1  1195 ? 15.600  61.562  61.790  1.00 20.16 ? 1193 ALA   B CA    1 
ATOM   17838 C  C     . ALA   B 1  1195 ? 16.285  62.757  61.157  1.00 22.90 ? 1193 ALA   B C     1 
ATOM   17839 O  O     . ALA   B 1  1195 ? 17.077  63.443  61.799  1.00 20.08 ? 1193 ALA   B O     1 
ATOM   17840 C  CB    . ALA   B 1  1195 ? 14.220  61.976  62.320  1.00 21.77 ? 1193 ALA   B CB    1 
ATOM   17841 N  N     . SER   B 1  1196 ? 15.988  62.988  59.887  1.00 21.53 ? 1194 SER   B N     1 
ATOM   17842 C  CA    . SER   B 1  1196 ? 16.439  64.214  59.261  1.00 22.02 ? 1194 SER   B CA    1 
ATOM   17843 C  C     . SER   B 1  1196 ? 15.502  65.353  59.640  1.00 22.05 ? 1194 SER   B C     1 
ATOM   17844 O  O     . SER   B 1  1196 ? 14.380  65.140  60.108  1.00 22.67 ? 1194 SER   B O     1 
ATOM   17845 C  CB    . SER   B 1  1196 ? 16.395  64.056  57.750  1.00 24.30 ? 1194 SER   B CB    1 
ATOM   17846 O  OG    . SER   B 1  1196 ? 15.049  63.924  57.347  1.00 23.90 ? 1194 SER   B OG    1 
ATOM   17847 N  N     . SER   B 1  1197 ? 15.978  66.583  59.423  1.00 22.15 ? 1195 SER   B N     1 
ATOM   17848 C  CA    . SER   B 1  1197 ? 15.130  67.751  59.630  1.00 22.65 ? 1195 SER   B CA    1 
ATOM   17849 C  C     . SER   B 1  1197 ? 13.863  67.669  58.791  1.00 23.12 ? 1195 SER   B C     1 
ATOM   17850 O  O     . SER   B 1  1197 ? 12.771  67.995  59.266  1.00 25.77 ? 1195 SER   B O     1 
ATOM   17851 C  CB    . SER   B 1  1197 ? 15.909  69.021  59.302  1.00 24.42 ? 1195 SER   B CB    1 
ATOM   17852 O  OG    . SER   B 1  1197 ? 17.055  69.116  60.123  1.00 24.65 ? 1195 SER   B OG    1 
ATOM   17853 N  N     . GLY   B 1  1198 ? 13.985  67.223  57.542  1.00 24.99 ? 1196 GLY   B N     1 
ATOM   17854 C  CA    . GLY   B 1  1198 ? 12.803  67.078  56.710  1.00 28.90 ? 1196 GLY   B CA    1 
ATOM   17855 C  C     . GLY   B 1  1198 ? 11.848  66.030  57.244  1.00 27.78 ? 1196 GLY   B C     1 
ATOM   17856 O  O     . GLY   B 1  1198 ? 10.629  66.204  57.193  1.00 27.08 ? 1196 GLY   B O     1 
ATOM   17857 N  N     . GLU   B 1  1199 ? 12.393  64.928  57.768  1.00 26.11 ? 1197 GLU   B N     1 
ATOM   17858 C  CA    . GLU   B 1  1199 ? 11.561  63.880  58.346  1.00 26.90 ? 1197 GLU   B CA    1 
ATOM   17859 C  C     . GLU   B 1  1199 ? 10.793  64.394  59.559  1.00 28.31 ? 1197 GLU   B C     1 
ATOM   17860 O  O     . GLU   B 1  1199 ? 9.614   64.075  59.740  1.00 28.04 ? 1197 GLU   B O     1 
ATOM   17861 C  CB    . GLU   B 1  1199 ? 12.452  62.697  58.723  1.00 27.13 ? 1197 GLU   B CB    1 
ATOM   17862 C  CG    . GLU   B 1  1199 ? 11.733  61.423  59.114  1.00 35.71 ? 1197 GLU   B CG    1 
ATOM   17863 C  CD    . GLU   B 1  1199 ? 12.706  60.270  59.311  1.00 40.20 ? 1197 GLU   B CD    1 
ATOM   17864 O  OE1   . GLU   B 1  1199 ? 13.926  60.474  59.099  1.00 40.84 ? 1197 GLU   B OE1   1 
ATOM   17865 O  OE2   . GLU   B 1  1199 ? 12.259  59.164  59.675  1.00 45.30 ? 1197 GLU   B OE2   1 
ATOM   17866 N  N     . ILE   B 1  1200 ? 11.439  65.207  60.395  1.00 22.63 ? 1198 ILE   B N     1 
ATOM   17867 C  CA    . ILE   B 1  1200 ? 10.751  65.780  61.547  1.00 24.24 ? 1198 ILE   B CA    1 
ATOM   17868 C  C     . ILE   B 1  1200 ? 9.596   66.665  61.100  1.00 28.70 ? 1198 ILE   B C     1 
ATOM   17869 O  O     . ILE   B 1  1200 ? 8.517   66.663  61.708  1.00 26.52 ? 1198 ILE   B O     1 
ATOM   17870 C  CB    . ILE   B 1  1200 ? 11.750  66.541  62.437  1.00 21.42 ? 1198 ILE   B CB    1 
ATOM   17871 C  CG1   . ILE   B 1  1200 ? 12.754  65.570  63.054  1.00 22.27 ? 1198 ILE   B CG1   1 
ATOM   17872 C  CG2   . ILE   B 1  1200 ? 11.021  67.320  63.513  1.00 24.41 ? 1198 ILE   B CG2   1 
ATOM   17873 C  CD1   . ILE   B 1  1200 ? 13.893  66.268  63.801  1.00 21.66 ? 1198 ILE   B CD1   1 
ATOM   17874 N  N     . ALA   B 1  1201 ? 9.798   67.430  60.026  1.00 27.59 ? 1199 ALA   B N     1 
ATOM   17875 C  CA    . ALA   B 1  1201 ? 8.747   68.322  59.547  1.00 29.30 ? 1199 ALA   B CA    1 
ATOM   17876 C  C     . ALA   B 1  1201 ? 7.600   67.548  58.907  1.00 26.86 ? 1199 ALA   B C     1 
ATOM   17877 O  O     . ALA   B 1  1201 ? 6.436   67.933  59.050  1.00 32.25 ? 1199 ALA   B O     1 
ATOM   17878 C  CB    . ALA   B 1  1201 ? 9.328   69.332  58.555  1.00 30.04 ? 1199 ALA   B CB    1 
ATOM   17879 N  N     . ARG   B 1  1202 ? 7.909   66.457  58.198  1.00 31.20 ? 1200 ARG   B N     1 
ATOM   17880 C  CA    . ARG   B 1  1202 ? 6.901   65.718  57.439  1.00 32.20 ? 1200 ARG   B CA    1 
ATOM   17881 C  C     . ARG   B 1  1202 ? 6.144   64.705  58.283  1.00 33.17 ? 1200 ARG   B C     1 
ATOM   17882 O  O     . ARG   B 1  1202 ? 4.950   64.482  58.055  1.00 35.16 ? 1200 ARG   B O     1 
ATOM   17883 C  CB    . ARG   B 1  1202 ? 7.559   64.947  56.288  1.00 31.64 ? 1200 ARG   B CB    1 
ATOM   17884 C  CG    . ARG   B 1  1202 ? 8.161   65.809  55.202  1.00 45.10 ? 1200 ARG   B CG    1 
ATOM   17885 C  CD    . ARG   B 1  1202 ? 8.668   64.958  54.050  1.00 49.08 ? 1200 ARG   B CD    1 
ATOM   17886 N  NE    . ARG   B 1  1202 ? 9.372   63.769  54.518  1.00 48.80 ? 1200 ARG   B NE    1 
ATOM   17887 C  CZ    . ARG   B 1  1202 ? 10.690  63.658  54.603  1.00 43.66 ? 1200 ARG   B CZ    1 
ATOM   17888 N  NH1   . ARG   B 1  1202 ? 11.494  64.646  54.239  1.00 42.44 ? 1200 ARG   B NH1   1 
ATOM   17889 N  NH2   . ARG   B 1  1202 ? 11.217  62.525  55.057  1.00 40.37 ? 1200 ARG   B NH2   1 
ATOM   17890 N  N     . ASN   B 1  1203 ? 6.817   64.083  59.241  1.00 28.07 ? 1201 ASN   B N     1 
ATOM   17891 C  CA    . ASN   B 1  1203 ? 6.316   62.874  59.890  1.00 27.66 ? 1201 ASN   B CA    1 
ATOM   17892 C  C     . ASN   B 1  1203 ? 6.098   63.126  61.372  1.00 29.45 ? 1201 ASN   B C     1 
ATOM   17893 O  O     . ASN   B 1  1203 ? 7.082   63.257  62.127  1.00 26.02 ? 1201 ASN   B O     1 
ATOM   17894 C  CB    . ASN   B 1  1203 ? 7.317   61.737  59.680  1.00 30.34 ? 1201 ASN   B CB    1 
ATOM   17895 C  CG    . ASN   B 1  1203 ? 6.875   60.429  60.318  1.00 29.75 ? 1201 ASN   B CG    1 
ATOM   17896 O  OD1   . ASN   B 1  1203 ? 5.751   60.304  60.809  1.00 34.74 ? 1201 ASN   B OD1   1 
ATOM   17897 N  ND2   . ASN   B 1  1203 ? 7.761   59.441  60.299  1.00 32.92 ? 1201 ASN   B ND2   1 
ATOM   17898 N  N     . PRO   B 1  1204 ? 4.846   63.173  61.836  1.00 29.87 ? 1202 PRO   B N     1 
ATOM   17899 C  CA    . PRO   B 1  1204 ? 4.599   63.339  63.278  1.00 29.82 ? 1202 PRO   B CA    1 
ATOM   17900 C  C     . PRO   B 1  1204 ? 5.216   62.244  64.128  1.00 27.06 ? 1202 PRO   B C     1 
ATOM   17901 O  O     . PRO   B 1  1204 ? 5.457   62.465  65.320  1.00 27.99 ? 1202 PRO   B O     1 
ATOM   17902 C  CB    . PRO   B 1  1204 ? 3.065   63.328  63.378  1.00 32.74 ? 1202 PRO   B CB    1 
ATOM   17903 C  CG    . PRO   B 1  1204 ? 2.581   63.644  61.997  1.00 38.53 ? 1202 PRO   B CG    1 
ATOM   17904 C  CD    . PRO   B 1  1204 ? 3.595   63.057  61.066  1.00 33.84 ? 1202 PRO   B CD    1 
ATOM   17905 N  N     . ASP   B 1  1205 ? 5.478   61.069  63.560  1.00 27.37 ? 1203 ASP   B N     1 
ATOM   17906 C  CA    . ASP   B 1  1205 ? 6.061   59.956  64.296  1.00 28.45 ? 1203 ASP   B CA    1 
ATOM   17907 C  C     . ASP   B 1  1205 ? 7.533   59.738  63.953  1.00 27.31 ? 1203 ASP   B C     1 
ATOM   17908 O  O     . ASP   B 1  1205 ? 8.048   58.625  64.082  1.00 26.84 ? 1203 ASP   B O     1 
ATOM   17909 C  CB    . ASP   B 1  1205 ? 5.250   58.676  64.087  1.00 30.70 ? 1203 ASP   B CB    1 
ATOM   17910 C  CG    . ASP   B 1  1205 ? 3.825   58.790  64.616  1.00 36.12 ? 1203 ASP   B CG    1 
ATOM   17911 O  OD1   . ASP   B 1  1205 ? 3.571   59.649  65.488  1.00 33.90 ? 1203 ASP   B OD1   1 
ATOM   17912 O  OD2   . ASP   B 1  1205 ? 2.957   58.016  64.159  1.00 38.59 ? 1203 ASP   B OD2   1 
ATOM   17913 N  N     . ALA   B 1  1206 ? 8.220   60.797  63.511  1.00 26.05 ? 1204 ALA   B N     1 
ATOM   17914 C  CA    . ALA   B 1  1206 ? 9.647   60.689  63.226  1.00 27.48 ? 1204 ALA   B CA    1 
ATOM   17915 C  C     . ALA   B 1  1206 ? 10.398  60.096  64.410  1.00 22.67 ? 1204 ALA   B C     1 
ATOM   17916 O  O     . ALA   B 1  1206 ? 11.285  59.252  64.239  1.00 25.56 ? 1204 ALA   B O     1 
ATOM   17917 C  CB    . ALA   B 1  1206 ? 10.208  62.064  62.861  1.00 27.24 ? 1204 ALA   B CB    1 
ATOM   17918 N  N     . TYR   B 1  1207 ? 10.045  60.516  65.622  1.00 20.19 ? 1205 TYR   B N     1 
ATOM   17919 C  CA    . TYR   B 1  1207 ? 10.534  59.894  66.838  1.00 22.16 ? 1205 TYR   B CA    1 
ATOM   17920 C  C     . TYR   B 1  1207 ? 9.391   59.117  67.466  1.00 20.90 ? 1205 TYR   B C     1 
ATOM   17921 O  O     . TYR   B 1  1207 ? 8.289   59.652  67.634  1.00 27.10 ? 1205 TYR   B O     1 
ATOM   17922 C  CB    . TYR   B 1  1207 ? 11.054  60.942  67.816  1.00 21.54 ? 1205 TYR   B CB    1 
ATOM   17923 C  CG    . TYR   B 1  1207 ? 12.226  61.706  67.270  1.00 19.20 ? 1205 TYR   B CG    1 
ATOM   17924 C  CD1   . TYR   B 1  1207 ? 13.383  61.046  66.891  1.00 18.53 ? 1205 TYR   B CD1   1 
ATOM   17925 C  CD2   . TYR   B 1  1207 ? 12.176  63.089  67.129  1.00 22.16 ? 1205 TYR   B CD2   1 
ATOM   17926 C  CE1   . TYR   B 1  1207 ? 14.474  61.743  66.397  1.00 17.09 ? 1205 TYR   B CE1   1 
ATOM   17927 C  CE2   . TYR   B 1  1207 ? 13.261  63.797  66.628  1.00 20.53 ? 1205 TYR   B CE2   1 
ATOM   17928 C  CZ    . TYR   B 1  1207 ? 14.396  63.115  66.263  1.00 18.37 ? 1205 TYR   B CZ    1 
ATOM   17929 O  OH    . TYR   B 1  1207 ? 15.465  63.825  65.767  1.00 19.27 ? 1205 TYR   B OH    1 
ATOM   17930 N  N     . CYS   B 1  1208 ? 9.654   57.867  67.800  1.00 17.08 ? 1206 CYS   B N     1 
ATOM   17931 C  CA    . CYS   B 1  1208 ? 8.629   56.982  68.331  1.00 17.10 ? 1206 CYS   B CA    1 
ATOM   17932 C  C     . CYS   B 1  1208 ? 8.637   57.067  69.852  1.00 16.65 ? 1206 CYS   B C     1 
ATOM   17933 O  O     . CYS   B 1  1208 ? 9.663   56.800  70.487  1.00 17.63 ? 1206 CYS   B O     1 
ATOM   17934 C  CB    . CYS   B 1  1208 ? 8.925   55.556  67.882  1.00 19.04 ? 1206 CYS   B CB    1 
ATOM   17935 S  SG    . CYS   B 1  1208 ? 7.711   54.376  68.432  1.00 22.06 ? 1206 CYS   B SG    1 
ATOM   17936 N  N     . LEU   B 1  1209 ? 7.480   57.401  70.437  1.00 16.84 ? 1207 LEU   B N     1 
ATOM   17937 C  CA    . LEU   B 1  1209 ? 7.400   57.488  71.893  1.00 17.22 ? 1207 LEU   B CA    1 
ATOM   17938 C  C     . LEU   B 1  1209 ? 7.453   56.124  72.571  1.00 16.73 ? 1207 LEU   B C     1 
ATOM   17939 O  O     . LEU   B 1  1209 ? 7.682   56.065  73.781  1.00 15.46 ? 1207 LEU   B O     1 
ATOM   17940 C  CB    . LEU   B 1  1209 ? 6.140   58.239  72.305  1.00 15.44 ? 1207 LEU   B CB    1 
ATOM   17941 C  CG    . LEU   B 1  1209 ? 5.948   59.609  71.672  1.00 18.24 ? 1207 LEU   B CG    1 
ATOM   17942 C  CD1   . LEU   B 1  1209 ? 4.755   60.310  72.321  1.00 21.55 ? 1207 LEU   B CD1   1 
ATOM   17943 C  CD2   . LEU   B 1  1209 ? 7.210   60.436  71.817  1.00 19.09 ? 1207 LEU   B CD2   1 
ATOM   17944 N  N     . ASN   B 1  1210 ? 7.263   55.034  71.826  1.00 16.57 ? 1208 ASN   B N     1 
ATOM   17945 C  CA    . ASN   B 1  1210 ? 7.353   53.712  72.432  1.00 18.75 ? 1208 ASN   B CA    1 
ATOM   17946 C  C     . ASN   B 1  1210 ? 8.722   53.481  73.055  1.00 16.87 ? 1208 ASN   B C     1 
ATOM   17947 O  O     . ASN   B 1  1210 ? 8.829   52.781  74.069  1.00 19.57 ? 1208 ASN   B O     1 
ATOM   17948 C  CB    . ASN   B 1  1210 ? 7.082   52.615  71.389  1.00 21.77 ? 1208 ASN   B CB    1 
ATOM   17949 C  CG    . ASN   B 1  1210 ? 5.663   52.675  70.799  1.00 21.61 ? 1208 ASN   B CG    1 
ATOM   17950 O  OD1   . ASN   B 1  1210 ? 4.942   53.653  70.971  1.00 28.32 ? 1208 ASN   B OD1   1 
ATOM   17951 N  ND2   . ASN   B 1  1210 ? 5.286   51.632  70.071  1.00 32.14 ? 1208 ASN   B ND2   1 
ATOM   17952 N  N     . TRP   B 1  1211 ? 9.775   54.064  72.477  1.00 16.53 ? 1209 TRP   B N     1 
ATOM   17953 C  CA    . TRP   B 1  1211 ? 11.128  53.773  72.931  1.00 16.75 ? 1209 TRP   B CA    1 
ATOM   17954 C  C     . TRP   B 1  1211 ? 11.607  54.744  73.987  1.00 17.36 ? 1209 TRP   B C     1 
ATOM   17955 O  O     . TRP   B 1  1211 ? 12.722  54.587  74.493  1.00 19.88 ? 1209 TRP   B O     1 
ATOM   17956 C  CB    . TRP   B 1  1211 ? 12.119  53.740  71.749  1.00 19.12 ? 1209 TRP   B CB    1 
ATOM   17957 C  CG    . TRP   B 1  1211 ? 11.536  53.088  70.546  1.00 18.61 ? 1209 TRP   B CG    1 
ATOM   17958 C  CD1   . TRP   B 1  1211 ? 11.487  53.600  69.281  1.00 19.92 ? 1209 TRP   B CD1   1 
ATOM   17959 C  CD2   . TRP   B 1  1211 ? 10.862  51.825  70.493  1.00 16.40 ? 1209 TRP   B CD2   1 
ATOM   17960 N  NE1   . TRP   B 1  1211 ? 10.843  52.727  68.443  1.00 21.76 ? 1209 TRP   B NE1   1 
ATOM   17961 C  CE2   . TRP   B 1  1211 ? 10.463  51.624  69.160  1.00 17.92 ? 1209 TRP   B CE2   1 
ATOM   17962 C  CE3   . TRP   B 1  1211 ? 10.591  50.825  71.439  1.00 18.25 ? 1209 TRP   B CE3   1 
ATOM   17963 C  CZ2   . TRP   B 1  1211 ? 9.770   50.484  68.746  1.00 21.45 ? 1209 TRP   B CZ2   1 
ATOM   17964 C  CZ3   . TRP   B 1  1211 ? 9.903   49.689  71.024  1.00 18.78 ? 1209 TRP   B CZ3   1 
ATOM   17965 C  CH2   . TRP   B 1  1211 ? 9.495   49.533  69.692  1.00 19.28 ? 1209 TRP   B CH2   1 
ATOM   17966 N  N     . LEU   B 1  1212 ? 10.791  55.733  74.325  1.00 15.88 ? 1210 LEU   B N     1 
ATOM   17967 C  CA    . LEU   B 1  1212 ? 11.157  56.765  75.275  1.00 14.49 ? 1210 LEU   B CA    1 
ATOM   17968 C  C     . LEU   B 1  1212 ? 10.535  56.544  76.640  1.00 14.71 ? 1210 LEU   B C     1 
ATOM   17969 O  O     . LEU   B 1  1212 ? 10.682  57.395  77.521  1.00 15.55 ? 1210 LEU   B O     1 
ATOM   17970 C  CB    . LEU   B 1  1212 ? 10.770  58.133  74.726  1.00 15.98 ? 1210 LEU   B CB    1 
ATOM   17971 C  CG    . LEU   B 1  1212 ? 11.684  58.576  73.577  1.00 14.38 ? 1210 LEU   B CG    1 
ATOM   17972 C  CD1   . LEU   B 1  1212 ? 11.062  59.721  72.830  1.00 17.45 ? 1210 LEU   B CD1   1 
ATOM   17973 C  CD2   . LEU   B 1  1212 ? 13.048  58.972  74.122  1.00 17.53 ? 1210 LEU   B CD2   1 
ATOM   17974 N  N     . VAL   B 1  1213 ? 9.842   55.429  76.818  1.00 16.03 ? 1211 VAL   B N     1 
ATOM   17975 C  CA    . VAL   B 1  1213 ? 9.371   54.996  78.120  1.00 16.25 ? 1211 VAL   B CA    1 
ATOM   17976 C  C     . VAL   B 1  1213 ? 10.094  53.707  78.468  1.00 15.33 ? 1211 VAL   B C     1 
ATOM   17977 O  O     . VAL   B 1  1213 ? 10.635  53.009  77.603  1.00 17.17 ? 1211 VAL   B O     1 
ATOM   17978 C  CB    . VAL   B 1  1213 ? 7.843   54.807  78.131  1.00 15.77 ? 1211 VAL   B CB    1 
ATOM   17979 C  CG1   . VAL   B 1  1213 ? 7.159   56.155  77.971  1.00 17.70 ? 1211 VAL   B CG1   1 
ATOM   17980 C  CG2   . VAL   B 1  1213 ? 7.422   53.849  77.027  1.00 17.27 ? 1211 VAL   B CG2   1 
ATOM   17981 N  N     . GLU   B 1  1214 ? 10.153  53.420  79.766  1.00 15.38 ? 1212 GLU   B N     1 
ATOM   17982 C  CA    . GLU   B 1  1214 ? 10.718  52.180  80.271  1.00 18.20 ? 1212 GLU   B CA    1 
ATOM   17983 C  C     . GLU   B 1  1214 ? 9.590   51.305  80.793  1.00 15.28 ? 1212 GLU   B C     1 
ATOM   17984 O  O     . GLU   B 1  1214 ? 8.753   51.759  81.575  1.00 16.28 ? 1212 GLU   B O     1 
ATOM   17985 C  CB    . GLU   B 1  1214 ? 11.698  52.440  81.414  1.00 19.13 ? 1212 GLU   B CB    1 
ATOM   17986 C  CG    . GLU   B 1  1214 ? 12.366  51.152  81.889  1.00 23.45 ? 1212 GLU   B CG    1 
ATOM   17987 C  CD    . GLU   B 1  1214 ? 13.215  51.307  83.139  1.00 28.60 ? 1212 GLU   B CD    1 
ATOM   17988 O  OE1   . GLU   B 1  1214 ? 13.702  52.420  83.416  1.00 27.27 ? 1212 GLU   B OE1   1 
ATOM   17989 O  OE2   . GLU   B 1  1214 ? 13.388  50.291  83.849  1.00 30.72 ? 1212 GLU   B OE2   1 
ATOM   17990 N  N     . GLU   B 1  1215 ? 9.576   50.059  80.352  1.00 15.44 ? 1213 GLU   B N     1 
ATOM   17991 C  CA    . GLU   B 1  1215 ? 8.622   49.093  80.857  1.00 15.12 ? 1213 GLU   B CA    1 
ATOM   17992 C  C     . GLU   B 1  1215 ? 9.125   48.507  82.163  1.00 13.85 ? 1213 GLU   B C     1 
ATOM   17993 O  O     . GLU   B 1  1215 ? 10.301  48.153  82.296  1.00 15.46 ? 1213 GLU   B O     1 
ATOM   17994 C  CB    . GLU   B 1  1215 ? 8.506   47.954  79.861  1.00 16.83 ? 1213 GLU   B CB    1 
ATOM   17995 C  CG    . GLU   B 1  1215 ? 8.043   48.368  78.476  1.00 17.79 ? 1213 GLU   B CG    1 
ATOM   17996 C  CD    . GLU   B 1  1215 ? 8.273   47.259  77.482  1.00 15.89 ? 1213 GLU   B CD    1 
ATOM   17997 O  OE1   . GLU   B 1  1215 ? 9.411   47.152  76.980  1.00 16.48 ? 1213 GLU   B OE1   1 
ATOM   17998 O  OE2   . GLU   B 1  1215 ? 7.324   46.492  77.227  1.00 16.28 ? 1213 GLU   B OE2   1 
ATOM   17999 N  N     . VAL   B 1  1216 ? 8.225   48.374  83.123  1.00 15.57 ? 1214 VAL   B N     1 
ATOM   18000 C  CA    . VAL   B 1  1216 ? 8.527   47.665  84.355  1.00 15.85 ? 1214 VAL   B CA    1 
ATOM   18001 C  C     . VAL   B 1  1216 ? 7.439   46.635  84.593  1.00 14.76 ? 1214 VAL   B C     1 
ATOM   18002 O  O     . VAL   B 1  1216 ? 6.244   46.960  84.563  1.00 15.37 ? 1214 VAL   B O     1 
ATOM   18003 C  CB    . VAL   B 1  1216 ? 8.655   48.612  85.560  1.00 14.63 ? 1214 VAL   B CB    1 
ATOM   18004 C  CG1   . VAL   B 1  1216 ? 8.861   47.809  86.846  1.00 17.94 ? 1214 VAL   B CG1   1 
ATOM   18005 C  CG2   . VAL   B 1  1216 ? 9.789   49.620  85.320  1.00 17.35 ? 1214 VAL   B CG2   1 
ATOM   18006 N  N     . SER   B 1  1217 ? 7.855   45.398  84.823  1.00 13.31 ? 1215 SER   B N     1 
ATOM   18007 C  CA    . SER   B 1  1217 ? 6.966   44.306  85.173  1.00 14.17 ? 1215 SER   B CA    1 
ATOM   18008 C  C     . SER   B 1  1217 ? 7.141   44.015  86.652  1.00 13.80 ? 1215 SER   B C     1 
ATOM   18009 O  O     . SER   B 1  1217 ? 8.267   43.999  87.154  1.00 14.54 ? 1215 SER   B O     1 
ATOM   18010 C  CB    . SER   B 1  1217 ? 7.376   43.066  84.381  1.00 16.18 ? 1215 SER   B CB    1 
ATOM   18011 O  OG    . SER   B 1  1217 ? 6.886   41.863  84.951  1.00 18.21 ? 1215 SER   B OG    1 
ATOM   18012 N  N     . ALA   B 1  1218 ? 6.040   43.796  87.349  1.00 14.62 ? 1216 ALA   B N     1 
ATOM   18013 C  CA    . ALA   B 1  1218 ? 6.093   43.433  88.758  1.00 15.76 ? 1216 ALA   B CA    1 
ATOM   18014 C  C     . ALA   B 1  1218 ? 5.167   42.251  88.964  1.00 15.95 ? 1216 ALA   B C     1 
ATOM   18015 O  O     . ALA   B 1  1218 ? 3.992   42.301  88.582  1.00 16.80 ? 1216 ALA   B O     1 
ATOM   18016 C  CB    . ALA   B 1  1218 ? 5.677   44.598  89.658  1.00 17.23 ? 1216 ALA   B CB    1 
ATOM   18017 N  N     . SER   B 1  1219 ? 5.692   41.182  89.548  1.00 14.66 ? 1217 SER   B N     1 
ATOM   18018 C  CA    . SER   B 1  1219 ? 4.905   39.993  89.834  1.00 14.32 ? 1217 SER   B CA    1 
ATOM   18019 C  C     . SER   B 1  1219 ? 4.829   39.836  91.340  1.00 13.73 ? 1217 SER   B C     1 
ATOM   18020 O  O     . SER   B 1  1219 ? 5.857   39.659  91.999  1.00 15.08 ? 1217 SER   B O     1 
ATOM   18021 C  CB    . SER   B 1  1219 ? 5.558   38.764  89.216  1.00 15.33 ? 1217 SER   B CB    1 
ATOM   18022 O  OG    . SER   B 1  1219 ? 4.782   37.599  89.473  1.00 16.65 ? 1217 SER   B OG    1 
ATOM   18023 N  N     . ILE   B 1  1220 ? 3.618   39.899  91.871  1.00 15.63 ? 1218 ILE   B N     1 
ATOM   18024 C  CA    . ILE   B 1  1220 ? 3.391   39.840  93.309  1.00 15.43 ? 1218 ILE   B CA    1 
ATOM   18025 C  C     . ILE   B 1  1220 ? 2.702   38.523  93.618  1.00 17.78 ? 1218 ILE   B C     1 
ATOM   18026 O  O     . ILE   B 1  1220 ? 1.622   38.245  93.088  1.00 17.36 ? 1218 ILE   B O     1 
ATOM   18027 C  CB    . ILE   B 1  1220 ? 2.519   41.012  93.765  1.00 18.61 ? 1218 ILE   B CB    1 
ATOM   18028 C  CG1   . ILE   B 1  1220 ? 3.158   42.330  93.324  1.00 20.45 ? 1218 ILE   B CG1   1 
ATOM   18029 C  CG2   . ILE   B 1  1220 ? 2.314   40.941  95.276  1.00 18.38 ? 1218 ILE   B CG2   1 
ATOM   18030 C  CD1   . ILE   B 1  1220 ? 2.197   43.476  93.269  1.00 31.06 ? 1218 ILE   B CD1   1 
ATOM   18031 N  N     . ASN   B 1  1221 ? 3.296   37.734  94.505  1.00 16.85 ? 1219 ASN   B N     1 
ATOM   18032 C  CA    . ASN   B 1  1221 ? 2.655   36.515  94.989  1.00 16.70 ? 1219 ASN   B CA    1 
ATOM   18033 C  C     . ASN   B 1  1221 ? 1.635   36.908  96.052  1.00 19.56 ? 1219 ASN   B C     1 
ATOM   18034 O  O     . ASN   B 1  1221 ? 2.014   37.262  97.175  1.00 19.65 ? 1219 ASN   B O     1 
ATOM   18035 C  CB    . ASN   B 1  1221 ? 3.720   35.606  95.594  1.00 17.45 ? 1219 ASN   B CB    1 
ATOM   18036 C  CG    . ASN   B 1  1221 ? 3.139   34.368  96.229  1.00 19.21 ? 1219 ASN   B CG    1 
ATOM   18037 O  OD1   . ASN   B 1  1221 ? 1.954   34.094  96.090  1.00 17.33 ? 1219 ASN   B OD1   1 
ATOM   18038 N  ND2   . ASN   B 1  1221 ? 3.978   33.602  96.928  1.00 20.06 ? 1219 ASN   B ND2   1 
ATOM   18039 N  N     . THR   B 1  1222 ? 0.345   36.838  95.714  1.00 17.42 ? 1220 THR   B N     1 
ATOM   18040 C  CA    . THR   B 1  1222 ? -0.720  37.217  96.634  1.00 18.38 ? 1220 THR   B CA    1 
ATOM   18041 C  C     . THR   B 1  1222 ? -1.237  36.037  97.435  1.00 21.83 ? 1220 THR   B C     1 
ATOM   18042 O  O     . THR   B 1  1222 ? -2.202  36.187  98.197  1.00 27.05 ? 1220 THR   B O     1 
ATOM   18043 C  CB    . THR   B 1  1222 ? -1.859  37.890  95.878  1.00 20.67 ? 1220 THR   B CB    1 
ATOM   18044 O  OG1   . THR   B 1  1222 ? -2.381  36.977  94.904  1.00 22.27 ? 1220 THR   B OG1   1 
ATOM   18045 C  CG2   . THR   B 1  1222 ? -1.362  39.140  95.168  1.00 22.65 ? 1220 THR   B CG2   1 
ATOM   18046 N  N     . ALA   B 1  1223 ? -0.613  34.874  97.290  1.00 20.23 ? 1221 ALA   B N     1 
ATOM   18047 C  CA    . ALA   B 1  1223 ? -0.878  33.725  98.138  1.00 25.40 ? 1221 ALA   B CA    1 
ATOM   18048 C  C     . ALA   B 1  1223 ? 0.150   33.578  99.255  1.00 35.18 ? 1221 ALA   B C     1 
ATOM   18049 O  O     . ALA   B 1  1223 ? 0.084   32.607  100.015 1.00 36.34 ? 1221 ALA   B O     1 
ATOM   18050 C  CB    . ALA   B 1  1223 ? -0.918  32.449  97.298  1.00 27.48 ? 1221 ALA   B CB    1 
ATOM   18051 N  N     . ALA   B 1  1224 ? 1.096   34.521  99.371  1.00 31.21 ? 1222 ALA   B N     1 
ATOM   18052 C  CA    . ALA   B 1  1224 ? 2.250   34.335  100.250 1.00 28.90 ? 1222 ALA   B CA    1 
ATOM   18053 C  C     . ALA   B 1  1224 ? 1.885   34.239  101.729 1.00 37.86 ? 1222 ALA   B C     1 
ATOM   18054 O  O     . ALA   B 1  1224 ? 2.654   33.654  102.499 1.00 38.49 ? 1222 ALA   B O     1 
ATOM   18055 C  CB    . ALA   B 1  1224 ? 3.294   35.433  100.025 1.00 28.43 ? 1222 ALA   B CB    1 
ATOM   18056 N  N     . ALA   B 1  1225 ? 0.742   34.792  102.148 1.00 39.06 ? 1223 ALA   B N     1 
ATOM   18057 C  CA    . ALA   B 1  1225 ? 0.327   34.693  103.547 1.00 40.69 ? 1223 ALA   B CA    1 
ATOM   18058 C  C     . ALA   B 1  1225 ? -0.218  33.320  103.914 1.00 47.73 ? 1223 ALA   B C     1 
ATOM   18059 O  O     . ALA   B 1  1225 ? -0.530  33.091  105.088 1.00 47.40 ? 1223 ALA   B O     1 
ATOM   18060 C  CB    . ALA   B 1  1225 ? -0.715  35.764  103.898 1.00 39.62 ? 1223 ALA   B CB    1 
ATOM   18061 N  N     . GLY   B 1  1226 ? -0.345  32.411  102.951 1.00 41.00 ? 1224 GLY   B N     1 
ATOM   18062 C  CA    . GLY   B 1  1226 ? -0.851  31.075  103.209 1.00 46.84 ? 1224 GLY   B CA    1 
ATOM   18063 C  C     . GLY   B 1  1226 ? -2.150  30.743  102.504 1.00 49.60 ? 1224 GLY   B C     1 
ATOM   18064 O  O     . GLY   B 1  1226 ? -2.659  29.627  102.681 1.00 45.00 ? 1224 GLY   B O     1 
ATOM   18065 N  N     . GLY   B 1  1227 ? -2.714  31.655  101.719 1.00 38.80 ? 1225 GLY   B N     1 
ATOM   18066 C  CA    . GLY   B 1  1227 ? -3.943  31.380  100.999 1.00 43.02 ? 1225 GLY   B CA    1 
ATOM   18067 C  C     . GLY   B 1  1227 ? -4.248  32.505  100.034 1.00 44.79 ? 1225 GLY   B C     1 
ATOM   18068 O  O     . GLY   B 1  1227 ? -3.527  33.504  99.959  1.00 40.27 ? 1225 GLY   B O     1 
ATOM   18069 N  N     . ASN   B 1  1228 ? -5.345  32.334  99.300  1.00 37.67 ? 1226 ASN   B N     1 
ATOM   18070 C  CA    . ASN   B 1  1228 ? -5.761  33.269  98.259  1.00 45.54 ? 1226 ASN   B CA    1 
ATOM   18071 C  C     . ASN   B 1  1228 ? -7.054  33.952  98.691  1.00 49.31 ? 1226 ASN   B C     1 
ATOM   18072 O  O     . ASN   B 1  1228 ? -8.065  33.282  98.932  1.00 53.22 ? 1226 ASN   B O     1 
ATOM   18073 C  CB    . ASN   B 1  1228 ? -5.961  32.526  96.937  1.00 43.49 ? 1226 ASN   B CB    1 
ATOM   18074 C  CG    . ASN   B 1  1228 ? -6.113  33.461  95.746  1.00 45.47 ? 1226 ASN   B CG    1 
ATOM   18075 O  OD1   . ASN   B 1  1228 ? -6.519  34.617  95.883  1.00 48.95 ? 1226 ASN   B OD1   1 
ATOM   18076 N  ND2   . ASN   B 1  1228 ? -5.792  32.954  94.565  1.00 34.09 ? 1226 ASN   B ND2   1 
ATOM   18077 N  N     . ALA   B 1  1229 ? -7.018  35.285  98.773  1.00 45.90 ? 1227 ALA   B N     1 
ATOM   18078 C  CA    . ALA   B 1  1229 ? -8.200  36.045  99.172  1.00 48.97 ? 1227 ALA   B CA    1 
ATOM   18079 C  C     . ALA   B 1  1229 ? -9.287  35.984  98.105  1.00 53.99 ? 1227 ALA   B C     1 
ATOM   18080 O  O     . ALA   B 1  1229 ? -10.466 35.770  98.416  1.00 47.64 ? 1227 ALA   B O     1 
ATOM   18081 C  CB    . ALA   B 1  1229 ? -7.815  37.497  99.450  1.00 42.62 ? 1227 ALA   B CB    1 
ATOM   18082 N  N     . SER   B 1  1230 ? -8.908  36.179  96.838  1.00 55.16 ? 1228 SER   B N     1 
ATOM   18083 C  CA    . SER   B 1  1230 ? -9.894  36.259  95.764  1.00 56.57 ? 1228 SER   B CA    1 
ATOM   18084 C  C     . SER   B 1  1230 ? -10.620 34.936  95.551  1.00 61.20 ? 1228 SER   B C     1 
ATOM   18085 O  O     . SER   B 1  1230 ? -11.798 34.933  95.173  1.00 61.40 ? 1228 SER   B O     1 
ATOM   18086 C  CB    . SER   B 1  1230 ? -9.228  36.729  94.469  1.00 54.69 ? 1228 SER   B CB    1 
ATOM   18087 N  N     . LEU   B 1  1231 ? -9.947  33.808  95.785  1.00 54.63 ? 1229 LEU   B N     1 
ATOM   18088 C  CA    . LEU   B 1  1231 ? -10.583 32.509  95.607  1.00 53.90 ? 1229 LEU   B CA    1 
ATOM   18089 C  C     . LEU   B 1  1231 ? -11.407 32.069  96.811  1.00 59.03 ? 1229 LEU   B C     1 
ATOM   18090 O  O     . LEU   B 1  1231 ? -12.080 31.034  96.733  1.00 58.70 ? 1229 LEU   B O     1 
ATOM   18091 C  CB    . LEU   B 1  1231 ? -9.547  31.438  95.261  1.00 52.61 ? 1229 LEU   B CB    1 
ATOM   18092 C  CG    . LEU   B 1  1231 ? -8.922  31.374  93.865  1.00 39.42 ? 1229 LEU   B CG    1 
ATOM   18093 C  CD1   . LEU   B 1  1231 ? -8.098  30.107  93.773  1.00 32.24 ? 1229 LEU   B CD1   1 
ATOM   18094 C  CD2   . LEU   B 1  1231 ? -9.971  31.408  92.766  1.00 44.55 ? 1229 LEU   B CD2   1 
ATOM   18095 N  N     . MET   B 1  1232 ? -11.371 32.818  97.918  1.00 58.67 ? 1230 MET   B N     1 
ATOM   18096 C  CA    . MET   B 1  1232 ? -12.282 32.530  99.023  1.00 56.80 ? 1230 MET   B CA    1 
ATOM   18097 C  C     . MET   B 1  1232 ? -13.738 32.761  98.625  1.00 58.60 ? 1230 MET   B C     1 
ATOM   18098 O  O     . MET   B 1  1232 ? -14.629 32.037  99.090  1.00 44.18 ? 1230 MET   B O     1 
ATOM   18099 C  CB    . MET   B 1  1232 ? -11.909 33.372  100.247 1.00 51.52 ? 1230 MET   B CB    1 
ATOM   18100 N  N     . ALA   B 1  1233 ? -13.994 33.749  97.763  1.00 65.71 ? 1231 ALA   B N     1 
ATOM   18101 C  CA    . ALA   B 1  1233 ? -15.329 33.989  97.229  1.00 69.43 ? 1231 ALA   B CA    1 
ATOM   18102 C  C     . ALA   B 1  1233 ? -15.682 33.062  96.073  1.00 68.44 ? 1231 ALA   B C     1 
ATOM   18103 O  O     . ALA   B 1  1233 ? -16.831 33.075  95.617  1.00 70.45 ? 1231 ALA   B O     1 
ATOM   18104 C  CB    . ALA   B 1  1233 ? -15.467 35.446  96.774  1.00 64.07 ? 1231 ALA   B CB    1 
ATOM   18105 N  N     . ILE   B 1  1234 ? -14.731 32.264  95.593  1.00 65.03 ? 1232 ILE   B N     1 
ATOM   18106 C  CA    . ILE   B 1  1234 ? -14.954 31.375  94.459  1.00 62.86 ? 1232 ILE   B CA    1 
ATOM   18107 C  C     . ILE   B 1  1234 ? -15.350 30.006  95.004  1.00 57.87 ? 1232 ILE   B C     1 
ATOM   18108 O  O     . ILE   B 1  1234 ? -14.506 29.221  95.442  1.00 52.47 ? 1232 ILE   B O     1 
ATOM   18109 C  CB    . ILE   B 1  1234 ? -13.735 31.308  93.538  1.00 54.40 ? 1232 ILE   B CB    1 
ATOM   18110 C  CG1   . ILE   B 1  1234 ? -13.474 32.686  92.916  1.00 58.49 ? 1232 ILE   B CG1   1 
ATOM   18111 C  CG2   . ILE   B 1  1234 ? -13.948 30.262  92.472  1.00 48.77 ? 1232 ILE   B CG2   1 
ATOM   18112 C  CD1   . ILE   B 1  1234 ? -13.122 32.660  91.439  1.00 46.91 ? 1232 ILE   B CD1   1 
ATOM   18113 N  N     . GLY   B 1  1235 ? -16.649 29.729  94.986  1.00 53.62 ? 1233 GLY   B N     1 
ATOM   18114 C  CA    . GLY   B 1  1235 ? -17.174 28.431  95.356  1.00 42.29 ? 1233 GLY   B CA    1 
ATOM   18115 C  C     . GLY   B 1  1235 ? -18.091 27.929  94.259  1.00 38.93 ? 1233 GLY   B C     1 
ATOM   18116 O  O     . GLY   B 1  1235 ? -18.879 28.683  93.689  1.00 58.68 ? 1233 GLY   B O     1 
ATOM   18117 O  OXT   . GLY   B 1  1235 ? -18.074 26.765  93.898  1.00 24.28 ? 1233 GLY   B OXT   1 
HETATM 18118 P  PA    A FAD   C 2  .    ? -37.939 43.398  82.582  0.58 21.10 ? 1301 FAD   A PA    1 
HETATM 18119 P  PA    B FAD   C 2  .    ? -37.972 43.462  82.413  0.42 21.71 ? 1301 FAD   A PA    1 
HETATM 18120 O  O1A   A FAD   C 2  .    ? -36.509 42.841  82.364  0.58 24.65 ? 1301 FAD   A O1A   1 
HETATM 18121 O  O1A   B FAD   C 2  .    ? -36.501 42.970  82.356  0.42 24.32 ? 1301 FAD   A O1A   1 
HETATM 18122 O  O2A   A FAD   C 2  .    ? -39.035 42.502  82.880  0.58 24.64 ? 1301 FAD   A O2A   1 
HETATM 18123 O  O2A   B FAD   C 2  .    ? -39.015 42.534  82.792  0.42 24.65 ? 1301 FAD   A O2A   1 
HETATM 18124 O  O5B   A FAD   C 2  .    ? -38.036 44.411  83.646  0.58 19.17 ? 1301 FAD   A O5B   1 
HETATM 18125 O  O5B   B FAD   C 2  .    ? -38.210 44.574  83.355  0.42 21.97 ? 1301 FAD   A O5B   1 
HETATM 18126 C  C5B   A FAD   C 2  .    ? -37.003 45.375  83.801  0.58 21.16 ? 1301 FAD   A C5B   1 
HETATM 18127 C  C5B   B FAD   C 2  .    ? -37.112 45.400  83.726  0.42 21.20 ? 1301 FAD   A C5B   1 
HETATM 18128 C  C4B   A FAD   C 2  .    ? -37.511 46.460  84.743  0.58 19.90 ? 1301 FAD   A C4B   1 
HETATM 18129 C  C4B   B FAD   C 2  .    ? -37.573 46.457  84.725  0.42 19.94 ? 1301 FAD   A C4B   1 
HETATM 18130 O  O4B   A FAD   C 2  .    ? -37.519 46.012  86.059  0.58 20.85 ? 1301 FAD   A O4B   1 
HETATM 18131 O  O4B   B FAD   C 2  .    ? -37.526 45.996  86.036  0.42 20.86 ? 1301 FAD   A O4B   1 
HETATM 18132 C  C3B   A FAD   C 2  .    ? -36.703 47.719  84.784  0.58 20.23 ? 1301 FAD   A C3B   1 
HETATM 18133 C  C3B   B FAD   C 2  .    ? -36.749 47.704  84.744  0.42 20.33 ? 1301 FAD   A C3B   1 
HETATM 18134 O  O3B   A FAD   C 2  .    ? -36.892 48.549  83.688  0.58 21.15 ? 1301 FAD   A O3B   1 
HETATM 18135 O  O3B   B FAD   C 2  .    ? -36.992 48.549  83.674  0.42 21.18 ? 1301 FAD   A O3B   1 
HETATM 18136 C  C2B   A FAD   C 2  .    ? -37.203 48.323  86.041  0.58 19.82 ? 1301 FAD   A C2B   1 
HETATM 18137 C  C2B   B FAD   C 2  .    ? -37.167 48.308  86.030  0.42 19.80 ? 1301 FAD   A C2B   1 
HETATM 18138 O  O2B   A FAD   C 2  .    ? -38.430 48.942  85.877  0.58 18.86 ? 1301 FAD   A O2B   1 
HETATM 18139 O  O2B   B FAD   C 2  .    ? -38.348 49.016  85.923  0.42 19.06 ? 1301 FAD   A O2B   1 
HETATM 18140 C  C1B   A FAD   C 2  .    ? -37.384 47.120  86.897  0.58 19.01 ? 1301 FAD   A C1B   1 
HETATM 18141 C  C1B   B FAD   C 2  .    ? -37.381 47.104  86.878  0.42 19.04 ? 1301 FAD   A C1B   1 
HETATM 18142 N  N9A   A FAD   C 2  .    ? -36.299 46.844  87.810  0.58 20.42 ? 1301 FAD   A N9A   1 
HETATM 18143 N  N9A   B FAD   C 2  .    ? -36.304 46.829  87.797  0.42 20.46 ? 1301 FAD   A N9A   1 
HETATM 18144 C  C8A   A FAD   C 2  .    ? -35.009 46.458  87.483  0.58 22.62 ? 1301 FAD   A C8A   1 
HETATM 18145 C  C8A   B FAD   C 2  .    ? -35.016 46.442  87.470  0.42 22.60 ? 1301 FAD   A C8A   1 
HETATM 18146 N  N7A   A FAD   C 2  .    ? -34.297 46.285  88.601  0.58 21.73 ? 1301 FAD   A N7A   1 
HETATM 18147 N  N7A   B FAD   C 2  .    ? -34.301 46.273  88.587  0.42 21.75 ? 1301 FAD   A N7A   1 
HETATM 18148 C  C5A   A FAD   C 2  .    ? -35.101 46.537  89.701  0.58 20.87 ? 1301 FAD   A C5A   1 
HETATM 18149 C  C5A   B FAD   C 2  .    ? -35.099 46.534  89.689  0.42 20.91 ? 1301 FAD   A C5A   1 
HETATM 18150 C  C6A   A FAD   C 2  .    ? -34.913 46.511  91.072  0.58 22.34 ? 1301 FAD   A C6A   1 
HETATM 18151 C  C6A   B FAD   C 2  .    ? -34.901 46.515  91.059  0.42 22.33 ? 1301 FAD   A C6A   1 
HETATM 18152 N  N6A   A FAD   C 2  .    ? -33.636 46.149  91.629  0.58 22.02 ? 1301 FAD   A N6A   1 
HETATM 18153 N  N6A   B FAD   C 2  .    ? -33.619 46.153  91.605  0.42 22.08 ? 1301 FAD   A N6A   1 
HETATM 18154 N  N1A   A FAD   C 2  .    ? -35.931 46.821  91.888  0.58 21.93 ? 1301 FAD   A N1A   1 
HETATM 18155 N  N1A   B FAD   C 2  .    ? -35.913 46.832  91.883  0.42 21.92 ? 1301 FAD   A N1A   1 
HETATM 18156 C  C2A   A FAD   C 2  .    ? -37.155 47.160  91.408  0.58 21.56 ? 1301 FAD   A C2A   1 
HETATM 18157 C  C2A   B FAD   C 2  .    ? -37.138 47.172  91.408  0.42 21.54 ? 1301 FAD   A C2A   1 
HETATM 18158 N  N3A   A FAD   C 2  .    ? -37.372 47.193  90.069  0.58 21.28 ? 1301 FAD   A N3A   1 
HETATM 18159 N  N3A   B FAD   C 2  .    ? -37.365 47.198  90.069  0.42 21.28 ? 1301 FAD   A N3A   1 
HETATM 18160 C  C4A   A FAD   C 2  .    ? -36.383 46.896  89.211  0.58 22.34 ? 1301 FAD   A C4A   1 
HETATM 18161 C  C4A   B FAD   C 2  .    ? -36.383 46.894  89.203  0.42 22.30 ? 1301 FAD   A C4A   1 
HETATM 18162 N  N1    A FAD   C 2  .    ? -41.193 53.495  81.494  0.58 14.83 ? 1301 FAD   A N1    1 
HETATM 18163 N  N1    B FAD   C 2  .    ? -40.723 53.714  81.175  0.42 18.22 ? 1301 FAD   A N1    1 
HETATM 18164 C  C2    A FAD   C 2  .    ? -41.432 54.764  82.080  0.58 17.43 ? 1301 FAD   A C2    1 
HETATM 18165 C  C2    B FAD   C 2  .    ? -41.257 54.751  82.009  0.42 16.88 ? 1301 FAD   A C2    1 
HETATM 18166 O  O2    A FAD   C 2  .    ? -40.918 55.031  83.272  0.58 15.92 ? 1301 FAD   A O2    1 
HETATM 18167 O  O2    B FAD   C 2  .    ? -40.703 55.013  83.198  0.42 17.10 ? 1301 FAD   A O2    1 
HETATM 18168 N  N3    A FAD   C 2  .    ? -42.195 55.719  81.445  0.58 16.34 ? 1301 FAD   A N3    1 
HETATM 18169 N  N3    B FAD   C 2  .    ? -42.268 55.572  81.556  0.42 16.17 ? 1301 FAD   A N3    1 
HETATM 18170 C  C4    A FAD   C 2  .    ? -42.739 55.476  80.207  0.58 17.82 ? 1301 FAD   A C4    1 
HETATM 18171 C  C4    B FAD   C 2  .    ? -42.854 55.336  80.342  0.42 17.42 ? 1301 FAD   A C4    1 
HETATM 18172 O  O4    A FAD   C 2  .    ? -43.497 56.438  79.614  0.58 18.90 ? 1301 FAD   A O4    1 
HETATM 18173 O  O4    B FAD   C 2  .    ? -43.853 56.154  79.918  0.42 13.87 ? 1301 FAD   A O4    1 
HETATM 18174 C  C4X   A FAD   C 2  .    ? -42.541 54.158  79.549  0.58 16.02 ? 1301 FAD   A C4X   1 
HETATM 18175 C  C4X   B FAD   C 2  .    ? -42.505 54.115  79.565  0.42 16.08 ? 1301 FAD   A C4X   1 
HETATM 18176 N  N5    A FAD   C 2  .    ? -43.086 53.840  78.306  0.58 17.01 ? 1301 FAD   A N5    1 
HETATM 18177 N  N5    B FAD   C 2  .    ? -43.227 53.718  78.449  0.42 17.73 ? 1301 FAD   A N5    1 
HETATM 18178 C  C5X   A FAD   C 2  .    ? -42.871 52.565  77.774  0.58 17.51 ? 1301 FAD   A C5X   1 
HETATM 18179 C  C5X   B FAD   C 2  .    ? -42.872 52.548  77.780  0.42 17.53 ? 1301 FAD   A C5X   1 
HETATM 18180 C  C6    A FAD   C 2  .    ? -43.412 52.200  76.534  0.58 16.36 ? 1301 FAD   A C6    1 
HETATM 18181 C  C6    B FAD   C 2  .    ? -43.592 52.147  76.651  0.42 16.75 ? 1301 FAD   A C6    1 
HETATM 18182 C  C7    A FAD   C 2  .    ? -43.178 50.922  76.032  0.58 17.90 ? 1301 FAD   A C7    1 
HETATM 18183 C  C7    B FAD   C 2  .    ? -43.245 50.984  75.982  0.42 17.88 ? 1301 FAD   A C7    1 
HETATM 18184 C  C7M   A FAD   C 2  .    ? -43.764 50.520  74.709  0.58 19.77 ? 1301 FAD   A C7M   1 
HETATM 18185 C  C7M   B FAD   C 2  .    ? -44.054 50.581  74.779  0.42 17.95 ? 1301 FAD   A C7M   1 
HETATM 18186 C  C8    A FAD   C 2  .    ? -42.419 50.000  76.731  0.58 17.82 ? 1301 FAD   A C8    1 
HETATM 18187 C  C8    B FAD   C 2  .    ? -42.185 50.209  76.421  0.42 18.67 ? 1301 FAD   A C8    1 
HETATM 18188 C  C8M   A FAD   C 2  .    ? -42.168 48.625  76.187  0.58 18.63 ? 1301 FAD   A C8M   1 
HETATM 18189 C  C8M   B FAD   C 2  .    ? -41.795 48.953  75.705  0.42 21.11 ? 1301 FAD   A C8M   1 
HETATM 18190 C  C9    A FAD   C 2  .    ? -41.876 50.351  77.959  0.58 17.40 ? 1301 FAD   A C9    1 
HETATM 18191 C  C9    B FAD   C 2  .    ? -41.461 50.598  77.546  0.42 16.32 ? 1301 FAD   A C9    1 
HETATM 18192 C  C9A   A FAD   C 2  .    ? -42.102 51.622  78.469  0.58 19.40 ? 1301 FAD   A C9A   1 
HETATM 18193 C  C9A   B FAD   C 2  .    ? -41.803 51.761  78.217  0.42 17.29 ? 1301 FAD   A C9A   1 
HETATM 18194 N  N10   A FAD   C 2  .    ? -41.532 51.939  79.723  0.58 19.61 ? 1301 FAD   A N10   1 
HETATM 18195 N  N10   B FAD   C 2  .    ? -41.057 52.148  79.359  0.42 17.98 ? 1301 FAD   A N10   1 
HETATM 18196 C  C10   A FAD   C 2  .    ? -41.745 53.198  80.276  0.58 15.92 ? 1301 FAD   A C10   1 
HETATM 18197 C  C10   B FAD   C 2  .    ? -41.405 53.319  80.049  0.42 15.47 ? 1301 FAD   A C10   1 
HETATM 18198 C  "C1'" A FAD   C 2  .    ? -40.777 50.913  80.477  0.58 21.08 ? 1301 FAD   A "C1'" 1 
HETATM 18199 C  "C1'" B FAD   C 2  .    ? -39.920 51.321  79.818  0.42 20.05 ? 1301 FAD   A "C1'" 1 
HETATM 18200 C  "C2'" A FAD   C 2  .    ? -39.283 51.042  80.544  0.58 21.89 ? 1301 FAD   A "C2'" 1 
HETATM 18201 C  "C2'" B FAD   C 2  .    ? -40.397 50.271  80.806  0.42 21.52 ? 1301 FAD   A "C2'" 1 
HETATM 18202 O  "O2'" A FAD   C 2  .    ? -38.870 51.867  79.534  0.58 23.46 ? 1301 FAD   A "O2'" 1 
HETATM 18203 O  "O2'" B FAD   C 2  .    ? -40.887 50.901  81.912  0.42 18.44 ? 1301 FAD   A "O2'" 1 
HETATM 18204 C  "C3'" A FAD   C 2  .    ? -38.723 49.618  80.408  0.58 19.48 ? 1301 FAD   A "C3'" 1 
HETATM 18205 C  "C3'" B FAD   C 2  .    ? -39.275 49.303  81.210  0.42 21.79 ? 1301 FAD   A "C3'" 1 
HETATM 18206 O  "O3'" A FAD   C 2  .    ? -38.844 49.210  79.102  0.58 22.82 ? 1301 FAD   A "O3'" 1 
HETATM 18207 O  "O3'" B FAD   C 2  .    ? -38.204 49.994  81.736  0.42 20.33 ? 1301 FAD   A "O3'" 1 
HETATM 18208 C  "C4'" A FAD   C 2  .    ? -39.415 48.602  81.306  0.58 19.21 ? 1301 FAD   A "C4'" 1 
HETATM 18209 C  "C4'" B FAD   C 2  .    ? -38.772 48.425  80.080  0.42 22.23 ? 1301 FAD   A "C4'" 1 
HETATM 18210 O  "O4'" A FAD   C 2  .    ? -39.390 49.053  82.602  0.58 20.23 ? 1301 FAD   A "O4'" 1 
HETATM 18211 O  "O4'" B FAD   C 2  .    ? -39.772 48.212  79.155  0.42 22.68 ? 1301 FAD   A "O4'" 1 
HETATM 18212 C  "C5'" A FAD   C 2  .    ? -38.754 47.233  81.242  0.58 21.43 ? 1301 FAD   A "C5'" 1 
HETATM 18213 C  "C5'" B FAD   C 2  .    ? -38.222 47.105  80.618  0.42 21.41 ? 1301 FAD   A "C5'" 1 
HETATM 18214 O  "O5'" A FAD   C 2  .    ? -39.630 46.245  81.742  0.58 23.04 ? 1301 FAD   A "O5'" 1 
HETATM 18215 O  "O5'" B FAD   C 2  .    ? -39.231 46.346  81.255  0.42 21.08 ? 1301 FAD   A "O5'" 1 
HETATM 18216 P  P     A FAD   C 2  .    ? -39.731 44.928  80.851  0.58 21.55 ? 1301 FAD   A P     1 
HETATM 18217 P  P     B FAD   C 2  .    ? -39.677 44.948  80.607  0.42 21.80 ? 1301 FAD   A P     1 
HETATM 18218 O  O1P   A FAD   C 2  .    ? -39.734 45.146  79.296  0.58 20.74 ? 1301 FAD   A O1P   1 
HETATM 18219 O  O1P   B FAD   C 2  .    ? -39.986 44.935  79.064  0.42 24.75 ? 1301 FAD   A O1P   1 
HETATM 18220 O  O2P   A FAD   C 2  .    ? -40.920 44.153  81.533  0.58 24.13 ? 1301 FAD   A O2P   1 
HETATM 18221 O  O2P   B FAD   C 2  .    ? -40.826 44.563  81.605  0.42 23.24 ? 1301 FAD   A O2P   1 
HETATM 18222 O  O3P   A FAD   C 2  .    ? -38.424 44.116  81.373  0.58 20.73 ? 1301 FAD   A O3P   1 
HETATM 18223 O  O3P   B FAD   C 2  .    ? -38.527 43.908  81.107  0.42 21.64 ? 1301 FAD   A O3P   1 
HETATM 18224 C  C     . FMT   D 3  .    ? -40.188 61.344  102.784 0.76 17.18 ? 1302 FMT   A C     1 
HETATM 18225 O  O1    . FMT   D 3  .    ? -39.494 60.797  103.656 0.76 33.22 ? 1302 FMT   A O1    1 
HETATM 18226 O  O2    . FMT   D 3  .    ? -41.440 61.388  102.679 0.76 31.12 ? 1302 FMT   A O2    1 
HETATM 18227 C  C1    . PEG   E 4  .    ? -62.821 39.586  85.569  1.00 38.69 ? 1303 PEG   A C1    1 
HETATM 18228 O  O1    . PEG   E 4  .    ? -63.166 38.409  84.863  1.00 45.42 ? 1303 PEG   A O1    1 
HETATM 18229 C  C2    . PEG   E 4  .    ? -61.580 40.218  84.985  1.00 41.17 ? 1303 PEG   A C2    1 
HETATM 18230 O  O2    . PEG   E 4  .    ? -60.417 39.498  85.329  1.00 40.43 ? 1303 PEG   A O2    1 
HETATM 18231 C  C3    . PEG   E 4  .    ? -59.517 40.242  86.116  1.00 36.99 ? 1303 PEG   A C3    1 
HETATM 18232 C  C4    . PEG   E 4  .    ? -58.250 39.462  86.372  1.00 38.19 ? 1303 PEG   A C4    1 
HETATM 18233 O  O4    . PEG   E 4  .    ? -58.376 38.148  85.869  1.00 35.54 ? 1303 PEG   A O4    1 
HETATM 18234 C  C1    . PEG   F 4  .    ? -0.661  62.883  96.975  1.00 32.42 ? 1304 PEG   A C1    1 
HETATM 18235 O  O1    . PEG   F 4  .    ? -1.420  61.772  96.548  1.00 37.53 ? 1304 PEG   A O1    1 
HETATM 18236 C  C2    . PEG   F 4  .    ? 0.706   62.830  96.347  1.00 40.29 ? 1304 PEG   A C2    1 
HETATM 18237 O  O2    . PEG   F 4  .    ? 1.358   61.668  96.777  1.00 43.19 ? 1304 PEG   A O2    1 
HETATM 18238 C  C3    . PEG   F 4  .    ? 2.261   61.154  95.825  1.00 46.19 ? 1304 PEG   A C3    1 
HETATM 18239 C  C4    . PEG   F 4  .    ? 2.657   59.744  96.197  1.00 43.06 ? 1304 PEG   A C4    1 
HETATM 18240 O  O4    . PEG   F 4  .    ? 1.844   58.805  95.528  1.00 50.93 ? 1304 PEG   A O4    1 
HETATM 18241 P  PA    . NAD   G 5  .    ? -18.118 88.290  107.200 1.00 21.12 ? 1305 NAD   A PA    1 
HETATM 18242 O  O1A   . NAD   G 5  .    ? -16.609 88.240  106.942 1.00 21.40 ? 1305 NAD   A O1A   1 
HETATM 18243 O  O2A   . NAD   G 5  .    ? -18.831 89.501  106.829 1.00 21.91 ? 1305 NAD   A O2A   1 
HETATM 18244 O  O5B   . NAD   G 5  .    ? -18.569 88.041  108.608 1.00 20.96 ? 1305 NAD   A O5B   1 
HETATM 18245 C  C5B   . NAD   G 5  .    ? -18.271 86.806  109.218 1.00 20.05 ? 1305 NAD   A C5B   1 
HETATM 18246 C  C4B   . NAD   G 5  .    ? -18.268 86.873  110.743 1.00 19.69 ? 1305 NAD   A C4B   1 
HETATM 18247 O  O4B   . NAD   G 5  .    ? -17.144 87.603  111.185 1.00 20.86 ? 1305 NAD   A O4B   1 
HETATM 18248 C  C3B   . NAD   G 5  .    ? -19.494 87.492  111.359 1.00 19.70 ? 1305 NAD   A C3B   1 
HETATM 18249 O  O3B   . NAD   G 5  .    ? -19.874 86.811  112.497 1.00 21.42 ? 1305 NAD   A O3B   1 
HETATM 18250 C  C2B   . NAD   G 5  .    ? -19.038 88.860  111.650 1.00 22.78 ? 1305 NAD   A C2B   1 
HETATM 18251 O  O2B   . NAD   G 5  .    ? -19.776 89.458  112.659 1.00 22.58 ? 1305 NAD   A O2B   1 
HETATM 18252 C  C1B   . NAD   G 5  .    ? -17.648 88.591  112.061 1.00 24.31 ? 1305 NAD   A C1B   1 
HETATM 18253 N  N9A   . NAD   G 5  .    ? -16.768 89.725  111.976 1.00 22.26 ? 1305 NAD   A N9A   1 
HETATM 18254 C  C8A   . NAD   G 5  .    ? -16.842 90.811  111.124 1.00 22.11 ? 1305 NAD   A C8A   1 
HETATM 18255 N  N7A   . NAD   G 5  .    ? -15.796 91.609  111.344 1.00 23.31 ? 1305 NAD   A N7A   1 
HETATM 18256 C  C5A   . NAD   G 5  .    ? -15.003 91.062  112.339 1.00 21.00 ? 1305 NAD   A C5A   1 
HETATM 18257 C  C6A   . NAD   G 5  .    ? -13.829 91.426  112.972 1.00 25.23 ? 1305 NAD   A C6A   1 
HETATM 18258 N  N6A   . NAD   G 5  .    ? -13.156 92.638  112.611 1.00 27.30 ? 1305 NAD   A N6A   1 
HETATM 18259 N  N1A   . NAD   G 5  .    ? -13.320 90.637  113.918 1.00 25.24 ? 1305 NAD   A N1A   1 
HETATM 18260 C  C2A   . NAD   G 5  .    ? -13.902 89.475  114.305 1.00 24.48 ? 1305 NAD   A C2A   1 
HETATM 18261 N  N3A   . NAD   G 5  .    ? -15.063 89.090  113.715 1.00 22.25 ? 1305 NAD   A N3A   1 
HETATM 18262 C  C4A   . NAD   G 5  .    ? -15.608 89.853  112.750 1.00 22.44 ? 1305 NAD   A C4A   1 
HETATM 18263 O  O3    . NAD   G 5  .    ? -18.843 87.238  106.385 1.00 21.01 ? 1305 NAD   A O3    1 
HETATM 18264 P  PN    . NAD   G 5  .    ? -20.376 86.889  106.088 1.00 21.36 ? 1305 NAD   A PN    1 
HETATM 18265 O  O1N   . NAD   G 5  .    ? -20.891 87.954  105.180 1.00 22.66 ? 1305 NAD   A O1N   1 
HETATM 18266 O  O2N   . NAD   G 5  .    ? -21.178 86.681  107.342 1.00 21.95 ? 1305 NAD   A O2N   1 
HETATM 18267 O  O5D   . NAD   G 5  .    ? -20.315 85.514  105.291 1.00 22.27 ? 1305 NAD   A O5D   1 
HETATM 18268 C  C5D   . NAD   G 5  .    ? -19.960 85.511  103.929 1.00 22.08 ? 1305 NAD   A C5D   1 
HETATM 18269 C  C4D   . NAD   G 5  .    ? -18.510 85.113  103.690 1.00 19.60 ? 1305 NAD   A C4D   1 
HETATM 18270 O  O4D   . NAD   G 5  .    ? -18.205 83.905  104.326 1.00 20.16 ? 1305 NAD   A O4D   1 
HETATM 18271 C  C3D   . NAD   G 5  .    ? -18.211 84.965  102.233 1.00 21.10 ? 1305 NAD   A C3D   1 
HETATM 18272 O  O3D   . NAD   G 5  .    ? -17.032 85.572  101.909 1.00 22.77 ? 1305 NAD   A O3D   1 
HETATM 18273 C  C2D   . NAD   G 5  .    ? -18.117 83.506  102.077 1.00 20.81 ? 1305 NAD   A C2D   1 
HETATM 18274 O  O2D   . NAD   G 5  .    ? -17.373 83.086  100.980 1.00 21.43 ? 1305 NAD   A O2D   1 
HETATM 18275 C  C1D   . NAD   G 5  .    ? -17.539 83.107  103.381 1.00 20.05 ? 1305 NAD   A C1D   1 
HETATM 18276 N  N1N   . NAD   G 5  .    ? -17.830 81.735  103.670 1.00 17.41 ? 1305 NAD   A N1N   1 
HETATM 18277 C  C2N   . NAD   G 5  .    ? -16.807 80.755  103.614 1.00 18.27 ? 1305 NAD   A C2N   1 
HETATM 18278 C  C3N   . NAD   G 5  .    ? -17.152 79.436  103.890 1.00 19.03 ? 1305 NAD   A C3N   1 
HETATM 18279 C  C7N   . NAD   G 5  .    ? -16.156 78.330  103.842 1.00 17.50 ? 1305 NAD   A C7N   1 
HETATM 18280 O  O7N   . NAD   G 5  .    ? -16.473 77.207  104.222 1.00 20.86 ? 1305 NAD   A O7N   1 
HETATM 18281 N  N7N   . NAD   G 5  .    ? -14.869 78.591  103.314 1.00 18.49 ? 1305 NAD   A N7N   1 
HETATM 18282 C  C4N   . NAD   G 5  .    ? -18.483 79.120  104.248 1.00 33.60 ? 1305 NAD   A C4N   1 
HETATM 18283 C  C5N   . NAD   G 5  .    ? -19.506 80.087  104.260 1.00 26.00 ? 1305 NAD   A C5N   1 
HETATM 18284 C  C6N   . NAD   G 5  .    ? -19.165 81.393  103.975 1.00 18.53 ? 1305 NAD   A C6N   1 
HETATM 18285 S  S     . SO4   H 6  .    ? -9.168  52.760  110.994 1.00 20.71 ? 1306 SO4   A S     1 
HETATM 18286 O  O1    . SO4   H 6  .    ? -8.100  52.983  109.982 1.00 21.43 ? 1306 SO4   A O1    1 
HETATM 18287 O  O2    . SO4   H 6  .    ? -10.233 51.913  110.392 1.00 24.09 ? 1306 SO4   A O2    1 
HETATM 18288 O  O3    . SO4   H 6  .    ? -8.632  52.028  112.206 1.00 20.57 ? 1306 SO4   A O3    1 
HETATM 18289 O  O4    . SO4   H 6  .    ? -9.701  54.094  111.396 1.00 24.06 ? 1306 SO4   A O4    1 
HETATM 18290 S  S     . SO4   I 6  .    ? 12.674  75.307  125.800 0.67 35.18 ? 1307 SO4   A S     1 
HETATM 18291 O  O1    . SO4   I 6  .    ? 13.466  75.673  124.577 0.67 36.41 ? 1307 SO4   A O1    1 
HETATM 18292 O  O2    . SO4   I 6  .    ? 11.317  74.801  125.417 0.67 33.50 ? 1307 SO4   A O2    1 
HETATM 18293 O  O3    . SO4   I 6  .    ? 13.427  74.236  126.529 0.67 40.70 ? 1307 SO4   A O3    1 
HETATM 18294 O  O4    . SO4   I 6  .    ? 12.511  76.510  126.681 0.67 49.73 ? 1307 SO4   A O4    1 
HETATM 18295 S  S     . SO4   J 6  .    ? 29.434  71.065  105.715 0.79 51.41 ? 1308 SO4   A S     1 
HETATM 18296 O  O1    . SO4   J 6  .    ? 29.564  70.500  104.333 0.79 54.41 ? 1308 SO4   A O1    1 
HETATM 18297 O  O2    . SO4   J 6  .    ? 27.996  71.354  106.012 0.79 51.72 ? 1308 SO4   A O2    1 
HETATM 18298 O  O3    . SO4   J 6  .    ? 29.968  70.072  106.701 0.79 52.67 ? 1308 SO4   A O3    1 
HETATM 18299 O  O4    . SO4   J 6  .    ? 30.213  72.343  105.809 0.79 48.94 ? 1308 SO4   A O4    1 
HETATM 18300 S  S     . SO4   K 6  .    ? -34.317 24.658  79.719  0.69 43.83 ? 1309 SO4   A S     1 
HETATM 18301 O  O1    . SO4   K 6  .    ? -33.439 25.651  79.014  0.69 41.82 ? 1309 SO4   A O1    1 
HETATM 18302 O  O2    . SO4   K 6  .    ? -35.491 24.328  78.852  0.69 45.22 ? 1309 SO4   A O2    1 
HETATM 18303 O  O3    . SO4   K 6  .    ? -33.531 23.407  79.977  0.69 57.04 ? 1309 SO4   A O3    1 
HETATM 18304 O  O4    . SO4   K 6  .    ? -34.776 25.211  81.036  0.69 39.81 ? 1309 SO4   A O4    1 
HETATM 18305 S  S     . SO4   L 6  .    ? -12.335 75.176  70.201  0.53 34.18 ? 1310 SO4   A S     1 
HETATM 18306 O  O1    . SO4   L 6  .    ? -11.127 75.068  71.070  0.53 28.70 ? 1310 SO4   A O1    1 
HETATM 18307 O  O2    . SO4   L 6  .    ? -12.439 76.575  69.677  0.53 38.87 ? 1310 SO4   A O2    1 
HETATM 18308 O  O3    . SO4   L 6  .    ? -12.158 74.236  69.048  0.53 42.10 ? 1310 SO4   A O3    1 
HETATM 18309 O  O4    . SO4   L 6  .    ? -13.576 74.820  70.960  0.53 26.07 ? 1310 SO4   A O4    1 
HETATM 18310 MG MG    . MG    M 7  .    ? -19.829 91.277  107.047 1.00 25.49 ? 1311 MG    A MG    1 
HETATM 18311 P  PA    A FAD   N 2  .    ? -17.148 22.996  104.100 0.73 20.74 ? 1301 FAD   B PA    1 
HETATM 18312 P  PA    B FAD   N 2  .    ? -17.081 22.922  104.209 0.27 20.99 ? 1301 FAD   B PA    1 
HETATM 18313 O  O1A   A FAD   N 2  .    ? -17.397 24.514  104.234 0.73 25.46 ? 1301 FAD   B O1A   1 
HETATM 18314 O  O1A   B FAD   N 2  .    ? -17.469 24.414  104.027 0.27 25.66 ? 1301 FAD   B O1A   1 
HETATM 18315 O  O2A   A FAD   N 2  .    ? -18.262 22.096  103.891 0.73 23.14 ? 1301 FAD   B O2A   1 
HETATM 18316 O  O2A   B FAD   N 2  .    ? -18.100 21.914  104.044 0.27 24.10 ? 1301 FAD   B O2A   1 
HETATM 18317 O  O5B   A FAD   N 2  .    ? -16.235 22.604  102.958 0.73 19.45 ? 1301 FAD   B O5B   1 
HETATM 18318 O  O5B   B FAD   N 2  .    ? -16.049 22.383  103.289 0.27 21.35 ? 1301 FAD   B O5B   1 
HETATM 18319 C  C5B   A FAD   N 2  .    ? -15.148 23.466  102.630 0.73 21.99 ? 1301 FAD   B C5B   1 
HETATM 18320 C  C5B   B FAD   N 2  .    ? -15.138 23.308  102.720 0.27 21.99 ? 1301 FAD   B C5B   1 
HETATM 18321 C  C4B   A FAD   N 2  .    ? -14.172 22.746  101.703 0.73 19.61 ? 1301 FAD   B C4B   1 
HETATM 18322 C  C4B   B FAD   N 2  .    ? -14.205 22.599  101.748 0.27 19.70 ? 1301 FAD   B C4B   1 
HETATM 18323 O  O4B   A FAD   N 2  .    ? -14.671 22.691  100.404 0.73 20.09 ? 1301 FAD   B O4B   1 
HETATM 18324 O  O4B   B FAD   N 2  .    ? -14.700 22.600  100.446 0.27 20.11 ? 1301 FAD   B O4B   1 
HETATM 18325 C  C3B   A FAD   N 2  .    ? -12.835 23.397  101.547 0.73 17.88 ? 1301 FAD   B C3B   1 
HETATM 18326 C  C3B   B FAD   N 2  .    ? -12.866 23.247  101.675 0.27 18.38 ? 1301 FAD   B C3B   1 
HETATM 18327 O  O3B   A FAD   N 2  .    ? -11.980 23.230  102.623 0.73 17.33 ? 1301 FAD   B O3B   1 
HETATM 18328 O  O3B   B FAD   N 2  .    ? -12.020 22.828  102.679 0.27 18.76 ? 1301 FAD   B O3B   1 
HETATM 18329 C  C2B   A FAD   N 2  .    ? -12.344 22.710  100.325 0.73 17.77 ? 1301 FAD   B C2B   1 
HETATM 18330 C  C2B   B FAD   N 2  .    ? -12.366 22.809  100.355 0.27 17.98 ? 1301 FAD   B C2B   1 
HETATM 18331 O  O2B   A FAD   N 2  .    ? -11.984 21.408  100.550 0.73 18.22 ? 1301 FAD   B O2B   1 
HETATM 18332 O  O2B   B FAD   N 2  .    ? -11.694 21.622  100.441 0.27 20.10 ? 1301 FAD   B O2B   1 
HETATM 18333 C  C1B   A FAD   N 2  .    ? -13.591 22.666  99.516  0.73 18.85 ? 1301 FAD   B C1B   1 
HETATM 18334 C  C1B   B FAD   N 2  .    ? -13.613 22.627  99.565  0.27 18.89 ? 1301 FAD   B C1B   1 
HETATM 18335 N  N9A   A FAD   N 2  .    ? -13.787 23.739  98.578  0.73 19.37 ? 1301 FAD   B N9A   1 
HETATM 18336 N  N9A   B FAD   N 2  .    ? -13.828 23.682  98.609  0.27 19.35 ? 1301 FAD   B N9A   1 
HETATM 18337 C  C8A   A FAD   N 2  .    ? -13.912 25.093  98.818  0.73 20.78 ? 1301 FAD   B C8A   1 
HETATM 18338 C  C8A   B FAD   N 2  .    ? -13.984 25.027  98.882  0.27 20.72 ? 1301 FAD   B C8A   1 
HETATM 18339 N  N7A   A FAD   N 2  .    ? -14.081 25.754  97.670  0.73 21.00 ? 1301 FAD   B N7A   1 
HETATM 18340 N  N7A   B FAD   N 2  .    ? -14.156 25.705  97.744  0.27 21.03 ? 1301 FAD   B N7A   1 
HETATM 18341 C  C5A   A FAD   N 2  .    ? -14.089 24.836  96.631  0.73 17.74 ? 1301 FAD   B C5A   1 
HETATM 18342 C  C5A   B FAD   N 2  .    ? -14.122 24.821  96.677  0.27 17.89 ? 1301 FAD   B C5A   1 
HETATM 18343 C  C6A   A FAD   N 2  .    ? -14.243 24.925  95.260  0.73 19.02 ? 1301 FAD   B C6A   1 
HETATM 18344 C  C6A   B FAD   N 2  .    ? -14.248 24.956  95.304  0.27 19.08 ? 1301 FAD   B C6A   1 
HETATM 18345 N  N6A   A FAD   N 2  .    ? -14.450 26.201  94.635  0.73 20.11 ? 1301 FAD   B N6A   1 
HETATM 18346 N  N6A   B FAD   N 2  .    ? -14.470 26.255  94.722  0.27 20.18 ? 1301 FAD   B N6A   1 
HETATM 18347 N  N1A   A FAD   N 2  .    ? -14.192 23.796  94.538  0.73 18.40 ? 1301 FAD   B N1A   1 
HETATM 18348 N  N1A   B FAD   N 2  .    ? -14.162 23.864  94.526  0.27 18.43 ? 1301 FAD   B N1A   1 
HETATM 18349 C  C2A   A FAD   N 2  .    ? -14.016 22.579  95.102  0.73 16.36 ? 1301 FAD   B C2A   1 
HETATM 18350 C  C2A   B FAD   N 2  .    ? -13.962 22.627  95.048  0.27 16.51 ? 1301 FAD   B C2A   1 
HETATM 18351 N  N3A   A FAD   N 2  .    ? -13.871 22.451  96.442  0.73 17.78 ? 1301 FAD   B N3A   1 
HETATM 18352 N  N3A   B FAD   N 2  .    ? -13.837 22.462  96.390  0.27 17.87 ? 1301 FAD   B N3A   1 
HETATM 18353 C  C4A   A FAD   N 2  .    ? -13.897 23.550  97.196  0.73 18.34 ? 1301 FAD   B C4A   1 
HETATM 18354 C  C4A   B FAD   N 2  .    ? -13.907 23.521  97.209  0.27 18.41 ? 1301 FAD   B C4A   1 
HETATM 18355 N  N1    A FAD   N 2  .    ? -7.584  18.361  104.936 0.73 15.24 ? 1301 FAD   B N1    1 
HETATM 18356 N  N1    B FAD   N 2  .    ? -7.258  18.730  105.156 0.27 17.23 ? 1301 FAD   B N1    1 
HETATM 18357 C  C2    A FAD   N 2  .    ? -6.426  17.868  104.290 0.73 17.03 ? 1301 FAD   B C2    1 
HETATM 18358 C  C2    B FAD   N 2  .    ? -6.259  18.064  104.367 0.27 16.97 ? 1301 FAD   B C2    1 
HETATM 18359 O  O2    A FAD   N 2  .    ? -6.219  18.310  103.053 0.73 15.89 ? 1301 FAD   B O2    1 
HETATM 18360 O  O2    B FAD   N 2  .    ? -5.936  18.576  103.155 0.27 18.77 ? 1301 FAD   B O2    1 
HETATM 18361 N  N3    A FAD   N 2  .    ? -5.568  16.982  104.884 0.73 17.35 ? 1301 FAD   B N3    1 
HETATM 18362 N  N3    B FAD   N 2  .    ? -5.593  16.954  104.848 0.27 17.35 ? 1301 FAD   B N3    1 
HETATM 18363 C  C4    A FAD   N 2  .    ? -5.794  16.543  106.161 0.73 16.86 ? 1301 FAD   B C4    1 
HETATM 18364 C  C4    B FAD   N 2  .    ? -5.906  16.424  106.080 0.27 17.14 ? 1301 FAD   B C4    1 
HETATM 18365 O  O4    A FAD   N 2  .    ? -4.936  15.654  106.714 0.73 18.45 ? 1301 FAD   B O4    1 
HETATM 18366 O  O4    B FAD   N 2  .    ? -5.233  15.318  106.532 0.27 15.28 ? 1301 FAD   B O4    1 
HETATM 18367 C  C4X   A FAD   N 2  .    ? -7.005  17.005  106.885 0.73 17.12 ? 1301 FAD   B C4X   1 
HETATM 18368 C  C4X   B FAD   N 2  .    ? -7.028  17.010  106.876 0.27 17.20 ? 1301 FAD   B C4X   1 
HETATM 18369 N  N5    A FAD   N 2  .    ? -7.317  16.563  108.164 0.73 18.87 ? 1301 FAD   B N5    1 
HETATM 18370 N  N5    B FAD   N 2  .    ? -7.457  16.441  108.070 0.27 18.90 ? 1301 FAD   B N5    1 
HETATM 18371 C  C5X   A FAD   N 2  .    ? -8.482  17.025  108.758 0.73 18.17 ? 1301 FAD   B C5X   1 
HETATM 18372 C  C5X   B FAD   N 2  .    ? -8.515  17.012  108.770 0.27 18.22 ? 1301 FAD   B C5X   1 
HETATM 18373 C  C6    A FAD   N 2  .    ? -8.824  16.596  110.043 0.73 17.72 ? 1301 FAD   B C6    1 
HETATM 18374 C  C6    B FAD   N 2  .    ? -8.937  16.438  109.974 0.27 17.85 ? 1301 FAD   B C6    1 
HETATM 18375 C  C7    A FAD   N 2  .    ? -9.995  17.069  110.623 0.73 18.41 ? 1301 FAD   B C7    1 
HETATM 18376 C  C7    B FAD   N 2  .    ? -9.993  17.001  110.676 0.27 18.49 ? 1301 FAD   B C7    1 
HETATM 18377 C  C7M   A FAD   N 2  .    ? -10.382 16.613  112.004 0.73 21.15 ? 1301 FAD   B C7M   1 
HETATM 18378 C  C7M   B FAD   N 2  .    ? -10.436 16.364  111.968 0.27 20.19 ? 1301 FAD   B C7M   1 
HETATM 18379 C  C8    A FAD   N 2  .    ? -10.824 17.945  109.957 0.73 18.07 ? 1301 FAD   B C8    1 
HETATM 18380 C  C8    B FAD   N 2  .    ? -10.632 18.129  110.199 0.27 18.75 ? 1301 FAD   B C8    1 
HETATM 18381 C  C8M   A FAD   N 2  .    ? -12.088 18.457  110.574 0.73 19.79 ? 1301 FAD   B C8M   1 
HETATM 18382 C  C8M   B FAD   N 2  .    ? -11.769 18.745  110.952 0.27 20.05 ? 1301 FAD   B C8M   1 
HETATM 18383 C  C9    A FAD   N 2  .    ? -10.489 18.370  108.685 0.73 19.10 ? 1301 FAD   B C9    1 
HETATM 18384 C  C9    B FAD   N 2  .    ? -10.218 18.709  109.004 0.27 18.03 ? 1301 FAD   B C9    1 
HETATM 18385 C  C9A   A FAD   N 2  .    ? -9.326  17.916  108.103 0.73 18.46 ? 1301 FAD   B C9A   1 
HETATM 18386 C  C9A   B FAD   N 2  .    ? -9.164  18.149  108.296 0.27 17.04 ? 1301 FAD   B C9A   1 
HETATM 18387 N  N10   A FAD   N 2  .    ? -9.011  18.383  106.799 0.73 19.85 ? 1301 FAD   B N10   1 
HETATM 18388 N  N10   B FAD   N 2  .    ? -8.746  18.751  107.074 0.27 17.55 ? 1301 FAD   B N10   1 
HETATM 18389 C  C10   A FAD   N 2  .    ? -7.864  17.918  106.191 0.73 18.54 ? 1301 FAD   B C10   1 
HETATM 18390 C  C10   B FAD   N 2  .    ? -7.680  18.184  106.352 0.27 17.85 ? 1301 FAD   B C10   1 
HETATM 18391 C  "C1'" A FAD   N 2  .    ? -9.949  19.269  106.066 0.73 20.96 ? 1301 FAD   B "C1'" 1 
HETATM 18392 C  "C1'" B FAD   N 2  .    ? -9.434  19.956  106.566 0.27 20.25 ? 1301 FAD   B "C1'" 1 
HETATM 18393 C  "C2'" A FAD   N 2  .    ? -9.640  20.734  105.886 0.73 23.68 ? 1301 FAD   B "C2'" 1 
HETATM 18394 C  "C2'" B FAD   N 2  .    ? -10.593 19.511  105.687 0.27 20.21 ? 1301 FAD   B "C2'" 1 
HETATM 18395 O  "O2'" A FAD   N 2  .    ? -8.718  21.165  106.811 0.73 22.44 ? 1301 FAD   B "O2'" 1 
HETATM 18396 O  "O2'" B FAD   N 2  .    ? -10.110 18.821  104.605 0.27 18.27 ? 1301 FAD   B "O2'" 1 
HETATM 18397 C  "C3'" A FAD   N 2  .    ? -10.977 21.479  106.021 0.73 21.36 ? 1301 FAD   B "C3'" 1 
HETATM 18398 C  "C3'" B FAD   N 2  .    ? -11.435 20.695  105.204 0.27 22.15 ? 1301 FAD   B "C3'" 1 
HETATM 18399 O  "O3'" A FAD   N 2  .    ? -11.368 21.502  107.343 0.73 22.03 ? 1301 FAD   B "O3'" 1 
HETATM 18400 O  "O3'" B FAD   N 2  .    ? -10.609 21.593  104.570 0.27 21.04 ? 1301 FAD   B "O3'" 1 
HETATM 18401 C  "C4'" A FAD   N 2  .    ? -12.109 20.870  105.211 0.73 23.85 ? 1301 FAD   B "C4'" 1 
HETATM 18402 C  "C4'" B FAD   N 2  .    ? -12.208 21.426  106.287 0.27 23.55 ? 1301 FAD   B "C4'" 1 
HETATM 18403 O  "O4'" A FAD   N 2  .    ? -11.771 20.860  103.873 0.73 20.66 ? 1301 FAD   B "O4'" 1 
HETATM 18404 O  "O4'" B FAD   N 2  .    ? -12.620 20.546  107.261 0.27 22.48 ? 1301 FAD   B "O4'" 1 
HETATM 18405 C  "C5'" A FAD   N 2  .    ? -13.402 21.646  105.428 0.73 20.92 ? 1301 FAD   B "C5'" 1 
HETATM 18406 C  "C5'" B FAD   N 2  .    ? -13.390 22.186  105.691 0.27 21.37 ? 1301 FAD   B "C5'" 1 
HETATM 18407 O  "O5'" A FAD   N 2  .    ? -14.528 20.894  105.008 0.73 19.33 ? 1301 FAD   B "O5'" 1 
HETATM 18408 O  "O5'" B FAD   N 2  .    ? -14.393 21.300  105.232 0.27 20.26 ? 1301 FAD   B "O5'" 1 
HETATM 18409 P  P     A FAD   N 2  .    ? -15.871 21.064  105.874 0.73 20.62 ? 1301 FAD   B P     1 
HETATM 18410 P  P     B FAD   N 2  .    ? -15.772 21.222  106.044 0.27 22.76 ? 1301 FAD   B P     1 
HETATM 18411 O  O1P   A FAD   N 2  .    ? -15.599 21.077  107.424 0.73 21.48 ? 1301 FAD   B O1P   1 
HETATM 18412 O  O1P   B FAD   N 2  .    ? -15.666 20.989  107.599 0.27 22.54 ? 1301 FAD   B O1P   1 
HETATM 18413 O  O2P   A FAD   N 2  .    ? -16.835 19.978  105.286 0.73 26.00 ? 1301 FAD   B O2P   1 
HETATM 18414 O  O2P   B FAD   N 2  .    ? -16.523 20.133  105.199 0.27 24.33 ? 1301 FAD   B O2P   1 
HETATM 18415 O  O3P   A FAD   N 2  .    ? -16.467 22.452  105.301 0.73 22.61 ? 1301 FAD   B O3P   1 
HETATM 18416 O  O3P   B FAD   N 2  .    ? -16.565 22.537  105.535 0.27 23.48 ? 1301 FAD   B O3P   1 
HETATM 18417 C  C1    . PGE   O 8  .    ? 1.300   59.868  87.334  1.00 39.62 ? 1302 PGE   B C1    1 
HETATM 18418 O  O1    . PGE   O 8  .    ? -0.093  59.652  87.314  1.00 43.02 ? 1302 PGE   B O1    1 
HETATM 18419 C  C2    . PGE   O 8  .    ? 1.930   59.142  86.175  1.00 37.44 ? 1302 PGE   B C2    1 
HETATM 18420 O  O2    . PGE   O 8  .    ? 3.306   58.949  86.420  1.00 45.77 ? 1302 PGE   B O2    1 
HETATM 18421 C  C3    . PGE   O 8  .    ? 4.019   58.330  85.373  1.00 33.01 ? 1302 PGE   B C3    1 
HETATM 18422 C  C4    . PGE   O 8  .    ? 4.580   56.959  85.696  1.00 33.36 ? 1302 PGE   B C4    1 
HETATM 18423 O  O4    . PGE   O 8  .    ? 2.117   54.436  87.629  1.00 43.24 ? 1302 PGE   B O4    1 
HETATM 18424 C  C6    . PGE   O 8  .    ? 2.775   53.884  86.512  1.00 40.94 ? 1302 PGE   B C6    1 
HETATM 18425 C  C5    . PGE   O 8  .    ? 3.984   54.748  86.203  1.00 38.32 ? 1302 PGE   B C5    1 
HETATM 18426 O  O3    . PGE   O 8  .    ? 3.550   56.077  86.065  1.00 40.04 ? 1302 PGE   B O3    1 
HETATM 18427 C  C     . FMT   P 3  .    ? -0.978  16.820  83.095  0.88 11.45 ? 1303 FMT   B C     1 
HETATM 18428 O  O1    . FMT   P 3  .    ? -1.205  15.612  83.338  0.88 34.06 ? 1303 FMT   B O1    1 
HETATM 18429 O  O2    . FMT   P 3  .    ? -1.377  17.513  82.154  0.88 33.13 ? 1303 FMT   B O2    1 
HETATM 18430 C  C10   . A1BDW Q 9  .    ? -4.225  18.538  108.356 0.68 20.94 ? 1304 A1BDW B C10   1 
HETATM 18431 C  C02   . A1BDW Q 9  .    ? -3.059  19.314  106.231 0.68 27.87 ? 1304 A1BDW B C02   1 
HETATM 18432 C  C03   . A1BDW Q 9  .    ? -4.122  19.447  107.312 0.68 24.69 ? 1304 A1BDW B C03   1 
HETATM 18433 C  C04   . A1BDW Q 9  .    ? -4.983  20.522  107.229 0.68 23.31 ? 1304 A1BDW B C04   1 
HETATM 18434 C  C05   . A1BDW Q 9  .    ? -5.966  20.697  108.177 0.68 23.90 ? 1304 A1BDW B C05   1 
HETATM 18435 C  C06   . A1BDW Q 9  .    ? -6.080  19.798  109.217 0.68 20.18 ? 1304 A1BDW B C06   1 
HETATM 18436 C  C07   . A1BDW Q 9  .    ? -7.176  20.026  110.251 0.68 25.19 ? 1304 A1BDW B C07   1 
HETATM 18437 C  C09   . A1BDW Q 9  .    ? -5.218  18.716  109.305 0.68 21.19 ? 1304 A1BDW B C09   1 
HETATM 18438 O  O01   . A1BDW Q 9  .    ? -2.583  18.002  106.183 0.68 24.83 ? 1304 A1BDW B O01   1 
HETATM 18439 O  O08   . A1BDW Q 9  .    ? -7.387  21.410  110.330 0.68 33.12 ? 1304 A1BDW B O08   1 
HETATM 18440 C  C1    . PEG   R 4  .    ? 22.814  13.579  96.691  0.69 32.98 ? 1305 PEG   B C1    1 
HETATM 18441 O  O1    . PEG   R 4  .    ? 24.130  13.557  96.193  0.69 36.94 ? 1305 PEG   B O1    1 
HETATM 18442 C  C2    . PEG   R 4  .    ? 22.758  14.423  97.937  0.69 35.02 ? 1305 PEG   B C2    1 
HETATM 18443 O  O2    . PEG   R 4  .    ? 21.547  14.196  98.611  0.69 38.19 ? 1305 PEG   B O2    1 
HETATM 18444 C  C3    . PEG   R 4  .    ? 21.477  14.876  99.838  0.69 33.83 ? 1305 PEG   B C3    1 
HETATM 18445 C  C4    . PEG   R 4  .    ? 21.960  13.989  100.954 0.69 36.00 ? 1305 PEG   B C4    1 
HETATM 18446 O  O4    . PEG   R 4  .    ? 21.469  14.480  102.177 0.69 35.31 ? 1305 PEG   B O4    1 
HETATM 18447 P  PA    . NAD   S 5  .    ? 27.558  35.487  75.288  1.00 15.87 ? 1306 NAD   B PA    1 
HETATM 18448 O  O1A   . NAD   S 5  .    ? 27.617  37.027  75.257  1.00 16.63 ? 1306 NAD   B O1A   1 
HETATM 18449 O  O2A   . NAD   S 5  .    ? 28.785  34.738  75.585  1.00 17.71 ? 1306 NAD   B O2A   1 
HETATM 18450 O  O5B   . NAD   S 5  .    ? 27.154  34.919  73.947  1.00 16.24 ? 1306 NAD   B O5B   1 
HETATM 18451 C  C5B   . NAD   S 5  .    ? 25.906  35.273  73.380  1.00 16.12 ? 1306 NAD   B C5B   1 
HETATM 18452 C  C4B   . NAD   S 5  .    ? 25.879  35.108  71.863  1.00 15.96 ? 1306 NAD   B C4B   1 
HETATM 18453 O  O4B   . NAD   S 5  .    ? 26.667  36.096  71.220  1.00 15.70 ? 1306 NAD   B O4B   1 
HETATM 18454 C  C3B   . NAD   S 5  .    ? 26.336  33.761  71.373  1.00 15.85 ? 1306 NAD   B C3B   1 
HETATM 18455 O  O3B   . NAD   S 5  .    ? 25.582  33.340  70.284  1.00 15.66 ? 1306 NAD   B O3B   1 
HETATM 18456 C  C2B   . NAD   S 5  .    ? 27.725  34.049  70.945  1.00 16.07 ? 1306 NAD   B C2B   1 
HETATM 18457 O  O2B   . NAD   S 5  .    ? 28.275  33.189  69.997  1.00 16.05 ? 1306 NAD   B O2B   1 
HETATM 18458 C  C1B   . NAD   S 5  .    ? 27.557  35.399  70.378  1.00 15.95 ? 1306 NAD   B C1B   1 
HETATM 18459 N  N9A   . NAD   S 5  .    ? 28.770  36.165  70.275  1.00 16.69 ? 1306 NAD   B N9A   1 
HETATM 18460 C  C8A   . NAD   S 5  .    ? 29.908  36.090  71.067  1.00 18.14 ? 1306 NAD   B C8A   1 
HETATM 18461 N  N7A   . NAD   S 5  .    ? 30.782  37.017  70.654  1.00 19.50 ? 1306 NAD   B N7A   1 
HETATM 18462 C  C5A   . NAD   S 5  .    ? 30.241  37.729  69.594  1.00 17.46 ? 1306 NAD   B C5A   1 
HETATM 18463 C  C6A   . NAD   S 5  .    ? 30.635  38.780  68.790  1.00 17.32 ? 1306 NAD   B C6A   1 
HETATM 18464 N  N6A   . NAD   S 5  .    ? 31.929  39.381  68.964  1.00 23.62 ? 1306 NAD   B N6A   1 
HETATM 18465 N  N1A   . NAD   S 5  .    ? 29.835  39.249  67.846  1.00 17.26 ? 1306 NAD   B N1A   1 
HETATM 18466 C  C2A   . NAD   S 5  .    ? 28.600  38.727  67.606  1.00 18.22 ? 1306 NAD   B C2A   1 
HETATM 18467 N  N3A   . NAD   S 5  .    ? 28.171  37.698  68.367  1.00 16.61 ? 1306 NAD   B N3A   1 
HETATM 18468 C  C4A   . NAD   S 5  .    ? 28.940  37.201  69.351  1.00 15.22 ? 1306 NAD   B C4A   1 
HETATM 18469 O  O3    . NAD   S 5  .    ? 26.477  34.967  76.202  1.00 16.14 ? 1306 NAD   B O3    1 
HETATM 18470 P  PN    . NAD   S 5  .    ? 26.088  33.524  76.762  1.00 16.68 ? 1306 NAD   B PN    1 
HETATM 18471 O  O1N   . NAD   S 5  .    ? 27.222  33.011  77.606  1.00 19.21 ? 1306 NAD   B O1N   1 
HETATM 18472 O  O2N   . NAD   S 5  .    ? 25.700  32.622  75.628  1.00 17.70 ? 1306 NAD   B O2N   1 
HETATM 18473 O  O5D   . NAD   S 5  .    ? 24.810  33.784  77.641  1.00 17.05 ? 1306 NAD   B O5D   1 
HETATM 18474 C  C5D   . NAD   S 5  .    ? 24.892  34.254  78.972  1.00 17.84 ? 1306 NAD   B C5D   1 
HETATM 18475 C  C4D   . NAD   S 5  .    ? 24.691  35.760  79.024  1.00 15.81 ? 1306 NAD   B C4D   1 
HETATM 18476 O  O4D   . NAD   S 5  .    ? 23.468  36.109  78.424  1.00 16.41 ? 1306 NAD   B O4D   1 
HETATM 18477 C  C3D   . NAD   S 5  .    ? 24.695  36.301  80.425  1.00 15.41 ? 1306 NAD   B C3D   1 
HETATM 18478 O  O3D   . NAD   S 5  .    ? 25.407  37.482  80.476  1.00 17.58 ? 1306 NAD   B O3D   1 
HETATM 18479 C  C2D   . NAD   S 5  .    ? 23.252  36.532  80.647  1.00 17.13 ? 1306 NAD   B C2D   1 
HETATM 18480 O  O2D   . NAD   S 5  .    ? 22.911  37.403  81.679  1.00 16.75 ? 1306 NAD   B O2D   1 
HETATM 18481 C  C1D   . NAD   S 5  .    ? 22.799  36.973  79.299  1.00 15.87 ? 1306 NAD   B C1D   1 
HETATM 18482 N  N1N   . NAD   S 5  .    ? 21.384  36.776  79.149  1.00 15.01 ? 1306 NAD   B N1N   1 
HETATM 18483 C  C2N   . NAD   S 5  .    ? 20.502  37.882  79.164  1.00 14.47 ? 1306 NAD   B C2N   1 
HETATM 18484 C  C3N   . NAD   S 5  .    ? 19.156  37.627  79.079  1.00 16.58 ? 1306 NAD   B C3N   1 
HETATM 18485 C  C7N   . NAD   S 5  .    ? 18.164  38.723  79.076  1.00 15.05 ? 1306 NAD   B C7N   1 
HETATM 18486 O  O7N   . NAD   S 5  .    ? 17.010  38.436  78.795  1.00 16.91 ? 1306 NAD   B O7N   1 
HETATM 18487 N  N7N   . NAD   S 5  .    ? 18.532  40.047  79.417  1.00 16.38 ? 1306 NAD   B N7N   1 
HETATM 18488 C  C4N   . NAD   S 5  .    ? 18.696  36.302  78.898  1.00 30.64 ? 1306 NAD   B C4N   1 
HETATM 18489 C  C5N   . NAD   S 5  .    ? 19.574  35.195  78.952  1.00 18.83 ? 1306 NAD   B C5N   1 
HETATM 18490 C  C6N   . NAD   S 5  .    ? 20.927  35.457  79.043  1.00 14.49 ? 1306 NAD   B C6N   1 
HETATM 18491 S  S     . SO4   T 6  .    ? -7.215  47.393  73.235  1.00 18.25 ? 1307 SO4   B S     1 
HETATM 18492 O  O1    . SO4   T 6  .    ? -6.001  46.637  72.784  1.00 22.98 ? 1307 SO4   B O1    1 
HETATM 18493 O  O2    . SO4   T 6  .    ? -7.968  47.901  72.060  1.00 17.54 ? 1307 SO4   B O2    1 
HETATM 18494 O  O3    . SO4   T 6  .    ? -8.116  46.531  74.034  1.00 21.71 ? 1307 SO4   B O3    1 
HETATM 18495 O  O4    . SO4   T 6  .    ? -6.740  48.535  74.055  1.00 22.02 ? 1307 SO4   B O4    1 
HETATM 18496 MG MG    . MG    U 7  .    ? 30.291  33.376  75.358  1.00 23.85 ? 1308 MG    B MG    1 
HETATM 18497 O  O     . HOH   V 10 .    ? -10.626 91.249  114.241 1.00 33.58 ? 1401 HOH   A O     1 
HETATM 18498 O  O     . HOH   V 10 .    ? -1.210  88.771  105.532 1.00 18.73 ? 1402 HOH   A O     1 
HETATM 18499 O  O     . HOH   V 10 .    ? -19.345 72.526  97.629  1.00 28.01 ? 1403 HOH   A O     1 
HETATM 18500 O  O     . HOH   V 10 .    ? 26.056  71.697  105.072 1.00 35.97 ? 1404 HOH   A O     1 
HETATM 18501 O  O     . HOH   V 10 .    ? 1.385   94.164  117.112 1.00 38.62 ? 1405 HOH   A O     1 
HETATM 18502 O  O     . HOH   V 10 .    ? -32.060 79.622  99.202  1.00 28.29 ? 1406 HOH   A O     1 
HETATM 18503 O  O     . HOH   V 10 .    ? -3.877  75.666  69.247  1.00 43.56 ? 1407 HOH   A O     1 
HETATM 18504 O  O     . HOH   V 10 .    ? -51.318 73.807  68.234  1.00 37.84 ? 1408 HOH   A O     1 
HETATM 18505 O  O     . HOH   V 10 .    ? -0.406  71.560  119.868 1.00 39.54 ? 1409 HOH   A O     1 
HETATM 18506 O  O     . HOH   V 10 .    ? -39.413 37.414  64.435  1.00 40.44 ? 1410 HOH   A O     1 
HETATM 18507 O  O     . HOH   V 10 .    ? -10.127 81.127  135.350 1.00 50.79 ? 1411 HOH   A O     1 
HETATM 18508 O  O     . HOH   V 10 .    ? -46.540 25.915  86.503  1.00 46.06 ? 1412 HOH   A O     1 
HETATM 18509 O  O     . HOH   V 10 .    ? -0.304  79.478  82.002  1.00 39.53 ? 1413 HOH   A O     1 
HETATM 18510 O  O     . HOH   V 10 .    ? -3.028  81.952  114.888 1.00 33.23 ? 1414 HOH   A O     1 
HETATM 18511 O  O     . HOH   V 10 .    ? 4.751   74.332  120.133 1.00 38.05 ? 1415 HOH   A O     1 
HETATM 18512 O  O     . HOH   V 10 .    ? -26.998 63.953  71.110  1.00 40.72 ? 1416 HOH   A O     1 
HETATM 18513 O  O     . HOH   V 10 .    ? -4.971  71.835  95.838  1.00 39.51 ? 1417 HOH   A O     1 
HETATM 18514 O  O     . HOH   V 10 .    ? -55.249 75.339  92.148  1.00 43.75 ? 1418 HOH   A O     1 
HETATM 18515 O  O     . HOH   V 10 .    ? 14.900  54.950  110.789 1.00 37.40 ? 1419 HOH   A O     1 
HETATM 18516 O  O     . HOH   V 10 .    ? -25.387 60.476  127.877 1.00 39.20 ? 1420 HOH   A O     1 
HETATM 18517 O  O     . HOH   V 10 .    ? -38.920 67.054  69.213  1.00 39.34 ? 1421 HOH   A O     1 
HETATM 18518 O  O     . HOH   V 10 .    ? -15.367 92.944  131.172 1.00 44.41 ? 1422 HOH   A O     1 
HETATM 18519 O  O     . HOH   V 10 .    ? -57.552 67.323  61.688  1.00 30.46 ? 1423 HOH   A O     1 
HETATM 18520 O  O     . HOH   V 10 .    ? -12.367 87.588  99.081  1.00 33.52 ? 1424 HOH   A O     1 
HETATM 18521 O  O     . HOH   V 10 .    ? -52.506 61.221  101.795 1.00 28.11 ? 1425 HOH   A O     1 
HETATM 18522 O  O     . HOH   V 10 .    ? -39.540 72.253  66.148  1.00 34.93 ? 1426 HOH   A O     1 
HETATM 18523 O  O     . HOH   V 10 .    ? -36.347 64.603  62.629  1.00 38.22 ? 1427 HOH   A O     1 
HETATM 18524 O  O     . HOH   V 10 .    ? -0.586  91.792  115.360 1.00 38.13 ? 1428 HOH   A O     1 
HETATM 18525 O  O     . HOH   V 10 .    ? 4.115   86.934  98.475  1.00 37.17 ? 1429 HOH   A O     1 
HETATM 18526 O  O     . HOH   V 10 .    ? 0.118   82.271  113.511 1.00 36.77 ? 1430 HOH   A O     1 
HETATM 18527 O  O     . HOH   V 10 .    ? -20.742 54.837  115.740 1.00 42.19 ? 1431 HOH   A O     1 
HETATM 18528 O  O     . HOH   V 10 .    ? -55.061 33.575  71.454  1.00 34.63 ? 1432 HOH   A O     1 
HETATM 18529 O  O     . HOH   V 10 .    ? -21.676 95.339  120.911 1.00 38.59 ? 1433 HOH   A O     1 
HETATM 18530 O  O     . HOH   V 10 .    ? 5.859   76.150  125.597 1.00 45.90 ? 1434 HOH   A O     1 
HETATM 18531 O  O     . HOH   V 10 .    ? -0.406  59.648  95.051  1.00 41.50 ? 1435 HOH   A O     1 
HETATM 18532 O  O     . HOH   V 10 .    ? -33.547 61.052  114.444 1.00 43.23 ? 1436 HOH   A O     1 
HETATM 18533 O  O     . HOH   V 10 .    ? -5.735  70.514  73.039  1.00 40.22 ? 1437 HOH   A O     1 
HETATM 18534 O  O     . HOH   V 10 .    ? -38.029 49.082  76.782  1.00 34.81 ? 1438 HOH   A O     1 
HETATM 18535 O  O     . HOH   V 10 .    ? -56.976 49.261  57.887  1.00 45.50 ? 1439 HOH   A O     1 
HETATM 18536 O  O     . HOH   V 10 .    ? -55.822 36.728  76.237  1.00 32.84 ? 1440 HOH   A O     1 
HETATM 18537 O  O     . HOH   V 10 .    ? -40.273 96.642  109.401 1.00 42.00 ? 1441 HOH   A O     1 
HETATM 18538 O  O     . HOH   V 10 .    ? -47.101 35.058  87.146  1.00 35.68 ? 1442 HOH   A O     1 
HETATM 18539 O  O     . HOH   V 10 .    ? -24.272 92.724  126.770 1.00 35.78 ? 1443 HOH   A O     1 
HETATM 18540 O  O     . HOH   V 10 .    ? -29.249 73.865  72.140  1.00 48.24 ? 1444 HOH   A O     1 
HETATM 18541 O  O     . HOH   V 10 .    ? -41.258 63.106  73.598  1.00 31.54 ? 1445 HOH   A O     1 
HETATM 18542 O  O     . HOH   V 10 .    ? -31.143 90.036  127.919 1.00 43.43 ? 1446 HOH   A O     1 
HETATM 18543 O  O     . HOH   V 10 .    ? -10.518 49.464  110.019 1.00 23.18 ? 1447 HOH   A O     1 
HETATM 18544 O  O     . HOH   V 10 .    ? 25.520  79.827  107.435 1.00 36.47 ? 1448 HOH   A O     1 
HETATM 18545 O  O     . HOH   V 10 .    ? -10.454 63.061  48.735  1.00 45.53 ? 1449 HOH   A O     1 
HETATM 18546 O  O     . HOH   V 10 .    ? -33.236 71.423  76.671  1.00 38.85 ? 1450 HOH   A O     1 
HETATM 18547 O  O     . HOH   V 10 .    ? -35.958 85.594  104.252 1.00 33.41 ? 1451 HOH   A O     1 
HETATM 18548 O  O     . HOH   V 10 .    ? -57.926 28.150  85.782  1.00 41.06 ? 1452 HOH   A O     1 
HETATM 18549 O  O     . HOH   V 10 .    ? -4.760  43.453  58.038  1.00 36.27 ? 1453 HOH   A O     1 
HETATM 18550 O  O     . HOH   V 10 .    ? -55.140 76.170  83.810  1.00 34.42 ? 1454 HOH   A O     1 
HETATM 18551 O  O     . HOH   V 10 .    ? -52.746 24.361  82.627  1.00 41.16 ? 1455 HOH   A O     1 
HETATM 18552 O  O     . HOH   V 10 .    ? -19.962 100.484 90.067  1.00 40.28 ? 1456 HOH   A O     1 
HETATM 18553 O  O     . HOH   V 10 .    ? -44.976 89.303  109.498 1.00 38.97 ? 1457 HOH   A O     1 
HETATM 18554 O  O     . HOH   V 10 .    ? -20.108 88.859  102.952 1.00 43.17 ? 1458 HOH   A O     1 
HETATM 18555 O  O     . HOH   V 10 .    ? -27.732 60.958  84.497  1.00 37.54 ? 1459 HOH   A O     1 
HETATM 18556 O  O     . HOH   V 10 .    ? -48.513 54.450  61.321  1.00 23.66 ? 1460 HOH   A O     1 
HETATM 18557 O  O     . HOH   V 10 .    ? 17.766  77.996  120.165 1.00 36.51 ? 1461 HOH   A O     1 
HETATM 18558 O  O     . HOH   V 10 .    ? -14.285 61.268  107.737 1.00 27.87 ? 1462 HOH   A O     1 
HETATM 18559 O  O     . HOH   V 10 .    ? 21.750  67.979  116.495 1.00 31.47 ? 1463 HOH   A O     1 
HETATM 18560 O  O     . HOH   V 10 .    ? -14.338 75.592  110.046 1.00 21.93 ? 1464 HOH   A O     1 
HETATM 18561 O  O     . HOH   V 10 .    ? -24.838 66.875  86.153  1.00 29.63 ? 1465 HOH   A O     1 
HETATM 18562 O  O     . HOH   V 10 .    ? -67.041 72.313  75.306  1.00 30.11 ? 1466 HOH   A O     1 
HETATM 18563 O  O     . HOH   V 10 .    ? -43.409 33.126  102.566 1.00 40.04 ? 1467 HOH   A O     1 
HETATM 18564 O  O     . HOH   V 10 .    ? -29.165 37.834  85.212  1.00 46.43 ? 1468 HOH   A O     1 
HETATM 18565 O  O     . HOH   V 10 .    ? -24.891 64.994  94.681  1.00 39.26 ? 1469 HOH   A O     1 
HETATM 18566 O  O     . HOH   V 10 .    ? -43.076 80.637  89.760  1.00 33.92 ? 1470 HOH   A O     1 
HETATM 18567 O  O     . HOH   V 10 .    ? -31.814 86.503  76.755  1.00 35.98 ? 1471 HOH   A O     1 
HETATM 18568 O  O     . HOH   V 10 .    ? -21.402 66.405  70.175  1.00 49.28 ? 1472 HOH   A O     1 
HETATM 18569 O  O     . HOH   V 10 .    ? -33.098 70.717  81.486  1.00 40.48 ? 1473 HOH   A O     1 
HETATM 18570 O  O     . HOH   V 10 .    ? -3.950  79.084  103.985 1.00 24.45 ? 1474 HOH   A O     1 
HETATM 18571 O  O     . HOH   V 10 .    ? 0.107   59.109  108.791 1.00 33.03 ? 1475 HOH   A O     1 
HETATM 18572 O  O     . HOH   V 10 .    ? -0.413  63.441  109.884 1.00 23.88 ? 1476 HOH   A O     1 
HETATM 18573 O  O     . HOH   V 10 .    ? -48.320 81.292  84.897  1.00 37.99 ? 1477 HOH   A O     1 
HETATM 18574 O  O     . HOH   V 10 .    ? -11.754 68.538  76.651  1.00 27.13 ? 1478 HOH   A O     1 
HETATM 18575 O  O     . HOH   V 10 .    ? -45.450 89.120  106.211 1.00 35.76 ? 1479 HOH   A O     1 
HETATM 18576 O  O     . HOH   V 10 .    ? -44.135 62.198  70.197  1.00 25.92 ? 1480 HOH   A O     1 
HETATM 18577 O  O     . HOH   V 10 .    ? -6.636  58.317  120.025 1.00 23.26 ? 1481 HOH   A O     1 
HETATM 18578 O  O     . HOH   V 10 .    ? -3.650  70.092  117.591 1.00 24.76 ? 1482 HOH   A O     1 
HETATM 18579 O  O     . HOH   V 10 .    ? -7.131  80.400  128.169 1.00 33.83 ? 1483 HOH   A O     1 
HETATM 18580 O  O     . HOH   V 10 .    ? -38.437 38.183  88.043  1.00 38.48 ? 1484 HOH   A O     1 
HETATM 18581 O  O     . HOH   V 10 .    ? -33.048 92.090  107.188 1.00 33.81 ? 1485 HOH   A O     1 
HETATM 18582 O  O     . HOH   V 10 .    ? -43.513 75.392  114.050 1.00 28.80 ? 1486 HOH   A O     1 
HETATM 18583 O  O     . HOH   V 10 .    ? -28.589 56.932  60.187  1.00 32.52 ? 1487 HOH   A O     1 
HETATM 18584 O  O     . HOH   V 10 .    ? -23.173 56.797  84.076  1.00 37.02 ? 1488 HOH   A O     1 
HETATM 18585 O  O     . HOH   V 10 .    ? 21.016  57.255  105.168 1.00 36.57 ? 1489 HOH   A O     1 
HETATM 18586 O  O     . HOH   V 10 .    ? -68.629 56.432  82.820  1.00 31.20 ? 1490 HOH   A O     1 
HETATM 18587 O  O     . HOH   V 10 .    ? -14.750 48.671  75.857  1.00 31.28 ? 1491 HOH   A O     1 
HETATM 18588 O  O     . HOH   V 10 .    ? -10.201 80.942  91.248  1.00 22.93 ? 1492 HOH   A O     1 
HETATM 18589 O  O     . HOH   V 10 .    ? -21.595 47.080  58.103  1.00 31.38 ? 1493 HOH   A O     1 
HETATM 18590 O  O     . HOH   V 10 .    ? -27.679 87.830  75.361  1.00 43.43 ? 1494 HOH   A O     1 
HETATM 18591 O  O     . HOH   V 10 .    ? -62.880 43.767  82.341  1.00 34.51 ? 1495 HOH   A O     1 
HETATM 18592 O  O     . HOH   V 10 .    ? -13.762 74.147  106.095 1.00 22.96 ? 1496 HOH   A O     1 
HETATM 18593 O  O     . HOH   V 10 .    ? -41.978 80.210  69.971  1.00 41.40 ? 1497 HOH   A O     1 
HETATM 18594 O  O     . HOH   V 10 .    ? -7.210  50.173  76.623  1.00 27.14 ? 1498 HOH   A O     1 
HETATM 18595 O  O     . HOH   V 10 .    ? -8.468  80.308  74.656  1.00 33.70 ? 1499 HOH   A O     1 
HETATM 18596 O  O     . HOH   V 10 .    ? -30.943 66.901  98.787  1.00 37.64 ? 1500 HOH   A O     1 
HETATM 18597 O  O     . HOH   V 10 .    ? -55.105 56.448  64.827  1.00 18.86 ? 1501 HOH   A O     1 
HETATM 18598 O  O     . HOH   V 10 .    ? 6.640   78.755  95.253  1.00 48.43 ? 1502 HOH   A O     1 
HETATM 18599 O  O     . HOH   V 10 .    ? -21.653 55.215  50.141  1.00 46.55 ? 1503 HOH   A O     1 
HETATM 18600 O  O     . HOH   V 10 .    ? -38.691 65.214  96.470  1.00 35.53 ? 1504 HOH   A O     1 
HETATM 18601 O  O     . HOH   V 10 .    ? -28.981 94.023  82.208  1.00 43.55 ? 1505 HOH   A O     1 
HETATM 18602 O  O     . HOH   V 10 .    ? -22.925 80.270  110.247 1.00 27.21 ? 1506 HOH   A O     1 
HETATM 18603 O  O     . HOH   V 10 .    ? -23.286 63.711  97.927  1.00 23.31 ? 1507 HOH   A O     1 
HETATM 18604 O  O     . HOH   V 10 .    ? -32.746 91.935  126.099 1.00 36.07 ? 1508 HOH   A O     1 
HETATM 18605 O  O     . HOH   V 10 .    ? -49.316 66.620  94.017  1.00 22.54 ? 1509 HOH   A O     1 
HETATM 18606 O  O     . HOH   V 10 .    ? -11.804 72.741  128.618 1.00 30.31 ? 1510 HOH   A O     1 
HETATM 18607 O  O     . HOH   V 10 .    ? -11.634 63.014  113.260 1.00 20.57 ? 1511 HOH   A O     1 
HETATM 18608 O  O     . HOH   V 10 .    ? -51.536 55.130  75.928  1.00 19.47 ? 1512 HOH   A O     1 
HETATM 18609 O  O     . HOH   V 10 .    ? -21.268 56.706  53.613  1.00 38.31 ? 1513 HOH   A O     1 
HETATM 18610 O  O     . HOH   V 10 .    ? 14.284  86.668  110.283 1.00 32.11 ? 1514 HOH   A O     1 
HETATM 18611 O  O     . HOH   V 10 .    ? 20.655  58.235  111.128 1.00 34.84 ? 1515 HOH   A O     1 
HETATM 18612 O  O     . HOH   V 10 .    ? 17.981  58.765  95.792  1.00 31.82 ? 1516 HOH   A O     1 
HETATM 18613 O  O     . HOH   V 10 .    ? -6.326  68.331  92.562  1.00 27.42 ? 1517 HOH   A O     1 
HETATM 18614 O  O     . HOH   V 10 .    ? -1.104  50.126  58.020  1.00 27.93 ? 1518 HOH   A O     1 
HETATM 18615 O  O     . HOH   V 10 .    ? -58.274 34.786  84.215  1.00 32.17 ? 1519 HOH   A O     1 
HETATM 18616 O  O     . HOH   V 10 .    ? -43.121 48.234  60.150  1.00 25.94 ? 1520 HOH   A O     1 
HETATM 18617 O  O     . HOH   V 10 .    ? -39.945 57.132  88.045  1.00 18.06 ? 1521 HOH   A O     1 
HETATM 18618 O  O     . HOH   V 10 .    ? -27.477 82.251  129.677 1.00 34.05 ? 1522 HOH   A O     1 
HETATM 18619 O  O     . HOH   V 10 .    ? -36.999 80.374  79.028  1.00 20.74 ? 1523 HOH   A O     1 
HETATM 18620 O  O     . HOH   V 10 .    ? -32.420 79.340  96.465  1.00 31.86 ? 1524 HOH   A O     1 
HETATM 18621 O  O     . HOH   V 10 .    ? 14.213  86.562  98.631  1.00 41.32 ? 1525 HOH   A O     1 
HETATM 18622 O  O     . HOH   V 10 .    ? -60.753 67.986  94.450  1.00 39.36 ? 1526 HOH   A O     1 
HETATM 18623 O  O     . HOH   V 10 .    ? -20.756 84.676  70.465  1.00 46.29 ? 1527 HOH   A O     1 
HETATM 18624 O  O     . HOH   V 10 .    ? -52.002 47.342  69.053  1.00 29.07 ? 1528 HOH   A O     1 
HETATM 18625 O  O     . HOH   V 10 .    ? -13.422 55.344  81.584  1.00 32.91 ? 1529 HOH   A O     1 
HETATM 18626 O  O     . HOH   V 10 .    ? -18.810 53.859  94.797  1.00 42.20 ? 1530 HOH   A O     1 
HETATM 18627 O  O     . HOH   V 10 .    ? -52.482 28.981  92.398  1.00 43.18 ? 1531 HOH   A O     1 
HETATM 18628 O  O     . HOH   V 10 .    ? -2.975  60.018  95.390  1.00 43.90 ? 1532 HOH   A O     1 
HETATM 18629 O  O     . HOH   V 10 .    ? -37.803 62.082  81.336  1.00 33.85 ? 1533 HOH   A O     1 
HETATM 18630 O  O     . HOH   V 10 .    ? -35.236 76.342  92.123  1.00 31.94 ? 1534 HOH   A O     1 
HETATM 18631 O  O     . HOH   V 10 .    ? -63.713 73.339  78.395  1.00 33.75 ? 1535 HOH   A O     1 
HETATM 18632 O  O     . HOH   V 10 .    ? -32.526 82.117  97.840  1.00 32.20 ? 1536 HOH   A O     1 
HETATM 18633 O  O     . HOH   V 10 .    ? -4.717  70.086  76.396  1.00 39.31 ? 1537 HOH   A O     1 
HETATM 18634 O  O     . HOH   V 10 .    ? -39.157 27.649  86.734  1.00 47.16 ? 1538 HOH   A O     1 
HETATM 18635 O  O     . HOH   V 10 .    ? -58.396 72.257  80.084  1.00 35.95 ? 1539 HOH   A O     1 
HETATM 18636 O  O     . HOH   V 10 .    ? -48.216 82.629  111.425 1.00 31.43 ? 1540 HOH   A O     1 
HETATM 18637 O  O     . HOH   V 10 .    ? -10.315 66.730  124.624 1.00 36.92 ? 1541 HOH   A O     1 
HETATM 18638 O  O     . HOH   V 10 .    ? -17.751 58.839  86.437  1.00 31.83 ? 1542 HOH   A O     1 
HETATM 18639 O  O     . HOH   V 10 .    ? 12.628  73.928  91.673  1.00 37.26 ? 1543 HOH   A O     1 
HETATM 18640 O  O     . HOH   V 10 .    ? -62.042 57.336  63.745  1.00 30.56 ? 1544 HOH   A O     1 
HETATM 18641 O  O     . HOH   V 10 .    ? -50.409 32.570  91.743  1.00 43.03 ? 1545 HOH   A O     1 
HETATM 18642 O  O     . HOH   V 10 .    ? -19.809 88.621  75.328  1.00 38.35 ? 1546 HOH   A O     1 
HETATM 18643 O  O     . HOH   V 10 .    ? -3.388  57.230  68.165  1.00 33.03 ? 1547 HOH   A O     1 
HETATM 18644 O  O     . HOH   V 10 .    ? -46.604 69.159  56.577  1.00 26.58 ? 1548 HOH   A O     1 
HETATM 18645 O  O     . HOH   V 10 .    ? -39.500 35.393  86.056  1.00 35.43 ? 1549 HOH   A O     1 
HETATM 18646 O  O     . HOH   V 10 .    ? -0.142  92.944  104.699 1.00 24.71 ? 1550 HOH   A O     1 
HETATM 18647 O  O     . HOH   V 10 .    ? 2.033   91.551  121.122 1.00 40.52 ? 1551 HOH   A O     1 
HETATM 18648 O  O     . HOH   V 10 .    ? -22.192 67.314  81.341  1.00 27.97 ? 1552 HOH   A O     1 
HETATM 18649 O  O     . HOH   V 10 .    ? 14.531  60.844  94.732  1.00 29.39 ? 1553 HOH   A O     1 
HETATM 18650 O  O     . HOH   V 10 .    ? -42.579 38.632  85.027  1.00 28.87 ? 1554 HOH   A O     1 
HETATM 18651 O  O     . HOH   V 10 .    ? -27.760 78.620  101.240 1.00 31.65 ? 1555 HOH   A O     1 
HETATM 18652 O  O     . HOH   V 10 .    ? -42.517 60.685  74.234  1.00 35.09 ? 1556 HOH   A O     1 
HETATM 18653 O  O     . HOH   V 10 .    ? -32.123 61.775  111.624 1.00 25.37 ? 1557 HOH   A O     1 
HETATM 18654 O  O     . HOH   V 10 .    ? -21.734 88.640  109.009 1.00 26.58 ? 1558 HOH   A O     1 
HETATM 18655 O  O     . HOH   V 10 .    ? 0.374   85.475  103.102 1.00 22.80 ? 1559 HOH   A O     1 
HETATM 18656 O  O     . HOH   V 10 .    ? 4.863   56.898  112.903 1.00 39.81 ? 1560 HOH   A O     1 
HETATM 18657 O  O     . HOH   V 10 .    ? -37.530 77.800  120.469 1.00 37.87 ? 1561 HOH   A O     1 
HETATM 18658 O  O     . HOH   V 10 .    ? -46.772 59.590  102.074 1.00 24.98 ? 1562 HOH   A O     1 
HETATM 18659 O  O     . HOH   V 10 .    ? -18.929 69.973  87.768  1.00 27.60 ? 1563 HOH   A O     1 
HETATM 18660 O  O     . HOH   V 10 .    ? 11.949  81.666  97.975  1.00 37.59 ? 1564 HOH   A O     1 
HETATM 18661 O  O     . HOH   V 10 .    ? -50.893 50.374  57.442  1.00 33.53 ? 1565 HOH   A O     1 
HETATM 18662 O  O     . HOH   V 10 .    ? -38.904 77.458  97.226  1.00 23.92 ? 1566 HOH   A O     1 
HETATM 18663 O  O     . HOH   V 10 .    ? -11.080 91.886  124.305 1.00 38.50 ? 1567 HOH   A O     1 
HETATM 18664 O  O     . HOH   V 10 .    ? -25.941 69.553  131.215 1.00 39.72 ? 1568 HOH   A O     1 
HETATM 18665 O  O     . HOH   V 10 .    ? -59.558 54.083  74.748  1.00 21.62 ? 1569 HOH   A O     1 
HETATM 18666 O  O     . HOH   V 10 .    ? -33.827 97.530  98.041  1.00 44.12 ? 1570 HOH   A O     1 
HETATM 18667 O  O     . HOH   V 10 .    ? -10.680 68.990  133.691 1.00 33.90 ? 1571 HOH   A O     1 
HETATM 18668 O  O     . HOH   V 10 .    ? -36.630 63.244  96.044  1.00 27.22 ? 1572 HOH   A O     1 
HETATM 18669 O  O     . HOH   V 10 .    ? 7.863   91.233  113.529 1.00 33.54 ? 1573 HOH   A O     1 
HETATM 18670 O  O     . HOH   V 10 .    ? 6.976   53.918  101.524 1.00 20.35 ? 1574 HOH   A O     1 
HETATM 18671 O  O     . HOH   V 10 .    ? -49.589 54.117  59.336  1.00 31.45 ? 1575 HOH   A O     1 
HETATM 18672 O  O     . HOH   V 10 .    ? -5.068  54.344  108.257 1.00 21.48 ? 1576 HOH   A O     1 
HETATM 18673 O  O     . HOH   V 10 .    ? -16.537 76.273  108.635 1.00 21.00 ? 1577 HOH   A O     1 
HETATM 18674 O  O     . HOH   V 10 .    ? -23.872 65.190  129.977 1.00 40.57 ? 1578 HOH   A O     1 
HETATM 18675 O  O     . HOH   V 10 .    ? -16.257 75.343  106.087 1.00 22.62 ? 1579 HOH   A O     1 
HETATM 18676 O  O     . HOH   V 10 .    ? -47.170 75.658  67.009  1.00 32.19 ? 1580 HOH   A O     1 
HETATM 18677 O  O     . HOH   V 10 .    ? -37.146 85.079  85.686  1.00 37.79 ? 1581 HOH   A O     1 
HETATM 18678 O  O     . HOH   V 10 .    ? -65.534 47.857  85.633  1.00 37.78 ? 1582 HOH   A O     1 
HETATM 18679 O  O     . HOH   V 10 .    ? -32.492 48.314  84.082  1.00 34.35 ? 1583 HOH   A O     1 
HETATM 18680 O  O     . HOH   V 10 .    ? -35.012 64.816  66.298  1.00 33.10 ? 1584 HOH   A O     1 
HETATM 18681 O  O     . HOH   V 10 .    ? -28.233 61.870  102.141 1.00 20.29 ? 1585 HOH   A O     1 
HETATM 18682 O  O     . HOH   V 10 .    ? -52.463 48.825  62.724  1.00 32.63 ? 1586 HOH   A O     1 
HETATM 18683 O  O     . HOH   V 10 .    ? -50.614 69.672  100.360 1.00 22.92 ? 1587 HOH   A O     1 
HETATM 18684 O  O     . HOH   V 10 .    ? -27.775 55.861  90.549  1.00 31.91 ? 1588 HOH   A O     1 
HETATM 18685 O  O     . HOH   V 10 .    ? -38.147 62.274  105.405 1.00 36.23 ? 1589 HOH   A O     1 
HETATM 18686 O  O     . HOH   V 10 .    ? -16.797 55.500  112.357 1.00 36.72 ? 1590 HOH   A O     1 
HETATM 18687 O  O     . HOH   V 10 .    ? -5.616  53.343  110.852 1.00 18.04 ? 1591 HOH   A O     1 
HETATM 18688 O  O     . HOH   V 10 .    ? -1.130  83.699  115.234 1.00 29.72 ? 1592 HOH   A O     1 
HETATM 18689 O  O     . HOH   V 10 .    ? -17.588 72.579  111.326 1.00 19.78 ? 1593 HOH   A O     1 
HETATM 18690 O  O     . HOH   V 10 .    ? -13.336 59.053  122.535 1.00 27.70 ? 1594 HOH   A O     1 
HETATM 18691 O  O     . HOH   V 10 .    ? -23.682 82.986  111.992 1.00 21.79 ? 1595 HOH   A O     1 
HETATM 18692 O  O     . HOH   V 10 .    ? -25.913 50.707  105.174 1.00 33.81 ? 1596 HOH   A O     1 
HETATM 18693 O  O     . HOH   V 10 .    ? -33.358 48.820  75.205  1.00 34.30 ? 1597 HOH   A O     1 
HETATM 18694 O  O     . HOH   V 10 .    ? -26.300 56.372  108.022 1.00 22.48 ? 1598 HOH   A O     1 
HETATM 18695 O  O     . HOH   V 10 .    ? -25.253 95.868  123.779 1.00 39.17 ? 1599 HOH   A O     1 
HETATM 18696 O  O     . HOH   V 10 .    ? -59.295 75.846  77.329  1.00 33.12 ? 1600 HOH   A O     1 
HETATM 18697 O  O     . HOH   V 10 .    ? -37.512 63.932  67.092  1.00 31.50 ? 1601 HOH   A O     1 
HETATM 18698 O  O     . HOH   V 10 .    ? -18.856 61.306  85.425  1.00 25.43 ? 1602 HOH   A O     1 
HETATM 18699 O  O     . HOH   V 10 .    ? -10.658 62.905  72.865  1.00 30.11 ? 1603 HOH   A O     1 
HETATM 18700 O  O     . HOH   V 10 .    ? -60.349 50.972  62.079  1.00 35.52 ? 1604 HOH   A O     1 
HETATM 18701 O  O     . HOH   V 10 .    ? -23.105 60.239  115.816 1.00 23.47 ? 1605 HOH   A O     1 
HETATM 18702 O  O     . HOH   V 10 .    ? -65.819 58.708  75.871  1.00 21.28 ? 1606 HOH   A O     1 
HETATM 18703 O  O     . HOH   V 10 .    ? -1.209  77.784  114.612 1.00 25.34 ? 1607 HOH   A O     1 
HETATM 18704 O  O     . HOH   V 10 .    ? -44.943 63.458  84.355  1.00 18.75 ? 1608 HOH   A O     1 
HETATM 18705 O  O     . HOH   V 10 .    ? -26.319 82.446  112.599 1.00 24.78 ? 1609 HOH   A O     1 
HETATM 18706 O  O     . HOH   V 10 .    ? -11.783 59.527  84.699  1.00 29.18 ? 1610 HOH   A O     1 
HETATM 18707 O  O     . HOH   V 10 .    ? -21.526 90.261  106.351 1.00 27.90 ? 1611 HOH   A O     1 
HETATM 18708 O  O     . HOH   V 10 .    ? 6.350   90.692  106.719 1.00 32.74 ? 1612 HOH   A O     1 
HETATM 18709 O  O     . HOH   V 10 .    ? -45.747 76.066  94.360  1.00 26.16 ? 1613 HOH   A O     1 
HETATM 18710 O  O     . HOH   V 10 .    ? -58.593 38.067  76.237  1.00 33.46 ? 1614 HOH   A O     1 
HETATM 18711 O  O     . HOH   V 10 .    ? -14.723 63.860  99.435  1.00 27.78 ? 1615 HOH   A O     1 
HETATM 18712 O  O     . HOH   V 10 .    ? -61.300 55.347  67.547  1.00 20.37 ? 1616 HOH   A O     1 
HETATM 18713 O  O     . HOH   V 10 .    ? -16.129 91.244  104.505 1.00 34.35 ? 1617 HOH   A O     1 
HETATM 18714 O  O     . HOH   V 10 .    ? -15.517 43.851  76.874  1.00 43.38 ? 1618 HOH   A O     1 
HETATM 18715 O  O     . HOH   V 10 .    ? -17.903 82.442  96.734  1.00 20.57 ? 1619 HOH   A O     1 
HETATM 18716 O  O     . HOH   V 10 .    ? -47.876 54.876  58.272  1.00 37.84 ? 1620 HOH   A O     1 
HETATM 18717 O  O     . HOH   V 10 .    ? -5.419  77.496  95.109  1.00 25.71 ? 1621 HOH   A O     1 
HETATM 18718 O  O     . HOH   V 10 .    ? -18.795 58.952  104.379 1.00 25.41 ? 1622 HOH   A O     1 
HETATM 18719 O  O     . HOH   V 10 .    ? -13.374 77.761  111.157 1.00 21.57 ? 1623 HOH   A O     1 
HETATM 18720 O  O     . HOH   V 10 .    ? -15.979 94.674  91.253  1.00 40.86 ? 1624 HOH   A O     1 
HETATM 18721 O  O     . HOH   V 10 .    ? -38.615 57.968  75.229  1.00 39.26 ? 1625 HOH   A O     1 
HETATM 18722 O  O     . HOH   V 10 .    ? -19.574 76.456  67.493  1.00 38.98 ? 1626 HOH   A O     1 
HETATM 18723 O  O     . HOH   V 10 .    ? -1.515  76.761  87.914  1.00 30.60 ? 1627 HOH   A O     1 
HETATM 18724 O  O     . HOH   V 10 .    ? -42.966 85.152  97.374  1.00 26.66 ? 1628 HOH   A O     1 
HETATM 18725 O  O     . HOH   V 10 .    ? -44.804 63.248  81.454  1.00 17.14 ? 1629 HOH   A O     1 
HETATM 18726 O  O     . HOH   V 10 .    ? -14.263 64.544  51.390  1.00 37.14 ? 1630 HOH   A O     1 
HETATM 18727 O  O     . HOH   V 10 .    ? -49.835 48.996  99.892  1.00 27.54 ? 1631 HOH   A O     1 
HETATM 18728 O  O     . HOH   V 10 .    ? -34.737 67.096  125.372 1.00 34.09 ? 1632 HOH   A O     1 
HETATM 18729 O  O     . HOH   V 10 .    ? 9.073   55.191  104.992 1.00 28.29 ? 1633 HOH   A O     1 
HETATM 18730 O  O     . HOH   V 10 .    ? -14.843 67.138  73.185  1.00 25.18 ? 1634 HOH   A O     1 
HETATM 18731 O  O     . HOH   V 10 .    ? -20.663 47.458  54.858  1.00 35.42 ? 1635 HOH   A O     1 
HETATM 18732 O  O     . HOH   V 10 .    ? -12.334 76.864  103.252 1.00 19.37 ? 1636 HOH   A O     1 
HETATM 18733 O  O     . HOH   V 10 .    ? -0.861  70.201  96.270  1.00 37.11 ? 1637 HOH   A O     1 
HETATM 18734 O  O     . HOH   V 10 .    ? -20.048 59.064  76.312  1.00 22.32 ? 1638 HOH   A O     1 
HETATM 18735 O  O     . HOH   V 10 .    ? -36.569 58.808  94.226  1.00 19.44 ? 1639 HOH   A O     1 
HETATM 18736 O  O     . HOH   V 10 .    ? -6.341  54.562  105.202 1.00 34.68 ? 1640 HOH   A O     1 
HETATM 18737 O  O     . HOH   V 10 .    ? -39.052 52.587  105.433 1.00 37.00 ? 1641 HOH   A O     1 
HETATM 18738 O  O     . HOH   V 10 .    ? 5.737   62.801  97.325  1.00 22.11 ? 1642 HOH   A O     1 
HETATM 18739 O  O     . HOH   V 10 .    ? -15.431 55.057  121.536 1.00 35.84 ? 1643 HOH   A O     1 
HETATM 18740 O  O     . HOH   V 10 .    ? -44.624 41.172  104.146 1.00 33.63 ? 1644 HOH   A O     1 
HETATM 18741 O  O     . HOH   V 10 .    ? -42.630 66.180  63.751  1.00 34.12 ? 1645 HOH   A O     1 
HETATM 18742 O  O     . HOH   V 10 .    ? 18.539  62.014  94.581  1.00 31.06 ? 1646 HOH   A O     1 
HETATM 18743 O  O     . HOH   V 10 .    ? -21.156 54.939  94.964  1.00 35.91 ? 1647 HOH   A O     1 
HETATM 18744 O  O     . HOH   V 10 .    ? -41.101 48.883  64.003  1.00 25.33 ? 1648 HOH   A O     1 
HETATM 18745 O  O     . HOH   V 10 .    ? -47.455 70.588  111.087 1.00 35.24 ? 1649 HOH   A O     1 
HETATM 18746 O  O     . HOH   V 10 .    ? -22.976 66.848  97.514  1.00 22.77 ? 1650 HOH   A O     1 
HETATM 18747 O  O     . HOH   V 10 .    ? -26.446 50.848  56.438  1.00 34.91 ? 1651 HOH   A O     1 
HETATM 18748 O  O     . HOH   V 10 .    ? -27.535 73.583  129.550 1.00 34.06 ? 1652 HOH   A O     1 
HETATM 18749 O  O     . HOH   V 10 .    ? -27.662 58.524  76.060  1.00 43.91 ? 1653 HOH   A O     1 
HETATM 18750 O  O     . HOH   V 10 .    ? -12.250 79.114  94.629  1.00 18.49 ? 1654 HOH   A O     1 
HETATM 18751 O  O     . HOH   V 10 .    ? -25.292 74.733  104.639 1.00 38.44 ? 1655 HOH   A O     1 
HETATM 18752 O  O     . HOH   V 10 .    ? 8.342   89.713  120.190 1.00 29.48 ? 1656 HOH   A O     1 
HETATM 18753 O  O     . HOH   V 10 .    ? -9.466  64.823  76.515  1.00 21.87 ? 1657 HOH   A O     1 
HETATM 18754 O  O     . HOH   V 10 .    ? -38.891 49.357  102.446 1.00 32.81 ? 1658 HOH   A O     1 
HETATM 18755 O  O     . HOH   V 10 .    ? -20.126 52.292  78.248  1.00 28.45 ? 1659 HOH   A O     1 
HETATM 18756 O  O     . HOH   V 10 .    ? 0.297   76.560  123.304 1.00 36.20 ? 1660 HOH   A O     1 
HETATM 18757 O  O     . HOH   V 10 .    ? -38.968 88.782  90.705  1.00 34.91 ? 1661 HOH   A O     1 
HETATM 18758 O  O     . HOH   V 10 .    ? -11.675 71.555  76.892  1.00 33.24 ? 1662 HOH   A O     1 
HETATM 18759 O  O     . HOH   V 10 .    ? -20.518 54.741  91.260  1.00 35.31 ? 1663 HOH   A O     1 
HETATM 18760 O  O     . HOH   V 10 .    ? -19.962 78.702  70.333  1.00 25.22 ? 1664 HOH   A O     1 
HETATM 18761 O  O     . HOH   V 10 .    ? 10.735  57.222  105.878 1.00 28.66 ? 1665 HOH   A O     1 
HETATM 18762 O  O     . HOH   V 10 .    ? -59.801 60.675  75.930  1.00 17.65 ? 1666 HOH   A O     1 
HETATM 18763 O  O     . HOH   V 10 .    ? -46.312 24.409  82.628  1.00 40.29 ? 1667 HOH   A O     1 
HETATM 18764 O  O     . HOH   V 10 .    ? -52.358 78.100  87.612  1.00 31.20 ? 1668 HOH   A O     1 
HETATM 18765 O  O     . HOH   V 10 .    ? -21.964 42.702  60.929  1.00 35.56 ? 1669 HOH   A O     1 
HETATM 18766 O  O     . HOH   V 10 .    ? -60.485 59.608  90.506  1.00 21.00 ? 1670 HOH   A O     1 
HETATM 18767 O  O     . HOH   V 10 .    ? -61.917 58.059  70.207  1.00 21.54 ? 1671 HOH   A O     1 
HETATM 18768 O  O     . HOH   V 10 .    ? -4.122  72.880  117.041 1.00 26.04 ? 1672 HOH   A O     1 
HETATM 18769 O  O     . HOH   V 10 .    ? -46.520 67.259  59.723  1.00 26.32 ? 1673 HOH   A O     1 
HETATM 18770 O  O     . HOH   V 10 .    ? -66.780 67.929  72.179  1.00 37.23 ? 1674 HOH   A O     1 
HETATM 18771 O  O     . HOH   V 10 .    ? -52.493 54.008  100.274 1.00 30.34 ? 1675 HOH   A O     1 
HETATM 18772 O  O     . HOH   V 10 .    ? -6.305  82.549  103.428 1.00 21.99 ? 1676 HOH   A O     1 
HETATM 18773 O  O     . HOH   V 10 .    ? -44.354 30.950  69.102  1.00 37.62 ? 1677 HOH   A O     1 
HETATM 18774 O  O     . HOH   V 10 .    ? -12.748 43.210  54.743  1.00 39.90 ? 1678 HOH   A O     1 
HETATM 18775 O  O     . HOH   V 10 .    ? 4.056   57.777  104.935 1.00 23.37 ? 1679 HOH   A O     1 
HETATM 18776 O  O     . HOH   V 10 .    ? -44.116 25.120  76.389  1.00 40.93 ? 1680 HOH   A O     1 
HETATM 18777 O  O     . HOH   V 10 .    ? -19.863 54.850  106.971 1.00 31.49 ? 1681 HOH   A O     1 
HETATM 18778 O  O     . HOH   V 10 .    ? -65.302 54.505  90.989  1.00 36.36 ? 1682 HOH   A O     1 
HETATM 18779 O  O     . HOH   V 10 .    ? -53.015 63.667  98.381  1.00 22.87 ? 1683 HOH   A O     1 
HETATM 18780 O  O     . HOH   V 10 .    ? -20.759 70.686  75.720  1.00 25.73 ? 1684 HOH   A O     1 
HETATM 18781 O  O     . HOH   V 10 .    ? -61.332 53.038  91.271  1.00 28.87 ? 1685 HOH   A O     1 
HETATM 18782 O  O     . HOH   V 10 .    ? -12.449 77.108  91.132  1.00 16.82 ? 1686 HOH   A O     1 
HETATM 18783 O  O     . HOH   V 10 .    ? -50.793 51.979  63.994  1.00 22.00 ? 1687 HOH   A O     1 
HETATM 18784 O  O     . HOH   V 10 .    ? 10.956  67.354  116.736 1.00 26.96 ? 1688 HOH   A O     1 
HETATM 18785 O  O     . HOH   V 10 .    ? -2.543  53.654  104.609 1.00 29.68 ? 1689 HOH   A O     1 
HETATM 18786 O  O     . HOH   V 10 .    ? -57.580 64.627  90.965  1.00 30.04 ? 1690 HOH   A O     1 
HETATM 18787 O  O     . HOH   V 10 .    ? -23.387 63.608  106.184 1.00 20.41 ? 1691 HOH   A O     1 
HETATM 18788 O  O     . HOH   V 10 .    ? -47.871 64.092  96.753  1.00 23.61 ? 1692 HOH   A O     1 
HETATM 18789 O  O     . HOH   V 10 .    ? -1.549  57.983  96.686  1.00 34.06 ? 1693 HOH   A O     1 
HETATM 18790 O  O     . HOH   V 10 .    ? -53.222 56.686  55.264  1.00 32.99 ? 1694 HOH   A O     1 
HETATM 18791 O  O     . HOH   V 10 .    ? -41.995 67.698  91.088  1.00 20.38 ? 1695 HOH   A O     1 
HETATM 18792 O  O     . HOH   V 10 .    ? -11.329 58.507  125.662 1.00 38.59 ? 1696 HOH   A O     1 
HETATM 18793 O  O     . HOH   V 10 .    ? -5.516  67.799  78.073  1.00 35.93 ? 1697 HOH   A O     1 
HETATM 18794 O  O     . HOH   V 10 .    ? -23.885 63.370  91.713  1.00 23.45 ? 1698 HOH   A O     1 
HETATM 18795 O  O     . HOH   V 10 .    ? 9.237   56.799  97.570  1.00 30.23 ? 1699 HOH   A O     1 
HETATM 18796 O  O     . HOH   V 10 .    ? -15.980 67.880  96.756  1.00 18.40 ? 1700 HOH   A O     1 
HETATM 18797 O  O     . HOH   V 10 .    ? -59.328 51.799  66.035  1.00 21.85 ? 1701 HOH   A O     1 
HETATM 18798 O  O     . HOH   V 10 .    ? -28.707 75.115  101.931 1.00 36.20 ? 1702 HOH   A O     1 
HETATM 18799 O  O     . HOH   V 10 .    ? -64.587 59.519  92.865  1.00 33.60 ? 1703 HOH   A O     1 
HETATM 18800 O  O     . HOH   V 10 .    ? -56.532 34.428  86.443  1.00 29.48 ? 1704 HOH   A O     1 
HETATM 18801 O  O     . HOH   V 10 .    ? -3.807  57.496  72.918  1.00 23.07 ? 1705 HOH   A O     1 
HETATM 18802 O  O     . HOH   V 10 .    ? -68.002 37.108  75.661  1.00 36.97 ? 1706 HOH   A O     1 
HETATM 18803 O  O     . HOH   V 10 .    ? -31.578 88.790  108.589 1.00 30.70 ? 1707 HOH   A O     1 
HETATM 18804 O  O     . HOH   V 10 .    ? -22.316 95.781  129.428 1.00 41.08 ? 1708 HOH   A O     1 
HETATM 18805 O  O     . HOH   V 10 .    ? -10.649 67.635  108.190 1.00 18.24 ? 1709 HOH   A O     1 
HETATM 18806 O  O     . HOH   V 10 .    ? -41.566 71.380  64.266  1.00 28.28 ? 1710 HOH   A O     1 
HETATM 18807 O  O     . HOH   V 10 .    ? 4.256   73.609  116.441 1.00 28.34 ? 1711 HOH   A O     1 
HETATM 18808 O  O     . HOH   V 10 .    ? -63.169 53.902  72.139  1.00 26.42 ? 1712 HOH   A O     1 
HETATM 18809 O  O     . HOH   V 10 .    ? -1.148  83.716  118.001 1.00 26.88 ? 1713 HOH   A O     1 
HETATM 18810 O  O     . HOH   V 10 .    ? 1.546   73.091  115.955 1.00 30.37 ? 1714 HOH   A O     1 
HETATM 18811 O  O     . HOH   V 10 .    ? 4.897   66.955  96.149  1.00 28.99 ? 1715 HOH   A O     1 
HETATM 18812 O  O     . HOH   V 10 .    ? -25.838 63.550  104.726 1.00 23.70 ? 1716 HOH   A O     1 
HETATM 18813 O  O     . HOH   V 10 .    ? -49.544 78.073  77.557  1.00 31.33 ? 1717 HOH   A O     1 
HETATM 18814 O  O     . HOH   V 10 .    ? -28.846 42.094  92.920  1.00 49.72 ? 1718 HOH   A O     1 
HETATM 18815 O  O     . HOH   V 10 .    ? -3.923  78.183  122.725 1.00 24.36 ? 1719 HOH   A O     1 
HETATM 18816 O  O     . HOH   V 10 .    ? -34.417 76.297  96.201  1.00 32.78 ? 1720 HOH   A O     1 
HETATM 18817 O  O     . HOH   V 10 .    ? -13.975 41.801  71.200  1.00 33.06 ? 1721 HOH   A O     1 
HETATM 18818 O  O     . HOH   V 10 .    ? -35.857 39.461  84.571  1.00 40.53 ? 1722 HOH   A O     1 
HETATM 18819 O  O     . HOH   V 10 .    ? -34.165 82.428  118.513 1.00 25.06 ? 1723 HOH   A O     1 
HETATM 18820 O  O     . HOH   V 10 .    ? -56.856 45.854  71.213  1.00 21.24 ? 1724 HOH   A O     1 
HETATM 18821 O  O     . HOH   V 10 .    ? -47.999 57.611  86.290  1.00 17.33 ? 1725 HOH   A O     1 
HETATM 18822 O  O     . HOH   V 10 .    ? 18.173  57.107  105.230 1.00 31.09 ? 1726 HOH   A O     1 
HETATM 18823 O  O     . HOH   V 10 .    ? -20.282 90.789  109.089 1.00 27.15 ? 1727 HOH   A O     1 
HETATM 18824 O  O     . HOH   V 10 .    ? -19.823 93.759  111.684 1.00 31.79 ? 1728 HOH   A O     1 
HETATM 18825 O  O     . HOH   V 10 .    ? -30.887 81.397  129.196 1.00 42.91 ? 1729 HOH   A O     1 
HETATM 18826 O  O     . HOH   V 10 .    ? -38.530 36.279  82.562  1.00 35.52 ? 1730 HOH   A O     1 
HETATM 18827 O  O     . HOH   V 10 .    ? -9.305  44.785  55.957  1.00 32.74 ? 1731 HOH   A O     1 
HETATM 18828 O  O     . HOH   V 10 .    ? -38.122 40.835  71.623  1.00 26.81 ? 1732 HOH   A O     1 
HETATM 18829 O  O     . HOH   V 10 .    ? -34.653 80.371  120.326 1.00 27.28 ? 1733 HOH   A O     1 
HETATM 18830 O  O     . HOH   V 10 .    ? -51.193 64.877  94.840  1.00 21.15 ? 1734 HOH   A O     1 
HETATM 18831 O  O     . HOH   V 10 .    ? -40.989 90.532  98.695  1.00 28.48 ? 1735 HOH   A O     1 
HETATM 18832 O  O     . HOH   V 10 .    ? -27.215 64.695  100.182 1.00 27.34 ? 1736 HOH   A O     1 
HETATM 18833 O  O     . HOH   V 10 .    ? -52.393 72.577  64.311  1.00 29.36 ? 1737 HOH   A O     1 
HETATM 18834 O  O     . HOH   V 10 .    ? -45.783 65.141  91.828  1.00 19.11 ? 1738 HOH   A O     1 
HETATM 18835 O  O     . HOH   V 10 .    ? -42.802 61.129  100.170 1.00 27.76 ? 1739 HOH   A O     1 
HETATM 18836 O  O     . HOH   V 10 .    ? -1.040  58.305  111.040 1.00 30.76 ? 1740 HOH   A O     1 
HETATM 18837 O  O     . HOH   V 10 .    ? 27.275  65.289  112.962 1.00 35.66 ? 1741 HOH   A O     1 
HETATM 18838 O  O     . HOH   V 10 .    ? -41.710 79.715  80.000  1.00 33.54 ? 1742 HOH   A O     1 
HETATM 18839 O  O     . HOH   V 10 .    ? -18.129 57.237  97.324  1.00 21.08 ? 1743 HOH   A O     1 
HETATM 18840 O  O     . HOH   V 10 .    ? -37.375 45.231  104.146 1.00 34.12 ? 1744 HOH   A O     1 
HETATM 18841 O  O     . HOH   V 10 .    ? -70.249 60.949  85.245  1.00 39.62 ? 1745 HOH   A O     1 
HETATM 18842 O  O     . HOH   V 10 .    ? -0.954  73.193  88.983  1.00 36.07 ? 1746 HOH   A O     1 
HETATM 18843 O  O     . HOH   V 10 .    ? 20.567  61.866  99.080  1.00 26.94 ? 1747 HOH   A O     1 
HETATM 18844 O  O     . HOH   V 10 .    ? -44.850 58.954  55.278  1.00 33.08 ? 1748 HOH   A O     1 
HETATM 18845 O  O     . HOH   V 10 .    ? 14.128  87.733  106.273 1.00 37.70 ? 1749 HOH   A O     1 
HETATM 18846 O  O     . HOH   V 10 .    ? -4.145  69.926  106.811 1.00 32.02 ? 1750 HOH   A O     1 
HETATM 18847 O  O     . HOH   V 10 .    ? -32.933 70.123  100.334 1.00 34.90 ? 1751 HOH   A O     1 
HETATM 18848 O  O     . HOH   V 10 .    ? -50.138 56.644  71.793  1.00 25.82 ? 1752 HOH   A O     1 
HETATM 18849 O  O     . HOH   V 10 .    ? -24.838 88.045  79.274  1.00 29.72 ? 1753 HOH   A O     1 
HETATM 18850 O  O     . HOH   V 10 .    ? -41.370 85.544  113.785 1.00 30.89 ? 1754 HOH   A O     1 
HETATM 18851 O  O     . HOH   V 10 .    ? 15.134  82.933  111.231 1.00 25.25 ? 1755 HOH   A O     1 
HETATM 18852 O  O     . HOH   V 10 .    ? -1.863  85.399  113.182 1.00 26.12 ? 1756 HOH   A O     1 
HETATM 18853 O  O     . HOH   V 10 .    ? -8.661  64.927  114.002 1.00 20.81 ? 1757 HOH   A O     1 
HETATM 18854 O  O     . HOH   V 10 .    ? -48.302 66.041  57.876  1.00 27.51 ? 1758 HOH   A O     1 
HETATM 18855 O  O     . HOH   V 10 .    ? -2.432  74.367  84.344  1.00 31.18 ? 1759 HOH   A O     1 
HETATM 18856 O  O     . HOH   V 10 .    ? -3.927  79.230  111.092 1.00 29.87 ? 1760 HOH   A O     1 
HETATM 18857 O  O     . HOH   V 10 .    ? -7.013  41.816  66.410  1.00 28.08 ? 1761 HOH   A O     1 
HETATM 18858 O  O     . HOH   V 10 .    ? -60.308 47.002  88.714  1.00 28.07 ? 1762 HOH   A O     1 
HETATM 18859 O  O     . HOH   V 10 .    ? -32.261 92.983  103.839 1.00 27.18 ? 1763 HOH   A O     1 
HETATM 18860 O  O     . HOH   V 10 .    ? -47.637 49.066  95.928  1.00 22.54 ? 1764 HOH   A O     1 
HETATM 18861 O  O     . HOH   V 10 .    ? -27.115 53.688  109.585 1.00 30.84 ? 1765 HOH   A O     1 
HETATM 18862 O  O     . HOH   V 10 .    ? -9.066  77.555  131.918 1.00 36.75 ? 1766 HOH   A O     1 
HETATM 18863 O  O     . HOH   V 10 .    ? -57.645 57.844  101.198 1.00 26.12 ? 1767 HOH   A O     1 
HETATM 18864 O  O     . HOH   V 10 .    ? -32.503 59.588  109.534 1.00 32.63 ? 1768 HOH   A O     1 
HETATM 18865 O  O     . HOH   V 10 .    ? -35.619 51.638  85.385  1.00 19.06 ? 1769 HOH   A O     1 
HETATM 18866 O  O     . HOH   V 10 .    ? -23.443 54.257  101.411 1.00 28.02 ? 1770 HOH   A O     1 
HETATM 18867 O  O     . HOH   V 10 .    ? -46.324 29.348  89.362  1.00 41.28 ? 1771 HOH   A O     1 
HETATM 18868 O  O     . HOH   V 10 .    ? -30.643 90.910  107.143 1.00 27.88 ? 1772 HOH   A O     1 
HETATM 18869 O  O     . HOH   V 10 .    ? -31.239 84.149  99.244  1.00 24.86 ? 1773 HOH   A O     1 
HETATM 18870 O  O     . HOH   V 10 .    ? -26.775 89.224  77.761  1.00 32.72 ? 1774 HOH   A O     1 
HETATM 18871 O  O     . HOH   V 10 .    ? -28.895 76.478  72.924  1.00 29.21 ? 1775 HOH   A O     1 
HETATM 18872 O  O     . HOH   V 10 .    ? 16.606  57.641  102.878 1.00 23.04 ? 1776 HOH   A O     1 
HETATM 18873 O  O     . HOH   V 10 .    ? -42.466 77.907  75.819  1.00 28.60 ? 1777 HOH   A O     1 
HETATM 18874 O  O     . HOH   V 10 .    ? -45.426 62.505  92.577  1.00 18.14 ? 1778 HOH   A O     1 
HETATM 18875 O  O     . HOH   V 10 .    ? -18.355 60.720  67.036  1.00 26.12 ? 1779 HOH   A O     1 
HETATM 18876 O  O     . HOH   V 10 .    ? -17.223 86.671  92.307  1.00 25.07 ? 1780 HOH   A O     1 
HETATM 18877 O  O     . HOH   V 10 .    ? -22.796 58.841  75.855  1.00 31.79 ? 1781 HOH   A O     1 
HETATM 18878 O  O     . HOH   V 10 .    ? -47.122 48.830  93.156  1.00 20.72 ? 1782 HOH   A O     1 
HETATM 18879 O  O     . HOH   V 10 .    ? -38.508 62.658  55.723  1.00 38.13 ? 1783 HOH   A O     1 
HETATM 18880 O  O     . HOH   V 10 .    ? -2.929  62.331  77.674  1.00 23.94 ? 1784 HOH   A O     1 
HETATM 18881 O  O     . HOH   V 10 .    ? -13.391 55.086  103.518 1.00 36.28 ? 1785 HOH   A O     1 
HETATM 18882 O  O     . HOH   V 10 .    ? -31.424 59.956  105.507 1.00 26.36 ? 1786 HOH   A O     1 
HETATM 18883 O  O     . HOH   V 10 .    ? -31.894 82.267  75.477  1.00 22.64 ? 1787 HOH   A O     1 
HETATM 18884 O  O     . HOH   V 10 .    ? -17.554 92.583  96.007  1.00 47.23 ? 1788 HOH   A O     1 
HETATM 18885 O  O     . HOH   V 10 .    ? -31.795 58.970  63.199  1.00 30.27 ? 1789 HOH   A O     1 
HETATM 18886 O  O     . HOH   V 10 .    ? 22.876  72.777  98.575  1.00 35.35 ? 1790 HOH   A O     1 
HETATM 18887 O  O     . HOH   V 10 .    ? -18.284 79.310  127.349 1.00 26.36 ? 1791 HOH   A O     1 
HETATM 18888 O  O     . HOH   V 10 .    ? -45.981 72.458  64.249  1.00 20.15 ? 1792 HOH   A O     1 
HETATM 18889 O  O     . HOH   V 10 .    ? -54.150 79.281  81.442  1.00 36.15 ? 1793 HOH   A O     1 
HETATM 18890 O  O     . HOH   V 10 .    ? -55.224 47.583  69.880  1.00 23.06 ? 1794 HOH   A O     1 
HETATM 18891 O  O     . HOH   V 10 .    ? -59.705 40.086  78.977  1.00 37.35 ? 1795 HOH   A O     1 
HETATM 18892 O  O     . HOH   V 10 .    ? -49.063 33.395  89.546  1.00 39.49 ? 1796 HOH   A O     1 
HETATM 18893 O  O     . HOH   V 10 .    ? -41.513 27.783  70.320  1.00 37.26 ? 1797 HOH   A O     1 
HETATM 18894 O  O     . HOH   V 10 .    ? -6.845  70.429  94.129  1.00 25.37 ? 1798 HOH   A O     1 
HETATM 18895 O  O     . HOH   V 10 .    ? 22.964  77.007  101.283 1.00 39.80 ? 1799 HOH   A O     1 
HETATM 18896 O  O     . HOH   V 10 .    ? -53.857 55.420  68.495  1.00 18.68 ? 1800 HOH   A O     1 
HETATM 18897 O  O     . HOH   V 10 .    ? -46.569 54.247  89.703  1.00 18.85 ? 1801 HOH   A O     1 
HETATM 18898 O  O     . HOH   V 10 .    ? -55.397 29.630  80.016  1.00 35.91 ? 1802 HOH   A O     1 
HETATM 18899 O  O     . HOH   V 10 .    ? -49.884 68.585  92.010  1.00 23.05 ? 1803 HOH   A O     1 
HETATM 18900 O  O     . HOH   V 10 .    ? -51.068 69.875  93.906  1.00 23.42 ? 1804 HOH   A O     1 
HETATM 18901 O  O     . HOH   V 10 .    ? -46.693 82.218  101.465 1.00 26.01 ? 1805 HOH   A O     1 
HETATM 18902 O  O     . HOH   V 10 .    ? -8.200  87.320  93.375  1.00 40.10 ? 1806 HOH   A O     1 
HETATM 18903 O  O     . HOH   V 10 .    ? -60.079 50.450  90.877  1.00 35.86 ? 1807 HOH   A O     1 
HETATM 18904 O  O     . HOH   V 10 .    ? -28.598 61.787  116.825 1.00 24.65 ? 1808 HOH   A O     1 
HETATM 18905 O  O     . HOH   V 10 .    ? -5.838  75.936  111.251 1.00 19.61 ? 1809 HOH   A O     1 
HETATM 18906 O  O     . HOH   V 10 .    ? -9.921  39.745  61.435  1.00 39.03 ? 1810 HOH   A O     1 
HETATM 18907 O  O     . HOH   V 10 .    ? -54.548 47.396  67.388  1.00 30.83 ? 1811 HOH   A O     1 
HETATM 18908 O  O     . HOH   V 10 .    ? 0.526   85.020  111.725 1.00 28.54 ? 1812 HOH   A O     1 
HETATM 18909 O  O     . HOH   V 10 .    ? -22.842 55.014  88.748  1.00 37.72 ? 1813 HOH   A O     1 
HETATM 18910 O  O     . HOH   V 10 .    ? -44.549 73.665  75.028  1.00 27.40 ? 1814 HOH   A O     1 
HETATM 18911 O  O     . HOH   V 10 .    ? -41.718 70.720  95.258  1.00 26.43 ? 1815 HOH   A O     1 
HETATM 18912 O  O     . HOH   V 10 .    ? 13.983  81.960  114.165 1.00 23.66 ? 1816 HOH   A O     1 
HETATM 18913 O  O     . HOH   V 10 .    ? -35.220 63.105  116.055 1.00 34.53 ? 1817 HOH   A O     1 
HETATM 18914 O  O     . HOH   V 10 .    ? 23.212  65.497  114.938 1.00 29.38 ? 1818 HOH   A O     1 
HETATM 18915 O  O     . HOH   V 10 .    ? -31.764 88.416  95.222  1.00 23.88 ? 1819 HOH   A O     1 
HETATM 18916 O  O     . HOH   V 10 .    ? -1.511  79.273  100.051 1.00 28.69 ? 1820 HOH   A O     1 
HETATM 18917 O  O     . HOH   V 10 .    ? 2.624   83.936  126.746 1.00 36.59 ? 1821 HOH   A O     1 
HETATM 18918 O  O     . HOH   V 10 .    ? -67.530 59.832  69.932  1.00 32.42 ? 1822 HOH   A O     1 
HETATM 18919 O  O     . HOH   V 10 .    ? 16.152  61.137  116.185 1.00 35.71 ? 1823 HOH   A O     1 
HETATM 18920 O  O     . HOH   V 10 .    ? -31.330 46.613  88.167  1.00 35.28 ? 1824 HOH   A O     1 
HETATM 18921 O  O     . HOH   V 10 .    ? 17.014  69.009  117.960 1.00 27.35 ? 1825 HOH   A O     1 
HETATM 18922 O  O     . HOH   V 10 .    ? -60.423 61.322  92.668  1.00 23.80 ? 1826 HOH   A O     1 
HETATM 18923 O  O     . HOH   V 10 .    ? -44.218 55.625  95.068  1.00 18.60 ? 1827 HOH   A O     1 
HETATM 18924 O  O     . HOH   V 10 .    ? -8.192  59.917  94.194  1.00 39.24 ? 1828 HOH   A O     1 
HETATM 18925 O  O     . HOH   V 10 .    ? -20.570 81.411  115.828 1.00 21.42 ? 1829 HOH   A O     1 
HETATM 18926 O  O     . HOH   V 10 .    ? -1.591  77.667  121.368 1.00 28.11 ? 1830 HOH   A O     1 
HETATM 18927 O  O     . HOH   V 10 .    ? -24.630 88.798  99.931  1.00 22.60 ? 1831 HOH   A O     1 
HETATM 18928 O  O     . HOH   V 10 .    ? 20.565  83.118  101.202 1.00 35.05 ? 1832 HOH   A O     1 
HETATM 18929 O  O     . HOH   V 10 .    ? -47.321 60.178  85.208  1.00 17.33 ? 1833 HOH   A O     1 
HETATM 18930 O  O     . HOH   V 10 .    ? -0.179  86.531  105.836 1.00 24.75 ? 1834 HOH   A O     1 
HETATM 18931 O  O     . HOH   V 10 .    ? -19.931 86.551  91.664  1.00 24.24 ? 1835 HOH   A O     1 
HETATM 18932 O  O     . HOH   V 10 .    ? -2.634  55.762  99.864  1.00 30.85 ? 1836 HOH   A O     1 
HETATM 18933 O  O     . HOH   V 10 .    ? 1.094   74.598  107.396 1.00 28.70 ? 1837 HOH   A O     1 
HETATM 18934 O  O     . HOH   V 10 .    ? -35.461 73.146  83.651  1.00 25.33 ? 1838 HOH   A O     1 
HETATM 18935 O  O     . HOH   V 10 .    ? -61.725 70.303  82.938  1.00 22.78 ? 1839 HOH   A O     1 
HETATM 18936 O  O     . HOH   V 10 .    ? -28.555 77.137  103.236 1.00 36.40 ? 1840 HOH   A O     1 
HETATM 18937 O  O     . HOH   V 10 .    ? -38.471 50.332  98.385  1.00 29.25 ? 1841 HOH   A O     1 
HETATM 18938 O  O     . HOH   V 10 .    ? -58.263 65.270  94.299  1.00 29.92 ? 1842 HOH   A O     1 
HETATM 18939 O  O     . HOH   V 10 .    ? -40.548 81.649  110.670 1.00 32.13 ? 1843 HOH   A O     1 
HETATM 18940 O  O     . HOH   V 10 .    ? -9.703  74.189  104.282 1.00 21.96 ? 1844 HOH   A O     1 
HETATM 18941 O  O     . HOH   V 10 .    ? -24.061 67.140  105.299 1.00 23.93 ? 1845 HOH   A O     1 
HETATM 18942 O  O     . HOH   V 10 .    ? 2.162   85.726  118.132 1.00 26.68 ? 1846 HOH   A O     1 
HETATM 18943 O  O     . HOH   V 10 .    ? -9.069  87.121  88.882  1.00 44.96 ? 1847 HOH   A O     1 
HETATM 18944 O  O     . HOH   V 10 .    ? -33.219 77.864  74.092  1.00 26.92 ? 1848 HOH   A O     1 
HETATM 18945 O  O     . HOH   V 10 .    ? -56.216 55.680  95.012  1.00 21.56 ? 1849 HOH   A O     1 
HETATM 18946 O  O     . HOH   V 10 .    ? -31.014 91.282  80.681  1.00 35.91 ? 1850 HOH   A O     1 
HETATM 18947 O  O     . HOH   V 10 .    ? -27.094 79.957  70.235  1.00 39.98 ? 1851 HOH   A O     1 
HETATM 18948 O  O     . HOH   V 10 .    ? -38.326 65.536  88.178  1.00 29.66 ? 1852 HOH   A O     1 
HETATM 18949 O  O     . HOH   V 10 .    ? -34.219 75.404  83.180  1.00 26.00 ? 1853 HOH   A O     1 
HETATM 18950 O  O     . HOH   V 10 .    ? 24.989  77.189  109.369 1.00 35.03 ? 1854 HOH   A O     1 
HETATM 18951 O  O     . HOH   V 10 .    ? -66.390 61.381  75.754  1.00 19.40 ? 1855 HOH   A O     1 
HETATM 18952 O  O     . HOH   V 10 .    ? -46.148 65.058  107.085 1.00 36.04 ? 1856 HOH   A O     1 
HETATM 18953 O  O     . HOH   V 10 .    ? -46.612 66.494  93.870  1.00 21.08 ? 1857 HOH   A O     1 
HETATM 18954 O  O     . HOH   V 10 .    ? 15.116  75.761  94.231  1.00 39.98 ? 1858 HOH   A O     1 
HETATM 18955 O  O     . HOH   V 10 .    ? -39.443 78.154  99.915  1.00 24.89 ? 1859 HOH   A O     1 
HETATM 18956 O  O     . HOH   V 10 .    ? -69.828 64.934  73.910  1.00 28.59 ? 1860 HOH   A O     1 
HETATM 18957 O  O     . HOH   V 10 .    ? -40.754 80.094  87.603  1.00 21.91 ? 1861 HOH   A O     1 
HETATM 18958 O  O     . HOH   V 10 .    ? -21.900 52.704  104.334 1.00 36.05 ? 1862 HOH   A O     1 
HETATM 18959 O  O     . HOH   V 10 .    ? -54.647 37.460  89.265  1.00 33.39 ? 1863 HOH   A O     1 
HETATM 18960 O  O     . HOH   V 10 .    ? -6.594  70.562  104.540 1.00 29.15 ? 1864 HOH   A O     1 
HETATM 18961 O  O     . HOH   V 10 .    ? -46.634 81.152  93.484  1.00 44.53 ? 1865 HOH   A O     1 
HETATM 18962 O  O     . HOH   V 10 .    ? -34.781 94.895  96.303  1.00 30.05 ? 1866 HOH   A O     1 
HETATM 18963 O  O     . HOH   V 10 .    ? -8.728  59.953  107.143 1.00 21.40 ? 1867 HOH   A O     1 
HETATM 18964 O  O     . HOH   V 10 .    ? -32.685 60.263  73.508  1.00 39.87 ? 1868 HOH   A O     1 
HETATM 18965 O  O     . HOH   V 10 .    ? -16.362 60.139  106.545 1.00 24.03 ? 1869 HOH   A O     1 
HETATM 18966 O  O     . HOH   V 10 .    ? 8.497   68.100  114.795 1.00 33.63 ? 1870 HOH   A O     1 
HETATM 18967 O  O     . HOH   V 10 .    ? -53.735 39.663  66.283  1.00 37.65 ? 1871 HOH   A O     1 
HETATM 18968 O  O     . HOH   V 10 .    ? 16.927  71.364  119.247 1.00 27.67 ? 1872 HOH   A O     1 
HETATM 18969 O  O     . HOH   V 10 .    ? -36.962 51.545  60.985  1.00 32.53 ? 1873 HOH   A O     1 
HETATM 18970 O  O     . HOH   V 10 .    ? 10.210  62.979  113.077 1.00 32.92 ? 1874 HOH   A O     1 
HETATM 18971 O  O     . HOH   V 10 .    ? -65.481 71.363  80.473  1.00 28.19 ? 1875 HOH   A O     1 
HETATM 18972 O  O     . HOH   V 10 .    ? -31.133 60.831  90.535  1.00 23.92 ? 1876 HOH   A O     1 
HETATM 18973 O  O     . HOH   V 10 .    ? -0.331  77.187  117.168 1.00 26.58 ? 1877 HOH   A O     1 
HETATM 18974 O  O     . HOH   V 10 .    ? -25.366 62.426  110.098 1.00 22.10 ? 1878 HOH   A O     1 
HETATM 18975 O  O     . HOH   V 10 .    ? -39.015 60.887  74.617  1.00 42.51 ? 1879 HOH   A O     1 
HETATM 18976 O  O     . HOH   V 10 .    ? -22.928 53.735  92.722  1.00 31.35 ? 1880 HOH   A O     1 
HETATM 18977 O  O     . HOH   V 10 .    ? -8.061  76.977  92.108  1.00 24.09 ? 1881 HOH   A O     1 
HETATM 18978 O  O     . HOH   V 10 .    ? -33.579 83.587  123.285 1.00 30.08 ? 1882 HOH   A O     1 
HETATM 18979 O  O     . HOH   V 10 .    ? -25.818 45.123  65.990  1.00 46.33 ? 1883 HOH   A O     1 
HETATM 18980 O  O     . HOH   V 10 .    ? -62.126 61.684  68.242  1.00 24.57 ? 1884 HOH   A O     1 
HETATM 18981 O  O     . HOH   V 10 .    ? -42.441 47.479  81.185  1.00 22.39 ? 1885 HOH   A O     1 
HETATM 18982 O  O     . HOH   V 10 .    ? -48.943 83.259  108.962 1.00 33.67 ? 1886 HOH   A O     1 
HETATM 18983 O  O     . HOH   V 10 .    ? -3.151  77.740  101.522 1.00 26.43 ? 1887 HOH   A O     1 
HETATM 18984 O  O     . HOH   V 10 .    ? 19.222  81.918  113.220 1.00 32.10 ? 1888 HOH   A O     1 
HETATM 18985 O  O     . HOH   V 10 .    ? -56.974 39.245  91.404  1.00 40.96 ? 1889 HOH   A O     1 
HETATM 18986 O  O     . HOH   V 10 .    ? -39.289 76.587  93.183  1.00 25.11 ? 1890 HOH   A O     1 
HETATM 18987 O  O     . HOH   V 10 .    ? -44.457 31.548  84.166  1.00 29.80 ? 1891 HOH   A O     1 
HETATM 18988 O  O     . HOH   V 10 .    ? -63.882 52.874  89.895  1.00 33.78 ? 1892 HOH   A O     1 
HETATM 18989 O  O     . HOH   V 10 .    ? -52.366 61.886  94.709  1.00 21.34 ? 1893 HOH   A O     1 
HETATM 18990 O  O     . HOH   V 10 .    ? -46.472 30.564  85.521  1.00 31.59 ? 1894 HOH   A O     1 
HETATM 18991 O  O     . HOH   V 10 .    ? -36.853 68.320  83.328  1.00 30.48 ? 1895 HOH   A O     1 
HETATM 18992 O  O     . HOH   V 10 .    ? -45.768 78.204  96.072  1.00 21.51 ? 1896 HOH   A O     1 
HETATM 18993 O  O     . HOH   V 10 .    ? -36.075 37.420  83.368  1.00 37.64 ? 1897 HOH   A O     1 
HETATM 18994 O  O     . HOH   V 10 .    ? -60.999 41.749  67.198  1.00 39.06 ? 1898 HOH   A O     1 
HETATM 18995 O  O     . HOH   V 10 .    ? -36.437 95.037  94.040  1.00 33.37 ? 1899 HOH   A O     1 
HETATM 18996 O  O     . HOH   V 10 .    ? -49.888 72.325  101.128 1.00 24.17 ? 1900 HOH   A O     1 
HETATM 18997 O  O     . HOH   V 10 .    ? -24.473 92.344  105.198 1.00 35.91 ? 1901 HOH   A O     1 
HETATM 18998 O  O     . HOH   V 10 .    ? 6.727   60.908  103.269 1.00 19.47 ? 1902 HOH   A O     1 
HETATM 18999 O  O     . HOH   V 10 .    ? -51.814 87.183  103.594 1.00 42.11 ? 1903 HOH   A O     1 
HETATM 19000 O  O     . HOH   V 10 .    ? -41.477 64.028  103.583 1.00 23.25 ? 1904 HOH   A O     1 
HETATM 19001 O  O     . HOH   V 10 .    ? -47.070 34.538  100.750 1.00 41.94 ? 1905 HOH   A O     1 
HETATM 19002 O  O     . HOH   V 10 .    ? -32.692 92.674  110.194 1.00 32.99 ? 1906 HOH   A O     1 
HETATM 19003 O  O     . HOH   V 10 .    ? -12.465 64.015  129.678 1.00 34.38 ? 1907 HOH   A O     1 
HETATM 19004 O  O     . HOH   V 10 .    ? 12.658  67.073  93.428  1.00 31.32 ? 1908 HOH   A O     1 
HETATM 19005 O  O     . HOH   V 10 .    ? -0.591  83.632  109.666 1.00 28.79 ? 1909 HOH   A O     1 
HETATM 19006 O  O     . HOH   V 10 .    ? -33.624 52.369  82.197  1.00 40.34 ? 1910 HOH   A O     1 
HETATM 19007 O  O     . HOH   V 10 .    ? -57.250 60.078  61.049  1.00 19.42 ? 1911 HOH   A O     1 
HETATM 19008 O  O     . HOH   V 10 .    ? -56.450 68.797  99.941  1.00 39.76 ? 1912 HOH   A O     1 
HETATM 19009 O  O     . HOH   V 10 .    ? -20.307 65.995  81.148  1.00 31.28 ? 1913 HOH   A O     1 
HETATM 19010 O  O     . HOH   V 10 .    ? -11.595 88.414  128.908 1.00 34.27 ? 1914 HOH   A O     1 
HETATM 19011 O  O     . HOH   V 10 .    ? -2.970  85.688  124.816 1.00 38.37 ? 1915 HOH   A O     1 
HETATM 19012 O  O     . HOH   V 10 .    ? -26.659 96.791  89.106  1.00 42.64 ? 1916 HOH   A O     1 
HETATM 19013 O  O     . HOH   V 10 .    ? -27.585 70.794  90.057  1.00 28.86 ? 1917 HOH   A O     1 
HETATM 19014 O  O     . HOH   V 10 .    ? -7.111  84.883  86.758  1.00 38.89 ? 1918 HOH   A O     1 
HETATM 19015 O  O     . HOH   V 10 .    ? -45.250 65.261  52.912  1.00 38.36 ? 1919 HOH   A O     1 
HETATM 19016 O  O     . HOH   V 10 .    ? -12.434 81.642  72.734  1.00 37.88 ? 1920 HOH   A O     1 
HETATM 19017 O  O     . HOH   V 10 .    ? -49.593 75.841  101.597 1.00 25.40 ? 1921 HOH   A O     1 
HETATM 19018 O  O     . HOH   V 10 .    ? -64.279 39.957  73.761  1.00 38.92 ? 1922 HOH   A O     1 
HETATM 19019 O  O     . HOH   V 10 .    ? -53.541 68.761  93.494  1.00 24.50 ? 1923 HOH   A O     1 
HETATM 19020 O  O     . HOH   V 10 .    ? 17.341  80.245  96.921  1.00 32.90 ? 1924 HOH   A O     1 
HETATM 19021 O  O     . HOH   V 10 .    ? 2.829   64.762  113.154 1.00 32.35 ? 1925 HOH   A O     1 
HETATM 19022 O  O     . HOH   V 10 .    ? -62.379 54.698  63.331  1.00 35.93 ? 1926 HOH   A O     1 
HETATM 19023 O  O     . HOH   V 10 .    ? -53.836 76.154  94.243  1.00 38.08 ? 1927 HOH   A O     1 
HETATM 19024 O  O     . HOH   V 10 .    ? 24.716  67.511  95.220  1.00 44.01 ? 1928 HOH   A O     1 
HETATM 19025 O  O     . HOH   V 10 .    ? -20.232 43.446  70.368  1.00 46.80 ? 1929 HOH   A O     1 
HETATM 19026 O  O     . HOH   V 10 .    ? -38.411 61.400  91.863  1.00 20.13 ? 1930 HOH   A O     1 
HETATM 19027 O  O     . HOH   V 10 .    ? -48.258 75.040  95.539  1.00 23.79 ? 1931 HOH   A O     1 
HETATM 19028 O  O     . HOH   V 10 .    ? -56.997 36.856  87.938  1.00 29.93 ? 1932 HOH   A O     1 
HETATM 19029 O  O     . HOH   V 10 .    ? -4.069  76.066  124.693 1.00 30.14 ? 1933 HOH   A O     1 
HETATM 19030 O  O     . HOH   V 10 .    ? -24.503 59.092  121.573 1.00 39.04 ? 1934 HOH   A O     1 
HETATM 19031 O  O     . HOH   V 10 .    ? -32.057 74.957  126.408 1.00 29.70 ? 1935 HOH   A O     1 
HETATM 19032 O  O     . HOH   V 10 .    ? -23.953 60.940  63.645  1.00 30.54 ? 1936 HOH   A O     1 
HETATM 19033 O  O     . HOH   V 10 .    ? 5.721   80.582  97.037  1.00 37.73 ? 1937 HOH   A O     1 
HETATM 19034 O  O     . HOH   V 10 .    ? -26.447 50.214  96.630  1.00 28.89 ? 1938 HOH   A O     1 
HETATM 19035 O  O     . HOH   V 10 .    ? 25.607  64.076  102.731 1.00 30.11 ? 1939 HOH   A O     1 
HETATM 19036 O  O     . HOH   V 10 .    ? -31.337 71.674  82.756  1.00 31.47 ? 1940 HOH   A O     1 
HETATM 19037 O  O     . HOH   V 10 .    ? -58.195 57.724  63.066  1.00 19.34 ? 1941 HOH   A O     1 
HETATM 19038 O  O     . HOH   V 10 .    ? -17.156 53.162  76.338  1.00 32.74 ? 1942 HOH   A O     1 
HETATM 19039 O  O     . HOH   V 10 .    ? -63.807 70.831  70.847  1.00 27.48 ? 1943 HOH   A O     1 
HETATM 19040 O  O     . HOH   V 10 .    ? -50.314 66.353  106.320 1.00 28.80 ? 1944 HOH   A O     1 
HETATM 19041 O  O     . HOH   V 10 .    ? -34.672 66.503  101.625 1.00 23.63 ? 1945 HOH   A O     1 
HETATM 19042 O  O     . HOH   V 10 .    ? -41.163 71.428  114.338 1.00 31.73 ? 1946 HOH   A O     1 
HETATM 19043 O  O     . HOH   V 10 .    ? -16.108 46.819  53.875  1.00 31.37 ? 1947 HOH   A O     1 
HETATM 19044 O  O     . HOH   V 10 .    ? -18.948 59.510  70.033  1.00 22.49 ? 1948 HOH   A O     1 
HETATM 19045 O  O     . HOH   V 10 .    ? -6.520  76.661  128.333 1.00 41.76 ? 1949 HOH   A O     1 
HETATM 19046 O  O     . HOH   V 10 .    ? 8.184   92.738  98.675  1.00 46.36 ? 1950 HOH   A O     1 
HETATM 19047 O  O     . HOH   V 10 .    ? -28.176 60.268  124.972 1.00 38.75 ? 1951 HOH   A O     1 
HETATM 19048 O  O     . HOH   V 10 .    ? -19.290 90.792  76.969  1.00 34.38 ? 1952 HOH   A O     1 
HETATM 19049 O  O     . HOH   V 10 .    ? -30.569 86.715  102.094 1.00 34.20 ? 1953 HOH   A O     1 
HETATM 19050 O  O     . HOH   V 10 .    ? 18.390  75.101  96.613  1.00 35.56 ? 1954 HOH   A O     1 
HETATM 19051 O  O     . HOH   V 10 .    ? -50.546 37.826  99.731  1.00 35.67 ? 1955 HOH   A O     1 
HETATM 19052 O  O     . HOH   V 10 .    ? -30.232 81.090  122.937 1.00 31.59 ? 1956 HOH   A O     1 
HETATM 19053 O  O     . HOH   V 10 .    ? -5.833  64.998  114.262 1.00 23.59 ? 1957 HOH   A O     1 
HETATM 19054 O  O     . HOH   V 10 .    ? -47.910 59.076  82.788  1.00 15.83 ? 1958 HOH   A O     1 
HETATM 19055 O  O     . HOH   V 10 .    ? -51.751 72.918  105.570 1.00 30.10 ? 1959 HOH   A O     1 
HETATM 19056 O  O     . HOH   V 10 .    ? -4.572  58.960  118.438 1.00 23.02 ? 1960 HOH   A O     1 
HETATM 19057 O  O     . HOH   V 10 .    ? -7.697  42.261  62.200  1.00 27.90 ? 1961 HOH   A O     1 
HETATM 19058 O  O     . HOH   V 10 .    ? -26.578 85.707  137.381 1.00 41.88 ? 1962 HOH   A O     1 
HETATM 19059 O  O     . HOH   V 10 .    ? -53.975 43.148  65.578  1.00 39.79 ? 1963 HOH   A O     1 
HETATM 19060 O  O     . HOH   V 10 .    ? -12.839 89.688  101.700 1.00 33.41 ? 1964 HOH   A O     1 
HETATM 19061 O  O     . HOH   V 10 .    ? -46.312 55.923  87.419  1.00 17.28 ? 1965 HOH   A O     1 
HETATM 19062 O  O     . HOH   V 10 .    ? 12.336  75.727  94.984  1.00 34.97 ? 1966 HOH   A O     1 
HETATM 19063 O  O     . HOH   V 10 .    ? -33.140 97.991  93.209  1.00 46.16 ? 1967 HOH   A O     1 
HETATM 19064 O  O     . HOH   V 10 .    ? -7.214  62.196  107.152 1.00 20.92 ? 1968 HOH   A O     1 
HETATM 19065 O  O     . HOH   V 10 .    ? -22.838 74.911  99.656  1.00 27.17 ? 1969 HOH   A O     1 
HETATM 19066 O  O     . HOH   V 10 .    ? 24.921  58.315  109.713 1.00 46.43 ? 1970 HOH   A O     1 
HETATM 19067 O  O     . HOH   V 10 .    ? -46.551 31.871  70.426  1.00 32.31 ? 1971 HOH   A O     1 
HETATM 19068 O  O     . HOH   V 10 .    ? -51.977 54.402  72.716  1.00 36.87 ? 1972 HOH   A O     1 
HETATM 19069 O  O     . HOH   V 10 .    ? -42.355 56.628  89.457  1.00 18.97 ? 1973 HOH   A O     1 
HETATM 19070 O  O     . HOH   V 10 .    ? -8.345  81.847  105.111 1.00 22.55 ? 1974 HOH   A O     1 
HETATM 19071 O  O     . HOH   V 10 .    ? 7.268   57.223  112.333 1.00 35.63 ? 1975 HOH   A O     1 
HETATM 19072 O  O     . HOH   V 10 .    ? -40.469 64.571  62.332  1.00 31.20 ? 1976 HOH   A O     1 
HETATM 19073 O  O     . HOH   V 10 .    ? -59.727 38.341  82.736  1.00 36.20 ? 1977 HOH   A O     1 
HETATM 19074 O  O     . HOH   V 10 .    ? -49.344 47.587  97.404  1.00 24.94 ? 1978 HOH   A O     1 
HETATM 19075 O  O     . HOH   V 10 .    ? -50.215 27.219  77.393  1.00 36.21 ? 1979 HOH   A O     1 
HETATM 19076 O  O     . HOH   V 10 .    ? -0.266  52.559  63.152  1.00 27.85 ? 1980 HOH   A O     1 
HETATM 19077 O  O     . HOH   V 10 .    ? -7.915  74.791  70.481  1.00 31.00 ? 1981 HOH   A O     1 
HETATM 19078 O  O     . HOH   V 10 .    ? -13.909 84.864  77.214  1.00 32.40 ? 1982 HOH   A O     1 
HETATM 19079 O  O     . HOH   V 10 .    ? -48.824 61.594  56.868  1.00 23.13 ? 1983 HOH   A O     1 
HETATM 19080 O  O     . HOH   V 10 .    ? -22.720 83.289  91.582  1.00 20.68 ? 1984 HOH   A O     1 
HETATM 19081 O  O     . HOH   V 10 .    ? -9.516  55.883  82.636  1.00 31.53 ? 1985 HOH   A O     1 
HETATM 19082 O  O     . HOH   V 10 .    ? -19.985 68.952  70.878  1.00 40.37 ? 1986 HOH   A O     1 
HETATM 19083 O  O     . HOH   V 10 .    ? -44.202 40.853  85.734  1.00 36.38 ? 1987 HOH   A O     1 
HETATM 19084 O  O     . HOH   V 10 .    ? -12.514 39.948  68.527  1.00 41.48 ? 1988 HOH   A O     1 
HETATM 19085 O  O     . HOH   V 10 .    ? -3.096  90.015  108.810 1.00 24.23 ? 1989 HOH   A O     1 
HETATM 19086 O  O     . HOH   V 10 .    ? 7.068   84.646  94.509  1.00 43.79 ? 1990 HOH   A O     1 
HETATM 19087 O  O     . HOH   V 10 .    ? -25.469 68.063  90.484  1.00 27.82 ? 1991 HOH   A O     1 
HETATM 19088 O  O     . HOH   V 10 .    ? -44.804 60.967  85.524  1.00 18.28 ? 1992 HOH   A O     1 
HETATM 19089 O  O     . HOH   V 10 .    ? -29.631 83.406  101.397 1.00 26.27 ? 1993 HOH   A O     1 
HETATM 19090 O  O     . HOH   V 10 .    ? -61.020 68.572  68.625  1.00 23.19 ? 1994 HOH   A O     1 
HETATM 19091 O  O     . HOH   V 10 .    ? -39.782 61.371  94.489  1.00 23.63 ? 1995 HOH   A O     1 
HETATM 19092 O  O     . HOH   V 10 .    ? -3.304  87.678  104.983 1.00 26.55 ? 1996 HOH   A O     1 
HETATM 19093 O  O     . HOH   V 10 .    ? -36.641 69.291  119.262 1.00 31.30 ? 1997 HOH   A O     1 
HETATM 19094 O  O     . HOH   V 10 .    ? -41.634 88.645  96.794  1.00 29.10 ? 1998 HOH   A O     1 
HETATM 19095 O  O     . HOH   V 10 .    ? -49.091 29.388  73.980  1.00 39.59 ? 1999 HOH   A O     1 
HETATM 19096 O  O     . HOH   V 10 .    ? -19.559 84.860  75.601  1.00 32.87 ? 2000 HOH   A O     1 
HETATM 19097 O  O     . HOH   V 10 .    ? 2.431   83.964  101.752 1.00 26.52 ? 2001 HOH   A O     1 
HETATM 19098 O  O     . HOH   V 10 .    ? -10.777 48.982  50.120  1.00 41.69 ? 2002 HOH   A O     1 
HETATM 19099 O  O     . HOH   V 10 .    ? -1.824  77.805  105.381 1.00 22.01 ? 2003 HOH   A O     1 
HETATM 19100 O  O     . HOH   V 10 .    ? -19.228 91.776  105.185 1.00 29.04 ? 2004 HOH   A O     1 
HETATM 19101 O  O     . HOH   V 10 .    ? -38.847 71.073  84.295  1.00 27.12 ? 2005 HOH   A O     1 
HETATM 19102 O  O     . HOH   V 10 .    ? -43.171 49.746  55.790  1.00 32.90 ? 2006 HOH   A O     1 
HETATM 19103 O  O     . HOH   V 10 .    ? -47.615 84.848  101.836 1.00 36.28 ? 2007 HOH   A O     1 
HETATM 19104 O  O     . HOH   V 10 .    ? -43.199 77.334  67.905  1.00 29.17 ? 2008 HOH   A O     1 
HETATM 19105 O  O     . HOH   V 10 .    ? -25.359 88.275  116.228 1.00 24.67 ? 2009 HOH   A O     1 
HETATM 19106 O  O     . HOH   V 10 .    ? -1.585  79.881  88.249  1.00 39.74 ? 2010 HOH   A O     1 
HETATM 19107 O  O     . HOH   V 10 .    ? -41.983 55.368  104.863 1.00 38.89 ? 2011 HOH   A O     1 
HETATM 19108 O  O     . HOH   V 10 .    ? -62.551 67.625  66.459  1.00 31.90 ? 2012 HOH   A O     1 
HETATM 19109 O  O     . HOH   V 10 .    ? -5.218  90.652  119.983 1.00 34.86 ? 2013 HOH   A O     1 
HETATM 19110 O  O     . HOH   V 10 .    ? -26.380 84.187  74.276  1.00 35.58 ? 2014 HOH   A O     1 
HETATM 19111 O  O     . HOH   V 10 .    ? -13.895 95.133  119.510 1.00 33.37 ? 2015 HOH   A O     1 
HETATM 19112 O  O     . HOH   V 10 .    ? -59.144 58.233  76.873  1.00 18.66 ? 2016 HOH   A O     1 
HETATM 19113 O  O     . HOH   V 10 .    ? -56.173 25.159  88.669  1.00 41.26 ? 2017 HOH   A O     1 
HETATM 19114 O  O     . HOH   V 10 .    ? -7.529  50.561  53.171  1.00 27.79 ? 2018 HOH   A O     1 
HETATM 19115 O  O     . HOH   V 10 .    ? -31.066 73.910  88.056  1.00 33.66 ? 2019 HOH   A O     1 
HETATM 19116 O  O     . HOH   V 10 .    ? 22.795  76.115  114.778 1.00 27.99 ? 2020 HOH   A O     1 
HETATM 19117 O  O     . HOH   V 10 .    ? -55.229 26.559  91.849  1.00 38.94 ? 2021 HOH   A O     1 
HETATM 19118 O  O     . HOH   V 10 .    ? -10.041 82.089  78.305  1.00 39.83 ? 2022 HOH   A O     1 
HETATM 19119 O  O     . HOH   V 10 .    ? 4.078   60.308  101.147 1.00 27.29 ? 2023 HOH   A O     1 
HETATM 19120 O  O     . HOH   V 10 .    ? -9.560  63.763  96.227  1.00 23.88 ? 2024 HOH   A O     1 
HETATM 19121 O  O     . HOH   V 10 .    ? -34.152 96.295  112.483 1.00 44.57 ? 2025 HOH   A O     1 
HETATM 19122 O  O     . HOH   V 10 .    ? -4.195  72.771  77.213  1.00 28.43 ? 2026 HOH   A O     1 
HETATM 19123 O  O     . HOH   V 10 .    ? 9.514   68.019  94.019  1.00 35.19 ? 2027 HOH   A O     1 
HETATM 19124 O  O     . HOH   V 10 .    ? -27.018 51.733  98.671  1.00 23.68 ? 2028 HOH   A O     1 
HETATM 19125 O  O     . HOH   V 10 .    ? 18.753  73.027  118.203 1.00 28.01 ? 2029 HOH   A O     1 
HETATM 19126 O  O     . HOH   V 10 .    ? -33.585 45.690  84.760  1.00 27.51 ? 2030 HOH   A O     1 
HETATM 19127 O  O     . HOH   V 10 .    ? -13.532 54.081  77.403  1.00 27.38 ? 2031 HOH   A O     1 
HETATM 19128 O  O     . HOH   V 10 .    ? 13.738  86.619  120.842 1.00 35.36 ? 2032 HOH   A O     1 
HETATM 19129 O  O     . HOH   V 10 .    ? -38.452 70.280  81.798  1.00 23.93 ? 2033 HOH   A O     1 
HETATM 19130 O  O     . HOH   V 10 .    ? -29.493 62.425  61.984  1.00 36.63 ? 2034 HOH   A O     1 
HETATM 19131 O  O     . HOH   V 10 .    ? -34.257 69.479  76.203  1.00 36.14 ? 2035 HOH   A O     1 
HETATM 19132 O  O     . HOH   V 10 .    ? 9.231   81.045  96.231  1.00 43.03 ? 2036 HOH   A O     1 
HETATM 19133 O  O     . HOH   V 10 .    ? -12.651 65.702  112.843 1.00 18.60 ? 2037 HOH   A O     1 
HETATM 19134 O  O     . HOH   V 10 .    ? -49.877 35.368  87.983  1.00 33.35 ? 2038 HOH   A O     1 
HETATM 19135 O  O     . HOH   V 10 .    ? 10.525  67.011  112.081 1.00 36.83 ? 2039 HOH   A O     1 
HETATM 19136 O  O     . HOH   V 10 .    ? -36.045 44.258  66.456  1.00 39.66 ? 2040 HOH   A O     1 
HETATM 19137 O  O     . HOH   V 10 .    ? -64.665 42.855  86.087  1.00 33.21 ? 2041 HOH   A O     1 
HETATM 19138 O  O     . HOH   V 10 .    ? -27.317 61.806  89.020  1.00 22.65 ? 2042 HOH   A O     1 
HETATM 19139 O  O     . HOH   V 10 .    ? -32.418 64.379  121.945 1.00 28.00 ? 2043 HOH   A O     1 
HETATM 19140 O  O     . HOH   V 10 .    ? -11.542 43.444  74.233  1.00 30.79 ? 2044 HOH   A O     1 
HETATM 19141 O  O     . HOH   V 10 .    ? -18.099 88.214  101.628 1.00 40.17 ? 2045 HOH   A O     1 
HETATM 19142 O  O     . HOH   V 10 .    ? -7.937  72.298  100.765 1.00 29.01 ? 2046 HOH   A O     1 
HETATM 19143 O  O     . HOH   V 10 .    ? -40.640 58.306  80.055  1.00 30.51 ? 2047 HOH   A O     1 
HETATM 19144 O  O     . HOH   V 10 .    ? -43.958 59.327  87.553  1.00 16.89 ? 2048 HOH   A O     1 
HETATM 19145 O  O     . HOH   V 10 .    ? -34.594 77.328  85.063  1.00 24.75 ? 2049 HOH   A O     1 
HETATM 19146 O  O     . HOH   V 10 .    ? 14.148  78.320  121.031 1.00 32.14 ? 2050 HOH   A O     1 
HETATM 19147 O  O     . HOH   V 10 .    ? -4.650  82.121  125.314 1.00 40.47 ? 2051 HOH   A O     1 
HETATM 19148 O  O     . HOH   V 10 .    ? -25.079 79.104  95.136  1.00 22.57 ? 2052 HOH   A O     1 
HETATM 19149 O  O     . HOH   V 10 .    ? -18.579 97.467  126.587 1.00 44.24 ? 2053 HOH   A O     1 
HETATM 19150 O  O     . HOH   V 10 .    ? -19.853 78.831  114.953 1.00 21.65 ? 2054 HOH   A O     1 
HETATM 19151 O  O     . HOH   V 10 .    ? 7.839   88.925  127.154 1.00 38.91 ? 2055 HOH   A O     1 
HETATM 19152 O  O     . HOH   V 10 .    ? -13.067 40.763  55.786  1.00 40.81 ? 2056 HOH   A O     1 
HETATM 19153 O  O     . HOH   V 10 .    ? -1.996  77.770  75.847  1.00 28.88 ? 2057 HOH   A O     1 
HETATM 19154 O  O     . HOH   V 10 .    ? -41.823 29.592  89.628  1.00 37.80 ? 2058 HOH   A O     1 
HETATM 19155 O  O     . HOH   V 10 .    ? -28.294 64.837  64.405  1.00 40.47 ? 2059 HOH   A O     1 
HETATM 19156 O  O     . HOH   V 10 .    ? -25.468 94.023  78.243  1.00 37.18 ? 2060 HOH   A O     1 
HETATM 19157 O  O     . HOH   V 10 .    ? -34.258 56.425  105.440 1.00 26.46 ? 2061 HOH   A O     1 
HETATM 19158 O  O     . HOH   V 10 .    ? 1.147   66.341  96.644  1.00 24.89 ? 2062 HOH   A O     1 
HETATM 19159 O  O     . HOH   V 10 .    ? -45.188 86.945  111.743 1.00 47.23 ? 2063 HOH   A O     1 
HETATM 19160 O  O     . HOH   V 10 .    ? -9.279  60.391  84.377  1.00 23.30 ? 2064 HOH   A O     1 
HETATM 19161 O  O     . HOH   V 10 .    ? -38.917 31.827  96.882  1.00 42.50 ? 2065 HOH   A O     1 
HETATM 19162 O  O     . HOH   V 10 .    ? -38.250 72.774  87.506  1.00 32.75 ? 2066 HOH   A O     1 
HETATM 19163 O  O     . HOH   V 10 .    ? -8.906  83.643  81.295  1.00 39.61 ? 2067 HOH   A O     1 
HETATM 19164 O  O     . HOH   V 10 .    ? -7.044  93.567  113.314 1.00 28.84 ? 2068 HOH   A O     1 
HETATM 19165 O  O     . HOH   V 10 .    ? -57.115 31.744  80.152  1.00 35.74 ? 2069 HOH   A O     1 
HETATM 19166 O  O     . HOH   V 10 .    ? -28.130 69.253  85.861  1.00 31.58 ? 2070 HOH   A O     1 
HETATM 19167 O  O     . HOH   V 10 .    ? -22.629 94.419  118.258 1.00 33.37 ? 2071 HOH   A O     1 
HETATM 19168 O  O     . HOH   V 10 .    ? -24.804 69.137  74.583  1.00 30.92 ? 2072 HOH   A O     1 
HETATM 19169 O  O     . HOH   V 10 .    ? -34.373 42.328  70.501  1.00 40.34 ? 2073 HOH   A O     1 
HETATM 19170 O  O     . HOH   V 10 .    ? 1.286   62.155  111.343 1.00 32.16 ? 2074 HOH   A O     1 
HETATM 19171 O  O     . HOH   V 10 .    ? 2.371   76.426  116.983 1.00 25.60 ? 2075 HOH   A O     1 
HETATM 19172 O  O     . HOH   V 10 .    ? -12.631 53.510  110.475 1.00 39.48 ? 2076 HOH   A O     1 
HETATM 19173 O  O     . HOH   V 10 .    ? -1.331  80.390  111.949 1.00 32.63 ? 2077 HOH   A O     1 
HETATM 19174 O  O     . HOH   V 10 .    ? -64.645 44.895  77.979  1.00 39.85 ? 2078 HOH   A O     1 
HETATM 19175 O  O     . HOH   V 10 .    ? -4.374  54.777  61.652  1.00 35.22 ? 2079 HOH   A O     1 
HETATM 19176 O  O     . HOH   V 10 .    ? -53.608 49.277  60.380  1.00 29.07 ? 2080 HOH   A O     1 
HETATM 19177 O  O     . HOH   V 10 .    ? 20.749  75.452  100.326 1.00 36.89 ? 2081 HOH   A O     1 
HETATM 19178 O  O     . HOH   V 10 .    ? -33.936 90.551  122.147 1.00 34.81 ? 2082 HOH   A O     1 
HETATM 19179 O  O     . HOH   V 10 .    ? -5.018  55.613  101.265 1.00 31.94 ? 2083 HOH   A O     1 
HETATM 19180 O  O     . HOH   V 10 .    ? -10.338 63.481  115.704 1.00 23.94 ? 2084 HOH   A O     1 
HETATM 19181 O  O     . HOH   V 10 .    ? -23.386 86.374  73.870  1.00 39.17 ? 2085 HOH   A O     1 
HETATM 19182 O  O     . HOH   V 10 .    ? -18.263 39.431  68.551  1.00 44.73 ? 2086 HOH   A O     1 
HETATM 19183 O  O     . HOH   V 10 .    ? -35.371 40.301  92.100  1.00 25.12 ? 2087 HOH   A O     1 
HETATM 19184 O  O     . HOH   V 10 .    ? -32.993 57.272  72.533  1.00 36.88 ? 2088 HOH   A O     1 
HETATM 19185 O  O     . HOH   V 10 .    ? -17.587 85.407  77.523  1.00 31.68 ? 2089 HOH   A O     1 
HETATM 19186 O  O     . HOH   V 10 .    ? -30.663 95.803  104.962 1.00 31.94 ? 2090 HOH   A O     1 
HETATM 19187 O  O     . HOH   V 10 .    ? -12.907 68.964  74.073  1.00 35.20 ? 2091 HOH   A O     1 
HETATM 19188 O  O     . HOH   V 10 .    ? 5.241   54.829  96.895  1.00 27.37 ? 2092 HOH   A O     1 
HETATM 19189 O  O     . HOH   V 10 .    ? -19.513 90.606  97.901  1.00 37.55 ? 2093 HOH   A O     1 
HETATM 19190 O  O     . HOH   V 10 .    ? -20.887 58.055  97.323  1.00 23.33 ? 2094 HOH   A O     1 
HETATM 19191 O  O     . HOH   V 10 .    ? 8.752   64.751  94.422  1.00 30.72 ? 2095 HOH   A O     1 
HETATM 19192 O  O     . HOH   V 10 .    ? -21.464 59.074  122.487 1.00 31.10 ? 2096 HOH   A O     1 
HETATM 19193 O  O     . HOH   V 10 .    ? -59.583 62.837  77.609  1.00 21.74 ? 2097 HOH   A O     1 
HETATM 19194 O  O     . HOH   V 10 .    ? -25.053 82.634  72.743  1.00 31.99 ? 2098 HOH   A O     1 
HETATM 19195 O  O     . HOH   V 10 .    ? 16.343  65.073  119.943 1.00 30.81 ? 2099 HOH   A O     1 
HETATM 19196 O  O     . HOH   V 10 .    ? 2.829   74.162  109.483 1.00 28.21 ? 2100 HOH   A O     1 
HETATM 19197 O  O     . HOH   V 10 .    ? -37.958 67.620  98.181  1.00 28.31 ? 2101 HOH   A O     1 
HETATM 19198 O  O     . HOH   V 10 .    ? -1.584  54.258  101.880 1.00 25.42 ? 2102 HOH   A O     1 
HETATM 19199 O  O     . HOH   V 10 .    ? -57.169 53.436  96.278  1.00 24.82 ? 2103 HOH   A O     1 
HETATM 19200 O  O     . HOH   V 10 .    ? -44.074 69.183  108.973 1.00 36.47 ? 2104 HOH   A O     1 
HETATM 19201 O  O     . HOH   V 10 .    ? -18.423 68.771  104.626 1.00 23.76 ? 2105 HOH   A O     1 
HETATM 19202 O  O     . HOH   V 10 .    ? -3.327  82.247  97.587  1.00 24.52 ? 2106 HOH   A O     1 
HETATM 19203 O  O     . HOH   V 10 .    ? -63.486 44.935  68.013  1.00 39.01 ? 2107 HOH   A O     1 
HETATM 19204 O  O     . HOH   V 10 .    ? -53.593 72.163  68.141  1.00 27.84 ? 2108 HOH   A O     1 
HETATM 19205 O  O     . HOH   V 10 .    ? -38.006 40.308  74.410  1.00 32.95 ? 2109 HOH   A O     1 
HETATM 19206 O  O     . HOH   V 10 .    ? -35.282 97.743  116.289 1.00 37.53 ? 2110 HOH   A O     1 
HETATM 19207 O  O     . HOH   V 10 .    ? -15.090 58.811  126.700 1.00 33.19 ? 2111 HOH   A O     1 
HETATM 19208 O  O     . HOH   V 10 .    ? -0.323  74.035  96.250  1.00 37.00 ? 2112 HOH   A O     1 
HETATM 19209 O  O     . HOH   V 10 .    ? -36.871 60.469  96.329  1.00 20.66 ? 2113 HOH   A O     1 
HETATM 19210 O  O     . HOH   V 10 .    ? -8.885  51.685  107.510 1.00 31.64 ? 2114 HOH   A O     1 
HETATM 19211 O  O     . HOH   V 10 .    ? -39.095 66.728  94.434  1.00 28.76 ? 2115 HOH   A O     1 
HETATM 19212 O  O     . HOH   V 10 .    ? -17.944 71.088  106.022 1.00 29.08 ? 2116 HOH   A O     1 
HETATM 19213 O  O     . HOH   V 10 .    ? -23.146 89.043  102.271 1.00 28.82 ? 2117 HOH   A O     1 
HETATM 19214 O  O     . HOH   V 10 .    ? -1.238  69.941  116.439 1.00 26.19 ? 2118 HOH   A O     1 
HETATM 19215 O  O     . HOH   V 10 .    ? -36.248 71.262  121.249 1.00 34.30 ? 2119 HOH   A O     1 
HETATM 19216 O  O     . HOH   V 10 .    ? -36.934 49.755  100.724 1.00 29.93 ? 2120 HOH   A O     1 
HETATM 19217 O  O     . HOH   V 10 .    ? -40.127 39.097  98.674  1.00 40.55 ? 2121 HOH   A O     1 
HETATM 19218 O  O     . HOH   V 10 .    ? -14.922 53.030  75.616  1.00 33.23 ? 2122 HOH   A O     1 
HETATM 19219 O  O     . HOH   V 10 .    ? -10.317 64.059  125.192 1.00 39.13 ? 2123 HOH   A O     1 
HETATM 19220 O  O     . HOH   V 10 .    ? -16.246 53.759  100.603 1.00 35.48 ? 2124 HOH   A O     1 
HETATM 19221 O  O     . HOH   V 10 .    ? 23.429  58.152  103.634 1.00 36.74 ? 2125 HOH   A O     1 
HETATM 19222 O  O     . HOH   V 10 .    ? -38.441 73.120  90.178  1.00 35.90 ? 2126 HOH   A O     1 
HETATM 19223 O  O     . HOH   V 10 .    ? -60.943 69.795  87.799  1.00 43.96 ? 2127 HOH   A O     1 
HETATM 19224 O  O     . HOH   V 10 .    ? -35.774 43.472  79.413  1.00 27.08 ? 2128 HOH   A O     1 
HETATM 19225 O  O     . HOH   V 10 .    ? -42.786 28.651  86.642  1.00 39.13 ? 2129 HOH   A O     1 
HETATM 19226 O  O     . HOH   V 10 .    ? -64.726 55.099  80.839  1.00 24.59 ? 2130 HOH   A O     1 
HETATM 19227 O  O     . HOH   V 10 .    ? -32.272 52.364  85.987  1.00 29.91 ? 2131 HOH   A O     1 
HETATM 19228 O  O     . HOH   V 10 .    ? -2.315  62.454  113.365 1.00 36.12 ? 2132 HOH   A O     1 
HETATM 19229 O  O     . HOH   V 10 .    ? -25.462 59.169  114.486 1.00 26.05 ? 2133 HOH   A O     1 
HETATM 19230 O  O     . HOH   V 10 .    ? -11.186 53.826  100.442 1.00 27.70 ? 2134 HOH   A O     1 
HETATM 19231 O  O     . HOH   V 10 .    ? -6.587  53.607  100.444 1.00 43.03 ? 2135 HOH   A O     1 
HETATM 19232 O  O     . HOH   V 10 .    ? -56.263 36.887  92.791  1.00 39.96 ? 2136 HOH   A O     1 
HETATM 19233 O  O     . HOH   V 10 .    ? 18.806  71.083  92.266  1.00 43.29 ? 2137 HOH   A O     1 
HETATM 19234 O  O     . HOH   V 10 .    ? -14.132 55.671  111.595 1.00 34.83 ? 2138 HOH   A O     1 
HETATM 19235 O  O     . HOH   V 10 .    ? -11.442 52.933  102.994 1.00 44.56 ? 2139 HOH   A O     1 
HETATM 19236 O  O     . HOH   V 10 .    ? -67.669 50.812  77.565  1.00 46.61 ? 2140 HOH   A O     1 
HETATM 19237 O  O     . HOH   V 10 .    ? 2.485   86.337  126.193 1.00 41.25 ? 2141 HOH   A O     1 
HETATM 19238 O  O     . HOH   V 10 .    ? -1.995  90.960  105.719 1.00 27.10 ? 2142 HOH   A O     1 
HETATM 19239 O  O     . HOH   V 10 .    ? 10.307  81.180  125.377 1.00 32.04 ? 2143 HOH   A O     1 
HETATM 19240 O  O     . HOH   V 10 .    ? -13.889 86.553  100.883 1.00 25.52 ? 2144 HOH   A O     1 
HETATM 19241 O  O     . HOH   V 10 .    ? 22.366  65.328  93.186  1.00 39.34 ? 2145 HOH   A O     1 
HETATM 19242 O  O     . HOH   V 10 .    ? -39.551 84.629  103.807 1.00 29.81 ? 2146 HOH   A O     1 
HETATM 19243 O  O     . HOH   V 10 .    ? -54.287 45.037  91.990  1.00 31.52 ? 2147 HOH   A O     1 
HETATM 19244 O  O     . HOH   V 10 .    ? 11.068  61.032  115.292 1.00 33.14 ? 2148 HOH   A O     1 
HETATM 19245 O  O     . HOH   V 10 .    ? -45.266 57.478  102.203 1.00 29.05 ? 2149 HOH   A O     1 
HETATM 19246 O  O     . HOH   V 10 .    ? -27.184 69.213  103.507 1.00 34.91 ? 2150 HOH   A O     1 
HETATM 19247 O  O     . HOH   V 10 .    ? -40.824 70.343  92.797  1.00 31.91 ? 2151 HOH   A O     1 
HETATM 19248 O  O     . HOH   V 10 .    ? -39.287 86.425  89.350  1.00 28.16 ? 2152 HOH   A O     1 
HETATM 19249 O  O     . HOH   V 10 .    ? -21.033 50.281  108.687 1.00 38.78 ? 2153 HOH   A O     1 
HETATM 19250 O  O     . HOH   V 10 .    ? -45.639 54.915  92.197  1.00 17.54 ? 2154 HOH   A O     1 
HETATM 19251 O  O     . HOH   V 10 .    ? -40.047 37.909  85.238  1.00 30.37 ? 2155 HOH   A O     1 
HETATM 19252 O  O     . HOH   V 10 .    ? 1.314   57.048  107.684 1.00 20.94 ? 2156 HOH   A O     1 
HETATM 19253 O  O     . HOH   V 10 .    ? -22.350 98.555  100.419 1.00 38.08 ? 2157 HOH   A O     1 
HETATM 19254 O  O     . HOH   V 10 .    ? -2.786  75.757  77.480  1.00 23.53 ? 2158 HOH   A O     1 
HETATM 19255 O  O     . HOH   V 10 .    ? -30.778 66.153  127.002 1.00 38.45 ? 2159 HOH   A O     1 
HETATM 19256 O  O     . HOH   V 10 .    ? -51.325 79.599  78.881  1.00 38.93 ? 2160 HOH   A O     1 
HETATM 19257 O  O     . HOH   V 10 .    ? 21.753  72.621  116.003 1.00 29.26 ? 2161 HOH   A O     1 
HETATM 19258 O  O     . HOH   V 10 .    ? -17.138 88.871  99.548  1.00 39.68 ? 2162 HOH   A O     1 
HETATM 19259 O  O     . HOH   V 10 .    ? -30.842 83.647  123.326 1.00 26.85 ? 2163 HOH   A O     1 
HETATM 19260 O  O     . HOH   V 10 .    ? -3.568  78.785  93.530  1.00 33.79 ? 2164 HOH   A O     1 
HETATM 19261 O  O     . HOH   V 10 .    ? 11.107  85.048  124.653 1.00 28.94 ? 2165 HOH   A O     1 
HETATM 19262 O  O     . HOH   V 10 .    ? -15.077 55.209  51.077  1.00 40.25 ? 2166 HOH   A O     1 
HETATM 19263 O  O     . HOH   V 10 .    ? 4.532   85.865  101.089 1.00 27.38 ? 2167 HOH   A O     1 
HETATM 19264 O  O     . HOH   V 10 .    ? -34.395 50.100  83.481  1.00 34.53 ? 2168 HOH   A O     1 
HETATM 19265 O  O     . HOH   V 10 .    ? 2.607   77.765  98.192  1.00 27.47 ? 2169 HOH   A O     1 
HETATM 19266 O  O     . HOH   V 10 .    ? -46.965 77.005  92.150  1.00 25.64 ? 2170 HOH   A O     1 
HETATM 19267 O  O     . HOH   V 10 .    ? -22.220 76.713  70.330  1.00 24.18 ? 2171 HOH   A O     1 
HETATM 19268 O  O     . HOH   V 10 .    ? -3.370  56.466  95.486  1.00 42.78 ? 2172 HOH   A O     1 
HETATM 19269 O  O     . HOH   V 10 .    ? -44.828 85.656  99.777  1.00 41.29 ? 2173 HOH   A O     1 
HETATM 19270 O  O     . HOH   V 10 .    ? -37.604 30.321  66.253  1.00 46.55 ? 2174 HOH   A O     1 
HETATM 19271 O  O     . HOH   V 10 .    ? -30.621 50.084  104.788 1.00 31.05 ? 2175 HOH   A O     1 
HETATM 19272 O  O     . HOH   V 10 .    ? -49.045 65.400  54.198  1.00 26.42 ? 2176 HOH   A O     1 
HETATM 19273 O  O     . HOH   V 10 .    ? 0.513   64.076  107.353 1.00 20.88 ? 2177 HOH   A O     1 
HETATM 19274 O  O     . HOH   V 10 .    ? 7.097   55.005  98.927  1.00 21.55 ? 2178 HOH   A O     1 
HETATM 19275 O  O     . HOH   V 10 .    ? -21.794 67.173  73.817  1.00 42.73 ? 2179 HOH   A O     1 
HETATM 19276 O  O     . HOH   V 10 .    ? -49.968 72.891  62.862  1.00 23.75 ? 2180 HOH   A O     1 
HETATM 19277 O  O     . HOH   V 10 .    ? -26.812 62.729  86.557  1.00 25.44 ? 2181 HOH   A O     1 
HETATM 19278 O  O     . HOH   V 10 .    ? 12.434  65.099  118.769 1.00 33.88 ? 2182 HOH   A O     1 
HETATM 19279 O  O     . HOH   V 10 .    ? -39.431 88.552  119.255 1.00 34.94 ? 2183 HOH   A O     1 
HETATM 19280 O  O     . HOH   V 10 .    ? -34.841 36.708  69.204  1.00 43.24 ? 2184 HOH   A O     1 
HETATM 19281 O  O     . HOH   V 10 .    ? -62.012 68.120  89.315  1.00 38.36 ? 2185 HOH   A O     1 
HETATM 19282 O  O     . HOH   V 10 .    ? -28.526 94.914  89.356  1.00 39.22 ? 2186 HOH   A O     1 
HETATM 19283 O  O     . HOH   V 10 .    ? -36.151 80.574  75.622  1.00 25.66 ? 2187 HOH   A O     1 
HETATM 19284 O  O     . HOH   V 10 .    ? -0.194  67.457  117.718 1.00 30.53 ? 2188 HOH   A O     1 
HETATM 19285 O  O     . HOH   V 10 .    ? -33.397 53.126  108.900 1.00 43.52 ? 2189 HOH   A O     1 
HETATM 19286 O  O     . HOH   V 10 .    ? -42.692 77.646  78.459  1.00 27.02 ? 2190 HOH   A O     1 
HETATM 19287 O  O     . HOH   V 10 .    ? -30.328 54.019  57.889  1.00 42.11 ? 2191 HOH   A O     1 
HETATM 19288 O  O     . HOH   V 10 .    ? -16.303 43.009  72.129  1.00 41.73 ? 2192 HOH   A O     1 
HETATM 19289 O  O     . HOH   V 10 .    ? -64.261 57.824  67.163  1.00 36.28 ? 2193 HOH   A O     1 
HETATM 19290 O  O     . HOH   V 10 .    ? -22.170 54.473  97.229  1.00 34.84 ? 2194 HOH   A O     1 
HETATM 19291 O  O     . HOH   V 10 .    ? 2.895   66.490  120.488 1.00 38.89 ? 2195 HOH   A O     1 
HETATM 19292 O  O     . HOH   V 10 .    ? 11.375  89.302  104.728 1.00 40.95 ? 2196 HOH   A O     1 
HETATM 19293 O  O     . HOH   V 10 .    ? 12.838  88.614  116.236 1.00 35.10 ? 2197 HOH   A O     1 
HETATM 19294 O  O     . HOH   V 10 .    ? -36.961 88.004  83.331  1.00 42.87 ? 2198 HOH   A O     1 
HETATM 19295 O  O     . HOH   V 10 .    ? -45.195 92.505  98.753  1.00 38.87 ? 2199 HOH   A O     1 
HETATM 19296 O  O     . HOH   V 10 .    ? -29.116 54.740  111.363 1.00 39.06 ? 2200 HOH   A O     1 
HETATM 19297 O  O     . HOH   V 10 .    ? -26.239 96.168  79.580  1.00 41.83 ? 2201 HOH   A O     1 
HETATM 19298 O  O     . HOH   V 10 .    ? -67.691 64.183  85.430  1.00 30.74 ? 2202 HOH   A O     1 
HETATM 19299 O  O     . HOH   V 10 .    ? -52.316 29.870  73.118  1.00 42.28 ? 2203 HOH   A O     1 
HETATM 19300 O  O     . HOH   V 10 .    ? -3.573  82.060  110.158 1.00 31.17 ? 2204 HOH   A O     1 
HETATM 19301 O  O     . HOH   V 10 .    ? -29.552 58.425  79.202  1.00 38.56 ? 2205 HOH   A O     1 
HETATM 19302 O  O     . HOH   V 10 .    ? -30.967 59.178  82.066  1.00 46.94 ? 2206 HOH   A O     1 
HETATM 19303 O  O     . HOH   V 10 .    ? -10.531 86.904  91.614  1.00 34.89 ? 2207 HOH   A O     1 
HETATM 19304 O  O     . HOH   V 10 .    ? -43.089 56.223  92.031  1.00 17.71 ? 2208 HOH   A O     1 
HETATM 19305 O  O     . HOH   V 10 .    ? -61.301 61.544  62.741  1.00 32.59 ? 2209 HOH   A O     1 
HETATM 19306 O  O     . HOH   V 10 .    ? -32.314 44.710  103.559 1.00 42.76 ? 2210 HOH   A O     1 
HETATM 19307 O  O     . HOH   V 10 .    ? 5.597   58.500  97.423  1.00 34.92 ? 2211 HOH   A O     1 
HETATM 19308 O  O     . HOH   V 10 .    ? -17.186 54.730  78.398  1.00 36.87 ? 2212 HOH   A O     1 
HETATM 19309 O  O     . HOH   V 10 .    ? -7.716  89.172  99.777  1.00 44.21 ? 2213 HOH   A O     1 
HETATM 19310 O  O     . HOH   V 10 .    ? -20.443 54.554  98.999  1.00 31.32 ? 2214 HOH   A O     1 
HETATM 19311 O  O     . HOH   V 10 .    ? -0.693  74.700  116.729 1.00 31.03 ? 2215 HOH   A O     1 
HETATM 19312 O  O     . HOH   V 10 .    ? -26.919 60.601  122.661 1.00 33.51 ? 2216 HOH   A O     1 
HETATM 19313 O  O     . HOH   V 10 .    ? -41.517 88.581  93.922  1.00 37.42 ? 2217 HOH   A O     1 
HETATM 19314 O  O     . HOH   V 10 .    ? -52.877 66.353  102.063 1.00 35.11 ? 2218 HOH   A O     1 
HETATM 19315 O  O     . HOH   V 10 .    ? -66.442 68.592  84.017  1.00 30.17 ? 2219 HOH   A O     1 
HETATM 19316 O  O     . HOH   V 10 .    ? -41.718 24.329  81.661  1.00 52.57 ? 2220 HOH   A O     1 
HETATM 19317 O  O     . HOH   V 10 .    ? -48.619 78.214  75.073  1.00 36.37 ? 2221 HOH   A O     1 
HETATM 19318 O  O     . HOH   V 10 .    ? -56.749 73.446  96.223  1.00 37.90 ? 2222 HOH   A O     1 
HETATM 19319 O  O     . HOH   V 10 .    ? -49.616 54.235  74.025  1.00 22.14 ? 2223 HOH   A O     1 
HETATM 19320 O  O     . HOH   V 10 .    ? 7.571   66.604  112.236 1.00 38.40 ? 2224 HOH   A O     1 
HETATM 19321 O  O     . HOH   V 10 .    ? -25.888 69.530  95.819  1.00 34.00 ? 2225 HOH   A O     1 
HETATM 19322 O  O     . HOH   V 10 .    ? -55.280 41.812  96.735  1.00 40.05 ? 2226 HOH   A O     1 
HETATM 19323 O  O     . HOH   V 10 .    ? -43.578 90.455  99.952  1.00 32.37 ? 2227 HOH   A O     1 
HETATM 19324 O  O     . HOH   V 10 .    ? -63.105 62.208  97.753  1.00 34.62 ? 2228 HOH   A O     1 
HETATM 19325 O  O     . HOH   V 10 .    ? -55.640 36.386  96.723  1.00 46.23 ? 2229 HOH   A O     1 
HETATM 19326 O  O     . HOH   V 10 .    ? -14.229 57.905  110.017 1.00 34.96 ? 2230 HOH   A O     1 
HETATM 19327 O  O     . HOH   V 10 .    ? -55.403 47.795  95.179  1.00 42.87 ? 2231 HOH   A O     1 
HETATM 19328 O  O     . HOH   V 10 .    ? -18.773 59.579  108.247 1.00 32.24 ? 2232 HOH   A O     1 
HETATM 19329 O  O     . HOH   V 10 .    ? -60.872 68.850  91.804  1.00 38.78 ? 2233 HOH   A O     1 
HETATM 19330 O  O     . HOH   V 10 .    ? -65.881 72.075  71.897  1.00 43.90 ? 2234 HOH   A O     1 
HETATM 19331 O  O     . HOH   V 10 .    ? -20.915 67.102  53.554  1.00 46.21 ? 2235 HOH   A O     1 
HETATM 19332 O  O     . HOH   V 10 .    ? -32.287 55.942  86.024  1.00 27.49 ? 2236 HOH   A O     1 
HETATM 19333 O  O     . HOH   V 10 .    ? -14.905 48.166  51.581  1.00 38.30 ? 2237 HOH   A O     1 
HETATM 19334 O  O     . HOH   V 10 .    ? -31.471 94.311  127.144 1.00 38.63 ? 2238 HOH   A O     1 
HETATM 19335 O  O     . HOH   V 10 .    ? -4.569  50.288  56.582  1.00 36.76 ? 2239 HOH   A O     1 
HETATM 19336 O  O     . HOH   V 10 .    ? 1.085   69.558  87.598  1.00 34.17 ? 2240 HOH   A O     1 
HETATM 19337 O  O     . HOH   V 10 .    ? -40.356 96.849  103.694 1.00 38.41 ? 2241 HOH   A O     1 
HETATM 19338 O  O     . HOH   V 10 .    ? -42.313 85.245  105.289 1.00 35.47 ? 2242 HOH   A O     1 
HETATM 19339 O  O     . HOH   V 10 .    ? -64.164 47.638  74.071  1.00 39.14 ? 2243 HOH   A O     1 
HETATM 19340 O  O     . HOH   V 10 .    ? -27.129 90.206  115.772 1.00 26.83 ? 2244 HOH   A O     1 
HETATM 19341 O  O     . HOH   V 10 .    ? 12.846  63.451  120.883 1.00 35.33 ? 2245 HOH   A O     1 
HETATM 19342 O  O     . HOH   V 10 .    ? -3.266  74.911  102.081 1.00 31.87 ? 2246 HOH   A O     1 
HETATM 19343 O  O     . HOH   V 10 .    ? -56.662 40.197  67.636  1.00 39.16 ? 2247 HOH   A O     1 
HETATM 19344 O  O     . HOH   V 10 .    ? -64.363 47.268  76.350  1.00 38.72 ? 2248 HOH   A O     1 
HETATM 19345 O  O     . HOH   V 10 .    ? -31.134 78.175  91.022  1.00 34.77 ? 2249 HOH   A O     1 
HETATM 19346 O  O     . HOH   V 10 .    ? -0.837  77.449  126.730 1.00 39.49 ? 2250 HOH   A O     1 
HETATM 19347 O  O     . HOH   V 10 .    ? -37.316 75.362  97.620  1.00 29.71 ? 2251 HOH   A O     1 
HETATM 19348 O  O     . HOH   V 10 .    ? -57.882 72.279  88.549  1.00 44.60 ? 2252 HOH   A O     1 
HETATM 19349 O  O     . HOH   V 10 .    ? -25.997 74.525  132.637 1.00 32.93 ? 2253 HOH   A O     1 
HETATM 19350 O  O     . HOH   V 10 .    ? -39.653 46.987  103.964 1.00 36.92 ? 2254 HOH   A O     1 
HETATM 19351 O  O     . HOH   V 10 .    ? -3.798  57.535  63.452  1.00 43.55 ? 2255 HOH   A O     1 
HETATM 19352 O  O     . HOH   V 10 .    ? -31.460 41.133  98.091  1.00 40.26 ? 2256 HOH   A O     1 
HETATM 19353 O  O     . HOH   V 10 .    ? 11.564  74.557  128.927 1.00 40.28 ? 2257 HOH   A O     1 
HETATM 19354 O  O     . HOH   V 10 .    ? -16.935 54.357  117.288 1.00 39.58 ? 2258 HOH   A O     1 
HETATM 19355 O  O     . HOH   V 10 .    ? 14.978  82.359  119.520 1.00 30.87 ? 2259 HOH   A O     1 
HETATM 19356 O  O     . HOH   V 10 .    ? -37.360 86.092  101.913 1.00 27.41 ? 2260 HOH   A O     1 
HETATM 19357 O  O     . HOH   V 10 .    ? -57.103 32.193  87.840  1.00 27.61 ? 2261 HOH   A O     1 
HETATM 19358 O  O     . HOH   V 10 .    ? 21.168  71.139  95.159  1.00 38.98 ? 2262 HOH   A O     1 
HETATM 19359 O  O     . HOH   V 10 .    ? -44.208 91.206  111.444 1.00 39.68 ? 2263 HOH   A O     1 
HETATM 19360 O  O     . HOH   V 10 .    ? -34.344 55.227  71.348  1.00 38.29 ? 2264 HOH   A O     1 
HETATM 19361 O  O     . HOH   V 10 .    ? -36.567 82.429  120.786 1.00 30.36 ? 2265 HOH   A O     1 
HETATM 19362 O  O     . HOH   V 10 .    ? -47.467 53.763  104.359 1.00 45.66 ? 2266 HOH   A O     1 
HETATM 19363 O  O     . HOH   V 10 .    ? -18.093 92.335  107.761 1.00 34.41 ? 2267 HOH   A O     1 
HETATM 19364 O  O     . HOH   V 10 .    ? -10.909 66.425  127.490 1.00 39.11 ? 2268 HOH   A O     1 
HETATM 19365 O  O     . HOH   V 10 .    ? -41.631 64.464  58.590  1.00 27.31 ? 2269 HOH   A O     1 
HETATM 19366 O  O     . HOH   V 10 .    ? -40.980 68.921  63.327  1.00 38.04 ? 2270 HOH   A O     1 
HETATM 19367 O  O     . HOH   V 10 .    ? -39.114 96.826  113.295 1.00 45.91 ? 2271 HOH   A O     1 
HETATM 19368 O  O     . HOH   V 10 .    ? -66.106 64.247  88.165  1.00 32.76 ? 2272 HOH   A O     1 
HETATM 19369 O  O     . HOH   V 10 .    ? -30.565 91.239  111.259 1.00 31.60 ? 2273 HOH   A O     1 
HETATM 19370 O  O     . HOH   V 10 .    ? -37.273 65.159  108.515 1.00 39.16 ? 2274 HOH   A O     1 
HETATM 19371 O  O     . HOH   V 10 .    ? -19.783 97.869  123.849 1.00 49.41 ? 2275 HOH   A O     1 
HETATM 19372 O  O     . HOH   V 10 .    ? -0.524  52.345  59.131  1.00 36.27 ? 2276 HOH   A O     1 
HETATM 19373 O  O     . HOH   V 10 .    ? -5.790  74.800  103.192 1.00 30.60 ? 2277 HOH   A O     1 
HETATM 19374 O  O     . HOH   V 10 .    ? -27.074 47.919  102.167 1.00 43.20 ? 2278 HOH   A O     1 
HETATM 19375 O  O     . HOH   V 10 .    ? -22.693 64.496  70.664  1.00 48.67 ? 2279 HOH   A O     1 
HETATM 19376 O  O     . HOH   V 10 .    ? -60.568 59.545  62.177  1.00 30.14 ? 2280 HOH   A O     1 
HETATM 19377 O  O     . HOH   V 10 .    ? -22.993 71.089  74.081  1.00 35.31 ? 2281 HOH   A O     1 
HETATM 19378 O  O     . HOH   V 10 .    ? -23.449 64.231  73.025  1.00 43.08 ? 2282 HOH   A O     1 
HETATM 19379 O  O     . HOH   V 10 .    ? -62.110 67.074  60.500  1.00 38.84 ? 2283 HOH   A O     1 
HETATM 19380 O  O     . HOH   V 10 .    ? -44.206 76.301  74.676  1.00 35.21 ? 2284 HOH   A O     1 
HETATM 19381 O  O     . HOH   V 10 .    ? -31.408 70.438  129.507 1.00 45.44 ? 2285 HOH   A O     1 
HETATM 19382 O  O     . HOH   V 10 .    ? -62.074 59.938  95.786  1.00 26.77 ? 2286 HOH   A O     1 
HETATM 19383 O  O     . HOH   V 10 .    ? -33.006 40.634  95.333  1.00 44.19 ? 2287 HOH   A O     1 
HETATM 19384 O  O     . HOH   V 10 .    ? -44.497 92.719  88.903  1.00 41.56 ? 2288 HOH   A O     1 
HETATM 19385 O  O     . HOH   V 10 .    ? -8.809  40.997  69.427  1.00 36.51 ? 2289 HOH   A O     1 
HETATM 19386 O  O     . HOH   V 10 .    ? -39.975 47.332  106.645 1.00 41.59 ? 2290 HOH   A O     1 
HETATM 19387 O  O     . HOH   V 10 .    ? 19.472  64.263  93.264  1.00 33.48 ? 2291 HOH   A O     1 
HETATM 19388 O  O     . HOH   V 10 .    ? -34.184 58.976  106.230 1.00 29.79 ? 2292 HOH   A O     1 
HETATM 19389 O  O     . HOH   V 10 .    ? 5.477   70.825  96.227  1.00 37.61 ? 2293 HOH   A O     1 
HETATM 19390 O  O     . HOH   V 10 .    ? -45.849 78.248  89.973  1.00 23.42 ? 2294 HOH   A O     1 
HETATM 19391 O  O     . HOH   V 10 .    ? 10.945  65.087  114.233 1.00 35.77 ? 2295 HOH   A O     1 
HETATM 19392 O  O     . HOH   V 10 .    ? 0.026   87.307  124.491 1.00 33.22 ? 2296 HOH   A O     1 
HETATM 19393 O  O     . HOH   V 10 .    ? -23.457 75.823  133.472 1.00 34.23 ? 2297 HOH   A O     1 
HETATM 19394 O  O     . HOH   V 10 .    ? -22.854 67.270  129.832 1.00 39.43 ? 2298 HOH   A O     1 
HETATM 19395 O  O     . HOH   V 10 .    ? -41.917 89.042  115.544 1.00 45.18 ? 2299 HOH   A O     1 
HETATM 19396 O  O     . HOH   V 10 .    ? -18.023 53.768  98.770  1.00 34.44 ? 2300 HOH   A O     1 
HETATM 19397 O  O     . HOH   V 10 .    ? -23.884 100.451 101.129 1.00 41.85 ? 2301 HOH   A O     1 
HETATM 19398 O  O     . HOH   V 10 .    ? -67.055 65.317  69.730  1.00 44.54 ? 2302 HOH   A O     1 
HETATM 19399 O  O     . HOH   V 10 .    ? -19.258 52.850  114.706 1.00 45.62 ? 2303 HOH   A O     1 
HETATM 19400 O  O     . HOH   V 10 .    ? -36.168 63.104  90.420  1.00 36.74 ? 2304 HOH   A O     1 
HETATM 19401 O  O     . HOH   V 10 .    ? -47.658 80.041  95.646  1.00 40.03 ? 2305 HOH   A O     1 
HETATM 19402 O  O     . HOH   V 10 .    ? -1.925  80.051  97.424  1.00 29.41 ? 2306 HOH   A O     1 
HETATM 19403 O  O     . HOH   V 10 .    ? -59.347 47.257  63.951  1.00 46.75 ? 2307 HOH   A O     1 
HETATM 19404 O  O     . HOH   V 10 .    ? -19.276 70.710  132.666 1.00 38.17 ? 2308 HOH   A O     1 
HETATM 19405 O  O     . HOH   V 10 .    ? 8.227   69.549  125.369 1.00 44.59 ? 2309 HOH   A O     1 
HETATM 19406 O  O     . HOH   V 10 .    ? -35.122 70.593  82.701  1.00 35.26 ? 2310 HOH   A O     1 
HETATM 19407 O  O     . HOH   V 10 .    ? -9.199  73.156  131.855 1.00 39.67 ? 2311 HOH   A O     1 
HETATM 19408 O  O     . HOH   V 10 .    ? -47.629 33.045  85.339  1.00 37.43 ? 2312 HOH   A O     1 
HETATM 19409 O  O     . HOH   V 10 .    ? -64.073 50.994  73.302  1.00 34.63 ? 2313 HOH   A O     1 
HETATM 19410 O  O     . HOH   V 10 .    ? -18.440 53.847  86.543  1.00 46.09 ? 2314 HOH   A O     1 
HETATM 19411 O  O     . HOH   V 10 .    ? -8.798  61.922  70.446  1.00 37.90 ? 2315 HOH   A O     1 
HETATM 19412 O  O     . HOH   V 10 .    ? -49.755 49.555  104.368 1.00 47.86 ? 2316 HOH   A O     1 
HETATM 19413 O  O     . HOH   V 10 .    ? 11.973  79.016  124.771 1.00 40.05 ? 2317 HOH   A O     1 
HETATM 19414 O  O     . HOH   V 10 .    ? 32.475  71.947  108.035 1.00 53.79 ? 2318 HOH   A O     1 
HETATM 19415 O  O     . HOH   V 10 .    ? -46.600 78.162  117.334 1.00 37.03 ? 2319 HOH   A O     1 
HETATM 19416 O  O     . HOH   V 10 .    ? 26.080  74.167  98.115  1.00 44.58 ? 2320 HOH   A O     1 
HETATM 19417 O  O     . HOH   V 10 .    ? -46.180 63.011  53.929  1.00 39.24 ? 2321 HOH   A O     1 
HETATM 19418 O  O     . HOH   V 10 .    ? -50.600 23.900  81.058  1.00 44.76 ? 2322 HOH   A O     1 
HETATM 19419 O  O     . HOH   V 10 .    ? -51.801 55.073  70.464  1.00 27.00 ? 2323 HOH   A O     1 
HETATM 19420 O  O     . HOH   V 10 .    ? -10.022 66.669  74.428  1.00 32.40 ? 2324 HOH   A O     1 
HETATM 19421 O  O     . HOH   V 10 .    ? -8.593  88.927  95.978  1.00 47.04 ? 2325 HOH   A O     1 
HETATM 19422 O  O     . HOH   V 10 .    ? -31.767 67.906  101.474 1.00 32.49 ? 2326 HOH   A O     1 
HETATM 19423 O  O     . HOH   V 10 .    ? -52.766 56.877  73.854  1.00 27.96 ? 2327 HOH   A O     1 
HETATM 19424 O  O     . HOH   V 10 .    ? -8.788  52.724  104.478 1.00 44.99 ? 2328 HOH   A O     1 
HETATM 19425 O  O     . HOH   V 10 .    ? 13.753  78.675  123.303 1.00 40.37 ? 2329 HOH   A O     1 
HETATM 19426 O  O     . HOH   V 10 .    ? 16.812  87.087  111.784 1.00 42.43 ? 2330 HOH   A O     1 
HETATM 19427 O  O     . HOH   V 10 .    ? -18.744 59.466  111.043 1.00 26.17 ? 2331 HOH   A O     1 
HETATM 19428 O  O     . HOH   V 10 .    ? -27.412 51.103  109.634 1.00 37.09 ? 2332 HOH   A O     1 
HETATM 19429 O  O     . HOH   V 10 .    ? -1.341  92.000  109.285 1.00 31.20 ? 2333 HOH   A O     1 
HETATM 19430 O  O     . HOH   V 10 .    ? -48.682 26.973  75.129  1.00 44.87 ? 2334 HOH   A O     1 
HETATM 19431 O  O     . HOH   V 10 .    ? -15.172 57.671  106.302 1.00 34.07 ? 2335 HOH   A O     1 
HETATM 19432 O  O     . HOH   V 10 .    ? -5.411  47.411  55.783  1.00 37.15 ? 2336 HOH   A O     1 
HETATM 19433 O  O     . HOH   V 10 .    ? -34.849 27.193  72.184  1.00 45.70 ? 2337 HOH   A O     1 
HETATM 19434 O  O     . HOH   V 10 .    ? -50.326 54.943  104.871 1.00 41.26 ? 2338 HOH   A O     1 
HETATM 19435 O  O     . HOH   V 10 .    ? -11.187 40.723  57.682  1.00 40.63 ? 2339 HOH   A O     1 
HETATM 19436 O  O     . HOH   V 10 .    ? -41.932 75.296  120.590 1.00 44.99 ? 2340 HOH   A O     1 
HETATM 19437 O  O     . HOH   V 10 .    ? -30.546 49.240  86.288  1.00 41.58 ? 2341 HOH   A O     1 
HETATM 19438 O  O     . HOH   V 10 .    ? -63.972 65.190  66.521  1.00 35.18 ? 2342 HOH   A O     1 
HETATM 19439 O  O     . HOH   V 10 .    ? -18.914 54.485  118.596 1.00 40.11 ? 2343 HOH   A O     1 
HETATM 19440 O  O     . HOH   V 10 .    ? -39.914 67.717  89.073  1.00 30.99 ? 2344 HOH   A O     1 
HETATM 19441 O  O     . HOH   V 10 .    ? 27.534  59.177  109.725 1.00 48.29 ? 2345 HOH   A O     1 
HETATM 19442 O  O     . HOH   V 10 .    ? -9.351  54.499  97.026  1.00 46.57 ? 2346 HOH   A O     1 
HETATM 19443 O  O     . HOH   V 10 .    ? -4.016  59.849  68.488  1.00 45.32 ? 2347 HOH   A O     1 
HETATM 19444 O  O     . HOH   V 10 .    ? -61.074 72.542  81.826  1.00 37.99 ? 2348 HOH   A O     1 
HETATM 19445 O  O     . HOH   V 10 .    ? -53.397 40.460  63.382  1.00 42.92 ? 2349 HOH   A O     1 
HETATM 19446 O  O     . HOH   V 10 .    ? -40.233 90.376  117.822 1.00 44.67 ? 2350 HOH   A O     1 
HETATM 19447 O  O     . HOH   V 10 .    ? -44.231 81.539  71.494  1.00 47.84 ? 2351 HOH   A O     1 
HETATM 19448 O  O     . HOH   V 10 .    ? -65.934 54.630  78.434  1.00 35.49 ? 2352 HOH   A O     1 
HETATM 19449 O  O     . HOH   V 10 .    ? -47.692 63.810  56.192  1.00 29.46 ? 2353 HOH   A O     1 
HETATM 19450 O  O     . HOH   V 10 .    ? -59.824 64.124  92.307  1.00 29.64 ? 2354 HOH   A O     1 
HETATM 19451 O  O     . HOH   V 10 .    ? -26.893 65.322  102.789 1.00 31.50 ? 2355 HOH   A O     1 
HETATM 19452 O  O     . HOH   V 10 .    ? -10.780 60.677  127.943 1.00 36.49 ? 2356 HOH   A O     1 
HETATM 19453 O  O     . HOH   V 10 .    ? -11.356 63.855  51.334  1.00 42.99 ? 2357 HOH   A O     1 
HETATM 19454 O  O     . HOH   V 10 .    ? -23.136 55.078  52.111  1.00 40.47 ? 2358 HOH   A O     1 
HETATM 19455 O  O     . HOH   V 10 .    ? -46.875 30.803  73.104  1.00 40.56 ? 2359 HOH   A O     1 
HETATM 19456 O  O     . HOH   V 10 .    ? -22.687 73.987  69.813  1.00 33.08 ? 2360 HOH   A O     1 
HETATM 19457 O  O     . HOH   V 10 .    ? -7.506  72.727  103.598 1.00 33.77 ? 2361 HOH   A O     1 
HETATM 19458 O  O     . HOH   V 10 .    ? -33.783 46.017  65.684  1.00 45.38 ? 2362 HOH   A O     1 
HETATM 19459 O  O     . HOH   V 10 .    ? -20.729 74.094  104.659 1.00 33.35 ? 2363 HOH   A O     1 
HETATM 19460 O  O     . HOH   V 10 .    ? 7.563   62.445  112.475 1.00 34.41 ? 2364 HOH   A O     1 
HETATM 19461 O  O     . HOH   V 10 .    ? -40.808 46.856  59.930  1.00 35.35 ? 2365 HOH   A O     1 
HETATM 19462 O  O     . HOH   V 10 .    ? -10.414 93.559  114.485 1.00 39.88 ? 2366 HOH   A O     1 
HETATM 19463 O  O     . HOH   V 10 .    ? 12.464  88.431  118.970 1.00 38.97 ? 2367 HOH   A O     1 
HETATM 19464 O  O     . HOH   V 10 .    ? -55.491 27.628  81.881  1.00 43.37 ? 2368 HOH   A O     1 
HETATM 19465 O  O     . HOH   V 10 .    ? -55.235 57.556  102.307 1.00 30.09 ? 2369 HOH   A O     1 
HETATM 19466 O  O     . HOH   V 10 .    ? -44.434 69.503  111.300 1.00 41.95 ? 2370 HOH   A O     1 
HETATM 19467 O  O     . HOH   V 10 .    ? -11.515 59.614  106.787 1.00 34.57 ? 2371 HOH   A O     1 
HETATM 19468 O  O     . HOH   V 10 .    ? -26.061 67.257  94.152  1.00 40.76 ? 2372 HOH   A O     1 
HETATM 19469 O  O     . HOH   V 10 .    ? -28.727 57.359  88.662  1.00 29.46 ? 2373 HOH   A O     1 
HETATM 19470 O  O     . HOH   V 10 .    ? 11.211  88.652  111.449 1.00 43.65 ? 2374 HOH   A O     1 
HETATM 19471 O  O     . HOH   V 10 .    ? 6.935   91.301  118.624 1.00 34.92 ? 2375 HOH   A O     1 
HETATM 19472 O  O     . HOH   V 10 .    ? -24.657 100.450 91.510  1.00 41.99 ? 2376 HOH   A O     1 
HETATM 19473 O  O     . HOH   V 10 .    ? -64.482 63.122  68.424  1.00 37.93 ? 2377 HOH   A O     1 
HETATM 19474 O  O     . HOH   V 10 .    ? -39.265 75.777  122.203 1.00 41.71 ? 2378 HOH   A O     1 
HETATM 19475 O  O     . HOH   V 10 .    ? 16.944  84.130  112.839 1.00 39.09 ? 2379 HOH   A O     1 
HETATM 19476 O  O     . HOH   V 10 .    ? -32.968 84.143  77.041  1.00 30.99 ? 2380 HOH   A O     1 
HETATM 19477 O  O     . HOH   V 10 .    ? 12.628  63.975  116.693 1.00 40.09 ? 2381 HOH   A O     1 
HETATM 19478 O  O     . HOH   V 10 .    ? -66.489 74.335  71.792  1.00 45.52 ? 2382 HOH   A O     1 
HETATM 19479 O  O     . HOH   V 10 .    ? -52.356 51.093  104.090 1.00 48.01 ? 2383 HOH   A O     1 
HETATM 19480 O  O     . HOH   V 10 .    ? -51.239 68.275  107.920 1.00 37.91 ? 2384 HOH   A O     1 
HETATM 19481 O  O     . HOH   V 10 .    ? -29.051 60.714  120.924 1.00 36.43 ? 2385 HOH   A O     1 
HETATM 19482 O  O     . HOH   V 10 .    ? -7.850  92.234  99.624  1.00 32.60 ? 2386 HOH   A O     1 
HETATM 19483 O  O     . HOH   V 10 .    ? -1.659  89.008  97.372  1.00 39.29 ? 2387 HOH   A O     1 
HETATM 19484 O  O     . HOH   V 10 .    ? -43.804 24.655  80.663  1.00 47.35 ? 2388 HOH   A O     1 
HETATM 19485 O  O     . HOH   V 10 .    ? -67.676 62.137  68.941  1.00 45.11 ? 2389 HOH   A O     1 
HETATM 19486 O  O     . HOH   V 10 .    ? -24.651 94.057  108.337 1.00 46.87 ? 2390 HOH   A O     1 
HETATM 19487 O  O     . HOH   V 10 .    ? -10.467 63.226  127.886 1.00 39.74 ? 2391 HOH   A O     1 
HETATM 19488 O  O     . HOH   V 10 .    ? -58.953 30.647  86.535  1.00 35.42 ? 2392 HOH   A O     1 
HETATM 19489 O  O     . HOH   V 10 .    ? -6.245  86.661  88.794  1.00 43.45 ? 2393 HOH   A O     1 
HETATM 19490 O  O     . HOH   V 10 .    ? -20.031 52.835  105.773 1.00 38.04 ? 2394 HOH   A O     1 
HETATM 19491 O  O     . HOH   V 10 .    ? -39.682 64.962  56.553  1.00 37.25 ? 2395 HOH   A O     1 
HETATM 19492 O  O     . HOH   V 10 .    ? -59.992 52.398  95.922  1.00 43.99 ? 2396 HOH   A O     1 
HETATM 19493 O  O     . HOH   V 10 .    ? -20.949 93.008  107.234 1.00 29.79 ? 2397 HOH   A O     1 
HETATM 19494 O  O     . HOH   V 10 .    ? -39.304 35.631  88.874  1.00 35.09 ? 2398 HOH   A O     1 
HETATM 19495 O  O     . HOH   V 10 .    ? -2.596  56.744  70.831  1.00 32.90 ? 2399 HOH   A O     1 
HETATM 19496 O  O     . HOH   V 10 .    ? -21.346 63.356  81.791  1.00 40.01 ? 2400 HOH   A O     1 
HETATM 19497 O  O     . HOH   V 10 .    ? -35.431 73.440  86.736  1.00 33.14 ? 2401 HOH   A O     1 
HETATM 19498 O  O     . HOH   V 10 .    ? -17.030 57.463  110.492 1.00 40.90 ? 2402 HOH   A O     1 
HETATM 19499 O  O     . HOH   V 10 .    ? -50.720 80.907  83.762  1.00 39.21 ? 2403 HOH   A O     1 
HETATM 19500 O  O     . HOH   V 10 .    ? -9.896  66.680  132.314 1.00 35.84 ? 2404 HOH   A O     1 
HETATM 19501 O  O     . HOH   V 10 .    ? -44.857 88.101  99.441  1.00 40.01 ? 2405 HOH   A O     1 
HETATM 19502 O  O     . HOH   V 10 .    ? -45.473 28.682  87.042  1.00 36.41 ? 2406 HOH   A O     1 
HETATM 19503 O  O     . HOH   V 10 .    ? -7.009  65.615  92.744  1.00 35.76 ? 2407 HOH   A O     1 
HETATM 19504 O  O     . HOH   V 10 .    ? -54.102 42.600  60.822  1.00 49.66 ? 2408 HOH   A O     1 
HETATM 19505 O  O     . HOH   V 10 .    ? -62.924 61.056  93.580  1.00 36.26 ? 2409 HOH   A O     1 
HETATM 19506 O  O     . HOH   V 10 .    ? -46.237 56.741  54.517  1.00 38.26 ? 2410 HOH   A O     1 
HETATM 19507 O  O     . HOH   V 10 .    ? -5.607  90.366  98.912  1.00 44.84 ? 2411 HOH   A O     1 
HETATM 19508 O  O     . HOH   V 10 .    ? -31.786 74.174  83.735  1.00 28.02 ? 2412 HOH   A O     1 
HETATM 19509 O  O     . HOH   V 10 .    ? -27.840 63.768  90.677  1.00 34.54 ? 2413 HOH   A O     1 
HETATM 19510 O  O     . HOH   V 10 .    ? -6.779  54.949  82.739  1.00 27.73 ? 2414 HOH   A O     1 
HETATM 19511 O  O     . HOH   V 10 .    ? -28.264 49.079  104.500 1.00 41.41 ? 2415 HOH   A O     1 
HETATM 19512 O  O     . HOH   V 10 .    ? 4.879   60.372  98.366  1.00 27.54 ? 2416 HOH   A O     1 
HETATM 19513 O  O     . HOH   V 10 .    ? -27.023 93.122  110.344 1.00 40.31 ? 2417 HOH   A O     1 
HETATM 19514 O  O     . HOH   V 10 .    ? -46.667 80.230  74.602  1.00 53.50 ? 2418 HOH   A O     1 
HETATM 19515 O  O     . HOH   V 10 .    ? -10.500 78.485  92.469  1.00 20.51 ? 2419 HOH   A O     1 
HETATM 19516 O  O     . HOH   V 10 .    ? -8.332  61.434  86.793  1.00 38.28 ? 2420 HOH   A O     1 
HETATM 19517 O  O     . HOH   V 10 .    ? -34.565 76.003  87.346  1.00 28.49 ? 2421 HOH   A O     1 
HETATM 19518 O  O     . HOH   V 10 .    ? 6.719   66.695  93.942  1.00 34.91 ? 2422 HOH   A O     1 
HETATM 19519 O  O     . HOH   V 10 .    ? -24.667 65.358  96.958  1.00 38.91 ? 2423 HOH   A O     1 
HETATM 19520 O  O     . HOH   V 10 .    ? 3.618   76.264  95.513  1.00 43.98 ? 2424 HOH   A O     1 
HETATM 19521 O  O     . HOH   V 10 .    ? -58.467 74.562  94.812  1.00 42.91 ? 2425 HOH   A O     1 
HETATM 19522 O  O     . HOH   V 10 .    ? -67.001 54.502  82.256  1.00 30.59 ? 2426 HOH   A O     1 
HETATM 19523 O  O     . HOH   V 10 .    ? -3.422  68.182  93.000  1.00 42.38 ? 2427 HOH   A O     1 
HETATM 19524 O  O     . HOH   V 10 .    ? -45.244 84.789  90.371  1.00 47.99 ? 2428 HOH   A O     1 
HETATM 19525 O  O     . HOH   V 10 .    ? -38.159 91.180  122.627 1.00 48.75 ? 2429 HOH   A O     1 
HETATM 19526 O  O     . HOH   V 10 .    ? -44.278 23.225  78.813  1.00 45.09 ? 2430 HOH   A O     1 
HETATM 19527 O  O     . HOH   V 10 .    ? -35.023 54.830  107.462 1.00 33.55 ? 2431 HOH   A O     1 
HETATM 19528 O  O     . HOH   V 10 .    ? -8.976  66.996  129.551 1.00 40.26 ? 2432 HOH   A O     1 
HETATM 19529 O  O     . HOH   V 10 .    ? -24.556 47.023  58.062  1.00 43.82 ? 2433 HOH   A O     1 
HETATM 19530 O  O     . HOH   V 10 .    ? 22.681  79.055  100.322 1.00 41.27 ? 2434 HOH   A O     1 
HETATM 19531 O  O     . HOH   V 10 .    ? -52.611 48.410  57.941  1.00 37.16 ? 2435 HOH   A O     1 
HETATM 19532 O  O     . HOH   V 10 .    ? -18.388 70.852  69.197  1.00 39.35 ? 2436 HOH   A O     1 
HETATM 19533 O  O     . HOH   V 10 .    ? -34.154 52.349  71.435  1.00 42.12 ? 2437 HOH   A O     1 
HETATM 19534 O  O     . HOH   V 10 .    ? -60.935 38.208  88.803  1.00 36.87 ? 2438 HOH   A O     1 
HETATM 19535 O  O     . HOH   V 10 .    ? -53.978 46.345  63.150  1.00 44.00 ? 2439 HOH   A O     1 
HETATM 19536 O  O     . HOH   V 10 .    ? -31.349 76.337  74.488  1.00 32.37 ? 2440 HOH   A O     1 
HETATM 19537 O  O     . HOH   V 10 .    ? -17.031 96.876  92.210  1.00 38.63 ? 2441 HOH   A O     1 
HETATM 19538 O  O     . HOH   V 10 .    ? -14.640 95.778  114.417 1.00 44.72 ? 2442 HOH   A O     1 
HETATM 19539 O  O     . HOH   V 10 .    ? -35.708 39.745  71.166  1.00 41.55 ? 2443 HOH   A O     1 
HETATM 19540 O  O     . HOH   V 10 .    ? -13.503 52.224  99.784  1.00 47.71 ? 2444 HOH   A O     1 
HETATM 19541 O  O     . HOH   V 10 .    ? -52.294 74.076  61.997  1.00 23.26 ? 2445 HOH   A O     1 
HETATM 19542 O  O     . HOH   V 10 .    ? -36.025 90.433  123.581 1.00 37.17 ? 2446 HOH   A O     1 
HETATM 19543 O  O     . HOH   V 10 .    ? -39.180 70.190  118.429 1.00 37.18 ? 2447 HOH   A O     1 
HETATM 19544 O  O     . HOH   V 10 .    ? -3.614  69.578  95.128  1.00 48.00 ? 2448 HOH   A O     1 
HETATM 19545 O  O     . HOH   V 10 .    ? -34.868 38.972  94.653  1.00 36.39 ? 2449 HOH   A O     1 
HETATM 19546 O  O     . HOH   V 10 .    ? -25.822 64.914  64.428  1.00 47.60 ? 2450 HOH   A O     1 
HETATM 19547 O  O     . HOH   V 10 .    ? 10.920  90.680  119.611 1.00 47.21 ? 2451 HOH   A O     1 
HETATM 19548 O  O     . HOH   V 10 .    ? -52.604 66.284  104.962 1.00 36.85 ? 2452 HOH   A O     1 
HETATM 19549 O  O     . HOH   V 10 .    ? -31.906 42.401  72.193  1.00 47.23 ? 2453 HOH   A O     1 
HETATM 19550 O  O     . HOH   V 10 .    ? -63.618 48.934  71.987  1.00 38.68 ? 2454 HOH   A O     1 
HETATM 19551 O  O     . HOH   V 10 .    ? -51.682 80.720  87.423  1.00 46.17 ? 2455 HOH   A O     1 
HETATM 19552 O  O     . HOH   V 10 .    ? -58.216 32.137  90.313  1.00 29.62 ? 2456 HOH   A O     1 
HETATM 19553 O  O     . HOH   V 10 .    ? -41.935 63.838  106.264 1.00 39.20 ? 2457 HOH   A O     1 
HETATM 19554 O  O     . HOH   V 10 .    ? -45.026 24.660  84.835  1.00 48.23 ? 2458 HOH   A O     1 
HETATM 19555 O  O     . HOH   V 10 .    ? -10.888 68.798  136.382 1.00 45.70 ? 2459 HOH   A O     1 
HETATM 19556 O  O     . HOH   V 10 .    ? -53.274 45.605  94.702  1.00 37.49 ? 2460 HOH   A O     1 
HETATM 19557 O  O     . HOH   V 10 .    ? -56.525 74.582  79.362  1.00 33.14 ? 2461 HOH   A O     1 
HETATM 19558 O  O     . HOH   V 10 .    ? -52.427 63.910  100.724 1.00 32.45 ? 2462 HOH   A O     1 
HETATM 19559 O  O     . HOH   V 10 .    ? -37.372 63.053  114.200 1.00 34.53 ? 2463 HOH   A O     1 
HETATM 19560 O  O     . HOH   V 10 .    ? -30.288 79.537  125.673 1.00 38.03 ? 2464 HOH   A O     1 
HETATM 19561 O  O     . HOH   V 10 .    ? -37.945 69.083  95.578  1.00 35.80 ? 2465 HOH   A O     1 
HETATM 19562 O  O     . HOH   V 10 .    ? -12.984 52.969  79.489  1.00 40.54 ? 2466 HOH   A O     1 
HETATM 19563 O  O     . HOH   V 10 .    ? 20.362  61.509  96.463  1.00 33.83 ? 2467 HOH   A O     1 
HETATM 19564 O  O     . HOH   V 10 .    ? -23.873 77.873  68.341  1.00 44.58 ? 2468 HOH   A O     1 
HETATM 19565 O  O     . HOH   V 10 .    ? -49.613 59.492  55.269  1.00 40.01 ? 2469 HOH   A O     1 
HETATM 19566 O  O     . HOH   V 10 .    ? -35.346 38.886  90.054  1.00 40.98 ? 2470 HOH   A O     1 
HETATM 19567 O  O     . HOH   V 10 .    ? -12.764 93.636  106.052 1.00 36.42 ? 2471 HOH   A O     1 
HETATM 19568 O  O     . HOH   V 10 .    ? -67.124 65.881  83.334  1.00 25.21 ? 2472 HOH   A O     1 
HETATM 19569 O  O     . HOH   V 10 .    ? -37.898 74.308  93.317  1.00 38.46 ? 2473 HOH   A O     1 
HETATM 19570 O  O     . HOH   V 10 .    ? 6.608   81.403  127.298 1.00 35.69 ? 2474 HOH   A O     1 
HETATM 19571 O  O     . HOH   V 10 .    ? -33.671 80.618  74.611  1.00 30.46 ? 2475 HOH   A O     1 
HETATM 19572 O  O     . HOH   V 10 .    ? 3.802   64.744  96.392  1.00 28.81 ? 2476 HOH   A O     1 
HETATM 19573 O  O     . HOH   V 10 .    ? -56.827 44.133  92.511  1.00 35.99 ? 2477 HOH   A O     1 
HETATM 19574 O  O     . HOH   V 10 .    ? -41.587 48.568  108.140 1.00 41.03 ? 2478 HOH   A O     1 
HETATM 19575 O  O     . HOH   V 10 .    ? -22.597 91.339  103.824 1.00 36.98 ? 2479 HOH   A O     1 
HETATM 19576 O  O     . HOH   V 10 .    ? -25.768 83.333  70.027  1.00 43.69 ? 2480 HOH   A O     1 
HETATM 19577 O  O     . HOH   V 10 .    ? -38.311 71.057  92.169  1.00 44.44 ? 2481 HOH   A O     1 
HETATM 19578 O  O     . HOH   V 10 .    ? -18.492 74.351  109.334 1.00 23.18 ? 2482 HOH   A O     1 
HETATM 19579 O  O     . HOH   V 10 .    ? -41.071 68.332  93.567  1.00 31.66 ? 2483 HOH   A O     1 
HETATM 19580 O  O     . HOH   V 10 .    ? -66.813 47.361  73.650  1.00 35.40 ? 2484 HOH   A O     1 
HETATM 19581 O  O     . HOH   V 10 .    ? 0.393   64.126  114.993 1.00 45.07 ? 2485 HOH   A O     1 
HETATM 19582 O  O     . HOH   V 10 .    ? -44.735 82.386  88.796  1.00 42.18 ? 2486 HOH   A O     1 
HETATM 19583 O  O     . HOH   V 10 .    ? -33.641 81.025  122.737 1.00 34.03 ? 2487 HOH   A O     1 
HETATM 19584 O  O     . HOH   V 10 .    ? -24.781 97.321  126.040 1.00 41.78 ? 2488 HOH   A O     1 
HETATM 19585 O  O     . HOH   V 10 .    ? -30.156 62.788  92.039  1.00 33.97 ? 2489 HOH   A O     1 
HETATM 19586 O  O     . HOH   V 10 .    ? 10.801  79.502  128.852 1.00 38.15 ? 2490 HOH   A O     1 
HETATM 19587 O  O     . HOH   V 10 .    ? 2.037   74.978  119.626 1.00 42.26 ? 2491 HOH   A O     1 
HETATM 19588 O  O     . HOH   V 10 .    ? -25.504 62.069  102.218 1.00 31.38 ? 2492 HOH   A O     1 
HETATM 19589 O  O     . HOH   V 10 .    ? -53.119 68.890  100.851 1.00 29.96 ? 2493 HOH   A O     1 
HETATM 19590 O  O     . HOH   V 10 .    ? -11.352 96.229  111.907 1.00 35.77 ? 2494 HOH   A O     1 
HETATM 19591 O  O     . HOH   V 10 .    ? -45.275 94.525  97.597  1.00 46.41 ? 2495 HOH   A O     1 
HETATM 19592 O  O     . HOH   V 10 .    ? 18.224  64.271  90.620  1.00 42.54 ? 2496 HOH   A O     1 
HETATM 19593 O  O     . HOH   V 10 .    ? -33.208 58.241  113.692 1.00 41.66 ? 2497 HOH   A O     1 
HETATM 19594 O  O     . HOH   V 10 .    ? -15.363 53.316  105.328 1.00 44.99 ? 2498 HOH   A O     1 
HETATM 19595 O  O     . HOH   V 10 .    ? -56.428 49.408  97.903  1.00 46.41 ? 2499 HOH   A O     1 
HETATM 19596 O  O     . HOH   V 10 .    ? -24.606 66.792  63.048  1.00 47.72 ? 2500 HOH   A O     1 
HETATM 19597 O  O     . HOH   V 10 .    ? -8.833  57.426  84.342  1.00 37.88 ? 2501 HOH   A O     1 
HETATM 19598 O  O     . HOH   V 10 .    ? -9.342  73.537  129.307 1.00 38.08 ? 2502 HOH   A O     1 
HETATM 19599 O  O     . HOH   V 10 .    ? -62.611 53.734  65.868  1.00 35.25 ? 2503 HOH   A O     1 
HETATM 19600 O  O     . HOH   V 10 .    ? -25.638 65.195  91.617  1.00 38.75 ? 2504 HOH   A O     1 
HETATM 19601 O  O     . HOH   V 10 .    ? -0.757  60.803  112.521 1.00 38.19 ? 2505 HOH   A O     1 
HETATM 19602 O  O     . HOH   V 10 .    ? -8.818  52.662  101.041 1.00 37.99 ? 2506 HOH   A O     1 
HETATM 19603 O  O     . HOH   V 10 .    ? -24.210 96.942  121.344 1.00 38.57 ? 2507 HOH   A O     1 
HETATM 19604 O  O     . HOH   V 10 .    ? -58.771 55.432  101.033 1.00 42.28 ? 2508 HOH   A O     1 
HETATM 19605 O  O     . HOH   V 10 .    ? -31.950 98.503  99.420  1.00 45.91 ? 2509 HOH   A O     1 
HETATM 19606 O  O     . HOH   V 10 .    ? -1.440  83.523  93.785  1.00 44.57 ? 2510 HOH   A O     1 
HETATM 19607 O  O     . HOH   V 10 .    ? -2.144  73.566  118.977 1.00 33.66 ? 2511 HOH   A O     1 
HETATM 19608 O  O     . HOH   V 10 .    ? -28.597 75.883  129.965 1.00 41.33 ? 2512 HOH   A O     1 
HETATM 19609 O  O     . HOH   V 10 .    ? -48.378 56.684  56.004  1.00 30.79 ? 2513 HOH   A O     1 
HETATM 19610 O  O     . HOH   V 10 .    ? -34.195 62.134  89.567  1.00 41.51 ? 2514 HOH   A O     1 
HETATM 19611 O  O     . HOH   V 10 .    ? -3.993  79.808  124.975 1.00 34.51 ? 2515 HOH   A O     1 
HETATM 19612 O  O     . HOH   V 10 .    ? -60.317 44.974  90.390  1.00 37.43 ? 2516 HOH   A O     1 
HETATM 19613 O  O     . HOH   V 10 .    ? -46.743 80.714  89.991  1.00 39.02 ? 2517 HOH   A O     1 
HETATM 19614 O  O     . HOH   V 10 .    ? -52.062 73.058  102.675 1.00 31.65 ? 2518 HOH   A O     1 
HETATM 19615 O  O     . HOH   V 10 .    ? -26.721 66.530  98.165  1.00 38.26 ? 2519 HOH   A O     1 
HETATM 19616 O  O     . HOH   V 10 .    ? -36.764 82.316  77.276  1.00 35.90 ? 2520 HOH   A O     1 
HETATM 19617 O  O     . HOH   V 10 .    ? 0.860   71.130  117.571 1.00 36.43 ? 2521 HOH   A O     1 
HETATM 19618 O  O     . HOH   V 10 .    ? -28.755 77.646  70.398  1.00 33.53 ? 2522 HOH   A O     1 
HETATM 19619 O  O     . HOH   V 10 .    ? -52.638 75.348  101.689 1.00 40.61 ? 2523 HOH   A O     1 
HETATM 19620 O  O     . HOH   V 10 .    ? -48.920 77.592  93.753  1.00 37.25 ? 2524 HOH   A O     1 
HETATM 19621 O  O     . HOH   V 10 .    ? -24.627 52.192  100.230 1.00 32.79 ? 2525 HOH   A O     1 
HETATM 19622 O  O     . HOH   V 10 .    ? -13.444 60.508  86.937  1.00 36.57 ? 2526 HOH   A O     1 
HETATM 19623 O  O     . HOH   V 10 .    ? -31.831 54.703  110.748 1.00 40.41 ? 2527 HOH   A O     1 
HETATM 19624 O  O     . HOH   V 10 .    ? 23.039  70.043  115.934 1.00 29.44 ? 2528 HOH   A O     1 
HETATM 19625 O  O     . HOH   V 10 .    ? 6.758   62.565  94.915  1.00 29.62 ? 2529 HOH   A O     1 
HETATM 19626 O  O     . HOH   V 10 .    ? -20.222 74.808  101.838 1.00 30.09 ? 2530 HOH   A O     1 
HETATM 19627 O  O     . HOH   V 10 .    ? -14.447 51.652  111.667 1.00 46.65 ? 2531 HOH   A O     1 
HETATM 19628 O  O     . HOH   V 10 .    ? -29.258 92.334  108.980 1.00 33.90 ? 2532 HOH   A O     1 
HETATM 19629 O  O     . HOH   V 10 .    ? -18.725 46.794  53.185  1.00 36.20 ? 2533 HOH   A O     1 
HETATM 19630 O  O     . HOH   V 10 .    ? 20.933  70.718  118.911 1.00 41.05 ? 2534 HOH   A O     1 
HETATM 19631 O  O     . HOH   V 10 .    ? -62.699 55.468  69.985  1.00 25.46 ? 2535 HOH   A O     1 
HETATM 19632 O  O     . HOH   V 10 .    ? -2.257  91.839  98.430  1.00 30.58 ? 2536 HOH   A O     1 
HETATM 19633 O  O     . HOH   V 10 .    ? -32.079 75.272  85.545  1.00 36.61 ? 2537 HOH   A O     1 
HETATM 19634 O  O     . HOH   V 10 .    ? -20.795 89.829  138.045 1.00 47.60 ? 2538 HOH   A O     1 
HETATM 19635 O  O     . HOH   V 10 .    ? -29.255 95.217  108.211 1.00 45.69 ? 2539 HOH   A O     1 
HETATM 19636 O  O     . HOH   V 10 .    ? -20.745 52.756  101.375 1.00 43.35 ? 2540 HOH   A O     1 
HETATM 19637 O  O     . HOH   V 10 .    ? -0.281  86.097  96.877  1.00 43.35 ? 2541 HOH   A O     1 
HETATM 19638 O  O     . HOH   V 10 .    ? -56.790 72.944  99.085  1.00 38.89 ? 2542 HOH   A O     1 
HETATM 19639 O  O     . HOH   V 10 .    ? -58.756 36.992  90.047  1.00 34.56 ? 2543 HOH   A O     1 
HETATM 19640 O  O     . HOH   V 10 .    ? -8.653  76.504  129.492 1.00 38.70 ? 2544 HOH   A O     1 
HETATM 19641 O  O     . HOH   V 10 .    ? -54.461 55.037  102.626 1.00 41.82 ? 2545 HOH   A O     1 
HETATM 19642 O  O     . HOH   V 10 .    ? -10.024 48.892  107.252 1.00 40.60 ? 2546 HOH   A O     1 
HETATM 19643 O  O     . HOH   V 10 .    ? -13.562 96.260  117.156 1.00 38.77 ? 2547 HOH   A O     1 
HETATM 19644 O  O     . HOH   V 10 .    ? -66.998 38.874  73.795  1.00 38.16 ? 2548 HOH   A O     1 
HETATM 19645 O  O     . HOH   V 10 .    ? 24.971  62.855  100.536 1.00 41.03 ? 2549 HOH   A O     1 
HETATM 19646 O  O     . HOH   V 10 .    ? -32.756 58.369  84.815  1.00 40.11 ? 2550 HOH   A O     1 
HETATM 19647 O  O     . HOH   V 10 .    ? 30.294  62.874  111.255 1.00 41.58 ? 2551 HOH   A O     1 
HETATM 19648 O  O     . HOH   V 10 .    ? 23.927  57.908  100.760 1.00 36.86 ? 2552 HOH   A O     1 
HETATM 19649 O  O     . HOH   V 10 .    ? -48.016 37.290  100.610 1.00 38.12 ? 2553 HOH   A O     1 
HETATM 19650 O  O     . HOH   V 10 .    ? -31.004 83.969  73.629  1.00 36.38 ? 2554 HOH   A O     1 
HETATM 19651 O  O     . HOH   V 10 .    ? -3.819  87.752  96.969  1.00 39.62 ? 2555 HOH   A O     1 
HETATM 19652 O  O     . HOH   V 10 .    ? -33.569 76.195  89.899  1.00 45.72 ? 2556 HOH   A O     1 
HETATM 19653 O  O     . HOH   V 10 .    ? -63.423 57.754  96.477  1.00 34.93 ? 2557 HOH   A O     1 
HETATM 19654 O  O     . HOH   V 10 .    ? -55.594 46.152  65.156  1.00 37.98 ? 2558 HOH   A O     1 
HETATM 19655 O  O     . HOH   V 10 .    ? 2.678   71.009  95.471  1.00 41.02 ? 2559 HOH   A O     1 
HETATM 19656 O  O     . HOH   V 10 .    ? -8.324  48.825  51.279  1.00 41.54 ? 2560 HOH   A O     1 
HETATM 19657 O  O     . HOH   V 10 .    ? -9.455  62.229  94.092  1.00 35.10 ? 2561 HOH   A O     1 
HETATM 19658 O  O     . HOH   V 10 .    ? 10.972  88.861  108.203 1.00 48.99 ? 2562 HOH   A O     1 
HETATM 19659 O  O     . HOH   V 10 .    ? -23.055 52.081  97.600  1.00 38.06 ? 2563 HOH   A O     1 
HETATM 19660 O  O     . HOH   V 10 .    ? -58.411 59.423  103.043 1.00 42.31 ? 2564 HOH   A O     1 
HETATM 19661 O  O     . HOH   V 10 .    ? -39.344 29.755  95.770  1.00 46.91 ? 2565 HOH   A O     1 
HETATM 19662 O  O     . HOH   V 10 .    ? 3.714   69.179  88.433  1.00 34.22 ? 2566 HOH   A O     1 
HETATM 19663 O  O     . HOH   V 10 .    ? -24.072 50.276  95.602  1.00 37.77 ? 2567 HOH   A O     1 
HETATM 19664 O  O     . HOH   V 10 .    ? -51.906 47.073  96.523  1.00 32.00 ? 2568 HOH   A O     1 
HETATM 19665 O  O     . HOH   V 10 .    ? -54.768 80.042  84.114  1.00 45.86 ? 2569 HOH   A O     1 
HETATM 19666 O  O     . HOH   V 10 .    ? 8.441   73.786  129.174 1.00 46.32 ? 2570 HOH   A O     1 
HETATM 19667 O  O     . HOH   V 10 .    ? -18.471 73.760  106.301 1.00 25.62 ? 2571 HOH   A O     1 
HETATM 19668 O  O     . HOH   V 10 .    ? -32.413 65.407  124.633 1.00 34.80 ? 2572 HOH   A O     1 
HETATM 19669 O  O     . HOH   V 10 .    ? -3.369  83.350  112.410 1.00 30.42 ? 2573 HOH   A O     1 
HETATM 19670 O  O     . HOH   V 10 .    ? -30.098 60.208  86.039  1.00 36.09 ? 2574 HOH   A O     1 
HETATM 19671 O  O     . HOH   V 10 .    ? -8.615  70.779  132.457 1.00 41.40 ? 2575 HOH   A O     1 
HETATM 19672 O  O     . HOH   V 10 .    ? -56.751 76.123  76.945  1.00 32.07 ? 2576 HOH   A O     1 
HETATM 19673 O  O     . HOH   V 10 .    ? 8.176   76.438  128.229 1.00 45.42 ? 2577 HOH   A O     1 
HETATM 19674 O  O     . HOH   V 10 .    ? -41.071 82.553  68.713  1.00 37.27 ? 2578 HOH   A O     1 
HETATM 19675 O  O     . HOH   V 10 .    ? -64.878 60.622  66.281  1.00 42.64 ? 2579 HOH   A O     1 
HETATM 19676 O  O     . HOH   V 10 .    ? -35.320 84.414  77.037  1.00 43.76 ? 2580 HOH   A O     1 
HETATM 19677 O  O     . HOH   V 10 .    ? -29.344 59.936  88.600  1.00 23.79 ? 2581 HOH   A O     1 
HETATM 19678 O  O     . HOH   V 10 .    ? -1.754  75.052  121.023 1.00 36.44 ? 2582 HOH   A O     1 
HETATM 19679 O  O     . HOH   V 10 .    ? 5.509   70.412  87.129  1.00 41.54 ? 2583 HOH   A O     1 
HETATM 19680 O  O     . HOH   V 10 .    ? -19.224 57.444  106.688 1.00 30.20 ? 2584 HOH   A O     1 
HETATM 19681 O  O     . HOH   V 10 .    ? -61.625 70.575  85.667  1.00 33.76 ? 2585 HOH   A O     1 
HETATM 19682 O  O     . HOH   V 10 .    ? -56.860 52.444  98.733  1.00 33.90 ? 2586 HOH   A O     1 
HETATM 19683 O  O     . HOH   V 10 .    ? -54.958 52.955  100.658 1.00 34.38 ? 2587 HOH   A O     1 
HETATM 19684 O  O     . HOH   V 10 .    ? -65.855 46.701  68.673  1.00 39.02 ? 2588 HOH   A O     1 
HETATM 19685 O  O     . HOH   V 10 .    ? -21.949 68.467  132.267 1.00 40.48 ? 2589 HOH   A O     1 
HETATM 19686 O  O     . HOH   V 10 .    ? -15.248 39.417  70.844  1.00 48.55 ? 2590 HOH   A O     1 
HETATM 19687 O  O     . HOH   V 10 .    ? -2.447  84.885  96.701  1.00 33.90 ? 2591 HOH   A O     1 
HETATM 19688 O  O     . HOH   V 10 .    ? 12.670  62.420  93.279  1.00 36.45 ? 2592 HOH   A O     1 
HETATM 19689 O  O     . HOH   V 10 .    ? -41.589 82.708  77.623  1.00 49.50 ? 2593 HOH   A O     1 
HETATM 19690 O  O     . HOH   V 10 .    ? -12.289 61.716  105.172 1.00 31.35 ? 2594 HOH   A O     1 
HETATM 19691 O  O     . HOH   V 10 .    ? -61.915 52.900  93.953  1.00 41.75 ? 2595 HOH   A O     1 
HETATM 19692 O  O     . HOH   V 10 .    ? -57.284 27.963  92.394  1.00 37.78 ? 2596 HOH   A O     1 
HETATM 19693 O  O     . HOH   V 10 .    ? -42.439 26.228  85.338  1.00 49.33 ? 2597 HOH   A O     1 
HETATM 19694 O  O     . HOH   V 10 .    ? 22.961  63.239  95.396  1.00 45.04 ? 2598 HOH   A O     1 
HETATM 19695 O  O     . HOH   V 10 .    ? -66.114 47.915  70.700  1.00 39.32 ? 2599 HOH   A O     1 
HETATM 19696 O  O     . HOH   V 10 .    ? -22.010 64.669  132.251 1.00 41.23 ? 2600 HOH   A O     1 
HETATM 19697 O  O     . HOH   V 10 .    ? -65.389 56.218  69.341  1.00 36.15 ? 2601 HOH   A O     1 
HETATM 19698 O  O     . HOH   V 10 .    ? -31.657 61.572  121.913 1.00 35.50 ? 2602 HOH   A O     1 
HETATM 19699 O  O     . HOH   V 10 .    ? -34.873 63.715  121.597 1.00 38.41 ? 2603 HOH   A O     1 
HETATM 19700 O  O     . HOH   V 10 .    ? -56.568 76.274  80.959  1.00 36.48 ? 2604 HOH   A O     1 
HETATM 19701 O  O     . HOH   V 10 .    ? -25.050 62.629  99.913  1.00 34.38 ? 2605 HOH   A O     1 
HETATM 19702 O  O     . HOH   V 10 .    ? -9.200  42.863  57.947  1.00 35.97 ? 2606 HOH   A O     1 
HETATM 19703 O  O     . HOH   V 10 .    ? -22.647 102.120 90.565  1.00 47.72 ? 2607 HOH   A O     1 
HETATM 19704 O  O     . HOH   V 10 .    ? -55.195 42.237  63.124  1.00 44.90 ? 2608 HOH   A O     1 
HETATM 19705 O  O     . HOH   V 10 .    ? -46.416 38.901  104.509 1.00 34.07 ? 2609 HOH   A O     1 
HETATM 19706 O  O     . HOH   V 10 .    ? -39.226 71.881  95.703  1.00 38.62 ? 2610 HOH   A O     1 
HETATM 19707 O  O     . HOH   V 10 .    ? -39.596 83.324  76.376  1.00 45.52 ? 2611 HOH   A O     1 
HETATM 19708 O  O     . HOH   V 10 .    ? -0.185  56.999  67.827  1.00 37.44 ? 2612 HOH   A O     1 
HETATM 19709 O  O     . HOH   V 10 .    ? -19.235 55.631  123.223 1.00 43.60 ? 2613 HOH   A O     1 
HETATM 19710 O  O     . HOH   V 10 .    ? -33.077 57.212  110.937 1.00 37.84 ? 2614 HOH   A O     1 
HETATM 19711 O  O     . HOH   V 10 .    ? 11.315  64.454  93.234  1.00 35.09 ? 2615 HOH   A O     1 
HETATM 19712 O  O     . HOH   V 10 .    ? -42.314 61.656  52.719  1.00 40.41 ? 2616 HOH   A O     1 
HETATM 19713 O  O     . HOH   V 10 .    ? -35.693 39.322  73.684  1.00 39.83 ? 2617 HOH   A O     1 
HETATM 19714 O  O     . HOH   V 10 .    ? -68.166 63.154  89.550  1.00 43.23 ? 2618 HOH   A O     1 
HETATM 19715 O  O     . HOH   V 10 .    ? 13.872  65.860  90.659  1.00 38.06 ? 2619 HOH   A O     1 
HETATM 19716 O  O     . HOH   V 10 .    ? -33.368 78.242  71.298  1.00 40.82 ? 2620 HOH   A O     1 
HETATM 19717 O  O     . HOH   V 10 .    ? -37.366 34.210  90.015  1.00 42.00 ? 2621 HOH   A O     1 
HETATM 19718 O  O     . HOH   V 10 .    ? 6.652   59.794  94.384  1.00 38.20 ? 2622 HOH   A O     1 
HETATM 19719 O  O     . HOH   V 10 .    ? -68.299 70.076  69.221  1.00 35.52 ? 2623 HOH   A O     1 
HETATM 19720 O  O     . HOH   V 10 .    ? -53.985 79.666  77.002  1.00 41.78 ? 2624 HOH   A O     1 
HETATM 19721 O  O     . HOH   V 10 .    ? -47.846 37.837  103.034 1.00 40.71 ? 2625 HOH   A O     1 
HETATM 19722 O  O     . HOH   V 10 .    ? -65.904 68.894  86.871  1.00 43.16 ? 2626 HOH   A O     1 
HETATM 19723 O  O     . HOH   V 10 .    ? -54.038 71.240  102.426 1.00 39.62 ? 2627 HOH   A O     1 
HETATM 19724 O  O     . HOH   V 10 .    ? 10.990  92.041  117.305 1.00 48.38 ? 2628 HOH   A O     1 
HETATM 19725 O  O     . HOH   V 10 .    ? -36.767 31.854  90.920  1.00 38.90 ? 2629 HOH   A O     1 
HETATM 19726 O  O     . HOH   V 10 .    ? -35.351 56.549  109.664 1.00 37.93 ? 2630 HOH   A O     1 
HETATM 19727 O  O     . HOH   V 10 .    ? -55.967 78.620  77.427  1.00 36.37 ? 2631 HOH   A O     1 
HETATM 19728 O  O     . HOH   V 10 .    ? -33.992 81.288  71.703  1.00 41.83 ? 2632 HOH   A O     1 
HETATM 19729 O  O     . HOH   V 10 .    ? -53.858 47.504  98.454  1.00 36.14 ? 2633 HOH   A O     1 
HETATM 19730 O  O     . HOH   V 10 .    ? 13.632  62.909  90.780  1.00 39.07 ? 2634 HOH   A O     1 
HETATM 19731 O  O     . HOH   W 10 .    ? 30.548  41.833  67.029  1.00 26.97 ? 1401 HOH   B O     1 
HETATM 19732 O  O     . HOH   W 10 .    ? -11.224 27.521  81.262  1.00 27.94 ? 1402 HOH   B O     1 
HETATM 19733 O  O     . HOH   W 10 .    ? 25.995  17.054  96.990  1.00 36.99 ? 1403 HOH   B O     1 
HETATM 19734 O  O     . HOH   W 10 .    ? -0.059  18.358  80.487  1.00 25.53 ? 1404 HOH   B O     1 
HETATM 19735 O  O     . HOH   W 10 .    ? 40.167  41.810  93.446  1.00 48.35 ? 1405 HOH   B O     1 
HETATM 19736 O  O     . HOH   W 10 .    ? -0.378  76.632  74.124  1.00 34.26 ? 1406 HOH   B O     1 
HETATM 19737 O  O     . HOH   W 10 .    ? 23.725  38.869  111.209 1.00 34.18 ? 1407 HOH   B O     1 
HETATM 19738 O  O     . HOH   W 10 .    ? 5.110   31.102  113.364 1.00 45.48 ? 1408 HOH   B O     1 
HETATM 19739 O  O     . HOH   W 10 .    ? -0.057  53.205  132.517 1.00 49.10 ? 1409 HOH   B O     1 
HETATM 19740 O  O     . HOH   W 10 .    ? 12.312  44.993  109.106 1.00 39.52 ? 1410 HOH   B O     1 
HETATM 19741 O  O     . HOH   W 10 .    ? 4.128   72.173  85.563  1.00 35.13 ? 1411 HOH   B O     1 
HETATM 19742 O  O     . HOH   W 10 .    ? -2.494  29.272  57.585  1.00 36.44 ? 1412 HOH   B O     1 
HETATM 19743 O  O     . HOH   W 10 .    ? -22.053 28.750  87.012  1.00 42.87 ? 1413 HOH   B O     1 
HETATM 19744 O  O     . HOH   W 10 .    ? 4.117   55.173  72.609  1.00 26.90 ? 1414 HOH   B O     1 
HETATM 19745 O  O     . HOH   W 10 .    ? 33.613  11.553  87.981  1.00 41.00 ? 1415 HOH   B O     1 
HETATM 19746 O  O     . HOH   W 10 .    ? -23.155 27.716  117.557 1.00 41.36 ? 1416 HOH   B O     1 
HETATM 19747 O  O     . HOH   W 10 .    ? 14.047  57.840  60.572  1.00 42.29 ? 1417 HOH   B O     1 
HETATM 19748 O  O     . HOH   W 10 .    ? 3.596   56.098  62.860  1.00 41.38 ? 1418 HOH   B O     1 
HETATM 19749 O  O     . HOH   W 10 .    ? 30.161  35.190  50.783  1.00 32.31 ? 1419 HOH   B O     1 
HETATM 19750 O  O     . HOH   W 10 .    ? 29.388  42.085  84.254  1.00 28.88 ? 1420 HOH   B O     1 
HETATM 19751 O  O     . HOH   W 10 .    ? -25.779 6.553   111.776 1.00 41.41 ? 1421 HOH   B O     1 
HETATM 19752 O  O     . HOH   W 10 .    ? -4.232  45.245  89.653  1.00 42.13 ? 1422 HOH   B O     1 
HETATM 19753 O  O     . HOH   W 10 .    ? 2.223   17.092  112.530 1.00 34.77 ? 1423 HOH   B O     1 
HETATM 19754 O  O     . HOH   W 10 .    ? -28.997 13.072  98.613  1.00 45.58 ? 1424 HOH   B O     1 
HETATM 19755 O  O     . HOH   W 10 .    ? 32.540  18.931  58.053  1.00 28.35 ? 1425 HOH   B O     1 
HETATM 19756 O  O     . HOH   W 10 .    ? -1.145  22.191  71.284  1.00 32.61 ? 1426 HOH   B O     1 
HETATM 19757 O  O     . HOH   W 10 .    ? -6.744  11.138  127.785 1.00 31.62 ? 1427 HOH   B O     1 
HETATM 19758 O  O     . HOH   W 10 .    ? -0.320  73.181  77.713  1.00 29.69 ? 1428 HOH   B O     1 
HETATM 19759 O  O     . HOH   W 10 .    ? 32.990  29.474  61.813  1.00 26.52 ? 1429 HOH   B O     1 
HETATM 19760 O  O     . HOH   W 10 .    ? 6.320   15.038  124.704 1.00 32.34 ? 1430 HOH   B O     1 
HETATM 19761 O  O     . HOH   W 10 .    ? 13.410  34.508  78.919  1.00 29.94 ? 1431 HOH   B O     1 
HETATM 19762 O  O     . HOH   W 10 .    ? 5.304   51.174  109.892 1.00 38.18 ? 1432 HOH   B O     1 
HETATM 19763 O  O     . HOH   W 10 .    ? 3.339   21.239  102.663 1.00 39.15 ? 1433 HOH   B O     1 
HETATM 19764 O  O     . HOH   W 10 .    ? -31.273 15.763  102.358 1.00 33.95 ? 1434 HOH   B O     1 
HETATM 19765 O  O     . HOH   W 10 .    ? 6.140   31.803  79.155  1.00 22.64 ? 1435 HOH   B O     1 
HETATM 19766 O  O     . HOH   W 10 .    ? -28.719 17.408  84.856  1.00 39.25 ? 1436 HOH   B O     1 
HETATM 19767 O  O     . HOH   W 10 .    ? -18.865 49.902  120.577 1.00 42.64 ? 1437 HOH   B O     1 
HETATM 19768 O  O     . HOH   W 10 .    ? 31.563  37.292  106.700 1.00 39.13 ? 1438 HOH   B O     1 
HETATM 19769 O  O     . HOH   W 10 .    ? 19.703  16.133  111.728 1.00 41.10 ? 1439 HOH   B O     1 
HETATM 19770 O  O     . HOH   W 10 .    ? 16.713  14.232  109.394 1.00 27.85 ? 1440 HOH   B O     1 
HETATM 19771 O  O     . HOH   W 10 .    ? 30.709  25.848  52.877  1.00 38.06 ? 1441 HOH   B O     1 
HETATM 19772 O  O     . HOH   W 10 .    ? 10.030  49.118  55.838  1.00 36.46 ? 1442 HOH   B O     1 
HETATM 19773 O  O     . HOH   W 10 .    ? 3.311   18.185  89.000  1.00 29.89 ? 1443 HOH   B O     1 
HETATM 19774 O  O     . HOH   W 10 .    ? 30.965  14.751  64.782  1.00 40.26 ? 1444 HOH   B O     1 
HETATM 19775 O  O     . HOH   W 10 .    ? 11.153  5.737   121.708 1.00 31.73 ? 1445 HOH   B O     1 
HETATM 19776 O  O     . HOH   W 10 .    ? 22.726  34.725  115.533 1.00 29.10 ? 1446 HOH   B O     1 
HETATM 19777 O  O     . HOH   W 10 .    ? -10.088 -2.739  115.705 1.00 32.09 ? 1447 HOH   B O     1 
HETATM 19778 O  O     . HOH   W 10 .    ? -14.506 -7.723  107.756 1.00 38.57 ? 1448 HOH   B O     1 
HETATM 19779 O  O     . HOH   W 10 .    ? 25.531  8.411   75.541  1.00 38.24 ? 1449 HOH   B O     1 
HETATM 19780 O  O     . HOH   W 10 .    ? -18.266 31.087  93.297  1.00 47.85 ? 1450 HOH   B O     1 
HETATM 19781 O  O     . HOH   W 10 .    ? 9.406   25.758  55.213  1.00 22.50 ? 1451 HOH   B O     1 
HETATM 19782 O  O     . HOH   W 10 .    ? 8.088   7.915   72.696  1.00 36.77 ? 1452 HOH   B O     1 
HETATM 19783 O  O     . HOH   W 10 .    ? 18.681  21.040  55.194  1.00 36.64 ? 1453 HOH   B O     1 
HETATM 19784 O  O     . HOH   W 10 .    ? 6.868   51.168  57.540  1.00 31.71 ? 1454 HOH   B O     1 
HETATM 19785 O  O     . HOH   W 10 .    ? -8.818  24.085  77.238  1.00 34.55 ? 1455 HOH   B O     1 
HETATM 19786 O  O     . HOH   W 10 .    ? 1.026   -10.507 110.772 1.00 28.80 ? 1456 HOH   B O     1 
HETATM 19787 O  O     . HOH   W 10 .    ? -14.374 9.203   118.524 1.00 30.79 ? 1457 HOH   B O     1 
HETATM 19788 O  O     . HOH   W 10 .    ? -5.747  39.485  90.131  1.00 38.41 ? 1458 HOH   B O     1 
HETATM 19789 O  O     . HOH   W 10 .    ? 34.331  62.372  78.291  1.00 18.76 ? 1459 HOH   B O     1 
HETATM 19790 O  O     . HOH   W 10 .    ? -16.995 15.112  79.778  1.00 36.20 ? 1460 HOH   B O     1 
HETATM 19791 O  O     . HOH   W 10 .    ? 3.657   7.699   92.334  1.00 22.87 ? 1461 HOH   B O     1 
HETATM 19792 O  O     . HOH   W 10 .    ? -4.750  6.664   81.784  1.00 42.79 ? 1462 HOH   B O     1 
HETATM 19793 O  O     . HOH   W 10 .    ? 28.982  69.096  79.845  1.00 25.66 ? 1463 HOH   B O     1 
HETATM 19794 O  O     . HOH   W 10 .    ? 18.950  67.064  82.520  1.00 25.98 ? 1464 HOH   B O     1 
HETATM 19795 O  O     . HOH   W 10 .    ? 33.208  17.619  89.820  1.00 38.44 ? 1465 HOH   B O     1 
HETATM 19796 O  O     . HOH   W 10 .    ? -12.526 49.166  130.121 1.00 42.66 ? 1466 HOH   B O     1 
HETATM 19797 O  O     . HOH   W 10 .    ? 1.584   20.278  103.999 1.00 32.24 ? 1467 HOH   B O     1 
HETATM 19798 O  O     . HOH   W 10 .    ? 14.037  41.326  76.935  1.00 18.35 ? 1468 HOH   B O     1 
HETATM 19799 O  O     . HOH   W 10 .    ? 5.614   43.752  58.590  1.00 29.97 ? 1469 HOH   B O     1 
HETATM 19800 O  O     . HOH   W 10 .    ? -4.706  26.841  70.260  1.00 34.04 ? 1470 HOH   B O     1 
HETATM 19801 O  O     . HOH   W 10 .    ? -29.892 11.742  96.189  1.00 38.33 ? 1471 HOH   B O     1 
HETATM 19802 O  O     . HOH   W 10 .    ? 6.048   -5.872  116.694 1.00 39.71 ? 1472 HOH   B O     1 
HETATM 19803 O  O     . HOH   W 10 .    ? -14.558 14.864  78.731  1.00 34.62 ? 1473 HOH   B O     1 
HETATM 19804 O  O     . HOH   W 10 .    ? 11.039  79.687  67.686  1.00 42.52 ? 1474 HOH   B O     1 
HETATM 19805 O  O     . HOH   W 10 .    ? 8.417   -1.280  107.197 1.00 37.58 ? 1475 HOH   B O     1 
HETATM 19806 O  O     . HOH   W 10 .    ? 6.141   19.589  94.368  1.00 39.16 ? 1476 HOH   B O     1 
HETATM 19807 O  O     . HOH   W 10 .    ? 27.369  13.041  66.667  1.00 33.13 ? 1477 HOH   B O     1 
HETATM 19808 O  O     . HOH   W 10 .    ? -2.576  4.766   85.054  1.00 28.68 ? 1478 HOH   B O     1 
HETATM 19809 O  O     . HOH   W 10 .    ? 4.948   32.136  89.270  1.00 32.83 ? 1479 HOH   B O     1 
HETATM 19810 O  O     . HOH   W 10 .    ? 29.799  27.143  56.125  1.00 23.25 ? 1480 HOH   B O     1 
HETATM 19811 O  O     . HOH   W 10 .    ? -10.327 10.710  129.750 1.00 33.33 ? 1481 HOH   B O     1 
HETATM 19812 O  O     . HOH   W 10 .    ? -7.837  24.395  116.652 1.00 40.57 ? 1482 HOH   B O     1 
HETATM 19813 O  O     . HOH   W 10 .    ? 10.953  19.026  61.431  1.00 27.76 ? 1483 HOH   B O     1 
HETATM 19814 O  O     . HOH   W 10 .    ? 18.464  38.237  115.680 1.00 31.98 ? 1484 HOH   B O     1 
HETATM 19815 O  O     . HOH   W 10 .    ? -5.562  -1.789  123.516 1.00 36.29 ? 1485 HOH   B O     1 
HETATM 19816 O  O     . HOH   W 10 .    ? 11.079  46.300  106.602 1.00 31.02 ? 1486 HOH   B O     1 
HETATM 19817 O  O     . HOH   W 10 .    ? 22.312  45.379  90.592  1.00 18.28 ? 1487 HOH   B O     1 
HETATM 19818 O  O     . HOH   W 10 .    ? 38.849  25.615  80.645  1.00 37.71 ? 1488 HOH   B O     1 
HETATM 19819 O  O     . HOH   W 10 .    ? -8.747  45.112  108.963 1.00 34.40 ? 1489 HOH   B O     1 
HETATM 19820 O  O     . HOH   W 10 .    ? 9.021   3.775   80.905  1.00 26.74 ? 1490 HOH   B O     1 
HETATM 19821 O  O     . HOH   W 10 .    ? 20.822  51.041  112.621 1.00 49.30 ? 1491 HOH   B O     1 
HETATM 19822 O  O     . HOH   W 10 .    ? 15.057  40.216  72.926  1.00 19.16 ? 1492 HOH   B O     1 
HETATM 19823 O  O     . HOH   W 10 .    ? 21.462  50.290  87.709  1.00 22.71 ? 1493 HOH   B O     1 
HETATM 19824 O  O     . HOH   W 10 .    ? -4.241  64.087  80.993  1.00 19.42 ? 1494 HOH   B O     1 
HETATM 19825 O  O     . HOH   W 10 .    ? 4.014   -8.874  104.220 1.00 32.31 ? 1495 HOH   B O     1 
HETATM 19826 O  O     . HOH   W 10 .    ? 31.720  38.245  84.146  1.00 30.46 ? 1496 HOH   B O     1 
HETATM 19827 O  O     . HOH   W 10 .    ? 18.811  24.689  54.424  1.00 24.16 ? 1497 HOH   B O     1 
HETATM 19828 O  O     . HOH   W 10 .    ? 14.983  20.697  92.677  1.00 31.10 ? 1498 HOH   B O     1 
HETATM 19829 O  O     . HOH   W 10 .    ? -17.586 0.035   99.600  1.00 31.82 ? 1499 HOH   B O     1 
HETATM 19830 O  O     . HOH   W 10 .    ? 18.873  31.206  73.243  1.00 20.86 ? 1500 HOH   B O     1 
HETATM 19831 O  O     . HOH   W 10 .    ? 18.806  34.409  46.115  1.00 39.01 ? 1501 HOH   B O     1 
HETATM 19832 O  O     . HOH   W 10 .    ? 6.608   5.603   92.340  1.00 21.89 ? 1502 HOH   B O     1 
HETATM 19833 O  O     . HOH   W 10 .    ? 21.845  79.596  70.147  1.00 39.53 ? 1503 HOH   B O     1 
HETATM 19834 O  O     . HOH   W 10 .    ? -7.078  8.267   111.107 1.00 22.59 ? 1504 HOH   B O     1 
HETATM 19835 O  O     . HOH   W 10 .    ? -22.566 19.055  102.195 1.00 31.23 ? 1505 HOH   B O     1 
HETATM 19836 O  O     . HOH   W 10 .    ? 24.159  18.879  98.017  1.00 33.51 ? 1506 HOH   B O     1 
HETATM 19837 O  O     . HOH   W 10 .    ? 23.519  64.898  82.234  1.00 38.29 ? 1507 HOH   B O     1 
HETATM 19838 O  O     . HOH   W 10 .    ? 20.990  5.291   68.217  1.00 38.44 ? 1508 HOH   B O     1 
HETATM 19839 O  O     . HOH   W 10 .    ? -4.100  46.061  133.088 1.00 46.25 ? 1509 HOH   B O     1 
HETATM 19840 O  O     . HOH   W 10 .    ? -2.278  48.695  63.647  1.00 18.68 ? 1510 HOH   B O     1 
HETATM 19841 O  O     . HOH   W 10 .    ? -14.133 53.982  118.075 1.00 29.35 ? 1511 HOH   B O     1 
HETATM 19842 O  O     . HOH   W 10 .    ? -25.482 6.930   98.514  1.00 36.55 ? 1512 HOH   B O     1 
HETATM 19843 O  O     . HOH   W 10 .    ? -6.332  50.913  73.077  1.00 16.36 ? 1513 HOH   B O     1 
HETATM 19844 O  O     . HOH   W 10 .    ? 39.271  26.613  87.536  1.00 35.99 ? 1514 HOH   B O     1 
HETATM 19845 O  O     . HOH   W 10 .    ? -10.675 46.419  74.504  1.00 21.41 ? 1515 HOH   B O     1 
HETATM 19846 O  O     . HOH   W 10 .    ? 15.123  21.320  88.595  1.00 36.45 ? 1516 HOH   B O     1 
HETATM 19847 O  O     . HOH   W 10 .    ? 10.001  50.371  90.149  1.00 29.03 ? 1517 HOH   B O     1 
HETATM 19848 O  O     . HOH   W 10 .    ? 28.749  46.349  92.380  1.00 38.09 ? 1518 HOH   B O     1 
HETATM 19849 O  O     . HOH   W 10 .    ? -0.438  26.865  68.595  1.00 17.71 ? 1519 HOH   B O     1 
HETATM 19850 O  O     . HOH   W 10 .    ? 17.772  12.570  117.249 1.00 28.14 ? 1520 HOH   B O     1 
HETATM 19851 O  O     . HOH   W 10 .    ? -6.441  12.069  125.367 1.00 27.42 ? 1521 HOH   B O     1 
HETATM 19852 O  O     . HOH   W 10 .    ? 23.438  18.179  80.356  1.00 26.80 ? 1522 HOH   B O     1 
HETATM 19853 O  O     . HOH   W 10 .    ? 15.057  55.703  74.838  1.00 27.90 ? 1523 HOH   B O     1 
HETATM 19854 O  O     . HOH   W 10 .    ? 7.840   40.842  122.533 1.00 40.48 ? 1524 HOH   B O     1 
HETATM 19855 O  O     . HOH   W 10 .    ? -13.872 -0.514  96.768  1.00 34.63 ? 1525 HOH   B O     1 
HETATM 19856 O  O     . HOH   W 10 .    ? 1.110   38.634  108.285 1.00 27.75 ? 1526 HOH   B O     1 
HETATM 19857 O  O     . HOH   W 10 .    ? 11.022  38.135  95.799  1.00 28.06 ? 1527 HOH   B O     1 
HETATM 19858 O  O     . HOH   W 10 .    ? -11.573 -4.783  97.740  1.00 39.13 ? 1528 HOH   B O     1 
HETATM 19859 O  O     . HOH   W 10 .    ? -5.771  37.201  77.766  1.00 28.79 ? 1529 HOH   B O     1 
HETATM 19860 O  O     . HOH   W 10 .    ? -13.590 17.893  105.700 1.00 23.81 ? 1530 HOH   B O     1 
HETATM 19861 O  O     . HOH   W 10 .    ? 14.243  25.451  110.681 1.00 38.93 ? 1531 HOH   B O     1 
HETATM 19862 O  O     . HOH   W 10 .    ? 25.942  54.986  77.475  1.00 24.16 ? 1532 HOH   B O     1 
HETATM 19863 O  O     . HOH   W 10 .    ? 28.325  18.613  57.999  1.00 32.22 ? 1533 HOH   B O     1 
HETATM 19864 O  O     . HOH   W 10 .    ? 25.285  10.217  70.344  1.00 44.61 ? 1534 HOH   B O     1 
HETATM 19865 O  O     . HOH   W 10 .    ? 13.511  10.201  91.385  1.00 24.65 ? 1535 HOH   B O     1 
HETATM 19866 O  O     . HOH   W 10 .    ? -1.339  14.437  85.938  1.00 24.17 ? 1536 HOH   B O     1 
HETATM 19867 O  O     . HOH   W 10 .    ? 21.528  39.900  47.776  1.00 45.65 ? 1537 HOH   B O     1 
HETATM 19868 O  O     . HOH   W 10 .    ? 15.484  53.459  81.722  1.00 24.02 ? 1538 HOH   B O     1 
HETATM 19869 O  O     . HOH   W 10 .    ? 9.174   22.990  109.099 1.00 37.32 ? 1539 HOH   B O     1 
HETATM 19870 O  O     . HOH   W 10 .    ? -2.393  45.202  102.601 1.00 33.93 ? 1540 HOH   B O     1 
HETATM 19871 O  O     . HOH   W 10 .    ? 18.775  12.886  95.467  1.00 27.96 ? 1541 HOH   B O     1 
HETATM 19872 O  O     . HOH   W 10 .    ? 10.153  50.596  64.652  1.00 25.89 ? 1542 HOH   B O     1 
HETATM 19873 O  O     . HOH   W 10 .    ? 17.472  27.283  82.927  1.00 27.41 ? 1543 HOH   B O     1 
HETATM 19874 O  O     . HOH   W 10 .    ? 11.690  38.562  112.475 1.00 41.24 ? 1544 HOH   B O     1 
HETATM 19875 O  O     . HOH   W 10 .    ? -4.638  -2.253  96.997  1.00 23.00 ? 1545 HOH   B O     1 
HETATM 19876 O  O     . HOH   W 10 .    ? 2.578   43.877  70.416  1.00 17.18 ? 1546 HOH   B O     1 
HETATM 19877 O  O     . HOH   W 10 .    ? -2.364  41.741  61.682  1.00 24.40 ? 1547 HOH   B O     1 
HETATM 19878 O  O     . HOH   W 10 .    ? -33.849 10.398  95.545  1.00 44.12 ? 1548 HOH   B O     1 
HETATM 19879 O  O     . HOH   W 10 .    ? -6.151  40.122  62.946  1.00 32.06 ? 1549 HOH   B O     1 
HETATM 19880 O  O     . HOH   W 10 .    ? -4.595  59.700  125.503 1.00 32.67 ? 1550 HOH   B O     1 
HETATM 19881 O  O     . HOH   W 10 .    ? 37.077  28.046  93.114  1.00 32.31 ? 1551 HOH   B O     1 
HETATM 19882 O  O     . HOH   W 10 .    ? -4.731  43.924  81.133  1.00 32.41 ? 1552 HOH   B O     1 
HETATM 19883 O  O     . HOH   W 10 .    ? -21.119 15.505  82.719  1.00 27.96 ? 1553 HOH   B O     1 
HETATM 19884 O  O     . HOH   W 10 .    ? 15.038  38.739  77.087  1.00 17.61 ? 1554 HOH   B O     1 
HETATM 19885 O  O     . HOH   W 10 .    ? -4.694  50.384  78.469  1.00 28.45 ? 1555 HOH   B O     1 
HETATM 19886 O  O     . HOH   W 10 .    ? -5.607  5.043   122.161 1.00 23.62 ? 1556 HOH   B O     1 
HETATM 19887 O  O     . HOH   W 10 .    ? 4.206   18.954  97.446  1.00 33.22 ? 1557 HOH   B O     1 
HETATM 19888 O  O     . HOH   W 10 .    ? -6.580  52.349  107.221 1.00 30.91 ? 1558 HOH   B O     1 
HETATM 19889 O  O     . HOH   W 10 .    ? 38.325  33.694  102.702 1.00 31.74 ? 1559 HOH   B O     1 
HETATM 19890 O  O     . HOH   W 10 .    ? 1.576   13.407  104.796 1.00 20.18 ? 1560 HOH   B O     1 
HETATM 19891 O  O     . HOH   W 10 .    ? 19.720  50.882  77.513  1.00 20.55 ? 1561 HOH   B O     1 
HETATM 19892 O  O     . HOH   W 10 .    ? -6.830  35.363  69.183  1.00 34.61 ? 1562 HOH   B O     1 
HETATM 19893 O  O     . HOH   W 10 .    ? 15.772  55.362  92.857  1.00 31.01 ? 1563 HOH   B O     1 
HETATM 19894 O  O     . HOH   W 10 .    ? 7.405   32.709  98.353  1.00 29.11 ? 1564 HOH   B O     1 
HETATM 19895 O  O     . HOH   W 10 .    ? -5.315  39.730  72.226  1.00 28.89 ? 1565 HOH   B O     1 
HETATM 19896 O  O     . HOH   W 10 .    ? 22.979  54.234  53.785  1.00 36.01 ? 1566 HOH   B O     1 
HETATM 19897 O  O     . HOH   W 10 .    ? 15.957  52.746  57.890  1.00 32.11 ? 1567 HOH   B O     1 
HETATM 19898 O  O     . HOH   W 10 .    ? -7.990  19.981  79.633  1.00 33.39 ? 1568 HOH   B O     1 
HETATM 19899 O  O     . HOH   W 10 .    ? 30.477  51.668  74.456  1.00 35.26 ? 1569 HOH   B O     1 
HETATM 19900 O  O     . HOH   W 10 .    ? 28.273  13.232  85.889  1.00 28.95 ? 1570 HOH   B O     1 
HETATM 19901 O  O     . HOH   W 10 .    ? 18.733  50.124  70.085  1.00 25.53 ? 1571 HOH   B O     1 
HETATM 19902 O  O     . HOH   W 10 .    ? -10.365 25.294  102.893 1.00 33.47 ? 1572 HOH   B O     1 
HETATM 19903 O  O     . HOH   W 10 .    ? -4.660  1.974   124.016 1.00 25.87 ? 1573 HOH   B O     1 
HETATM 19904 O  O     . HOH   W 10 .    ? -20.148 25.309  102.847 1.00 40.55 ? 1574 HOH   B O     1 
HETATM 19905 O  O     . HOH   W 10 .    ? 19.701  19.369  105.646 1.00 18.95 ? 1575 HOH   B O     1 
HETATM 19906 O  O     . HOH   W 10 .    ? 31.273  28.634  77.541  1.00 28.44 ? 1576 HOH   B O     1 
HETATM 19907 O  O     . HOH   W 10 .    ? 29.260  68.065  72.280  1.00 37.01 ? 1577 HOH   B O     1 
HETATM 19908 O  O     . HOH   W 10 .    ? 13.687  3.577   84.414  1.00 40.81 ? 1578 HOH   B O     1 
HETATM 19909 O  O     . HOH   W 10 .    ? 2.566   21.741  130.241 1.00 31.32 ? 1579 HOH   B O     1 
HETATM 19910 O  O     . HOH   W 10 .    ? -9.767  -4.938  107.188 1.00 27.43 ? 1580 HOH   B O     1 
HETATM 19911 O  O     . HOH   W 10 .    ? 29.397  32.025  76.481  1.00 22.62 ? 1581 HOH   B O     1 
HETATM 19912 O  O     . HOH   W 10 .    ? 2.577   39.353  98.685  1.00 22.11 ? 1582 HOH   B O     1 
HETATM 19913 O  O     . HOH   W 10 .    ? 1.590   12.981  101.929 1.00 21.18 ? 1583 HOH   B O     1 
HETATM 19914 O  O     . HOH   W 10 .    ? 33.808  67.750  80.471  1.00 22.65 ? 1584 HOH   B O     1 
HETATM 19915 O  O     . HOH   W 10 .    ? -5.681  39.151  106.773 1.00 31.95 ? 1585 HOH   B O     1 
HETATM 19916 O  O     . HOH   W 10 .    ? 6.973   42.454  49.626  1.00 26.15 ? 1586 HOH   B O     1 
HETATM 19917 O  O     . HOH   W 10 .    ? -4.188  18.604  98.143  1.00 17.72 ? 1587 HOH   B O     1 
HETATM 19918 O  O     . HOH   W 10 .    ? 6.161   51.484  93.792  1.00 39.73 ? 1588 HOH   B O     1 
HETATM 19919 O  O     . HOH   W 10 .    ? 21.915  53.138  67.168  1.00 25.05 ? 1589 HOH   B O     1 
HETATM 19920 O  O     . HOH   W 10 .    ? -12.966 8.697   124.413 1.00 31.87 ? 1590 HOH   B O     1 
HETATM 19921 O  O     . HOH   W 10 .    ? -26.879 14.825  100.701 1.00 35.39 ? 1591 HOH   B O     1 
HETATM 19922 O  O     . HOH   W 10 .    ? -4.210  -0.563  110.623 1.00 23.94 ? 1592 HOH   B O     1 
HETATM 19923 O  O     . HOH   W 10 .    ? 26.537  20.346  55.776  1.00 32.71 ? 1593 HOH   B O     1 
HETATM 19924 O  O     . HOH   W 10 .    ? 16.194  10.245  112.316 1.00 45.91 ? 1594 HOH   B O     1 
HETATM 19925 O  O     . HOH   W 10 .    ? 3.450   33.616  86.646  1.00 21.22 ? 1595 HOH   B O     1 
HETATM 19926 O  O     . HOH   W 10 .    ? 2.594   30.528  80.131  1.00 19.73 ? 1596 HOH   B O     1 
HETATM 19927 O  O     . HOH   W 10 .    ? 4.820   30.517  54.764  1.00 34.62 ? 1597 HOH   B O     1 
HETATM 19928 O  O     . HOH   W 10 .    ? 18.946  62.092  57.459  1.00 34.20 ? 1598 HOH   B O     1 
HETATM 19929 O  O     . HOH   W 10 .    ? 5.904   25.548  86.246  1.00 32.78 ? 1599 HOH   B O     1 
HETATM 19930 O  O     . HOH   W 10 .    ? -5.178  51.510  75.525  1.00 21.69 ? 1600 HOH   B O     1 
HETATM 19931 O  O     . HOH   W 10 .    ? 6.240   49.751  88.269  1.00 33.74 ? 1601 HOH   B O     1 
HETATM 19932 O  O     . HOH   W 10 .    ? -2.945  30.813  63.691  1.00 28.70 ? 1602 HOH   B O     1 
HETATM 19933 O  O     . HOH   W 10 .    ? 31.717  59.930  65.477  1.00 26.46 ? 1603 HOH   B O     1 
HETATM 19934 O  O     . HOH   W 10 .    ? 10.510  70.236  86.480  1.00 41.38 ? 1604 HOH   B O     1 
HETATM 19935 O  O     . HOH   W 10 .    ? 18.227  52.486  66.660  1.00 23.85 ? 1605 HOH   B O     1 
HETATM 19936 O  O     . HOH   W 10 .    ? -5.992  -4.189  120.547 1.00 42.64 ? 1606 HOH   B O     1 
HETATM 19937 O  O     . HOH   W 10 .    ? 25.824  8.524   78.939  1.00 36.57 ? 1607 HOH   B O     1 
HETATM 19938 O  O     . HOH   W 10 .    ? 32.511  26.609  68.583  1.00 38.43 ? 1608 HOH   B O     1 
HETATM 19939 O  O     . HOH   W 10 .    ? -4.940  30.638  77.417  1.00 18.99 ? 1609 HOH   B O     1 
HETATM 19940 O  O     . HOH   W 10 .    ? 32.701  47.352  92.170  1.00 36.82 ? 1610 HOH   B O     1 
HETATM 19941 O  O     . HOH   W 10 .    ? 6.191   5.597   86.062  1.00 20.73 ? 1611 HOH   B O     1 
HETATM 19942 O  O     . HOH   W 10 .    ? 1.427   38.522  105.510 1.00 36.57 ? 1612 HOH   B O     1 
HETATM 19943 O  O     . HOH   W 10 .    ? 4.305   42.012  84.339  1.00 23.65 ? 1613 HOH   B O     1 
HETATM 19944 O  O     . HOH   W 10 .    ? -2.262  39.368  87.217  1.00 19.24 ? 1614 HOH   B O     1 
HETATM 19945 O  O     . HOH   W 10 .    ? 33.564  12.014  74.783  1.00 33.40 ? 1615 HOH   B O     1 
HETATM 19946 O  O     . HOH   W 10 .    ? -1.451  -6.336  117.293 1.00 37.54 ? 1616 HOH   B O     1 
HETATM 19947 O  O     . HOH   W 10 .    ? 32.432  32.873  70.746  1.00 26.49 ? 1617 HOH   B O     1 
HETATM 19948 O  O     . HOH   W 10 .    ? -12.638 19.824  83.979  1.00 23.34 ? 1618 HOH   B O     1 
HETATM 19949 O  O     . HOH   W 10 .    ? 8.327   24.691  105.709 1.00 41.16 ? 1619 HOH   B O     1 
HETATM 19950 O  O     . HOH   W 10 .    ? -36.373 24.466  116.052 1.00 33.75 ? 1620 HOH   B O     1 
HETATM 19951 O  O     . HOH   W 10 .    ? 10.021  71.006  61.749  1.00 31.22 ? 1621 HOH   B O     1 
HETATM 19952 O  O     . HOH   W 10 .    ? 19.529  5.264   76.865  1.00 31.94 ? 1622 HOH   B O     1 
HETATM 19953 O  O     . HOH   W 10 .    ? -28.769 7.971   116.974 1.00 39.63 ? 1623 HOH   B O     1 
HETATM 19954 O  O     . HOH   W 10 .    ? 30.198  49.787  71.471  1.00 28.42 ? 1624 HOH   B O     1 
HETATM 19955 O  O     . HOH   W 10 .    ? 35.442  38.606  90.511  1.00 37.01 ? 1625 HOH   B O     1 
HETATM 19956 O  O     . HOH   W 10 .    ? 18.491  7.234   100.669 1.00 35.47 ? 1626 HOH   B O     1 
HETATM 19957 O  O     . HOH   W 10 .    ? 9.912   30.649  109.919 1.00 41.29 ? 1627 HOH   B O     1 
HETATM 19958 O  O     . HOH   W 10 .    ? 8.049   56.540  87.396  1.00 33.85 ? 1628 HOH   B O     1 
HETATM 19959 O  O     . HOH   W 10 .    ? -8.901  23.797  100.850 1.00 18.65 ? 1629 HOH   B O     1 
HETATM 19960 O  O     . HOH   W 10 .    ? -19.744 27.781  91.337  1.00 38.27 ? 1630 HOH   B O     1 
HETATM 19961 O  O     . HOH   W 10 .    ? 23.384  55.855  99.098  1.00 31.45 ? 1631 HOH   B O     1 
HETATM 19962 O  O     . HOH   W 10 .    ? -32.182 17.173  91.521  1.00 39.60 ? 1632 HOH   B O     1 
HETATM 19963 O  O     . HOH   W 10 .    ? 23.507  2.438   81.946  1.00 43.14 ? 1633 HOH   B O     1 
HETATM 19964 O  O     . HOH   W 10 .    ? -1.335  38.172  80.188  1.00 23.98 ? 1634 HOH   B O     1 
HETATM 19965 O  O     . HOH   W 10 .    ? -7.725  -0.982  119.876 1.00 26.40 ? 1635 HOH   B O     1 
HETATM 19966 O  O     . HOH   W 10 .    ? 27.989  67.420  68.267  1.00 27.34 ? 1636 HOH   B O     1 
HETATM 19967 O  O     . HOH   W 10 .    ? 7.810   65.245  63.855  1.00 29.52 ? 1637 HOH   B O     1 
HETATM 19968 O  O     . HOH   W 10 .    ? -11.002 20.025  122.803 1.00 29.83 ? 1638 HOH   B O     1 
HETATM 19969 O  O     . HOH   W 10 .    ? -10.954 27.162  110.803 1.00 38.82 ? 1639 HOH   B O     1 
HETATM 19970 O  O     . HOH   W 10 .    ? -29.171 22.703  90.019  1.00 38.16 ? 1640 HOH   B O     1 
HETATM 19971 O  O     . HOH   W 10 .    ? 7.581   49.001  106.627 1.00 22.84 ? 1641 HOH   B O     1 
HETATM 19972 O  O     . HOH   W 10 .    ? 12.234  21.211  101.401 1.00 26.00 ? 1642 HOH   B O     1 
HETATM 19973 O  O     . HOH   W 10 .    ? 20.863  37.330  112.523 1.00 22.44 ? 1643 HOH   B O     1 
HETATM 19974 O  O     . HOH   W 10 .    ? 3.822   13.904  72.812  1.00 35.25 ? 1644 HOH   B O     1 
HETATM 19975 O  O     . HOH   W 10 .    ? 18.892  5.749   74.281  1.00 27.77 ? 1645 HOH   B O     1 
HETATM 19976 O  O     . HOH   W 10 .    ? -5.529  55.001  78.715  1.00 25.67 ? 1646 HOH   B O     1 
HETATM 19977 O  O     . HOH   W 10 .    ? 11.199  49.101  76.599  1.00 31.93 ? 1647 HOH   B O     1 
HETATM 19978 O  O     . HOH   W 10 .    ? -1.433  32.502  69.155  1.00 16.52 ? 1648 HOH   B O     1 
HETATM 19979 O  O     . HOH   W 10 .    ? 22.925  48.359  78.045  1.00 21.41 ? 1649 HOH   B O     1 
HETATM 19980 O  O     . HOH   W 10 .    ? 17.178  40.839  71.518  1.00 18.97 ? 1650 HOH   B O     1 
HETATM 19981 O  O     . HOH   W 10 .    ? -5.115  42.521  72.689  1.00 34.26 ? 1651 HOH   B O     1 
HETATM 19982 O  O     . HOH   W 10 .    ? 2.669   11.549  94.474  1.00 19.54 ? 1652 HOH   B O     1 
HETATM 19983 O  O     . HOH   W 10 .    ? -11.843 18.122  126.605 1.00 27.08 ? 1653 HOH   B O     1 
HETATM 19984 O  O     . HOH   W 10 .    ? -9.402  9.876   123.006 1.00 24.77 ? 1654 HOH   B O     1 
HETATM 19985 O  O     . HOH   W 10 .    ? -5.613  -6.670  112.059 1.00 30.12 ? 1655 HOH   B O     1 
HETATM 19986 O  O     . HOH   W 10 .    ? 11.924  10.875  71.602  1.00 23.76 ? 1656 HOH   B O     1 
HETATM 19987 O  O     . HOH   W 10 .    ? 2.240   29.931  54.787  1.00 36.40 ? 1657 HOH   B O     1 
HETATM 19988 O  O     . HOH   W 10 .    ? 22.894  67.167  64.664  1.00 24.86 ? 1658 HOH   B O     1 
HETATM 19989 O  O     . HOH   W 10 .    ? -10.061 39.620  127.211 1.00 37.52 ? 1659 HOH   B O     1 
HETATM 19990 O  O     . HOH   W 10 .    ? 1.519   6.059   91.818  1.00 20.71 ? 1660 HOH   B O     1 
HETATM 19991 O  O     . HOH   W 10 .    ? -3.473  10.562  84.479  1.00 22.53 ? 1661 HOH   B O     1 
HETATM 19992 O  O     . HOH   W 10 .    ? 4.233   21.105  119.140 1.00 35.51 ? 1662 HOH   B O     1 
HETATM 19993 O  O     . HOH   W 10 .    ? -9.519  19.065  81.000  1.00 37.04 ? 1663 HOH   B O     1 
HETATM 19994 O  O     . HOH   W 10 .    ? 19.919  24.132  46.238  1.00 23.55 ? 1664 HOH   B O     1 
HETATM 19995 O  O     . HOH   W 10 .    ? 26.128  47.212  100.095 1.00 30.34 ? 1665 HOH   B O     1 
HETATM 19996 O  O     . HOH   W 10 .    ? -7.265  15.420  81.781  1.00 34.09 ? 1666 HOH   B O     1 
HETATM 19997 O  O     . HOH   W 10 .    ? 0.921   42.103  76.170  1.00 26.04 ? 1667 HOH   B O     1 
HETATM 19998 O  O     . HOH   W 10 .    ? -14.760 6.013   117.546 1.00 25.66 ? 1668 HOH   B O     1 
HETATM 19999 O  O     . HOH   W 10 .    ? 17.305  54.861  97.259  1.00 27.90 ? 1669 HOH   B O     1 
HETATM 20000 O  O     . HOH   W 10 .    ? 17.084  42.705  79.345  1.00 16.44 ? 1670 HOH   B O     1 
HETATM 20001 O  O     . HOH   W 10 .    ? 15.969  22.531  112.732 1.00 38.73 ? 1671 HOH   B O     1 
HETATM 20002 O  O     . HOH   W 10 .    ? 27.285  37.859  89.876  1.00 20.39 ? 1672 HOH   B O     1 
HETATM 20003 O  O     . HOH   W 10 .    ? -0.214  -7.458  106.949 1.00 24.61 ? 1673 HOH   B O     1 
HETATM 20004 O  O     . HOH   W 10 .    ? 5.064   65.111  68.693  1.00 36.62 ? 1674 HOH   B O     1 
HETATM 20005 O  O     . HOH   W 10 .    ? 15.310  16.714  87.903  1.00 21.49 ? 1675 HOH   B O     1 
HETATM 20006 O  O     . HOH   W 10 .    ? 6.615   16.312  121.375 1.00 33.84 ? 1676 HOH   B O     1 
HETATM 20007 O  O     . HOH   W 10 .    ? 28.972  22.671  76.521  1.00 21.53 ? 1677 HOH   B O     1 
HETATM 20008 O  O     . HOH   W 10 .    ? 18.719  44.932  53.792  1.00 28.15 ? 1678 HOH   B O     1 
HETATM 20009 O  O     . HOH   W 10 .    ? 11.985  49.492  88.518  1.00 19.82 ? 1679 HOH   B O     1 
HETATM 20010 O  O     . HOH   W 10 .    ? 23.479  52.441  70.590  1.00 30.39 ? 1680 HOH   B O     1 
HETATM 20011 O  O     . HOH   W 10 .    ? 21.503  30.008  71.461  1.00 14.99 ? 1681 HOH   B O     1 
HETATM 20012 O  O     . HOH   W 10 .    ? -10.345 31.704  80.333  1.00 30.55 ? 1682 HOH   B O     1 
HETATM 20013 O  O     . HOH   W 10 .    ? 12.853  49.879  65.007  1.00 24.25 ? 1683 HOH   B O     1 
HETATM 20014 O  O     . HOH   W 10 .    ? -11.398 20.298  88.194  1.00 23.59 ? 1684 HOH   B O     1 
HETATM 20015 O  O     . HOH   W 10 .    ? 13.678  58.100  64.650  1.00 26.88 ? 1685 HOH   B O     1 
HETATM 20016 O  O     . HOH   W 10 .    ? 5.115   35.802  49.028  1.00 33.62 ? 1686 HOH   B O     1 
HETATM 20017 O  O     . HOH   W 10 .    ? 29.950  23.539  103.296 1.00 44.40 ? 1687 HOH   B O     1 
HETATM 20018 O  O     . HOH   W 10 .    ? -30.451 16.664  123.967 1.00 39.68 ? 1688 HOH   B O     1 
HETATM 20019 O  O     . HOH   W 10 .    ? 31.762  59.125  72.196  1.00 25.51 ? 1689 HOH   B O     1 
HETATM 20020 O  O     . HOH   W 10 .    ? 27.664  31.661  73.944  1.00 20.53 ? 1690 HOH   B O     1 
HETATM 20021 O  O     . HOH   W 10 .    ? 34.443  54.718  75.677  1.00 35.32 ? 1691 HOH   B O     1 
HETATM 20022 O  O     . HOH   W 10 .    ? -15.207 47.088  113.948 1.00 30.61 ? 1692 HOH   B O     1 
HETATM 20023 O  O     . HOH   W 10 .    ? 39.649  29.501  87.702  1.00 25.19 ? 1693 HOH   B O     1 
HETATM 20024 O  O     . HOH   W 10 .    ? 11.743  -2.231  109.856 1.00 44.78 ? 1694 HOH   B O     1 
HETATM 20025 O  O     . HOH   W 10 .    ? 19.259  79.078  68.516  1.00 30.88 ? 1695 HOH   B O     1 
HETATM 20026 O  O     . HOH   W 10 .    ? 11.910  37.872  47.410  1.00 32.53 ? 1696 HOH   B O     1 
HETATM 20027 O  O     . HOH   W 10 .    ? 25.524  54.662  62.123  1.00 22.42 ? 1697 HOH   B O     1 
HETATM 20028 O  O     . HOH   W 10 .    ? -24.244 23.640  104.207 1.00 39.70 ? 1698 HOH   B O     1 
HETATM 20029 O  O     . HOH   W 10 .    ? 16.035  42.935  50.480  1.00 31.69 ? 1699 HOH   B O     1 
HETATM 20030 O  O     . HOH   W 10 .    ? 12.235  53.360  90.752  1.00 37.37 ? 1700 HOH   B O     1 
HETATM 20031 O  O     . HOH   W 10 .    ? -7.957  26.942  99.945  1.00 30.82 ? 1701 HOH   B O     1 
HETATM 20032 O  O     . HOH   W 10 .    ? 31.147  21.198  79.867  1.00 19.20 ? 1702 HOH   B O     1 
HETATM 20033 O  O     . HOH   W 10 .    ? 32.261  8.616   74.834  1.00 40.45 ? 1703 HOH   B O     1 
HETATM 20034 O  O     . HOH   W 10 .    ? 10.421  24.487  103.501 1.00 31.93 ? 1704 HOH   B O     1 
HETATM 20035 O  O     . HOH   W 10 .    ? -2.427  24.047  76.482  1.00 26.12 ? 1705 HOH   B O     1 
HETATM 20036 O  O     . HOH   W 10 .    ? 0.956   28.686  83.038  1.00 16.67 ? 1706 HOH   B O     1 
HETATM 20037 O  O     . HOH   W 10 .    ? 1.012   55.465  110.452 1.00 28.53 ? 1707 HOH   B O     1 
HETATM 20038 O  O     . HOH   W 10 .    ? -25.056 10.319  87.637  1.00 31.89 ? 1708 HOH   B O     1 
HETATM 20039 O  O     . HOH   W 10 .    ? 1.280   14.889  116.129 1.00 26.15 ? 1709 HOH   B O     1 
HETATM 20040 O  O     . HOH   W 10 .    ? 23.397  51.841  62.500  1.00 21.38 ? 1710 HOH   B O     1 
HETATM 20041 O  O     . HOH   W 10 .    ? 17.851  68.356  84.639  1.00 36.19 ? 1711 HOH   B O     1 
HETATM 20042 O  O     . HOH   W 10 .    ? 18.281  43.575  91.480  1.00 14.80 ? 1712 HOH   B O     1 
HETATM 20043 O  O     . HOH   W 10 .    ? 2.697   53.333  69.503  1.00 31.13 ? 1713 HOH   B O     1 
HETATM 20044 O  O     . HOH   W 10 .    ? -2.450  42.747  58.236  1.00 30.68 ? 1714 HOH   B O     1 
HETATM 20045 O  O     . HOH   W 10 .    ? 33.810  47.455  97.647  1.00 42.55 ? 1715 HOH   B O     1 
HETATM 20046 O  O     . HOH   W 10 .    ? 13.073  51.142  86.395  1.00 31.62 ? 1716 HOH   B O     1 
HETATM 20047 O  O     . HOH   W 10 .    ? -0.600  23.863  74.257  1.00 21.26 ? 1717 HOH   B O     1 
HETATM 20048 O  O     . HOH   W 10 .    ? -4.672  7.704   131.528 1.00 40.23 ? 1718 HOH   B O     1 
HETATM 20049 O  O     . HOH   W 10 .    ? -17.942 25.690  83.010  1.00 37.32 ? 1719 HOH   B O     1 
HETATM 20050 O  O     . HOH   W 10 .    ? -0.144  40.021  77.753  1.00 23.69 ? 1720 HOH   B O     1 
HETATM 20051 O  O     . HOH   W 10 .    ? 9.194   61.777  85.144  1.00 26.74 ? 1721 HOH   B O     1 
HETATM 20052 O  O     . HOH   W 10 .    ? -22.348 20.268  88.246  1.00 32.50 ? 1722 HOH   B O     1 
HETATM 20053 O  O     . HOH   W 10 .    ? 29.971  20.055  76.844  1.00 28.34 ? 1723 HOH   B O     1 
HETATM 20054 O  O     . HOH   W 10 .    ? 7.603   44.871  75.079  1.00 15.89 ? 1724 HOH   B O     1 
HETATM 20055 O  O     . HOH   W 10 .    ? 33.241  57.792  74.192  1.00 30.28 ? 1725 HOH   B O     1 
HETATM 20056 O  O     . HOH   W 10 .    ? 15.644  6.708   108.210 1.00 34.28 ? 1726 HOH   B O     1 
HETATM 20057 O  O     . HOH   W 10 .    ? 20.704  55.369  85.392  1.00 37.69 ? 1727 HOH   B O     1 
HETATM 20058 O  O     . HOH   W 10 .    ? -2.950  -2.475  94.719  1.00 23.68 ? 1728 HOH   B O     1 
HETATM 20059 O  O     . HOH   W 10 .    ? -4.782  36.878  89.886  1.00 30.74 ? 1729 HOH   B O     1 
HETATM 20060 O  O     . HOH   W 10 .    ? -17.828 54.317  121.147 1.00 42.41 ? 1730 HOH   B O     1 
HETATM 20061 O  O     . HOH   W 10 .    ? 37.373  31.016  81.543  1.00 30.39 ? 1731 HOH   B O     1 
HETATM 20062 O  O     . HOH   W 10 .    ? -0.940  -9.126  102.128 1.00 26.65 ? 1732 HOH   B O     1 
HETATM 20063 O  O     . HOH   W 10 .    ? -0.124  4.151   88.506  1.00 22.00 ? 1733 HOH   B O     1 
HETATM 20064 O  O     . HOH   W 10 .    ? 22.580  54.085  93.114  1.00 27.67 ? 1734 HOH   B O     1 
HETATM 20065 O  O     . HOH   W 10 .    ? -1.282  15.222  131.155 1.00 36.36 ? 1735 HOH   B O     1 
HETATM 20066 O  O     . HOH   W 10 .    ? 3.556   -3.825  92.876  1.00 36.39 ? 1736 HOH   B O     1 
HETATM 20067 O  O     . HOH   W 10 .    ? 1.130   9.256   89.694  1.00 23.32 ? 1737 HOH   B O     1 
HETATM 20068 O  O     . HOH   W 10 .    ? -2.588  21.327  91.649  1.00 18.20 ? 1738 HOH   B O     1 
HETATM 20069 O  O     . HOH   W 10 .    ? 29.716  58.049  82.166  1.00 40.11 ? 1739 HOH   B O     1 
HETATM 20070 O  O     . HOH   W 10 .    ? 4.765   49.147  68.650  1.00 23.49 ? 1740 HOH   B O     1 
HETATM 20071 O  O     . HOH   W 10 .    ? -0.834  -3.037  86.300  1.00 40.43 ? 1741 HOH   B O     1 
HETATM 20072 O  O     . HOH   W 10 .    ? 11.670  37.228  72.284  1.00 15.08 ? 1742 HOH   B O     1 
HETATM 20073 O  O     . HOH   W 10 .    ? 27.099  32.578  104.865 1.00 38.97 ? 1743 HOH   B O     1 
HETATM 20074 O  O     . HOH   W 10 .    ? 20.064  43.342  87.781  1.00 14.92 ? 1744 HOH   B O     1 
HETATM 20075 O  O     . HOH   W 10 .    ? -9.742  5.957   87.100  1.00 25.06 ? 1745 HOH   B O     1 
HETATM 20076 O  O     . HOH   W 10 .    ? -16.930 16.064  131.309 1.00 41.29 ? 1746 HOH   B O     1 
HETATM 20077 O  O     . HOH   W 10 .    ? 12.394  1.854   111.356 1.00 28.53 ? 1747 HOH   B O     1 
HETATM 20078 O  O     . HOH   W 10 .    ? 17.322  48.858  58.990  1.00 21.12 ? 1748 HOH   B O     1 
HETATM 20079 O  O     . HOH   W 10 .    ? 28.559  37.049  82.818  1.00 32.46 ? 1749 HOH   B O     1 
HETATM 20080 O  O     . HOH   W 10 .    ? 11.539  24.853  108.324 1.00 31.90 ? 1750 HOH   B O     1 
HETATM 20081 O  O     . HOH   W 10 .    ? 4.994   62.754  84.186  1.00 23.39 ? 1751 HOH   B O     1 
HETATM 20082 O  O     . HOH   W 10 .    ? 3.961   29.458  84.701  1.00 26.27 ? 1752 HOH   B O     1 
HETATM 20083 O  O     . HOH   W 10 .    ? 8.520   35.718  102.751 1.00 27.32 ? 1753 HOH   B O     1 
HETATM 20084 O  O     . HOH   W 10 .    ? -6.686  34.720  129.117 1.00 41.76 ? 1754 HOH   B O     1 
HETATM 20085 O  O     . HOH   W 10 .    ? 15.552  26.532  81.053  1.00 31.30 ? 1755 HOH   B O     1 
HETATM 20086 O  O     . HOH   W 10 .    ? 1.263   80.649  75.632  1.00 41.10 ? 1756 HOH   B O     1 
HETATM 20087 O  O     . HOH   W 10 .    ? 31.738  53.711  67.978  1.00 27.59 ? 1757 HOH   B O     1 
HETATM 20088 O  O     . HOH   W 10 .    ? 25.114  29.909  108.534 1.00 37.47 ? 1758 HOH   B O     1 
HETATM 20089 O  O     . HOH   W 10 .    ? 1.756   20.516  89.663  1.00 23.34 ? 1759 HOH   B O     1 
HETATM 20090 O  O     . HOH   W 10 .    ? -23.241 3.136   101.503 1.00 36.36 ? 1760 HOH   B O     1 
HETATM 20091 O  O     . HOH   W 10 .    ? -25.105 4.041   111.810 1.00 37.50 ? 1761 HOH   B O     1 
HETATM 20092 O  O     . HOH   W 10 .    ? -0.150  55.854  86.404  1.00 32.49 ? 1762 HOH   B O     1 
HETATM 20093 O  O     . HOH   W 10 .    ? 20.642  27.462  71.285  1.00 16.61 ? 1763 HOH   B O     1 
HETATM 20094 O  O     . HOH   W 10 .    ? 1.677   9.808   79.113  1.00 27.73 ? 1764 HOH   B O     1 
HETATM 20095 O  O     . HOH   W 10 .    ? -2.767  54.702  83.732  1.00 31.44 ? 1765 HOH   B O     1 
HETATM 20096 O  O     . HOH   W 10 .    ? 8.565   23.036  84.686  1.00 30.01 ? 1766 HOH   B O     1 
HETATM 20097 O  O     . HOH   W 10 .    ? -6.420  0.112   86.219  1.00 28.22 ? 1767 HOH   B O     1 
HETATM 20098 O  O     . HOH   W 10 .    ? 14.259  33.486  83.968  1.00 23.63 ? 1768 HOH   B O     1 
HETATM 20099 O  O     . HOH   W 10 .    ? -6.699  14.143  91.496  1.00 18.57 ? 1769 HOH   B O     1 
HETATM 20100 O  O     . HOH   W 10 .    ? 7.862   74.280  62.068  1.00 40.10 ? 1770 HOH   B O     1 
HETATM 20101 O  O     . HOH   W 10 .    ? 17.951  23.636  110.480 1.00 27.02 ? 1771 HOH   B O     1 
HETATM 20102 O  O     . HOH   W 10 .    ? -19.196 -3.202  110.180 1.00 45.87 ? 1772 HOH   B O     1 
HETATM 20103 O  O     . HOH   W 10 .    ? 24.215  68.669  67.365  1.00 23.34 ? 1773 HOH   B O     1 
HETATM 20104 O  O     . HOH   W 10 .    ? 15.534  9.888   89.496  1.00 20.54 ? 1774 HOH   B O     1 
HETATM 20105 O  O     . HOH   W 10 .    ? 30.601  40.108  57.311  1.00 26.19 ? 1775 HOH   B O     1 
HETATM 20106 O  O     . HOH   W 10 .    ? -3.313  66.090  77.229  1.00 30.19 ? 1776 HOH   B O     1 
HETATM 20107 O  O     . HOH   W 10 .    ? 1.062   10.381  129.522 1.00 28.29 ? 1777 HOH   B O     1 
HETATM 20108 O  O     . HOH   W 10 .    ? 37.484  23.664  84.705  1.00 40.55 ? 1778 HOH   B O     1 
HETATM 20109 O  O     . HOH   W 10 .    ? 18.704  9.087   92.330  1.00 36.59 ? 1779 HOH   B O     1 
HETATM 20110 O  O     . HOH   W 10 .    ? -11.026 1.575   121.601 1.00 24.29 ? 1780 HOH   B O     1 
HETATM 20111 O  O     . HOH   W 10 .    ? -1.951  11.047  101.390 1.00 17.22 ? 1781 HOH   B O     1 
HETATM 20112 O  O     . HOH   W 10 .    ? 26.944  48.741  94.544  1.00 29.69 ? 1782 HOH   B O     1 
HETATM 20113 O  O     . HOH   W 10 .    ? 15.602  38.121  74.556  1.00 16.49 ? 1783 HOH   B O     1 
HETATM 20114 O  O     . HOH   W 10 .    ? 2.383   61.896  68.842  1.00 35.24 ? 1784 HOH   B O     1 
HETATM 20115 O  O     . HOH   W 10 .    ? 24.830  15.984  95.155  1.00 25.95 ? 1785 HOH   B O     1 
HETATM 20116 O  O     . HOH   W 10 .    ? 0.912   30.709  74.823  1.00 17.92 ? 1786 HOH   B O     1 
HETATM 20117 O  O     . HOH   W 10 .    ? -11.603 -4.938  109.394 1.00 30.84 ? 1787 HOH   B O     1 
HETATM 20118 O  O     . HOH   W 10 .    ? 17.029  1.104   82.562  1.00 46.38 ? 1788 HOH   B O     1 
HETATM 20119 O  O     . HOH   W 10 .    ? 23.180  72.628  65.105  1.00 32.57 ? 1789 HOH   B O     1 
HETATM 20120 O  O     . HOH   W 10 .    ? 23.240  48.327  106.873 1.00 32.01 ? 1790 HOH   B O     1 
HETATM 20121 O  O     . HOH   W 10 .    ? 10.756  9.094   69.907  1.00 31.38 ? 1791 HOH   B O     1 
HETATM 20122 O  O     . HOH   W 10 .    ? 1.200   -0.941  92.816  1.00 27.09 ? 1792 HOH   B O     1 
HETATM 20123 O  O     . HOH   W 10 .    ? -6.243  12.573  99.260  1.00 16.48 ? 1793 HOH   B O     1 
HETATM 20124 O  O     . HOH   W 10 .    ? 27.199  62.345  84.941  1.00 40.97 ? 1794 HOH   B O     1 
HETATM 20125 O  O     . HOH   W 10 .    ? 15.288  3.733   98.393  1.00 30.81 ? 1795 HOH   B O     1 
HETATM 20126 O  O     . HOH   W 10 .    ? -2.034  2.516   125.826 1.00 24.34 ? 1796 HOH   B O     1 
HETATM 20127 O  O     . HOH   W 10 .    ? 33.804  37.540  62.068  1.00 25.84 ? 1797 HOH   B O     1 
HETATM 20128 O  O     . HOH   W 10 .    ? 15.193  48.740  57.245  1.00 26.95 ? 1798 HOH   B O     1 
HETATM 20129 O  O     . HOH   W 10 .    ? 2.666   5.835   80.308  1.00 27.95 ? 1799 HOH   B O     1 
HETATM 20130 O  O     . HOH   W 10 .    ? 14.592  22.342  101.781 1.00 23.10 ? 1800 HOH   B O     1 
HETATM 20131 O  O     . HOH   W 10 .    ? -4.660  10.661  100.414 1.00 18.71 ? 1801 HOH   B O     1 
HETATM 20132 O  O     . HOH   W 10 .    ? 11.230  41.237  54.455  1.00 19.18 ? 1802 HOH   B O     1 
HETATM 20133 O  O     . HOH   W 10 .    ? -31.399 6.158   107.615 1.00 43.31 ? 1803 HOH   B O     1 
HETATM 20134 O  O     . HOH   W 10 .    ? -2.619  62.749  85.511  1.00 27.30 ? 1804 HOH   B O     1 
HETATM 20135 O  O     . HOH   W 10 .    ? -7.829  29.797  76.002  1.00 24.98 ? 1805 HOH   B O     1 
HETATM 20136 O  O     . HOH   W 10 .    ? 27.078  52.517  75.413  1.00 29.76 ? 1806 HOH   B O     1 
HETATM 20137 O  O     . HOH   W 10 .    ? 18.504  13.346  74.443  1.00 26.68 ? 1807 HOH   B O     1 
HETATM 20138 O  O     . HOH   W 10 .    ? 12.005  0.479   94.132  1.00 43.42 ? 1808 HOH   B O     1 
HETATM 20139 O  O     . HOH   W 10 .    ? -4.703  37.238  98.592  1.00 38.69 ? 1809 HOH   B O     1 
HETATM 20140 O  O     . HOH   W 10 .    ? 5.467   69.421  63.231  1.00 37.02 ? 1810 HOH   B O     1 
HETATM 20141 O  O     . HOH   W 10 .    ? 0.060   12.168  93.781  1.00 18.05 ? 1811 HOH   B O     1 
HETATM 20142 O  O     . HOH   W 10 .    ? 11.467  34.320  51.850  1.00 30.87 ? 1812 HOH   B O     1 
HETATM 20143 O  O     . HOH   W 10 .    ? 26.677  21.853  75.302  1.00 22.78 ? 1813 HOH   B O     1 
HETATM 20144 O  O     . HOH   W 10 .    ? -18.417 7.949   122.168 1.00 35.14 ? 1814 HOH   B O     1 
HETATM 20145 O  O     . HOH   W 10 .    ? 8.068   13.729  71.568  1.00 23.10 ? 1815 HOH   B O     1 
HETATM 20146 O  O     . HOH   W 10 .    ? -16.812 4.646   116.490 1.00 26.13 ? 1816 HOH   B O     1 
HETATM 20147 O  O     . HOH   W 10 .    ? -9.483  10.003  82.740  1.00 37.85 ? 1817 HOH   B O     1 
HETATM 20148 O  O     . HOH   W 10 .    ? -8.313  -9.101  105.851 1.00 24.55 ? 1818 HOH   B O     1 
HETATM 20149 O  O     . HOH   W 10 .    ? 3.600   33.482  92.955  1.00 20.87 ? 1819 HOH   B O     1 
HETATM 20150 O  O     . HOH   W 10 .    ? 0.305   20.092  69.982  1.00 25.68 ? 1820 HOH   B O     1 
HETATM 20151 O  O     . HOH   W 10 .    ? 16.033  48.389  70.767  1.00 15.96 ? 1821 HOH   B O     1 
HETATM 20152 O  O     . HOH   W 10 .    ? 6.550   33.530  86.810  1.00 20.45 ? 1822 HOH   B O     1 
HETATM 20153 O  O     . HOH   W 10 .    ? 14.881  6.792   68.950  1.00 29.73 ? 1823 HOH   B O     1 
HETATM 20154 O  O     . HOH   W 10 .    ? 28.028  29.453  83.103  1.00 17.53 ? 1824 HOH   B O     1 
HETATM 20155 O  O     . HOH   W 10 .    ? 10.793  14.823  124.817 1.00 38.19 ? 1825 HOH   B O     1 
HETATM 20156 O  O     . HOH   W 10 .    ? -13.649 11.666  91.228  1.00 19.94 ? 1826 HOH   B O     1 
HETATM 20157 O  O     . HOH   W 10 .    ? 6.335   -4.370  104.555 1.00 29.19 ? 1827 HOH   B O     1 
HETATM 20158 O  O     . HOH   W 10 .    ? 5.682   55.678  104.723 1.00 25.56 ? 1828 HOH   B O     1 
HETATM 20159 O  O     . HOH   W 10 .    ? -12.044 3.827   129.802 1.00 44.75 ? 1829 HOH   B O     1 
HETATM 20160 O  O     . HOH   W 10 .    ? 4.640   77.516  80.218  1.00 29.77 ? 1830 HOH   B O     1 
HETATM 20161 O  O     . HOH   W 10 .    ? -1.120  66.653  83.902  1.00 29.61 ? 1831 HOH   B O     1 
HETATM 20162 O  O     . HOH   W 10 .    ? 35.078  64.596  81.317  1.00 20.44 ? 1832 HOH   B O     1 
HETATM 20163 O  O     . HOH   W 10 .    ? 19.248  70.430  59.110  1.00 35.04 ? 1833 HOH   B O     1 
HETATM 20164 O  O     . HOH   W 10 .    ? -29.814 18.151  103.616 1.00 30.56 ? 1834 HOH   B O     1 
HETATM 20165 O  O     . HOH   W 10 .    ? 9.441   -6.099  109.085 1.00 37.85 ? 1835 HOH   B O     1 
HETATM 20166 O  O     . HOH   W 10 .    ? 12.296  70.001  61.087  1.00 38.12 ? 1836 HOH   B O     1 
HETATM 20167 O  O     . HOH   W 10 .    ? 13.206  55.658  65.647  1.00 28.17 ? 1837 HOH   B O     1 
HETATM 20168 O  O     . HOH   W 10 .    ? 31.014  37.555  77.468  1.00 35.89 ? 1838 HOH   B O     1 
HETATM 20169 O  O     . HOH   W 10 .    ? 8.359   27.042  119.355 1.00 44.24 ? 1839 HOH   B O     1 
HETATM 20170 O  O     . HOH   W 10 .    ? -3.265  67.557  70.667  1.00 39.51 ? 1840 HOH   B O     1 
HETATM 20171 O  O     . HOH   W 10 .    ? 9.784   43.550  110.218 1.00 27.98 ? 1841 HOH   B O     1 
HETATM 20172 O  O     . HOH   W 10 .    ? 32.977  45.663  67.215  1.00 30.98 ? 1842 HOH   B O     1 
HETATM 20173 O  O     . HOH   W 10 .    ? -1.096  60.364  77.482  1.00 23.75 ? 1843 HOH   B O     1 
HETATM 20174 O  O     . HOH   W 10 .    ? -31.921 14.648  114.091 1.00 39.49 ? 1844 HOH   B O     1 
HETATM 20175 O  O     . HOH   W 10 .    ? 8.460   40.562  86.798  1.00 17.01 ? 1845 HOH   B O     1 
HETATM 20176 O  O     . HOH   W 10 .    ? 5.535   7.073   94.284  1.00 23.25 ? 1846 HOH   B O     1 
HETATM 20177 O  O     . HOH   W 10 .    ? 12.583  37.182  107.818 1.00 24.77 ? 1847 HOH   B O     1 
HETATM 20178 O  O     . HOH   W 10 .    ? 22.211  24.379  108.482 1.00 26.44 ? 1848 HOH   B O     1 
HETATM 20179 O  O     . HOH   W 10 .    ? 2.217   41.443  54.098  1.00 26.97 ? 1849 HOH   B O     1 
HETATM 20180 O  O     . HOH   W 10 .    ? 18.652  14.611  105.186 1.00 37.22 ? 1850 HOH   B O     1 
HETATM 20181 O  O     . HOH   W 10 .    ? 2.825   69.887  64.201  1.00 35.34 ? 1851 HOH   B O     1 
HETATM 20182 O  O     . HOH   W 10 .    ? 3.018   23.020  58.780  1.00 31.86 ? 1852 HOH   B O     1 
HETATM 20183 O  O     . HOH   W 10 .    ? -1.668  25.374  80.041  1.00 23.14 ? 1853 HOH   B O     1 
HETATM 20184 O  O     . HOH   W 10 .    ? 17.002  52.779  64.151  1.00 27.10 ? 1854 HOH   B O     1 
HETATM 20185 O  O     . HOH   W 10 .    ? 19.746  32.852  67.401  1.00 15.31 ? 1855 HOH   B O     1 
HETATM 20186 O  O     . HOH   W 10 .    ? -13.622 12.397  93.913  1.00 19.33 ? 1856 HOH   B O     1 
HETATM 20187 O  O     . HOH   W 10 .    ? 29.892  32.921  73.552  1.00 23.34 ? 1857 HOH   B O     1 
HETATM 20188 O  O     . HOH   W 10 .    ? 22.778  23.475  84.744  1.00 19.90 ? 1858 HOH   B O     1 
HETATM 20189 O  O     . HOH   W 10 .    ? 22.742  37.132  86.022  1.00 17.84 ? 1859 HOH   B O     1 
HETATM 20190 O  O     . HOH   W 10 .    ? 2.692   32.808  78.460  1.00 16.48 ? 1860 HOH   B O     1 
HETATM 20191 O  O     . HOH   W 10 .    ? 2.109   40.309  114.419 1.00 28.74 ? 1861 HOH   B O     1 
HETATM 20192 O  O     . HOH   W 10 .    ? -16.258 4.289   92.915  1.00 36.61 ? 1862 HOH   B O     1 
HETATM 20193 O  O     . HOH   W 10 .    ? 22.260  11.892  71.477  1.00 24.37 ? 1863 HOH   B O     1 
HETATM 20194 O  O     . HOH   W 10 .    ? 29.672  60.155  59.022  1.00 28.37 ? 1864 HOH   B O     1 
HETATM 20195 O  O     . HOH   W 10 .    ? 2.477   63.124  78.393  1.00 18.71 ? 1865 HOH   B O     1 
HETATM 20196 O  O     . HOH   W 10 .    ? -7.731  35.731  80.697  1.00 37.11 ? 1866 HOH   B O     1 
HETATM 20197 O  O     . HOH   W 10 .    ? -0.741  55.760  121.718 1.00 35.21 ? 1867 HOH   B O     1 
HETATM 20198 O  O     . HOH   W 10 .    ? 9.867   2.304   117.434 1.00 28.52 ? 1868 HOH   B O     1 
HETATM 20199 O  O     . HOH   W 10 .    ? 31.783  29.899  74.415  1.00 39.25 ? 1869 HOH   B O     1 
HETATM 20200 O  O     . HOH   W 10 .    ? 9.383   18.753  103.731 1.00 25.08 ? 1870 HOH   B O     1 
HETATM 20201 O  O     . HOH   W 10 .    ? 20.233  54.010  81.236  1.00 22.52 ? 1871 HOH   B O     1 
HETATM 20202 O  O     . HOH   W 10 .    ? 11.922  11.740  121.408 1.00 27.63 ? 1872 HOH   B O     1 
HETATM 20203 O  O     . HOH   W 10 .    ? -18.976 23.769  115.137 1.00 27.46 ? 1873 HOH   B O     1 
HETATM 20204 O  O     . HOH   W 10 .    ? 22.764  11.762  87.552  1.00 28.28 ? 1874 HOH   B O     1 
HETATM 20205 O  O     . HOH   W 10 .    ? -11.842 27.261  102.072 1.00 39.58 ? 1875 HOH   B O     1 
HETATM 20206 O  O     . HOH   W 10 .    ? 32.909  44.982  75.092  1.00 27.78 ? 1876 HOH   B O     1 
HETATM 20207 O  O     . HOH   W 10 .    ? -36.812 7.915   96.836  1.00 45.12 ? 1877 HOH   B O     1 
HETATM 20208 O  O     . HOH   W 10 .    ? 19.620  19.010  66.334  1.00 16.01 ? 1878 HOH   B O     1 
HETATM 20209 O  O     . HOH   W 10 .    ? -1.688  49.131  101.333 1.00 31.78 ? 1879 HOH   B O     1 
HETATM 20210 O  O     . HOH   W 10 .    ? 0.358   11.148  81.041  1.00 32.48 ? 1880 HOH   B O     1 
HETATM 20211 O  O     . HOH   W 10 .    ? -5.199  9.602   115.026 1.00 26.60 ? 1881 HOH   B O     1 
HETATM 20212 O  O     . HOH   W 10 .    ? 10.905  52.760  104.705 1.00 32.47 ? 1882 HOH   B O     1 
HETATM 20213 O  O     . HOH   W 10 .    ? 25.608  53.594  73.814  1.00 23.29 ? 1883 HOH   B O     1 
HETATM 20214 O  O     . HOH   W 10 .    ? 19.596  54.644  93.492  1.00 27.73 ? 1884 HOH   B O     1 
HETATM 20215 O  O     . HOH   W 10 .    ? 5.800   15.072  94.755  1.00 18.81 ? 1885 HOH   B O     1 
HETATM 20216 O  O     . HOH   W 10 .    ? 33.255  26.232  59.137  1.00 23.14 ? 1886 HOH   B O     1 
HETATM 20217 O  O     . HOH   W 10 .    ? 7.450   20.440  102.234 1.00 30.18 ? 1887 HOH   B O     1 
HETATM 20218 O  O     . HOH   W 10 .    ? 32.889  28.304  53.045  1.00 34.38 ? 1888 HOH   B O     1 
HETATM 20219 O  O     . HOH   W 10 .    ? 23.564  32.840  91.545  1.00 19.19 ? 1889 HOH   B O     1 
HETATM 20220 O  O     . HOH   W 10 .    ? 4.942   60.214  67.830  1.00 35.69 ? 1890 HOH   B O     1 
HETATM 20221 O  O     . HOH   W 10 .    ? 3.836   10.358  92.344  1.00 19.05 ? 1891 HOH   B O     1 
HETATM 20222 O  O     . HOH   W 10 .    ? -32.596 16.152  98.519  1.00 36.87 ? 1892 HOH   B O     1 
HETATM 20223 O  O     . HOH   W 10 .    ? -1.482  31.311  125.503 1.00 38.60 ? 1893 HOH   B O     1 
HETATM 20224 O  O     . HOH   W 10 .    ? 12.424  5.909   84.524  1.00 24.12 ? 1894 HOH   B O     1 
HETATM 20225 O  O     . HOH   W 10 .    ? 14.141  72.032  60.969  1.00 28.11 ? 1895 HOH   B O     1 
HETATM 20226 O  O     . HOH   W 10 .    ? 0.227   47.662  76.476  1.00 20.21 ? 1896 HOH   B O     1 
HETATM 20227 O  O     . HOH   W 10 .    ? 3.079   35.360  121.254 1.00 33.14 ? 1897 HOH   B O     1 
HETATM 20228 O  O     . HOH   W 10 .    ? -1.211  50.801  64.931  1.00 18.98 ? 1898 HOH   B O     1 
HETATM 20229 O  O     . HOH   W 10 .    ? -5.567  12.437  84.508  1.00 27.94 ? 1899 HOH   B O     1 
HETATM 20230 O  O     . HOH   W 10 .    ? 26.888  41.654  49.644  1.00 45.77 ? 1900 HOH   B O     1 
HETATM 20231 O  O     . HOH   W 10 .    ? 0.137   27.885  122.262 1.00 36.53 ? 1901 HOH   B O     1 
HETATM 20232 O  O     . HOH   W 10 .    ? 20.393  52.288  69.346  1.00 20.38 ? 1902 HOH   B O     1 
HETATM 20233 O  O     . HOH   W 10 .    ? 6.728   81.803  75.394  1.00 34.63 ? 1903 HOH   B O     1 
HETATM 20234 O  O     . HOH   W 10 .    ? 12.508  2.173   92.195  1.00 36.38 ? 1904 HOH   B O     1 
HETATM 20235 O  O     . HOH   W 10 .    ? 11.895  20.717  58.951  1.00 19.10 ? 1905 HOH   B O     1 
HETATM 20236 O  O     . HOH   W 10 .    ? 25.236  13.647  65.168  1.00 30.43 ? 1906 HOH   B O     1 
HETATM 20237 O  O     . HOH   W 10 .    ? 2.735   45.629  53.826  1.00 35.14 ? 1907 HOH   B O     1 
HETATM 20238 O  O     . HOH   W 10 .    ? 9.407   36.660  110.041 1.00 38.07 ? 1908 HOH   B O     1 
HETATM 20239 O  O     . HOH   W 10 .    ? 18.278  23.254  85.187  1.00 19.55 ? 1909 HOH   B O     1 
HETATM 20240 O  O     . HOH   W 10 .    ? 23.787  25.968  50.628  1.00 27.39 ? 1910 HOH   B O     1 
HETATM 20241 O  O     . HOH   W 10 .    ? 10.726  29.222  94.297  1.00 26.23 ? 1911 HOH   B O     1 
HETATM 20242 O  O     . HOH   W 10 .    ? 19.536  78.037  76.987  1.00 41.24 ? 1912 HOH   B O     1 
HETATM 20243 O  O     . HOH   W 10 .    ? 14.537  45.520  78.349  1.00 19.15 ? 1913 HOH   B O     1 
HETATM 20244 O  O     . HOH   W 10 .    ? 14.072  81.023  69.675  1.00 41.06 ? 1914 HOH   B O     1 
HETATM 20245 O  O     . HOH   W 10 .    ? 1.582   49.270  89.381  1.00 36.25 ? 1915 HOH   B O     1 
HETATM 20246 O  O     . HOH   W 10 .    ? 15.925  15.898  85.330  1.00 21.18 ? 1916 HOH   B O     1 
HETATM 20247 O  O     . HOH   W 10 .    ? 17.314  28.455  110.885 1.00 26.93 ? 1917 HOH   B O     1 
HETATM 20248 O  O     . HOH   W 10 .    ? 5.951   48.085  110.633 1.00 33.14 ? 1918 HOH   B O     1 
HETATM 20249 O  O     . HOH   W 10 .    ? 23.583  51.613  83.811  1.00 26.99 ? 1919 HOH   B O     1 
HETATM 20250 O  O     . HOH   W 10 .    ? 11.638  26.261  52.066  1.00 29.85 ? 1920 HOH   B O     1 
HETATM 20251 O  O     . HOH   W 10 .    ? 36.864  21.512  83.882  1.00 34.92 ? 1921 HOH   B O     1 
HETATM 20252 O  O     . HOH   W 10 .    ? 4.676   18.702  124.150 1.00 27.52 ? 1922 HOH   B O     1 
HETATM 20253 O  O     . HOH   W 10 .    ? 3.926   17.435  75.448  1.00 29.44 ? 1923 HOH   B O     1 
HETATM 20254 O  O     . HOH   W 10 .    ? 26.257  39.653  52.820  1.00 25.46 ? 1924 HOH   B O     1 
HETATM 20255 O  O     . HOH   W 10 .    ? 11.621  26.070  101.812 1.00 27.05 ? 1925 HOH   B O     1 
HETATM 20256 O  O     . HOH   W 10 .    ? -5.912  -7.702  115.562 1.00 33.62 ? 1926 HOH   B O     1 
HETATM 20257 O  O     . HOH   W 10 .    ? 15.318  53.885  66.545  1.00 26.71 ? 1927 HOH   B O     1 
HETATM 20258 O  O     . HOH   W 10 .    ? 3.462   40.910  117.246 1.00 29.43 ? 1928 HOH   B O     1 
HETATM 20259 O  O     . HOH   W 10 .    ? 16.986  33.722  48.605  1.00 30.76 ? 1929 HOH   B O     1 
HETATM 20260 O  O     . HOH   W 10 .    ? 26.486  65.252  54.486  1.00 37.20 ? 1930 HOH   B O     1 
HETATM 20261 O  O     . HOH   W 10 .    ? -30.841 20.956  83.858  1.00 43.81 ? 1931 HOH   B O     1 
HETATM 20262 O  O     . HOH   W 10 .    ? 3.800   19.147  60.382  1.00 34.14 ? 1932 HOH   B O     1 
HETATM 20263 O  O     . HOH   W 10 .    ? -8.029  12.252  97.109  1.00 19.93 ? 1933 HOH   B O     1 
HETATM 20264 O  O     . HOH   W 10 .    ? 6.734   7.886   75.008  1.00 26.65 ? 1934 HOH   B O     1 
HETATM 20265 O  O     . HOH   W 10 .    ? -6.616  6.198   118.619 1.00 22.56 ? 1935 HOH   B O     1 
HETATM 20266 O  O     . HOH   W 10 .    ? 5.186   3.286   93.143  1.00 22.86 ? 1936 HOH   B O     1 
HETATM 20267 O  O     . HOH   W 10 .    ? 13.216  25.784  96.031  1.00 29.97 ? 1937 HOH   B O     1 
HETATM 20268 O  O     . HOH   W 10 .    ? 25.558  53.248  96.346  1.00 40.84 ? 1938 HOH   B O     1 
HETATM 20269 O  O     . HOH   W 10 .    ? -4.235  53.760  130.718 1.00 35.09 ? 1939 HOH   B O     1 
HETATM 20270 O  O     . HOH   W 10 .    ? -3.306  -11.403 100.821 1.00 25.39 ? 1940 HOH   B O     1 
HETATM 20271 O  O     . HOH   W 10 .    ? -0.971  55.350  72.345  1.00 31.12 ? 1941 HOH   B O     1 
HETATM 20272 O  O     . HOH   W 10 .    ? -14.600 6.994   120.222 1.00 28.60 ? 1942 HOH   B O     1 
HETATM 20273 O  O     . HOH   W 10 .    ? 30.218  46.226  57.937  1.00 37.49 ? 1943 HOH   B O     1 
HETATM 20274 O  O     . HOH   W 10 .    ? 20.247  50.517  67.126  1.00 26.41 ? 1944 HOH   B O     1 
HETATM 20275 O  O     . HOH   W 10 .    ? 10.893  20.086  120.608 1.00 40.08 ? 1945 HOH   B O     1 
HETATM 20276 O  O     . HOH   W 10 .    ? 25.590  69.092  81.797  1.00 37.95 ? 1946 HOH   B O     1 
HETATM 20277 O  O     . HOH   W 10 .    ? 8.478   14.826  90.468  1.00 25.42 ? 1947 HOH   B O     1 
HETATM 20278 O  O     . HOH   W 10 .    ? 22.820  61.548  83.052  1.00 35.32 ? 1948 HOH   B O     1 
HETATM 20279 O  O     . HOH   W 10 .    ? 15.448  61.828  84.586  1.00 35.78 ? 1949 HOH   B O     1 
HETATM 20280 O  O     . HOH   W 10 .    ? -10.629 1.525   91.380  1.00 25.85 ? 1950 HOH   B O     1 
HETATM 20281 O  O     . HOH   W 10 .    ? 27.799  10.614  84.798  1.00 29.11 ? 1951 HOH   B O     1 
HETATM 20282 O  O     . HOH   W 10 .    ? -10.083 32.278  89.132  1.00 22.61 ? 1952 HOH   B O     1 
HETATM 20283 O  O     . HOH   W 10 .    ? 1.641   46.297  98.991  1.00 27.71 ? 1953 HOH   B O     1 
HETATM 20284 O  O     . HOH   W 10 .    ? -28.878 17.172  117.501 1.00 34.46 ? 1954 HOH   B O     1 
HETATM 20285 O  O     . HOH   W 10 .    ? 27.265  22.844  88.631  1.00 17.18 ? 1955 HOH   B O     1 
HETATM 20286 O  O     . HOH   W 10 .    ? 20.687  75.165  62.974  1.00 38.84 ? 1956 HOH   B O     1 
HETATM 20287 O  O     . HOH   W 10 .    ? 19.035  8.119   84.017  1.00 26.34 ? 1957 HOH   B O     1 
HETATM 20288 O  O     . HOH   W 10 .    ? 17.976  53.719  82.922  1.00 25.36 ? 1958 HOH   B O     1 
HETATM 20289 O  O     . HOH   W 10 .    ? 1.499   15.086  82.376  1.00 20.75 ? 1959 HOH   B O     1 
HETATM 20290 O  O     . HOH   W 10 .    ? -8.162  2.311   92.382  1.00 21.46 ? 1960 HOH   B O     1 
HETATM 20291 O  O     . HOH   W 10 .    ? 29.413  32.289  103.257 1.00 27.64 ? 1961 HOH   B O     1 
HETATM 20292 O  O     . HOH   W 10 .    ? 4.510   35.373  118.046 1.00 46.76 ? 1962 HOH   B O     1 
HETATM 20293 O  O     . HOH   W 10 .    ? 27.170  59.011  78.549  1.00 21.43 ? 1963 HOH   B O     1 
HETATM 20294 O  O     . HOH   W 10 .    ? 9.174   31.957  83.788  1.00 30.66 ? 1964 HOH   B O     1 
HETATM 20295 O  O     . HOH   W 10 .    ? 25.593  33.197  109.847 1.00 37.31 ? 1965 HOH   B O     1 
HETATM 20296 O  O     . HOH   W 10 .    ? 19.430  15.900  63.615  1.00 21.26 ? 1966 HOH   B O     1 
HETATM 20297 O  O     . HOH   W 10 .    ? 4.822   21.831  83.836  1.00 22.79 ? 1967 HOH   B O     1 
HETATM 20298 O  O     . HOH   W 10 .    ? -0.014  19.328  94.068  1.00 22.82 ? 1968 HOH   B O     1 
HETATM 20299 O  O     . HOH   W 10 .    ? 10.995  16.058  121.875 1.00 33.45 ? 1969 HOH   B O     1 
HETATM 20300 O  O     . HOH   W 10 .    ? 31.483  52.266  65.655  1.00 29.71 ? 1970 HOH   B O     1 
HETATM 20301 O  O     . HOH   W 10 .    ? -13.889 -8.318  103.374 1.00 35.31 ? 1971 HOH   B O     1 
HETATM 20302 O  O     . HOH   W 10 .    ? -7.708  25.540  103.732 1.00 43.13 ? 1972 HOH   B O     1 
HETATM 20303 O  O     . HOH   W 10 .    ? -5.326  -2.422  117.048 1.00 27.16 ? 1973 HOH   B O     1 
HETATM 20304 O  O     . HOH   W 10 .    ? -2.754  26.302  60.541  1.00 33.78 ? 1974 HOH   B O     1 
HETATM 20305 O  O     . HOH   W 10 .    ? -1.527  5.282   92.228  1.00 20.16 ? 1975 HOH   B O     1 
HETATM 20306 O  O     . HOH   W 10 .    ? -3.040  10.802  103.821 1.00 18.02 ? 1976 HOH   B O     1 
HETATM 20307 O  O     . HOH   W 10 .    ? -5.081  16.188  96.944  1.00 17.52 ? 1977 HOH   B O     1 
HETATM 20308 O  O     . HOH   W 10 .    ? 12.144  7.729   90.460  1.00 22.84 ? 1978 HOH   B O     1 
HETATM 20309 O  O     . HOH   W 10 .    ? 26.161  20.038  52.889  1.00 30.63 ? 1979 HOH   B O     1 
HETATM 20310 O  O     . HOH   W 10 .    ? 0.334   26.805  94.844  1.00 22.10 ? 1980 HOH   B O     1 
HETATM 20311 O  O     . HOH   W 10 .    ? -2.542  20.295  110.933 1.00 34.20 ? 1981 HOH   B O     1 
HETATM 20312 O  O     . HOH   W 10 .    ? 24.974  57.309  78.354  1.00 22.79 ? 1982 HOH   B O     1 
HETATM 20313 O  O     . HOH   W 10 .    ? 6.443   11.851  126.553 1.00 23.11 ? 1983 HOH   B O     1 
HETATM 20314 O  O     . HOH   W 10 .    ? -6.117  41.631  84.050  1.00 33.39 ? 1984 HOH   B O     1 
HETATM 20315 O  O     . HOH   W 10 .    ? 23.155  12.292  68.087  1.00 24.85 ? 1985 HOH   B O     1 
HETATM 20316 O  O     . HOH   W 10 .    ? -6.169  34.324  83.863  1.00 25.69 ? 1986 HOH   B O     1 
HETATM 20317 O  O     . HOH   W 10 .    ? 22.066  46.128  76.754  1.00 18.74 ? 1987 HOH   B O     1 
HETATM 20318 O  O     . HOH   W 10 .    ? 0.886   -8.108  109.484 1.00 29.14 ? 1988 HOH   B O     1 
HETATM 20319 O  O     . HOH   W 10 .    ? 14.698  16.626  91.956  1.00 22.02 ? 1989 HOH   B O     1 
HETATM 20320 O  O     . HOH   W 10 .    ? -14.494 39.755  124.836 1.00 38.70 ? 1990 HOH   B O     1 
HETATM 20321 O  O     . HOH   W 10 .    ? -27.317 26.718  99.273  1.00 40.99 ? 1991 HOH   B O     1 
HETATM 20322 O  O     . HOH   W 10 .    ? 33.759  18.435  70.773  1.00 41.21 ? 1992 HOH   B O     1 
HETATM 20323 O  O     . HOH   W 10 .    ? 7.918   65.662  68.523  1.00 32.29 ? 1993 HOH   B O     1 
HETATM 20324 O  O     . HOH   W 10 .    ? 10.608  51.105  75.450  1.00 23.31 ? 1994 HOH   B O     1 
HETATM 20325 O  O     . HOH   W 10 .    ? 18.607  66.831  58.470  1.00 30.02 ? 1995 HOH   B O     1 
HETATM 20326 O  O     . HOH   W 10 .    ? 19.076  51.876  79.984  1.00 21.16 ? 1996 HOH   B O     1 
HETATM 20327 O  O     . HOH   W 10 .    ? -2.614  59.914  120.020 1.00 28.49 ? 1997 HOH   B O     1 
HETATM 20328 O  O     . HOH   W 10 .    ? 16.325  21.377  99.783  1.00 22.02 ? 1998 HOH   B O     1 
HETATM 20329 O  O     . HOH   W 10 .    ? 6.947   -8.455  107.359 1.00 36.44 ? 1999 HOH   B O     1 
HETATM 20330 O  O     . HOH   W 10 .    ? 10.466  66.437  86.515  1.00 42.62 ? 2000 HOH   B O     1 
HETATM 20331 O  O     . HOH   W 10 .    ? 17.049  34.138  56.000  1.00 16.94 ? 2001 HOH   B O     1 
HETATM 20332 O  O     . HOH   W 10 .    ? 34.627  26.844  100.219 1.00 41.02 ? 2002 HOH   B O     1 
HETATM 20333 O  O     . HOH   W 10 .    ? 21.436  53.574  83.595  1.00 26.75 ? 2003 HOH   B O     1 
HETATM 20334 O  O     . HOH   W 10 .    ? -14.245 9.224   87.367  1.00 23.98 ? 2004 HOH   B O     1 
HETATM 20335 O  O     . HOH   W 10 .    ? 2.613   48.934  76.178  1.00 19.52 ? 2005 HOH   B O     1 
HETATM 20336 O  O     . HOH   W 10 .    ? -9.437  0.412   112.582 1.00 24.22 ? 2006 HOH   B O     1 
HETATM 20337 O  O     . HOH   W 10 .    ? 24.177  21.547  97.278  1.00 30.75 ? 2007 HOH   B O     1 
HETATM 20338 O  O     . HOH   W 10 .    ? -1.360  67.122  75.380  1.00 28.32 ? 2008 HOH   B O     1 
HETATM 20339 O  O     . HOH   W 10 .    ? 2.806   44.226  58.422  1.00 28.17 ? 2009 HOH   B O     1 
HETATM 20340 O  O     . HOH   W 10 .    ? 28.676  46.321  87.848  1.00 27.55 ? 2010 HOH   B O     1 
HETATM 20341 O  O     . HOH   W 10 .    ? 34.221  24.724  67.637  1.00 42.86 ? 2011 HOH   B O     1 
HETATM 20342 O  O     . HOH   W 10 .    ? 18.900  30.423  88.558  1.00 18.94 ? 2012 HOH   B O     1 
HETATM 20343 O  O     . HOH   W 10 .    ? 4.682   46.541  69.184  1.00 17.20 ? 2013 HOH   B O     1 
HETATM 20344 O  O     . HOH   W 10 .    ? 26.568  22.407  50.341  1.00 38.21 ? 2014 HOH   B O     1 
HETATM 20345 O  O     . HOH   W 10 .    ? 25.126  23.498  81.702  1.00 29.23 ? 2015 HOH   B O     1 
HETATM 20346 O  O     . HOH   W 10 .    ? 4.942   49.069  54.304  1.00 42.41 ? 2016 HOH   B O     1 
HETATM 20347 O  O     . HOH   W 10 .    ? 0.523   36.243  108.990 1.00 37.11 ? 2017 HOH   B O     1 
HETATM 20348 O  O     . HOH   W 10 .    ? 35.079  19.203  59.763  1.00 36.15 ? 2018 HOH   B O     1 
HETATM 20349 O  O     . HOH   W 10 .    ? 9.391   29.176  98.255  1.00 33.72 ? 2019 HOH   B O     1 
HETATM 20350 O  O     . HOH   W 10 .    ? 18.007  76.276  63.794  1.00 30.35 ? 2020 HOH   B O     1 
HETATM 20351 O  O     . HOH   W 10 .    ? 27.179  42.395  104.801 1.00 29.28 ? 2021 HOH   B O     1 
HETATM 20352 O  O     . HOH   W 10 .    ? 17.946  11.529  106.150 1.00 41.99 ? 2022 HOH   B O     1 
HETATM 20353 O  O     . HOH   W 10 .    ? -15.913 52.106  123.399 1.00 39.31 ? 2023 HOH   B O     1 
HETATM 20354 O  O     . HOH   W 10 .    ? 1.697   36.508  49.662  1.00 43.70 ? 2024 HOH   B O     1 
HETATM 20355 O  O     . HOH   W 10 .    ? 18.307  14.800  97.517  1.00 27.12 ? 2025 HOH   B O     1 
HETATM 20356 O  O     . HOH   W 10 .    ? -11.491 -2.179  96.565  1.00 29.28 ? 2026 HOH   B O     1 
HETATM 20357 O  O     . HOH   W 10 .    ? 18.549  53.053  76.003  1.00 20.01 ? 2027 HOH   B O     1 
HETATM 20358 O  O     . HOH   W 10 .    ? 27.061  35.264  90.909  1.00 18.43 ? 2028 HOH   B O     1 
HETATM 20359 O  O     . HOH   W 10 .    ? -4.190  30.642  94.857  1.00 26.68 ? 2029 HOH   B O     1 
HETATM 20360 O  O     . HOH   W 10 .    ? 4.930   47.367  87.087  1.00 20.97 ? 2030 HOH   B O     1 
HETATM 20361 O  O     . HOH   W 10 .    ? 19.961  22.334  74.507  1.00 30.01 ? 2031 HOH   B O     1 
HETATM 20362 O  O     . HOH   W 10 .    ? -1.103  20.606  89.576  1.00 19.20 ? 2032 HOH   B O     1 
HETATM 20363 O  O     . HOH   W 10 .    ? 7.267   37.594  102.885 1.00 31.20 ? 2033 HOH   B O     1 
HETATM 20364 O  O     . HOH   W 10 .    ? 23.928  31.438  110.328 1.00 30.55 ? 2034 HOH   B O     1 
HETATM 20365 O  O     . HOH   W 10 .    ? 41.206  34.414  91.241  1.00 26.99 ? 2035 HOH   B O     1 
HETATM 20366 O  O     . HOH   W 10 .    ? -1.469  48.682  136.030 1.00 52.86 ? 2036 HOH   B O     1 
HETATM 20367 O  O     . HOH   W 10 .    ? -18.107 1.620   95.681  1.00 43.47 ? 2037 HOH   B O     1 
HETATM 20368 O  O     . HOH   W 10 .    ? -4.181  42.392  108.330 1.00 34.78 ? 2038 HOH   B O     1 
HETATM 20369 O  O     . HOH   W 10 .    ? 5.219   42.639  70.755  1.00 14.60 ? 2039 HOH   B O     1 
HETATM 20370 O  O     . HOH   W 10 .    ? 28.850  23.867  51.073  1.00 31.61 ? 2040 HOH   B O     1 
HETATM 20371 O  O     . HOH   W 10 .    ? 5.499   11.829  77.711  1.00 30.21 ? 2041 HOH   B O     1 
HETATM 20372 O  O     . HOH   W 10 .    ? -16.340 -8.800  106.291 1.00 32.80 ? 2042 HOH   B O     1 
HETATM 20373 O  O     . HOH   W 10 .    ? 8.868   5.905   85.125  1.00 21.28 ? 2043 HOH   B O     1 
HETATM 20374 O  O     . HOH   W 10 .    ? 28.299  44.200  89.707  1.00 26.11 ? 2044 HOH   B O     1 
HETATM 20375 O  O     . HOH   W 10 .    ? 28.088  25.448  67.702  1.00 20.02 ? 2045 HOH   B O     1 
HETATM 20376 O  O     . HOH   W 10 .    ? 24.817  50.764  67.143  1.00 22.44 ? 2046 HOH   B O     1 
HETATM 20377 O  O     . HOH   W 10 .    ? -4.467  44.543  108.741 1.00 30.79 ? 2047 HOH   B O     1 
HETATM 20378 O  O     . HOH   W 10 .    ? 26.178  27.396  67.137  1.00 16.79 ? 2048 HOH   B O     1 
HETATM 20379 O  O     . HOH   W 10 .    ? 5.527   53.233  113.334 1.00 37.54 ? 2049 HOH   B O     1 
HETATM 20380 O  O     . HOH   W 10 .    ? 17.404  33.941  68.414  1.00 14.85 ? 2050 HOH   B O     1 
HETATM 20381 O  O     . HOH   W 10 .    ? -3.023  33.678  62.489  1.00 22.88 ? 2051 HOH   B O     1 
HETATM 20382 O  O     . HOH   W 10 .    ? -34.465 13.247  110.982 1.00 37.23 ? 2052 HOH   B O     1 
HETATM 20383 O  O     . HOH   W 10 .    ? -7.788  23.836  125.233 1.00 34.04 ? 2053 HOH   B O     1 
HETATM 20384 O  O     . HOH   W 10 .    ? -24.897 16.695  82.057  1.00 31.46 ? 2054 HOH   B O     1 
HETATM 20385 O  O     . HOH   W 10 .    ? -8.111  -2.058  124.331 1.00 40.56 ? 2055 HOH   B O     1 
HETATM 20386 O  O     . HOH   W 10 .    ? 16.333  53.532  104.846 1.00 28.26 ? 2056 HOH   B O     1 
HETATM 20387 O  O     . HOH   W 10 .    ? 21.490  6.777   83.617  1.00 37.47 ? 2057 HOH   B O     1 
HETATM 20388 O  O     . HOH   W 10 .    ? 8.165   62.537  66.309  1.00 33.36 ? 2058 HOH   B O     1 
HETATM 20389 O  O     . HOH   W 10 .    ? -3.418  45.795  106.907 1.00 24.78 ? 2059 HOH   B O     1 
HETATM 20390 O  O     . HOH   W 10 .    ? -0.132  75.640  68.189  1.00 37.17 ? 2060 HOH   B O     1 
HETATM 20391 O  O     . HOH   W 10 .    ? 18.087  23.182  61.435  1.00 22.52 ? 2061 HOH   B O     1 
HETATM 20392 O  O     . HOH   W 10 .    ? -4.617  34.173  56.928  1.00 43.37 ? 2062 HOH   B O     1 
HETATM 20393 O  O     . HOH   W 10 .    ? 1.373   22.329  63.623  1.00 26.14 ? 2063 HOH   B O     1 
HETATM 20394 O  O     . HOH   W 10 .    ? -1.799  -1.213  109.032 1.00 25.37 ? 2064 HOH   B O     1 
HETATM 20395 O  O     . HOH   W 10 .    ? 7.968   28.454  81.036  1.00 28.15 ? 2065 HOH   B O     1 
HETATM 20396 O  O     . HOH   W 10 .    ? -4.356  55.613  81.691  1.00 29.35 ? 2066 HOH   B O     1 
HETATM 20397 O  O     . HOH   W 10 .    ? 1.956   30.510  95.990  1.00 21.91 ? 2067 HOH   B O     1 
HETATM 20398 O  O     . HOH   W 10 .    ? 33.374  22.915  64.446  1.00 30.24 ? 2068 HOH   B O     1 
HETATM 20399 O  O     . HOH   W 10 .    ? 11.624  16.186  67.676  1.00 31.45 ? 2069 HOH   B O     1 
HETATM 20400 O  O     . HOH   W 10 .    ? -0.943  13.398  100.792 1.00 17.44 ? 2070 HOH   B O     1 
HETATM 20401 O  O     . HOH   W 10 .    ? -2.572  14.377  98.795  1.00 17.54 ? 2071 HOH   B O     1 
HETATM 20402 O  O     . HOH   W 10 .    ? -31.831 22.130  117.812 1.00 42.12 ? 2072 HOH   B O     1 
HETATM 20403 O  O     . HOH   W 10 .    ? 18.561  47.815  90.035  1.00 22.39 ? 2073 HOH   B O     1 
HETATM 20404 O  O     . HOH   W 10 .    ? 31.055  34.305  77.267  1.00 29.40 ? 2074 HOH   B O     1 
HETATM 20405 O  O     . HOH   W 10 .    ? -32.737 19.848  101.637 1.00 42.32 ? 2075 HOH   B O     1 
HETATM 20406 O  O     . HOH   W 10 .    ? 8.179   31.632  93.961  1.00 24.80 ? 2076 HOH   B O     1 
HETATM 20407 O  O     . HOH   W 10 .    ? 11.974  49.392  78.941  1.00 32.05 ? 2077 HOH   B O     1 
HETATM 20408 O  O     . HOH   W 10 .    ? -1.705  36.645  87.417  1.00 21.62 ? 2078 HOH   B O     1 
HETATM 20409 O  O     . HOH   W 10 .    ? -23.092 25.544  103.422 1.00 37.04 ? 2079 HOH   B O     1 
HETATM 20410 O  O     . HOH   W 10 .    ? -1.666  -2.744  118.710 1.00 38.56 ? 2080 HOH   B O     1 
HETATM 20411 O  O     . HOH   W 10 .    ? -14.553 26.758  101.464 1.00 28.17 ? 2081 HOH   B O     1 
HETATM 20412 O  O     . HOH   W 10 .    ? -9.215  45.524  131.000 1.00 34.34 ? 2082 HOH   B O     1 
HETATM 20413 O  O     . HOH   W 10 .    ? -0.162  39.413  131.378 1.00 36.21 ? 2083 HOH   B O     1 
HETATM 20414 O  O     . HOH   W 10 .    ? 8.347   37.322  79.199  1.00 17.69 ? 2084 HOH   B O     1 
HETATM 20415 O  O     . HOH   W 10 .    ? 30.524  20.066  73.614  1.00 33.34 ? 2085 HOH   B O     1 
HETATM 20416 O  O     . HOH   W 10 .    ? 27.939  8.853   73.846  1.00 34.23 ? 2086 HOH   B O     1 
HETATM 20417 O  O     . HOH   W 10 .    ? 23.304  76.331  65.354  1.00 43.46 ? 2087 HOH   B O     1 
HETATM 20418 O  O     . HOH   W 10 .    ? 22.832  9.621   85.108  1.00 42.86 ? 2088 HOH   B O     1 
HETATM 20419 O  O     . HOH   W 10 .    ? 33.388  19.255  87.585  1.00 24.36 ? 2089 HOH   B O     1 
HETATM 20420 O  O     . HOH   W 10 .    ? -1.864  28.082  62.737  1.00 25.68 ? 2090 HOH   B O     1 
HETATM 20421 O  O     . HOH   W 10 .    ? 17.566  43.944  111.946 1.00 35.26 ? 2091 HOH   B O     1 
HETATM 20422 O  O     . HOH   W 10 .    ? -8.622  31.424  86.878  1.00 20.13 ? 2092 HOH   B O     1 
HETATM 20423 O  O     A HOH   W 10 .    ? 0.670   63.307  84.621  0.61 25.35 ? 2093 HOH   B O     1 
HETATM 20424 O  O     . HOH   W 10 .    ? 12.709  61.729  84.476  1.00 34.09 ? 2094 HOH   B O     1 
HETATM 20425 O  O     . HOH   W 10 .    ? 27.183  18.158  62.038  1.00 22.61 ? 2095 HOH   B O     1 
HETATM 20426 O  O     . HOH   W 10 .    ? 28.423  33.709  80.120  1.00 38.06 ? 2096 HOH   B O     1 
HETATM 20427 O  O     . HOH   W 10 .    ? 30.603  34.197  84.479  1.00 30.29 ? 2097 HOH   B O     1 
HETATM 20428 O  O     . HOH   W 10 .    ? 2.620   48.814  99.028  1.00 22.44 ? 2098 HOH   B O     1 
HETATM 20429 O  O     . HOH   W 10 .    ? 2.336   55.916  119.248 1.00 44.80 ? 2099 HOH   B O     1 
HETATM 20430 O  O     . HOH   W 10 .    ? -18.207 5.982   95.740  1.00 33.93 ? 2100 HOH   B O     1 
HETATM 20431 O  O     . HOH   W 10 .    ? -2.044  57.566  75.168  1.00 19.71 ? 2101 HOH   B O     1 
HETATM 20432 O  O     . HOH   W 10 .    ? -16.371 21.845  82.367  1.00 27.14 ? 2102 HOH   B O     1 
HETATM 20433 O  O     . HOH   W 10 .    ? 29.577  41.420  80.025  1.00 28.78 ? 2103 HOH   B O     1 
HETATM 20434 O  O     . HOH   W 10 .    ? 35.909  31.238  103.715 1.00 31.73 ? 2104 HOH   B O     1 
HETATM 20435 O  O     . HOH   W 10 .    ? 32.520  29.057  64.591  1.00 23.94 ? 2105 HOH   B O     1 
HETATM 20436 O  O     . HOH   W 10 .    ? 25.938  78.954  71.747  1.00 45.33 ? 2106 HOH   B O     1 
HETATM 20437 O  O     . HOH   W 10 .    ? 4.848   17.743  91.214  1.00 23.91 ? 2107 HOH   B O     1 
HETATM 20438 O  O     . HOH   W 10 .    ? 10.537  33.315  109.434 1.00 29.05 ? 2108 HOH   B O     1 
HETATM 20439 O  O     . HOH   W 10 .    ? 22.019  25.001  82.516  1.00 22.51 ? 2109 HOH   B O     1 
HETATM 20440 O  O     . HOH   W 10 .    ? 16.327  55.825  63.956  1.00 26.49 ? 2110 HOH   B O     1 
HETATM 20441 O  O     . HOH   W 10 .    ? 0.696   -0.058  96.203  1.00 26.76 ? 2111 HOH   B O     1 
HETATM 20442 O  O     . HOH   W 10 .    ? -0.487  17.859  91.524  1.00 23.67 ? 2112 HOH   B O     1 
HETATM 20443 O  O     . HOH   W 10 .    ? 4.442   76.980  63.097  1.00 34.32 ? 2113 HOH   B O     1 
HETATM 20444 O  O     . HOH   W 10 .    ? 24.868  62.847  54.548  1.00 35.41 ? 2114 HOH   B O     1 
HETATM 20445 O  O     . HOH   W 10 .    ? 34.033  22.273  78.250  1.00 26.27 ? 2115 HOH   B O     1 
HETATM 20446 O  O     . HOH   W 10 .    ? 33.000  37.770  104.454 1.00 32.78 ? 2116 HOH   B O     1 
HETATM 20447 O  O     . HOH   W 10 .    ? -31.859 20.943  98.396  1.00 41.73 ? 2117 HOH   B O     1 
HETATM 20448 O  O     . HOH   W 10 .    ? 8.052   57.978  85.233  1.00 25.47 ? 2118 HOH   B O     1 
HETATM 20449 O  O     . HOH   W 10 .    ? -3.361  12.243  130.858 1.00 37.30 ? 2119 HOH   B O     1 
HETATM 20450 O  O     . HOH   W 10 .    ? 26.991  65.713  57.986  1.00 36.86 ? 2120 HOH   B O     1 
HETATM 20451 O  O     . HOH   W 10 .    ? -7.199  27.801  74.442  1.00 29.21 ? 2121 HOH   B O     1 
HETATM 20452 O  O     . HOH   W 10 .    ? 4.522   15.675  65.936  1.00 38.06 ? 2122 HOH   B O     1 
HETATM 20453 O  O     . HOH   W 10 .    ? -29.240 26.263  120.564 1.00 46.22 ? 2123 HOH   B O     1 
HETATM 20454 O  O     . HOH   W 10 .    ? -21.170 1.182   121.065 1.00 39.40 ? 2124 HOH   B O     1 
HETATM 20455 O  O     . HOH   W 10 .    ? 13.176  47.886  82.069  1.00 28.16 ? 2125 HOH   B O     1 
HETATM 20456 O  O     . HOH   W 10 .    ? 26.324  12.905  88.030  1.00 30.33 ? 2126 HOH   B O     1 
HETATM 20457 O  O     . HOH   W 10 .    ? -15.357 10.122  89.855  1.00 21.68 ? 2127 HOH   B O     1 
HETATM 20458 O  O     . HOH   W 10 .    ? 5.027   57.628  68.912  1.00 23.91 ? 2128 HOH   B O     1 
HETATM 20459 O  O     . HOH   W 10 .    ? -10.765 36.319  76.312  1.00 38.29 ? 2129 HOH   B O     1 
HETATM 20460 O  O     . HOH   W 10 .    ? -12.318 34.756  86.566  1.00 39.91 ? 2130 HOH   B O     1 
HETATM 20461 O  O     . HOH   W 10 .    ? 28.618  49.938  86.266  1.00 36.96 ? 2131 HOH   B O     1 
HETATM 20462 O  O     . HOH   W 10 .    ? -5.447  22.920  80.655  1.00 22.75 ? 2132 HOH   B O     1 
HETATM 20463 O  O     . HOH   W 10 .    ? -6.993  43.866  73.820  1.00 32.97 ? 2133 HOH   B O     1 
HETATM 20464 O  O     . HOH   W 10 .    ? 11.431  18.405  97.904  1.00 27.23 ? 2134 HOH   B O     1 
HETATM 20465 O  O     . HOH   W 10 .    ? -19.715 23.743  112.551 1.00 35.09 ? 2135 HOH   B O     1 
HETATM 20466 O  O     . HOH   W 10 .    ? -20.444 25.175  94.438  1.00 26.44 ? 2136 HOH   B O     1 
HETATM 20467 O  O     . HOH   W 10 .    ? 21.367  11.339  99.090  1.00 42.87 ? 2137 HOH   B O     1 
HETATM 20468 O  O     . HOH   W 10 .    ? -6.020  35.528  92.594  1.00 29.88 ? 2138 HOH   B O     1 
HETATM 20469 O  O     . HOH   W 10 .    ? 21.210  47.533  55.993  1.00 33.22 ? 2139 HOH   B O     1 
HETATM 20470 O  O     . HOH   W 10 .    ? 7.763   54.148  64.491  1.00 30.40 ? 2140 HOH   B O     1 
HETATM 20471 O  O     . HOH   W 10 .    ? 10.027  53.062  65.675  1.00 25.02 ? 2141 HOH   B O     1 
HETATM 20472 O  O     . HOH   W 10 .    ? 10.550  37.503  77.624  1.00 23.55 ? 2142 HOH   B O     1 
HETATM 20473 O  O     . HOH   W 10 .    ? 5.655   18.478  87.454  1.00 26.55 ? 2143 HOH   B O     1 
HETATM 20474 O  O     . HOH   W 10 .    ? -13.571 48.854  110.651 1.00 31.79 ? 2144 HOH   B O     1 
HETATM 20475 O  O     . HOH   W 10 .    ? 31.115  67.165  82.404  1.00 32.03 ? 2145 HOH   B O     1 
HETATM 20476 O  O     . HOH   W 10 .    ? -2.281  -7.735  110.489 1.00 23.52 ? 2146 HOH   B O     1 
HETATM 20477 O  O     . HOH   W 10 .    ? -3.306  52.296  82.574  1.00 28.55 ? 2147 HOH   B O     1 
HETATM 20478 O  O     . HOH   W 10 .    ? 1.918   20.006  92.422  1.00 37.39 ? 2148 HOH   B O     1 
HETATM 20479 O  O     . HOH   W 10 .    ? -5.494  46.537  84.274  1.00 24.70 ? 2149 HOH   B O     1 
HETATM 20480 O  O     . HOH   W 10 .    ? 10.054  21.907  102.660 1.00 33.35 ? 2150 HOH   B O     1 
HETATM 20481 O  O     . HOH   W 10 .    ? 33.100  25.341  101.907 1.00 30.80 ? 2151 HOH   B O     1 
HETATM 20482 O  O     . HOH   W 10 .    ? -12.136 7.794   127.074 1.00 27.96 ? 2152 HOH   B O     1 
HETATM 20483 O  O     . HOH   W 10 .    ? 15.848  10.123  95.610  1.00 23.96 ? 2153 HOH   B O     1 
HETATM 20484 O  O     . HOH   W 10 .    ? 8.518   -0.991  98.753  1.00 37.07 ? 2154 HOH   B O     1 
HETATM 20485 O  O     . HOH   W 10 .    ? -16.413 25.146  106.902 1.00 33.21 ? 2155 HOH   B O     1 
HETATM 20486 O  O     . HOH   W 10 .    ? 16.920  51.269  59.933  1.00 26.64 ? 2156 HOH   B O     1 
HETATM 20487 O  O     . HOH   W 10 .    ? 23.207  72.619  81.720  1.00 30.67 ? 2157 HOH   B O     1 
HETATM 20488 O  O     . HOH   W 10 .    ? 31.177  50.905  79.897  1.00 30.97 ? 2158 HOH   B O     1 
HETATM 20489 O  O     . HOH   W 10 .    ? -2.595  30.337  70.694  1.00 19.92 ? 2159 HOH   B O     1 
HETATM 20490 O  O     . HOH   W 10 .    ? -7.425  13.060  94.545  1.00 17.98 ? 2160 HOH   B O     1 
HETATM 20491 O  O     . HOH   W 10 .    ? 25.101  53.153  68.588  1.00 24.08 ? 2161 HOH   B O     1 
HETATM 20492 O  O     . HOH   W 10 .    ? 31.738  62.163  75.011  1.00 21.39 ? 2162 HOH   B O     1 
HETATM 20493 O  O     . HOH   W 10 .    ? 3.127   31.197  98.353  1.00 26.97 ? 2163 HOH   B O     1 
HETATM 20494 O  O     . HOH   W 10 .    ? 3.357   53.663  57.500  1.00 40.11 ? 2164 HOH   B O     1 
HETATM 20495 O  O     . HOH   W 10 .    ? 12.364  77.399  64.274  1.00 37.59 ? 2165 HOH   B O     1 
HETATM 20496 O  O     . HOH   W 10 .    ? -11.955 21.807  85.647  1.00 23.92 ? 2166 HOH   B O     1 
HETATM 20497 O  O     . HOH   W 10 .    ? -10.730 52.289  128.459 1.00 38.17 ? 2167 HOH   B O     1 
HETATM 20498 O  O     . HOH   W 10 .    ? 5.358   23.962  119.339 1.00 44.49 ? 2168 HOH   B O     1 
HETATM 20499 O  O     . HOH   W 10 .    ? 35.070  32.200  55.193  1.00 28.52 ? 2169 HOH   B O     1 
HETATM 20500 O  O     . HOH   W 10 .    ? 6.527   16.762  115.231 1.00 33.61 ? 2170 HOH   B O     1 
HETATM 20501 O  O     . HOH   W 10 .    ? 25.024  17.831  100.231 1.00 33.81 ? 2171 HOH   B O     1 
HETATM 20502 O  O     . HOH   W 10 .    ? -7.973  47.989  76.656  1.00 31.83 ? 2172 HOH   B O     1 
HETATM 20503 O  O     . HOH   W 10 .    ? -14.909 18.639  80.109  1.00 35.69 ? 2173 HOH   B O     1 
HETATM 20504 O  O     . HOH   W 10 .    ? 27.335  39.187  104.687 1.00 32.84 ? 2174 HOH   B O     1 
HETATM 20505 O  O     . HOH   W 10 .    ? -2.872  39.827  57.890  1.00 23.85 ? 2175 HOH   B O     1 
HETATM 20506 O  O     . HOH   W 10 .    ? 1.342   42.068  98.377  1.00 32.03 ? 2176 HOH   B O     1 
HETATM 20507 O  O     . HOH   W 10 .    ? 4.841   56.080  74.996  1.00 18.37 ? 2177 HOH   B O     1 
HETATM 20508 O  O     . HOH   W 10 .    ? 11.676  17.876  94.836  1.00 33.50 ? 2178 HOH   B O     1 
HETATM 20509 O  O     . HOH   W 10 .    ? 4.752   -3.897  95.269  1.00 34.25 ? 2179 HOH   B O     1 
HETATM 20510 O  O     . HOH   W 10 .    ? 35.687  32.962  80.913  1.00 44.27 ? 2180 HOH   B O     1 
HETATM 20511 O  O     . HOH   W 10 .    ? 14.188  75.570  62.941  1.00 29.71 ? 2181 HOH   B O     1 
HETATM 20512 O  O     . HOH   W 10 .    ? 35.456  25.337  77.607  1.00 26.21 ? 2182 HOH   B O     1 
HETATM 20513 O  O     . HOH   W 10 .    ? -5.627  35.563  87.872  1.00 29.84 ? 2183 HOH   B O     1 
HETATM 20514 O  O     . HOH   W 10 .    ? 18.059  49.778  111.759 1.00 33.24 ? 2184 HOH   B O     1 
HETATM 20515 O  O     . HOH   W 10 .    ? 32.386  40.236  90.594  1.00 31.39 ? 2185 HOH   B O     1 
HETATM 20516 O  O     . HOH   W 10 .    ? -10.189 18.303  131.031 1.00 33.57 ? 2186 HOH   B O     1 
HETATM 20517 O  O     . HOH   W 10 .    ? 34.812  16.745  67.662  1.00 29.05 ? 2187 HOH   B O     1 
HETATM 20518 O  O     . HOH   W 10 .    ? 29.618  8.583   86.174  1.00 40.00 ? 2188 HOH   B O     1 
HETATM 20519 O  O     . HOH   W 10 .    ? -4.788  56.410  127.081 1.00 38.63 ? 2189 HOH   B O     1 
HETATM 20520 O  O     . HOH   W 10 .    ? 28.036  65.308  84.766  1.00 42.95 ? 2190 HOH   B O     1 
HETATM 20521 O  O     . HOH   W 10 .    ? -22.941 21.620  101.984 1.00 32.07 ? 2191 HOH   B O     1 
HETATM 20522 O  O     . HOH   W 10 .    ? 2.924   44.879  67.870  1.00 18.19 ? 2192 HOH   B O     1 
HETATM 20523 O  O     . HOH   W 10 .    ? -6.468  8.860   82.088  1.00 35.30 ? 2193 HOH   B O     1 
HETATM 20524 O  O     . HOH   W 10 .    ? -0.947  37.626  76.290  1.00 27.17 ? 2194 HOH   B O     1 
HETATM 20525 O  O     . HOH   W 10 .    ? 16.292  51.248  53.923  1.00 39.42 ? 2195 HOH   B O     1 
HETATM 20526 O  O     . HOH   W 10 .    ? -27.106 12.508  100.139 1.00 45.58 ? 2196 HOH   B O     1 
HETATM 20527 O  O     . HOH   W 10 .    ? -9.425  -5.849  94.398  1.00 46.48 ? 2197 HOH   B O     1 
HETATM 20528 O  O     . HOH   W 10 .    ? 25.835  75.118  76.723  1.00 32.18 ? 2198 HOH   B O     1 
HETATM 20529 O  O     . HOH   W 10 .    ? 0.545   20.941  132.043 1.00 36.92 ? 2199 HOH   B O     1 
HETATM 20530 O  O     . HOH   W 10 .    ? 20.204  18.807  60.150  1.00 25.69 ? 2200 HOH   B O     1 
HETATM 20531 O  O     . HOH   W 10 .    ? 9.830   18.236  101.169 1.00 26.51 ? 2201 HOH   B O     1 
HETATM 20532 O  O     . HOH   W 10 .    ? 24.356  67.551  80.815  1.00 38.42 ? 2202 HOH   B O     1 
HETATM 20533 O  O     . HOH   W 10 .    ? -13.501 53.743  122.585 1.00 29.55 ? 2203 HOH   B O     1 
HETATM 20534 O  O     . HOH   W 10 .    ? 40.287  22.421  57.949  1.00 46.61 ? 2204 HOH   B O     1 
HETATM 20535 O  O     . HOH   W 10 .    ? 18.291  75.802  78.794  1.00 38.88 ? 2205 HOH   B O     1 
HETATM 20536 O  O     . HOH   W 10 .    ? 19.270  58.251  82.355  1.00 29.19 ? 2206 HOH   B O     1 
HETATM 20537 O  O     . HOH   W 10 .    ? 37.173  37.350  88.920  1.00 21.79 ? 2207 HOH   B O     1 
HETATM 20538 O  O     . HOH   W 10 .    ? 22.743  49.968  53.688  1.00 39.86 ? 2208 HOH   B O     1 
HETATM 20539 O  O     . HOH   W 10 .    ? -2.708  64.419  83.389  1.00 18.75 ? 2209 HOH   B O     1 
HETATM 20540 O  O     . HOH   W 10 .    ? 18.861  35.313  112.966 1.00 21.25 ? 2210 HOH   B O     1 
HETATM 20541 O  O     . HOH   W 10 .    ? 14.435  8.959   93.591  1.00 23.56 ? 2211 HOH   B O     1 
HETATM 20542 O  O     . HOH   W 10 .    ? 20.521  21.782  61.005  1.00 16.67 ? 2212 HOH   B O     1 
HETATM 20543 O  O     . HOH   W 10 .    ? 7.418   66.243  86.508  1.00 33.76 ? 2213 HOH   B O     1 
HETATM 20544 O  O     . HOH   W 10 .    ? 28.889  22.457  72.283  1.00 30.22 ? 2214 HOH   B O     1 
HETATM 20545 O  O     . HOH   W 10 .    ? 3.043   54.125  66.956  1.00 34.31 ? 2215 HOH   B O     1 
HETATM 20546 O  O     . HOH   W 10 .    ? 20.186  20.313  109.246 1.00 22.34 ? 2216 HOH   B O     1 
HETATM 20547 O  O     . HOH   W 10 .    ? 42.163  37.741  95.775  1.00 32.98 ? 2217 HOH   B O     1 
HETATM 20548 O  O     . HOH   W 10 .    ? -0.607  -8.086  99.612  1.00 24.07 ? 2218 HOH   B O     1 
HETATM 20549 O  O     . HOH   W 10 .    ? 6.861   19.123  116.597 1.00 33.76 ? 2219 HOH   B O     1 
HETATM 20550 O  O     . HOH   W 10 .    ? 29.132  65.156  62.423  1.00 32.09 ? 2220 HOH   B O     1 
HETATM 20551 O  O     . HOH   W 10 .    ? -33.015 7.728   107.970 1.00 42.42 ? 2221 HOH   B O     1 
HETATM 20552 O  O     . HOH   W 10 .    ? 13.425  29.854  79.617  1.00 35.31 ? 2222 HOH   B O     1 
HETATM 20553 O  O     . HOH   W 10 .    ? 22.077  14.759  81.096  1.00 23.57 ? 2223 HOH   B O     1 
HETATM 20554 O  O     . HOH   W 10 .    ? 35.392  31.304  58.488  1.00 30.66 ? 2224 HOH   B O     1 
HETATM 20555 O  O     . HOH   W 10 .    ? 27.428  56.557  81.169  1.00 35.79 ? 2225 HOH   B O     1 
HETATM 20556 O  O     . HOH   W 10 .    ? 4.563   0.021   86.708  1.00 33.44 ? 2226 HOH   B O     1 
HETATM 20557 O  O     . HOH   W 10 .    ? -5.795  15.362  94.479  1.00 18.44 ? 2227 HOH   B O     1 
HETATM 20558 O  O     . HOH   W 10 .    ? 2.490   18.770  77.259  1.00 30.41 ? 2228 HOH   B O     1 
HETATM 20559 O  O     . HOH   W 10 .    ? -24.101 10.291  126.757 1.00 42.81 ? 2229 HOH   B O     1 
HETATM 20560 O  O     . HOH   W 10 .    ? 23.964  49.885  102.522 1.00 42.81 ? 2230 HOH   B O     1 
HETATM 20561 O  O     . HOH   W 10 .    ? 34.438  12.767  80.849  1.00 32.37 ? 2231 HOH   B O     1 
HETATM 20562 O  O     . HOH   W 10 .    ? 9.082   45.780  131.973 1.00 40.73 ? 2232 HOH   B O     1 
HETATM 20563 O  O     . HOH   W 10 .    ? 28.249  30.680  80.706  1.00 24.27 ? 2233 HOH   B O     1 
HETATM 20564 O  O     . HOH   W 10 .    ? -1.801  62.326  69.656  1.00 36.86 ? 2234 HOH   B O     1 
HETATM 20565 O  O     . HOH   W 10 .    ? -19.472 28.737  88.418  1.00 30.76 ? 2235 HOH   B O     1 
HETATM 20566 O  O     . HOH   W 10 .    ? 9.989   76.969  64.825  1.00 44.36 ? 2236 HOH   B O     1 
HETATM 20567 O  O     . HOH   W 10 .    ? 23.033  51.133  65.175  1.00 22.87 ? 2237 HOH   B O     1 
HETATM 20568 O  O     . HOH   W 10 .    ? 5.029   42.862  55.929  1.00 29.85 ? 2238 HOH   B O     1 
HETATM 20569 O  O     . HOH   W 10 .    ? 25.704  53.648  54.280  1.00 43.89 ? 2239 HOH   B O     1 
HETATM 20570 O  O     . HOH   W 10 .    ? 16.382  52.014  79.604  1.00 22.87 ? 2240 HOH   B O     1 
HETATM 20571 O  O     . HOH   W 10 .    ? -12.750 31.321  83.732  1.00 36.81 ? 2241 HOH   B O     1 
HETATM 20572 O  O     . HOH   W 10 .    ? 7.976   77.455  85.567  1.00 39.55 ? 2242 HOH   B O     1 
HETATM 20573 O  O     . HOH   W 10 .    ? 8.387   15.845  92.798  1.00 33.75 ? 2243 HOH   B O     1 
HETATM 20574 O  O     . HOH   W 10 .    ? -27.373 9.451   88.927  1.00 45.10 ? 2244 HOH   B O     1 
HETATM 20575 O  O     . HOH   W 10 .    ? -34.673 22.040  116.208 1.00 47.73 ? 2245 HOH   B O     1 
HETATM 20576 O  O     . HOH   W 10 .    ? 12.725  29.223  50.471  1.00 28.39 ? 2246 HOH   B O     1 
HETATM 20577 O  O     . HOH   W 10 .    ? 22.380  11.736  79.618  1.00 36.59 ? 2247 HOH   B O     1 
HETATM 20578 O  O     . HOH   W 10 .    ? 10.040  51.977  107.879 1.00 44.22 ? 2248 HOH   B O     1 
HETATM 20579 O  O     . HOH   W 10 .    ? -7.497  10.273  112.927 1.00 19.75 ? 2249 HOH   B O     1 
HETATM 20580 O  O     . HOH   W 10 .    ? -2.008  2.544   83.292  1.00 40.10 ? 2250 HOH   B O     1 
HETATM 20581 O  O     . HOH   W 10 .    ? 13.444  18.537  87.546  1.00 26.05 ? 2251 HOH   B O     1 
HETATM 20582 O  O     . HOH   W 10 .    ? 5.756   -3.809  99.525  1.00 41.14 ? 2252 HOH   B O     1 
HETATM 20583 O  O     . HOH   W 10 .    ? 18.110  74.525  81.761  1.00 37.62 ? 2253 HOH   B O     1 
HETATM 20584 O  O     . HOH   W 10 .    ? -14.978 19.178  82.639  1.00 28.27 ? 2254 HOH   B O     1 
HETATM 20585 O  O     . HOH   W 10 .    ? 4.417   17.809  127.825 1.00 36.49 ? 2255 HOH   B O     1 
HETATM 20586 O  O     . HOH   W 10 .    ? 34.702  6.103   81.661  1.00 41.47 ? 2256 HOH   B O     1 
HETATM 20587 O  O     . HOH   W 10 .    ? -36.145 21.510  114.087 1.00 46.54 ? 2257 HOH   B O     1 
HETATM 20588 O  O     . HOH   W 10 .    ? 19.236  54.477  104.191 1.00 27.77 ? 2258 HOH   B O     1 
HETATM 20589 O  O     . HOH   W 10 .    ? 24.093  31.478  47.222  1.00 36.31 ? 2259 HOH   B O     1 
HETATM 20590 O  O     . HOH   W 10 .    ? 23.384  24.434  47.667  1.00 35.42 ? 2260 HOH   B O     1 
HETATM 20591 O  O     . HOH   W 10 .    ? 9.257   -0.591  90.333  1.00 36.23 ? 2261 HOH   B O     1 
HETATM 20592 O  O     . HOH   W 10 .    ? 28.155  48.960  97.868  1.00 34.73 ? 2262 HOH   B O     1 
HETATM 20593 O  O     . HOH   W 10 .    ? -14.083 44.466  113.315 1.00 40.09 ? 2263 HOH   B O     1 
HETATM 20594 O  O     . HOH   W 10 .    ? 26.707  40.929  81.237  1.00 26.52 ? 2264 HOH   B O     1 
HETATM 20595 O  O     . HOH   W 10 .    ? 23.861  16.939  82.604  1.00 24.54 ? 2265 HOH   B O     1 
HETATM 20596 O  O     . HOH   W 10 .    ? 42.453  32.041  96.558  1.00 40.54 ? 2266 HOH   B O     1 
HETATM 20597 O  O     . HOH   W 10 .    ? 13.220  23.287  89.285  1.00 40.82 ? 2267 HOH   B O     1 
HETATM 20598 O  O     . HOH   W 10 .    ? 30.829  19.669  56.268  1.00 27.96 ? 2268 HOH   B O     1 
HETATM 20599 O  O     . HOH   W 10 .    ? -2.635  26.347  113.323 1.00 42.71 ? 2269 HOH   B O     1 
HETATM 20600 O  O     . HOH   W 10 .    ? 15.169  28.880  49.215  1.00 31.36 ? 2270 HOH   B O     1 
HETATM 20601 O  O     . HOH   W 10 .    ? -4.727  -4.067  91.768  1.00 27.55 ? 2271 HOH   B O     1 
HETATM 20602 O  O     . HOH   W 10 .    ? -22.112 22.326  86.681  1.00 37.91 ? 2272 HOH   B O     1 
HETATM 20603 O  O     . HOH   W 10 .    ? -37.551 13.543  94.851  1.00 52.24 ? 2273 HOH   B O     1 
HETATM 20604 O  O     . HOH   W 10 .    ? -3.283  -2.901  85.151  1.00 38.16 ? 2274 HOH   B O     1 
HETATM 20605 O  O     . HOH   W 10 .    ? 17.064  7.655   89.978  1.00 37.12 ? 2275 HOH   B O     1 
HETATM 20606 O  O     . HOH   W 10 .    ? 38.070  22.877  90.067  1.00 46.23 ? 2276 HOH   B O     1 
HETATM 20607 O  O     . HOH   W 10 .    ? 6.415   24.617  83.682  1.00 25.86 ? 2277 HOH   B O     1 
HETATM 20608 O  O     . HOH   W 10 .    ? -23.745 23.322  84.478  1.00 39.15 ? 2278 HOH   B O     1 
HETATM 20609 O  O     . HOH   W 10 .    ? 20.840  30.499  113.226 1.00 38.10 ? 2279 HOH   B O     1 
HETATM 20610 O  O     . HOH   W 10 .    ? -9.394  14.007  114.815 1.00 31.37 ? 2280 HOH   B O     1 
HETATM 20611 O  O     . HOH   W 10 .    ? 33.491  37.999  71.691  1.00 40.84 ? 2281 HOH   B O     1 
HETATM 20612 O  O     . HOH   W 10 .    ? -30.680 5.516   99.994  1.00 37.33 ? 2282 HOH   B O     1 
HETATM 20613 O  O     . HOH   W 10 .    ? 20.781  62.581  54.145  1.00 35.80 ? 2283 HOH   B O     1 
HETATM 20614 O  O     . HOH   W 10 .    ? 5.451   66.701  61.789  1.00 41.00 ? 2284 HOH   B O     1 
HETATM 20615 O  O     . HOH   W 10 .    ? 12.705  46.061  111.393 1.00 40.66 ? 2285 HOH   B O     1 
HETATM 20616 O  O     . HOH   W 10 .    ? -29.583 11.704  87.497  1.00 46.71 ? 2286 HOH   B O     1 
HETATM 20617 O  O     . HOH   W 10 .    ? -4.303  26.496  99.773  1.00 27.25 ? 2287 HOH   B O     1 
HETATM 20618 O  O     . HOH   W 10 .    ? 31.890  36.867  51.194  1.00 40.69 ? 2288 HOH   B O     1 
HETATM 20619 O  O     . HOH   W 10 .    ? 15.470  49.433  79.001  1.00 27.07 ? 2289 HOH   B O     1 
HETATM 20620 O  O     . HOH   W 10 .    ? 33.044  25.997  54.586  1.00 39.94 ? 2290 HOH   B O     1 
HETATM 20621 O  O     . HOH   W 10 .    ? -5.418  37.388  86.023  1.00 29.78 ? 2291 HOH   B O     1 
HETATM 20622 O  O     . HOH   W 10 .    ? 32.664  70.143  73.544  1.00 38.12 ? 2292 HOH   B O     1 
HETATM 20623 O  O     . HOH   W 10 .    ? -27.827 14.096  86.415  1.00 34.90 ? 2293 HOH   B O     1 
HETATM 20624 O  O     . HOH   W 10 .    ? 28.254  25.340  104.562 1.00 46.15 ? 2294 HOH   B O     1 
HETATM 20625 O  O     . HOH   W 10 .    ? 12.174  22.499  113.389 1.00 42.11 ? 2295 HOH   B O     1 
HETATM 20626 O  O     . HOH   W 10 .    ? 8.832   30.571  88.681  1.00 35.97 ? 2296 HOH   B O     1 
HETATM 20627 O  O     . HOH   W 10 .    ? 31.640  35.060  74.432  1.00 31.89 ? 2297 HOH   B O     1 
HETATM 20628 O  O     . HOH   W 10 .    ? -9.049  -7.268  113.257 1.00 38.52 ? 2298 HOH   B O     1 
HETATM 20629 O  O     . HOH   W 10 .    ? -2.632  -5.660  89.681  1.00 34.25 ? 2299 HOH   B O     1 
HETATM 20630 O  O     . HOH   W 10 .    ? -1.031  22.514  96.980  1.00 30.91 ? 2300 HOH   B O     1 
HETATM 20631 O  O     . HOH   W 10 .    ? 3.718   66.966  60.192  1.00 41.99 ? 2301 HOH   B O     1 
HETATM 20632 O  O     . HOH   W 10 .    ? 2.401   3.688   84.576  1.00 31.62 ? 2302 HOH   B O     1 
HETATM 20633 O  O     . HOH   W 10 .    ? 12.233  57.783  94.078  1.00 34.38 ? 2303 HOH   B O     1 
HETATM 20634 O  O     . HOH   W 10 .    ? 23.121  7.987   73.595  1.00 40.67 ? 2304 HOH   B O     1 
HETATM 20635 O  O     . HOH   W 10 .    ? -6.667  38.974  67.343  1.00 32.77 ? 2305 HOH   B O     1 
HETATM 20636 O  O     . HOH   W 10 .    ? -2.769  77.034  70.681  1.00 42.26 ? 2306 HOH   B O     1 
HETATM 20637 O  O     . HOH   W 10 .    ? 39.760  34.841  82.390  1.00 47.78 ? 2307 HOH   B O     1 
HETATM 20638 O  O     . HOH   W 10 .    ? 4.520   25.211  128.849 1.00 34.58 ? 2308 HOH   B O     1 
HETATM 20639 O  O     . HOH   W 10 .    ? -5.302  50.992  83.431  1.00 36.67 ? 2309 HOH   B O     1 
HETATM 20640 O  O     . HOH   W 10 .    ? 15.003  56.839  72.139  1.00 24.08 ? 2310 HOH   B O     1 
HETATM 20641 O  O     . HOH   W 10 .    ? -9.202  7.483   82.099  1.00 41.47 ? 2311 HOH   B O     1 
HETATM 20642 O  O     . HOH   W 10 .    ? 32.121  44.997  61.623  1.00 37.04 ? 2312 HOH   B O     1 
HETATM 20643 O  O     . HOH   W 10 .    ? 35.597  19.684  85.501  1.00 36.39 ? 2313 HOH   B O     1 
HETATM 20644 O  O     . HOH   W 10 .    ? 35.535  17.030  83.322  1.00 42.90 ? 2314 HOH   B O     1 
HETATM 20645 O  O     . HOH   W 10 .    ? 5.943   70.329  61.027  1.00 37.03 ? 2315 HOH   B O     1 
HETATM 20646 O  O     . HOH   W 10 .    ? -2.542  42.169  74.351  1.00 34.67 ? 2316 HOH   B O     1 
HETATM 20647 O  O     . HOH   W 10 .    ? -4.181  25.487  114.654 1.00 42.49 ? 2317 HOH   B O     1 
HETATM 20648 O  O     . HOH   W 10 .    ? -2.781  22.738  79.487  1.00 25.04 ? 2318 HOH   B O     1 
HETATM 20649 O  O     . HOH   W 10 .    ? -0.966  44.202  75.518  1.00 33.88 ? 2319 HOH   B O     1 
HETATM 20650 O  O     . HOH   W 10 .    ? -16.888 49.480  116.406 1.00 44.31 ? 2320 HOH   B O     1 
HETATM 20651 O  O     . HOH   W 10 .    ? 23.054  67.568  59.601  1.00 27.57 ? 2321 HOH   B O     1 
HETATM 20652 O  O     . HOH   W 10 .    ? 9.854   68.356  55.001  1.00 45.48 ? 2322 HOH   B O     1 
HETATM 20653 O  O     . HOH   W 10 .    ? 32.977  47.236  87.457  1.00 44.83 ? 2323 HOH   B O     1 
HETATM 20654 O  O     . HOH   W 10 .    ? 26.555  51.558  55.780  1.00 34.46 ? 2324 HOH   B O     1 
HETATM 20655 O  O     . HOH   W 10 .    ? 24.292  45.232  49.381  1.00 47.86 ? 2325 HOH   B O     1 
HETATM 20656 O  O     . HOH   W 10 .    ? -0.992  56.948  124.561 1.00 45.14 ? 2326 HOH   B O     1 
HETATM 20657 O  O     . HOH   W 10 .    ? 27.792  71.495  81.038  1.00 45.03 ? 2327 HOH   B O     1 
HETATM 20658 O  O     . HOH   W 10 .    ? 18.080  46.238  111.839 1.00 37.89 ? 2328 HOH   B O     1 
HETATM 20659 O  O     . HOH   W 10 .    ? 7.668   -9.353  111.387 1.00 34.76 ? 2329 HOH   B O     1 
HETATM 20660 O  O     . HOH   W 10 .    ? -24.147 -2.175  112.607 1.00 44.66 ? 2330 HOH   B O     1 
HETATM 20661 O  O     . HOH   W 10 .    ? 16.345  13.923  106.877 1.00 26.06 ? 2331 HOH   B O     1 
HETATM 20662 O  O     . HOH   W 10 .    ? 28.394  41.365  53.252  1.00 31.26 ? 2332 HOH   B O     1 
HETATM 20663 O  O     . HOH   W 10 .    ? 32.802  20.067  72.353  1.00 39.35 ? 2333 HOH   B O     1 
HETATM 20664 O  O     . HOH   W 10 .    ? -0.740  43.746  56.001  1.00 31.46 ? 2334 HOH   B O     1 
HETATM 20665 O  O     . HOH   W 10 .    ? -14.946 51.022  126.986 1.00 44.81 ? 2335 HOH   B O     1 
HETATM 20666 O  O     . HOH   W 10 .    ? -6.132  39.701  86.262  1.00 33.41 ? 2336 HOH   B O     1 
HETATM 20667 O  O     . HOH   W 10 .    ? 34.609  16.125  62.019  1.00 38.11 ? 2337 HOH   B O     1 
HETATM 20668 O  O     . HOH   W 10 .    ? -0.338  45.072  77.460  1.00 36.57 ? 2338 HOH   B O     1 
HETATM 20669 O  O     . HOH   W 10 .    ? 1.161   55.781  65.697  1.00 37.21 ? 2339 HOH   B O     1 
HETATM 20670 O  O     . HOH   W 10 .    ? 7.565   33.742  51.415  1.00 34.51 ? 2340 HOH   B O     1 
HETATM 20671 O  O     . HOH   W 10 .    ? 30.042  49.206  82.046  1.00 46.85 ? 2341 HOH   B O     1 
HETATM 20672 O  O     . HOH   W 10 .    ? 26.536  47.074  102.857 1.00 38.47 ? 2342 HOH   B O     1 
HETATM 20673 O  O     . HOH   W 10 .    ? -3.937  -4.857  94.168  1.00 36.73 ? 2343 HOH   B O     1 
HETATM 20674 O  O     . HOH   W 10 .    ? 2.927   57.014  70.829  1.00 31.06 ? 2344 HOH   B O     1 
HETATM 20675 O  O     . HOH   W 10 .    ? 8.740   -3.538  119.435 1.00 48.95 ? 2345 HOH   B O     1 
HETATM 20676 O  O     . HOH   W 10 .    ? -6.691  45.845  81.693  1.00 46.51 ? 2346 HOH   B O     1 
HETATM 20677 O  O     . HOH   W 10 .    ? 9.288   23.350  122.048 1.00 39.24 ? 2347 HOH   B O     1 
HETATM 20678 O  O     . HOH   W 10 .    ? 10.745  9.896   123.164 1.00 31.39 ? 2348 HOH   B O     1 
HETATM 20679 O  O     . HOH   W 10 .    ? -14.639 12.735  76.829  1.00 47.13 ? 2349 HOH   B O     1 
HETATM 20680 O  O     . HOH   W 10 .    ? 11.366  43.601  51.008  1.00 33.47 ? 2350 HOH   B O     1 
HETATM 20681 O  O     . HOH   W 10 .    ? 39.649  29.412  80.978  1.00 35.14 ? 2351 HOH   B O     1 
HETATM 20682 O  O     . HOH   W 10 .    ? -2.229  60.196  124.057 1.00 41.18 ? 2352 HOH   B O     1 
HETATM 20683 O  O     . HOH   W 10 .    ? -16.096 51.892  115.711 1.00 44.94 ? 2353 HOH   B O     1 
HETATM 20684 O  O     . HOH   W 10 .    ? 34.142  38.075  66.915  1.00 36.71 ? 2354 HOH   B O     1 
HETATM 20685 O  O     . HOH   W 10 .    ? -4.611  39.183  56.119  1.00 42.03 ? 2355 HOH   B O     1 
HETATM 20686 O  O     . HOH   W 10 .    ? 12.999  34.997  109.571 1.00 37.09 ? 2356 HOH   B O     1 
HETATM 20687 O  O     . HOH   W 10 .    ? 25.210  24.106  49.674  1.00 40.11 ? 2357 HOH   B O     1 
HETATM 20688 O  O     . HOH   W 10 .    ? 2.051   24.319  95.310  1.00 39.61 ? 2358 HOH   B O     1 
HETATM 20689 O  O     . HOH   W 10 .    ? -5.783  48.316  132.869 1.00 43.18 ? 2359 HOH   B O     1 
HETATM 20690 O  O     . HOH   W 10 .    ? -1.419  37.550  73.561  1.00 21.26 ? 2360 HOH   B O     1 
HETATM 20691 O  O     . HOH   W 10 .    ? 18.303  10.570  120.104 1.00 44.12 ? 2361 HOH   B O     1 
HETATM 20692 O  O     . HOH   W 10 .    ? -34.546 16.379  94.285  1.00 46.31 ? 2362 HOH   B O     1 
HETATM 20693 O  O     . HOH   W 10 .    ? 7.359   19.200  97.520  1.00 37.20 ? 2363 HOH   B O     1 
HETATM 20694 O  O     . HOH   W 10 .    ? 4.361   29.512  82.010  1.00 26.79 ? 2364 HOH   B O     1 
HETATM 20695 O  O     . HOH   W 10 .    ? 9.581   18.907  98.816  1.00 35.46 ? 2365 HOH   B O     1 
HETATM 20696 O  O     . HOH   W 10 .    ? 9.257   0.516   119.573 1.00 40.45 ? 2366 HOH   B O     1 
HETATM 20697 O  O     . HOH   W 10 .    ? 30.241  70.967  72.687  1.00 35.97 ? 2367 HOH   B O     1 
HETATM 20698 O  O     . HOH   W 10 .    ? 30.686  42.218  55.504  1.00 32.64 ? 2368 HOH   B O     1 
HETATM 20699 O  O     . HOH   W 10 .    ? 16.798  56.103  94.937  1.00 36.05 ? 2369 HOH   B O     1 
HETATM 20700 O  O     . HOH   W 10 .    ? 6.310   17.187  96.506  1.00 31.87 ? 2370 HOH   B O     1 
HETATM 20701 O  O     . HOH   W 10 .    ? -3.622  14.338  131.911 1.00 37.34 ? 2371 HOH   B O     1 
HETATM 20702 O  O     . HOH   W 10 .    ? -2.618  69.261  75.611  1.00 33.78 ? 2372 HOH   B O     1 
HETATM 20703 O  O     . HOH   W 10 .    ? 12.515  39.518  132.149 1.00 44.21 ? 2373 HOH   B O     1 
HETATM 20704 O  O     . HOH   W 10 .    ? 16.098  7.861   110.835 1.00 40.66 ? 2374 HOH   B O     1 
HETATM 20705 O  O     . HOH   W 10 .    ? 17.081  24.487  52.459  1.00 30.86 ? 2375 HOH   B O     1 
HETATM 20706 O  O     . HOH   W 10 .    ? -7.705  12.204  82.902  1.00 39.15 ? 2376 HOH   B O     1 
HETATM 20707 O  O     . HOH   W 10 .    ? 9.506   48.589  108.550 1.00 36.76 ? 2377 HOH   B O     1 
HETATM 20708 O  O     . HOH   W 10 .    ? -33.405 16.408  121.542 1.00 35.57 ? 2378 HOH   B O     1 
HETATM 20709 O  O     . HOH   W 10 .    ? 30.664  31.743  83.738  1.00 36.86 ? 2379 HOH   B O     1 
HETATM 20710 O  O     . HOH   W 10 .    ? 32.933  34.902  72.321  1.00 34.26 ? 2380 HOH   B O     1 
HETATM 20711 O  O     . HOH   W 10 .    ? -30.435 15.180  119.126 1.00 38.96 ? 2381 HOH   B O     1 
HETATM 20712 O  O     . HOH   W 10 .    ? -6.743  7.936   116.388 1.00 25.38 ? 2382 HOH   B O     1 
HETATM 20713 O  O     . HOH   W 10 .    ? 5.246   44.349  53.693  1.00 28.01 ? 2383 HOH   B O     1 
HETATM 20714 O  O     . HOH   W 10 .    ? 21.180  5.964   73.353  1.00 39.24 ? 2384 HOH   B O     1 
HETATM 20715 O  O     . HOH   W 10 .    ? 15.974  35.163  113.430 1.00 34.32 ? 2385 HOH   B O     1 
HETATM 20716 O  O     . HOH   W 10 .    ? 40.657  30.125  90.201  1.00 26.62 ? 2386 HOH   B O     1 
HETATM 20717 O  O     . HOH   W 10 .    ? 0.565   24.090  99.210  1.00 42.33 ? 2387 HOH   B O     1 
HETATM 20718 O  O     . HOH   W 10 .    ? -2.635  29.692  96.857  1.00 31.63 ? 2388 HOH   B O     1 
HETATM 20719 O  O     . HOH   W 10 .    ? 12.872  47.018  79.510  1.00 33.44 ? 2389 HOH   B O     1 
HETATM 20720 O  O     . HOH   W 10 .    ? 4.807   4.334   78.879  1.00 40.31 ? 2390 HOH   B O     1 
HETATM 20721 O  O     . HOH   W 10 .    ? -6.757  2.602   85.042  1.00 33.52 ? 2391 HOH   B O     1 
HETATM 20722 O  O     . HOH   W 10 .    ? -32.961 17.280  100.953 1.00 39.07 ? 2392 HOH   B O     1 
HETATM 20723 O  O     . HOH   W 10 .    ? -0.066  -2.290  94.911  1.00 28.88 ? 2393 HOH   B O     1 
HETATM 20724 O  O     . HOH   W 10 .    ? -5.183  51.502  102.221 1.00 45.50 ? 2394 HOH   B O     1 
HETATM 20725 O  O     . HOH   W 10 .    ? 38.558  32.482  83.811  1.00 31.17 ? 2395 HOH   B O     1 
HETATM 20726 O  O     . HOH   W 10 .    ? 34.343  35.702  68.879  1.00 41.01 ? 2396 HOH   B O     1 
HETATM 20727 O  O     . HOH   W 10 .    ? 5.121   66.746  64.101  1.00 42.49 ? 2397 HOH   B O     1 
HETATM 20728 O  O     . HOH   W 10 .    ? 32.991  58.559  67.354  1.00 28.43 ? 2398 HOH   B O     1 
HETATM 20729 O  O     . HOH   W 10 .    ? -13.108 9.280   129.520 1.00 35.21 ? 2399 HOH   B O     1 
HETATM 20730 O  O     . HOH   W 10 .    ? 43.769  33.832  95.723  1.00 46.65 ? 2400 HOH   B O     1 
HETATM 20731 O  O     . HOH   W 10 .    ? -36.351 27.383  115.434 1.00 38.19 ? 2401 HOH   B O     1 
HETATM 20732 O  O     . HOH   W 10 .    ? 14.556  55.745  61.767  1.00 38.07 ? 2402 HOH   B O     1 
HETATM 20733 O  O     . HOH   W 10 .    ? 29.766  45.666  85.182  1.00 36.81 ? 2403 HOH   B O     1 
HETATM 20734 O  O     . HOH   W 10 .    ? 19.703  45.322  89.778  1.00 16.54 ? 2404 HOH   B O     1 
HETATM 20735 O  O     . HOH   W 10 .    ? 33.330  22.924  102.420 1.00 46.07 ? 2405 HOH   B O     1 
HETATM 20736 O  O     . HOH   W 10 .    ? 33.259  40.130  61.544  1.00 33.87 ? 2406 HOH   B O     1 
HETATM 20737 O  O     . HOH   W 10 .    ? -7.219  37.181  66.092  1.00 39.16 ? 2407 HOH   B O     1 
HETATM 20738 O  O     . HOH   W 10 .    ? 2.299   3.675   82.075  1.00 34.17 ? 2408 HOH   B O     1 
HETATM 20739 O  O     . HOH   W 10 .    ? 14.288  53.287  86.838  1.00 43.00 ? 2409 HOH   B O     1 
HETATM 20740 O  O     . HOH   W 10 .    ? 23.864  68.596  62.291  1.00 29.85 ? 2410 HOH   B O     1 
HETATM 20741 O  O     . HOH   W 10 .    ? -2.523  41.227  78.108  1.00 35.29 ? 2411 HOH   B O     1 
HETATM 20742 O  O     . HOH   W 10 .    ? 32.394  51.913  69.921  1.00 40.32 ? 2412 HOH   B O     1 
HETATM 20743 O  O     . HOH   W 10 .    ? 6.253   18.907  119.827 1.00 42.72 ? 2413 HOH   B O     1 
HETATM 20744 O  O     . HOH   W 10 .    ? -4.059  63.926  69.822  1.00 44.19 ? 2414 HOH   B O     1 
HETATM 20745 O  O     . HOH   W 10 .    ? 4.801   43.366  51.032  1.00 28.02 ? 2415 HOH   B O     1 
HETATM 20746 O  O     . HOH   W 10 .    ? -1.912  26.168  64.596  1.00 30.87 ? 2416 HOH   B O     1 
HETATM 20747 O  O     . HOH   W 10 .    ? 19.340  60.063  54.358  1.00 42.51 ? 2417 HOH   B O     1 
HETATM 20748 O  O     . HOH   W 10 .    ? 29.907  73.359  72.552  1.00 36.14 ? 2418 HOH   B O     1 
HETATM 20749 O  O     . HOH   W 10 .    ? 3.656   49.359  96.550  1.00 34.12 ? 2419 HOH   B O     1 
HETATM 20750 O  O     . HOH   W 10 .    ? 28.794  64.719  59.811  1.00 37.29 ? 2420 HOH   B O     1 
HETATM 20751 O  O     . HOH   W 10 .    ? 20.859  74.313  81.867  1.00 42.88 ? 2421 HOH   B O     1 
HETATM 20752 O  O     . HOH   W 10 .    ? -2.353  51.725  100.960 1.00 29.14 ? 2422 HOH   B O     1 
HETATM 20753 O  O     . HOH   W 10 .    ? 32.683  20.423  76.194  1.00 36.34 ? 2423 HOH   B O     1 
HETATM 20754 O  O     . HOH   W 10 .    ? -10.391 29.957  76.206  1.00 37.98 ? 2424 HOH   B O     1 
HETATM 20755 O  O     . HOH   W 10 .    ? 24.365  11.903  99.407  1.00 50.47 ? 2425 HOH   B O     1 
HETATM 20756 O  O     . HOH   W 10 .    ? 27.702  50.763  95.737  1.00 37.69 ? 2426 HOH   B O     1 
HETATM 20757 O  O     A HOH   W 10 .    ? 2.479   61.978  83.500  0.61 24.17 ? 2427 HOH   B O     1 
HETATM 20758 O  O     . HOH   W 10 .    ? 7.330   49.804  90.272  1.00 41.28 ? 2428 HOH   B O     1 
HETATM 20759 O  O     . HOH   W 10 .    ? 28.723  69.099  66.024  1.00 41.39 ? 2429 HOH   B O     1 
HETATM 20760 O  O     . HOH   W 10 .    ? 11.987  -2.152  113.296 1.00 47.49 ? 2430 HOH   B O     1 
HETATM 20761 O  O     . HOH   W 10 .    ? 0.270   18.287  71.978  1.00 32.49 ? 2431 HOH   B O     1 
HETATM 20762 O  O     . HOH   W 10 .    ? 0.075   18.966  75.575  1.00 42.42 ? 2432 HOH   B O     1 
HETATM 20763 O  O     . HOH   W 10 .    ? 20.994  68.540  58.536  1.00 42.08 ? 2433 HOH   B O     1 
HETATM 20764 O  O     . HOH   W 10 .    ? 35.178  39.858  104.629 1.00 43.80 ? 2434 HOH   B O     1 
HETATM 20765 O  O     . HOH   W 10 .    ? 6.300   60.468  87.851  1.00 38.78 ? 2435 HOH   B O     1 
HETATM 20766 O  O     . HOH   W 10 .    ? 8.710   17.154  123.138 1.00 39.87 ? 2436 HOH   B O     1 
HETATM 20767 O  O     . HOH   W 10 .    ? 32.990  42.172  66.845  1.00 31.54 ? 2437 HOH   B O     1 
HETATM 20768 O  O     . HOH   W 10 .    ? 10.415  -2.475  92.086  1.00 43.47 ? 2438 HOH   B O     1 
HETATM 20769 O  O     . HOH   W 10 .    ? -22.102 25.809  91.911  1.00 38.73 ? 2439 HOH   B O     1 
HETATM 20770 O  O     . HOH   W 10 .    ? -25.293 22.516  98.303  1.00 35.47 ? 2440 HOH   B O     1 
HETATM 20771 O  O     . HOH   W 10 .    ? 31.036  58.674  60.740  1.00 31.44 ? 2441 HOH   B O     1 
HETATM 20772 O  O     . HOH   W 10 .    ? 5.119   79.863  79.160  1.00 42.95 ? 2442 HOH   B O     1 
HETATM 20773 O  O     . HOH   W 10 .    ? 29.815  14.134  61.988  1.00 44.61 ? 2443 HOH   B O     1 
HETATM 20774 O  O     . HOH   W 10 .    ? -3.332  47.834  87.784  1.00 45.27 ? 2444 HOH   B O     1 
HETATM 20775 O  O     . HOH   W 10 .    ? -2.822  28.159  68.976  1.00 29.27 ? 2445 HOH   B O     1 
HETATM 20776 O  O     . HOH   W 10 .    ? 26.573  68.870  62.038  1.00 39.59 ? 2446 HOH   B O     1 
HETATM 20777 O  O     . HOH   W 10 .    ? 14.135  51.847  63.442  1.00 32.00 ? 2447 HOH   B O     1 
HETATM 20778 O  O     . HOH   W 10 .    ? 21.413  18.192  110.829 1.00 37.49 ? 2448 HOH   B O     1 
HETATM 20779 O  O     . HOH   W 10 .    ? 15.190  3.983   72.669  1.00 44.45 ? 2449 HOH   B O     1 
HETATM 20780 O  O     . HOH   W 10 .    ? -5.783  50.437  134.084 1.00 44.96 ? 2450 HOH   B O     1 
HETATM 20781 O  O     . HOH   W 10 .    ? 32.477  27.477  74.422  1.00 34.21 ? 2451 HOH   B O     1 
HETATM 20782 O  O     . HOH   W 10 .    ? 1.868   43.509  55.741  1.00 32.48 ? 2452 HOH   B O     1 
HETATM 20783 O  O     . HOH   W 10 .    ? -7.316  22.262  78.652  1.00 31.80 ? 2453 HOH   B O     1 
HETATM 20784 O  O     . HOH   W 10 .    ? 32.923  40.654  58.870  1.00 33.70 ? 2454 HOH   B O     1 
HETATM 20785 O  O     . HOH   W 10 .    ? -37.606 15.652  96.088  1.00 52.49 ? 2455 HOH   B O     1 
HETATM 20786 O  O     . HOH   W 10 .    ? 15.042  52.387  51.850  1.00 44.09 ? 2456 HOH   B O     1 
HETATM 20787 O  O     . HOH   W 10 .    ? 28.386  48.496  92.608  1.00 37.86 ? 2457 HOH   B O     1 
HETATM 20788 O  O     . HOH   W 10 .    ? 18.269  6.843   98.166  1.00 37.40 ? 2458 HOH   B O     1 
HETATM 20789 O  O     . HOH   W 10 .    ? 42.496  31.920  99.497  1.00 39.47 ? 2459 HOH   B O     1 
HETATM 20790 O  O     . HOH   W 10 .    ? 6.756   2.465   79.779  1.00 41.36 ? 2460 HOH   B O     1 
HETATM 20791 O  O     . HOH   W 10 .    ? 11.905  17.320  89.577  1.00 36.69 ? 2461 HOH   B O     1 
HETATM 20792 O  O     . HOH   W 10 .    ? 33.118  41.513  54.030  1.00 44.87 ? 2462 HOH   B O     1 
HETATM 20793 O  O     . HOH   W 10 .    ? -0.614  3.649   81.440  1.00 42.04 ? 2463 HOH   B O     1 
HETATM 20794 O  O     . HOH   W 10 .    ? 5.055   77.318  83.138  1.00 42.09 ? 2464 HOH   B O     1 
HETATM 20795 O  O     . HOH   W 10 .    ? 16.754  25.994  109.730 1.00 28.41 ? 2465 HOH   B O     1 
HETATM 20796 O  O     . HOH   W 10 .    ? 39.263  26.410  92.211  1.00 40.73 ? 2466 HOH   B O     1 
HETATM 20797 O  O     . HOH   W 10 .    ? 22.002  77.725  78.147  1.00 42.85 ? 2467 HOH   B O     1 
HETATM 20798 O  O     . HOH   W 10 .    ? 31.977  32.404  75.331  1.00 26.16 ? 2468 HOH   B O     1 
HETATM 20799 O  O     . HOH   W 10 .    ? -32.208 29.421  121.148 1.00 45.76 ? 2469 HOH   B O     1 
HETATM 20800 O  O     . HOH   W 10 .    ? -11.982 30.031  81.394  1.00 40.97 ? 2470 HOH   B O     1 
HETATM 20801 O  O     . HOH   W 10 .    ? 7.713   25.528  103.737 1.00 38.77 ? 2471 HOH   B O     1 
HETATM 20802 O  O     . HOH   W 10 .    ? 4.520   15.656  128.918 1.00 34.28 ? 2472 HOH   B O     1 
HETATM 20803 O  O     . HOH   W 10 .    ? 36.456  41.802  88.790  1.00 40.99 ? 2473 HOH   B O     1 
HETATM 20804 O  O     . HOH   W 10 .    ? -12.811 5.687   83.495  1.00 43.22 ? 2474 HOH   B O     1 
HETATM 20805 O  O     . HOH   W 10 .    ? 1.342   14.325  79.679  1.00 29.57 ? 2475 HOH   B O     1 
HETATM 20806 O  O     . HOH   W 10 .    ? 20.774  58.150  52.937  1.00 43.18 ? 2476 HOH   B O     1 
HETATM 20807 O  O     . HOH   W 10 .    ? 22.648  16.759  107.989 1.00 41.11 ? 2477 HOH   B O     1 
HETATM 20808 O  O     . HOH   W 10 .    ? 11.205  53.202  87.083  1.00 43.08 ? 2478 HOH   B O     1 
HETATM 20809 O  O     . HOH   W 10 .    ? 10.186  53.079  89.190  1.00 39.81 ? 2479 HOH   B O     1 
HETATM 20810 O  O     . HOH   W 10 .    ? 33.261  15.279  64.858  1.00 40.73 ? 2480 HOH   B O     1 
HETATM 20811 O  O     . HOH   W 10 .    ? 0.383   4.487   86.042  1.00 30.04 ? 2481 HOH   B O     1 
HETATM 20812 O  O     . HOH   W 10 .    ? -8.857  41.943  72.152  1.00 39.87 ? 2482 HOH   B O     1 
HETATM 20813 O  O     . HOH   W 10 .    ? 37.207  44.061  90.421  1.00 40.91 ? 2483 HOH   B O     1 
HETATM 20814 O  O     . HOH   W 10 .    ? 12.250  21.066  98.620  1.00 32.71 ? 2484 HOH   B O     1 
HETATM 20815 O  O     . HOH   W 10 .    ? 8.736   -3.532  105.586 1.00 36.68 ? 2485 HOH   B O     1 
HETATM 20816 O  O     . HOH   W 10 .    ? 5.668   10.680  75.160  1.00 31.14 ? 2486 HOH   B O     1 
HETATM 20817 O  O     . HOH   W 10 .    ? 3.906   29.660  94.293  1.00 31.20 ? 2487 HOH   B O     1 
HETATM 20818 O  O     . HOH   W 10 .    ? 6.956   18.702  89.804  1.00 33.42 ? 2488 HOH   B O     1 
HETATM 20819 O  O     . HOH   W 10 .    ? -10.420 -7.101  105.800 1.00 29.11 ? 2489 HOH   B O     1 
HETATM 20820 O  O     . HOH   W 10 .    ? 24.058  32.463  115.388 1.00 36.45 ? 2490 HOH   B O     1 
HETATM 20821 O  O     . HOH   W 10 .    ? 25.112  70.398  65.363  1.00 35.16 ? 2491 HOH   B O     1 
HETATM 20822 O  O     . HOH   W 10 .    ? -16.133 6.491   122.334 1.00 38.36 ? 2492 HOH   B O     1 
HETATM 20823 O  O     . HOH   W 10 .    ? 5.007   16.111  123.044 1.00 32.92 ? 2493 HOH   B O     1 
HETATM 20824 O  O     . HOH   W 10 .    ? 8.633   57.803  95.012  1.00 40.97 ? 2494 HOH   B O     1 
HETATM 20825 O  O     . HOH   W 10 .    ? 6.680   41.701  46.738  1.00 40.98 ? 2495 HOH   B O     1 
HETATM 20826 O  O     B HOH   W 10 .    ? -3.581  59.829  85.132  0.39 24.79 ? 2496 HOH   B O     1 
HETATM 20827 O  O     . HOH   W 10 .    ? 10.997  38.202  130.788 1.00 41.95 ? 2497 HOH   B O     1 
HETATM 20828 O  O     . HOH   W 10 .    ? 30.355  30.788  78.999  1.00 30.48 ? 2498 HOH   B O     1 
HETATM 20829 O  O     . HOH   W 10 .    ? -8.027  37.493  79.332  1.00 38.50 ? 2499 HOH   B O     1 
HETATM 20830 O  O     . HOH   W 10 .    ? 6.871   13.364  69.107  1.00 40.15 ? 2500 HOH   B O     1 
HETATM 20831 O  O     . HOH   W 10 .    ? -2.297  26.020  101.332 1.00 43.48 ? 2501 HOH   B O     1 
HETATM 20832 O  O     . HOH   W 10 .    ? 35.395  12.539  78.480  1.00 41.82 ? 2502 HOH   B O     1 
HETATM 20833 O  O     . HOH   W 10 .    ? -4.058  40.033  60.590  1.00 31.31 ? 2503 HOH   B O     1 
HETATM 20834 O  O     . HOH   W 10 .    ? 33.648  46.990  64.921  1.00 41.49 ? 2504 HOH   B O     1 
HETATM 20835 O  O     . HOH   W 10 .    ? -18.766 13.104  79.945  1.00 44.09 ? 2505 HOH   B O     1 
HETATM 20836 O  O     . HOH   W 10 .    ? 20.409  22.765  109.835 1.00 34.42 ? 2506 HOH   B O     1 
HETATM 20837 O  O     . HOH   W 10 .    ? 12.654  18.065  91.880  1.00 36.07 ? 2507 HOH   B O     1 
HETATM 20838 O  O     . HOH   W 10 .    ? -21.679 25.673  96.808  1.00 41.72 ? 2508 HOH   B O     1 
HETATM 20839 O  O     . HOH   W 10 .    ? 25.939  68.061  59.097  1.00 44.44 ? 2509 HOH   B O     1 
HETATM 20840 O  O     . HOH   W 10 .    ? 13.966  24.950  100.759 1.00 24.18 ? 2510 HOH   B O     1 
HETATM 20841 O  O     . HOH   W 10 .    ? -4.157  68.321  73.823  1.00 43.12 ? 2511 HOH   B O     1 
HETATM 20842 O  O     . HOH   W 10 .    ? -15.307 7.528   124.773 1.00 36.81 ? 2512 HOH   B O     1 
HETATM 20843 O  O     . HOH   W 10 .    ? -17.793 6.832   93.045  1.00 32.73 ? 2513 HOH   B O     1 
HETATM 20844 O  O     . HOH   W 10 .    ? 35.636  29.290  53.948  1.00 44.14 ? 2514 HOH   B O     1 
HETATM 20845 O  O     . HOH   W 10 .    ? -4.748  40.385  98.601  1.00 43.84 ? 2515 HOH   B O     1 
HETATM 20846 O  O     . HOH   W 10 .    ? 17.249  3.400   90.142  1.00 49.33 ? 2516 HOH   B O     1 
HETATM 20847 O  O     . HOH   W 10 .    ? -13.382 4.856   86.032  1.00 39.84 ? 2517 HOH   B O     1 
HETATM 20848 O  O     . HOH   W 10 .    ? -8.109  -2.644  117.545 1.00 32.42 ? 2518 HOH   B O     1 
HETATM 20849 O  O     . HOH   W 10 .    ? 30.841  62.898  58.690  1.00 39.22 ? 2519 HOH   B O     1 
HETATM 20850 O  O     . HOH   W 10 .    ? 5.290   31.680  92.940  1.00 36.58 ? 2520 HOH   B O     1 
HETATM 20851 O  O     . HOH   W 10 .    ? 14.802  21.909  97.620  1.00 25.71 ? 2521 HOH   B O     1 
HETATM 20852 O  O     . HOH   W 10 .    ? 17.892  3.543   73.251  1.00 39.22 ? 2522 HOH   B O     1 
HETATM 20853 O  O     . HOH   W 10 .    ? 1.042   31.472  82.646  1.00 29.23 ? 2523 HOH   B O     1 
HETATM 20854 O  O     . HOH   W 10 .    ? 1.466   11.264  76.820  1.00 34.25 ? 2524 HOH   B O     1 
HETATM 20855 O  O     . HOH   W 10 .    ? -32.939 16.834  88.727  1.00 45.30 ? 2525 HOH   B O     1 
HETATM 20856 O  O     . HOH   W 10 .    ? 23.531  71.391  61.570  1.00 40.24 ? 2526 HOH   B O     1 
HETATM 20857 O  O     . HOH   W 10 .    ? 6.639   23.552  124.752 1.00 36.64 ? 2527 HOH   B O     1 
HETATM 20858 O  O     . HOH   W 10 .    ? -19.406 31.783  88.635  1.00 43.36 ? 2528 HOH   B O     1 
HETATM 20859 O  O     . HOH   W 10 .    ? 0.757   6.729   78.954  1.00 44.82 ? 2529 HOH   B O     1 
HETATM 20860 O  O     . HOH   W 10 .    ? 10.549  0.539   107.159 1.00 35.12 ? 2530 HOH   B O     1 
HETATM 20861 O  O     . HOH   W 10 .    ? 0.944   55.462  70.091  1.00 35.99 ? 2531 HOH   B O     1 
HETATM 20862 O  O     . HOH   W 10 .    ? 11.559  0.478   113.696 1.00 37.02 ? 2532 HOH   B O     1 
HETATM 20863 O  O     . HOH   W 10 .    ? 35.906  22.317  65.006  1.00 39.23 ? 2533 HOH   B O     1 
HETATM 20864 O  O     . HOH   W 10 .    ? 6.401   -10.104 104.841 1.00 40.07 ? 2534 HOH   B O     1 
HETATM 20865 O  O     . HOH   W 10 .    ? 6.180   27.809  87.898  1.00 39.17 ? 2535 HOH   B O     1 
HETATM 20866 O  O     . HOH   W 10 .    ? 6.357   15.722  92.058  1.00 30.87 ? 2536 HOH   B O     1 
HETATM 20867 O  O     . HOH   W 10 .    ? 6.745   60.759  85.209  1.00 28.12 ? 2537 HOH   B O     1 
HETATM 20868 O  O     . HOH   W 10 .    ? 19.988  33.970  115.018 1.00 26.09 ? 2538 HOH   B O     1 
HETATM 20869 O  O     . HOH   W 10 .    ? 13.516  36.317  74.176  1.00 18.11 ? 2539 HOH   B O     1 
HETATM 20870 O  O     . HOH   W 10 .    ? 34.602  26.223  56.877  1.00 26.03 ? 2540 HOH   B O     1 
HETATM 20871 O  O     . HOH   W 10 .    ? 22.919  56.517  53.550  1.00 43.16 ? 2541 HOH   B O     1 
HETATM 20872 O  O     . HOH   W 10 .    ? 14.776  51.041  56.122  1.00 36.94 ? 2542 HOH   B O     1 
HETATM 20873 O  O     . HOH   W 10 .    ? 8.986   47.709  110.759 1.00 42.76 ? 2543 HOH   B O     1 
HETATM 20874 O  O     . HOH   W 10 .    ? 5.019   55.829  66.952  1.00 35.66 ? 2544 HOH   B O     1 
HETATM 20875 O  O     . HOH   W 10 .    ? 11.965  43.671  53.443  1.00 28.70 ? 2545 HOH   B O     1 
HETATM 20876 O  O     . HOH   W 10 .    ? 5.106   3.093   85.846  1.00 31.44 ? 2546 HOH   B O     1 
HETATM 20877 O  O     . HOH   W 10 .    ? 13.101  3.997   94.272  1.00 48.44 ? 2547 HOH   B O     1 
HETATM 20878 O  O     . HOH   W 10 .    ? 18.723  65.821  55.843  1.00 33.91 ? 2548 HOH   B O     1 
HETATM 20879 O  O     . HOH   W 10 .    ? 16.444  76.852  62.056  1.00 43.23 ? 2549 HOH   B O     1 
HETATM 20880 O  O     . HOH   W 10 .    ? 3.114   13.204  77.530  1.00 31.33 ? 2550 HOH   B O     1 
HETATM 20881 O  O     . HOH   W 10 .    ? 6.173   30.411  98.380  1.00 41.94 ? 2551 HOH   B O     1 
HETATM 20882 O  O     . HOH   W 10 .    ? 34.461  27.378  61.305  1.00 28.15 ? 2552 HOH   B O     1 
HETATM 20883 O  O     . HOH   W 10 .    ? 18.885  48.316  56.546  1.00 30.95 ? 2553 HOH   B O     1 
HETATM 20884 O  O     . HOH   W 10 .    ? 14.681  44.176  52.850  1.00 35.62 ? 2554 HOH   B O     1 
HETATM 20885 O  O     . HOH   W 10 .    ? 30.844  61.462  72.696  1.00 26.86 ? 2555 HOH   B O     1 
HETATM 20886 O  O     . HOH   W 10 .    ? -2.004  19.176  78.385  1.00 40.49 ? 2556 HOH   B O     1 
HETATM 20887 O  O     . HOH   W 10 .    ? 2.370   27.408  93.110  1.00 34.82 ? 2557 HOH   B O     1 
HETATM 20888 O  O     . HOH   W 10 .    ? 18.282  81.624  67.985  1.00 41.16 ? 2558 HOH   B O     1 
HETATM 20889 O  O     . HOH   W 10 .    ? -16.426 3.646   123.658 1.00 43.45 ? 2559 HOH   B O     1 
HETATM 20890 O  O     . HOH   W 10 .    ? 5.385   50.101  113.022 1.00 37.48 ? 2560 HOH   B O     1 
HETATM 20891 O  O     . HOH   W 10 .    ? 9.272   3.711   83.724  1.00 29.07 ? 2561 HOH   B O     1 
HETATM 20892 O  O     . HOH   W 10 .    ? -4.909  3.016   83.108  1.00 44.01 ? 2562 HOH   B O     1 
HETATM 20893 O  O     . HOH   W 10 .    ? 2.170   44.428  96.998  1.00 32.09 ? 2563 HOH   B O     1 
HETATM 20894 O  O     . HOH   W 10 .    ? -19.740 3.626   95.871  1.00 44.16 ? 2564 HOH   B O     1 
HETATM 20895 O  O     . HOH   W 10 .    ? 15.718  59.631  92.719  1.00 42.58 ? 2565 HOH   B O     1 
HETATM 20896 O  O     . HOH   W 10 .    ? 21.808  19.602  107.156 1.00 26.41 ? 2566 HOH   B O     1 
HETATM 20897 O  O     . HOH   W 10 .    ? 5.463   81.681  77.675  1.00 43.45 ? 2567 HOH   B O     1 
HETATM 20898 O  O     . HOH   W 10 .    ? 14.895  22.097  95.048  1.00 41.54 ? 2568 HOH   B O     1 
HETATM 20899 O  O     . HOH   W 10 .    ? -15.425 6.516   86.819  1.00 37.93 ? 2569 HOH   B O     1 
HETATM 20900 O  O     . HOH   W 10 .    ? 26.850  24.399  106.428 1.00 43.83 ? 2570 HOH   B O     1 
HETATM 20901 O  O     . HOH   W 10 .    ? 18.606  63.554  55.120  1.00 35.48 ? 2571 HOH   B O     1 
HETATM 20902 O  O     . HOH   W 10 .    ? 13.187  36.675  77.216  1.00 19.84 ? 2572 HOH   B O     1 
HETATM 20903 O  O     . HOH   W 10 .    ? 12.688  55.382  105.481 1.00 33.89 ? 2573 HOH   B O     1 
HETATM 20904 O  O     . HOH   W 10 .    ? 8.942   64.705  66.269  1.00 35.81 ? 2574 HOH   B O     1 
HETATM 20905 O  O     . HOH   W 10 .    ? 25.610  11.079  68.007  1.00 45.41 ? 2575 HOH   B O     1 
HETATM 20906 O  O     . HOH   W 10 .    ? 7.578   27.845  83.725  1.00 41.90 ? 2576 HOH   B O     1 
HETATM 20907 O  O     . HOH   W 10 .    ? -13.561 16.967  78.693  1.00 39.29 ? 2577 HOH   B O     1 
HETATM 20908 O  O     . HOH   W 10 .    ? 7.963   31.126  86.227  1.00 34.16 ? 2578 HOH   B O     1 
HETATM 20909 O  O     . HOH   W 10 .    ? 18.301  9.005   95.700  1.00 33.13 ? 2579 HOH   B O     1 
HETATM 20910 O  O     . HOH   W 10 .    ? 31.719  32.179  80.954  1.00 37.70 ? 2580 HOH   B O     1 
HETATM 20911 O  O     . HOH   W 10 .    ? 11.422  2.289   84.522  1.00 39.00 ? 2581 HOH   B O     1 
HETATM 20912 O  O     . HOH   W 10 .    ? 30.383  23.785  74.382  1.00 25.20 ? 2582 HOH   B O     1 
HETATM 20913 O  O     . HOH   W 10 .    ? 15.661  72.832  58.530  1.00 40.39 ? 2583 HOH   B O     1 
HETATM 20914 O  O     . HOH   W 10 .    ? 9.100   24.388  87.129  1.00 39.21 ? 2584 HOH   B O     1 
HETATM 20915 O  O     . HOH   W 10 .    ? 13.770  39.902  114.022 1.00 41.54 ? 2585 HOH   B O     1 
HETATM 20916 O  O     . HOH   W 10 .    ? -6.029  35.846  61.546  1.00 42.35 ? 2586 HOH   B O     1 
HETATM 20917 O  O     . HOH   W 10 .    ? -19.111 14.628  131.946 1.00 47.77 ? 2587 HOH   B O     1 
HETATM 20918 O  O     . HOH   W 10 .    ? 12.481  7.581   68.082  1.00 40.01 ? 2588 HOH   B O     1 
HETATM 20919 O  O     . HOH   W 10 .    ? 18.890  78.484  65.338  1.00 41.11 ? 2589 HOH   B O     1 
HETATM 20920 O  O     . HOH   W 10 .    ? 14.405  35.159  81.664  1.00 25.23 ? 2590 HOH   B O     1 
HETATM 20921 O  O     . HOH   W 10 .    ? 22.455  81.936  68.948  1.00 44.21 ? 2591 HOH   B O     1 
HETATM 20922 O  O     . HOH   W 10 .    ? -10.960 46.980  77.263  1.00 37.48 ? 2592 HOH   B O     1 
HETATM 20923 O  O     . HOH   W 10 .    ? 5.646   30.074  86.504  1.00 37.73 ? 2593 HOH   B O     1 
HETATM 20924 O  O     . HOH   W 10 .    ? 20.088  10.739  96.454  1.00 39.76 ? 2594 HOH   B O     1 
HETATM 20925 O  O     . HOH   W 10 .    ? 2.848   9.966   74.896  1.00 38.95 ? 2595 HOH   B O     1 
HETATM 20926 O  O     . HOH   W 10 .    ? -8.449  33.484  85.248  1.00 31.10 ? 2596 HOH   B O     1 
HETATM 20927 O  O     . HOH   W 10 .    ? 30.315  64.020  71.021  1.00 36.89 ? 2597 HOH   B O     1 
HETATM 20928 O  O     . HOH   W 10 .    ? -4.104  23.119  72.410  1.00 42.61 ? 2598 HOH   B O     1 
HETATM 20929 O  O     . HOH   W 10 .    ? -7.172  24.888  75.014  1.00 33.94 ? 2599 HOH   B O     1 
HETATM 20930 O  O     . HOH   W 10 .    ? 26.408  52.167  83.925  1.00 33.14 ? 2600 HOH   B O     1 
HETATM 20931 O  O     . HOH   W 10 .    ? 31.745  69.366  80.332  1.00 33.66 ? 2601 HOH   B O     1 
HETATM 20932 O  O     . HOH   W 10 .    ? 10.422  59.524  86.269  1.00 41.21 ? 2602 HOH   B O     1 
HETATM 20933 O  O     . HOH   W 10 .    ? 13.704  24.476  98.189  1.00 29.56 ? 2603 HOH   B O     1 
HETATM 20934 O  O     . HOH   W 10 .    ? 10.726  45.107  130.236 1.00 45.27 ? 2604 HOH   B O     1 
HETATM 20935 O  O     . HOH   W 10 .    ? -7.576  46.913  133.261 1.00 41.95 ? 2605 HOH   B O     1 
HETATM 20936 O  O     . HOH   W 10 .    ? 12.106  50.407  54.531  1.00 42.62 ? 2606 HOH   B O     1 
HETATM 20937 O  O     . HOH   W 10 .    ? -9.212  -0.467  86.525  1.00 42.97 ? 2607 HOH   B O     1 
HETATM 20938 O  O     . HOH   W 10 .    ? -22.556 24.382  82.380  1.00 42.42 ? 2608 HOH   B O     1 
HETATM 20939 O  O     . HOH   W 10 .    ? 6.106   12.024  73.018  1.00 32.85 ? 2609 HOH   B O     1 
HETATM 20940 O  O     . HOH   W 10 .    ? 40.935  31.523  84.229  1.00 42.27 ? 2610 HOH   B O     1 
HETATM 20941 O  O     . HOH   W 10 .    ? 0.092   28.271  99.283  1.00 41.02 ? 2611 HOH   B O     1 
HETATM 20942 O  O     . HOH   W 10 .    ? 32.575  59.770  62.790  1.00 31.92 ? 2612 HOH   B O     1 
HETATM 20943 O  O     . HOH   W 10 .    ? 8.809   44.353  50.338  1.00 37.19 ? 2613 HOH   B O     1 
HETATM 20944 O  O     . HOH   W 10 .    ? -5.660  38.203  61.656  1.00 35.08 ? 2614 HOH   B O     1 
HETATM 20945 O  O     . HOH   W 10 .    ? -7.663  36.737  83.838  1.00 38.84 ? 2615 HOH   B O     1 
HETATM 20946 O  O     . HOH   W 10 .    ? 5.747   4.945   75.991  1.00 48.64 ? 2616 HOH   B O     1 
HETATM 20947 O  O     . HOH   W 10 .    ? -11.584 1.716   89.042  1.00 35.73 ? 2617 HOH   B O     1 
HETATM 20948 O  O     . HOH   W 10 .    ? 13.065  74.732  60.838  1.00 37.51 ? 2618 HOH   B O     1 
HETATM 20949 O  O     . HOH   W 10 .    ? 12.512  0.253   109.084 1.00 34.70 ? 2619 HOH   B O     1 
HETATM 20950 O  O     . HOH   W 10 .    ? -19.366 0.518   97.522  1.00 42.68 ? 2620 HOH   B O     1 
HETATM 20951 O  O     . HOH   W 10 .    ? 18.536  2.791   77.698  1.00 39.64 ? 2621 HOH   B O     1 
HETATM 20952 O  O     . HOH   W 10 .    ? 15.176  55.724  104.398 1.00 30.79 ? 2622 HOH   B O     1 
HETATM 20953 O  O     . HOH   W 10 .    ? -16.263 7.694   90.898  1.00 29.66 ? 2623 HOH   B O     1 
HETATM 20954 O  O     . HOH   W 10 .    ? -25.309 12.841  86.664  1.00 33.95 ? 2624 HOH   B O     1 
HETATM 20955 O  O     . HOH   W 10 .    ? 14.783  6.760   91.954  1.00 39.15 ? 2625 HOH   B O     1 
HETATM 20956 O  O     . HOH   W 10 .    ? -0.670  80.049  77.300  1.00 44.59 ? 2626 HOH   B O     1 
HETATM 20957 O  O     . HOH   W 10 .    ? 9.392   16.905  89.874  1.00 31.28 ? 2627 HOH   B O     1 
HETATM 20958 O  O     . HOH   W 10 .    ? -8.999  3.485   84.835  1.00 36.99 ? 2628 HOH   B O     1 
HETATM 20959 O  O     . HOH   W 10 .    ? 24.189  76.387  78.596  1.00 46.73 ? 2629 HOH   B O     1 
HETATM 20960 O  O     . HOH   W 10 .    ? 22.633  50.167  68.741  1.00 26.30 ? 2630 HOH   B O     1 
HETATM 20961 O  O     . HOH   W 10 .    ? 15.060  4.285   70.007  1.00 39.75 ? 2631 HOH   B O     1 
HETATM 20962 O  O     . HOH   W 10 .    ? 4.816   63.958  86.661  1.00 37.98 ? 2632 HOH   B O     1 
HETATM 20963 O  O     . HOH   W 10 .    ? 27.522  54.756  83.454  1.00 38.59 ? 2633 HOH   B O     1 
HETATM 20964 O  O     . HOH   W 10 .    ? 3.720   47.653  89.368  1.00 35.32 ? 2634 HOH   B O     1 
HETATM 20965 O  O     . HOH   W 10 .    ? 11.834  1.285   116.046 1.00 34.70 ? 2635 HOH   B O     1 
HETATM 20966 O  O     . HOH   W 10 .    ? 12.781  59.217  85.776  1.00 37.05 ? 2636 HOH   B O     1 
HETATM 20967 O  O     . HOH   W 10 .    ? -4.538  29.677  59.734  1.00 43.28 ? 2637 HOH   B O     1 
HETATM 20968 O  O     . HOH   W 10 .    ? 33.567  6.967   76.877  1.00 46.65 ? 2638 HOH   B O     1 
HETATM 20969 O  O     . HOH   W 10 .    ? -21.128 16.376  80.081  1.00 36.70 ? 2639 HOH   B O     1 
HETATM 20970 O  O     . HOH   W 10 .    ? 0.556   19.860  64.580  1.00 36.49 ? 2640 HOH   B O     1 
HETATM 20971 O  O     . HOH   W 10 .    ? -4.994  -0.808  84.292  1.00 41.60 ? 2641 HOH   B O     1 
HETATM 20972 O  O     . HOH   W 10 .    ? -23.484 14.178  82.299  1.00 31.34 ? 2642 HOH   B O     1 
HETATM 20973 O  O     . HOH   W 10 .    ? -0.007  28.718  96.623  1.00 23.98 ? 2643 HOH   B O     1 
HETATM 20974 O  O     . HOH   W 10 .    ? 6.344   -5.041  101.915 1.00 38.00 ? 2644 HOH   B O     1 
HETATM 20975 O  O     . HOH   W 10 .    ? -11.126 3.692   86.844  1.00 32.11 ? 2645 HOH   B O     1 
HETATM 20976 O  O     . HOH   W 10 .    ? -7.164  -5.307  91.554  1.00 39.56 ? 2646 HOH   B O     1 
HETATM 20977 O  O     . HOH   W 10 .    ? 13.871  44.359  49.535  1.00 40.12 ? 2647 HOH   B O     1 
HETATM 20978 O  O     . HOH   W 10 .    ? -3.027  37.799  77.989  1.00 30.74 ? 2648 HOH   B O     1 
HETATM 20979 O  O     . HOH   W 10 .    ? 2.105   21.766  61.154  1.00 31.57 ? 2649 HOH   B O     1 
HETATM 20980 O  O     . HOH   W 10 .    ? 35.024  38.622  64.569  1.00 37.96 ? 2650 HOH   B O     1 
HETATM 20981 O  O     . HOH   W 10 .    ? -1.307  23.201  63.950  1.00 31.82 ? 2651 HOH   B O     1 
HETATM 20982 O  O     . HOH   W 10 .    ? 33.570  19.299  54.041  1.00 35.06 ? 2652 HOH   B O     1 
HETATM 20983 O  O     . HOH   W 10 .    ? -13.793 22.528  81.636  1.00 37.65 ? 2653 HOH   B O     1 
HETATM 20984 O  O     . HOH   W 10 .    ? 3.195   14.914  75.528  1.00 31.74 ? 2654 HOH   B O     1 
HETATM 20985 O  O     . HOH   W 10 .    ? 1.740   44.099  78.644  1.00 29.44 ? 2655 HOH   B O     1 
HETATM 20986 O  O     . HOH   W 10 .    ? -12.826 -0.703  121.445 1.00 45.56 ? 2656 HOH   B O     1 
HETATM 20987 O  O     . HOH   W 10 .    ? 2.208   31.676  85.056  1.00 25.02 ? 2657 HOH   B O     1 
HETATM 20988 O  O     . HOH   W 10 .    ? -11.669 -2.674  93.625  1.00 43.70 ? 2658 HOH   B O     1 
HETATM 20989 O  O     . HOH   W 10 .    ? 9.415   9.988   67.884  1.00 37.10 ? 2659 HOH   B O     1 
HETATM 20990 O  O     . HOH   W 10 .    ? -4.900  11.143  80.772  1.00 47.12 ? 2660 HOH   B O     1 
HETATM 20991 O  O     . HOH   W 10 .    ? -6.534  17.626  77.845  1.00 40.37 ? 2661 HOH   B O     1 
HETATM 20992 O  O     . HOH   W 10 .    ? 36.247  28.145  56.249  1.00 41.17 ? 2662 HOH   B O     1 
HETATM 20993 O  O     . HOH   W 10 .    ? 28.626  50.888  84.095  1.00 40.69 ? 2663 HOH   B O     1 
HETATM 20994 O  O     . HOH   W 10 .    ? 31.618  64.469  62.563  1.00 43.31 ? 2664 HOH   B O     1 
HETATM 20995 O  O     . HOH   W 10 .    ? -8.424  35.157  87.564  1.00 42.04 ? 2665 HOH   B O     1 
HETATM 20996 O  O     . HOH   W 10 .    ? 2.116   17.034  65.954  1.00 39.82 ? 2666 HOH   B O     1 
HETATM 20997 O  O     . HOH   W 10 .    ? -12.622 52.609  126.301 1.00 46.11 ? 2667 HOH   B O     1 
HETATM 20998 O  O     . HOH   W 10 .    ? -4.857  23.472  75.138  1.00 30.54 ? 2668 HOH   B O     1 
HETATM 20999 O  O     . HOH   W 10 .    ? 41.339  27.736  91.176  1.00 40.54 ? 2669 HOH   B O     1 
HETATM 21000 O  O     . HOH   W 10 .    ? 32.544  25.051  50.856  1.00 46.08 ? 2670 HOH   B O     1 
HETATM 21001 O  O     . HOH   W 10 .    ? -26.328 24.284  97.168  1.00 39.40 ? 2671 HOH   B O     1 
HETATM 21002 O  O     . HOH   W 10 .    ? 22.164  31.167  45.353  1.00 35.40 ? 2672 HOH   B O     1 
HETATM 21003 O  O     . HOH   W 10 .    ? 14.844  1.321   90.642  1.00 48.37 ? 2673 HOH   B O     1 
HETATM 21004 O  O     . HOH   W 10 .    ? 5.952   1.309   82.136  1.00 44.19 ? 2674 HOH   B O     1 
HETATM 21005 O  O     . HOH   W 10 .    ? 11.288  59.980  92.561  1.00 35.86 ? 2675 HOH   B O     1 
HETATM 21006 O  O     . HOH   W 10 .    ? -2.524  23.312  61.508  1.00 38.30 ? 2676 HOH   B O     1 
HETATM 21007 O  O     . HOH   W 10 .    ? 22.741  29.006  44.010  1.00 40.79 ? 2677 HOH   B O     1 
HETATM 21008 O  O     . HOH   W 10 .    ? 19.240  31.516  45.491  1.00 40.38 ? 2678 HOH   B O     1 
HETATM 21009 O  O     . HOH   W 10 .    ? 32.979  22.842  75.131  1.00 40.99 ? 2679 HOH   B O     1 
HETATM 21010 O  O     . HOH   W 10 .    ? -24.863 12.782  83.982  1.00 34.28 ? 2680 HOH   B O     1 
HETATM 21011 O  O     . HOH   W 10 .    ? 7.077   1.931   84.434  1.00 35.56 ? 2681 HOH   B O     1 
HETATM 21012 O  O     . HOH   W 10 .    ? 32.731  62.513  61.783  1.00 43.08 ? 2682 HOH   B O     1 
HETATM 21013 O  O     . HOH   W 10 .    ? -16.077 5.616   88.991  1.00 36.92 ? 2683 HOH   B O     1 
HETATM 21014 O  O     . HOH   W 10 .    ? 18.087  1.573   75.280  1.00 46.79 ? 2684 HOH   B O     1 
HETATM 21015 O  O     . HOH   W 10 .    ? 10.505  -1.911  103.762 1.00 43.23 ? 2685 HOH   B O     1 
HETATM 21016 O  O     . HOH   W 10 .    ? -24.966 25.880  95.266  1.00 47.95 ? 2686 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   ? 0.6133 0.6444 0.6891 0.0874  -0.0206 -0.1262 14   ALA A N   
2     C CA  . ALA A 16   ? 0.6185 0.6484 0.6850 0.0841  -0.0180 -0.1198 14   ALA A CA  
3     C C   . ALA A 16   ? 0.5776 0.6146 0.6352 0.0829  -0.0128 -0.1136 14   ALA A C   
4     O O   . ALA A 16   ? 0.5256 0.5746 0.5813 0.0858  -0.0105 -0.1171 14   ALA A O   
5     C CB  . ALA A 16   ? 0.6219 0.6572 0.6866 0.0860  -0.0189 -0.1257 14   ALA A CB  
6     N N   . PRO A 17   ? 0.5649 0.5950 0.6175 0.0786  -0.0110 -0.1045 15   PRO A N   
7     C CA  . PRO A 17   ? 0.4255 0.4614 0.4706 0.0772  -0.0063 -0.0982 15   PRO A CA  
8     C C   . PRO A 17   ? 0.4522 0.4988 0.4898 0.0782  -0.0035 -0.0990 15   PRO A C   
9     O O   . PRO A 17   ? 0.4327 0.4784 0.4683 0.0780  -0.0045 -0.1006 15   PRO A O   
10    C CB  . PRO A 17   ? 0.4564 0.4814 0.4989 0.0724  -0.0060 -0.0892 15   PRO A CB  
11    C CG  . PRO A 17   ? 0.5403 0.5566 0.5856 0.0713  -0.0095 -0.0907 15   PRO A CG  
12    C CD  . PRO A 17   ? 0.4837 0.5009 0.5377 0.0749  -0.0132 -0.0995 15   PRO A CD  
13    N N   . ALA A 18   ? 0.4068 0.4640 0.4406 0.0793  0.0000  -0.0978 16   ALA A N   
14    C CA  . ALA A 18   ? 0.3599 0.4287 0.3868 0.0804  0.0028  -0.0981 16   ALA A CA  
15    C C   . ALA A 18   ? 0.3356 0.3994 0.3557 0.0766  0.0044  -0.0905 16   ALA A C   
16    O O   . ALA A 18   ? 0.3554 0.4108 0.3746 0.0731  0.0051  -0.0834 16   ALA A O   
17    C CB  . ALA A 18   ? 0.4245 0.5053 0.4490 0.0819  0.0064  -0.0969 16   ALA A CB  
18    N N   . PRO A 19   ? 0.3087 0.3776 0.3244 0.0772  0.0048  -0.0919 17   PRO A N   
19    C CA  . PRO A 19   ? 0.3132 0.3772 0.3229 0.0737  0.0061  -0.0850 17   PRO A CA  
20    C C   . PRO A 19   ? 0.3053 0.3720 0.3102 0.0713  0.0099  -0.0766 17   PRO A C   
21    O O   . PRO A 19   ? 0.3577 0.4357 0.3604 0.0729  0.0125  -0.0764 17   PRO A O   
22    C CB  . PRO A 19   ? 0.3654 0.4380 0.3715 0.0757  0.0061  -0.0891 17   PRO A CB  
23    C CG  . PRO A 19   ? 0.4156 0.4929 0.4274 0.0798  0.0034  -0.0992 17   PRO A CG  
24    C CD  . PRO A 19   ? 0.3420 0.4213 0.3582 0.0812  0.0039  -0.1004 17   PRO A CD  
25    N N   . PHE A 20   ? 0.2962 0.3524 0.2998 0.0675  0.0100  -0.0698 18   PHE A N   
26    C CA  . PHE A 20   ? 0.3010 0.3575 0.3004 0.0647  0.0131  -0.0615 18   PHE A CA  
27    C C   . PHE A 20   ? 0.2933 0.3526 0.2952 0.0650  0.0146  -0.0599 18   PHE A C   
28    O O   . PHE A 20   ? 0.3049 0.3667 0.3038 0.0632  0.0173  -0.0536 18   PHE A O   
29    C CB  . PHE A 20   ? 0.2891 0.3551 0.2822 0.0648  0.0157  -0.0587 18   PHE A CB  
30    C CG  . PHE A 20   ? 0.3156 0.3790 0.3060 0.0643  0.0144  -0.0597 18   PHE A CG  
31    C CD1 . PHE A 20   ? 0.2921 0.3452 0.2810 0.0610  0.0139  -0.0547 18   PHE A CD1 
32    C CD2 . PHE A 20   ? 0.3174 0.3892 0.3069 0.0673  0.0137  -0.0659 18   PHE A CD2 
33    C CE1 . PHE A 20   ? 0.2872 0.3381 0.2738 0.0605  0.0127  -0.0556 18   PHE A CE1 
34    C CE2 . PHE A 20   ? 0.3262 0.3957 0.3134 0.0669  0.0124  -0.0669 18   PHE A CE2 
35    C CZ  . PHE A 20   ? 0.3246 0.3836 0.3103 0.0634  0.0120  -0.0616 18   PHE A CZ  
36    N N   . ALA A 21   ? 0.3399 0.3987 0.3475 0.0673  0.0127  -0.0655 19   ALA A N   
37    C CA  . ALA A 21   ? 0.3453 0.4067 0.3557 0.0677  0.0139  -0.0642 19   ALA A CA  
38    C C   . ALA A 21   ? 0.3484 0.3994 0.3594 0.0640  0.0141  -0.0574 19   ALA A C   
39    O O   . ALA A 21   ? 0.3597 0.4133 0.3716 0.0635  0.0158  -0.0544 19   ALA A O   
40    C CB  . ALA A 21   ? 0.3963 0.4593 0.4133 0.0711  0.0115  -0.0722 19   ALA A CB  
41    N N   . ASP A 22   ? 0.3204 0.3605 0.3312 0.0615  0.0123  -0.0551 20   ASP A N   
42    C CA  . ASP A 22   ? 0.3679 0.3985 0.3790 0.0580  0.0123  -0.0489 20   ASP A CA  
43    C C   . ASP A 22   ? 0.3080 0.3341 0.3141 0.0550  0.0130  -0.0438 20   ASP A C   
44    O O   . ASP A 22   ? 0.3039 0.3203 0.3107 0.0524  0.0116  -0.0409 20   ASP A O   
45    C CB  . ASP A 22   ? 0.3815 0.4025 0.3985 0.0577  0.0088  -0.0512 20   ASP A CB  
46    C CG  . ASP A 22   ? 0.5657 0.5901 0.5885 0.0605  0.0078  -0.0559 20   ASP A CG  
47    O OD1 . ASP A 22   ? 0.6141 0.6471 0.6361 0.0618  0.0102  -0.0557 20   ASP A OD1 
48    O OD2 . ASP A 22   ? 0.7325 0.7511 0.7610 0.0613  0.0046  -0.0596 20   ASP A OD2 
49    N N   . PHE A 23   ? 0.2581 0.2917 0.2594 0.0553  0.0152  -0.0424 21   PHE A N   
50    C CA  . PHE A 23   ? 0.2486 0.2783 0.2457 0.0531  0.0155  -0.0387 21   PHE A CA  
51    C C   . PHE A 23   ? 0.2799 0.3027 0.2758 0.0495  0.0165  -0.0317 21   PHE A C   
52    O O   . PHE A 23   ? 0.2523 0.2663 0.2481 0.0473  0.0151  -0.0300 21   PHE A O   
53    C CB  . PHE A 23   ? 0.2672 0.3070 0.2596 0.0542  0.0176  -0.0384 21   PHE A CB  
54    C CG  . PHE A 23   ? 0.2320 0.2682 0.2202 0.0519  0.0181  -0.0340 21   PHE A CG  
55    C CD1 . PHE A 23   ? 0.2652 0.2944 0.2534 0.0512  0.0158  -0.0360 21   PHE A CD1 
56    C CD2 . PHE A 23   ? 0.2745 0.3142 0.2595 0.0502  0.0206  -0.0278 21   PHE A CD2 
57    C CE1 . PHE A 23   ? 0.2663 0.2924 0.2509 0.0491  0.0162  -0.0321 21   PHE A CE1 
58    C CE2 . PHE A 23   ? 0.2991 0.3353 0.2809 0.0481  0.0209  -0.0239 21   PHE A CE2 
59    C CZ  . PHE A 23   ? 0.2584 0.2879 0.2398 0.0476  0.0187  -0.0262 21   PHE A CZ  
60    N N   . ALA A 24   ? 0.2692 0.2964 0.2645 0.0489  0.0188  -0.0277 22   ALA A N   
61    C CA  . ALA A 24   ? 0.2729 0.2944 0.2674 0.0456  0.0197  -0.0214 22   ALA A CA  
62    C C   . ALA A 24   ? 0.2451 0.2705 0.2413 0.0454  0.0215  -0.0186 22   ALA A C   
63    O O   . ALA A 24   ? 0.2479 0.2764 0.2423 0.0439  0.0236  -0.0135 22   ALA A O   
64    C CB  . ALA A 24   ? 0.2940 0.3162 0.2841 0.0440  0.0210  -0.0173 22   ALA A CB  
65    N N   . PRO A 25   ? 0.2830 0.3083 0.2832 0.0467  0.0206  -0.0215 23   PRO A N   
66    C CA  . PRO A 25   ? 0.2657 0.2952 0.2678 0.0465  0.0223  -0.0190 23   PRO A CA  
67    C C   . PRO A 25   ? 0.2875 0.3102 0.2896 0.0431  0.0227  -0.0131 23   PRO A C   
68    O O   . PRO A 25   ? 0.2701 0.2836 0.2728 0.0414  0.0209  -0.0126 23   PRO A O   
69    C CB  . PRO A 25   ? 0.3096 0.3381 0.3164 0.0485  0.0205  -0.0239 23   PRO A CB  
70    C CG  . PRO A 25   ? 0.3184 0.3378 0.3265 0.0481  0.0176  -0.0265 23   PRO A CG  
71    C CD  . PRO A 25   ? 0.3038 0.3240 0.3076 0.0480  0.0177  -0.0268 23   PRO A CD  
72    N N   . PRO A 26   ? 0.2613 0.2888 0.2629 0.0421  0.0249  -0.0085 24   PRO A N   
73    C CA  . PRO A 26   ? 0.2570 0.2785 0.2592 0.0390  0.0252  -0.0033 24   PRO A CA  
74    C C   . PRO A 26   ? 0.2588 0.2745 0.2648 0.0385  0.0237  -0.0042 24   PRO A C   
75    O O   . PRO A 26   ? 0.2894 0.3077 0.2982 0.0405  0.0231  -0.0079 24   PRO A O   
76    C CB  . PRO A 26   ? 0.3061 0.3355 0.3081 0.0385  0.0278  0.0011  24   PRO A CB  
77    C CG  . PRO A 26   ? 0.3757 0.4153 0.3782 0.0416  0.0288  -0.0023 24   PRO A CG  
78    C CD  . PRO A 26   ? 0.2948 0.3340 0.2958 0.0438  0.0273  -0.0080 24   PRO A CD  
79    N N   . VAL A 27   ? 0.2567 0.2650 0.2630 0.0357  0.0230  -0.0009 25   VAL A N   
80    C CA  . VAL A 27   ? 0.2894 0.2924 0.2990 0.0348  0.0217  -0.0008 25   VAL A CA  
81    C C   . VAL A 27   ? 0.2695 0.2784 0.2821 0.0357  0.0229  -0.0003 25   VAL A C   
82    O O   . VAL A 27   ? 0.2926 0.3005 0.3086 0.0367  0.0217  -0.0028 25   VAL A O   
83    C CB  . VAL A 27   ? 0.2861 0.2821 0.2952 0.0316  0.0212  0.0031  25   VAL A CB  
84    C CG1 . VAL A 27   ? 0.2946 0.2870 0.3071 0.0306  0.0202  0.0038  25   VAL A CG1 
85    C CG2 . VAL A 27   ? 0.2870 0.2769 0.2937 0.0308  0.0196  0.0020  25   VAL A CG2 
86    N N   . ARG A 28   ? 0.2950 0.3103 0.3070 0.0353  0.0252  0.0030  26   ARG A N   
87    C CA  . ARG A 28   ? 0.3207 0.3426 0.3356 0.0359  0.0267  0.0042  26   ARG A CA  
88    C C   . ARG A 28   ? 0.3572 0.3890 0.3703 0.0368  0.0291  0.0061  26   ARG A C   
89    O O   . ARG A 28   ? 0.3170 0.3491 0.3269 0.0361  0.0297  0.0078  26   ARG A O   
90    C CB  . ARG A 28   ? 0.3453 0.3630 0.3624 0.0332  0.0267  0.0085  26   ARG A CB  
91    C CG  . ARG A 28   ? 0.3477 0.3650 0.3634 0.0308  0.0278  0.0135  26   ARG A CG  
92    C CD  . ARG A 28   ? 0.3829 0.3951 0.4013 0.0282  0.0273  0.0168  26   ARG A CD  
93    N NE  . ARG A 28   ? 0.3892 0.3922 0.4071 0.0270  0.0251  0.0153  26   ARG A NE  
94    C CZ  . ARG A 28   ? 0.4725 0.4720 0.4925 0.0272  0.0235  0.0132  26   ARG A CZ  
95    N NH1 . ARG A 28   ? 0.4526 0.4560 0.4756 0.0285  0.0238  0.0122  26   ARG A NH1 
96    N NH2 . ARG A 28   ? 0.4041 0.3961 0.4233 0.0261  0.0215  0.0122  26   ARG A NH2 
97    N N   . PRO A 29   ? 0.3176 0.3581 0.3327 0.0382  0.0306  0.0060  27   PRO A N   
98    C CA  . PRO A 29   ? 0.3218 0.3726 0.3354 0.0386  0.0331  0.0088  27   PRO A CA  
99    C C   . PRO A 29   ? 0.2917 0.3403 0.3053 0.0355  0.0339  0.0154  27   PRO A C   
100   O O   . PRO A 29   ? 0.3390 0.3819 0.3552 0.0334  0.0333  0.0179  27   PRO A O   
101   C CB  . PRO A 29   ? 0.3168 0.3763 0.3335 0.0404  0.0344  0.0078  27   PRO A CB  
102   C CG  . PRO A 29   ? 0.3593 0.4140 0.3784 0.0420  0.0323  0.0024  27   PRO A CG  
103   C CD  . PRO A 29   ? 0.3400 0.3821 0.3591 0.0396  0.0302  0.0033  27   PRO A CD  
104   N N   . GLN A 30   ? 0.3090 0.3623 0.3199 0.0352  0.0352  0.0181  28   GLN A N   
105   C CA  . GLN A 30   ? 0.3161 0.3666 0.3273 0.0323  0.0356  0.0241  28   GLN A CA  
106   C C   . GLN A 30   ? 0.3029 0.3606 0.3175 0.0313  0.0374  0.0292  28   GLN A C   
107   O O   . GLN A 30   ? 0.3283 0.3971 0.3425 0.0326  0.0392  0.0303  28   GLN A O   
108   C CB  . GLN A 30   ? 0.2971 0.3495 0.3044 0.0325  0.0359  0.0251  28   GLN A CB  
109   C CG  . GLN A 30   ? 0.2591 0.3049 0.2633 0.0336  0.0341  0.0201  28   GLN A CG  
110   C CD  . GLN A 30   ? 0.2989 0.3328 0.3038 0.0314  0.0323  0.0203  28   GLN A CD  
111   O OE1 . GLN A 30   ? 0.2691 0.2993 0.2736 0.0294  0.0321  0.0239  28   GLN A OE1 
112   N NE2 . GLN A 30   ? 0.2735 0.3016 0.2797 0.0318  0.0307  0.0166  28   GLN A NE2 
113   N N   . SER A 31   ? 0.2646 0.3166 0.2828 0.0289  0.0368  0.0323  29   SER A N   
114   C CA  . SER A 31   ? 0.2509 0.3087 0.2731 0.0275  0.0382  0.0374  29   SER A CA  
115   C C   . SER A 31   ? 0.2910 0.3536 0.3131 0.0261  0.0393  0.0433  29   SER A C   
116   O O   . SER A 31   ? 0.2698 0.3295 0.2888 0.0259  0.0388  0.0435  29   SER A O   
117   C CB  . SER A 31   ? 0.2699 0.3195 0.2962 0.0251  0.0369  0.0390  29   SER A CB  
118   O OG  . SER A 31   ? 0.2498 0.2913 0.2757 0.0230  0.0356  0.0411  29   SER A OG  
119   N N   . THR A 32   ? 0.2587 0.3287 0.2845 0.0250  0.0408  0.0485  30   THR A N   
120   C CA  . THR A 32   ? 0.2603 0.3344 0.2872 0.0232  0.0416  0.0551  30   THR A CA  
121   C C   . THR A 32   ? 0.2459 0.3092 0.2738 0.0209  0.0398  0.0570  30   THR A C   
122   O O   . THR A 32   ? 0.2614 0.3248 0.2875 0.0204  0.0398  0.0594  30   THR A O   
123   C CB  . THR A 32   ? 0.2718 0.3538 0.3039 0.0218  0.0430  0.0607  30   THR A CB  
124   O OG1 . THR A 32   ? 0.3443 0.4375 0.3753 0.0242  0.0448  0.0587  30   THR A OG1 
125   C CG2 . THR A 32   ? 0.2981 0.3843 0.3321 0.0198  0.0436  0.0682  30   THR A CG2 
126   N N   . LEU A 33   ? 0.2469 0.3009 0.2775 0.0195  0.0383  0.0557  31   LEU A N   
127   C CA  . LEU A 33   ? 0.2365 0.2808 0.2685 0.0174  0.0365  0.0570  31   LEU A CA  
128   C C   . LEU A 33   ? 0.2421 0.2807 0.2688 0.0185  0.0355  0.0527  31   LEU A C   
129   O O   . LEU A 33   ? 0.2381 0.2730 0.2644 0.0174  0.0348  0.0547  31   LEU A O   
130   C CB  . LEU A 33   ? 0.2736 0.3104 0.3095 0.0159  0.0351  0.0560  31   LEU A CB  
131   C CG  . LEU A 33   ? 0.2780 0.3192 0.3204 0.0140  0.0357  0.0614  31   LEU A CG  
132   C CD1 . LEU A 33   ? 0.3009 0.3366 0.3469 0.0130  0.0345  0.0596  31   LEU A CD1 
133   C CD2 . LEU A 33   ? 0.3374 0.3774 0.3833 0.0118  0.0352  0.0671  31   LEU A CD2 
134   N N   . ARG A 34   ? 0.2297 0.2673 0.2527 0.0206  0.0353  0.0470  32   ARG A N   
135   C CA  . ARG A 34   ? 0.2277 0.2602 0.2460 0.0216  0.0343  0.0431  32   ARG A CA  
136   C C   . ARG A 34   ? 0.2413 0.2803 0.2564 0.0226  0.0353  0.0447  32   ARG A C   
137   O O   . ARG A 34   ? 0.2580 0.2928 0.2708 0.0223  0.0345  0.0445  32   ARG A O   
138   C CB  . ARG A 34   ? 0.2663 0.2968 0.2822 0.0237  0.0336  0.0369  32   ARG A CB  
139   C CG  . ARG A 34   ? 0.2679 0.2903 0.2860 0.0226  0.0320  0.0349  32   ARG A CG  
140   C CD  . ARG A 34   ? 0.2354 0.2483 0.2524 0.0211  0.0303  0.0342  32   ARG A CD  
141   N NE  . ARG A 34   ? 0.2484 0.2589 0.2609 0.0226  0.0295  0.0303  32   ARG A NE  
142   C CZ  . ARG A 34   ? 0.3071 0.3134 0.3184 0.0235  0.0283  0.0258  32   ARG A CZ  
143   N NH1 . ARG A 34   ? 0.2893 0.2935 0.3031 0.0233  0.0275  0.0246  32   ARG A NH1 
144   N NH2 . ARG A 34   ? 0.3044 0.3087 0.3121 0.0246  0.0275  0.0227  32   ARG A NH2 
145   N N   . ARG A 35   ? 0.2367 0.2867 0.2517 0.0239  0.0372  0.0462  33   ARG A N   
146   C CA  . ARG A 35   ? 0.2361 0.2935 0.2479 0.0249  0.0382  0.0478  33   ARG A CA  
147   C C   . ARG A 35   ? 0.2319 0.2886 0.2457 0.0226  0.0381  0.0542  33   ARG A C   
148   O O   . ARG A 35   ? 0.2597 0.3175 0.2706 0.0230  0.0381  0.0549  33   ARG A O   
149   C CB  . ARG A 35   ? 0.2801 0.3505 0.2913 0.0268  0.0403  0.0480  33   ARG A CB  
150   C CG  . ARG A 35   ? 0.2770 0.3486 0.2859 0.0296  0.0401  0.0408  33   ARG A CG  
151   C CD  . ARG A 35   ? 0.3666 0.4517 0.3755 0.0316  0.0421  0.0406  33   ARG A CD  
152   N NE  . ARG A 35   ? 0.4952 0.5808 0.5028 0.0344  0.0417  0.0333  33   ARG A NE  
153   C CZ  . ARG A 35   ? 0.5939 0.6813 0.5977 0.0369  0.0413  0.0279  33   ARG A CZ  
154   N NH1 . ARG A 35   ? 0.6473 0.7370 0.6476 0.0371  0.0414  0.0289  33   ARG A NH1 
155   N NH2 . ARG A 35   ? 0.5559 0.6426 0.5598 0.0393  0.0405  0.0213  33   ARG A NH2 
156   N N   . ALA A 36   ? 0.2384 0.2931 0.2577 0.0203  0.0379  0.0588  34   ALA A N   
157   C CA  . ALA A 36   ? 0.2461 0.2994 0.2685 0.0181  0.0375  0.0648  34   ALA A CA  
158   C C   . ALA A 36   ? 0.2479 0.2904 0.2691 0.0174  0.0355  0.0626  34   ALA A C   
159   O O   . ALA A 36   ? 0.2608 0.3028 0.2823 0.0165  0.0351  0.0659  34   ALA A O   
160   C CB  . ALA A 36   ? 0.2612 0.3145 0.2905 0.0158  0.0374  0.0697  34   ALA A CB  
161   N N   . ILE A 37   ? 0.2367 0.2711 0.2567 0.0177  0.0344  0.0572  35   ILE A N   
162   C CA  . ILE A 37   ? 0.2180 0.2431 0.2361 0.0173  0.0327  0.0545  35   ILE A CA  
163   C C   . ILE A 37   ? 0.2157 0.2434 0.2284 0.0190  0.0330  0.0525  35   ILE A C   
164   O O   . ILE A 37   ? 0.2207 0.2462 0.2328 0.0184  0.0323  0.0544  35   ILE A O   
165   C CB  . ILE A 37   ? 0.2216 0.2391 0.2392 0.0174  0.0315  0.0494  35   ILE A CB  
166   C CG1 . ILE A 37   ? 0.2332 0.2475 0.2564 0.0154  0.0309  0.0514  35   ILE A CG1 
167   C CG2 . ILE A 37   ? 0.2191 0.2286 0.2339 0.0172  0.0299  0.0462  35   ILE A CG2 
168   C CD1 . ILE A 37   ? 0.2506 0.2593 0.2735 0.0156  0.0298  0.0467  35   ILE A CD1 
169   N N   . THR A 38   ? 0.2214 0.2536 0.2301 0.0213  0.0337  0.0485  36   THR A N   
170   C CA  . THR A 38   ? 0.2372 0.2715 0.2409 0.0230  0.0338  0.0458  36   THR A CA  
171   C C   . THR A 38   ? 0.2309 0.2727 0.2342 0.0229  0.0348  0.0508  36   THR A C   
172   O O   . THR A 38   ? 0.2441 0.2847 0.2446 0.0232  0.0342  0.0505  36   THR A O   
173   C CB  . THR A 38   ? 0.2432 0.2821 0.2439 0.0256  0.0344  0.0406  36   THR A CB  
174   O OG1 . THR A 38   ? 0.2577 0.2898 0.2596 0.0255  0.0333  0.0368  36   THR A OG1 
175   C CG2 . THR A 38   ? 0.2632 0.3032 0.2590 0.0274  0.0340  0.0368  36   THR A CG2 
176   N N   . ALA A 39   ? 0.2491 0.2988 0.2555 0.0223  0.0361  0.0558  37   ALA A N   
177   C CA  . ALA A 39   ? 0.2701 0.3280 0.2765 0.0220  0.0371  0.0614  37   ALA A CA  
178   C C   . ALA A 39   ? 0.3028 0.3546 0.3115 0.0200  0.0357  0.0653  37   ALA A C   
179   O O   . ALA A 39   ? 0.3080 0.3644 0.3154 0.0201  0.0359  0.0685  37   ALA A O   
180   C CB  . ALA A 39   ? 0.2577 0.3248 0.2680 0.0213  0.0386  0.0667  37   ALA A CB  
181   N N   . ALA A 40   ? 0.2388 0.2805 0.2511 0.0183  0.0343  0.0650  38   ALA A N   
182   C CA  . ALA A 40   ? 0.2554 0.2912 0.2710 0.0165  0.0328  0.0684  38   ALA A CA  
183   C C   . ALA A 40   ? 0.2603 0.2885 0.2723 0.0170  0.0315  0.0638  38   ALA A C   
184   O O   . ALA A 40   ? 0.2683 0.2915 0.2828 0.0158  0.0302  0.0659  38   ALA A O   
185   C CB  . ALA A 40   ? 0.2432 0.2731 0.2655 0.0143  0.0318  0.0705  38   ALA A CB  
186   N N   . TYR A 41   ? 0.2383 0.2657 0.2450 0.0189  0.0316  0.0578  39   TYR A N   
187   C CA  . TYR A 41   ? 0.2356 0.2551 0.2393 0.0193  0.0303  0.0531  39   TYR A CA  
188   C C   . TYR A 41   ? 0.2499 0.2684 0.2533 0.0188  0.0295  0.0555  39   TYR A C   
189   O O   . TYR A 41   ? 0.2474 0.2581 0.2524 0.0177  0.0281  0.0548  39   TYR A O   
190   C CB  . TYR A 41   ? 0.2497 0.2713 0.2480 0.0215  0.0307  0.0473  39   TYR A CB  
191   C CG  . TYR A 41   ? 0.2352 0.2484 0.2310 0.0218  0.0293  0.0417  39   TYR A CG  
192   C CD1 . TYR A 41   ? 0.2526 0.2586 0.2487 0.0207  0.0279  0.0415  39   TYR A CD1 
193   C CD2 . TYR A 41   ? 0.2467 0.2596 0.2401 0.0233  0.0292  0.0366  39   TYR A CD2 
194   C CE1 . TYR A 41   ? 0.2276 0.2270 0.2215 0.0209  0.0267  0.0367  39   TYR A CE1 
195   C CE2 . TYR A 41   ? 0.2530 0.2588 0.2446 0.0234  0.0278  0.0321  39   TYR A CE2 
196   C CZ  . TYR A 41   ? 0.2345 0.2337 0.2261 0.0222  0.0267  0.0323  39   TYR A CZ  
197   O OH  . TYR A 41   ? 0.2447 0.2376 0.2346 0.0221  0.0253  0.0281  39   TYR A OH  
198   N N   . ARG A 42   ? 0.2588 0.2854 0.2602 0.0197  0.0305  0.0583  40   ARG A N   
199   C CA  . ARG A 42   ? 0.2655 0.2918 0.2665 0.0195  0.0297  0.0608  40   ARG A CA  
200   C C   . ARG A 42   ? 0.2456 0.2794 0.2500 0.0186  0.0304  0.0683  40   ARG A C   
201   O O   . ARG A 42   ? 0.3104 0.3489 0.3131 0.0191  0.0304  0.0707  40   ARG A O   
202   C CB  . ARG A 42   ? 0.3145 0.3427 0.3092 0.0214  0.0298  0.0564  40   ARG A CB  
203   C CG  . ARG A 42   ? 0.2954 0.3149 0.2879 0.0218  0.0287  0.0499  40   ARG A CG  
204   C CD  . ARG A 42   ? 0.3077 0.3293 0.2946 0.0238  0.0286  0.0451  40   ARG A CD  
205   N NE  . ARG A 42   ? 0.2891 0.3040 0.2747 0.0241  0.0278  0.0394  40   ARG A NE  
206   C CZ  . ARG A 42   ? 0.2773 0.2838 0.2630 0.0232  0.0265  0.0371  40   ARG A CZ  
207   N NH1 . ARG A 42   ? 0.2871 0.2905 0.2739 0.0223  0.0257  0.0394  40   ARG A NH1 
208   N NH2 . ARG A 42   ? 0.2762 0.2775 0.2612 0.0233  0.0258  0.0327  40   ARG A NH2 
209   N N   . ARG A 43   ? 0.2693 0.3044 0.2790 0.0172  0.0307  0.0721  41   ARG A N   
210   C CA  . ARG A 43   ? 0.2892 0.3318 0.3030 0.0161  0.0313  0.0799  41   ARG A CA  
211   C C   . ARG A 43   ? 0.3201 0.3594 0.3372 0.0149  0.0297  0.0839  41   ARG A C   
212   O O   . ARG A 43   ? 0.2865 0.3160 0.3061 0.0141  0.0281  0.0819  41   ARG A O   
213   C CB  . ARG A 43   ? 0.2817 0.3237 0.3016 0.0144  0.0314  0.0829  41   ARG A CB  
214   C CG  . ARG A 43   ? 0.2744 0.3230 0.3001 0.0128  0.0317  0.0915  41   ARG A CG  
215   C CD  . ARG A 43   ? 0.3119 0.3616 0.3426 0.0116  0.0322  0.0935  41   ARG A CD  
216   N NE  . ARG A 43   ? 0.2946 0.3509 0.3207 0.0132  0.0342  0.0901  41   ARG A NE  
217   C CZ  . ARG A 43   ? 0.2621 0.3174 0.2901 0.0130  0.0346  0.0884  41   ARG A CZ  
218   N NH1 . ARG A 43   ? 0.3012 0.3491 0.3354 0.0110  0.0333  0.0894  41   ARG A NH1 
219   N NH2 . ARG A 43   ? 0.3030 0.3652 0.3270 0.0147  0.0364  0.0854  41   ARG A NH2 
220   N N   . PRO A 44   ? 0.2969 0.3444 0.3141 0.0150  0.0302  0.0895  42   PRO A N   
221   C CA  . PRO A 44   ? 0.3000 0.3445 0.3211 0.0138  0.0285  0.0939  42   PRO A CA  
222   C C   . PRO A 44   ? 0.2475 0.2842 0.2772 0.0116  0.0269  0.0967  42   PRO A C   
223   O O   . PRO A 44   ? 0.3050 0.3430 0.3392 0.0104  0.0272  0.0992  42   PRO A O   
224   C CB  . PRO A 44   ? 0.3220 0.3786 0.3431 0.0138  0.0295  0.1010  42   PRO A CB  
225   C CG  . PRO A 44   ? 0.3572 0.4224 0.3710 0.0160  0.0316  0.0972  42   PRO A CG  
226   C CD  . PRO A 44   ? 0.3536 0.4140 0.3672 0.0161  0.0321  0.0920  42   PRO A CD  
227   N N   . GLU A 45   ? 0.2974 0.3260 0.3295 0.0111  0.0249  0.0956  43   GLU A N   
228   C CA  . GLU A 45   ? 0.3035 0.3238 0.3437 0.0093  0.0230  0.0967  43   GLU A CA  
229   C C   . GLU A 45   ? 0.3020 0.3267 0.3506 0.0074  0.0225  0.1053  43   GLU A C   
230   O O   . GLU A 45   ? 0.3219 0.3428 0.3773 0.0059  0.0217  0.1066  43   GLU A O   
231   C CB  . GLU A 45   ? 0.3507 0.3631 0.3917 0.0095  0.0210  0.0939  43   GLU A CB  
232   C CG  . GLU A 45   ? 0.3661 0.3684 0.4106 0.0088  0.0196  0.0891  43   GLU A CG  
233   C CD  . GLU A 45   ? 0.2880 0.2833 0.3309 0.0095  0.0181  0.0843  43   GLU A CD  
234   O OE1 . GLU A 45   ? 0.2895 0.2869 0.3262 0.0109  0.0187  0.0825  43   GLU A OE1 
235   O OE2 . GLU A 45   ? 0.3009 0.2888 0.3490 0.0086  0.0164  0.0822  43   GLU A OE2 
236   N N   . THR A 46   ? 0.3355 0.3685 0.3842 0.0074  0.0229  0.1117  44   THR A N   
237   C CA  . THR A 46   ? 0.3811 0.4195 0.4379 0.0055  0.0224  0.1208  44   THR A CA  
238   C C   . THR A 46   ? 0.3599 0.4040 0.4176 0.0048  0.0241  0.1226  44   THR A C   
239   O O   . THR A 46   ? 0.3912 0.4371 0.4573 0.0028  0.0234  0.1291  44   THR A O   
240   C CB  . THR A 46   ? 0.3632 0.4109 0.4188 0.0057  0.0227  0.1273  44   THR A CB  
241   O OG1 . THR A 46   ? 0.3665 0.4226 0.4122 0.0077  0.0251  0.1243  44   THR A OG1 
242   C CG2 . THR A 46   ? 0.3443 0.3861 0.4015 0.0059  0.0206  0.1271  44   THR A CG2 
243   N N   . GLU A 47   ? 0.3233 0.3707 0.3732 0.0065  0.0262  0.1171  45   GLU A N   
244   C CA  . GLU A 47   ? 0.3197 0.3726 0.3704 0.0061  0.0279  0.1182  45   GLU A CA  
245   C C   . GLU A 47   ? 0.3108 0.3542 0.3651 0.0052  0.0270  0.1138  45   GLU A C   
246   O O   . GLU A 47   ? 0.3441 0.3898 0.4033 0.0039  0.0274  0.1169  45   GLU A O   
247   C CB  . GLU A 47   ? 0.3509 0.4120 0.3921 0.0084  0.0304  0.1142  45   GLU A CB  
248   C CG  . GLU A 47   ? 0.4970 0.5671 0.5336 0.0096  0.0311  0.1169  45   GLU A CG  
249   C CD  . GLU A 47   ? 0.5457 0.6262 0.5743 0.0118  0.0336  0.1139  45   GLU A CD  
250   O OE1 . GLU A 47   ? 0.5737 0.6543 0.6007 0.0124  0.0347  0.1098  45   GLU A OE1 
251   O OE2 . GLU A 47   ? 0.6418 0.7305 0.6660 0.0130  0.0342  0.1154  45   GLU A OE2 
252   N N   . CYS A 48   ? 0.2849 0.3182 0.3370 0.0059  0.0258  0.1069  46   CYS A N   
253   C CA  . CYS A 48   ? 0.2866 0.3116 0.3414 0.0053  0.0250  0.1023  46   CYS A CA  
254   C C   . CYS A 48   ? 0.2226 0.2423 0.2880 0.0030  0.0228  0.1064  46   CYS A C   
255   O O   . CYS A 48   ? 0.2737 0.2908 0.3436 0.0019  0.0224  0.1057  46   CYS A O   
256   C CB  . CYS A 48   ? 0.3242 0.3407 0.3737 0.0066  0.0242  0.0941  46   CYS A CB  
257   S SG  . CYS A 48   ? 0.3172 0.3375 0.3552 0.0093  0.0263  0.0880  46   CYS A SG  
258   N N   . LEU A 49   ? 0.3009 0.3188 0.3709 0.0023  0.0210  0.1102  47   LEU A N   
259   C CA  . LEU A 49   ? 0.3090 0.3196 0.3893 0.0004  0.0183  0.1120  47   LEU A CA  
260   C C   . LEU A 49   ? 0.2668 0.2812 0.3562 -0.0017 0.0179  0.1192  47   LEU A C   
261   O O   . LEU A 49   ? 0.3079 0.3163 0.4040 -0.0030 0.0164  0.1177  47   LEU A O   
262   C CB  . LEU A 49   ? 0.3145 0.3212 0.3975 0.0005  0.0163  0.1132  47   LEU A CB  
263   C CG  . LEU A 49   ? 0.3272 0.3244 0.4077 0.0015  0.0150  0.1051  47   LEU A CG  
264   C CD1 . LEU A 49   ? 0.3300 0.3196 0.4172 0.0004  0.0133  0.1019  47   LEU A CD1 
265   C CD2 . LEU A 49   ? 0.3270 0.3249 0.3959 0.0035  0.0171  0.0984  47   LEU A CD2 
266   N N   . PRO A 50   ? 0.3290 0.3533 0.4195 -0.0024 0.0191  0.1269  48   PRO A N   
267   C CA  . PRO A 50   ? 0.3417 0.3694 0.4422 -0.0048 0.0184  0.1346  48   PRO A CA  
268   C C   . PRO A 50   ? 0.2973 0.3233 0.3999 -0.0055 0.0189  0.1317  48   PRO A C   
269   O O   . PRO A 50   ? 0.3582 0.3795 0.4706 -0.0074 0.0168  0.1337  48   PRO A O   
270   C CB  . PRO A 50   ? 0.3353 0.3762 0.4333 -0.0048 0.0204  0.1421  48   PRO A CB  
271   C CG  . PRO A 50   ? 0.3226 0.3643 0.4136 -0.0030 0.0207  0.1404  48   PRO A CG  
272   C CD  . PRO A 50   ? 0.3125 0.3455 0.3963 -0.0011 0.0207  0.1297  48   PRO A CD  
273   N N   . PRO A 51   ? 0.3065 0.3360 0.4005 -0.0039 0.0214  0.1270  49   PRO A N   
274   C CA  . PRO A 51   ? 0.3519 0.3790 0.4483 -0.0046 0.0216  0.1242  49   PRO A CA  
275   C C   . PRO A 51   ? 0.2701 0.2854 0.3695 -0.0048 0.0193  0.1176  49   PRO A C   
276   O O   . PRO A 51   ? 0.3343 0.3465 0.4399 -0.0062 0.0183  0.1174  49   PRO A O   
277   C CB  . PRO A 51   ? 0.3293 0.3626 0.4156 -0.0026 0.0245  0.1201  49   PRO A CB  
278   C CG  . PRO A 51   ? 0.3392 0.3737 0.4172 -0.0006 0.0253  0.1174  49   PRO A CG  
279   C CD  . PRO A 51   ? 0.3209 0.3568 0.4037 -0.0016 0.0239  0.1241  49   PRO A CD  
280   N N   . LEU A 52   ? 0.3190 0.3279 0.4140 -0.0035 0.0184  0.1123  50   LEU A N   
281   C CA  . LEU A 52   ? 0.3075 0.3060 0.4053 -0.0037 0.0162  0.1062  50   LEU A CA  
282   C C   . LEU A 52   ? 0.2649 0.2591 0.3750 -0.0057 0.0132  0.1102  50   LEU A C   
283   O O   . LEU A 52   ? 0.2901 0.2788 0.4065 -0.0067 0.0115  0.1077  50   LEU A O   
284   C CB  . LEU A 52   ? 0.3036 0.2975 0.3938 -0.0018 0.0162  0.0998  50   LEU A CB  
285   C CG  . LEU A 52   ? 0.3251 0.3218 0.4038 0.0002  0.0186  0.0948  50   LEU A CG  
286   C CD1 . LEU A 52   ? 0.2783 0.2708 0.3507 0.0018  0.0183  0.0897  50   LEU A CD1 
287   C CD2 . LEU A 52   ? 0.2880 0.2822 0.3653 0.0003  0.0190  0.0898  50   LEU A CD2 
288   N N   . VAL A 53   ? 0.2917 0.2885 0.4057 -0.0062 0.0124  0.1165  51   VAL A N   
289   C CA  . VAL A 53   ? 0.3275 0.3208 0.4543 -0.0082 0.0094  0.1213  51   VAL A CA  
290   C C   . VAL A 53   ? 0.2674 0.2632 0.4024 -0.0103 0.0090  0.1257  51   VAL A C   
291   O O   . VAL A 53   ? 0.3309 0.3205 0.4755 -0.0116 0.0064  0.1248  51   VAL A O   
292   C CB  . VAL A 53   ? 0.3189 0.3162 0.4481 -0.0085 0.0088  0.1284  51   VAL A CB  
293   C CG1 . VAL A 53   ? 0.3331 0.3278 0.4769 -0.0107 0.0056  0.1347  51   VAL A CG1 
294   C CG2 . VAL A 53   ? 0.3046 0.2981 0.4274 -0.0066 0.0086  0.1236  51   VAL A CG2 
295   N N   . GLU A 54   ? 0.3137 0.3187 0.4453 -0.0105 0.0116  0.1303  52   GLU A N   
296   C CA  . GLU A 54   ? 0.3643 0.3725 0.5036 -0.0125 0.0115  0.1347  52   GLU A CA  
297   C C   . GLU A 54   ? 0.3131 0.3151 0.4527 -0.0125 0.0110  0.1274  52   GLU A C   
298   O O   . GLU A 54   ? 0.3564 0.3547 0.5061 -0.0143 0.0088  0.1286  52   GLU A O   
299   C CB  . GLU A 54   ? 0.3989 0.4192 0.5335 -0.0125 0.0147  0.1403  52   GLU A CB  
300   N N   . ALA A 55   ? 0.3261 0.3266 0.4549 -0.0104 0.0128  0.1197  53   ALA A N   
301   C CA  . ALA A 55   ? 0.3222 0.3178 0.4504 -0.0102 0.0124  0.1131  53   ALA A CA  
302   C C   . ALA A 55   ? 0.3129 0.2984 0.4473 -0.0107 0.0091  0.1083  53   ALA A C   
303   O O   . ALA A 55   ? 0.3053 0.2871 0.4442 -0.0114 0.0079  0.1051  53   ALA A O   
304   C CB  . ALA A 55   ? 0.3373 0.3339 0.4529 -0.0079 0.0149  0.1066  53   ALA A CB  
305   N N   . ALA A 56   ? 0.3013 0.2829 0.4361 -0.0101 0.0077  0.1075  54   ALA A N   
306   C CA  . ALA A 56   ? 0.3201 0.2930 0.4602 -0.0101 0.0047  0.1022  54   ALA A CA  
307   C C   . ALA A 56   ? 0.3565 0.3267 0.5109 -0.0121 0.0015  0.1070  54   ALA A C   
308   O O   . ALA A 56   ? 0.3216 0.2847 0.4822 -0.0122 -0.0014 0.1024  54   ALA A O   
309   C CB  . ALA A 56   ? 0.2564 0.2263 0.3899 -0.0083 0.0047  0.0983  54   ALA A CB  
310   N N   . THR A 57   ? 0.3456 0.3216 0.5060 -0.0137 0.0017  0.1160  55   THR A N   
311   C CA  . THR A 57   ? 0.3214 0.2952 0.4963 -0.0158 -0.0016 0.1215  55   THR A CA  
312   C C   . THR A 57   ? 0.3307 0.2999 0.5142 -0.0171 -0.0037 0.1184  55   THR A C   
313   O O   . THR A 57   ? 0.3668 0.3385 0.5469 -0.0173 -0.0021 0.1168  55   THR A O   
314   C CB  . THR A 57   ? 0.4101 0.3929 0.5881 -0.0173 -0.0005 0.1319  55   THR A CB  
315   O OG1 . THR A 57   ? 0.3744 0.3610 0.5454 -0.0161 0.0011  0.1349  55   THR A OG1 
316   C CG2 . THR A 57   ? 0.3873 0.3707 0.5786 -0.0190 -0.0042 0.1350  55   THR A CG2 
317   N N   . GLN A 58   ? 0.3466 0.3103 0.5401 -0.0176 -0.0076 0.1159  56   GLN A N   
318   C CA  . GLN A 58   ? 0.3419 0.3022 0.5443 -0.0187 -0.0102 0.1123  56   GLN A CA  
319   C C   . GLN A 58   ? 0.3017 0.2632 0.5169 -0.0199 -0.0139 0.1156  56   GLN A C   
320   O O   . GLN A 58   ? 0.3638 0.3272 0.5808 -0.0198 -0.0147 0.1193  56   GLN A O   
321   C CB  . GLN A 58   ? 0.3840 0.3359 0.5851 -0.0174 -0.0116 0.1025  56   GLN A CB  
322   C CG  . GLN A 58   ? 0.3153 0.2680 0.5019 -0.0156 -0.0083 0.0969  56   GLN A CG  
323   C CD  . GLN A 58   ? 0.3104 0.2572 0.4954 -0.0146 -0.0097 0.0868  56   GLN A CD  
324   O OE1 . GLN A 58   ? 0.3492 0.2951 0.5380 -0.0154 -0.0106 0.0842  56   GLN A OE1 
325   N NE2 . GLN A 58   ? 0.3509 0.2944 0.5304 -0.0127 -0.0100 0.0811  56   GLN A NE2 
326   N N   . SER A 59   ? 0.3301 0.2907 0.5545 -0.0212 -0.0162 0.1143  57   SER A N   
327   C CA  . SER A 59   ? 0.3215 0.2834 0.5590 -0.0225 -0.0198 0.1177  57   SER A CA  
328   C C   . SER A 59   ? 0.3643 0.3206 0.6069 -0.0214 -0.0230 0.1129  57   SER A C   
329   O O   . SER A 59   ? 0.3175 0.2678 0.5554 -0.0199 -0.0232 0.1053  57   SER A O   
330   C CB  . SER A 59   ? 0.3700 0.3312 0.6161 -0.0238 -0.0217 0.1160  57   SER A CB  
331   O OG  . SER A 59   ? 0.3759 0.3298 0.6230 -0.0229 -0.0236 0.1065  57   SER A OG  
332   N N   . LYS A 60   ? 0.3406 0.2992 0.5933 -0.0223 -0.0258 0.1176  58   LYS A N   
333   C CA  . LYS A 60   ? 0.3544 0.3082 0.6137 -0.0214 -0.0292 0.1134  58   LYS A CA  
334   C C   . LYS A 60   ? 0.3473 0.2946 0.6116 -0.0208 -0.0319 0.1040  58   LYS A C   
335   O O   . LYS A 60   ? 0.4023 0.3443 0.6652 -0.0191 -0.0331 0.0971  58   LYS A O   
336   C CB  . LYS A 60   ? 0.3636 0.3214 0.6348 -0.0227 -0.0321 0.1203  58   LYS A CB  
337   C CG  . LYS A 60   ? 0.3845 0.3379 0.6636 -0.0218 -0.0358 0.1167  58   LYS A CG  
338   C CD  . LYS A 60   ? 0.4553 0.4064 0.7245 -0.0200 -0.0340 0.1142  58   LYS A CD  
339   C CE  . LYS A 60   ? 0.5096 0.4591 0.7870 -0.0195 -0.0373 0.1142  58   LYS A CE  
340   N NZ  . LYS A 60   ? 0.5402 0.4844 0.8284 -0.0191 -0.0415 0.1068  58   LYS A NZ  
341   N N   . GLU A 61   ? 0.3683 0.3161 0.6382 -0.0219 -0.0329 0.1034  59   GLU A N   
342   C CA  . GLU A 61   ? 0.3884 0.3308 0.6629 -0.0213 -0.0354 0.0944  59   GLU A CA  
343   C C   . GLU A 61   ? 0.4365 0.3747 0.6992 -0.0197 -0.0331 0.0868  59   GLU A C   
344   O O   . GLU A 61   ? 0.4052 0.3385 0.6694 -0.0183 -0.0351 0.0784  59   GLU A O   
345   C CB  . GLU A 61   ? 0.3798 0.3243 0.6612 -0.0230 -0.0364 0.0959  59   GLU A CB  
346   N N   . ILE A 62   ? 0.3735 0.3138 0.6246 -0.0197 -0.0289 0.0895  60   ILE A N   
347   C CA  . ILE A 62   ? 0.3445 0.2811 0.5845 -0.0181 -0.0267 0.0829  60   ILE A CA  
348   C C   . ILE A 62   ? 0.3926 0.3264 0.6277 -0.0163 -0.0266 0.0802  60   ILE A C   
349   O O   . ILE A 62   ? 0.3401 0.2693 0.5721 -0.0148 -0.0272 0.0720  60   ILE A O   
350   C CB  . ILE A 62   ? 0.3545 0.2945 0.5843 -0.0186 -0.0224 0.0869  60   ILE A CB  
351   C CG1 . ILE A 62   ? 0.4170 0.3581 0.6508 -0.0200 -0.0227 0.0864  60   ILE A CG1 
352   C CG2 . ILE A 62   ? 0.3580 0.2947 0.5755 -0.0168 -0.0198 0.0818  60   ILE A CG2 
353   C CD1 . ILE A 62   ? 0.4181 0.3618 0.6421 -0.0202 -0.0188 0.0884  60   ILE A CD1 
354   N N   . ARG A 63   ? 0.3302 0.2671 0.5646 -0.0165 -0.0258 0.0869  61   ARG A N   
355   C CA  . ARG A 63   ? 0.3657 0.3003 0.5959 -0.0148 -0.0258 0.0848  61   ARG A CA  
356   C C   . ARG A 63   ? 0.3930 0.3232 0.6320 -0.0139 -0.0298 0.0780  61   ARG A C   
357   O O   . ARG A 63   ? 0.3439 0.2702 0.5784 -0.0121 -0.0299 0.0714  61   ARG A O   
358   C CB  . ARG A 63   ? 0.3783 0.3178 0.6071 -0.0153 -0.0245 0.0936  61   ARG A CB  
359   C CG  . ARG A 63   ? 0.4192 0.3633 0.6372 -0.0155 -0.0202 0.0990  61   ARG A CG  
360   C CD  . ARG A 63   ? 0.5216 0.4710 0.7368 -0.0156 -0.0188 0.1068  61   ARG A CD  
361   N NE  . ARG A 63   ? 0.5432 0.4983 0.7675 -0.0175 -0.0201 0.1145  61   ARG A NE  
362   C CZ  . ARG A 63   ? 0.5476 0.5035 0.7812 -0.0180 -0.0231 0.1173  61   ARG A CZ  
363   N NH1 . ARG A 63   ? 0.5821 0.5335 0.8173 -0.0167 -0.0250 0.1131  61   ARG A NH1 
364   N NH2 . ARG A 63   ? 0.5248 0.4864 0.7667 -0.0198 -0.0242 0.1247  61   ARG A NH2 
365   N N   . ASP A 64   ? 0.3964 0.3275 0.6483 -0.0151 -0.0333 0.0792  62   ASP A N   
366   C CA  . ASP A 64   ? 0.3926 0.3199 0.6538 -0.0142 -0.0373 0.0723  62   ASP A CA  
367   C C   . ASP A 64   ? 0.4102 0.3336 0.6689 -0.0131 -0.0378 0.0623  62   ASP A C   
368   O O   . ASP A 64   ? 0.3785 0.2986 0.6371 -0.0113 -0.0393 0.0547  62   ASP A O   
369   C CB  . ASP A 64   ? 0.3852 0.3146 0.6612 -0.0157 -0.0410 0.0761  62   ASP A CB  
370   C CG  . ASP A 64   ? 0.4118 0.3450 0.6916 -0.0166 -0.0412 0.0853  62   ASP A CG  
371   O OD1 . ASP A 64   ? 0.4046 0.3387 0.6759 -0.0159 -0.0388 0.0880  62   ASP A OD1 
372   O OD2 . ASP A 64   ? 0.4910 0.4268 0.7827 -0.0181 -0.0439 0.0899  62   ASP A OD2 
373   N N   . ALA A 65   ? 0.3267 0.2508 0.5835 -0.0140 -0.0367 0.0619  63   ALA A N   
374   C CA  . ALA A 65   ? 0.3441 0.2651 0.5983 -0.0131 -0.0371 0.0526  63   ALA A CA  
375   C C   . ALA A 65   ? 0.3772 0.2960 0.6186 -0.0114 -0.0342 0.0483  63   ALA A C   
376   O O   . ALA A 65   ? 0.3700 0.2860 0.6101 -0.0099 -0.0354 0.0395  63   ALA A O   
377   C CB  . ALA A 65   ? 0.3751 0.2977 0.6300 -0.0146 -0.0364 0.0539  63   ALA A CB  
378   N N   . ALA A 66   ? 0.3207 0.2412 0.5525 -0.0115 -0.0306 0.0544  64   ALA A N   
379   C CA  . ALA A 66   ? 0.3444 0.2629 0.5643 -0.0099 -0.0279 0.0510  64   ALA A CA  
380   C C   . ALA A 66   ? 0.3659 0.2821 0.5866 -0.0081 -0.0295 0.0469  64   ALA A C   
381   O O   . ALA A 66   ? 0.3256 0.2392 0.5411 -0.0065 -0.0292 0.0395  64   ALA A O   
382   C CB  . ALA A 66   ? 0.3394 0.2609 0.5501 -0.0104 -0.0239 0.0589  64   ALA A CB  
383   N N   . ALA A 67   ? 0.2952 0.2128 0.5226 -0.0085 -0.0311 0.0517  65   ALA A N   
384   C CA  . ALA A 67   ? 0.3574 0.2730 0.5866 -0.0069 -0.0327 0.0481  65   ALA A CA  
385   C C   . ALA A 67   ? 0.3567 0.2698 0.5928 -0.0058 -0.0361 0.0383  65   ALA A C   
386   O O   . ALA A 67   ? 0.3559 0.2670 0.5889 -0.0040 -0.0365 0.0316  65   ALA A O   
387   C CB  . ALA A 67   ? 0.3915 0.3094 0.6277 -0.0077 -0.0341 0.0555  65   ALA A CB  
388   N N   . SER A 68   ? 0.3676 0.2814 0.6132 -0.0070 -0.0386 0.0373  66   SER A N   
389   C CA  . SER A 68   ? 0.3885 0.3007 0.6408 -0.0059 -0.0419 0.0278  66   SER A CA  
390   C C   . SER A 68   ? 0.4143 0.3251 0.6577 -0.0047 -0.0403 0.0197  66   SER A C   
391   O O   . SER A 68   ? 0.3802 0.2899 0.6236 -0.0029 -0.0417 0.0112  66   SER A O   
392   C CB  . SER A 68   ? 0.4412 0.3547 0.7056 -0.0074 -0.0448 0.0289  66   SER A CB  
393   O OG  . SER A 68   ? 0.4933 0.4059 0.7636 -0.0063 -0.0478 0.0192  66   SER A OG  
394   N N   . THR A 69   ? 0.3774 0.2887 0.6132 -0.0057 -0.0374 0.0222  67   THR A N   
395   C CA  . THR A 69   ? 0.3454 0.2555 0.5723 -0.0046 -0.0358 0.0152  67   THR A CA  
396   C C   . THR A 69   ? 0.3040 0.2140 0.5206 -0.0028 -0.0337 0.0127  67   THR A C   
397   O O   . THR A 69   ? 0.3343 0.2451 0.5467 -0.0012 -0.0340 0.0041  67   THR A O   
398   C CB  . THR A 69   ? 0.3582 0.2703 0.5780 -0.0060 -0.0328 0.0194  67   THR A CB  
399   O OG1 . THR A 69   ? 0.3387 0.2509 0.5682 -0.0076 -0.0350 0.0201  67   THR A OG1 
400   C CG2 . THR A 69   ? 0.3147 0.2297 0.5205 -0.0048 -0.0303 0.0129  67   THR A CG2 
401   N N   . ALA A 70   ? 0.3221 0.2328 0.5336 -0.0030 -0.0314 0.0200  68   ALA A N   
402   C CA  . ALA A 70   ? 0.3322 0.2440 0.5331 -0.0013 -0.0293 0.0181  68   ALA A CA  
403   C C   . ALA A 70   ? 0.3656 0.2748 0.5734 0.0004  -0.0323 0.0117  68   ALA A C   
404   O O   . ALA A 70   ? 0.3363 0.2468 0.5367 0.0020  -0.0315 0.0049  68   ALA A O   
405   C CB  . ALA A 70   ? 0.3369 0.2499 0.5333 -0.0018 -0.0269 0.0274  68   ALA A CB  
406   N N   . ARG A 71   ? 0.3435 0.2512 0.5643 -0.0001 -0.0356 0.0138  69   ARG A N   
407   C CA  . ARG A 71   ? 0.3625 0.2698 0.5895 0.0016  -0.0386 0.0074  69   ARG A CA  
408   C C   . ARG A 71   ? 0.3438 0.2514 0.5721 0.0027  -0.0402 -0.0034 69   ARG A C   
409   O O   . ARG A 71   ? 0.3778 0.2855 0.6039 0.0047  -0.0407 -0.0106 69   ARG A O   
410   C CB  . ARG A 71   ? 0.3823 0.2904 0.6222 0.0006  -0.0418 0.0116  69   ARG A CB  
411   C CG  . ARG A 71   ? 0.3944 0.3024 0.6433 0.0022  -0.0455 0.0041  69   ARG A CG  
412   C CD  . ARG A 71   ? 0.4064 0.3150 0.6683 0.0012  -0.0487 0.0090  69   ARG A CD  
413   N NE  . ARG A 71   ? 0.4495 0.3581 0.7094 0.0011  -0.0476 0.0162  69   ARG A NE  
414   C CZ  . ARG A 71   ? 0.4519 0.3598 0.7103 0.0028  -0.0479 0.0134  69   ARG A CZ  
415   N NH1 . ARG A 71   ? 0.4555 0.3631 0.7144 0.0048  -0.0493 0.0036  69   ARG A NH1 
416   N NH2 . ARG A 71   ? 0.4546 0.3627 0.7110 0.0025  -0.0469 0.0206  69   ARG A NH2 
417   N N   . LYS A 72   ? 0.3308 0.2390 0.5624 0.0016  -0.0410 -0.0047 70   LYS A N   
418   C CA  . LYS A 72   ? 0.3674 0.2767 0.6000 0.0026  -0.0426 -0.0149 70   LYS A CA  
419   C C   . LYS A 72   ? 0.4074 0.3177 0.6267 0.0039  -0.0397 -0.0199 70   LYS A C   
420   O O   . LYS A 72   ? 0.3499 0.2621 0.5681 0.0056  -0.0407 -0.0287 70   LYS A O   
421   C CB  . LYS A 72   ? 0.3578 0.2678 0.5955 0.0010  -0.0437 -0.0143 70   LYS A CB  
422   C CG  . LYS A 72   ? 0.4388 0.3505 0.6772 0.0019  -0.0453 -0.0246 70   LYS A CG  
423   C CD  . LYS A 72   ? 0.4325 0.3449 0.6763 0.0002  -0.0464 -0.0234 70   LYS A CD  
424   C CE  . LYS A 72   ? 0.5365 0.4512 0.7816 0.0012  -0.0483 -0.0338 70   LYS A CE  
425   N NZ  . LYS A 72   ? 0.6132 0.5297 0.8685 0.0027  -0.0522 -0.0405 70   LYS A NZ  
426   N N   . LEU A 73   ? 0.3565 0.2689 0.5635 0.0029  -0.0357 -0.0140 71   LEU A N   
427   C CA  . LEU A 73   ? 0.3342 0.2505 0.5260 0.0039  -0.0324 -0.0176 71   LEU A CA  
428   C C   . LEU A 73   ? 0.3609 0.2776 0.5491 0.0057  -0.0320 -0.0200 71   LEU A C   
429   O O   . LEU A 73   ? 0.3752 0.2949 0.5569 0.0070  -0.0314 -0.0270 71   LEU A O   
430   C CB  . LEU A 73   ? 0.3084 0.2265 0.4892 0.0026  -0.0285 -0.0103 71   LEU A CB  
431   C CG  . LEU A 73   ? 0.3429 0.2616 0.5249 0.0009  -0.0282 -0.0077 71   LEU A CG  
432   C CD1 . LEU A 73   ? 0.3196 0.2398 0.4918 -0.0001 -0.0245 0.0001  71   LEU A CD1 
433   C CD2 . LEU A 73   ? 0.3567 0.2782 0.5353 0.0013  -0.0286 -0.0156 71   LEU A CD2 
434   N N   . ILE A 74   ? 0.3314 0.2453 0.5235 0.0056  -0.0322 -0.0140 72   ILE A N   
435   C CA  . ILE A 74   ? 0.3376 0.2518 0.5261 0.0072  -0.0317 -0.0157 72   ILE A CA  
436   C C   . ILE A 74   ? 0.3625 0.2760 0.5602 0.0090  -0.0352 -0.0244 72   ILE A C   
437   O O   . ILE A 74   ? 0.3686 0.2845 0.5609 0.0106  -0.0346 -0.0300 72   ILE A O   
438   C CB  . ILE A 74   ? 0.3560 0.2678 0.5464 0.0067  -0.0311 -0.0066 72   ILE A CB  
439   C CG1 . ILE A 74   ? 0.3567 0.2706 0.5354 0.0054  -0.0271 0.0006  72   ILE A CG1 
440   C CG2 . ILE A 74   ? 0.3526 0.2640 0.5425 0.0084  -0.0315 -0.0085 72   ILE A CG2 
441   C CD1 . ILE A 74   ? 0.3407 0.2532 0.5226 0.0044  -0.0267 0.0103  72   ILE A CD1 
442   N N   . GLU A 75   ? 0.3839 0.2946 0.5961 0.0087  -0.0390 -0.0259 73   GLU A N   
443   C CA  . GLU A 75   ? 0.3957 0.3072 0.6165 0.0104  -0.0425 -0.0349 73   GLU A CA  
444   C C   . GLU A 75   ? 0.4380 0.3533 0.6526 0.0115  -0.0420 -0.0446 73   GLU A C   
445   O O   . GLU A 75   ? 0.3999 0.3177 0.6144 0.0135  -0.0429 -0.0523 73   GLU A O   
446   C CB  . GLU A 75   ? 0.4304 0.3421 0.6647 0.0094  -0.0461 -0.0337 73   GLU A CB  
447   C CG  . GLU A 75   ? 0.4580 0.3682 0.6993 0.0090  -0.0474 -0.0266 73   GLU A CG  
448   C CD  . GLU A 75   ? 0.5102 0.4204 0.7642 0.0074  -0.0504 -0.0227 73   GLU A CD  
449   O OE1 . GLU A 75   ? 0.4993 0.4103 0.7565 0.0066  -0.0514 -0.0251 73   GLU A OE1 
450   O OE2 . GLU A 75   ? 0.5380 0.4475 0.7989 0.0069  -0.0519 -0.0172 73   GLU A OE2 
451   N N   . ALA A 76   ? 0.4251 0.3427 0.6337 0.0102  -0.0404 -0.0439 74   ALA A N   
452   C CA  . ALA A 76   ? 0.3769 0.2999 0.5773 0.0109  -0.0394 -0.0518 74   ALA A CA  
453   C C   . ALA A 76   ? 0.4089 0.3357 0.5952 0.0118  -0.0360 -0.0523 74   ALA A C   
454   O O   . ALA A 76   ? 0.4612 0.3925 0.6441 0.0133  -0.0362 -0.0602 74   ALA A O   
455   C CB  . ALA A 76   ? 0.4579 0.3822 0.6546 0.0092  -0.0383 -0.0497 74   ALA A CB  
456   N N   . LEU A 77   ? 0.3966 0.3221 0.5748 0.0109  -0.0329 -0.0441 75   LEU A N   
457   C CA  . LEU A 77   ? 0.3735 0.3022 0.5385 0.0116  -0.0297 -0.0441 75   LEU A CA  
458   C C   . LEU A 77   ? 0.4357 0.3649 0.6036 0.0135  -0.0310 -0.0488 75   LEU A C   
459   O O   . LEU A 77   ? 0.4742 0.4082 0.6354 0.0147  -0.0300 -0.0546 75   LEU A O   
460   C CB  . LEU A 77   ? 0.3724 0.2992 0.5300 0.0104  -0.0267 -0.0345 75   LEU A CB  
461   C CG  . LEU A 77   ? 0.4054 0.3335 0.5544 0.0088  -0.0241 -0.0304 75   LEU A CG  
462   C CD1 . LEU A 77   ? 0.3778 0.3045 0.5204 0.0080  -0.0213 -0.0217 75   LEU A CD1 
463   C CD2 . LEU A 77   ? 0.3778 0.3111 0.5165 0.0092  -0.0225 -0.0359 75   LEU A CD2 
464   N N   . ARG A 78   ? 0.3813 0.3061 0.5595 0.0139  -0.0331 -0.0460 76   ARG A N   
465   C CA  . ARG A 78   ? 0.3715 0.2965 0.5535 0.0159  -0.0345 -0.0503 76   ARG A CA  
466   C C   . ARG A 78   ? 0.4030 0.3304 0.5929 0.0176  -0.0376 -0.0609 76   ARG A C   
467   O O   . ARG A 78   ? 0.4872 0.4172 0.6772 0.0194  -0.0382 -0.0664 76   ARG A O   
468   C CB  . ARG A 78   ? 0.3630 0.2825 0.5542 0.0158  -0.0361 -0.0438 76   ARG A CB  
469   C CG  . ARG A 78   ? 0.4066 0.3251 0.5887 0.0146  -0.0328 -0.0344 76   ARG A CG  
470   C CD  . ARG A 78   ? 0.3818 0.2959 0.5726 0.0145  -0.0344 -0.0280 76   ARG A CD  
471   N NE  . ARG A 78   ? 0.3694 0.2841 0.5500 0.0142  -0.0312 -0.0214 76   ARG A NE  
472   C CZ  . ARG A 78   ? 0.3907 0.3028 0.5754 0.0141  -0.0317 -0.0149 76   ARG A CZ  
473   N NH1 . ARG A 78   ? 0.4181 0.3264 0.6172 0.0141  -0.0353 -0.0131 76   ARG A NH1 
474   N NH2 . ARG A 78   ? 0.4205 0.3340 0.5950 0.0140  -0.0288 -0.0099 76   ARG A NH2 
475   N N   . GLY A 79   ? 0.4254 0.3528 0.6219 0.0170  -0.0397 -0.0640 77   GLY A N   
476   C CA  . GLY A 79   ? 0.4944 0.4247 0.6990 0.0187  -0.0429 -0.0746 77   GLY A CA  
477   C C   . GLY A 79   ? 0.5598 0.4979 0.7539 0.0195  -0.0412 -0.0819 77   GLY A C   
478   O O   . GLY A 79   ? 0.5591 0.5012 0.7577 0.0214  -0.0433 -0.0912 77   GLY A O   
479   N N   . LYS A 80   ? 0.5290 0.4698 0.7094 0.0181  -0.0375 -0.0778 78   LYS A N   
480   C CA  . LYS A 80   ? 0.5346 0.4831 0.7046 0.0186  -0.0357 -0.0835 78   LYS A CA  
481   C C   . LYS A 80   ? 0.5181 0.4693 0.6756 0.0188  -0.0322 -0.0808 78   LYS A C   
482   O O   . LYS A 80   ? 0.6159 0.5737 0.7639 0.0190  -0.0305 -0.0843 78   LYS A O   
483   C CB  . LYS A 80   ? 0.5282 0.4786 0.6930 0.0169  -0.0346 -0.0821 78   LYS A CB  
484   C CG  . LYS A 80   ? 0.5577 0.5039 0.7159 0.0148  -0.0319 -0.0718 78   LYS A CG  
485   C CD  . LYS A 80   ? 0.5224 0.4698 0.6785 0.0133  -0.0316 -0.0708 78   LYS A CD  
486   C CE  . LYS A 80   ? 0.5183 0.4622 0.6681 0.0114  -0.0288 -0.0610 78   LYS A CE  
487   N NZ  . LYS A 80   ? 0.3666 0.3117 0.5147 0.0100  -0.0286 -0.0602 78   LYS A NZ  
488   N N   . HIS A 81   ? 0.5347 0.4812 0.6923 0.0187  -0.0313 -0.0746 79   HIS A N   
489   C CA  . HIS A 81   ? 0.5672 0.5155 0.7133 0.0188  -0.0281 -0.0713 79   HIS A CA  
490   C C   . HIS A 81   ? 0.6254 0.5805 0.7679 0.0205  -0.0280 -0.0791 79   HIS A C   
491   O O   . HIS A 81   ? 0.6747 0.6300 0.8250 0.0223  -0.0301 -0.0838 79   HIS A O   
492   C CB  . HIS A 81   ? 0.6114 0.5538 0.7607 0.0188  -0.0280 -0.0646 79   HIS A CB  
493   N N   . SER A 84   ? 0.6309 0.6054 0.7137 0.0185  -0.0128 -0.0686 82   SER A N   
494   C CA  . SER A 84   ? 0.6125 0.5918 0.7012 0.0204  -0.0146 -0.0767 82   SER A CA  
495   C C   . SER A 84   ? 0.5424 0.5310 0.6233 0.0205  -0.0132 -0.0806 82   SER A C   
496   O O   . SER A 84   ? 0.5227 0.5162 0.6061 0.0220  -0.0139 -0.0863 82   SER A O   
497   C CB  . SER A 84   ? 0.5755 0.5546 0.6741 0.0212  -0.0175 -0.0821 82   SER A CB  
498   N N   . GLY A 85   ? 0.5707 0.5621 0.6427 0.0187  -0.0113 -0.0775 83   GLY A N   
499   C CA  . GLY A 85   ? 0.4886 0.4890 0.5529 0.0184  -0.0099 -0.0799 83   GLY A CA  
500   C C   . GLY A 85   ? 0.3738 0.3753 0.4338 0.0186  -0.0084 -0.0781 83   GLY A C   
501   O O   . GLY A 85   ? 0.3732 0.3816 0.4335 0.0198  -0.0086 -0.0833 83   GLY A O   
502   N N   . VAL A 86   ? 0.4044 0.3996 0.4604 0.0176  -0.0069 -0.0708 84   VAL A N   
503   C CA  . VAL A 86   ? 0.3846 0.3799 0.4372 0.0179  -0.0056 -0.0687 84   VAL A CA  
504   C C   . VAL A 86   ? 0.4055 0.3992 0.4664 0.0200  -0.0073 -0.0725 84   VAL A C   
505   O O   . VAL A 86   ? 0.3223 0.3206 0.3824 0.0210  -0.0070 -0.0754 84   VAL A O   
506   C CB  . VAL A 86   ? 0.4726 0.4613 0.5200 0.0165  -0.0040 -0.0605 84   VAL A CB  
507   C CG1 . VAL A 86   ? 0.4636 0.4512 0.5091 0.0170  -0.0031 -0.0585 84   VAL A CG1 
508   C CG2 . VAL A 86   ? 0.4839 0.4751 0.5229 0.0146  -0.0023 -0.0572 84   VAL A CG2 
509   N N   . GLU A 87   ? 0.4126 0.4000 0.4820 0.0208  -0.0092 -0.0725 85   GLU A N   
510   C CA  . GLU A 87   ? 0.4560 0.4414 0.5345 0.0228  -0.0112 -0.0760 85   GLU A CA  
511   C C   . GLU A 87   ? 0.4242 0.4177 0.5064 0.0245  -0.0125 -0.0851 85   GLU A C   
512   O O   . GLU A 87   ? 0.4301 0.4257 0.5153 0.0261  -0.0130 -0.0882 85   GLU A O   
513   C CB  . GLU A 87   ? 0.4962 0.4739 0.5838 0.0230  -0.0133 -0.0743 85   GLU A CB  
514   N N   . GLY A 88   ? 0.3766 0.3752 0.4587 0.0243  -0.0131 -0.0895 86   GLY A N   
515   C CA  . GLY A 88   ? 0.3409 0.3484 0.4264 0.0260  -0.0143 -0.0986 86   GLY A CA  
516   C C   . GLY A 88   ? 0.3411 0.3572 0.4187 0.0259  -0.0123 -0.0998 86   GLY A C   
517   O O   . GLY A 88   ? 0.3676 0.3898 0.4486 0.0277  -0.0131 -0.1062 86   GLY A O   
518   N N   . LEU A 89   ? 0.3426 0.3593 0.4101 0.0237  -0.0098 -0.0936 87   LEU A N   
519   C CA  . LEU A 89   ? 0.3184 0.3428 0.3783 0.0233  -0.0078 -0.0935 87   LEU A CA  
520   C C   . LEU A 89   ? 0.2970 0.3187 0.3587 0.0243  -0.0076 -0.0924 87   LEU A C   
521   O O   . LEU A 89   ? 0.2922 0.3210 0.3542 0.0255  -0.0075 -0.0970 87   LEU A O   
522   C CB  . LEU A 89   ? 0.3395 0.3635 0.3895 0.0206  -0.0055 -0.0864 87   LEU A CB  
523   C CG  . LEU A 89   ? 0.4465 0.4781 0.4881 0.0194  -0.0035 -0.0847 87   LEU A CG  
524   C CD1 . LEU A 89   ? 0.4407 0.4843 0.4822 0.0202  -0.0038 -0.0918 87   LEU A CD1 
525   C CD2 . LEU A 89   ? 0.4431 0.4727 0.4767 0.0169  -0.0018 -0.0777 87   LEU A CD2 
526   N N   . VAL A 90   ? 0.3120 0.3238 0.3748 0.0240  -0.0075 -0.0863 88   VAL A N   
527   C CA  . VAL A 90   ? 0.3198 0.3283 0.3851 0.0250  -0.0076 -0.0849 88   VAL A CA  
528   C C   . VAL A 90   ? 0.3152 0.3259 0.3902 0.0277  -0.0099 -0.0924 88   VAL A C   
529   O O   . VAL A 90   ? 0.3184 0.3327 0.3941 0.0289  -0.0097 -0.0947 88   VAL A O   
530   C CB  . VAL A 90   ? 0.3191 0.3168 0.3851 0.0243  -0.0075 -0.0775 88   VAL A CB  
531   C CG1 . VAL A 90   ? 0.3675 0.3615 0.4383 0.0257  -0.0082 -0.0767 88   VAL A CG1 
532   C CG2 . VAL A 90   ? 0.3371 0.3334 0.3932 0.0220  -0.0051 -0.0705 88   VAL A CG2 
533   N N   . GLN A 91   ? 0.3453 0.3541 0.4285 0.0287  -0.0122 -0.0965 89   GLN A N   
534   C CA  . GLN A 91   ? 0.3551 0.3657 0.4488 0.0314  -0.0148 -0.1042 89   GLN A CA  
535   C C   . GLN A 91   ? 0.3561 0.3788 0.4482 0.0325  -0.0145 -0.1121 89   GLN A C   
536   O O   . GLN A 91   ? 0.3623 0.3885 0.4583 0.0345  -0.0152 -0.1166 89   GLN A O   
537   C CB  . GLN A 91   ? 0.3750 0.3808 0.4782 0.0320  -0.0175 -0.1066 89   GLN A CB  
538   N N   . GLU A 92   ? 0.3130 0.3427 0.3993 0.0314  -0.0136 -0.1139 90   GLU A N   
539   C CA  . GLU A 92   ? 0.3128 0.3552 0.3982 0.0325  -0.0135 -0.1219 90   GLU A CA  
540   C C   . GLU A 92   ? 0.3201 0.3687 0.3997 0.0325  -0.0115 -0.1211 90   GLU A C   
541   O O   . GLU A 92   ? 0.3216 0.3786 0.4043 0.0345  -0.0121 -0.1282 90   GLU A O   
542   C CB  . GLU A 92   ? 0.3237 0.3725 0.4030 0.0309  -0.0127 -0.1224 90   GLU A CB  
543   C CG  . GLU A 92   ? 0.3445 0.4080 0.4211 0.0317  -0.0122 -0.1296 90   GLU A CG  
544   C CD  . GLU A 92   ? 0.4334 0.5037 0.5040 0.0301  -0.0115 -0.1297 90   GLU A CD  
545   O OE1 . GLU A 92   ? 0.4817 0.5450 0.5496 0.0282  -0.0111 -0.1239 90   GLU A OE1 
546   O OE2 . GLU A 92   ? 0.4553 0.5384 0.5240 0.0307  -0.0113 -0.1357 90   GLU A OE2 
547   N N   . TYR A 93   ? 0.3132 0.3579 0.3849 0.0304  -0.0093 -0.1127 91   TYR A N   
548   C CA  . TYR A 93   ? 0.3222 0.3724 0.3879 0.0300  -0.0073 -0.1111 91   TYR A CA  
549   C C   . TYR A 93   ? 0.3004 0.3430 0.3687 0.0307  -0.0074 -0.1075 91   TYR A C   
550   O O   . TYR A 93   ? 0.2923 0.3379 0.3555 0.0301  -0.0057 -0.1049 91   TYR A O   
551   C CB  . TYR A 93   ? 0.2895 0.3429 0.3441 0.0271  -0.0048 -0.1050 91   TYR A CB  
552   C CG  . TYR A 93   ? 0.3004 0.3642 0.3520 0.0265  -0.0045 -0.1091 91   TYR A CG  
553   C CD1 . TYR A 93   ? 0.2826 0.3595 0.3322 0.0271  -0.0039 -0.1141 91   TYR A CD1 
554   C CD2 . TYR A 93   ? 0.3311 0.3922 0.3823 0.0255  -0.0051 -0.1081 91   TYR A CD2 
555   C CE1 . TYR A 93   ? 0.3012 0.3886 0.3480 0.0266  -0.0037 -0.1178 91   TYR A CE1 
556   C CE2 . TYR A 93   ? 0.3541 0.4252 0.4027 0.0250  -0.0051 -0.1118 91   TYR A CE2 
557   C CZ  . TYR A 93   ? 0.3027 0.3870 0.3489 0.0256  -0.0044 -0.1166 91   TYR A CZ  
558   O OH  . TYR A 93   ? 0.3909 0.4862 0.4344 0.0251  -0.0043 -0.1203 91   TYR A OH  
559   N N   . SER A 94   ? 0.2820 0.3154 0.3587 0.0320  -0.0095 -0.1073 92   SER A N   
560   C CA  . SER A 94   ? 0.2945 0.3208 0.3747 0.0328  -0.0100 -0.1041 92   SER A CA  
561   C C   . SER A 94   ? 0.2537 0.2765 0.3248 0.0306  -0.0075 -0.0954 92   SER A C   
562   O O   . SER A 94   ? 0.2919 0.3153 0.3614 0.0310  -0.0068 -0.0939 92   SER A O   
563   C CB  . SER A 94   ? 0.3106 0.3430 0.3964 0.0354  -0.0110 -0.1108 92   SER A CB  
564   O OG  . SER A 94   ? 0.3780 0.4145 0.4723 0.0375  -0.0133 -0.1195 92   SER A OG  
565   N N   . LEU A 95   ? 0.2313 0.2506 0.2966 0.0284  -0.0064 -0.0900 93   LEU A N   
566   C CA  . LEU A 95   ? 0.2533 0.2695 0.3100 0.0263  -0.0042 -0.0823 93   LEU A CA  
567   C C   . LEU A 95   ? 0.2504 0.2565 0.3099 0.0266  -0.0048 -0.0769 93   LEU A C   
568   O O   . LEU A 95   ? 0.2710 0.2706 0.3368 0.0272  -0.0064 -0.0763 93   LEU A O   
569   C CB  . LEU A 95   ? 0.2209 0.2367 0.2710 0.0240  -0.0030 -0.0785 93   LEU A CB  
570   C CG  . LEU A 95   ? 0.2064 0.2324 0.2531 0.0234  -0.0025 -0.0829 93   LEU A CG  
571   C CD1 . LEU A 95   ? 0.2631 0.2877 0.3031 0.0210  -0.0013 -0.0780 93   LEU A CD1 
572   C CD2 . LEU A 95   ? 0.2521 0.2871 0.2946 0.0234  -0.0012 -0.0846 93   LEU A CD2 
573   N N   . SER A 96   ? 0.2343 0.2396 0.2892 0.0260  -0.0035 -0.0727 94   SER A N   
574   C CA  . SER A 96   ? 0.2264 0.2229 0.2813 0.0256  -0.0034 -0.0662 94   SER A CA  
575   C C   . SER A 96   ? 0.2420 0.2344 0.2912 0.0235  -0.0023 -0.0607 94   SER A C   
576   O O   . SER A 96   ? 0.2389 0.2353 0.2835 0.0222  -0.0014 -0.0614 94   SER A O   
577   C CB  . SER A 96   ? 0.2437 0.2411 0.2943 0.0254  -0.0023 -0.0634 94   SER A CB  
578   O OG  . SER A 96   ? 0.2226 0.2241 0.2642 0.0234  -0.0002 -0.0612 94   SER A OG  
579   N N   . SER A 97   ? 0.2531 0.2379 0.3027 0.0232  -0.0024 -0.0550 95   SER A N   
580   C CA  . SER A 97   ? 0.2572 0.2382 0.3016 0.0214  -0.0013 -0.0498 95   SER A CA  
581   C C   . SER A 97   ? 0.2196 0.2042 0.2546 0.0197  0.0008  -0.0475 95   SER A C   
582   O O   . SER A 97   ? 0.2181 0.2039 0.2488 0.0182  0.0016  -0.0464 95   SER A O   
583   C CB  . SER A 97   ? 0.3102 0.2836 0.3564 0.0215  -0.0016 -0.0441 95   SER A CB  
584   O OG  . SER A 97   ? 0.4193 0.3891 0.4742 0.0226  -0.0035 -0.0452 95   SER A OG  
585   N N   . GLN A 98   ? 0.2059 0.1923 0.2382 0.0198  0.0015  -0.0466 96   GLN A N   
586   C CA  . GLN A 98   ? 0.2134 0.2031 0.2376 0.0180  0.0032  -0.0442 96   GLN A CA  
587   C C   . GLN A 98   ? 0.1949 0.1925 0.2170 0.0173  0.0036  -0.0481 96   GLN A C   
588   O O   . GLN A 98   ? 0.2112 0.2108 0.2275 0.0155  0.0047  -0.0457 96   GLN A O   
589   C CB  . GLN A 98   ? 0.2275 0.2178 0.2499 0.0183  0.0037  -0.0428 96   GLN A CB  
590   C CG  . GLN A 98   ? 0.2179 0.2011 0.2401 0.0185  0.0036  -0.0376 96   GLN A CG  
591   C CD  . GLN A 98   ? 0.2334 0.2135 0.2498 0.0168  0.0047  -0.0328 96   GLN A CD  
592   O OE1 . GLN A 98   ? 0.2574 0.2343 0.2746 0.0165  0.0045  -0.0316 96   GLN A OE1 
593   N NE2 . GLN A 98   ? 0.2624 0.2433 0.2733 0.0157  0.0057  -0.0302 96   GLN A NE2 
594   N N   . GLU A 99   ? 0.1982 0.2009 0.2251 0.0188  0.0027  -0.0541 97   GLU A N   
595   C CA  . GLU A 99   ? 0.1915 0.2028 0.2167 0.0182  0.0030  -0.0582 97   GLU A CA  
596   C C   . GLU A 99   ? 0.2138 0.2242 0.2382 0.0173  0.0029  -0.0578 97   GLU A C   
597   O O   . GLU A 99   ? 0.2021 0.2173 0.2212 0.0157  0.0038  -0.0570 97   GLU A O   
598   C CB  . GLU A 99   ? 0.1856 0.2026 0.2168 0.0203  0.0019  -0.0652 97   GLU A CB  
599   C CG  . GLU A 99   ? 0.1873 0.2080 0.2179 0.0209  0.0024  -0.0658 97   GLU A CG  
600   C CD  . GLU A 99   ? 0.2231 0.2484 0.2606 0.0233  0.0011  -0.0728 97   GLU A CD  
601   O OE1 . GLU A 99   ? 0.2161 0.2408 0.2596 0.0247  -0.0004 -0.0771 97   GLU A OE1 
602   O OE2 . GLU A 99   ? 0.2307 0.2601 0.2682 0.0239  0.0015  -0.0740 97   GLU A OE2 
603   N N   . GLY A 100  ? 0.2020 0.2062 0.2318 0.0182  0.0016  -0.0581 98   GLY A N   
604   C CA  . GLY A 100  ? 0.1971 0.1998 0.2264 0.0173  0.0014  -0.0574 98   GLY A CA  
605   C C   . GLY A 100  ? 0.2177 0.2179 0.2398 0.0152  0.0028  -0.0513 98   GLY A C   
606   O O   . GLY A 100  ? 0.2155 0.2190 0.2340 0.0139  0.0033  -0.0510 98   GLY A O   
607   N N   . VAL A 101  ? 0.1991 0.1934 0.2193 0.0149  0.0035  -0.0463 99   VAL A N   
608   C CA  . VAL A 101  ? 0.1973 0.1890 0.2112 0.0131  0.0047  -0.0408 99   VAL A CA  
609   C C   . VAL A 101  ? 0.2048 0.2032 0.2129 0.0116  0.0057  -0.0405 99   VAL A C   
610   O O   . VAL A 101  ? 0.2152 0.2149 0.2194 0.0100  0.0062  -0.0385 99   VAL A O   
611   C CB  . VAL A 101  ? 0.2083 0.1935 0.2215 0.0134  0.0050  -0.0363 99   VAL A CB  
612   C CG1 . VAL A 101  ? 0.2290 0.2125 0.2358 0.0117  0.0062  -0.0314 99   VAL A CG1 
613   C CG2 . VAL A 101  ? 0.2380 0.2168 0.2567 0.0145  0.0040  -0.0354 99   VAL A CG2 
614   N N   . ALA A 102  ? 0.1885 0.1915 0.1964 0.0120  0.0059  -0.0424 100  ALA A N   
615   C CA  . ALA A 102  ? 0.2041 0.2139 0.2069 0.0105  0.0069  -0.0416 100  ALA A CA  
616   C C   . ALA A 102  ? 0.1833 0.2004 0.1853 0.0097  0.0068  -0.0445 100  ALA A C   
617   O O   . ALA A 102  ? 0.2161 0.2367 0.2135 0.0078  0.0074  -0.0418 100  ALA A O   
618   C CB  . ALA A 102  ? 0.2096 0.2236 0.2131 0.0112  0.0071  -0.0436 100  ALA A CB  
619   N N   . LEU A 103  ? 0.1814 0.2012 0.1883 0.0113  0.0058  -0.0500 101  LEU A N   
620   C CA  . LEU A 103  ? 0.1909 0.2181 0.1974 0.0109  0.0056  -0.0533 101  LEU A CA  
621   C C   . LEU A 103  ? 0.2022 0.2261 0.2061 0.0094  0.0056  -0.0498 101  LEU A C   
622   O O   . LEU A 103  ? 0.2275 0.2574 0.2276 0.0078  0.0060  -0.0489 101  LEU A O   
623   C CB  . LEU A 103  ? 0.1919 0.2211 0.2052 0.0131  0.0042  -0.0601 101  LEU A CB  
624   C CG  . LEU A 103  ? 0.2161 0.2530 0.2295 0.0128  0.0037  -0.0642 101  LEU A CG  
625   C CD1 . LEU A 103  ? 0.2308 0.2792 0.2395 0.0117  0.0047  -0.0651 101  LEU A CD1 
626   C CD2 . LEU A 103  ? 0.2395 0.2770 0.2604 0.0152  0.0021  -0.0710 101  LEU A CD2 
627   N N   . MET A 104  ? 0.1916 0.2063 0.1976 0.0098  0.0052  -0.0474 102  MET A N   
628   C CA  . MET A 104  ? 0.2152 0.2270 0.2191 0.0085  0.0053  -0.0443 102  MET A CA  
629   C C   . MET A 104  ? 0.2209 0.2323 0.2187 0.0065  0.0064  -0.0387 102  MET A C   
630   O O   . MET A 104  ? 0.2347 0.2480 0.2296 0.0051  0.0065  -0.0367 102  MET A O   
631   C CB  . MET A 104  ? 0.2314 0.2343 0.2393 0.0094  0.0046  -0.0431 102  MET A CB  
632   C CG  . MET A 104  ? 0.2350 0.2381 0.2500 0.0113  0.0032  -0.0486 102  MET A CG  
633   S SD  . MET A 104  ? 0.3250 0.3371 0.3410 0.0112  0.0024  -0.0544 102  MET A SD  
634   C CE  . MET A 104  ? 0.3375 0.3460 0.3508 0.0096  0.0025  -0.0502 102  MET A CE  
635   N N   . CYS A 105  ? 0.1966 0.2056 0.1926 0.0064  0.0070  -0.0361 103  CYS A N   
636   C CA  . CYS A 105  ? 0.2049 0.2138 0.1959 0.0045  0.0077  -0.0311 103  CYS A CA  
637   C C   . CYS A 105  ? 0.2579 0.2764 0.2460 0.0030  0.0080  -0.0316 103  CYS A C   
638   O O   . CYS A 105  ? 0.2561 0.2758 0.2409 0.0012  0.0081  -0.0281 103  CYS A O   
639   C CB  . CYS A 105  ? 0.2243 0.2295 0.2146 0.0049  0.0082  -0.0290 103  CYS A CB  
640   S SG  . CYS A 105  ? 0.2506 0.2453 0.2431 0.0062  0.0080  -0.0268 103  CYS A SG  
641   N N   . LEU A 106  ? 0.2197 0.2453 0.2092 0.0038  0.0080  -0.0359 104  LEU A N   
642   C CA  . LEU A 106  ? 0.2371 0.2733 0.2241 0.0024  0.0083  -0.0366 104  LEU A CA  
643   C C   . LEU A 106  ? 0.2576 0.2972 0.2441 0.0018  0.0078  -0.0374 104  LEU A C   
644   O O   . LEU A 106  ? 0.2449 0.2898 0.2280 -0.0002 0.0080  -0.0345 104  LEU A O   
645   C CB  . LEU A 106  ? 0.2374 0.2812 0.2267 0.0038  0.0083  -0.0420 104  LEU A CB  
646   C CG  . LEU A 106  ? 0.2381 0.2945 0.2251 0.0026  0.0086  -0.0435 104  LEU A CG  
647   C CD1 . LEU A 106  ? 0.3038 0.3634 0.2864 0.0001  0.0093  -0.0378 104  LEU A CD1 
648   C CD2 . LEU A 106  ? 0.2708 0.3348 0.2608 0.0044  0.0085  -0.0499 104  LEU A CD2 
649   N N   . ALA A 107  ? 0.2228 0.2597 0.2131 0.0034  0.0070  -0.0412 105  ALA A N   
650   C CA  . ALA A 107  ? 0.2443 0.2846 0.2345 0.0029  0.0065  -0.0424 105  ALA A CA  
651   C C   . ALA A 107  ? 0.2867 0.3222 0.2737 0.0011  0.0066  -0.0365 105  ALA A C   
652   O O   . ALA A 107  ? 0.2710 0.3122 0.2554 -0.0005 0.0065  -0.0349 105  ALA A O   
653   C CB  . ALA A 107  ? 0.2226 0.2597 0.2183 0.0049  0.0054  -0.0474 105  ALA A CB  
654   N N   . GLU A 108  ? 0.2502 0.2757 0.2376 0.0013  0.0068  -0.0331 106  GLU A N   
655   C CA  . GLU A 108  ? 0.2696 0.2902 0.2543 -0.0002 0.0069  -0.0277 106  GLU A CA  
656   C C   . GLU A 108  ? 0.3282 0.3540 0.3089 -0.0023 0.0072  -0.0238 106  GLU A C   
657   O O   . GLU A 108  ? 0.3286 0.3560 0.3073 -0.0039 0.0069  -0.0208 106  GLU A O   
658   C CB  . GLU A 108  ? 0.2920 0.3024 0.2777 0.0007  0.0071  -0.0252 106  GLU A CB  
659   C CG  . GLU A 108  ? 0.3196 0.3247 0.3028 -0.0006 0.0072  -0.0199 106  GLU A CG  
660   C CD  . GLU A 108  ? 0.3400 0.3375 0.3233 0.0001  0.0076  -0.0174 106  GLU A CD  
661   O OE1 . GLU A 108  ? 0.3329 0.3276 0.3185 0.0016  0.0078  -0.0195 106  GLU A OE1 
662   O OE2 . GLU A 108  ? 0.3671 0.3616 0.3481 -0.0010 0.0077  -0.0134 106  GLU A OE2 
663   N N   . ALA A 109  ? 0.2903 0.3189 0.2700 -0.0025 0.0077  -0.0235 107  ALA A N   
664   C CA  . ALA A 109  ? 0.3014 0.3351 0.2780 -0.0047 0.0079  -0.0195 107  ALA A CA  
665   C C   . ALA A 109  ? 0.3370 0.3817 0.3121 -0.0060 0.0077  -0.0204 107  ALA A C   
666   O O   . ALA A 109  ? 0.3584 0.4062 0.3313 -0.0081 0.0074  -0.0161 107  ALA A O   
667   C CB  . ALA A 109  ? 0.3242 0.3589 0.3006 -0.0046 0.0084  -0.0195 107  ALA A CB  
668   N N   . LEU A 110  ? 0.2856 0.3368 0.2624 -0.0047 0.0077  -0.0261 108  LEU A N   
669   C CA  . LEU A 110  ? 0.2822 0.3451 0.2576 -0.0056 0.0075  -0.0276 108  LEU A CA  
670   C C   . LEU A 110  ? 0.3290 0.3910 0.3038 -0.0064 0.0068  -0.0261 108  LEU A C   
671   O O   . LEU A 110  ? 0.3576 0.4280 0.3302 -0.0081 0.0066  -0.0241 108  LEU A O   
672   C CB  . LEU A 110  ? 0.2777 0.3471 0.2556 -0.0036 0.0075  -0.0350 108  LEU A CB  
673   C CG  . LEU A 110  ? 0.3035 0.3773 0.2817 -0.0031 0.0082  -0.0366 108  LEU A CG  
674   C CD1 . LEU A 110  ? 0.2789 0.3567 0.2608 -0.0006 0.0080  -0.0443 108  LEU A CD1 
675   C CD2 . LEU A 110  ? 0.3384 0.4234 0.3131 -0.0054 0.0087  -0.0334 108  LEU A CD2 
676   N N   . LEU A 111  ? 0.3097 0.3621 0.2866 -0.0052 0.0064  -0.0266 109  LEU A N   
677   C CA  . LEU A 111  ? 0.3475 0.3984 0.3241 -0.0058 0.0057  -0.0251 109  LEU A CA  
678   C C   . LEU A 111  ? 0.4252 0.4724 0.3994 -0.0078 0.0056  -0.0182 109  LEU A C   
679   O O   . LEU A 111  ? 0.4295 0.4770 0.4031 -0.0087 0.0049  -0.0163 109  LEU A O   
680   C CB  . LEU A 111  ? 0.3393 0.3818 0.3195 -0.0039 0.0053  -0.0281 109  LEU A CB  
681   C CG  . LEU A 111  ? 0.3184 0.3655 0.3020 -0.0020 0.0050  -0.0353 109  LEU A CG  
682   C CD1 . LEU A 111  ? 0.3571 0.3950 0.3452 -0.0001 0.0045  -0.0377 109  LEU A CD1 
683   C CD2 . LEU A 111  ? 0.3362 0.3933 0.3190 -0.0025 0.0043  -0.0379 109  LEU A CD2 
684   N N   . ARG A 112  ? 0.4028 0.4465 0.3760 -0.0085 0.0060  -0.0146 110  ARG A N   
685   C CA  . ARG A 112  ? 0.4438 0.4854 0.4152 -0.0106 0.0056  -0.0082 110  ARG A CA  
686   C C   . ARG A 112  ? 0.5002 0.5526 0.4695 -0.0129 0.0053  -0.0055 110  ARG A C   
687   O O   . ARG A 112  ? 0.5087 0.5605 0.4771 -0.0148 0.0046  -0.0001 110  ARG A O   
688   C CB  . ARG A 112  ? 0.4093 0.4437 0.3808 -0.0105 0.0059  -0.0056 110  ARG A CB  
689   C CG  . ARG A 112  ? 0.4078 0.4314 0.3812 -0.0086 0.0062  -0.0069 110  ARG A CG  
690   C CD  . ARG A 112  ? 0.4709 0.4897 0.4443 -0.0081 0.0067  -0.0061 110  ARG A CD  
691   N NE  . ARG A 112  ? 0.5541 0.5701 0.5266 -0.0096 0.0062  -0.0010 110  ARG A NE  
692   C CZ  . ARG A 112  ? 0.6845 0.6924 0.6574 -0.0094 0.0059  0.0014  110  ARG A CZ  
693   N NH1 . ARG A 112  ? 0.6591 0.6611 0.6331 -0.0078 0.0061  -0.0004 110  ARG A NH1 
694   N NH2 . ARG A 112  ? 0.7087 0.7147 0.6814 -0.0108 0.0052  0.0055  110  ARG A NH2 
695   N N   . ILE A 113  ? 0.4531 0.5157 0.4219 -0.0127 0.0057  -0.0091 111  ILE A N   
696   C CA  . ILE A 113  ? 0.4588 0.5337 0.4256 -0.0147 0.0054  -0.0070 111  ILE A CA  
697   C C   . ILE A 113  ? 0.4757 0.5542 0.4422 -0.0148 0.0047  -0.0082 111  ILE A C   
698   O O   . ILE A 113  ? 0.5210 0.6014 0.4887 -0.0129 0.0047  -0.0142 111  ILE A O   
699   C CB  . ILE A 113  ? 0.4159 0.5010 0.3822 -0.0143 0.0062  -0.0108 111  ILE A CB  
700   C CG1 . ILE A 113  ? 0.4219 0.5042 0.3883 -0.0148 0.0068  -0.0086 111  ILE A CG1 
701   C CG2 . ILE A 113  ? 0.5006 0.6000 0.4648 -0.0162 0.0060  -0.0095 111  ILE A CG2 
702   C CD1 . ILE A 113  ? 0.4399 0.5303 0.4065 -0.0138 0.0077  -0.0131 111  ILE A CD1 
703   N N   . PRO A 114  ? 0.5829 0.6625 0.5483 -0.0168 0.0038  -0.0028 112  PRO A N   
704   C CA  . PRO A 114  ? 0.5110 0.5926 0.4764 -0.0168 0.0030  -0.0037 112  PRO A CA  
705   C C   . PRO A 114  ? 0.5073 0.6028 0.4714 -0.0168 0.0029  -0.0073 112  PRO A C   
706   O O   . PRO A 114  ? 0.6109 0.7072 0.5761 -0.0153 0.0026  -0.0126 112  PRO A O   
707   C CB  . PRO A 114  ? 0.5234 0.6026 0.4882 -0.0190 0.0019  0.0038  112  PRO A CB  
708   C CG  . PRO A 114  ? 0.6033 0.6747 0.5688 -0.0195 0.0022  0.0075  112  PRO A CG  
709   C CD  . PRO A 114  ? 0.5832 0.6597 0.5481 -0.0190 0.0033  0.0045  112  PRO A CD  
710   N N   . ASP A 115  ? 0.6081 0.7150 0.5702 -0.0187 0.0030  -0.0047 113  ASP A N   
711   C CA  . ASP A 115  ? 0.5924 0.7141 0.5529 -0.0189 0.0030  -0.0078 113  ASP A CA  
712   C C   . ASP A 115  ? 0.5638 0.6889 0.5256 -0.0164 0.0038  -0.0164 113  ASP A C   
713   O O   . ASP A 115  ? 0.5492 0.6738 0.5113 -0.0158 0.0047  -0.0176 113  ASP A O   
714   C CB  . ASP A 115  ? 0.5441 0.6774 0.5023 -0.0217 0.0030  -0.0022 113  ASP A CB  
715   N N   . THR A 116  ? 0.5549 0.6836 0.5176 -0.0148 0.0033  -0.0224 114  THR A N   
716   C CA  . THR A 116  ? 0.4797 0.6105 0.4447 -0.0121 0.0037  -0.0310 114  THR A CA  
717   C C   . THR A 116  ? 0.5509 0.6956 0.5144 -0.0123 0.0045  -0.0334 114  THR A C   
718   O O   . THR A 116  ? 0.4734 0.6171 0.4387 -0.0106 0.0052  -0.0377 114  THR A O   
719   C CB  . THR A 116  ? 0.5099 0.6427 0.4767 -0.0106 0.0027  -0.0368 114  THR A CB  
720   O OG1 . THR A 116  ? 0.5884 0.7076 0.5571 -0.0101 0.0021  -0.0352 114  THR A OG1 
721   C CG2 . THR A 116  ? 0.5433 0.6796 0.5132 -0.0078 0.0027  -0.0462 114  THR A CG2 
722   N N   . ALA A 117  ? 0.4834 0.6417 0.4439 -0.0143 0.0044  -0.0304 115  ALA A N   
723   C CA  . ALA A 117  ? 0.4859 0.6588 0.4448 -0.0146 0.0052  -0.0323 115  ALA A CA  
724   C C   . ALA A 117  ? 0.4582 0.6274 0.4167 -0.0157 0.0062  -0.0278 115  ALA A C   
725   O O   . ALA A 117  ? 0.4333 0.6088 0.3923 -0.0147 0.0071  -0.0316 115  ALA A O   
726   C CB  . ALA A 117  ? 0.5258 0.7144 0.4812 -0.0168 0.0048  -0.0290 115  ALA A CB  
727   N N   . THR A 118  ? 0.4505 0.6098 0.4086 -0.0176 0.0060  -0.0200 116  THR A N   
728   C CA  . THR A 118  ? 0.4620 0.6169 0.4202 -0.0186 0.0067  -0.0159 116  THR A CA  
729   C C   . THR A 118  ? 0.4214 0.5666 0.3824 -0.0158 0.0073  -0.0214 116  THR A C   
730   O O   . THR A 118  ? 0.4531 0.6012 0.4144 -0.0155 0.0082  -0.0226 116  THR A O   
731   C CB  . THR A 118  ? 0.4572 0.6025 0.4152 -0.0209 0.0060  -0.0072 116  THR A CB  
732   O OG1 . THR A 118  ? 0.6109 0.7650 0.5669 -0.0234 0.0051  -0.0018 116  THR A OG1 
733   C CG2 . THR A 118  ? 0.4653 0.6076 0.4237 -0.0221 0.0065  -0.0029 116  THR A CG2 
734   N N   . ARG A 119  ? 0.4181 0.5518 0.3812 -0.0139 0.0068  -0.0246 117  ARG A N   
735   C CA  . ARG A 119  ? 0.4247 0.5489 0.3909 -0.0113 0.0072  -0.0294 117  ARG A CA  
736   C C   . ARG A 119  ? 0.3871 0.5206 0.3547 -0.0092 0.0077  -0.0373 117  ARG A C   
737   O O   . ARG A 119  ? 0.3975 0.5295 0.3665 -0.0082 0.0084  -0.0393 117  ARG A O   
738   C CB  . ARG A 119  ? 0.4010 0.5130 0.3695 -0.0098 0.0065  -0.0311 117  ARG A CB  
739   C CG  . ARG A 119  ? 0.3526 0.4539 0.3245 -0.0073 0.0067  -0.0351 117  ARG A CG  
740   C CD  . ARG A 119  ? 0.3876 0.4801 0.3622 -0.0058 0.0059  -0.0377 117  ARG A CD  
741   N NE  . ARG A 119  ? 0.4154 0.5022 0.3885 -0.0074 0.0054  -0.0320 117  ARG A NE  
742   C CZ  . ARG A 119  ? 0.3756 0.4640 0.3488 -0.0076 0.0046  -0.0327 117  ARG A CZ  
743   N NH1 . ARG A 119  ? 0.4252 0.5205 0.4001 -0.0062 0.0040  -0.0391 117  ARG A NH1 
744   N NH2 . ARG A 119  ? 0.5233 0.6063 0.4952 -0.0090 0.0041  -0.0271 117  ARG A NH2 
745   N N   . ASP A 120  ? 0.4196 0.5632 0.3872 -0.0085 0.0072  -0.0421 118  ASP A N   
746   C CA  . ASP A 120  ? 0.4082 0.5614 0.3778 -0.0063 0.0074  -0.0505 118  ASP A CA  
747   C C   . ASP A 120  ? 0.4441 0.6088 0.4118 -0.0073 0.0085  -0.0495 118  ASP A C   
748   O O   . ASP A 120  ? 0.4307 0.5983 0.4007 -0.0053 0.0090  -0.0550 118  ASP A O   
749   C CB  . ASP A 120  ? 0.4028 0.5655 0.3726 -0.0055 0.0065  -0.0557 118  ASP A CB  
750   C CG  . ASP A 120  ? 0.4980 0.6495 0.4703 -0.0044 0.0054  -0.0573 118  ASP A CG  
751   O OD1 . ASP A 120  ? 0.5071 0.6439 0.4810 -0.0042 0.0054  -0.0543 118  ASP A OD1 
752   O OD2 . ASP A 120  ? 0.4983 0.6560 0.4713 -0.0037 0.0044  -0.0615 118  ASP A OD2 
753   N N   . ALA A 121  ? 0.4602 0.6317 0.4241 -0.0104 0.0089  -0.0421 119  ALA A N   
754   C CA  . ALA A 121  ? 0.4632 0.6460 0.4254 -0.0117 0.0099  -0.0401 119  ALA A CA  
755   C C   . ALA A 121  ? 0.4280 0.6011 0.3916 -0.0115 0.0106  -0.0380 119  ALA A C   
756   O O   . ALA A 121  ? 0.4834 0.6629 0.4479 -0.0107 0.0114  -0.0411 119  ALA A O   
757   C CB  . ALA A 121  ? 0.4212 0.6128 0.3797 -0.0153 0.0099  -0.0319 119  ALA A CB  
758   N N   . LEU A 122  ? 0.4850 0.6430 0.4490 -0.0122 0.0102  -0.0330 120  LEU A N   
759   C CA  . LEU A 122  ? 0.4469 0.5950 0.4124 -0.0118 0.0107  -0.0314 120  LEU A CA  
760   C C   . LEU A 122  ? 0.4337 0.5781 0.4027 -0.0084 0.0108  -0.0395 120  LEU A C   
761   O O   . LEU A 122  ? 0.4333 0.5784 0.4034 -0.0077 0.0115  -0.0408 120  LEU A O   
762   C CB  . LEU A 122  ? 0.4653 0.5983 0.4308 -0.0128 0.0100  -0.0255 120  LEU A CB  
763   C CG  . LEU A 122  ? 0.4013 0.5253 0.3676 -0.0131 0.0104  -0.0222 120  LEU A CG  
764   C CD1 . LEU A 122  ? 0.4869 0.6191 0.4515 -0.0160 0.0108  -0.0163 120  LEU A CD1 
765   C CD2 . LEU A 122  ? 0.4138 0.5223 0.3807 -0.0131 0.0097  -0.0187 120  LEU A CD2 
766   N N   . ILE A 123  ? 0.4135 0.5540 0.3847 -0.0062 0.0101  -0.0449 121  ILE A N   
767   C CA  . ILE A 123  ? 0.4225 0.5593 0.3979 -0.0030 0.0099  -0.0526 121  ILE A CA  
768   C C   . ILE A 123  ? 0.4391 0.5902 0.4153 -0.0019 0.0105  -0.0584 121  ILE A C   
769   O O   . ILE A 123  ? 0.4242 0.5744 0.4025 -0.0005 0.0110  -0.0609 121  ILE A O   
770   C CB  . ILE A 123  ? 0.3926 0.5238 0.3708 -0.0012 0.0088  -0.0571 121  ILE A CB  
771   C CG1 . ILE A 123  ? 0.3484 0.4643 0.3266 -0.0018 0.0083  -0.0519 121  ILE A CG1 
772   C CG2 . ILE A 123  ? 0.3619 0.4926 0.3453 0.0022  0.0083  -0.0658 121  ILE A CG2 
773   C CD1 . ILE A 123  ? 0.3433 0.4547 0.3238 -0.0007 0.0072  -0.0550 121  ILE A CD1 
774   N N   . ARG A 124  ? 0.4339 0.5989 0.4084 -0.0023 0.0104  -0.0608 122  ARG A N   
775   C CA  . ARG A 124  ? 0.3825 0.5622 0.3581 -0.0008 0.0109  -0.0677 122  ARG A CA  
776   C C   . ARG A 124  ? 0.4676 0.6551 0.4412 -0.0024 0.0122  -0.0641 122  ARG A C   
777   O O   . ARG A 124  ? 0.5093 0.7019 0.4853 -0.0005 0.0126  -0.0693 122  ARG A O   
778   C CB  . ARG A 124  ? 0.4313 0.6249 0.4052 -0.0011 0.0105  -0.0707 122  ARG A CB  
779   N N   . ASP A 125  ? 0.5086 0.6968 0.4783 -0.0057 0.0126  -0.0551 123  ASP A N   
780   C CA  . ASP A 125  ? 0.5759 0.7738 0.5437 -0.0077 0.0138  -0.0512 123  ASP A CA  
781   C C   . ASP A 125  ? 0.5807 0.7672 0.5492 -0.0084 0.0141  -0.0464 123  ASP A C   
782   O O   . ASP A 125  ? 0.6188 0.8123 0.5871 -0.0092 0.0150  -0.0452 123  ASP A O   
783   C CB  . ASP A 125  ? 0.6170 0.8255 0.5806 -0.0112 0.0139  -0.0441 123  ASP A CB  
784   C CG  . ASP A 125  ? 0.6408 0.8624 0.6031 -0.0107 0.0136  -0.0485 123  ASP A CG  
785   O OD1 . ASP A 125  ? 0.6575 0.8875 0.6218 -0.0080 0.0137  -0.0573 123  ASP A OD1 
786   O OD2 . ASP A 125  ? 0.6541 0.8779 0.6138 -0.0129 0.0130  -0.0434 123  ASP A OD2 
787   N N   . LYS A 126  ? 0.5369 0.7066 0.5064 -0.0081 0.0134  -0.0438 124  LYS A N   
788   C CA  . LYS A 126  ? 0.4965 0.6558 0.4664 -0.0090 0.0136  -0.0388 124  LYS A CA  
789   C C   . LYS A 126  ? 0.5328 0.6781 0.5061 -0.0062 0.0132  -0.0428 124  LYS A C   
790   O O   . LYS A 126  ? 0.5805 0.7235 0.5555 -0.0053 0.0137  -0.0439 124  LYS A O   
791   C CB  . LYS A 126  ? 0.5881 0.7410 0.5556 -0.0121 0.0131  -0.0299 124  LYS A CB  
792   C CG  . LYS A 126  ? 0.6146 0.7807 0.5791 -0.0153 0.0133  -0.0244 124  LYS A CG  
793   C CD  . LYS A 126  ? 0.6271 0.8032 0.5915 -0.0166 0.0142  -0.0226 124  LYS A CD  
794   C CE  . LYS A 126  ? 0.7086 0.8954 0.6705 -0.0204 0.0142  -0.0149 124  LYS A CE  
795   N NZ  . LYS A 126  ? 0.7223 0.9176 0.6845 -0.0221 0.0150  -0.0120 124  LYS A NZ  
796   N N   . ILE A 127  ? 0.4833 0.6193 0.4578 -0.0049 0.0124  -0.0446 125  ILE A N   
797   C CA  . ILE A 127  ? 0.4421 0.5646 0.4200 -0.0025 0.0119  -0.0472 125  ILE A CA  
798   C C   . ILE A 127  ? 0.4805 0.6070 0.4623 0.0005  0.0119  -0.0554 125  ILE A C   
799   O O   . ILE A 127  ? 0.5261 0.6470 0.5103 0.0018  0.0120  -0.0565 125  ILE A O   
800   C CB  . ILE A 127  ? 0.4271 0.5396 0.4056 -0.0021 0.0110  -0.0468 125  ILE A CB  
801   C CG1 . ILE A 127  ? 0.4769 0.5863 0.4518 -0.0050 0.0109  -0.0390 125  ILE A CG1 
802   C CG2 . ILE A 127  ? 0.4159 0.5147 0.3978 0.0001  0.0106  -0.0483 125  ILE A CG2 
803   C CD1 . ILE A 127  ? 0.4844 0.5873 0.4580 -0.0066 0.0112  -0.0327 125  ILE A CD1 
804   N N   . ALA A 128  ? 0.4033 0.5396 0.3863 0.0018  0.0116  -0.0615 126  ALA A N   
805   C CA  . ALA A 128  ? 0.4315 0.5717 0.4191 0.0049  0.0113  -0.0700 126  ALA A CA  
806   C C   . ALA A 128  ? 0.5179 0.6665 0.5056 0.0050  0.0123  -0.0710 126  ALA A C   
807   O O   . ALA A 128  ? 0.4910 0.6374 0.4829 0.0075  0.0120  -0.0758 126  ALA A O   
808   C CB  . ALA A 128  ? 0.4070 0.5572 0.3957 0.0061  0.0107  -0.0765 126  ALA A CB  
809   N N   . ASP A 129  ? 0.6573 0.8156 0.6407 0.0023  0.0133  -0.0661 127  ASP A N   
810   C CA  . ASP A 129  ? 0.7067 0.8746 0.6899 0.0020  0.0143  -0.0663 127  ASP A CA  
811   C C   . ASP A 129  ? 0.6791 0.8365 0.6636 0.0020  0.0145  -0.0632 127  ASP A C   
812   O O   . ASP A 129  ? 0.7683 0.9320 0.7539 0.0025  0.0152  -0.0648 127  ASP A O   
813   C CB  . ASP A 129  ? 0.6810 0.8615 0.6595 -0.0014 0.0153  -0.0607 127  ASP A CB  
814   N N   . GLY A 130  ? 0.7260 0.8682 0.7105 0.0017  0.0139  -0.0590 128  GLY A N   
815   C CA  . GLY A 130  ? 0.7167 0.8489 0.7026 0.0021  0.0139  -0.0569 128  GLY A CA  
816   C C   . GLY A 130  ? 0.7521 0.8729 0.7355 0.0000  0.0137  -0.0490 128  GLY A C   
817   O O   . GLY A 130  ? 0.7287 0.8371 0.7132 0.0009  0.0130  -0.0485 128  GLY A O   
818   N N   . ASN A 131  ? 0.7788 0.9039 0.7590 -0.0030 0.0143  -0.0429 129  ASN A N   
819   C CA  . ASN A 131  ? 0.7698 0.8847 0.7482 -0.0050 0.0140  -0.0358 129  ASN A CA  
820   C C   . ASN A 131  ? 0.6082 0.7152 0.5853 -0.0056 0.0133  -0.0331 129  ASN A C   
821   O O   . ASN A 131  ? 0.7157 0.8262 0.6902 -0.0082 0.0132  -0.0283 129  ASN A O   
822   C CB  . ASN A 131  ? 0.7341 0.8568 0.7103 -0.0082 0.0145  -0.0300 129  ASN A CB  
823   N N   . TRP A 132  ? 0.5831 0.6797 0.5622 -0.0034 0.0127  -0.0359 130  TRP A N   
824   C CA  . TRP A 132  ? 0.4600 0.5484 0.4380 -0.0040 0.0121  -0.0332 130  TRP A CA  
825   C C   . TRP A 132  ? 0.4468 0.5268 0.4231 -0.0059 0.0119  -0.0263 130  TRP A C   
826   O O   . TRP A 132  ? 0.5492 0.6261 0.5238 -0.0074 0.0114  -0.0224 130  TRP A O   
827   C CB  . TRP A 132  ? 0.4720 0.5519 0.4531 -0.0012 0.0115  -0.0377 130  TRP A CB  
828   C CG  . TRP A 132  ? 0.3889 0.4596 0.3723 0.0005  0.0114  -0.0381 130  TRP A CG  
829   C CD1 . TRP A 132  ? 0.3569 0.4289 0.3435 0.0027  0.0114  -0.0429 130  TRP A CD1 
830   C CD2 . TRP A 132  ? 0.3117 0.3709 0.2945 0.0001  0.0111  -0.0337 130  TRP A CD2 
831   N NE1 . TRP A 132  ? 0.3522 0.4144 0.3402 0.0036  0.0112  -0.0413 130  TRP A NE1 
832   C CE2 . TRP A 132  ? 0.3031 0.3575 0.2885 0.0021  0.0110  -0.0358 130  TRP A CE2 
833   C CE3 . TRP A 132  ? 0.3527 0.4055 0.3331 -0.0016 0.0109  -0.0283 130  TRP A CE3 
834   C CZ2 . TRP A 132  ? 0.3034 0.3476 0.2888 0.0023  0.0108  -0.0326 130  TRP A CZ2 
835   C CZ3 . TRP A 132  ? 0.3068 0.3493 0.2873 -0.0012 0.0107  -0.0256 130  TRP A CZ3 
836   C CH2 . TRP A 132  ? 0.2989 0.3374 0.2816 0.0007  0.0107  -0.0277 130  TRP A CH2 
837   N N   . LYS A 133  ? 0.5164 0.5924 0.4933 -0.0057 0.0120  -0.0251 131  LYS A N   
838   C CA  . LYS A 133  ? 0.5957 0.6640 0.5715 -0.0074 0.0116  -0.0192 131  LYS A CA  
839   C C   . LYS A 133  ? 0.6855 0.7604 0.6593 -0.0106 0.0115  -0.0138 131  LYS A C   
840   O O   . LYS A 133  ? 0.7471 0.8165 0.7199 -0.0122 0.0108  -0.0090 131  LYS A O   
841   C CB  . LYS A 133  ? 0.5445 0.6083 0.5216 -0.0064 0.0117  -0.0195 131  LYS A CB  
842   N N   . SER A 134  ? 0.6852 0.7724 0.6586 -0.0116 0.0121  -0.0145 132  SER A N   
843   C CA  . SER A 134  ? 0.7393 0.8340 0.7113 -0.0149 0.0119  -0.0089 132  SER A CA  
844   C C   . SER A 134  ? 0.7693 0.8651 0.7397 -0.0163 0.0113  -0.0061 132  SER A C   
845   O O   . SER A 134  ? 0.8399 0.9376 0.8096 -0.0191 0.0107  0.0000  132  SER A O   
846   C CB  . SER A 134  ? 0.6716 0.7806 0.6436 -0.0155 0.0128  -0.0106 132  SER A CB  
847   N N   . HIS A 135  ? 0.7566 0.8510 0.7270 -0.0145 0.0114  -0.0103 133  HIS A N   
848   C CA  . HIS A 135  ? 0.7239 0.8204 0.6928 -0.0157 0.0109  -0.0082 133  HIS A CA  
849   C C   . HIS A 135  ? 0.7427 0.8267 0.7119 -0.0148 0.0101  -0.0074 133  HIS A C   
850   O O   . HIS A 135  ? 0.7600 0.8441 0.7282 -0.0163 0.0095  -0.0041 133  HIS A O   
851   C CB  . HIS A 135  ? 0.6891 0.7967 0.6575 -0.0146 0.0114  -0.0134 133  HIS A CB  
852   C CG  . HIS A 135  ? 0.7679 0.8893 0.7361 -0.0152 0.0122  -0.0148 133  HIS A CG  
853   N ND1 . HIS A 135  ? 0.7704 0.8943 0.7402 -0.0129 0.0129  -0.0208 133  HIS A ND1 
854   C CD2 . HIS A 135  ? 0.7162 0.8498 0.6828 -0.0179 0.0124  -0.0110 133  HIS A CD2 
855   C CE1 . HIS A 135  ? 0.8307 0.9682 0.7999 -0.0140 0.0136  -0.0208 133  HIS A CE1 
856   N NE2 . HIS A 135  ? 0.8388 0.9825 0.8059 -0.0171 0.0134  -0.0148 133  HIS A NE2 
857   N N   . LEU A 136  ? 0.6789 0.7528 0.6496 -0.0125 0.0102  -0.0102 134  LEU A N   
858   C CA  . LEU A 136  ? 0.6887 0.7512 0.6597 -0.0117 0.0096  -0.0094 134  LEU A CA  
859   C C   . LEU A 136  ? 0.7426 0.7945 0.7145 -0.0110 0.0095  -0.0079 134  LEU A C   
860   O O   . LEU A 136  ? 0.7536 0.7962 0.7255 -0.0106 0.0090  -0.0061 134  LEU A O   
861   C CB  . LEU A 136  ? 0.6578 0.7190 0.6299 -0.0093 0.0098  -0.0150 134  LEU A CB  
862   C CG  . LEU A 136  ? 0.5814 0.6514 0.5528 -0.0096 0.0097  -0.0169 134  LEU A CG  
863   C CD1 . LEU A 136  ? 0.4601 0.5291 0.4338 -0.0069 0.0097  -0.0236 134  LEU A CD1 
864   C CD2 . LEU A 136  ? 0.4411 0.5087 0.4111 -0.0114 0.0089  -0.0124 134  LEU A CD2 
865   N N   . SER A 139  ? 0.5814 0.6031 0.5551 -0.0160 0.0053  0.0116  137  SER A N   
866   C CA  . SER A 139  ? 0.6252 0.6378 0.5999 -0.0158 0.0043  0.0136  137  SER A CA  
867   C C   . SER A 139  ? 0.6195 0.6250 0.5936 -0.0131 0.0049  0.0104  137  SER A C   
868   O O   . SER A 139  ? 0.6021 0.6002 0.5768 -0.0124 0.0042  0.0112  137  SER A O   
869   C CB  . SER A 139  ? 0.6824 0.6959 0.6579 -0.0180 0.0029  0.0181  137  SER A CB  
870   N N   . ARG A 140  ? 0.4773 0.4854 0.4506 -0.0117 0.0060  0.0068  138  ARG A N   
871   C CA  . ARG A 140  ? 0.3935 0.3958 0.3667 -0.0094 0.0065  0.0039  138  ARG A CA  
872   C C   . ARG A 140  ? 0.4177 0.4230 0.3911 -0.0077 0.0075  -0.0004 138  ARG A C   
873   O O   . ARG A 140  ? 0.4012 0.4139 0.3744 -0.0082 0.0079  -0.0020 138  ARG A O   
874   C CB  . ARG A 140  ? 0.4633 0.4653 0.4363 -0.0097 0.0063  0.0045  138  ARG A CB  
875   C CG  . ARG A 140  ? 0.4973 0.4952 0.4706 -0.0075 0.0069  0.0014  138  ARG A CG  
876   C CD  . ARG A 140  ? 0.5665 0.5668 0.5397 -0.0080 0.0067  0.0015  138  ARG A CD  
877   N NE  . ARG A 140  ? 0.5824 0.5790 0.5565 -0.0061 0.0071  -0.0013 138  ARG A NE  
878   C CZ  . ARG A 140  ? 0.6651 0.6648 0.6401 -0.0050 0.0076  -0.0051 138  ARG A CZ  
879   N NH1 . ARG A 140  ? 0.5853 0.5923 0.5601 -0.0054 0.0079  -0.0071 138  ARG A NH1 
880   N NH2 . ARG A 140  ? 0.6143 0.6101 0.5908 -0.0035 0.0078  -0.0071 138  ARG A NH2 
881   N N   . SER A 141  ? 0.3475 0.3474 0.3216 -0.0058 0.0079  -0.0023 139  SER A N   
882   C CA  . SER A 141  ? 0.3143 0.3161 0.2893 -0.0040 0.0086  -0.0063 139  SER A CA  
883   C C   . SER A 141  ? 0.2955 0.2996 0.2712 -0.0034 0.0088  -0.0088 139  SER A C   
884   O O   . SER A 141  ? 0.3153 0.3158 0.2910 -0.0033 0.0086  -0.0079 139  SER A O   
885   C CB  . SER A 141  ? 0.3345 0.3293 0.3105 -0.0020 0.0087  -0.0071 139  SER A CB  
886   O OG  . SER A 141  ? 0.3026 0.2986 0.2802 -0.0003 0.0091  -0.0108 139  SER A OG  
887   N N   . LEU A 142  ? 0.2948 0.3052 0.2715 -0.0028 0.0092  -0.0123 140  LEU A N   
888   C CA  . LEU A 142  ? 0.2892 0.3015 0.2673 -0.0018 0.0092  -0.0157 140  LEU A CA  
889   C C   . LEU A 142  ? 0.2483 0.2528 0.2284 0.0001  0.0091  -0.0168 140  LEU A C   
890   O O   . LEU A 142  ? 0.2620 0.2658 0.2434 0.0007  0.0089  -0.0184 140  LEU A O   
891   C CB  . LEU A 142  ? 0.2928 0.3126 0.2723 -0.0010 0.0095  -0.0200 140  LEU A CB  
892   C CG  . LEU A 142  ? 0.3602 0.3883 0.3397 -0.0015 0.0094  -0.0225 140  LEU A CG  
893   C CD1 . LEU A 142  ? 0.4265 0.4608 0.4031 -0.0041 0.0095  -0.0189 140  LEU A CD1 
894   C CD2 . LEU A 142  ? 0.3581 0.3924 0.3398 0.0000  0.0097  -0.0276 140  LEU A CD2 
895   N N   . PHE A 143  ? 0.2504 0.2491 0.2309 0.0010  0.0092  -0.0158 141  PHE A N   
896   C CA  . PHE A 143  ? 0.2413 0.2339 0.2242 0.0030  0.0091  -0.0170 141  PHE A CA  
897   C C   . PHE A 143  ? 0.2597 0.2454 0.2417 0.0030  0.0091  -0.0137 141  PHE A C   
898   O O   . PHE A 143  ? 0.2618 0.2425 0.2453 0.0044  0.0091  -0.0137 141  PHE A O   
899   C CB  . PHE A 143  ? 0.2254 0.2179 0.2099 0.0043  0.0092  -0.0186 141  PHE A CB  
900   C CG  . PHE A 143  ? 0.2201 0.2201 0.2058 0.0044  0.0092  -0.0221 141  PHE A CG  
901   C CD1 . PHE A 143  ? 0.2099 0.2135 0.1981 0.0052  0.0090  -0.0259 141  PHE A CD1 
902   C CD2 . PHE A 143  ? 0.2362 0.2401 0.2205 0.0037  0.0095  -0.0216 141  PHE A CD2 
903   C CE1 . PHE A 143  ? 0.2167 0.2279 0.2059 0.0054  0.0090  -0.0296 141  PHE A CE1 
904   C CE2 . PHE A 143  ? 0.2361 0.2478 0.2215 0.0038  0.0096  -0.0249 141  PHE A CE2 
905   C CZ  . PHE A 143  ? 0.2060 0.2215 0.1937 0.0048  0.0094  -0.0290 141  PHE A CZ  
906   N N   . VAL A 144  ? 0.2461 0.2318 0.2258 0.0014  0.0090  -0.0110 142  VAL A N   
907   C CA  . VAL A 144  ? 0.2751 0.2547 0.2539 0.0015  0.0089  -0.0082 142  VAL A CA  
908   C C   . VAL A 144  ? 0.2877 0.2635 0.2686 0.0028  0.0090  -0.0090 142  VAL A C   
909   O O   . VAL A 144  ? 0.3094 0.2802 0.2906 0.0037  0.0091  -0.0076 142  VAL A O   
910   C CB  . VAL A 144  ? 0.3057 0.2865 0.2826 -0.0004 0.0085  -0.0055 142  VAL A CB  
911   C CG1 . VAL A 144  ? 0.3538 0.3289 0.3306 -0.0001 0.0083  -0.0033 142  VAL A CG1 
912   C CG2 . VAL A 144  ? 0.3156 0.2990 0.2912 -0.0018 0.0082  -0.0037 142  VAL A CG2 
913   N N   . ASN A 145  ? 0.2662 0.2446 0.2488 0.0029  0.0088  -0.0114 143  ASN A N   
914   C CA  . ASN A 145  ? 0.2967 0.2717 0.2820 0.0040  0.0088  -0.0121 143  ASN A CA  
915   C C   . ASN A 145  ? 0.2978 0.2727 0.2868 0.0056  0.0086  -0.0151 143  ASN A C   
916   O O   . ASN A 145  ? 0.2725 0.2461 0.2647 0.0063  0.0082  -0.0166 143  ASN A O   
917   C CB  . ASN A 145  ? 0.2954 0.2726 0.2808 0.0032  0.0085  -0.0127 143  ASN A CB  
918   C CG  . ASN A 145  ? 0.3047 0.2806 0.2875 0.0019  0.0084  -0.0093 143  ASN A CG  
919   O OD1 . ASN A 145  ? 0.3949 0.3658 0.3772 0.0023  0.0086  -0.0070 143  ASN A OD1 
920   N ND2 . ASN A 145  ? 0.3649 0.3455 0.3461 0.0004  0.0081  -0.0090 143  ASN A ND2 
921   N N   . ALA A 146  ? 0.2433 0.2193 0.2324 0.0062  0.0087  -0.0160 144  ALA A N   
922   C CA  . ALA A 146  ? 0.2551 0.2314 0.2484 0.0077  0.0083  -0.0189 144  ALA A CA  
923   C C   . ALA A 146  ? 0.2329 0.2033 0.2292 0.0090  0.0080  -0.0177 144  ALA A C   
924   O O   . ALA A 146  ? 0.2934 0.2635 0.2944 0.0101  0.0074  -0.0200 144  ALA A O   
925   C CB  . ALA A 146  ? 0.2434 0.2222 0.2362 0.0080  0.0084  -0.0199 144  ALA A CB  
926   N N   . ALA A 147  ? 0.2591 0.2255 0.2533 0.0088  0.0085  -0.0140 145  ALA A N   
927   C CA  . ALA A 147  ? 0.3093 0.2712 0.3065 0.0099  0.0083  -0.0124 145  ALA A CA  
928   C C   . ALA A 147  ? 0.3179 0.2791 0.3183 0.0098  0.0079  -0.0133 145  ALA A C   
929   O O   . ALA A 147  ? 0.3025 0.2616 0.3077 0.0108  0.0073  -0.0137 145  ALA A O   
930   C CB  . ALA A 147  ? 0.3373 0.2960 0.3313 0.0097  0.0090  -0.0086 145  ALA A CB  
931   N N   . THR A 148  ? 0.2751 0.2381 0.2733 0.0087  0.0080  -0.0137 146  THR A N   
932   C CA  . THR A 148  ? 0.2787 0.2416 0.2799 0.0085  0.0075  -0.0148 146  THR A CA  
933   C C   . THR A 148  ? 0.2614 0.2273 0.2670 0.0092  0.0066  -0.0193 146  THR A C   
934   O O   . THR A 148  ? 0.2819 0.2458 0.2927 0.0100  0.0058  -0.0204 146  THR A O   
935   C CB  . THR A 148  ? 0.3275 0.2923 0.3251 0.0071  0.0078  -0.0141 146  THR A CB  
936   O OG1 . THR A 148  ? 0.3414 0.3032 0.3357 0.0067  0.0085  -0.0103 146  THR A OG1 
937   C CG2 . THR A 148  ? 0.3952 0.3600 0.3958 0.0070  0.0072  -0.0153 146  THR A CG2 
938   N N   . TRP A 149  ? 0.2574 0.2282 0.2614 0.0090  0.0066  -0.0220 147  TRP A N   
939   C CA  . TRP A 149  ? 0.2554 0.2297 0.2637 0.0098  0.0057  -0.0268 147  TRP A CA  
940   C C   . TRP A 149  ? 0.2392 0.2106 0.2525 0.0114  0.0050  -0.0276 147  TRP A C   
941   O O   . TRP A 149  ? 0.2487 0.2206 0.2677 0.0124  0.0038  -0.0311 147  TRP A O   
942   C CB  . TRP A 149  ? 0.2566 0.2377 0.2619 0.0093  0.0060  -0.0294 147  TRP A CB  
943   C CG  . TRP A 149  ? 0.2492 0.2342 0.2508 0.0077  0.0063  -0.0289 147  TRP A CG  
944   C CD1 . TRP A 149  ? 0.2818 0.2688 0.2781 0.0062  0.0070  -0.0260 147  TRP A CD1 
945   C CD2 . TRP A 149  ? 0.2664 0.2536 0.2697 0.0074  0.0056  -0.0310 147  TRP A CD2 
946   N NE1 . TRP A 149  ? 0.2861 0.2766 0.2806 0.0050  0.0069  -0.0260 147  TRP A NE1 
947   C CE2 . TRP A 149  ? 0.2804 0.2712 0.2788 0.0057  0.0061  -0.0291 147  TRP A CE2 
948   C CE3 . TRP A 149  ? 0.2736 0.2602 0.2822 0.0084  0.0046  -0.0344 147  TRP A CE3 
949   C CZ2 . TRP A 149  ? 0.3040 0.2981 0.3025 0.0051  0.0056  -0.0304 147  TRP A CZ2 
950   C CZ3 . TRP A 149  ? 0.3208 0.3105 0.3295 0.0078  0.0041  -0.0360 147  TRP A CZ3 
951   C CH2 . TRP A 149  ? 0.3377 0.3313 0.3412 0.0061  0.0047  -0.0340 147  TRP A CH2 
952   N N   . GLY A 150  ? 0.2355 0.2039 0.2471 0.0117  0.0055  -0.0245 148  GLY A N   
953   C CA  . GLY A 150  ? 0.2641 0.2295 0.2807 0.0132  0.0048  -0.0244 148  GLY A CA  
954   C C   . GLY A 150  ? 0.2742 0.2354 0.2960 0.0136  0.0040  -0.0230 148  GLY A C   
955   O O   . GLY A 150  ? 0.2829 0.2429 0.3113 0.0147  0.0027  -0.0249 148  GLY A O   
956   N N   . LEU A 151  ? 0.2647 0.2236 0.2839 0.0126  0.0047  -0.0198 149  LEU A N   
957   C CA  . LEU A 151  ? 0.3056 0.2610 0.3298 0.0128  0.0040  -0.0183 149  LEU A CA  
958   C C   . LEU A 151  ? 0.2782 0.2354 0.3074 0.0130  0.0027  -0.0228 149  LEU A C   
959   O O   . LEU A 151  ? 0.3307 0.2856 0.3670 0.0137  0.0013  -0.0235 149  LEU A O   
960   C CB  . LEU A 151  ? 0.3473 0.3008 0.3674 0.0118  0.0051  -0.0143 149  LEU A CB  
961   C CG  . LEU A 151  ? 0.3981 0.3479 0.4219 0.0119  0.0048  -0.0109 149  LEU A CG  
962   C CD1 . LEU A 151  ? 0.3623 0.3098 0.3898 0.0129  0.0044  -0.0085 149  LEU A CD1 
963   C CD2 . LEU A 151  ? 0.4599 0.4089 0.4784 0.0111  0.0062  -0.0073 149  LEU A CD2 
964   N N   . VAL A 152  ? 0.2754 0.2370 0.3015 0.0123  0.0029  -0.0259 150  VAL A N   
965   C CA  . VAL A 152  ? 0.2929 0.2573 0.3234 0.0126  0.0016  -0.0307 150  VAL A CA  
966   C C   . VAL A 152  ? 0.3146 0.2803 0.3513 0.0141  0.0002  -0.0351 150  VAL A C   
967   O O   . VAL A 152  ? 0.3441 0.3088 0.3880 0.0149  -0.0014 -0.0379 150  VAL A O   
968   C CB  . VAL A 152  ? 0.3080 0.2781 0.3331 0.0115  0.0023  -0.0328 150  VAL A CB  
969   C CG1 . VAL A 152  ? 0.3421 0.3166 0.3714 0.0120  0.0010  -0.0387 150  VAL A CG1 
970   C CG2 . VAL A 152  ? 0.3277 0.2961 0.3484 0.0101  0.0032  -0.0288 150  VAL A CG2 
971   N N   . VAL A 153  ? 0.2984 0.2664 0.3328 0.0146  0.0007  -0.0359 151  VAL A N   
972   C CA  . VAL A 153  ? 0.3189 0.2892 0.3588 0.0161  -0.0006 -0.0407 151  VAL A CA  
973   C C   . VAL A 153  ? 0.2949 0.2598 0.3413 0.0173  -0.0017 -0.0389 151  VAL A C   
974   O O   . VAL A 153  ? 0.3355 0.2999 0.3900 0.0185  -0.0036 -0.0425 151  VAL A O   
975   C CB  . VAL A 153  ? 0.2866 0.2620 0.3214 0.0161  0.0004  -0.0423 151  VAL A CB  
976   C CG1 . VAL A 153  ? 0.3262 0.3039 0.3669 0.0179  -0.0009 -0.0471 151  VAL A CG1 
977   C CG2 . VAL A 153  ? 0.2627 0.2443 0.2923 0.0149  0.0012  -0.0443 151  VAL A CG2 
978   N N   . THR A 154  ? 0.3044 0.2655 0.3480 0.0170  -0.0008 -0.0333 152  THR A N   
979   C CA  . THR A 154  ? 0.3083 0.2654 0.3572 0.0180  -0.0017 -0.0309 152  THR A CA  
980   C C   . THR A 154  ? 0.3489 0.3008 0.4006 0.0175  -0.0020 -0.0259 152  THR A C   
981   O O   . THR A 154  ? 0.3842 0.3330 0.4418 0.0183  -0.0032 -0.0238 152  THR A O   
982   C CB  . THR A 154  ? 0.3538 0.3113 0.3978 0.0182  -0.0006 -0.0284 152  THR A CB  
983   O OG1 . THR A 154  ? 0.3613 0.3168 0.3988 0.0170  0.0010  -0.0231 152  THR A OG1 
984   C CG2 . THR A 154  ? 0.3452 0.3083 0.3850 0.0182  0.0000  -0.0325 152  THR A CG2 
985   N N   . GLY A 155  ? 0.3658 0.3172 0.4136 0.0163  -0.0010 -0.0238 153  GLY A N   
986   C CA  . GLY A 155  ? 0.3339 0.2813 0.3836 0.0158  -0.0010 -0.0186 153  GLY A CA  
987   C C   . GLY A 155  ? 0.4348 0.3806 0.4801 0.0156  0.0003  -0.0131 153  GLY A C   
988   O O   . GLY A 155  ? 0.4051 0.3482 0.4518 0.0153  0.0005  -0.0084 153  GLY A O   
989   N N   . LYS A 156  ? 0.3586 0.3063 0.3987 0.0159  0.0012  -0.0135 154  LYS A N   
990   C CA  . LYS A 156  ? 0.3893 0.3360 0.4250 0.0159  0.0023  -0.0089 154  LYS A CA  
991   C C   . LYS A 156  ? 0.4081 0.3567 0.4350 0.0150  0.0041  -0.0085 154  LYS A C   
992   O O   . LYS A 156  ? 0.3563 0.3077 0.3804 0.0146  0.0043  -0.0120 154  LYS A O   
993   C CB  . LYS A 156  ? 0.4541 0.4013 0.4919 0.0171  0.0016  -0.0096 154  LYS A CB  
994   N N   . LEU A 157  ? 0.3562 0.3036 0.3792 0.0147  0.0051  -0.0042 155  LEU A N   
995   C CA  . LEU A 157  ? 0.3853 0.3340 0.4008 0.0139  0.0065  -0.0035 155  LEU A CA  
996   C C   . LEU A 157  ? 0.5001 0.4497 0.5124 0.0145  0.0069  -0.0026 155  LEU A C   
997   O O   . LEU A 157  ? 0.4926 0.4410 0.5062 0.0152  0.0068  0.0003  155  LEU A O   
998   C CB  . LEU A 157  ? 0.3841 0.3314 0.3975 0.0134  0.0074  0.0001  155  LEU A CB  
999   C CG  . LEU A 157  ? 0.4950 0.4432 0.5014 0.0128  0.0086  0.0008  155  LEU A CG  
1000  C CD1 . LEU A 157  ? 0.4640 0.4140 0.4682 0.0119  0.0086  -0.0024 155  LEU A CD1 
1001  C CD2 . LEU A 157  ? 0.5273 0.4744 0.5326 0.0126  0.0093  0.0041  155  LEU A CD2 
1002  N N   . THR A 158  ? 0.5441 0.4959 0.5523 0.0141  0.0073  -0.0050 156  THR A N   
1003  C CA  . THR A 158  ? 0.5653 0.5181 0.5699 0.0143  0.0077  -0.0043 156  THR A CA  
1004  C C   . THR A 158  ? 0.5598 0.5133 0.5584 0.0133  0.0086  -0.0035 156  THR A C   
1005  O O   . THR A 158  ? 0.6594 0.6145 0.6563 0.0123  0.0088  -0.0055 156  THR A O   
1006  C CB  . THR A 158  ? 0.5593 0.5146 0.5653 0.0147  0.0071  -0.0078 156  THR A CB  
1007  N N   . SER A 159  ? 0.5037 0.4562 0.4993 0.0136  0.0091  -0.0007 157  SER A N   
1008  C CA  . SER A 159  ? 0.3360 0.2885 0.3270 0.0128  0.0098  0.0002  157  SER A CA  
1009  C C   . SER A 159  ? 0.4206 0.3751 0.4085 0.0119  0.0098  -0.0017 157  SER A C   
1010  O O   . SER A 159  ? 0.4452 0.3999 0.4308 0.0108  0.0100  -0.0018 157  SER A O   
1011  C CB  . SER A 159  ? 0.5488 0.5006 0.5377 0.0136  0.0102  0.0030  157  SER A CB  
1012  O OG  . SER A 159  ? 0.5581 0.5105 0.5477 0.0144  0.0099  0.0033  157  SER A OG  
1013  N N   . THR A 160  ? 0.4094 0.3653 0.3973 0.0122  0.0095  -0.0029 158  THR A N   
1014  C CA  . THR A 160  ? 0.3604 0.3188 0.3460 0.0112  0.0094  -0.0045 158  THR A CA  
1015  C C   . THR A 160  ? 0.3144 0.2754 0.3028 0.0112  0.0091  -0.0074 158  THR A C   
1016  O O   . THR A 160  ? 0.3578 0.3183 0.3501 0.0122  0.0087  -0.0082 158  THR A O   
1017  C CB  . THR A 160  ? 0.3192 0.2779 0.3024 0.0114  0.0094  -0.0037 158  THR A CB  
1018  O OG1 . THR A 160  ? 0.4239 0.3826 0.4093 0.0127  0.0091  -0.0037 158  THR A OG1 
1019  C CG2 . THR A 160  ? 0.4642 0.4209 0.4449 0.0115  0.0096  -0.0015 158  THR A CG2 
1020  N N   . VAL A 161  ? 0.2473 0.2116 0.2340 0.0101  0.0091  -0.0088 159  VAL A N   
1021  C CA  . VAL A 161  ? 0.2590 0.2271 0.2476 0.0099  0.0089  -0.0119 159  VAL A CA  
1022  C C   . VAL A 161  ? 0.2430 0.2138 0.2315 0.0102  0.0088  -0.0130 159  VAL A C   
1023  O O   . VAL A 161  ? 0.2353 0.2069 0.2209 0.0093  0.0089  -0.0117 159  VAL A O   
1024  C CB  . VAL A 161  ? 0.2797 0.2507 0.2661 0.0083  0.0091  -0.0123 159  VAL A CB  
1025  C CG1 . VAL A 161  ? 0.3184 0.2949 0.3060 0.0080  0.0090  -0.0154 159  VAL A CG1 
1026  C CG2 . VAL A 161  ? 0.3429 0.3116 0.3298 0.0081  0.0091  -0.0114 159  VAL A CG2 
1027  N N   . ASN A 162  ? 0.2078 0.1801 0.2000 0.0114  0.0084  -0.0155 160  ASN A N   
1028  C CA  . ASN A 162  ? 0.2088 0.1845 0.2012 0.0116  0.0082  -0.0170 160  ASN A CA  
1029  C C   . ASN A 162  ? 0.2000 0.1816 0.1915 0.0104  0.0085  -0.0193 160  ASN A C   
1030  O O   . ASN A 162  ? 0.2197 0.2046 0.2142 0.0110  0.0082  -0.0227 160  ASN A O   
1031  C CB  . ASN A 162  ? 0.2209 0.1959 0.2178 0.0134  0.0076  -0.0186 160  ASN A CB  
1032  C CG  . ASN A 162  ? 0.2306 0.2089 0.2277 0.0138  0.0074  -0.0199 160  ASN A CG  
1033  O OD1 . ASN A 162  ? 0.2307 0.2130 0.2251 0.0125  0.0079  -0.0204 160  ASN A OD1 
1034  N ND2 . ASN A 162  ? 0.2840 0.2609 0.2845 0.0154  0.0068  -0.0202 160  ASN A ND2 
1035  N N   . ASP A 163  ? 0.2028 0.1859 0.1905 0.0087  0.0089  -0.0175 161  ASP A N   
1036  C CA  . ASP A 163  ? 0.2093 0.1984 0.1958 0.0072  0.0091  -0.0187 161  ASP A CA  
1037  C C   . ASP A 163  ? 0.1933 0.1883 0.1810 0.0074  0.0091  -0.0213 161  ASP A C   
1038  O O   . ASP A 163  ? 0.2110 0.2123 0.1990 0.0068  0.0093  -0.0236 161  ASP A O   
1039  C CB  . ASP A 163  ? 0.2409 0.2300 0.2238 0.0052  0.0092  -0.0155 161  ASP A CB  
1040  C CG  . ASP A 163  ? 0.2546 0.2411 0.2358 0.0049  0.0091  -0.0131 161  ASP A CG  
1041  O OD1 . ASP A 163  ? 0.2423 0.2245 0.2242 0.0063  0.0089  -0.0126 161  ASP A OD1 
1042  O OD2 . ASP A 163  ? 0.2842 0.2731 0.2635 0.0031  0.0090  -0.0114 161  ASP A OD2 
1043  N N   . ARG A 164  ? 0.2060 0.1999 0.1944 0.0083  0.0090  -0.0211 162  ARG A N   
1044  C CA  A ARG A 164  ? 0.2013 0.2009 0.1913 0.0087  0.0090  -0.0238 162  ARG A CA  
1045  C CA  B ARG A 164  ? 0.2017 0.2013 0.1917 0.0087  0.0090  -0.0238 162  ARG A CA  
1046  C C   . ARG A 164  ? 0.1904 0.1915 0.1849 0.0106  0.0086  -0.0280 162  ARG A C   
1047  O O   . ARG A 164  ? 0.2057 0.2135 0.2016 0.0108  0.0087  -0.0314 162  ARG A O   
1048  C CB  A ARG A 164  ? 0.2261 0.2241 0.2158 0.0090  0.0088  -0.0224 162  ARG A CB  
1049  C CB  B ARG A 164  ? 0.2259 0.2236 0.2155 0.0091  0.0088  -0.0224 162  ARG A CB  
1050  C CG  A ARG A 164  ? 0.2225 0.2203 0.2085 0.0071  0.0089  -0.0190 162  ARG A CG  
1051  C CG  B ARG A 164  ? 0.2237 0.2204 0.2097 0.0072  0.0089  -0.0188 162  ARG A CG  
1052  C CD  A ARG A 164  ? 0.2810 0.2846 0.2652 0.0049  0.0093  -0.0186 162  ARG A CD  
1053  C CD  B ARG A 164  ? 0.2482 0.2518 0.2331 0.0055  0.0091  -0.0188 162  ARG A CD  
1054  N NE  A ARG A 164  ? 0.3397 0.3512 0.3254 0.0049  0.0096  -0.0215 162  ARG A NE  
1055  N NE  B ARG A 164  ? 0.3284 0.3377 0.3131 0.0044  0.0095  -0.0201 162  ARG A NE  
1056  C CZ  A ARG A 164  ? 0.3118 0.3300 0.2967 0.0034  0.0100  -0.0220 162  ARG A CZ  
1057  C CZ  B ARG A 164  ? 0.3070 0.3157 0.2898 0.0030  0.0096  -0.0182 162  ARG A CZ  
1058  N NH1 A ARG A 164  ? 0.3192 0.3369 0.3019 0.0018  0.0100  -0.0196 162  ARG A NH1 
1059  N NH1 B ARG A 164  ? 0.3413 0.3437 0.3225 0.0026  0.0093  -0.0152 162  ARG A NH1 
1060  N NH2 A ARG A 164  ? 0.2865 0.3125 0.2727 0.0037  0.0103  -0.0251 162  ARG A NH2 
1061  N NH2 B ARG A 164  ? 0.3555 0.3703 0.3381 0.0022  0.0099  -0.0195 162  ARG A NH2 
1062  N N   . SER A 165  ? 0.1800 0.1753 0.1771 0.0121  0.0081  -0.0279 163  SER A N   
1063  C CA  . SER A 165  ? 0.1705 0.1665 0.1729 0.0139  0.0074  -0.0318 163  SER A CA  
1064  C C   . SER A 165  ? 0.1928 0.1929 0.1954 0.0133  0.0075  -0.0344 163  SER A C   
1065  O O   . SER A 165  ? 0.1813 0.1864 0.1871 0.0142  0.0072  -0.0389 163  SER A O   
1066  C CB  . SER A 165  ? 0.2116 0.2004 0.2169 0.0152  0.0067  -0.0302 163  SER A CB  
1067  O OG  . SER A 165  ? 0.2291 0.2179 0.2401 0.0167  0.0058  -0.0336 163  SER A OG  
1068  N N   . LEU A 166  ? 0.1919 0.1900 0.1912 0.0118  0.0079  -0.0317 164  LEU A N   
1069  C CA  . LEU A 166  ? 0.1957 0.1978 0.1949 0.0111  0.0080  -0.0338 164  LEU A CA  
1070  C C   . LEU A 166  ? 0.1808 0.1919 0.1779 0.0100  0.0085  -0.0355 164  LEU A C   
1071  O O   . LEU A 166  ? 0.1867 0.2037 0.1855 0.0103  0.0084  -0.0394 164  LEU A O   
1072  C CB  . LEU A 166  ? 0.1819 0.1798 0.1780 0.0098  0.0083  -0.0301 164  LEU A CB  
1073  C CG  . LEU A 166  ? 0.1958 0.1862 0.1945 0.0109  0.0078  -0.0288 164  LEU A CG  
1074  C CD1 . LEU A 166  ? 0.2184 0.2050 0.2136 0.0096  0.0082  -0.0250 164  LEU A CD1 
1075  C CD2 . LEU A 166  ? 0.2230 0.2141 0.2267 0.0122  0.0070  -0.0328 164  LEU A CD2 
1076  N N   . ALA A 167  ? 0.1814 0.1941 0.1749 0.0086  0.0091  -0.0326 165  ALA A N   
1077  C CA  . ALA A 167  ? 0.1926 0.2146 0.1845 0.0073  0.0096  -0.0338 165  ALA A CA  
1078  C C   . ALA A 167  ? 0.1809 0.2087 0.1765 0.0090  0.0095  -0.0388 165  ALA A C   
1079  O O   . ALA A 167  ? 0.1966 0.2328 0.1924 0.0088  0.0097  -0.0421 165  ALA A O   
1080  C CB  . ALA A 167  ? 0.2161 0.2381 0.2045 0.0055  0.0100  -0.0296 165  ALA A CB  
1081  N N   . ALA A 168  ? 0.1915 0.2152 0.1898 0.0107  0.0090  -0.0396 166  ALA A N   
1082  C CA  . ALA A 168  ? 0.1929 0.2215 0.1956 0.0126  0.0087  -0.0446 166  ALA A CA  
1083  C C   . ALA A 168  ? 0.1870 0.2172 0.1938 0.0141  0.0079  -0.0495 166  ALA A C   
1084  O O   . ALA A 168  ? 0.1876 0.2260 0.1964 0.0149  0.0079  -0.0544 166  ALA A O   
1085  C CB  . ALA A 168  ? 0.1976 0.2202 0.2029 0.0142  0.0081  -0.0439 166  ALA A CB  
1086  N N   . ALA A 169  ? 0.1790 0.2020 0.1872 0.0146  0.0073  -0.0485 167  ALA A N   
1087  C CA  . ALA A 169  ? 0.1739 0.1976 0.1867 0.0160  0.0064  -0.0530 167  ALA A CA  
1088  C C   . ALA A 169  ? 0.1885 0.2203 0.1991 0.0149  0.0069  -0.0553 167  ALA A C   
1089  O O   . ALA A 169  ? 0.1871 0.2244 0.2013 0.0162  0.0062  -0.0609 167  ALA A O   
1090  C CB  . ALA A 169  ? 0.1969 0.2112 0.2115 0.0163  0.0057  -0.0504 167  ALA A CB  
1091  N N   . LEU A 170  ? 0.1694 0.2020 0.1742 0.0125  0.0078  -0.0509 168  LEU A N   
1092  C CA  . LEU A 170  ? 0.1643 0.2050 0.1666 0.0112  0.0082  -0.0522 168  LEU A CA  
1093  C C   . LEU A 170  ? 0.1829 0.2350 0.1849 0.0112  0.0087  -0.0556 168  LEU A C   
1094  O O   . LEU A 170  ? 0.1964 0.2566 0.1997 0.0117  0.0086  -0.0603 168  LEU A O   
1095  C CB  . LEU A 170  ? 0.1916 0.2301 0.1884 0.0086  0.0089  -0.0462 168  LEU A CB  
1096  C CG  . LEU A 170  ? 0.1825 0.2286 0.1767 0.0071  0.0092  -0.0465 168  LEU A CG  
1097  C CD1 . LEU A 170  ? 0.2210 0.2669 0.2187 0.0085  0.0083  -0.0509 168  LEU A CD1 
1098  C CD2 . LEU A 170  ? 0.2249 0.2672 0.2146 0.0048  0.0095  -0.0402 168  LEU A CD2 
1099  N N   . THR A 171  ? 0.1893 0.2427 0.1897 0.0106  0.0094  -0.0533 169  THR A N   
1100  C CA  . THR A 171  ? 0.1995 0.2639 0.2000 0.0107  0.0099  -0.0565 169  THR A CA  
1101  C C   . THR A 171  ? 0.1862 0.2537 0.1927 0.0136  0.0090  -0.0639 169  THR A C   
1102  O O   . THR A 171  ? 0.1872 0.2651 0.1946 0.0142  0.0091  -0.0687 169  THR A O   
1103  C CB  . THR A 171  ? 0.2290 0.2924 0.2278 0.0099  0.0105  -0.0530 169  THR A CB  
1104  O OG1 . THR A 171  ? 0.2469 0.3080 0.2408 0.0072  0.0110  -0.0466 169  THR A OG1 
1105  C CG2 . THR A 171  ? 0.2436 0.3186 0.2432 0.0101  0.0110  -0.0563 169  THR A CG2 
1106  N N   . ARG A 172  ? 0.1901 0.2489 0.2011 0.0156  0.0080  -0.0649 170  ARG A N   
1107  C CA  . ARG A 172  ? 0.1832 0.2439 0.2010 0.0185  0.0069  -0.0717 170  ARG A CA  
1108  C C   . ARG A 172  ? 0.1777 0.2421 0.1981 0.0194  0.0061  -0.0767 170  ARG A C   
1109  O O   . ARG A 172  ? 0.1870 0.2601 0.2107 0.0209  0.0057  -0.0832 170  ARG A O   
1110  C CB  . ARG A 172  ? 0.1928 0.2425 0.2151 0.0202  0.0057  -0.0705 170  ARG A CB  
1111  C CG  . ARG A 172  ? 0.1806 0.2321 0.2107 0.0232  0.0043  -0.0771 170  ARG A CG  
1112  C CD  . ARG A 172  ? 0.2045 0.2451 0.2397 0.0247  0.0029  -0.0754 170  ARG A CD  
1113  N NE  . ARG A 172  ? 0.1881 0.2224 0.2191 0.0234  0.0037  -0.0687 170  ARG A NE  
1114  C CZ  . ARG A 172  ? 0.1915 0.2176 0.2197 0.0222  0.0039  -0.0632 170  ARG A CZ  
1115  N NH1 . ARG A 172  ? 0.1837 0.2063 0.2127 0.0219  0.0034  -0.0630 170  ARG A NH1 
1116  N NH2 . ARG A 172  ? 0.1911 0.2129 0.2157 0.0212  0.0045  -0.0579 170  ARG A NH2 
1117  N N   . LEU A 173  ? 0.1901 0.2483 0.2091 0.0184  0.0058  -0.0739 171  LEU A N   
1118  C CA  . LEU A 173  ? 0.1752 0.2361 0.1973 0.0193  0.0048  -0.0788 171  LEU A CA  
1119  C C   . LEU A 173  ? 0.1807 0.2542 0.1990 0.0182  0.0057  -0.0811 171  LEU A C   
1120  O O   . LEU A 173  ? 0.2065 0.2871 0.2282 0.0197  0.0049  -0.0877 171  LEU A O   
1121  C CB  . LEU A 173  ? 0.2155 0.2665 0.2376 0.0187  0.0043  -0.0752 171  LEU A CB  
1122  C CG  . LEU A 173  ? 0.2035 0.2532 0.2188 0.0159  0.0054  -0.0691 171  LEU A CG  
1123  C CD1 . LEU A 173  ? 0.2407 0.2979 0.2547 0.0153  0.0053  -0.0719 171  LEU A CD1 
1124  C CD2 . LEU A 173  ? 0.2128 0.2503 0.2285 0.0156  0.0050  -0.0644 171  LEU A CD2 
1125  N N   . ILE A 174  ? 0.2023 0.2791 0.2138 0.0155  0.0072  -0.0756 172  ILE A N   
1126  C CA  . ILE A 174  ? 0.1879 0.2775 0.1958 0.0142  0.0080  -0.0769 172  ILE A CA  
1127  C C   . ILE A 174  ? 0.2042 0.3051 0.2140 0.0155  0.0083  -0.0823 172  ILE A C   
1128  O O   . ILE A 174  ? 0.2123 0.3243 0.2228 0.0162  0.0082  -0.0878 172  ILE A O   
1129  C CB  . ILE A 174  ? 0.2027 0.2925 0.2035 0.0109  0.0092  -0.0690 172  ILE A CB  
1130  C CG1 . ILE A 174  ? 0.2325 0.3134 0.2315 0.0097  0.0089  -0.0647 172  ILE A CG1 
1131  C CG2 . ILE A 174  ? 0.2587 0.3633 0.2560 0.0094  0.0101  -0.0698 172  ILE A CG2 
1132  C CD1 . ILE A 174  ? 0.2563 0.3353 0.2497 0.0068  0.0098  -0.0570 172  ILE A CD1 
1133  N N   . SER A 175  ? 0.1987 0.2975 0.2094 0.0160  0.0086  -0.0812 173  SER A N   
1134  C CA  . SER A 175  ? 0.1888 0.2985 0.2016 0.0174  0.0089  -0.0864 173  SER A CA  
1135  C C   . SER A 175  ? 0.2168 0.3281 0.2371 0.0208  0.0074  -0.0952 173  SER A C   
1136  O O   . SER A 175  ? 0.2422 0.3654 0.2644 0.0221  0.0075  -0.1013 173  SER A O   
1137  C CB  . SER A 175  ? 0.2366 0.3432 0.2492 0.0172  0.0095  -0.0832 173  SER A CB  
1138  O OG  . SER A 175  ? 0.2703 0.3776 0.2766 0.0140  0.0108  -0.0759 173  SER A OG  
1139  N N   . ARG A 176  ? 0.2044 0.3046 0.2293 0.0222  0.0059  -0.0960 174  ARG A N   
1140  C CA  . ARG A 176  ? 0.2001 0.3008 0.2332 0.0255  0.0041  -0.1042 174  ARG A CA  
1141  C C   . ARG A 176  ? 0.2431 0.3497 0.2771 0.0259  0.0034  -0.1091 174  ARG A C   
1142  O O   . ARG A 176  ? 0.2710 0.3865 0.3096 0.0281  0.0025  -0.1173 174  ARG A O   
1143  C CB  . ARG A 176  ? 0.2490 0.3351 0.2874 0.0268  0.0026  -0.1025 174  ARG A CB  
1144  C CG  . ARG A 176  ? 0.2615 0.3465 0.3098 0.0302  0.0003  -0.1103 174  ARG A CG  
1145  C CD  . ARG A 176  ? 0.2517 0.3224 0.3049 0.0310  -0.0010 -0.1069 174  ARG A CD  
1146  N NE  . ARG A 176  ? 0.2428 0.3049 0.2954 0.0299  -0.0015 -0.1031 174  ARG A NE  
1147  C CZ  . ARG A 176  ? 0.2575 0.3104 0.3057 0.0279  -0.0007 -0.0952 174  ARG A CZ  
1148  N NH1 . ARG A 176  ? 0.2253 0.2755 0.2695 0.0269  0.0005  -0.0898 174  ARG A NH1 
1149  N NH2 . ARG A 176  ? 0.2725 0.3191 0.3206 0.0271  -0.0012 -0.0927 174  ARG A NH2 
1150  N N   . CYS A 177  ? 0.2274 0.3298 0.2572 0.0238  0.0037  -0.1044 175  CYS A N   
1151  C CA  . CYS A 177  ? 0.2430 0.3484 0.2745 0.0242  0.0026  -0.1087 175  CYS A CA  
1152  C C   . CYS A 177  ? 0.2715 0.3866 0.2958 0.0218  0.0039  -0.1065 175  CYS A C   
1153  O O   . CYS A 177  ? 0.3047 0.4257 0.3303 0.0224  0.0031  -0.1113 175  CYS A O   
1154  C CB  . CYS A 177  ? 0.2728 0.3643 0.3071 0.0243  0.0013  -0.1059 175  CYS A CB  
1155  S SG  . CYS A 177  ? 0.3065 0.3859 0.3499 0.0269  -0.0005 -0.1074 175  CYS A SG  
1156  N N   . GLY A 178  ? 0.2613 0.3781 0.2786 0.0191  0.0057  -0.0994 176  GLY A N   
1157  C CA  . GLY A 178  ? 0.2562 0.3844 0.2673 0.0169  0.0068  -0.0975 176  GLY A CA  
1158  C C   . GLY A 178  ? 0.2246 0.3499 0.2331 0.0153  0.0064  -0.0947 176  GLY A C   
1159  O O   . GLY A 178  ? 0.2575 0.3702 0.2673 0.0152  0.0057  -0.0918 176  GLY A O   
1160  N N   . GLU A 179  ? 0.2492 0.3871 0.2539 0.0141  0.0069  -0.0956 177  GLU A N   
1161  C CA  . GLU A 179  ? 0.2548 0.3918 0.2566 0.0125  0.0066  -0.0928 177  GLU A CA  
1162  C C   . GLU A 179  ? 0.2282 0.3571 0.2353 0.0143  0.0048  -0.0970 177  GLU A C   
1163  O O   . GLU A 179  ? 0.2520 0.3723 0.2574 0.0130  0.0046  -0.0922 177  GLU A O   
1164  C CB  . GLU A 179  ? 0.2536 0.4074 0.2512 0.0112  0.0073  -0.0940 177  GLU A CB  
1165  C CG  . GLU A 179  ? 0.3541 0.5080 0.3477 0.0090  0.0071  -0.0896 177  GLU A CG  
1166  C CD  . GLU A 179  ? 0.5337 0.6899 0.5307 0.0108  0.0055  -0.0964 177  GLU A CD  
1167  O OE1 . GLU A 179  ? 0.4929 0.6539 0.4951 0.0136  0.0046  -0.1052 177  GLU A OE1 
1168  O OE2 . GLU A 179  ? 0.5368 0.6902 0.5316 0.0093  0.0051  -0.0931 177  GLU A OE2 
1169  N N   . PRO A 180  ? 0.2287 0.3598 0.2425 0.0174  0.0035  -0.1058 178  PRO A N   
1170  C CA  . PRO A 180  ? 0.2488 0.3722 0.2680 0.0188  0.0016  -0.1094 178  PRO A CA  
1171  C C   . PRO A 180  ? 0.2550 0.3616 0.2758 0.0184  0.0012  -0.1037 178  PRO A C   
1172  O O   . PRO A 180  ? 0.2590 0.3595 0.2805 0.0178  0.0004  -0.1021 178  PRO A O   
1173  C CB  . PRO A 180  ? 0.2696 0.3979 0.2967 0.0222  0.0001  -0.1195 178  PRO A CB  
1174  C CG  . PRO A 180  ? 0.2717 0.4159 0.2955 0.0222  0.0013  -0.1225 178  PRO A CG  
1175  C CD  . PRO A 180  ? 0.2567 0.3995 0.2735 0.0195  0.0034  -0.1134 178  PRO A CD  
1176  N N   . VAL A 181  ? 0.2387 0.3380 0.2601 0.0186  0.0018  -0.1004 179  VAL A N   
1177  C CA  . VAL A 181  ? 0.2340 0.3183 0.2567 0.0181  0.0015  -0.0948 179  VAL A CA  
1178  C C   . VAL A 181  ? 0.2314 0.3121 0.2470 0.0152  0.0028  -0.0864 179  VAL A C   
1179  O O   . VAL A 181  ? 0.2265 0.2973 0.2426 0.0147  0.0023  -0.0829 179  VAL A O   
1180  C CB  . VAL A 181  ? 0.2383 0.3161 0.2640 0.0194  0.0016  -0.0939 179  VAL A CB  
1181  C CG1 . VAL A 181  ? 0.2178 0.2991 0.2373 0.0176  0.0035  -0.0889 179  VAL A CG1 
1182  C CG2 . VAL A 181  ? 0.2729 0.3362 0.3016 0.0195  0.0008  -0.0899 179  VAL A CG2 
1183  N N   . ILE A 182  ? 0.2233 0.3120 0.2325 0.0132  0.0042  -0.0830 180  ILE A N   
1184  C CA  . ILE A 182  ? 0.2333 0.3191 0.2363 0.0104  0.0052  -0.0752 180  ILE A CA  
1185  C C   . ILE A 182  ? 0.2670 0.3544 0.2695 0.0098  0.0044  -0.0759 180  ILE A C   
1186  O O   . ILE A 182  ? 0.2521 0.3310 0.2532 0.0086  0.0043  -0.0711 180  ILE A O   
1187  C CB  . ILE A 182  ? 0.2275 0.3226 0.2247 0.0083  0.0066  -0.0716 180  ILE A CB  
1188  C CG1 . ILE A 182  ? 0.2436 0.3370 0.2415 0.0089  0.0073  -0.0709 180  ILE A CG1 
1189  C CG2 . ILE A 182  ? 0.2408 0.3329 0.2326 0.0054  0.0072  -0.0637 180  ILE A CG2 
1190  C CD1 . ILE A 182  ? 0.2970 0.4013 0.2905 0.0071  0.0086  -0.0686 180  ILE A CD1 
1191  N N   . ARG A 183  ? 0.2456 0.3444 0.2492 0.0106  0.0039  -0.0821 181  ARG A N   
1192  C CA  A ARG A 183  ? 0.2897 0.3911 0.2931 0.0102  0.0030  -0.0836 181  ARG A CA  
1193  C CA  B ARG A 183  ? 0.2897 0.3912 0.2932 0.0102  0.0029  -0.0838 181  ARG A CA  
1194  C C   . ARG A 183  ? 0.2915 0.3808 0.3002 0.0114  0.0016  -0.0847 181  ARG A C   
1195  O O   . ARG A 183  ? 0.2847 0.3692 0.2918 0.0102  0.0013  -0.0810 181  ARG A O   
1196  C CB  A ARG A 183  ? 0.2809 0.3967 0.2857 0.0115  0.0024  -0.0915 181  ARG A CB  
1197  C CB  B ARG A 183  ? 0.2797 0.3954 0.2851 0.0117  0.0023  -0.0921 181  ARG A CB  
1198  C CG  A ARG A 183  ? 0.3418 0.4610 0.3475 0.0115  0.0011  -0.0946 181  ARG A CG  
1199  C CG  B ARG A 183  ? 0.3425 0.4633 0.3480 0.0116  0.0012  -0.0951 181  ARG A CG  
1200  C CD  A ARG A 183  ? 0.3518 0.4699 0.3515 0.0086  0.0018  -0.0869 181  ARG A CD  
1201  C CD  B ARG A 183  ? 0.3684 0.4958 0.3666 0.0087  0.0022  -0.0889 181  ARG A CD  
1202  N NE  A ARG A 183  ? 0.3402 0.4670 0.3335 0.0064  0.0033  -0.0819 181  ARG A NE  
1203  N NE  B ARG A 183  ? 0.3395 0.4555 0.3360 0.0070  0.0022  -0.0818 181  ARG A NE  
1204  C CZ  A ARG A 183  ? 0.3710 0.4960 0.3591 0.0037  0.0040  -0.0739 181  ARG A CZ  
1205  C CZ  B ARG A 183  ? 0.3917 0.5078 0.3824 0.0043  0.0031  -0.0740 181  ARG A CZ  
1206  N NH1 A ARG A 183  ? 0.3952 0.5102 0.3833 0.0029  0.0035  -0.0699 181  ARG A NH1 
1207  N NH1 B ARG A 183  ? 0.3875 0.5141 0.3736 0.0027  0.0042  -0.0714 181  ARG A NH1 
1208  N NH2 A ARG A 183  ? 0.3986 0.5323 0.3819 0.0017  0.0051  -0.0696 181  ARG A NH2 
1209  N NH2 B ARG A 183  ? 0.3649 0.4705 0.3548 0.0031  0.0029  -0.0686 181  ARG A NH2 
1210  N N   . ARG A 184  ? 0.2641 0.3485 0.2794 0.0138  0.0006  -0.0893 182  ARG A N   
1211  C CA  . ARG A 184  ? 0.2738 0.3472 0.2950 0.0149  -0.0008 -0.0901 182  ARG A CA  
1212  C C   . ARG A 184  ? 0.2674 0.3287 0.2861 0.0134  0.0000  -0.0818 182  ARG A C   
1213  O O   . ARG A 184  ? 0.2619 0.3160 0.2821 0.0130  -0.0007 -0.0798 182  ARG A O   
1214  C CB  . ARG A 184  ? 0.2958 0.3670 0.3251 0.0177  -0.0022 -0.0964 182  ARG A CB  
1215  C CG  . ARG A 184  ? 0.3588 0.4404 0.3926 0.0196  -0.0037 -0.1059 182  ARG A CG  
1216  C CD  . ARG A 184  ? 0.3796 0.4561 0.4198 0.0206  -0.0058 -0.1094 182  ARG A CD  
1217  N NE  . ARG A 184  ? 0.3860 0.4533 0.4351 0.0226  -0.0075 -0.1118 182  ARG A NE  
1218  C CZ  . ARG A 184  ? 0.3740 0.4291 0.4265 0.0223  -0.0081 -0.1075 182  ARG A CZ  
1219  N NH1 . ARG A 184  ? 0.3967 0.4470 0.4446 0.0202  -0.0073 -0.1012 182  ARG A NH1 
1220  N NH2 . ARG A 184  ? 0.3203 0.3681 0.3812 0.0241  -0.0098 -0.1097 182  ARG A NH2 
1221  N N   . GLY A 185  ? 0.2436 0.3026 0.2587 0.0126  0.0013  -0.0772 183  GLY A N   
1222  C CA  . GLY A 185  ? 0.2324 0.2810 0.2448 0.0113  0.0021  -0.0696 183  GLY A CA  
1223  C C   . GLY A 185  ? 0.2683 0.3174 0.2753 0.0090  0.0027  -0.0647 183  GLY A C   
1224  O O   . GLY A 185  ? 0.2429 0.2836 0.2501 0.0085  0.0025  -0.0610 183  GLY A O   
1225  N N   . VAL A 186  ? 0.2518 0.3112 0.2542 0.0077  0.0033  -0.0645 184  VAL A N   
1226  C CA  . VAL A 186  ? 0.2810 0.3417 0.2786 0.0054  0.0037  -0.0597 184  VAL A CA  
1227  C C   . VAL A 186  ? 0.2806 0.3394 0.2810 0.0058  0.0024  -0.0619 184  VAL A C   
1228  O O   . VAL A 186  ? 0.2538 0.3063 0.2528 0.0047  0.0024  -0.0573 184  VAL A O   
1229  C CB  . VAL A 186  ? 0.2621 0.3356 0.2550 0.0040  0.0043  -0.0594 184  VAL A CB  
1230  C CG1 . VAL A 186  ? 0.2810 0.3574 0.2702 0.0019  0.0042  -0.0555 184  VAL A CG1 
1231  C CG2 . VAL A 186  ? 0.2622 0.3360 0.2520 0.0029  0.0055  -0.0552 184  VAL A CG2 
1232  N N   . ASP A 187  ? 0.2481 0.3122 0.2529 0.0076  0.0013  -0.0692 185  ASP A N   
1233  C CA  . ASP A 187  ? 0.2956 0.3587 0.3034 0.0079  -0.0001 -0.0718 185  ASP A CA  
1234  C C   . ASP A 187  ? 0.3474 0.3975 0.3598 0.0086  -0.0007 -0.0700 185  ASP A C   
1235  O O   . ASP A 187  ? 0.3309 0.3768 0.3436 0.0079  -0.0012 -0.0679 185  ASP A O   
1236  C CB  . ASP A 187  ? 0.3022 0.3745 0.3144 0.0098  -0.0014 -0.0807 185  ASP A CB  
1237  C CG  . ASP A 187  ? 0.3518 0.4387 0.3591 0.0089  -0.0008 -0.0824 185  ASP A CG  
1238  O OD1 . ASP A 187  ? 0.3955 0.4851 0.3966 0.0066  0.0003  -0.0763 185  ASP A OD1 
1239  O OD2 . ASP A 187  ? 0.3852 0.4813 0.3953 0.0105  -0.0016 -0.0898 185  ASP A OD2 
1240  N N   . MET A 188  ? 0.3133 0.3572 0.3292 0.0100  -0.0007 -0.0704 186  MET A N   
1241  C CA  . MET A 188  ? 0.2978 0.3299 0.3179 0.0105  -0.0011 -0.0679 186  MET A CA  
1242  C C   . MET A 188  ? 0.3134 0.3388 0.3285 0.0087  0.0001  -0.0600 186  MET A C   
1243  O O   . MET A 188  ? 0.3011 0.3201 0.3177 0.0084  -0.0003 -0.0576 186  MET A O   
1244  C CB  . MET A 188  ? 0.3259 0.3539 0.3503 0.0122  -0.0014 -0.0696 186  MET A CB  
1245  C CG  . MET A 188  ? 0.4218 0.4386 0.4512 0.0129  -0.0020 -0.0671 186  MET A CG  
1246  S SD  . MET A 188  ? 0.5187 0.5338 0.5564 0.0139  -0.0043 -0.0720 186  MET A SD  
1247  C CE  . MET A 188  ? 0.4110 0.4353 0.4538 0.0161  -0.0058 -0.0816 186  MET A CE  
1248  N N   . ALA A 189  ? 0.2743 0.3010 0.2839 0.0076  0.0015  -0.0559 187  ALA A N   
1249  C CA  . ALA A 189  ? 0.2739 0.2947 0.2790 0.0060  0.0025  -0.0489 187  ALA A CA  
1250  C C   . ALA A 189  ? 0.3021 0.3251 0.3046 0.0045  0.0023  -0.0469 187  ALA A C   
1251  O O   . ALA A 189  ? 0.2900 0.3064 0.2920 0.0039  0.0025  -0.0428 187  ALA A O   
1252  C CB  . ALA A 189  ? 0.2837 0.3067 0.2839 0.0050  0.0038  -0.0455 187  ALA A CB  
1253  N N   . MET A 190  ? 0.2780 0.3109 0.2789 0.0040  0.0020  -0.0499 188  MET A N   
1254  C CA  . MET A 190  ? 0.2836 0.3195 0.2820 0.0026  0.0017  -0.0481 188  MET A CA  
1255  C C   . MET A 190  ? 0.2981 0.3286 0.3010 0.0033  0.0006  -0.0496 188  MET A C   
1256  O O   . MET A 190  ? 0.3144 0.3406 0.3159 0.0023  0.0006  -0.0455 188  MET A O   
1257  C CB  . MET A 190  ? 0.2949 0.3436 0.2914 0.0022  0.0013  -0.0517 188  MET A CB  
1258  C CG  . MET A 190  ? 0.3939 0.4471 0.3870 0.0004  0.0011  -0.0489 188  MET A CG  
1259  S SD  . MET A 190  ? 0.4793 0.5487 0.4705 0.0002  0.0006  -0.0538 188  MET A SD  
1260  C CE  . MET A 190  ? 0.3983 0.4735 0.3874 0.0002  0.0018  -0.0540 188  MET A CE  
1261  N N   . ARG A 191  ? 0.2594 0.2899 0.2682 0.0051  -0.0005 -0.0554 189  ARG A N   
1262  C CA  . ARG A 191  ? 0.3078 0.3330 0.3219 0.0058  -0.0018 -0.0570 189  ARG A CA  
1263  C C   . ARG A 191  ? 0.3108 0.3248 0.3262 0.0057  -0.0012 -0.0519 189  ARG A C   
1264  O O   . ARG A 191  ? 0.3084 0.3179 0.3247 0.0051  -0.0015 -0.0495 189  ARG A O   
1265  C CB  . ARG A 191  ? 0.3215 0.3488 0.3425 0.0078  -0.0033 -0.0645 189  ARG A CB  
1266  C CG  . ARG A 191  ? 0.4440 0.4670 0.4715 0.0084  -0.0049 -0.0667 189  ARG A CG  
1267  C CD  . ARG A 191  ? 0.5576 0.5833 0.5926 0.0104  -0.0068 -0.0746 189  ARG A CD  
1268  N NE  . ARG A 191  ? 0.6633 0.6844 0.7020 0.0117  -0.0068 -0.0752 189  ARG A NE  
1269  C CZ  . ARG A 191  ? 0.7756 0.7870 0.8189 0.0122  -0.0071 -0.0724 189  ARG A CZ  
1270  N NH1 . ARG A 191  ? 0.8772 0.8822 0.9219 0.0113  -0.0073 -0.0686 189  ARG A NH1 
1271  N NH2 . ARG A 191  ? 0.7394 0.7476 0.7860 0.0134  -0.0072 -0.0731 189  ARG A NH2 
1272  N N   . MET A 192  ? 0.2821 0.2917 0.2976 0.0063  -0.0005 -0.0502 190  MET A N   
1273  C CA  . MET A 192  ? 0.2973 0.2972 0.3142 0.0064  0.0000  -0.0456 190  MET A CA  
1274  C C   . MET A 192  ? 0.3163 0.3137 0.3276 0.0048  0.0011  -0.0395 190  MET A C   
1275  O O   . MET A 192  ? 0.3090 0.3007 0.3216 0.0045  0.0011  -0.0366 190  MET A O   
1276  C CB  . MET A 192  ? 0.3221 0.3188 0.3400 0.0074  0.0005  -0.0452 190  MET A CB  
1277  C CG  . MET A 192  ? 0.3136 0.3109 0.3384 0.0092  -0.0009 -0.0508 190  MET A CG  
1278  S SD  . MET A 192  ? 0.4294 0.4230 0.4554 0.0103  -0.0003 -0.0498 190  MET A SD  
1279  C CE  . MET A 192  ? 0.3962 0.3793 0.4246 0.0103  -0.0002 -0.0441 190  MET A CE  
1280  N N   . MET A 193  ? 0.2909 0.2926 0.2964 0.0037  0.0020  -0.0375 191  MET A N   
1281  C CA  A MET A 193  ? 0.3131 0.3124 0.3140 0.0023  0.0028  -0.0318 191  MET A CA  
1282  C CA  B MET A 193  ? 0.3133 0.3125 0.3143 0.0023  0.0028  -0.0318 191  MET A CA  
1283  C C   . MET A 193  ? 0.3286 0.3307 0.3284 0.0012  0.0023  -0.0311 191  MET A C   
1284  O O   . MET A 193  ? 0.3566 0.3549 0.3543 0.0003  0.0027  -0.0266 191  MET A O   
1285  C CB  A MET A 193  ? 0.2966 0.2994 0.2926 0.0014  0.0037  -0.0296 191  MET A CB  
1286  C CB  B MET A 193  ? 0.2976 0.2998 0.2938 0.0014  0.0038  -0.0294 191  MET A CB  
1287  C CG  A MET A 193  ? 0.3083 0.3092 0.3052 0.0024  0.0043  -0.0305 191  MET A CG  
1288  C CG  B MET A 193  ? 0.3131 0.3107 0.3099 0.0024  0.0044  -0.0287 191  MET A CG  
1289  S SD  A MET A 193  ? 0.3456 0.3508 0.3371 0.0012  0.0052  -0.0278 191  MET A SD  
1290  S SD  B MET A 193  ? 0.3593 0.3581 0.3505 0.0011  0.0054  -0.0245 191  MET A SD  
1291  C CE  A MET A 193  ? 0.3988 0.3960 0.3879 0.0004  0.0058  -0.0214 191  MET A CE  
1292  C CE  B MET A 193  ? 0.3776 0.3879 0.3670 0.0003  0.0052  -0.0276 191  MET A CE  
1293  N N   . GLY A 194  ? 0.3155 0.3242 0.3168 0.0013  0.0013  -0.0355 192  GLY A N   
1294  C CA  . GLY A 194  ? 0.3660 0.3782 0.3662 0.0002  0.0007  -0.0349 192  GLY A CA  
1295  C C   . GLY A 194  ? 0.3570 0.3662 0.3621 0.0009  -0.0004 -0.0372 192  GLY A C   
1296  O O   . GLY A 194  ? 0.3582 0.3678 0.3625 0.0000  -0.0009 -0.0355 192  GLY A O   
1297  N N   . GLU A 195  ? 0.3134 0.3196 0.3241 0.0024  -0.0010 -0.0410 193  GLU A N   
1298  C CA  . GLU A 195  ? 0.3063 0.3104 0.3228 0.0031  -0.0024 -0.0438 193  GLU A CA  
1299  C C   . GLU A 195  ? 0.2843 0.2796 0.3061 0.0040  -0.0025 -0.0427 193  GLU A C   
1300  O O   . GLU A 195  ? 0.2878 0.2802 0.3143 0.0041  -0.0034 -0.0432 193  GLU A O   
1301  C CB  . GLU A 195  ? 0.3526 0.3639 0.3727 0.0040  -0.0038 -0.0510 193  GLU A CB  
1302  C CG  . GLU A 195  ? 0.4482 0.4699 0.4634 0.0032  -0.0038 -0.0528 193  GLU A CG  
1303  C CD  . GLU A 195  ? 0.5713 0.6005 0.5901 0.0045  -0.0051 -0.0605 193  GLU A CD  
1304  O OE1 . GLU A 195  ? 0.5831 0.6091 0.6089 0.0058  -0.0065 -0.0647 193  GLU A OE1 
1305  O OE2 . GLU A 195  ? 0.6887 0.7270 0.7037 0.0043  -0.0048 -0.0625 193  GLU A OE2 
1306  N N   . GLN A 196  ? 0.3238 0.3154 0.3456 0.0047  -0.0016 -0.0412 194  GLN A N   
1307  C CA  . GLN A 196  ? 0.3066 0.2907 0.3337 0.0055  -0.0018 -0.0399 194  GLN A CA  
1308  C C   . GLN A 196  ? 0.3277 0.3057 0.3516 0.0050  -0.0004 -0.0335 194  GLN A C   
1309  O O   . GLN A 196  ? 0.3725 0.3457 0.3994 0.0049  -0.0005 -0.0309 194  GLN A O   
1310  C CB  . GLN A 196  ? 0.3235 0.3077 0.3539 0.0069  -0.0023 -0.0433 194  GLN A CB  
1311  N N   . PHE A 197  ? 0.2857 0.2643 0.3039 0.0046  0.0009  -0.0309 195  PHE A N   
1312  C CA  . PHE A 197  ? 0.3119 0.2855 0.3271 0.0042  0.0022  -0.0253 195  PHE A CA  
1313  C C   . PHE A 197  ? 0.3229 0.2965 0.3352 0.0031  0.0025  -0.0225 195  PHE A C   
1314  O O   . PHE A 197  ? 0.3590 0.3281 0.3703 0.0029  0.0033  -0.0184 195  PHE A O   
1315  C CB  . PHE A 197  ? 0.3480 0.3225 0.3583 0.0041  0.0033  -0.0238 195  PHE A CB  
1316  C CG  . PHE A 197  ? 0.3982 0.3723 0.4111 0.0053  0.0031  -0.0261 195  PHE A CG  
1317  C CD1 . PHE A 197  ? 0.4041 0.3739 0.4228 0.0063  0.0025  -0.0265 195  PHE A CD1 
1318  C CD2 . PHE A 197  ? 0.3722 0.3506 0.3821 0.0053  0.0035  -0.0276 195  PHE A CD2 
1319  C CE1 . PHE A 197  ? 0.4769 0.4464 0.4984 0.0075  0.0022  -0.0285 195  PHE A CE1 
1320  C CE2 . PHE A 197  ? 0.3931 0.3712 0.4055 0.0064  0.0033  -0.0298 195  PHE A CE2 
1321  C CZ  . PHE A 197  ? 0.3562 0.3298 0.3745 0.0076  0.0026  -0.0303 195  PHE A CZ  
1322  N N   . VAL A 198  ? 0.2725 0.2515 0.2833 0.0023  0.0018  -0.0245 196  VAL A N   
1323  C CA  . VAL A 198  ? 0.2733 0.2527 0.2823 0.0013  0.0017  -0.0221 196  VAL A CA  
1324  C C   . VAL A 198  ? 0.2658 0.2492 0.2781 0.0012  0.0003  -0.0260 196  VAL A C   
1325  O O   . VAL A 198  ? 0.3214 0.3092 0.3357 0.0017  -0.0005 -0.0307 196  VAL A O   
1326  C CB  . VAL A 198  ? 0.2646 0.2472 0.2676 0.0001  0.0023  -0.0194 196  VAL A CB  
1327  C CG1 . VAL A 198  ? 0.3101 0.2885 0.3102 0.0002  0.0035  -0.0157 196  VAL A CG1 
1328  C CG2 . VAL A 198  ? 0.3046 0.2951 0.3056 -0.0003 0.0018  -0.0225 196  VAL A CG2 
1329  N N   . THR A 199  ? 0.2571 0.2391 0.2703 0.0006  0.0000  -0.0243 197  THR A N   
1330  C CA  . THR A 199  ? 0.2665 0.2529 0.2822 0.0004  -0.0014 -0.0278 197  THR A CA  
1331  C C   . THR A 199  ? 0.3137 0.3078 0.3246 -0.0006 -0.0017 -0.0286 197  THR A C   
1332  O O   . THR A 199  ? 0.3432 0.3435 0.3554 -0.0005 -0.0028 -0.0331 197  THR A O   
1333  C CB  . THR A 199  ? 0.2854 0.2682 0.3036 0.0000  -0.0017 -0.0255 197  THR A CB  
1334  O OG1 . THR A 199  ? 0.3092 0.2856 0.3318 0.0008  -0.0014 -0.0241 197  THR A OG1 
1335  C CG2 . THR A 199  ? 0.3384 0.3254 0.3600 -0.0001 -0.0033 -0.0294 197  THR A CG2 
1336  N N   . GLY A 200  ? 0.2740 0.2682 0.2797 -0.0015 -0.0007 -0.0243 198  GLY A N   
1337  C CA  . GLY A 200  ? 0.2848 0.2864 0.2860 -0.0026 -0.0009 -0.0240 198  GLY A CA  
1338  C C   . GLY A 200  ? 0.2618 0.2615 0.2586 -0.0033 0.0001  -0.0191 198  GLY A C   
1339  O O   . GLY A 200  ? 0.2568 0.2496 0.2538 -0.0030 0.0009  -0.0160 198  GLY A O   
1340  N N   . GLU A 201  ? 0.2748 0.2812 0.2679 -0.0044 0.0000  -0.0185 199  GLU A N   
1341  C CA  . GLU A 201  ? 0.2751 0.2801 0.2645 -0.0053 0.0007  -0.0139 199  GLU A CA  
1342  C C   . GLU A 201  ? 0.2950 0.2974 0.2834 -0.0062 0.0003  -0.0093 199  GLU A C   
1343  O O   . GLU A 201  ? 0.3167 0.3146 0.3038 -0.0064 0.0008  -0.0056 199  GLU A O   
1344  C CB  . GLU A 201  ? 0.3165 0.3301 0.3028 -0.0063 0.0006  -0.0143 199  GLU A CB  
1345  C CG  . GLU A 201  ? 0.4430 0.4560 0.4260 -0.0075 0.0010  -0.0095 199  GLU A CG  
1346  C CD  . GLU A 201  ? 0.5877 0.6100 0.5680 -0.0086 0.0009  -0.0097 199  GLU A CD  
1347  O OE1 . GLU A 201  ? 0.6277 0.6574 0.6083 -0.0084 0.0005  -0.0137 199  GLU A OE1 
1348  O OE2 . GLU A 201  ? 0.6903 0.7129 0.6684 -0.0097 0.0011  -0.0059 199  GLU A OE2 
1349  N N   . THR A 202  ? 0.2660 0.2715 0.2554 -0.0067 -0.0006 -0.0099 200  THR A N   
1350  C CA  . THR A 202  ? 0.2572 0.2607 0.2463 -0.0074 -0.0012 -0.0059 200  THR A CA  
1351  C C   . THR A 202  ? 0.2395 0.2405 0.2321 -0.0067 -0.0016 -0.0077 200  THR A C   
1352  O O   . THR A 202  ? 0.2530 0.2556 0.2481 -0.0060 -0.0019 -0.0121 200  THR A O   
1353  C CB  . THR A 202  ? 0.2865 0.2979 0.2731 -0.0091 -0.0022 -0.0041 200  THR A CB  
1354  O OG1 . THR A 202  ? 0.3077 0.3258 0.2952 -0.0090 -0.0030 -0.0084 200  THR A OG1 
1355  C CG2 . THR A 202  ? 0.3190 0.3344 0.3024 -0.0101 -0.0019 -0.0022 200  THR A CG2 
1356  N N   . ILE A 203  ? 0.2474 0.2445 0.2405 -0.0070 -0.0018 -0.0043 201  ILE A N   
1357  C CA  . ILE A 203  ? 0.2603 0.2548 0.2570 -0.0064 -0.0022 -0.0056 201  ILE A CA  
1358  C C   . ILE A 203  ? 0.2589 0.2604 0.2565 -0.0069 -0.0035 -0.0087 201  ILE A C   
1359  O O   . ILE A 203  ? 0.2556 0.2564 0.2568 -0.0062 -0.0039 -0.0121 201  ILE A O   
1360  C CB  . ILE A 203  ? 0.2415 0.2312 0.2387 -0.0064 -0.0021 -0.0015 201  ILE A CB  
1361  C CG1 . ILE A 203  ? 0.2223 0.2091 0.2236 -0.0058 -0.0023 -0.0029 201  ILE A CG1 
1362  C CG2 . ILE A 203  ? 0.2555 0.2492 0.2505 -0.0078 -0.0032 0.0017  201  ILE A CG2 
1363  C CD1 . ILE A 203  ? 0.2242 0.2067 0.2285 -0.0045 -0.0014 -0.0051 201  ILE A CD1 
1364  N N   . ARG A 204  ? 0.2530 0.2616 0.2476 -0.0081 -0.0043 -0.0077 202  ARG A N   
1365  C CA  . ARG A 204  ? 0.2670 0.2834 0.2620 -0.0085 -0.0056 -0.0109 202  ARG A CA  
1366  C C   . ARG A 204  ? 0.2477 0.2674 0.2443 -0.0076 -0.0055 -0.0168 202  ARG A C   
1367  O O   . ARG A 204  ? 0.2716 0.2936 0.2713 -0.0071 -0.0065 -0.0210 202  ARG A O   
1368  C CB  . ARG A 204  ? 0.3210 0.3452 0.3123 -0.0101 -0.0064 -0.0081 202  ARG A CB  
1369  C CG  . ARG A 204  ? 0.4081 0.4310 0.3993 -0.0110 -0.0072 -0.0035 202  ARG A CG  
1370  C CD  . ARG A 204  ? 0.4379 0.4665 0.4257 -0.0127 -0.0079 0.0010  202  ARG A CD  
1371  N NE  . ARG A 204  ? 0.4436 0.4709 0.4322 -0.0134 -0.0090 0.0053  202  ARG A NE  
1372  C CZ  . ARG A 204  ? 0.4332 0.4525 0.4231 -0.0131 -0.0087 0.0087  202  ARG A CZ  
1373  N NH1 . ARG A 204  ? 0.3514 0.3635 0.3418 -0.0121 -0.0073 0.0085  202  ARG A NH1 
1374  N NH2 . ARG A 204  ? 0.3726 0.3914 0.3635 -0.0137 -0.0099 0.0123  202  ARG A NH2 
1375  N N   . GLU A 205  ? 0.2583 0.2785 0.2532 -0.0073 -0.0046 -0.0175 203  GLU A N   
1376  C CA  . GLU A 205  ? 0.2729 0.2955 0.2698 -0.0062 -0.0047 -0.0233 203  GLU A CA  
1377  C C   . GLU A 205  ? 0.2677 0.2829 0.2698 -0.0049 -0.0046 -0.0256 203  GLU A C   
1378  O O   . GLU A 205  ? 0.2685 0.2859 0.2745 -0.0041 -0.0056 -0.0307 203  GLU A O   
1379  C CB  . GLU A 205  ? 0.2879 0.3118 0.2821 -0.0062 -0.0036 -0.0229 203  GLU A CB  
1380  C CG  . GLU A 205  ? 0.3338 0.3615 0.3300 -0.0050 -0.0037 -0.0291 203  GLU A CG  
1381  C CD  . GLU A 205  ? 0.4706 0.5012 0.4636 -0.0052 -0.0028 -0.0286 203  GLU A CD  
1382  O OE1 . GLU A 205  ? 0.3998 0.4237 0.3926 -0.0048 -0.0017 -0.0261 203  GLU A OE1 
1383  O OE2 . GLU A 205  ? 0.4956 0.5359 0.4864 -0.0057 -0.0031 -0.0306 203  GLU A OE2 
1384  N N   . ALA A 206  ? 0.2388 0.2456 0.2416 -0.0046 -0.0036 -0.0219 204  ALA A N   
1385  C CA  . ALA A 206  ? 0.2469 0.2469 0.2547 -0.0035 -0.0035 -0.0233 204  ALA A CA  
1386  C C   . ALA A 206  ? 0.2584 0.2589 0.2700 -0.0036 -0.0047 -0.0249 204  ALA A C   
1387  O O   . ALA A 206  ? 0.2657 0.2648 0.2825 -0.0027 -0.0055 -0.0286 204  ALA A O   
1388  C CB  . ALA A 206  ? 0.2579 0.2501 0.2651 -0.0033 -0.0021 -0.0185 204  ALA A CB  
1389  N N   . LEU A 207  ? 0.2329 0.2354 0.2425 -0.0046 -0.0052 -0.0221 205  LEU A N   
1390  C CA  . LEU A 207  ? 0.2342 0.2375 0.2473 -0.0047 -0.0064 -0.0234 205  LEU A CA  
1391  C C   . LEU A 207  ? 0.2758 0.2863 0.2910 -0.0045 -0.0079 -0.0294 205  LEU A C   
1392  O O   . LEU A 207  ? 0.2758 0.2852 0.2963 -0.0040 -0.0090 -0.0327 205  LEU A O   
1393  C CB  . LEU A 207  ? 0.2411 0.2456 0.2515 -0.0058 -0.0067 -0.0191 205  LEU A CB  
1394  C CG  . LEU A 207  ? 0.2509 0.2479 0.2611 -0.0057 -0.0055 -0.0141 205  LEU A CG  
1395  C CD1 . LEU A 207  ? 0.2526 0.2515 0.2597 -0.0067 -0.0059 -0.0099 205  LEU A CD1 
1396  C CD2 . LEU A 207  ? 0.2497 0.2416 0.2653 -0.0050 -0.0056 -0.0147 205  LEU A CD2 
1397  N N   . LYS A 208  ? 0.2504 0.2685 0.2617 -0.0049 -0.0081 -0.0310 206  LYS A N   
1398  C CA  . LYS A 208  ? 0.2659 0.2920 0.2789 -0.0045 -0.0095 -0.0373 206  LYS A CA  
1399  C C   . LYS A 208  ? 0.3164 0.3395 0.3350 -0.0030 -0.0099 -0.0425 206  LYS A C   
1400  O O   . LYS A 208  ? 0.3554 0.3810 0.3788 -0.0024 -0.0115 -0.0476 206  LYS A O   
1401  C CB  . LYS A 208  ? 0.3401 0.3754 0.3477 -0.0051 -0.0094 -0.0376 206  LYS A CB  
1402  N N   . ARG A 209  ? 0.2741 0.2920 0.2925 -0.0024 -0.0086 -0.0411 207  ARG A N   
1403  C CA  . ARG A 209  ? 0.3089 0.3236 0.3328 -0.0010 -0.0089 -0.0454 207  ARG A CA  
1404  C C   . ARG A 209  ? 0.3200 0.3267 0.3503 -0.0006 -0.0094 -0.0447 207  ARG A C   
1405  O O   . ARG A 209  ? 0.3691 0.3730 0.4052 0.0005  -0.0101 -0.0482 207  ARG A O   
1406  C CB  . ARG A 209  ? 0.3060 0.3184 0.3272 -0.0006 -0.0074 -0.0438 207  ARG A CB  
1407  C CG  . ARG A 209  ? 0.3365 0.3577 0.3527 -0.0009 -0.0072 -0.0455 207  ARG A CG  
1408  C CD  . ARG A 209  ? 0.3494 0.3680 0.3625 -0.0007 -0.0056 -0.0430 207  ARG A CD  
1409  N NE  . ARG A 209  ? 0.3985 0.4259 0.4069 -0.0012 -0.0053 -0.0442 207  ARG A NE  
1410  C CZ  . ARG A 209  ? 0.4702 0.4973 0.4754 -0.0012 -0.0041 -0.0422 207  ARG A CZ  
1411  N NH1 . ARG A 209  ? 0.3986 0.4172 0.4045 -0.0008 -0.0030 -0.0392 207  ARG A NH1 
1412  N NH2 . ARG A 209  ? 0.5152 0.5512 0.5165 -0.0018 -0.0039 -0.0432 207  ARG A NH2 
1413  N N   . SER A 210  ? 0.2908 0.2937 0.3204 -0.0014 -0.0090 -0.0401 208  SER A N   
1414  C CA  . SER A 210  ? 0.2651 0.2609 0.3007 -0.0012 -0.0092 -0.0387 208  SER A CA  
1415  C C   . SER A 210  ? 0.2957 0.2937 0.3372 -0.0012 -0.0113 -0.0428 208  SER A C   
1416  O O   . SER A 210  ? 0.2919 0.2847 0.3399 -0.0009 -0.0119 -0.0427 208  SER A O   
1417  C CB  . SER A 210  ? 0.2643 0.2555 0.2969 -0.0019 -0.0079 -0.0322 208  SER A CB  
1418  O OG  . SER A 210  ? 0.3061 0.2944 0.3343 -0.0018 -0.0061 -0.0286 208  SER A OG  
1419  N N   . LYS A 211  ? 0.3008 0.3067 0.3404 -0.0015 -0.0125 -0.0462 209  LYS A N   
1420  C CA  . LYS A 211  ? 0.2991 0.3076 0.3438 -0.0016 -0.0145 -0.0499 209  LYS A CA  
1421  C C   . LYS A 211  ? 0.3176 0.3244 0.3707 -0.0005 -0.0162 -0.0556 209  LYS A C   
1422  O O   . LYS A 211  ? 0.3277 0.3318 0.3876 -0.0005 -0.0176 -0.0567 209  LYS A O   
1423  C CB  . LYS A 211  ? 0.3659 0.3844 0.4063 -0.0021 -0.0155 -0.0527 209  LYS A CB  
1424  N N   . GLU A 212  ? 0.3243 0.3327 0.3777 0.0005  -0.0161 -0.0591 210  GLU A N   
1425  C CA  . GLU A 212  ? 0.3572 0.3647 0.4191 0.0018  -0.0181 -0.0652 210  GLU A CA  
1426  C C   . GLU A 212  ? 0.3633 0.3614 0.4325 0.0018  -0.0183 -0.0623 210  GLU A C   
1427  O O   . GLU A 212  ? 0.3728 0.3695 0.4503 0.0020  -0.0204 -0.0655 210  GLU A O   
1428  C CB  . GLU A 212  ? 0.4061 0.4163 0.4667 0.0029  -0.0177 -0.0687 210  GLU A CB  
1429  C CG  . GLU A 212  ? 0.4997 0.5086 0.5697 0.0044  -0.0198 -0.0751 210  GLU A CG  
1430  C CD  . GLU A 212  ? 0.6604 0.6718 0.7294 0.0056  -0.0194 -0.0783 210  GLU A CD  
1431  O OE1 . GLU A 212  ? 0.7126 0.7275 0.7733 0.0053  -0.0175 -0.0759 210  GLU A OE1 
1432  O OE2 . GLU A 212  ? 0.7422 0.7520 0.8192 0.0070  -0.0211 -0.0833 210  GLU A OE2 
1433  N N   . LEU A 213  ? 0.3141 0.3060 0.3806 0.0015  -0.0162 -0.0562 211  LEU A N   
1434  C CA  . LEU A 213  ? 0.3154 0.2992 0.3885 0.0015  -0.0163 -0.0529 211  LEU A CA  
1435  C C   . LEU A 213  ? 0.3067 0.2880 0.3809 0.0003  -0.0161 -0.0486 211  LEU A C   
1436  O O   . LEU A 213  ? 0.2982 0.2749 0.3801 0.0002  -0.0171 -0.0477 211  LEU A O   
1437  C CB  . LEU A 213  ? 0.2747 0.2535 0.3450 0.0018  -0.0142 -0.0483 211  LEU A CB  
1438  C CG  . LEU A 213  ? 0.3407 0.3205 0.4129 0.0031  -0.0148 -0.0526 211  LEU A CG  
1439  C CD1 . LEU A 213  ? 0.3373 0.3123 0.4069 0.0033  -0.0128 -0.0478 211  LEU A CD1 
1440  C CD2 . LEU A 213  ? 0.3770 0.3554 0.4602 0.0038  -0.0175 -0.0576 211  LEU A CD2 
1441  N N   . GLU A 214  ? 0.2690 0.2534 0.3361 -0.0005 -0.0151 -0.0460 212  GLU A N   
1442  C CA  . GLU A 214  ? 0.2801 0.2630 0.3487 -0.0014 -0.0152 -0.0429 212  GLU A CA  
1443  C C   . GLU A 214  ? 0.3121 0.2972 0.3884 -0.0015 -0.0179 -0.0479 212  GLU A C   
1444  O O   . GLU A 214  ? 0.3441 0.3256 0.4263 -0.0020 -0.0186 -0.0460 212  GLU A O   
1445  C CB  . GLU A 214  ? 0.2765 0.2630 0.3367 -0.0022 -0.0140 -0.0399 212  GLU A CB  
1446  C CG  . GLU A 214  ? 0.2883 0.2713 0.3424 -0.0023 -0.0115 -0.0340 212  GLU A CG  
1447  C CD  . GLU A 214  ? 0.3016 0.2874 0.3486 -0.0030 -0.0106 -0.0307 212  GLU A CD  
1448  O OE1 . GLU A 214  ? 0.3335 0.3254 0.3789 -0.0035 -0.0119 -0.0332 212  GLU A OE1 
1449  O OE2 . GLU A 214  ? 0.3525 0.3348 0.3958 -0.0032 -0.0089 -0.0257 212  GLU A OE2 
1450  N N   . GLU A 215  ? 0.3149 0.3063 0.3916 -0.0009 -0.0196 -0.0546 213  GLU A N   
1451  C CA  . GLU A 215  ? 0.3658 0.3599 0.4499 -0.0008 -0.0224 -0.0603 213  GLU A CA  
1452  C C   . GLU A 215  ? 0.4195 0.4078 0.5145 -0.0003 -0.0240 -0.0618 213  GLU A C   
1453  O O   . GLU A 215  ? 0.4284 0.4166 0.5311 -0.0005 -0.0263 -0.0647 213  GLU A O   
1454  C CB  . GLU A 215  ? 0.3818 0.3848 0.4637 0.0000  -0.0237 -0.0675 213  GLU A CB  
1455  N N   . LYS A 216  ? 0.3996 0.3830 0.4955 0.0002  -0.0229 -0.0596 214  LYS A N   
1456  C CA  . LYS A 216  ? 0.3837 0.3613 0.4900 0.0006  -0.0244 -0.0602 214  LYS A CA  
1457  C C   . LYS A 216  ? 0.4219 0.3927 0.5307 -0.0004 -0.0232 -0.0525 214  LYS A C   
1458  O O   . LYS A 216  ? 0.4629 0.4289 0.5810 -0.0004 -0.0245 -0.0518 214  LYS A O   
1459  C CB  . LYS A 216  ? 0.3519 0.3288 0.4587 0.0019  -0.0242 -0.0625 214  LYS A CB  
1460  C CG  . LYS A 216  ? 0.4795 0.4638 0.5851 0.0030  -0.0257 -0.0707 214  LYS A CG  
1461  C CD  . LYS A 216  ? 0.6281 0.6120 0.7339 0.0044  -0.0255 -0.0732 214  LYS A CD  
1462  C CE  . LYS A 216  ? 0.6075 0.5997 0.7133 0.0057  -0.0271 -0.0820 214  LYS A CE  
1463  N NZ  . LYS A 216  ? 0.7780 0.7715 0.8817 0.0070  -0.0264 -0.0841 214  LYS A NZ  
1464  N N   . GLY A 217  ? 0.3317 0.3023 0.4330 -0.0012 -0.0208 -0.0468 215  GLY A N   
1465  C CA  . GLY A 217  ? 0.3234 0.2887 0.4265 -0.0021 -0.0195 -0.0398 215  GLY A CA  
1466  C C   . GLY A 217  ? 0.2891 0.2516 0.3854 -0.0020 -0.0166 -0.0340 215  GLY A C   
1467  O O   . GLY A 217  ? 0.3440 0.3029 0.4414 -0.0026 -0.0153 -0.0281 215  GLY A O   
1468  N N   . PHE A 218  ? 0.2922 0.2567 0.3816 -0.0012 -0.0155 -0.0355 216  PHE A N   
1469  C CA  . PHE A 218  ? 0.2405 0.2029 0.3231 -0.0011 -0.0128 -0.0302 216  PHE A CA  
1470  C C   . PHE A 218  ? 0.2627 0.2272 0.3372 -0.0017 -0.0112 -0.0272 216  PHE A C   
1471  O O   . PHE A 218  ? 0.2653 0.2340 0.3381 -0.0021 -0.0121 -0.0297 216  PHE A O   
1472  C CB  . PHE A 218  ? 0.2413 0.2051 0.3196 -0.0001 -0.0124 -0.0328 216  PHE A CB  
1473  C CG  . PHE A 218  ? 0.2713 0.2322 0.3568 0.0007  -0.0135 -0.0348 216  PHE A CG  
1474  C CD1 . PHE A 218  ? 0.3089 0.2716 0.4015 0.0012  -0.0162 -0.0412 216  PHE A CD1 
1475  C CD2 . PHE A 218  ? 0.2603 0.2170 0.3454 0.0010  -0.0121 -0.0305 216  PHE A CD2 
1476  C CE1 . PHE A 218  ? 0.2920 0.2518 0.3917 0.0021  -0.0175 -0.0431 216  PHE A CE1 
1477  C CE2 . PHE A 218  ? 0.2945 0.2485 0.3864 0.0017  -0.0134 -0.0320 216  PHE A CE2 
1478  C CZ  . PHE A 218  ? 0.2936 0.2490 0.3931 0.0022  -0.0161 -0.0383 216  PHE A CZ  
1479  N N   . SER A 219  ? 0.2452 0.2071 0.3150 -0.0017 -0.0090 -0.0218 217  SER A N   
1480  C CA  . SER A 219  ? 0.2392 0.2028 0.3011 -0.0020 -0.0074 -0.0189 217  SER A CA  
1481  C C   . SER A 219  ? 0.2459 0.2089 0.3012 -0.0015 -0.0057 -0.0174 217  SER A C   
1482  O O   . SER A 219  ? 0.2214 0.1828 0.2782 -0.0008 -0.0057 -0.0184 217  SER A O   
1483  C CB  . SER A 219  ? 0.2655 0.2267 0.3285 -0.0026 -0.0064 -0.0139 217  SER A CB  
1484  O OG  . SER A 219  ? 0.2920 0.2493 0.3571 -0.0023 -0.0052 -0.0102 217  SER A OG  
1485  N N   . TYR A 220  ? 0.2212 0.1854 0.2695 -0.0017 -0.0044 -0.0148 218  TYR A N   
1486  C CA  . TYR A 220  ? 0.2203 0.1844 0.2622 -0.0013 -0.0030 -0.0135 218  TYR A CA  
1487  C C   . TYR A 220  ? 0.2222 0.1841 0.2601 -0.0013 -0.0012 -0.0085 218  TYR A C   
1488  O O   . TYR A 220  ? 0.2169 0.1792 0.2548 -0.0017 -0.0012 -0.0067 218  TYR A O   
1489  C CB  . TYR A 220  ? 0.2348 0.2039 0.2718 -0.0015 -0.0036 -0.0165 218  TYR A CB  
1490  C CG  . TYR A 220  ? 0.2181 0.1897 0.2577 -0.0011 -0.0048 -0.0216 218  TYR A CG  
1491  C CD1 . TYR A 220  ? 0.2680 0.2421 0.3127 -0.0011 -0.0067 -0.0259 218  TYR A CD1 
1492  C CD2 . TYR A 220  ? 0.2392 0.2107 0.2763 -0.0005 -0.0041 -0.0223 218  TYR A CD2 
1493  C CE1 . TYR A 220  ? 0.2491 0.2257 0.2968 -0.0005 -0.0080 -0.0312 218  TYR A CE1 
1494  C CE2 . TYR A 220  ? 0.2446 0.2185 0.2842 0.0001  -0.0052 -0.0273 218  TYR A CE2 
1495  C CZ  . TYR A 220  ? 0.2573 0.2339 0.3024 0.0001  -0.0072 -0.0318 218  TYR A CZ  
1496  O OH  . TYR A 220  ? 0.2758 0.2551 0.3239 0.0009  -0.0084 -0.0373 218  TYR A OH  
1497  N N   . SER A 221  ? 0.2205 0.1805 0.2552 -0.0007 0.0001  -0.0067 219  SER A N   
1498  C CA  . SER A 221  ? 0.2240 0.1828 0.2538 -0.0005 0.0016  -0.0030 219  SER A CA  
1499  C C   . SER A 221  ? 0.2088 0.1686 0.2331 -0.0003 0.0021  -0.0037 219  SER A C   
1500  O O   . SER A 221  ? 0.2575 0.2163 0.2823 0.0002  0.0023  -0.0047 219  SER A O   
1501  C CB  . SER A 221  ? 0.2594 0.2147 0.2911 0.0001  0.0029  0.0004  219  SER A CB  
1502  O OG  . SER A 221  ? 0.2566 0.2113 0.2839 0.0004  0.0042  0.0034  219  SER A OG  
1503  N N   . TYR A 222  ? 0.1945 0.1563 0.2142 -0.0008 0.0021  -0.0029 220  TYR A N   
1504  C CA  . TYR A 222  ? 0.2073 0.1709 0.2224 -0.0009 0.0022  -0.0035 220  TYR A CA  
1505  C C   . TYR A 222  ? 0.2489 0.2096 0.2607 -0.0003 0.0036  -0.0005 220  TYR A C   
1506  O O   . TYR A 222  ? 0.2490 0.2082 0.2601 -0.0002 0.0041  0.0021  220  TYR A O   
1507  C CB  . TYR A 222  ? 0.2187 0.1868 0.2310 -0.0018 0.0012  -0.0042 220  TYR A CB  
1508  C CG  . TYR A 222  ? 0.2016 0.1734 0.2169 -0.0022 -0.0002 -0.0078 220  TYR A CG  
1509  C CD1 . TYR A 222  ? 0.2117 0.1864 0.2273 -0.0021 -0.0007 -0.0116 220  TYR A CD1 
1510  C CD2 . TYR A 222  ? 0.2006 0.1731 0.2186 -0.0026 -0.0010 -0.0078 220  TYR A CD2 
1511  C CE1 . TYR A 222  ? 0.2261 0.2045 0.2449 -0.0023 -0.0022 -0.0156 220  TYR A CE1 
1512  C CE2 . TYR A 222  ? 0.2230 0.1990 0.2441 -0.0029 -0.0025 -0.0115 220  TYR A CE2 
1513  C CZ  . TYR A 222  ? 0.2239 0.2028 0.2453 -0.0027 -0.0031 -0.0155 220  TYR A CZ  
1514  O OH  . TYR A 222  ? 0.2632 0.2461 0.2880 -0.0028 -0.0046 -0.0198 220  TYR A OH  
1515  N N   . ASP A 223  ? 0.2580 0.2184 0.2681 0.0000  0.0040  -0.0013 221  ASP A N   
1516  C CA  . ASP A 223  ? 0.3074 0.2655 0.3144 0.0006  0.0052  0.0009  221  ASP A CA  
1517  C C   . ASP A 223  ? 0.3215 0.2822 0.3243 0.0000  0.0048  0.0006  221  ASP A C   
1518  O O   . ASP A 223  ? 0.2768 0.2397 0.2788 -0.0002 0.0045  -0.0017 221  ASP A O   
1519  C CB  . ASP A 223  ? 0.3196 0.2757 0.3284 0.0014  0.0058  0.0003  221  ASP A CB  
1520  C CG  . ASP A 223  ? 0.3567 0.3111 0.3621 0.0020  0.0068  0.0020  221  ASP A CG  
1521  O OD1 . ASP A 223  ? 0.3890 0.3429 0.3916 0.0020  0.0071  0.0039  221  ASP A OD1 
1522  O OD2 . ASP A 223  ? 0.4709 0.4244 0.4769 0.0026  0.0071  0.0012  221  ASP A OD2 
1523  N N   . MET A 224  ? 0.2881 0.2486 0.2884 -0.0004 0.0048  0.0029  222  MET A N   
1524  C CA  . MET A 224  ? 0.3263 0.2891 0.3231 -0.0012 0.0043  0.0034  222  MET A CA  
1525  C C   . MET A 224  ? 0.3427 0.3039 0.3373 -0.0007 0.0051  0.0039  222  MET A C   
1526  O O   . MET A 224  ? 0.4489 0.4116 0.4409 -0.0014 0.0047  0.0047  222  MET A O   
1527  C CB  . MET A 224  ? 0.3271 0.2903 0.3230 -0.0018 0.0036  0.0059  222  MET A CB  
1528  C CG  . MET A 224  ? 0.3796 0.3450 0.3774 -0.0024 0.0027  0.0056  222  MET A CG  
1529  S SD  . MET A 224  ? 0.4117 0.3828 0.4097 -0.0033 0.0018  0.0023  222  MET A SD  
1530  C CE  . MET A 224  ? 0.4356 0.4110 0.4295 -0.0046 0.0011  0.0037  222  MET A CE  
1531  N N   . LEU A 225  ? 0.4028 0.3611 0.3987 0.0004  0.0060  0.0035  223  LEU A N   
1532  C CA  . LEU A 225  ? 0.3763 0.3334 0.3706 0.0010  0.0067  0.0034  223  LEU A CA  
1533  C C   . LEU A 225  ? 0.4739 0.4291 0.4657 0.0012  0.0069  0.0055  223  LEU A C   
1534  O O   . LEU A 225  ? 0.4835 0.4382 0.4737 0.0015  0.0073  0.0055  223  LEU A O   
1535  C CB  . LEU A 225  ? 0.4001 0.3604 0.3933 0.0004  0.0063  0.0011  223  LEU A CB  
1536  C CG  . LEU A 225  ? 0.3871 0.3488 0.3834 0.0007  0.0061  -0.0018 223  LEU A CG  
1537  C CD1 . LEU A 225  ? 0.4145 0.3806 0.4094 0.0002  0.0056  -0.0043 223  LEU A CD1 
1538  C CD2 . LEU A 225  ? 0.4012 0.3594 0.3999 0.0019  0.0068  -0.0018 223  LEU A CD2 
1539  N N   . GLY A 226  ? 0.4396 0.3940 0.4316 0.0011  0.0066  0.0072  224  GLY A N   
1540  C CA  . GLY A 226  ? 0.4536 0.4060 0.4442 0.0016  0.0067  0.0088  224  GLY A CA  
1541  C C   . GLY A 226  ? 0.4388 0.3887 0.4299 0.0031  0.0079  0.0090  224  GLY A C   
1542  O O   . GLY A 226  ? 0.4022 0.3516 0.3954 0.0037  0.0085  0.0090  224  GLY A O   
1543  N N   . GLU A 227  ? 0.3891 0.3379 0.3786 0.0037  0.0080  0.0094  225  GLU A N   
1544  C CA  . GLU A 227  ? 0.4329 0.3802 0.4224 0.0052  0.0091  0.0095  225  GLU A CA  
1545  C C   . GLU A 227  ? 0.3750 0.3214 0.3627 0.0057  0.0089  0.0096  225  GLU A C   
1546  O O   . GLU A 227  ? 0.3438 0.2905 0.3301 0.0048  0.0081  0.0094  225  GLU A O   
1547  C CB  . GLU A 227  ? 0.5338 0.4814 0.5236 0.0053  0.0098  0.0086  225  GLU A CB  
1548  C CG  . GLU A 227  ? 0.5895 0.5363 0.5795 0.0067  0.0109  0.0092  225  GLU A CG  
1549  C CD  . GLU A 227  ? 0.5913 0.5384 0.5826 0.0067  0.0112  0.0086  225  GLU A CD  
1550  O OE1 . GLU A 227  ? 0.4774 0.4252 0.4702 0.0059  0.0107  0.0075  225  GLU A OE1 
1551  O OE2 . GLU A 227  ? 0.6331 0.5799 0.6242 0.0076  0.0119  0.0092  225  GLU A OE2 
1552  N N   . ALA A 228  ? 0.3372 0.2829 0.3252 0.0071  0.0095  0.0098  226  ALA A N   
1553  C CA  . ALA A 228  ? 0.3492 0.2942 0.3358 0.0080  0.0093  0.0094  226  ALA A CA  
1554  C C   . ALA A 228  ? 0.3004 0.2447 0.2867 0.0071  0.0077  0.0095  226  ALA A C   
1555  O O   . ALA A 228  ? 0.3505 0.2947 0.3356 0.0065  0.0072  0.0092  226  ALA A O   
1556  C CB  . ALA A 228  ? 0.3954 0.3406 0.3804 0.0084  0.0100  0.0089  226  ALA A CB  
1557  N N   . ALA A 229  ? 0.2677 0.2116 0.2557 0.0070  0.0069  0.0100  227  ALA A N   
1558  C CA  . ALA A 229  ? 0.2536 0.1967 0.2424 0.0062  0.0051  0.0105  227  ALA A CA  
1559  C C   . ALA A 229  ? 0.2504 0.1924 0.2389 0.0073  0.0048  0.0094  227  ALA A C   
1560  O O   . ALA A 229  ? 0.2514 0.1934 0.2400 0.0091  0.0055  0.0083  227  ALA A O   
1561  C CB  . ALA A 229  ? 0.2731 0.2158 0.2643 0.0064  0.0043  0.0112  227  ALA A CB  
1562  N N   . THR A 230  ? 0.2439 0.1854 0.2322 0.0062  0.0035  0.0098  228  THR A N   
1563  C CA  . THR A 230  ? 0.2669 0.2073 0.2555 0.0071  0.0027  0.0086  228  THR A CA  
1564  C C   . THR A 230  ? 0.2353 0.1741 0.2271 0.0070  0.0007  0.0089  228  THR A C   
1565  O O   . THR A 230  ? 0.2485 0.1863 0.2415 0.0084  0.0000  0.0072  228  THR A O   
1566  C CB  . THR A 230  ? 0.2753 0.2163 0.2622 0.0058  0.0025  0.0090  228  THR A CB  
1567  O OG1 . THR A 230  ? 0.3580 0.3003 0.3425 0.0059  0.0043  0.0085  228  THR A OG1 
1568  C CG2 . THR A 230  ? 0.3239 0.2637 0.3111 0.0066  0.0017  0.0076  228  THR A CG2 
1569  N N   . THR A 231  ? 0.2434 0.1822 0.2369 0.0056  -0.0005 0.0108  229  THR A N   
1570  C CA  . THR A 231  ? 0.2255 0.1627 0.2227 0.0053  -0.0028 0.0116  229  THR A CA  
1571  C C   . THR A 231  ? 0.2415 0.1790 0.2406 0.0052  -0.0031 0.0127  229  THR A C   
1572  O O   . THR A 231  ? 0.2372 0.1762 0.2344 0.0049  -0.0017 0.0132  229  THR A O   
1573  C CB  . THR A 231  ? 0.2493 0.1868 0.2474 0.0029  -0.0046 0.0140  229  THR A CB  
1574  O OG1 . THR A 231  ? 0.2536 0.1934 0.2504 0.0011  -0.0042 0.0162  229  THR A OG1 
1575  C CG2 . THR A 231  ? 0.2453 0.1830 0.2413 0.0027  -0.0041 0.0131  229  THR A CG2 
1576  N N   . ALA A 232  ? 0.2496 0.1854 0.2527 0.0056  -0.0051 0.0130  230  ALA A N   
1577  C CA  . ALA A 232  ? 0.2396 0.1755 0.2449 0.0054  -0.0058 0.0144  230  ALA A CA  
1578  C C   . ALA A 232  ? 0.2769 0.2149 0.2811 0.0029  -0.0061 0.0174  230  ALA A C   
1579  O O   . ALA A 232  ? 0.2700 0.2094 0.2736 0.0026  -0.0054 0.0181  230  ALA A O   
1580  C CB  . ALA A 232  ? 0.2577 0.1914 0.2683 0.0060  -0.0084 0.0144  230  ALA A CB  
1581  N N   . ALA A 233  ? 0.2736 0.2122 0.2775 0.0010  -0.0072 0.0192  231  ALA A N   
1582  C CA  . ALA A 233  ? 0.3093 0.2509 0.3119 -0.0014 -0.0075 0.0220  231  ALA A CA  
1583  C C   . ALA A 233  ? 0.2807 0.2249 0.2792 -0.0015 -0.0051 0.0209  231  ALA A C   
1584  O O   . ALA A 233  ? 0.3139 0.2606 0.3118 -0.0025 -0.0050 0.0220  231  ALA A O   
1585  C CB  . ALA A 233  ? 0.3305 0.2731 0.3337 -0.0034 -0.0090 0.0242  231  ALA A CB  
1586  N N   . ASP A 234  ? 0.2695 0.2131 0.2654 -0.0003 -0.0034 0.0185  232  ASP A N   
1587  C CA  . ASP A 234  ? 0.2912 0.2368 0.2843 -0.0001 -0.0013 0.0172  232  ASP A CA  
1588  C C   . ASP A 234  ? 0.2841 0.2294 0.2780 0.0008  -0.0006 0.0168  232  ASP A C   
1589  O O   . ASP A 234  ? 0.2862 0.2337 0.2793 0.0001  0.0000  0.0169  232  ASP A O   
1590  C CB  . ASP A 234  ? 0.3265 0.2710 0.3177 0.0013  0.0003  0.0150  232  ASP A CB  
1591  C CG  . ASP A 234  ? 0.4320 0.3771 0.4216 0.0004  0.0001  0.0150  232  ASP A CG  
1592  O OD1 . ASP A 234  ? 0.4232 0.3706 0.4127 -0.0015 -0.0008 0.0168  232  ASP A OD1 
1593  O OD2 . ASP A 234  ? 0.4129 0.3567 0.4016 0.0017  0.0009  0.0134  232  ASP A OD2 
1594  N N   . ALA A 235  ? 0.2517 0.1948 0.2475 0.0026  -0.0006 0.0158  233  ALA A N   
1595  C CA  . ALA A 235  ? 0.2467 0.1899 0.2436 0.0036  0.0002  0.0154  233  ALA A CA  
1596  C C   . ALA A 235  ? 0.2757 0.2202 0.2743 0.0023  -0.0012 0.0173  233  ALA A C   
1597  O O   . ALA A 235  ? 0.2671 0.2130 0.2657 0.0021  -0.0004 0.0173  233  ALA A O   
1598  C CB  . ALA A 235  ? 0.2668 0.2082 0.2656 0.0057  0.0003  0.0139  233  ALA A CB  
1599  N N   . GLU A 236  ? 0.2790 0.2231 0.2795 0.0012  -0.0033 0.0192  234  GLU A N   
1600  C CA  . GLU A 236  ? 0.2817 0.2275 0.2838 -0.0002 -0.0047 0.0215  234  GLU A CA  
1601  C C   . GLU A 236  ? 0.2605 0.2101 0.2600 -0.0020 -0.0042 0.0223  234  GLU A C   
1602  O O   . GLU A 236  ? 0.2647 0.2164 0.2645 -0.0026 -0.0044 0.0229  234  GLU A O   
1603  C CB  . GLU A 236  ? 0.3249 0.2696 0.3301 -0.0011 -0.0073 0.0238  234  GLU A CB  
1604  C CG  . GLU A 236  ? 0.4525 0.3941 0.4617 0.0007  -0.0084 0.0230  234  GLU A CG  
1605  C CD  . GLU A 236  ? 0.5899 0.5292 0.6020 0.0005  -0.0105 0.0238  234  GLU A CD  
1606  O OE1 . GLU A 236  ? 0.6345 0.5750 0.6460 -0.0015 -0.0115 0.0260  234  GLU A OE1 
1607  O OE2 . GLU A 236  ? 0.6033 0.5399 0.6187 0.0023  -0.0113 0.0221  234  GLU A OE2 
1608  N N   . ARG A 237  ? 0.2522 0.2030 0.2492 -0.0028 -0.0037 0.0220  235  ARG A N   
1609  C CA  . ARG A 237  ? 0.2799 0.2348 0.2744 -0.0043 -0.0032 0.0220  235  ARG A CA  
1610  C C   . ARG A 237  ? 0.3045 0.2600 0.2981 -0.0033 -0.0015 0.0197  235  ARG A C   
1611  O O   . ARG A 237  ? 0.2831 0.2416 0.2764 -0.0042 -0.0016 0.0197  235  ARG A O   
1612  C CB  . ARG A 237  ? 0.2943 0.2504 0.2867 -0.0050 -0.0029 0.0218  235  ARG A CB  
1613  C CG  . ARG A 237  ? 0.3970 0.3577 0.3868 -0.0061 -0.0021 0.0210  235  ARG A CG  
1614  C CD  . ARG A 237  ? 0.5121 0.4748 0.5003 -0.0072 -0.0021 0.0213  235  ARG A CD  
1615  N NE  . ARG A 237  ? 0.5481 0.5071 0.5359 -0.0058 -0.0012 0.0197  235  ARG A NE  
1616  C CZ  . ARG A 237  ? 0.6003 0.5587 0.5865 -0.0046 0.0005  0.0170  235  ARG A CZ  
1617  N NH1 . ARG A 237  ? 0.6390 0.5999 0.6243 -0.0046 0.0013  0.0154  235  ARG A NH1 
1618  N NH2 . ARG A 237  ? 0.5460 0.5012 0.5318 -0.0034 0.0011  0.0160  235  ARG A NH2 
1619  N N   . TYR A 238  ? 0.2497 0.2023 0.2430 -0.0016 0.0000  0.0177  236  TYR A N   
1620  C CA  . TYR A 238  ? 0.2649 0.2178 0.2581 -0.0009 0.0014  0.0159  236  TYR A CA  
1621  C C   . TYR A 238  ? 0.2338 0.1869 0.2294 -0.0007 0.0010  0.0166  236  TYR A C   
1622  O O   . TYR A 238  ? 0.2607 0.2157 0.2565 -0.0010 0.0013  0.0158  236  TYR A O   
1623  C CB  . TYR A 238  ? 0.2409 0.1913 0.2337 0.0008  0.0030  0.0144  236  TYR A CB  
1624  C CG  . TYR A 238  ? 0.2610 0.2116 0.2517 0.0007  0.0036  0.0135  236  TYR A CG  
1625  C CD1 . TYR A 238  ? 0.3475 0.3010 0.3369 -0.0005 0.0036  0.0129  236  TYR A CD1 
1626  C CD2 . TYR A 238  ? 0.2784 0.2268 0.2684 0.0018  0.0041  0.0130  236  TYR A CD2 
1627  C CE1 . TYR A 238  ? 0.3527 0.3066 0.3403 -0.0006 0.0041  0.0119  236  TYR A CE1 
1628  C CE2 . TYR A 238  ? 0.3416 0.2903 0.3298 0.0017  0.0046  0.0122  236  TYR A CE2 
1629  C CZ  . TYR A 238  ? 0.3918 0.3432 0.3788 0.0005  0.0046  0.0117  236  TYR A CZ  
1630  O OH  . TYR A 238  ? 0.4233 0.3751 0.4087 0.0005  0.0051  0.0109  236  TYR A OH  
1631  N N   . TYR A 239  ? 0.2301 0.1813 0.2275 -0.0001 0.0001  0.0177  237  TYR A N   
1632  C CA  . TYR A 239  ? 0.2262 0.1777 0.2261 0.0001  -0.0005 0.0185  237  TYR A CA  
1633  C C   . TYR A 239  ? 0.2516 0.2065 0.2513 -0.0017 -0.0017 0.0197  237  TYR A C   
1634  O O   . TYR A 239  ? 0.2452 0.2019 0.2457 -0.0018 -0.0014 0.0191  237  TYR A O   
1635  C CB  . TYR A 239  ? 0.2558 0.2050 0.2582 0.0010  -0.0017 0.0194  237  TYR A CB  
1636  C CG  . TYR A 239  ? 0.2665 0.2163 0.2716 0.0013  -0.0023 0.0201  237  TYR A CG  
1637  C CD1 . TYR A 239  ? 0.2806 0.2321 0.2869 -0.0001 -0.0041 0.0222  237  TYR A CD1 
1638  C CD2 . TYR A 239  ? 0.2676 0.2167 0.2740 0.0029  -0.0010 0.0188  237  TYR A CD2 
1639  C CE1 . TYR A 239  ? 0.3168 0.2690 0.3256 0.0001  -0.0048 0.0229  237  TYR A CE1 
1640  C CE2 . TYR A 239  ? 0.2871 0.2369 0.2960 0.0030  -0.0015 0.0194  237  TYR A CE2 
1641  C CZ  . TYR A 239  ? 0.3020 0.2532 0.3121 0.0017  -0.0034 0.0213  237  TYR A CZ  
1642  O OH  . TYR A 239  ? 0.3515 0.3036 0.3643 0.0019  -0.0041 0.0219  237  TYR A OH  
1643  N N   . ARG A 240  ? 0.2391 0.1956 0.2383 -0.0031 -0.0032 0.0216  238  ARG A N   
1644  C CA  . ARG A 240  ? 0.2351 0.1960 0.2341 -0.0048 -0.0044 0.0231  238  ARG A CA  
1645  C C   . ARG A 240  ? 0.2475 0.2119 0.2442 -0.0055 -0.0034 0.0210  238  ARG A C   
1646  O O   . ARG A 240  ? 0.2386 0.2067 0.2356 -0.0063 -0.0040 0.0211  238  ARG A O   
1647  C CB  . ARG A 240  ? 0.2954 0.2578 0.2947 -0.0064 -0.0064 0.0263  238  ARG A CB  
1648  C CG  . ARG A 240  ? 0.3256 0.2888 0.3227 -0.0071 -0.0060 0.0262  238  ARG A CG  
1649  C CD  . ARG A 240  ? 0.2875 0.2532 0.2853 -0.0090 -0.0081 0.0299  238  ARG A CD  
1650  N NE  . ARG A 240  ? 0.2994 0.2655 0.2955 -0.0096 -0.0077 0.0299  238  ARG A NE  
1651  C CZ  . ARG A 240  ? 0.3572 0.3193 0.3545 -0.0090 -0.0081 0.0302  238  ARG A CZ  
1652  N NH1 . ARG A 240  ? 0.2918 0.2494 0.2923 -0.0078 -0.0090 0.0306  238  ARG A NH1 
1653  N NH2 . ARG A 240  ? 0.3796 0.3425 0.3751 -0.0096 -0.0076 0.0299  238  ARG A NH2 
1654  N N   . ASP A 241  ? 0.2334 0.1970 0.2283 -0.0049 -0.0020 0.0190  239  ASP A N   
1655  C CA  . ASP A 241  ? 0.2278 0.1942 0.2215 -0.0052 -0.0011 0.0165  239  ASP A CA  
1656  C C   . ASP A 241  ? 0.2531 0.2185 0.2488 -0.0042 -0.0005 0.0148  239  ASP A C   
1657  O O   . ASP A 241  ? 0.2454 0.2140 0.2414 -0.0048 -0.0007 0.0134  239  ASP A O   
1658  C CB  . ASP A 241  ? 0.2843 0.2495 0.2763 -0.0046 0.0001  0.0148  239  ASP A CB  
1659  C CG  . ASP A 241  ? 0.4276 0.3951 0.4176 -0.0058 -0.0005 0.0160  239  ASP A CG  
1660  O OD1 . ASP A 241  ? 0.5004 0.4711 0.4902 -0.0072 -0.0019 0.0183  239  ASP A OD1 
1661  O OD2 . ASP A 241  ? 0.5812 0.5474 0.5699 -0.0053 0.0004  0.0149  239  ASP A OD2 
1662  N N   . TYR A 242  ? 0.2263 0.1875 0.2236 -0.0028 0.0004  0.0148  240  TYR A N   
1663  C CA  . TYR A 242  ? 0.2227 0.1832 0.2223 -0.0020 0.0010  0.0138  240  TYR A CA  
1664  C C   . TYR A 242  ? 0.2099 0.1724 0.2112 -0.0027 -0.0003 0.0149  240  TYR A C   
1665  O O   . TYR A 242  ? 0.2079 0.1723 0.2106 -0.0030 -0.0004 0.0136  240  TYR A O   
1666  C CB  . TYR A 242  ? 0.2044 0.1610 0.2052 -0.0004 0.0022  0.0141  240  TYR A CB  
1667  C CG  . TYR A 242  ? 0.2084 0.1632 0.2082 0.0005  0.0036  0.0130  240  TYR A CG  
1668  C CD1 . TYR A 242  ? 0.2286 0.1844 0.2280 0.0002  0.0042  0.0112  240  TYR A CD1 
1669  C CD2 . TYR A 242  ? 0.2333 0.1855 0.2329 0.0017  0.0043  0.0135  240  TYR A CD2 
1670  C CE1 . TYR A 242  ? 0.2639 0.2180 0.2628 0.0011  0.0054  0.0105  240  TYR A CE1 
1671  C CE2 . TYR A 242  ? 0.2218 0.1727 0.2203 0.0026  0.0056  0.0127  240  TYR A CE2 
1672  C CZ  . TYR A 242  ? 0.2110 0.1628 0.2093 0.0022  0.0061  0.0114  240  TYR A CZ  
1673  O OH  . TYR A 242  ? 0.2340 0.1845 0.2316 0.0031  0.0072  0.0109  240  TYR A OH  
1674  N N   . GLU A 243  ? 0.2047 0.1669 0.2062 -0.0030 -0.0015 0.0173  241  GLU A N   
1675  C CA  . GLU A 243  ? 0.2172 0.1814 0.2204 -0.0037 -0.0029 0.0187  241  GLU A CA  
1676  C C   . GLU A 243  ? 0.2194 0.1889 0.2215 -0.0052 -0.0038 0.0182  241  GLU A C   
1677  O O   . GLU A 243  ? 0.2200 0.1916 0.2235 -0.0055 -0.0043 0.0174  241  GLU A O   
1678  C CB  . GLU A 243  ? 0.2418 0.2046 0.2460 -0.0037 -0.0042 0.0214  241  GLU A CB  
1679  C CG  . GLU A 243  ? 0.2814 0.2461 0.2878 -0.0043 -0.0060 0.0234  241  GLU A CG  
1680  C CD  . GLU A 243  ? 0.3060 0.2697 0.3137 -0.0047 -0.0078 0.0264  241  GLU A CD  
1681  O OE1 . GLU A 243  ? 0.3909 0.3543 0.3971 -0.0053 -0.0081 0.0273  241  GLU A OE1 
1682  O OE2 . GLU A 243  ? 0.2953 0.2585 0.3058 -0.0044 -0.0090 0.0279  241  GLU A OE2 
1683  N N   . SER A 244  ? 0.2218 0.1937 0.2212 -0.0063 -0.0041 0.0185  242  SER A N   
1684  C CA  . SER A 244  ? 0.2146 0.1927 0.2126 -0.0077 -0.0050 0.0178  242  SER A CA  
1685  C C   . SER A 244  ? 0.2197 0.1991 0.2182 -0.0072 -0.0040 0.0139  242  SER A C   
1686  O O   . SER A 244  ? 0.2425 0.2262 0.2414 -0.0078 -0.0049 0.0127  242  SER A O   
1687  C CB  . SER A 244  ? 0.2376 0.2187 0.2329 -0.0088 -0.0053 0.0189  242  SER A CB  
1688  O OG  . SER A 244  ? 0.3082 0.2874 0.3021 -0.0081 -0.0038 0.0167  242  SER A OG  
1689  N N   . ALA A 245  ? 0.2162 0.1918 0.2149 -0.0060 -0.0025 0.0120  243  ALA A N   
1690  C CA  . ALA A 245  ? 0.2041 0.1803 0.2043 -0.0056 -0.0019 0.0086  243  ALA A CA  
1691  C C   . ALA A 245  ? 0.2154 0.1906 0.2190 -0.0052 -0.0022 0.0083  243  ALA A C   
1692  O O   . ALA A 245  ? 0.2213 0.1993 0.2265 -0.0055 -0.0027 0.0059  243  ALA A O   
1693  C CB  . ALA A 245  ? 0.2346 0.2069 0.2348 -0.0045 -0.0004 0.0073  243  ALA A CB  
1694  N N   . ILE A 246  ? 0.2037 0.1751 0.2086 -0.0045 -0.0018 0.0105  244  ILE A N   
1695  C CA  . ILE A 246  ? 0.2123 0.1832 0.2206 -0.0042 -0.0021 0.0104  244  ILE A CA  
1696  C C   . ILE A 246  ? 0.2160 0.1916 0.2246 -0.0053 -0.0038 0.0105  244  ILE A C   
1697  O O   . ILE A 246  ? 0.2081 0.1853 0.2192 -0.0054 -0.0042 0.0087  244  ILE A O   
1698  C CB  . ILE A 246  ? 0.2047 0.1716 0.2142 -0.0031 -0.0015 0.0128  244  ILE A CB  
1699  C CG1 . ILE A 246  ? 0.2141 0.1773 0.2239 -0.0019 0.0003  0.0122  244  ILE A CG1 
1700  C CG2 . ILE A 246  ? 0.2138 0.1811 0.2266 -0.0030 -0.0020 0.0132  244  ILE A CG2 
1701  C CD1 . ILE A 246  ? 0.2199 0.1801 0.2301 -0.0007 0.0010  0.0141  244  ILE A CD1 
1702  N N   . HIS A 247  ? 0.2026 0.1808 0.2089 -0.0062 -0.0049 0.0126  245  HIS A N   
1703  C CA  . HIS A 247  ? 0.2060 0.1896 0.2124 -0.0074 -0.0066 0.0130  245  HIS A CA  
1704  C C   . HIS A 247  ? 0.2155 0.2039 0.2213 -0.0079 -0.0069 0.0094  245  HIS A C   
1705  O O   . HIS A 247  ? 0.2222 0.2136 0.2300 -0.0082 -0.0078 0.0078  245  HIS A O   
1706  C CB  . HIS A 247  ? 0.2118 0.1979 0.2160 -0.0085 -0.0078 0.0164  245  HIS A CB  
1707  C CG  . HIS A 247  ? 0.2402 0.2226 0.2461 -0.0080 -0.0083 0.0197  245  HIS A CG  
1708  N ND1 . HIS A 247  ? 0.2500 0.2323 0.2588 -0.0078 -0.0092 0.0206  245  HIS A ND1 
1709  C CD2 . HIS A 247  ? 0.2694 0.2483 0.2751 -0.0077 -0.0083 0.0221  245  HIS A CD2 
1710  C CE1 . HIS A 247  ? 0.2810 0.2599 0.2912 -0.0072 -0.0096 0.0233  245  HIS A CE1 
1711  N NE2 . HIS A 247  ? 0.2591 0.2358 0.2676 -0.0071 -0.0091 0.0241  245  HIS A NE2 
1712  N N   . ALA A 248  ? 0.2144 0.2038 0.2180 -0.0080 -0.0062 0.0078  246  ALA A N   
1713  C CA  . ALA A 248  ? 0.2112 0.2057 0.2145 -0.0083 -0.0065 0.0038  246  ALA A CA  
1714  C C   . ALA A 248  ? 0.2160 0.2081 0.2232 -0.0074 -0.0062 0.0005  246  ALA A C   
1715  O O   . ALA A 248  ? 0.2142 0.2104 0.2232 -0.0077 -0.0072 -0.0024 246  ALA A O   
1716  C CB  . ALA A 248  ? 0.2300 0.2260 0.2304 -0.0084 -0.0058 0.0028  246  ALA A CB  
1717  N N   . ILE A 249  ? 0.2068 0.1926 0.2158 -0.0063 -0.0048 0.0009  247  ILE A N   
1718  C CA  . ILE A 249  ? 0.1814 0.1646 0.1948 -0.0056 -0.0045 -0.0015 247  ILE A CA  
1719  C C   . ILE A 249  ? 0.2087 0.1924 0.2251 -0.0059 -0.0054 -0.0009 247  ILE A C   
1720  O O   . ILE A 249  ? 0.2251 0.2102 0.2451 -0.0059 -0.0062 -0.0038 247  ILE A O   
1721  C CB  . ILE A 249  ? 0.1996 0.1766 0.2138 -0.0046 -0.0028 -0.0002 247  ILE A CB  
1722  C CG1 . ILE A 249  ? 0.2093 0.1861 0.2209 -0.0043 -0.0021 -0.0013 247  ILE A CG1 
1723  C CG2 . ILE A 249  ? 0.2187 0.1931 0.2381 -0.0040 -0.0026 -0.0016 247  ILE A CG2 
1724  C CD1 . ILE A 249  ? 0.2263 0.1977 0.2374 -0.0034 -0.0005 0.0009  247  ILE A CD1 
1725  N N   . GLY A 250  ? 0.1957 0.1781 0.2114 -0.0059 -0.0054 0.0026  248  GLY A N   
1726  C CA  . GLY A 250  ? 0.2136 0.1965 0.2323 -0.0061 -0.0063 0.0034  248  GLY A CA  
1727  C C   . GLY A 250  ? 0.2101 0.1993 0.2285 -0.0071 -0.0081 0.0017  248  GLY A C   
1728  O O   . GLY A 250  ? 0.2202 0.2107 0.2421 -0.0072 -0.0090 0.0002  248  GLY A O   
1729  N N   . LYS A 251  ? 0.2139 0.2077 0.2284 -0.0079 -0.0088 0.0022  249  LYS A N   
1730  C CA  . LYS A 251  ? 0.2091 0.2102 0.2230 -0.0089 -0.0106 0.0005  249  LYS A CA  
1731  C C   . LYS A 251  ? 0.2337 0.2371 0.2500 -0.0086 -0.0109 -0.0048 249  LYS A C   
1732  O O   . LYS A 251  ? 0.2442 0.2516 0.2626 -0.0089 -0.0123 -0.0071 249  LYS A O   
1733  C CB  . LYS A 251  ? 0.2402 0.2463 0.2495 -0.0098 -0.0111 0.0020  249  LYS A CB  
1734  C CG  . LYS A 251  ? 0.2439 0.2493 0.2516 -0.0104 -0.0115 0.0073  249  LYS A CG  
1735  C CD  . LYS A 251  ? 0.2622 0.2719 0.2658 -0.0113 -0.0117 0.0088  249  LYS A CD  
1736  C CE  . LYS A 251  ? 0.2704 0.2793 0.2730 -0.0120 -0.0125 0.0143  249  LYS A CE  
1737  N NZ  . LYS A 251  ? 0.2593 0.2727 0.2582 -0.0132 -0.0127 0.0159  249  LYS A NZ  
1738  N N   . ALA A 252  ? 0.2238 0.2248 0.2401 -0.0079 -0.0098 -0.0070 250  ALA A N   
1739  C CA  . ALA A 252  ? 0.2078 0.2105 0.2269 -0.0075 -0.0103 -0.0122 250  ALA A CA  
1740  C C   . ALA A 252  ? 0.2355 0.2338 0.2606 -0.0070 -0.0104 -0.0134 250  ALA A C   
1741  O O   . ALA A 252  ? 0.2516 0.2526 0.2804 -0.0070 -0.0117 -0.0175 250  ALA A O   
1742  C CB  . ALA A 252  ? 0.2475 0.2486 0.2654 -0.0069 -0.0091 -0.0138 250  ALA A CB  
1743  N N   . SER A 253  ? 0.2334 0.2254 0.2597 -0.0066 -0.0091 -0.0099 251  SER A N   
1744  C CA  . SER A 253  ? 0.2287 0.2170 0.2608 -0.0062 -0.0091 -0.0103 251  SER A CA  
1745  C C   . SER A 253  ? 0.2517 0.2436 0.2864 -0.0069 -0.0108 -0.0114 251  SER A C   
1746  O O   . SER A 253  ? 0.2463 0.2383 0.2864 -0.0068 -0.0118 -0.0143 251  SER A O   
1747  C CB  . SER A 253  ? 0.2233 0.2059 0.2554 -0.0058 -0.0074 -0.0059 251  SER A CB  
1748  O OG  . SER A 253  ? 0.2386 0.2185 0.2765 -0.0056 -0.0074 -0.0059 251  SER A OG  
1749  N N   . ALA A 254  ? 0.2403 0.2355 0.2718 -0.0074 -0.0114 -0.0090 252  ALA A N   
1750  C CA  . ALA A 254  ? 0.2607 0.2604 0.2939 -0.0081 -0.0132 -0.0099 252  ALA A CA  
1751  C C   . ALA A 254  ? 0.2715 0.2679 0.3108 -0.0079 -0.0134 -0.0100 252  ALA A C   
1752  O O   . ALA A 254  ? 0.2751 0.2743 0.3183 -0.0082 -0.0149 -0.0133 252  ALA A O   
1753  C CB  . ALA A 254  ? 0.2981 0.3050 0.3305 -0.0085 -0.0148 -0.0146 252  ALA A CB  
1754  N N   . GLY A 255  ? 0.2484 0.2393 0.2888 -0.0074 -0.0118 -0.0064 253  GLY A N   
1755  C CA  . GLY A 255  ? 0.2732 0.2615 0.3191 -0.0074 -0.0118 -0.0056 253  GLY A CA  
1756  C C   . GLY A 255  ? 0.2415 0.2270 0.2930 -0.0071 -0.0117 -0.0079 253  GLY A C   
1757  O O   . GLY A 255  ? 0.2896 0.2738 0.3465 -0.0073 -0.0120 -0.0075 253  GLY A O   
1758  N N   . ARG A 256  ? 0.2533 0.2378 0.3040 -0.0068 -0.0113 -0.0101 254  ARG A N   
1759  C CA  . ARG A 256  ? 0.2409 0.2223 0.2975 -0.0066 -0.0113 -0.0119 254  ARG A CA  
1760  C C   . ARG A 256  ? 0.2506 0.2269 0.3095 -0.0063 -0.0095 -0.0077 254  ARG A C   
1761  O O   . ARG A 256  ? 0.2630 0.2369 0.3280 -0.0063 -0.0096 -0.0080 254  ARG A O   
1762  C CB  . ARG A 256  ? 0.2360 0.2177 0.2915 -0.0062 -0.0114 -0.0152 254  ARG A CB  
1763  C CG  . ARG A 256  ? 0.2689 0.2561 0.3257 -0.0065 -0.0136 -0.0207 254  ARG A CG  
1764  C CD  . ARG A 256  ? 0.2976 0.2855 0.3531 -0.0059 -0.0136 -0.0241 254  ARG A CD  
1765  N NE  . ARG A 256  ? 0.2658 0.2556 0.3135 -0.0058 -0.0125 -0.0225 254  ARG A NE  
1766  C CZ  . ARG A 256  ? 0.3098 0.3002 0.3550 -0.0053 -0.0120 -0.0244 254  ARG A CZ  
1767  N NH1 . ARG A 256  ? 0.2948 0.2834 0.3447 -0.0047 -0.0124 -0.0277 254  ARG A NH1 
1768  N NH2 . ARG A 256  ? 0.2815 0.2745 0.3200 -0.0055 -0.0112 -0.0228 254  ARG A NH2 
1769  N N   . GLY A 257  ? 0.2348 0.2097 0.2891 -0.0059 -0.0078 -0.0039 255  GLY A N   
1770  C CA  . GLY A 257  ? 0.2230 0.1941 0.2790 -0.0054 -0.0060 -0.0001 255  GLY A CA  
1771  C C   . GLY A 257  ? 0.2208 0.1889 0.2754 -0.0048 -0.0046 0.0005  255  GLY A C   
1772  O O   . GLY A 257  ? 0.2313 0.1997 0.2839 -0.0047 -0.0049 -0.0020 255  GLY A O   
1773  N N   . ILE A 258  ? 0.2001 0.1656 0.2561 -0.0043 -0.0029 0.0040  256  ILE A N   
1774  C CA  . ILE A 258  ? 0.2042 0.1672 0.2577 -0.0036 -0.0013 0.0054  256  ILE A CA  
1775  C C   . ILE A 258  ? 0.2198 0.1810 0.2779 -0.0037 -0.0017 0.0040  256  ILE A C   
1776  O O   . ILE A 258  ? 0.2318 0.1914 0.2877 -0.0032 -0.0008 0.0043  256  ILE A O   
1777  C CB  . ILE A 258  ? 0.2102 0.1720 0.2629 -0.0029 0.0006  0.0094  256  ILE A CB  
1778  C CG1 . ILE A 258  ? 0.2376 0.1994 0.2969 -0.0033 0.0008  0.0114  256  ILE A CG1 
1779  C CG2 . ILE A 258  ? 0.2144 0.1776 0.2627 -0.0025 0.0008  0.0104  256  ILE A CG2 
1780  C CD1 . ILE A 258  ? 0.2405 0.2022 0.2991 -0.0025 0.0028  0.0152  256  ILE A CD1 
1781  N N   . TYR A 259  ? 0.2367 0.1983 0.3016 -0.0045 -0.0032 0.0026  257  TYR A N   
1782  C CA  . TYR A 259  ? 0.2223 0.1820 0.2928 -0.0046 -0.0039 0.0015  257  TYR A CA  
1783  C C   . TYR A 259  ? 0.2654 0.2263 0.3365 -0.0047 -0.0058 -0.0038 257  TYR A C   
1784  O O   . TYR A 259  ? 0.2902 0.2498 0.3608 -0.0042 -0.0057 -0.0052 257  TYR A O   
1785  C CB  . TYR A 259  ? 0.2391 0.1981 0.3179 -0.0054 -0.0045 0.0033  257  TYR A CB  
1786  C CG  . TYR A 259  ? 0.2578 0.2167 0.3359 -0.0052 -0.0025 0.0084  257  TYR A CG  
1787  C CD1 . TYR A 259  ? 0.2602 0.2177 0.3355 -0.0045 -0.0004 0.0117  257  TYR A CD1 
1788  C CD2 . TYR A 259  ? 0.2601 0.2208 0.3402 -0.0057 -0.0026 0.0097  257  TYR A CD2 
1789  C CE1 . TYR A 259  ? 0.2675 0.2258 0.3421 -0.0042 0.0014  0.0159  257  TYR A CE1 
1790  C CE2 . TYR A 259  ? 0.2672 0.2285 0.3467 -0.0054 -0.0008 0.0139  257  TYR A CE2 
1791  C CZ  . TYR A 259  ? 0.2641 0.2244 0.3408 -0.0046 0.0013  0.0169  257  TYR A CZ  
1792  O OH  . TYR A 259  ? 0.2475 0.2093 0.3235 -0.0042 0.0031  0.0207  257  TYR A OH  
1793  N N   . GLU A 260  ? 0.2296 0.1935 0.3016 -0.0052 -0.0075 -0.0070 258  GLU A N   
1794  C CA  . GLU A 260  ? 0.2556 0.2219 0.3278 -0.0051 -0.0093 -0.0124 258  GLU A CA  
1795  C C   . GLU A 260  ? 0.2937 0.2623 0.3575 -0.0046 -0.0086 -0.0134 258  GLU A C   
1796  O O   . GLU A 260  ? 0.3255 0.2954 0.3883 -0.0043 -0.0092 -0.0169 258  GLU A O   
1797  C CB  . GLU A 260  ? 0.2984 0.2681 0.3742 -0.0057 -0.0115 -0.0156 258  GLU A CB  
1798  C CG  . GLU A 260  ? 0.4101 0.3835 0.4862 -0.0055 -0.0134 -0.0218 258  GLU A CG  
1799  C CD  . GLU A 260  ? 0.4821 0.4599 0.5604 -0.0061 -0.0155 -0.0253 258  GLU A CD  
1800  O OE1 . GLU A 260  ? 0.4858 0.4631 0.5675 -0.0067 -0.0159 -0.0232 258  GLU A OE1 
1801  O OE2 . GLU A 260  ? 0.4280 0.4104 0.5047 -0.0059 -0.0169 -0.0302 258  GLU A OE2 
1802  N N   . GLY A 261  ? 0.2328 0.2021 0.2909 -0.0047 -0.0073 -0.0102 259  GLY A N   
1803  C CA  . GLY A 261  ? 0.2423 0.2142 0.2930 -0.0045 -0.0070 -0.0107 259  GLY A CA  
1804  C C   . GLY A 261  ? 0.2361 0.2053 0.2827 -0.0039 -0.0051 -0.0085 259  GLY A C   
1805  O O   . GLY A 261  ? 0.2288 0.1942 0.2772 -0.0035 -0.0039 -0.0058 259  GLY A O   
1806  N N   . PRO A 262  ? 0.2112 0.1828 0.2521 -0.0038 -0.0050 -0.0095 260  PRO A N   
1807  C CA  . PRO A 262  ? 0.2282 0.1976 0.2651 -0.0032 -0.0035 -0.0079 260  PRO A CA  
1808  C C   . PRO A 262  ? 0.2155 0.1825 0.2492 -0.0030 -0.0020 -0.0033 260  PRO A C   
1809  O O   . PRO A 262  ? 0.2394 0.2072 0.2728 -0.0033 -0.0022 -0.0016 260  PRO A O   
1810  C CB  . PRO A 262  ? 0.2418 0.2154 0.2738 -0.0035 -0.0041 -0.0103 260  PRO A CB  
1811  C CG  . PRO A 262  ? 0.2437 0.2216 0.2753 -0.0042 -0.0054 -0.0110 260  PRO A CG  
1812  C CD  . PRO A 262  ? 0.2271 0.2041 0.2652 -0.0043 -0.0064 -0.0122 260  PRO A CD  
1813  N N   . GLY A 263  ? 0.2242 0.1884 0.2556 -0.0023 -0.0005 -0.0017 261  GLY A N   
1814  C CA  . GLY A 263  ? 0.2220 0.1842 0.2504 -0.0018 0.0009  0.0019  261  GLY A CA  
1815  C C   . GLY A 263  ? 0.2031 0.1647 0.2266 -0.0015 0.0017  0.0022  261  GLY A C   
1816  O O   . GLY A 263  ? 0.2123 0.1756 0.2345 -0.0017 0.0011  -0.0003 261  GLY A O   
1817  N N   . ILE A 264  ? 0.1923 0.1520 0.2134 -0.0008 0.0029  0.0050  262  ILE A N   
1818  C CA  . ILE A 264  ? 0.2115 0.1704 0.2283 -0.0005 0.0036  0.0055  262  ILE A CA  
1819  C C   . ILE A 264  ? 0.2187 0.1746 0.2359 0.0006  0.0051  0.0074  262  ILE A C   
1820  O O   . ILE A 264  ? 0.2165 0.1714 0.2363 0.0010  0.0057  0.0091  262  ILE A O   
1821  C CB  . ILE A 264  ? 0.2009 0.1608 0.2140 -0.0007 0.0031  0.0069  262  ILE A CB  
1822  C CG1 . ILE A 264  ? 0.2474 0.2072 0.2564 -0.0007 0.0034  0.0069  262  ILE A CG1 
1823  C CG2 . ILE A 264  ? 0.2269 0.1851 0.2408 -0.0001 0.0038  0.0095  262  ILE A CG2 
1824  C CD1 . ILE A 264  ? 0.2464 0.2075 0.2527 -0.0013 0.0026  0.0085  262  ILE A CD1 
1825  N N   . SER A 265  ? 0.2013 0.1563 0.2161 0.0010  0.0057  0.0070  263  SER A N   
1826  C CA  . SER A 265  ? 0.2019 0.1547 0.2160 0.0020  0.0071  0.0088  263  SER A CA  
1827  C C   . SER A 265  ? 0.2458 0.1982 0.2554 0.0023  0.0074  0.0095  263  SER A C   
1828  O O   . SER A 265  ? 0.2677 0.2212 0.2748 0.0017  0.0067  0.0083  263  SER A O   
1829  C CB  . SER A 265  ? 0.2238 0.1757 0.2396 0.0022  0.0074  0.0080  263  SER A CB  
1830  O OG  . SER A 265  ? 0.2610 0.2126 0.2820 0.0020  0.0071  0.0079  263  SER A OG  
1831  N N   . ILE A 266  ? 0.2090 0.1603 0.2178 0.0033  0.0084  0.0113  264  ILE A N   
1832  C CA  . ILE A 266  ? 0.2060 0.1567 0.2113 0.0038  0.0085  0.0118  264  ILE A CA  
1833  C C   . ILE A 266  ? 0.1987 0.1483 0.2032 0.0050  0.0098  0.0125  264  ILE A C   
1834  O O   . ILE A 266  ? 0.2232 0.1729 0.2300 0.0055  0.0107  0.0134  264  ILE A O   
1835  C CB  . ILE A 266  ? 0.2286 0.1795 0.2339 0.0040  0.0080  0.0128  264  ILE A CB  
1836  C CG1 . ILE A 266  ? 0.2321 0.1830 0.2397 0.0051  0.0090  0.0140  264  ILE A CG1 
1837  C CG2 . ILE A 266  ? 0.2465 0.1989 0.2526 0.0028  0.0066  0.0124  264  ILE A CG2 
1838  C CD1 . ILE A 266  ? 0.2351 0.1863 0.2429 0.0057  0.0086  0.0146  264  ILE A CD1 
1839  N N   . LYS A 267  ? 0.2125 0.1616 0.2140 0.0054  0.0098  0.0122  265  LYS A N   
1840  C CA  . LYS A 267  ? 0.1960 0.1444 0.1961 0.0066  0.0109  0.0128  265  LYS A CA  
1841  C C   . LYS A 267  ? 0.2228 0.1711 0.2218 0.0075  0.0107  0.0130  265  LYS A C   
1842  O O   . LYS A 267  ? 0.2261 0.1739 0.2238 0.0069  0.0096  0.0126  265  LYS A O   
1843  C CB  . LYS A 267  ? 0.2344 0.1823 0.2324 0.0065  0.0109  0.0119  265  LYS A CB  
1844  C CG  . LYS A 267  ? 0.2619 0.2099 0.2617 0.0062  0.0111  0.0116  265  LYS A CG  
1845  C CD  . LYS A 267  ? 0.3190 0.2666 0.3167 0.0062  0.0111  0.0106  265  LYS A CD  
1846  C CE  . LYS A 267  ? 0.4062 0.3537 0.4065 0.0062  0.0113  0.0104  265  LYS A CE  
1847  N NZ  . LYS A 267  ? 0.4449 0.3928 0.4483 0.0053  0.0106  0.0093  265  LYS A NZ  
1848  N N   . LEU A 268  ? 0.2031 0.1522 0.2028 0.0088  0.0117  0.0137  266  LEU A N   
1849  C CA  . LEU A 268  ? 0.2034 0.1526 0.2026 0.0099  0.0114  0.0133  266  LEU A CA  
1850  C C   . LEU A 268  ? 0.2146 0.1626 0.2113 0.0102  0.0109  0.0123  266  LEU A C   
1851  O O   . LEU A 268  ? 0.2278 0.1751 0.2245 0.0104  0.0097  0.0118  266  LEU A O   
1852  C CB  . LEU A 268  ? 0.2126 0.1639 0.2129 0.0115  0.0128  0.0139  266  LEU A CB  
1853  C CG  . LEU A 268  ? 0.2299 0.1826 0.2333 0.0111  0.0132  0.0151  266  LEU A CG  
1854  C CD1 . LEU A 268  ? 0.2378 0.1934 0.2422 0.0126  0.0147  0.0159  266  LEU A CD1 
1855  C CD2 . LEU A 268  ? 0.2619 0.2138 0.2667 0.0105  0.0119  0.0148  266  LEU A CD2 
1856  N N   . SER A 269  ? 0.2101 0.1580 0.2050 0.0101  0.0114  0.0121  267  SER A N   
1857  C CA  . SER A 269  ? 0.2415 0.1884 0.2342 0.0104  0.0109  0.0112  267  SER A CA  
1858  C C   . SER A 269  ? 0.2462 0.1919 0.2384 0.0089  0.0093  0.0110  267  SER A C   
1859  O O   . SER A 269  ? 0.2471 0.1920 0.2382 0.0089  0.0085  0.0104  267  SER A O   
1860  C CB  . SER A 269  ? 0.2328 0.1800 0.2240 0.0106  0.0117  0.0111  267  SER A CB  
1861  O OG  . SER A 269  ? 0.2437 0.1904 0.2349 0.0092  0.0115  0.0112  267  SER A OG  
1862  N N   . ALA A 270  ? 0.2062 0.1523 0.1993 0.0075  0.0089  0.0115  268  ALA A N   
1863  C CA  . ALA A 270  ? 0.2194 0.1653 0.2120 0.0061  0.0074  0.0117  268  ALA A CA  
1864  C C   . ALA A 270  ? 0.2136 0.1590 0.2077 0.0061  0.0061  0.0123  268  ALA A C   
1865  O O   . ALA A 270  ? 0.2357 0.1809 0.2296 0.0050  0.0047  0.0129  268  ALA A O   
1866  C CB  . ALA A 270  ? 0.2415 0.1888 0.2347 0.0047  0.0072  0.0117  268  ALA A CB  
1867  N N   . LEU A 271  ? 0.2120 0.1573 0.2079 0.0074  0.0065  0.0123  269  LEU A N   
1868  C CA  . LEU A 271  ? 0.2189 0.1638 0.2169 0.0074  0.0052  0.0128  269  LEU A CA  
1869  C C   . LEU A 271  ? 0.2116 0.1554 0.2105 0.0089  0.0046  0.0119  269  LEU A C   
1870  O O   . LEU A 271  ? 0.2325 0.1757 0.2339 0.0092  0.0033  0.0122  269  LEU A O   
1871  C CB  . LEU A 271  ? 0.2344 0.1804 0.2345 0.0077  0.0057  0.0133  269  LEU A CB  
1872  C CG  . LEU A 271  ? 0.2446 0.1918 0.2446 0.0061  0.0056  0.0139  269  LEU A CG  
1873  C CD1 . LEU A 271  ? 0.2898 0.2379 0.2921 0.0065  0.0063  0.0142  269  LEU A CD1 
1874  C CD2 . LEU A 271  ? 0.2617 0.2092 0.2619 0.0046  0.0037  0.0148  269  LEU A CD2 
1875  N N   . HIS A 272  ? 0.2460 0.1897 0.2433 0.0100  0.0054  0.0108  270  HIS A N   
1876  C CA  . HIS A 272  ? 0.2274 0.1702 0.2257 0.0114  0.0046  0.0094  270  HIS A CA  
1877  C C   . HIS A 272  ? 0.2262 0.1688 0.2221 0.0117  0.0051  0.0084  270  HIS A C   
1878  O O   . HIS A 272  ? 0.2402 0.1840 0.2340 0.0119  0.0067  0.0084  270  HIS A O   
1879  C CB  . HIS A 272  ? 0.2521 0.1965 0.2519 0.0135  0.0056  0.0082  270  HIS A CB  
1880  C CG  . HIS A 272  ? 0.2668 0.2106 0.2688 0.0151  0.0042  0.0064  270  HIS A CG  
1881  N ND1 . HIS A 272  ? 0.2854 0.2290 0.2866 0.0162  0.0040  0.0045  270  HIS A ND1 
1882  C CD2 . HIS A 272  ? 0.2819 0.2252 0.2875 0.0158  0.0028  0.0059  270  HIS A CD2 
1883  C CE1 . HIS A 272  ? 0.3074 0.2504 0.3117 0.0175  0.0024  0.0027  270  HIS A CE1 
1884  N NE2 . HIS A 272  ? 0.3192 0.2619 0.3264 0.0173  0.0017  0.0035  270  HIS A NE2 
1885  N N   . PRO A 273  ? 0.2420 0.1831 0.2384 0.0117  0.0036  0.0077  271  PRO A N   
1886  C CA  . PRO A 273  ? 0.2361 0.1771 0.2303 0.0119  0.0039  0.0067  271  PRO A CA  
1887  C C   . PRO A 273  ? 0.2404 0.1830 0.2339 0.0142  0.0050  0.0047  271  PRO A C   
1888  O O   . PRO A 273  ? 0.2652 0.2082 0.2566 0.0145  0.0056  0.0040  271  PRO A O   
1889  C CB  . PRO A 273  ? 0.2488 0.1878 0.2448 0.0111  0.0016  0.0067  271  PRO A CB  
1890  C CG  . PRO A 273  ? 0.2508 0.1890 0.2505 0.0118  0.0002  0.0066  271  PRO A CG  
1891  C CD  . PRO A 273  ? 0.2687 0.2081 0.2683 0.0114  0.0012  0.0079  271  PRO A CD  
1892  N N   . ARG A 274  ? 0.2267 0.1706 0.2219 0.0159  0.0054  0.0037  272  ARG A N   
1893  C CA  . ARG A 274  ? 0.2351 0.1817 0.2294 0.0181  0.0067  0.0018  272  ARG A CA  
1894  C C   . ARG A 274  ? 0.2310 0.1805 0.2251 0.0188  0.0086  0.0027  272  ARG A C   
1895  O O   . ARG A 274  ? 0.2570 0.2090 0.2526 0.0206  0.0090  0.0014  272  ARG A O   
1896  C CB  . ARG A 274  ? 0.2443 0.1909 0.2412 0.0199  0.0051  -0.0010 272  ARG A CB  
1897  C CG  . ARG A 274  ? 0.2377 0.1815 0.2354 0.0192  0.0030  -0.0020 272  ARG A CG  
1898  C CD  . ARG A 274  ? 0.2472 0.1916 0.2416 0.0191  0.0038  -0.0023 272  ARG A CD  
1899  N NE  . ARG A 274  ? 0.2609 0.2091 0.2535 0.0212  0.0053  -0.0041 272  ARG A NE  
1900  C CZ  . ARG A 274  ? 0.2540 0.2038 0.2478 0.0233  0.0046  -0.0074 272  ARG A CZ  
1901  N NH1 . ARG A 274  ? 0.2634 0.2109 0.2607 0.0237  0.0022  -0.0094 272  ARG A NH1 
1902  N NH2 . ARG A 274  ? 0.2764 0.2306 0.2681 0.0252  0.0062  -0.0087 272  ARG A NH2 
1903  N N   . TYR A 275  ? 0.2253 0.1747 0.2182 0.0173  0.0097  0.0049  273  TYR A N   
1904  C CA  . TYR A 275  ? 0.2112 0.1632 0.2046 0.0176  0.0114  0.0063  273  TYR A CA  
1905  C C   . TYR A 275  ? 0.2266 0.1818 0.2181 0.0189  0.0130  0.0063  273  TYR A C   
1906  O O   . TYR A 275  ? 0.2432 0.1984 0.2331 0.0182  0.0137  0.0075  273  TYR A O   
1907  C CB  . TYR A 275  ? 0.2185 0.1690 0.2121 0.0156  0.0115  0.0084  273  TYR A CB  
1908  C CG  . TYR A 275  ? 0.2177 0.1704 0.2123 0.0157  0.0131  0.0100  273  TYR A CG  
1909  C CD1 . TYR A 275  ? 0.2200 0.1750 0.2166 0.0168  0.0135  0.0100  273  TYR A CD1 
1910  C CD2 . TYR A 275  ? 0.2121 0.1649 0.2062 0.0147  0.0139  0.0115  273  TYR A CD2 
1911  C CE1 . TYR A 275  ? 0.2432 0.2006 0.2411 0.0167  0.0149  0.0118  273  TYR A CE1 
1912  C CE2 . TYR A 275  ? 0.2214 0.1762 0.2172 0.0147  0.0151  0.0133  273  TYR A CE2 
1913  C CZ  . TYR A 275  ? 0.2281 0.1852 0.2257 0.0156  0.0157  0.0135  273  TYR A CZ  
1914  O OH  . TYR A 275  ? 0.2463 0.2057 0.2460 0.0154  0.0168  0.0156  273  TYR A OH  
1915  N N   . SER A 276  ? 0.2190 0.1776 0.2109 0.0210  0.0135  0.0047  274  SER A N   
1916  C CA  . SER A 276  ? 0.2062 0.1690 0.1963 0.0223  0.0150  0.0047  274  SER A CA  
1917  C C   . SER A 276  ? 0.2223 0.1899 0.2136 0.0244  0.0157  0.0034  274  SER A C   
1918  O O   . SER A 276  ? 0.2256 0.1925 0.2191 0.0251  0.0147  0.0015  274  SER A O   
1919  C CB  . SER A 276  ? 0.2725 0.2347 0.2604 0.0229  0.0142  0.0028  274  SER A CB  
1920  O OG  . SER A 276  ? 0.3149 0.2772 0.3041 0.0244  0.0129  -0.0005 274  SER A OG  
1921  N N   . ARG A 277  ? 0.2114 0.1842 0.2016 0.0253  0.0175  0.0046  275  ARG A N   
1922  C CA  . ARG A 277  ? 0.2206 0.1995 0.2116 0.0274  0.0185  0.0033  275  ARG A CA  
1923  C C   . ARG A 277  ? 0.2222 0.2021 0.2133 0.0295  0.0172  -0.0012 275  ARG A C   
1924  O O   . ARG A 277  ? 0.2234 0.2060 0.2165 0.0311  0.0171  -0.0034 275  ARG A O   
1925  C CB  . ARG A 277  ? 0.2179 0.2029 0.2073 0.0279  0.0205  0.0058  275  ARG A CB  
1926  C CG  . ARG A 277  ? 0.2331 0.2260 0.2227 0.0303  0.0217  0.0044  275  ARG A CG  
1927  C CD  . ARG A 277  ? 0.2343 0.2285 0.2270 0.0305  0.0220  0.0045  275  ARG A CD  
1928  N NE  . ARG A 277  ? 0.2328 0.2355 0.2259 0.0329  0.0232  0.0030  275  ARG A NE  
1929  C CZ  . ARG A 277  ? 0.2121 0.2170 0.2058 0.0352  0.0224  -0.0017 275  ARG A CZ  
1930  N NH1 . ARG A 277  ? 0.2285 0.2277 0.2226 0.0354  0.0202  -0.0051 275  ARG A NH1 
1931  N NH2 . ARG A 277  ? 0.2322 0.2455 0.2264 0.0373  0.0236  -0.0031 275  ARG A NH2 
1932  N N   . ALA A 278  ? 0.2272 0.2049 0.2164 0.0295  0.0162  -0.0028 276  ALA A N   
1933  C CA  . ALA A 278  ? 0.2528 0.2312 0.2428 0.0315  0.0147  -0.0073 276  ALA A CA  
1934  C C   . ALA A 278  ? 0.2381 0.2124 0.2317 0.0315  0.0128  -0.0092 276  ALA A C   
1935  O O   . ALA A 278  ? 0.2594 0.2352 0.2552 0.0335  0.0116  -0.0131 276  ALA A O   
1936  C CB  . ALA A 278  ? 0.2656 0.2416 0.2534 0.0311  0.0137  -0.0084 276  ALA A CB  
1937  N N   . GLN A 279  ? 0.2227 0.1919 0.2174 0.0292  0.0122  -0.0066 277  GLN A N   
1938  C CA  . GLN A 279  ? 0.2245 0.1896 0.2227 0.0288  0.0102  -0.0075 277  GLN A CA  
1939  C C   . GLN A 279  ? 0.2405 0.2066 0.2407 0.0285  0.0111  -0.0055 277  GLN A C   
1940  O O   . GLN A 279  ? 0.2402 0.2023 0.2425 0.0271  0.0098  -0.0044 277  GLN A O   
1941  C CB  . GLN A 279  ? 0.2511 0.2101 0.2492 0.0265  0.0086  -0.0060 277  GLN A CB  
1942  C CG  . GLN A 279  ? 0.2600 0.2178 0.2566 0.0267  0.0076  -0.0078 277  GLN A CG  
1943  C CD  . GLN A 279  ? 0.2908 0.2491 0.2903 0.0288  0.0057  -0.0120 277  GLN A CD  
1944  O OE1 . GLN A 279  ? 0.3745 0.3315 0.3780 0.0293  0.0043  -0.0131 277  GLN A OE1 
1945  N NE2 . GLN A 279  ? 0.2804 0.2410 0.2784 0.0302  0.0057  -0.0146 277  GLN A NE2 
1946  N N   . ALA A 280  ? 0.2340 0.2058 0.2335 0.0296  0.0131  -0.0050 278  ALA A N   
1947  C CA  . ALA A 280  ? 0.2163 0.1893 0.2177 0.0290  0.0141  -0.0028 278  ALA A CA  
1948  C C   . ALA A 280  ? 0.2363 0.2075 0.2417 0.0297  0.0125  -0.0045 278  ALA A C   
1949  O O   . ALA A 280  ? 0.2299 0.1989 0.2369 0.0282  0.0122  -0.0024 278  ALA A O   
1950  C CB  . ALA A 280  ? 0.2482 0.2286 0.2489 0.0304  0.0165  -0.0021 278  ALA A CB  
1951  N N   . ALA A 281  ? 0.2270 0.1992 0.2343 0.0318  0.0111  -0.0085 279  ALA A N   
1952  C CA  . ALA A 281  ? 0.2298 0.2002 0.2417 0.0325  0.0093  -0.0101 279  ALA A CA  
1953  C C   . ALA A 281  ? 0.2490 0.2124 0.2622 0.0301  0.0072  -0.0082 279  ALA A C   
1954  O O   . ALA A 281  ? 0.2584 0.2201 0.2742 0.0294  0.0064  -0.0068 279  ALA A O   
1955  C CB  . ALA A 281  ? 0.2666 0.2392 0.2811 0.0354  0.0079  -0.0152 279  ALA A CB  
1956  N N   . ARG A 282  ? 0.2257 0.1856 0.2369 0.0289  0.0062  -0.0078 280  ARG A N   
1957  C CA  . ARG A 282  ? 0.2267 0.1810 0.2388 0.0265  0.0044  -0.0055 280  ARG A CA  
1958  C C   . ARG A 282  ? 0.2460 0.1997 0.2562 0.0242  0.0057  -0.0017 280  ARG A C   
1959  O O   . ARG A 282  ? 0.2390 0.1900 0.2510 0.0226  0.0045  0.0001  280  ARG A O   
1960  C CB  . ARG A 282  ? 0.2476 0.1989 0.2581 0.0256  0.0032  -0.0059 280  ARG A CB  
1961  C CG  . ARG A 282  ? 0.2641 0.2146 0.2776 0.0273  0.0011  -0.0096 280  ARG A CG  
1962  C CD  . ARG A 282  ? 0.2815 0.2283 0.2939 0.0257  -0.0004 -0.0090 280  ARG A CD  
1963  N NE  . ARG A 282  ? 0.2662 0.2090 0.2797 0.0231  -0.0018 -0.0057 280  ARG A NE  
1964  C CZ  . ARG A 282  ? 0.2710 0.2112 0.2831 0.0210  -0.0026 -0.0038 280  ARG A CZ  
1965  N NH1 . ARG A 282  ? 0.2723 0.2128 0.2818 0.0211  -0.0021 -0.0049 280  ARG A NH1 
1966  N NH2 . ARG A 282  ? 0.3060 0.2437 0.3192 0.0187  -0.0038 -0.0007 280  ARG A NH2 
1967  N N   . VAL A 283  ? 0.2274 0.1840 0.2344 0.0241  0.0081  -0.0005 281  VAL A N   
1968  C CA  . VAL A 283  ? 0.2158 0.1720 0.2217 0.0221  0.0092  0.0027  281  VAL A CA  
1969  C C   . VAL A 283  ? 0.2219 0.1792 0.2308 0.0223  0.0093  0.0034  281  VAL A C   
1970  O O   . VAL A 283  ? 0.2310 0.1861 0.2409 0.0205  0.0085  0.0054  281  VAL A O   
1971  C CB  . VAL A 283  ? 0.2064 0.1656 0.2093 0.0222  0.0116  0.0039  281  VAL A CB  
1972  C CG1 . VAL A 283  ? 0.2680 0.2273 0.2711 0.0205  0.0126  0.0068  281  VAL A CG1 
1973  C CG2 . VAL A 283  ? 0.2419 0.1993 0.2419 0.0216  0.0113  0.0036  281  VAL A CG2 
1974  N N   . MET A 284  ? 0.2175 0.1789 0.2281 0.0244  0.0101  0.0018  282  MET A N   
1975  C CA  . MET A 284  ? 0.2193 0.1823 0.2330 0.0247  0.0102  0.0024  282  MET A CA  
1976  C C   . MET A 284  ? 0.2441 0.2037 0.2612 0.0246  0.0077  0.0016  282  MET A C   
1977  O O   . MET A 284  ? 0.2732 0.2322 0.2925 0.0236  0.0072  0.0032  282  MET A O   
1978  C CB  . MET A 284  ? 0.2322 0.2012 0.2468 0.0271  0.0119  0.0008  282  MET A CB  
1979  C CG  . MET A 284  ? 0.2573 0.2303 0.2689 0.0271  0.0143  0.0023  282  MET A CG  
1980  S SD  . MET A 284  ? 0.2855 0.2576 0.2965 0.0244  0.0156  0.0068  282  MET A SD  
1981  C CE  . MET A 284  ? 0.2768 0.2513 0.2920 0.0247  0.0157  0.0073  282  MET A CE  
1982  N N   . GLY A 285  ? 0.2373 0.1948 0.2554 0.0254  0.0058  -0.0006 283  GLY A N   
1983  C CA  . GLY A 285  ? 0.2432 0.1976 0.2655 0.0254  0.0031  -0.0011 283  GLY A CA  
1984  C C   . GLY A 285  ? 0.2551 0.2051 0.2768 0.0226  0.0016  0.0018  283  GLY A C   
1985  O O   . GLY A 285  ? 0.2837 0.2319 0.3085 0.0219  -0.0002 0.0030  283  GLY A O   
1986  N N   . GLU A 286  ? 0.2350 0.1837 0.2529 0.0211  0.0022  0.0029  284  GLU A N   
1987  C CA  . GLU A 286  ? 0.2253 0.1705 0.2425 0.0186  0.0006  0.0052  284  GLU A CA  
1988  C C   . GLU A 286  ? 0.2557 0.2014 0.2696 0.0165  0.0020  0.0077  284  GLU A C   
1989  O O   . GLU A 286  ? 0.2876 0.2320 0.3018 0.0146  0.0009  0.0098  284  GLU A O   
1990  C CB  . GLU A 286  ? 0.2406 0.1839 0.2568 0.0185  -0.0004 0.0042  284  GLU A CB  
1991  C CG  . GLU A 286  ? 0.2760 0.2186 0.2960 0.0206  -0.0022 0.0013  284  GLU A CG  
1992  C CD  . GLU A 286  ? 0.2904 0.2316 0.3092 0.0208  -0.0029 -0.0002 284  GLU A CD  
1993  O OE1 . GLU A 286  ? 0.3092 0.2489 0.3252 0.0187  -0.0029 0.0017  284  GLU A OE1 
1994  O OE2 . GLU A 286  ? 0.3302 0.2722 0.3511 0.0230  -0.0036 -0.0036 284  GLU A OE2 
1995  N N   . LEU A 287  ? 0.2151 0.1628 0.2262 0.0169  0.0043  0.0075  285  LEU A N   
1996  C CA  A LEU A 287  ? 0.2279 0.1758 0.2366 0.0151  0.0055  0.0095  285  LEU A CA  
1997  C CA  B LEU A 287  ? 0.2281 0.1760 0.2368 0.0151  0.0055  0.0095  285  LEU A CA  
1998  C C   . LEU A 287  ? 0.2473 0.1969 0.2579 0.0148  0.0061  0.0106  285  LEU A C   
1999  O O   . LEU A 287  ? 0.2459 0.1949 0.2565 0.0130  0.0056  0.0122  285  LEU A O   
2000  C CB  A LEU A 287  ? 0.2260 0.1753 0.2317 0.0155  0.0075  0.0091  285  LEU A CB  
2001  C CB  B LEU A 287  ? 0.2262 0.1755 0.2319 0.0155  0.0075  0.0091  285  LEU A CB  
2002  C CG  A LEU A 287  ? 0.2397 0.1883 0.2428 0.0137  0.0081  0.0104  285  LEU A CG  
2003  C CG  B LEU A 287  ? 0.2453 0.1954 0.2497 0.0142  0.0089  0.0108  285  LEU A CG  
2004  C CD1 A LEU A 287  ? 0.2382 0.1880 0.2389 0.0145  0.0098  0.0100  285  LEU A CD1 
2005  C CD1 B LEU A 287  ? 0.2966 0.2447 0.3003 0.0120  0.0077  0.0118  285  LEU A CD1 
2006  C CD2 A LEU A 287  ? 0.2885 0.2379 0.2926 0.0125  0.0086  0.0119  285  LEU A CD2 
2007  C CD2 B LEU A 287  ? 0.2395 0.1907 0.2414 0.0147  0.0104  0.0106  285  LEU A CD2 
2008  N N   . LEU A 288  ? 0.2308 0.1829 0.2430 0.0166  0.0072  0.0097  286  LEU A N   
2009  C CA  . LEU A 288  ? 0.2267 0.1808 0.2411 0.0164  0.0079  0.0109  286  LEU A CA  
2010  C C   . LEU A 288  ? 0.2345 0.1870 0.2512 0.0152  0.0059  0.0119  286  LEU A C   
2011  O O   . LEU A 288  ? 0.2398 0.1926 0.2565 0.0137  0.0062  0.0134  286  LEU A O   
2012  C CB  . LEU A 288  ? 0.2629 0.2206 0.2791 0.0187  0.0091  0.0096  286  LEU A CB  
2013  C CG  . LEU A 288  ? 0.3354 0.2954 0.3545 0.0187  0.0096  0.0106  286  LEU A CG  
2014  C CD1 . LEU A 288  ? 0.2923 0.2531 0.3105 0.0170  0.0110  0.0128  286  LEU A CD1 
2015  C CD2 . LEU A 288  ? 0.4173 0.3815 0.4382 0.0211  0.0107  0.0090  286  LEU A CD2 
2016  N N   . PRO A 289  ? 0.2337 0.1846 0.2525 0.0157  0.0039  0.0113  287  PRO A N   
2017  C CA  . PRO A 289  ? 0.2531 0.2029 0.2740 0.0143  0.0020  0.0128  287  PRO A CA  
2018  C C   . PRO A 289  ? 0.2590 0.2077 0.2776 0.0118  0.0014  0.0146  287  PRO A C   
2019  O O   . PRO A 289  ? 0.2310 0.1803 0.2507 0.0106  0.0006  0.0161  287  PRO A O   
2020  C CB  . PRO A 289  ? 0.2894 0.2373 0.3131 0.0153  -0.0003 0.0120  287  PRO A CB  
2021  C CG  . PRO A 289  ? 0.3382 0.2872 0.3623 0.0178  0.0007  0.0092  287  PRO A CG  
2022  C CD  . PRO A 289  ? 0.2488 0.1991 0.2687 0.0175  0.0031  0.0091  287  PRO A CD  
2023  N N   . ARG A 290  ? 0.2253 0.1730 0.2408 0.0112  0.0018  0.0144  288  ARG A N   
2024  C CA  . ARG A 290  ? 0.2193 0.1667 0.2325 0.0090  0.0013  0.0158  288  ARG A CA  
2025  C C   . ARG A 290  ? 0.2062 0.1553 0.2185 0.0083  0.0029  0.0160  288  ARG A C   
2026  O O   . ARG A 290  ? 0.2223 0.1722 0.2346 0.0067  0.0022  0.0169  288  ARG A O   
2027  C CB  . ARG A 290  ? 0.2480 0.1941 0.2584 0.0086  0.0014  0.0153  288  ARG A CB  
2028  C CG  . ARG A 290  ? 0.2895 0.2338 0.3014 0.0089  -0.0005 0.0153  288  ARG A CG  
2029  C CD  . ARG A 290  ? 0.3490 0.2922 0.3584 0.0089  -0.0003 0.0145  288  ARG A CD  
2030  N NE  . ARG A 290  ? 0.4022 0.3434 0.4138 0.0094  -0.0023 0.0143  288  ARG A NE  
2031  C CZ  . ARG A 290  ? 0.4148 0.3548 0.4255 0.0101  -0.0023 0.0129  288  ARG A CZ  
2032  N NH1 . ARG A 290  ? 0.3257 0.2664 0.3331 0.0104  -0.0005 0.0118  288  ARG A NH1 
2033  N NH2 . ARG A 290  ? 0.4707 0.4089 0.4845 0.0105  -0.0045 0.0127  288  ARG A NH2 
2034  N N   . VAL A 291  ? 0.2085 0.1584 0.2204 0.0094  0.0049  0.0152  289  VAL A N   
2035  C CA  . VAL A 291  ? 0.2044 0.1558 0.2166 0.0087  0.0061  0.0156  289  VAL A CA  
2036  C C   . VAL A 291  ? 0.2108 0.1634 0.2260 0.0085  0.0056  0.0163  289  VAL A C   
2037  O O   . VAL A 291  ? 0.2110 0.1644 0.2268 0.0072  0.0053  0.0168  289  VAL A O   
2038  C CB  . VAL A 291  ? 0.2113 0.1637 0.2230 0.0100  0.0082  0.0152  289  VAL A CB  
2039  C CG1 . VAL A 291  ? 0.2382 0.1917 0.2510 0.0091  0.0091  0.0160  289  VAL A CG1 
2040  C CG2 . VAL A 291  ? 0.2597 0.2109 0.2684 0.0102  0.0085  0.0145  289  VAL A CG2 
2041  N N   . LYS A 292  ? 0.2125 0.1656 0.2300 0.0099  0.0052  0.0161  290  LYS A N   
2042  C CA  . LYS A 292  ? 0.1849 0.1393 0.2055 0.0098  0.0047  0.0168  290  LYS A CA  
2043  C C   . LYS A 292  ? 0.2203 0.1743 0.2411 0.0081  0.0027  0.0177  290  LYS A C   
2044  O O   . LYS A 292  ? 0.1975 0.1528 0.2197 0.0071  0.0024  0.0183  290  LYS A O   
2045  C CB  . LYS A 292  ? 0.2104 0.1654 0.2336 0.0118  0.0044  0.0161  290  LYS A CB  
2046  C CG  . LYS A 292  ? 0.2268 0.1832 0.2535 0.0117  0.0037  0.0168  290  LYS A CG  
2047  C CD  . LYS A 292  ? 0.2455 0.2030 0.2753 0.0137  0.0034  0.0159  290  LYS A CD  
2048  C CE  . LYS A 292  ? 0.2714 0.2303 0.3048 0.0135  0.0025  0.0167  290  LYS A CE  
2049  N NZ  . LYS A 292  ? 0.2635 0.2240 0.3004 0.0158  0.0025  0.0155  290  LYS A NZ  
2050  N N   . ALA A 293  ? 0.2115 0.1639 0.2310 0.0076  0.0011  0.0180  291  ALA A N   
2051  C CA  . ALA A 293  ? 0.2120 0.1649 0.2316 0.0059  -0.0008 0.0194  291  ALA A CA  
2052  C C   . ALA A 293  ? 0.1955 0.1498 0.2130 0.0042  -0.0004 0.0193  291  ALA A C   
2053  O O   . ALA A 293  ? 0.2222 0.1784 0.2406 0.0030  -0.0014 0.0199  291  ALA A O   
2054  C CB  . ALA A 293  ? 0.2088 0.1601 0.2279 0.0056  -0.0025 0.0202  291  ALA A CB  
2055  N N   . LEU A 294  ? 0.1957 0.1494 0.2106 0.0041  0.0010  0.0183  292  LEU A N   
2056  C CA  . LEU A 294  ? 0.1901 0.1451 0.2037 0.0028  0.0013  0.0177  292  LEU A CA  
2057  C C   . LEU A 294  ? 0.1828 0.1390 0.1989 0.0029  0.0021  0.0173  292  LEU A C   
2058  O O   . LEU A 294  ? 0.2001 0.1581 0.2168 0.0017  0.0014  0.0169  292  LEU A O   
2059  C CB  . LEU A 294  ? 0.2129 0.1668 0.2239 0.0030  0.0025  0.0167  292  LEU A CB  
2060  C CG  . LEU A 294  ? 0.2051 0.1581 0.2137 0.0027  0.0018  0.0170  292  LEU A CG  
2061  C CD1 . LEU A 294  ? 0.2403 0.1921 0.2467 0.0032  0.0032  0.0160  292  LEU A CD1 
2062  C CD2 . LEU A 294  ? 0.2320 0.1871 0.2393 0.0009  0.0002  0.0177  292  LEU A CD2 
2063  N N   . ALA A 295  ? 0.1803 0.1360 0.1982 0.0043  0.0034  0.0174  293  ALA A N   
2064  C CA  . ALA A 295  ? 0.1963 0.1533 0.2172 0.0043  0.0041  0.0174  293  ALA A CA  
2065  C C   . ALA A 295  ? 0.1995 0.1580 0.2229 0.0037  0.0027  0.0180  293  ALA A C   
2066  O O   . ALA A 295  ? 0.1981 0.1580 0.2235 0.0029  0.0025  0.0177  293  ALA A O   
2067  C CB  . ALA A 295  ? 0.2072 0.1642 0.2294 0.0059  0.0059  0.0177  293  ALA A CB  
2068  N N   . LEU A 296  ? 0.1893 0.1475 0.2130 0.0042  0.0016  0.0187  294  LEU A N   
2069  C CA  . LEU A 296  ? 0.1884 0.1482 0.2145 0.0037  0.0000  0.0195  294  LEU A CA  
2070  C C   . LEU A 296  ? 0.2034 0.1649 0.2283 0.0018  -0.0014 0.0194  294  LEU A C   
2071  O O   . LEU A 296  ? 0.2052 0.1687 0.2322 0.0011  -0.0022 0.0194  294  LEU A O   
2072  C CB  . LEU A 296  ? 0.2010 0.1600 0.2280 0.0045  -0.0013 0.0205  294  LEU A CB  
2073  C CG  . LEU A 296  ? 0.2274 0.1859 0.2567 0.0066  -0.0003 0.0201  294  LEU A CG  
2074  C CD1 . LEU A 296  ? 0.2462 0.2033 0.2764 0.0075  -0.0019 0.0205  294  LEU A CD1 
2075  C CD2 . LEU A 296  ? 0.2790 0.2395 0.3119 0.0069  0.0001  0.0203  294  LEU A CD2 
2076  N N   . LEU A 297  ? 0.1985 0.1597 0.2201 0.0010  -0.0017 0.0192  295  LEU A N   
2077  C CA  . LEU A 297  ? 0.2128 0.1765 0.2330 -0.0006 -0.0029 0.0188  295  LEU A CA  
2078  C C   . LEU A 297  ? 0.1981 0.1628 0.2191 -0.0011 -0.0021 0.0168  295  LEU A C   
2079  O O   . LEU A 297  ? 0.2038 0.1713 0.2260 -0.0020 -0.0032 0.0161  295  LEU A O   
2080  C CB  . LEU A 297  ? 0.2305 0.1942 0.2472 -0.0013 -0.0034 0.0191  295  LEU A CB  
2081  C CG  . LEU A 297  ? 0.2559 0.2235 0.2710 -0.0030 -0.0049 0.0192  295  LEU A CG  
2082  C CD1 . LEU A 297  ? 0.3245 0.2944 0.3413 -0.0036 -0.0069 0.0212  295  LEU A CD1 
2083  C CD2 . LEU A 297  ? 0.3049 0.2727 0.3166 -0.0036 -0.0051 0.0196  295  LEU A CD2 
2084  N N   . ALA A 298  ? 0.1881 0.1508 0.2090 -0.0003 -0.0004 0.0159  296  ALA A N   
2085  C CA  . ALA A 298  ? 0.1926 0.1559 0.2155 -0.0007 0.0002  0.0143  296  ALA A CA  
2086  C C   . ALA A 298  ? 0.1983 0.1626 0.2254 -0.0007 0.0000  0.0146  296  ALA A C   
2087  O O   . ALA A 298  ? 0.2024 0.1683 0.2315 -0.0016 -0.0008 0.0131  296  ALA A O   
2088  C CB  . ALA A 298  ? 0.2100 0.1708 0.2326 0.0002  0.0020  0.0141  296  ALA A CB  
2089  N N   . LYS A 299  ? 0.1987 0.1623 0.2273 0.0003  0.0005  0.0162  297  LYS A N   
2090  C CA  A LYS A 299  ? 0.2036 0.1685 0.2362 0.0003  0.0002  0.0167  297  LYS A CA  
2091  C CA  B LYS A 299  ? 0.2037 0.1687 0.2364 0.0003  0.0002  0.0167  297  LYS A CA  
2092  C C   . LYS A 299  ? 0.2225 0.1900 0.2557 -0.0009 -0.0019 0.0163  297  LYS A C   
2093  O O   . LYS A 299  ? 0.2072 0.1763 0.2435 -0.0015 -0.0024 0.0155  297  LYS A O   
2094  C CB  A LYS A 299  ? 0.2032 0.1675 0.2370 0.0017  0.0010  0.0182  297  LYS A CB  
2095  C CB  B LYS A 299  ? 0.2035 0.1677 0.2372 0.0017  0.0010  0.0182  297  LYS A CB  
2096  C CG  A LYS A 299  ? 0.2165 0.1827 0.2542 0.0017  0.0003  0.0189  297  LYS A CG  
2097  C CG  B LYS A 299  ? 0.2166 0.1827 0.2544 0.0018  0.0005  0.0189  297  LYS A CG  
2098  C CD  A LYS A 299  ? 0.2343 0.2003 0.2733 0.0034  0.0011  0.0200  297  LYS A CD  
2099  C CD  B LYS A 299  ? 0.2225 0.1884 0.2617 0.0035  0.0016  0.0200  297  LYS A CD  
2100  C CE  A LYS A 299  ? 0.2250 0.1931 0.2678 0.0034  0.0000  0.0207  297  LYS A CE  
2101  C CE  B LYS A 299  ? 0.2477 0.2155 0.2906 0.0036  0.0007  0.0207  297  LYS A CE  
2102  N NZ  A LYS A 299  ? 0.2421 0.2108 0.2872 0.0051  0.0010  0.0213  297  LYS A NZ  
2103  N NZ  B LYS A 299  ? 0.2638 0.2322 0.3060 0.0029  -0.0016 0.0209  297  LYS A NZ  
2104  N N   . ASN A 300  ? 0.2053 0.1734 0.2357 -0.0012 -0.0031 0.0170  298  ASN A N   
2105  C CA  . ASN A 300  ? 0.1963 0.1676 0.2273 -0.0022 -0.0051 0.0172  298  ASN A CA  
2106  C C   . ASN A 300  ? 0.2035 0.1774 0.2341 -0.0035 -0.0059 0.0148  298  ASN A C   
2107  O O   . ASN A 300  ? 0.2545 0.2314 0.2873 -0.0042 -0.0071 0.0141  298  ASN A O   
2108  C CB  . ASN A 300  ? 0.2580 0.2299 0.2866 -0.0025 -0.0065 0.0190  298  ASN A CB  
2109  C CG  . ASN A 300  ? 0.3652 0.3406 0.3950 -0.0034 -0.0086 0.0199  298  ASN A CG  
2110  O OD1 . ASN A 300  ? 0.4210 0.3964 0.4539 -0.0029 -0.0091 0.0211  298  ASN A OD1 
2111  N ND2 . ASN A 300  ? 0.3196 0.2986 0.3473 -0.0048 -0.0098 0.0193  298  ASN A ND2 
2112  N N   . TYR A 301  ? 0.2067 0.1800 0.2348 -0.0037 -0.0052 0.0134  299  TYR A N   
2113  C CA  . TYR A 301  ? 0.2192 0.1950 0.2475 -0.0045 -0.0058 0.0105  299  TYR A CA  
2114  C C   . TYR A 301  ? 0.2168 0.1911 0.2491 -0.0043 -0.0050 0.0089  299  TYR A C   
2115  O O   . TYR A 301  ? 0.2365 0.2127 0.2704 -0.0049 -0.0058 0.0061  299  TYR A O   
2116  C CB  . TYR A 301  ? 0.2052 0.1812 0.2294 -0.0048 -0.0054 0.0096  299  TYR A CB  
2117  C CG  . TYR A 301  ? 0.2076 0.1865 0.2282 -0.0055 -0.0066 0.0110  299  TYR A CG  
2118  C CD1 . TYR A 301  ? 0.2173 0.2016 0.2374 -0.0066 -0.0084 0.0101  299  TYR A CD1 
2119  C CD2 . TYR A 301  ? 0.2097 0.1866 0.2276 -0.0052 -0.0061 0.0131  299  TYR A CD2 
2120  C CE1 . TYR A 301  ? 0.2360 0.2236 0.2528 -0.0075 -0.0095 0.0119  299  TYR A CE1 
2121  C CE2 . TYR A 301  ? 0.2214 0.2010 0.2364 -0.0061 -0.0073 0.0147  299  TYR A CE2 
2122  C CZ  . TYR A 301  ? 0.2386 0.2237 0.2531 -0.0073 -0.0090 0.0144  299  TYR A CZ  
2123  O OH  . TYR A 301  ? 0.2453 0.2338 0.2571 -0.0083 -0.0102 0.0167  299  TYR A OH  
2124  N N   . ASP A 302  ? 0.1936 0.1647 0.2280 -0.0034 -0.0035 0.0105  300  ASP A N   
2125  C CA  . ASP A 302  ? 0.1962 0.1659 0.2349 -0.0032 -0.0026 0.0098  300  ASP A CA  
2126  C C   . ASP A 302  ? 0.2046 0.1732 0.2427 -0.0033 -0.0023 0.0077  300  ASP A C   
2127  O O   . ASP A 302  ? 0.2084 0.1777 0.2499 -0.0039 -0.0030 0.0055  300  ASP A O   
2128  C CB  . ASP A 302  ? 0.2127 0.1843 0.2561 -0.0039 -0.0038 0.0090  300  ASP A CB  
2129  C CG  . ASP A 302  ? 0.2392 0.2091 0.2877 -0.0037 -0.0028 0.0097  300  ASP A CG  
2130  O OD1 . ASP A 302  ? 0.2508 0.2188 0.2990 -0.0028 -0.0010 0.0120  300  ASP A OD1 
2131  O OD2 . ASP A 302  ? 0.2873 0.2581 0.3405 -0.0044 -0.0038 0.0081  300  ASP A OD2 
2132  N N   . ILE A 303  ? 0.1868 0.1537 0.2210 -0.0028 -0.0012 0.0085  301  ILE A N   
2133  C CA  . ILE A 303  ? 0.1927 0.1583 0.2264 -0.0027 -0.0006 0.0069  301  ILE A CA  
2134  C C   . ILE A 303  ? 0.2018 0.1643 0.2354 -0.0017 0.0013  0.0090  301  ILE A C   
2135  O O   . ILE A 303  ? 0.1924 0.1542 0.2252 -0.0010 0.0022  0.0113  301  ILE A O   
2136  C CB  . ILE A 303  ? 0.1999 0.1670 0.2287 -0.0030 -0.0012 0.0055  301  ILE A CB  
2137  C CG1 . ILE A 303  ? 0.1992 0.1648 0.2237 -0.0024 -0.0003 0.0079  301  ILE A CG1 
2138  C CG2 . ILE A 303  ? 0.2166 0.1880 0.2449 -0.0039 -0.0030 0.0038  301  ILE A CG2 
2139  C CD1 . ILE A 303  ? 0.2264 0.1933 0.2466 -0.0027 -0.0006 0.0070  301  ILE A CD1 
2140  N N   . GLY A 304  ? 0.2018 0.1629 0.2366 -0.0016 0.0018  0.0081  302  GLY A N   
2141  C CA  . GLY A 304  ? 0.2037 0.1625 0.2381 -0.0007 0.0035  0.0102  302  GLY A CA  
2142  C C   . GLY A 304  ? 0.2024 0.1604 0.2312 0.0000  0.0042  0.0106  302  GLY A C   
2143  O O   . GLY A 304  ? 0.2000 0.1589 0.2257 -0.0004 0.0034  0.0091  302  GLY A O   
2144  N N   . LEU A 305  ? 0.1995 0.1564 0.2273 0.0009  0.0057  0.0128  303  LEU A N   
2145  C CA  . LEU A 305  ? 0.1899 0.1457 0.2131 0.0017  0.0064  0.0132  303  LEU A CA  
2146  C C   . LEU A 305  ? 0.1983 0.1530 0.2221 0.0026  0.0079  0.0146  303  LEU A C   
2147  O O   . LEU A 305  ? 0.2047 0.1600 0.2301 0.0033  0.0089  0.0164  303  LEU A O   
2148  C CB  . LEU A 305  ? 0.2115 0.1676 0.2327 0.0022  0.0062  0.0143  303  LEU A CB  
2149  C CG  . LEU A 305  ? 0.2628 0.2178 0.2798 0.0028  0.0065  0.0144  303  LEU A CG  
2150  C CD1 . LEU A 305  ? 0.2903 0.2458 0.3060 0.0026  0.0053  0.0148  303  LEU A CD1 
2151  C CD2 . LEU A 305  ? 0.3602 0.3143 0.3768 0.0042  0.0081  0.0155  303  LEU A CD2 
2152  N N   . ASN A 306  ? 0.2053 0.1589 0.2278 0.0026  0.0082  0.0138  304  ASN A N   
2153  C CA  . ASN A 306  ? 0.2134 0.1663 0.2368 0.0033  0.0095  0.0153  304  ASN A CA  
2154  C C   . ASN A 306  ? 0.2026 0.1549 0.2215 0.0043  0.0103  0.0155  304  ASN A C   
2155  O O   . ASN A 306  ? 0.2150 0.1667 0.2306 0.0041  0.0097  0.0141  304  ASN A O   
2156  C CB  . ASN A 306  ? 0.2079 0.1600 0.2337 0.0027  0.0089  0.0141  304  ASN A CB  
2157  C CG  . ASN A 306  ? 0.2276 0.1790 0.2539 0.0034  0.0101  0.0158  304  ASN A CG  
2158  O OD1 . ASN A 306  ? 0.2806 0.2311 0.3037 0.0038  0.0104  0.0152  304  ASN A OD1 
2159  N ND2 . ASN A 306  ? 0.2104 0.1624 0.2406 0.0034  0.0107  0.0182  304  ASN A ND2 
2160  N N   . ILE A 307  ? 0.1963 0.1491 0.2151 0.0053  0.0117  0.0174  305  ILE A N   
2161  C CA  . ILE A 307  ? 0.1954 0.1479 0.2103 0.0064  0.0125  0.0175  305  ILE A CA  
2162  C C   . ILE A 307  ? 0.1974 0.1494 0.2127 0.0065  0.0131  0.0181  305  ILE A C   
2163  O O   . ILE A 307  ? 0.2104 0.1635 0.2285 0.0067  0.0139  0.0201  305  ILE A O   
2164  C CB  . ILE A 307  ? 0.1996 0.1538 0.2140 0.0077  0.0136  0.0187  305  ILE A CB  
2165  C CG1 . ILE A 307  ? 0.2323 0.1867 0.2468 0.0077  0.0127  0.0181  305  ILE A CG1 
2166  C CG2 . ILE A 307  ? 0.2553 0.2096 0.2662 0.0089  0.0143  0.0185  305  ILE A CG2 
2167  C CD1 . ILE A 307  ? 0.3033 0.2600 0.3188 0.0090  0.0136  0.0190  305  ILE A CD1 
2168  N N   . ASP A 308  ? 0.1973 0.1480 0.2101 0.0063  0.0125  0.0165  306  ASP A N   
2169  C CA  . ASP A 308  ? 0.2135 0.1636 0.2266 0.0064  0.0129  0.0168  306  ASP A CA  
2170  C C   . ASP A 308  ? 0.2149 0.1661 0.2262 0.0077  0.0142  0.0186  306  ASP A C   
2171  O O   . ASP A 308  ? 0.2285 0.1805 0.2371 0.0085  0.0147  0.0185  306  ASP A O   
2172  C CB  . ASP A 308  ? 0.2287 0.1776 0.2390 0.0060  0.0121  0.0145  306  ASP A CB  
2173  C CG  . ASP A 308  ? 0.2842 0.2330 0.2967 0.0049  0.0108  0.0125  306  ASP A CG  
2174  O OD1 . ASP A 308  ? 0.2676 0.2166 0.2840 0.0044  0.0104  0.0127  306  ASP A OD1 
2175  O OD2 . ASP A 308  ? 0.2930 0.2418 0.3032 0.0045  0.0101  0.0105  306  ASP A OD2 
2176  N N   . ALA A 309  ? 0.1915 0.1430 0.2046 0.0078  0.0147  0.0201  307  ALA A N   
2177  C CA  . ALA A 309  ? 0.1800 0.1335 0.1914 0.0090  0.0160  0.0220  307  ALA A CA  
2178  C C   . ALA A 309  ? 0.2186 0.1710 0.2266 0.0094  0.0159  0.0207  307  ALA A C   
2179  O O   . ALA A 309  ? 0.2164 0.1670 0.2253 0.0088  0.0151  0.0197  307  ALA A O   
2180  C CB  . ALA A 309  ? 0.2138 0.1689 0.2293 0.0088  0.0166  0.0252  307  ALA A CB  
2181  N N   . GLU A 310  ? 0.2076 0.1614 0.2121 0.0106  0.0166  0.0207  308  GLU A N   
2182  C CA  . GLU A 310  ? 0.2046 0.1574 0.2056 0.0110  0.0164  0.0193  308  GLU A CA  
2183  C C   . GLU A 310  ? 0.1965 0.1517 0.1967 0.0121  0.0174  0.0211  308  GLU A C   
2184  O O   . GLU A 310  ? 0.2162 0.1728 0.2194 0.0119  0.0178  0.0237  308  GLU A O   
2185  C CB  . GLU A 310  ? 0.2234 0.1754 0.2213 0.0113  0.0158  0.0171  308  GLU A CB  
2186  C CG  . GLU A 310  ? 0.2562 0.2063 0.2551 0.0100  0.0147  0.0157  308  GLU A CG  
2187  C CD  . GLU A 310  ? 0.2610 0.2102 0.2572 0.0099  0.0139  0.0141  308  GLU A CD  
2188  O OE1 . GLU A 310  ? 0.2879 0.2361 0.2818 0.0097  0.0134  0.0130  308  GLU A OE1 
2189  O OE2 . GLU A 310  ? 0.2440 0.1935 0.2408 0.0101  0.0136  0.0140  308  GLU A OE2 
2190  N N   . GLU A 311  ? 0.2140 0.1700 0.2105 0.0131  0.0176  0.0200  309  GLU A N   
2191  C CA  . GLU A 311  ? 0.2303 0.1892 0.2256 0.0142  0.0184  0.0214  309  GLU A CA  
2192  C C   . GLU A 311  ? 0.2049 0.1681 0.2013 0.0150  0.0197  0.0237  309  GLU A C   
2193  O O   . GLU A 311  ? 0.2061 0.1702 0.2032 0.0152  0.0199  0.0234  309  GLU A O   
2194  C CB  . GLU A 311  ? 0.2371 0.1960 0.2283 0.0152  0.0182  0.0192  309  GLU A CB  
2195  C CG  . GLU A 311  ? 0.2528 0.2082 0.2427 0.0144  0.0171  0.0173  309  GLU A CG  
2196  C CD  . GLU A 311  ? 0.3140 0.2668 0.3034 0.0136  0.0161  0.0151  309  GLU A CD  
2197  O OE1 . GLU A 311  ? 0.2532 0.2062 0.2439 0.0134  0.0161  0.0152  309  GLU A OE1 
2198  O OE2 . GLU A 311  ? 0.3677 0.3186 0.3556 0.0130  0.0153  0.0136  309  GLU A OE2 
2199  N N   . ALA A 312  ? 0.2002 0.1667 0.1968 0.0156  0.0205  0.0262  310  ALA A N   
2200  C CA  . ALA A 312  ? 0.1930 0.1648 0.1908 0.0162  0.0217  0.0290  310  ALA A CA  
2201  C C   . ALA A 312  ? 0.1929 0.1679 0.1880 0.0177  0.0223  0.0269  310  ALA A C   
2202  O O   . ALA A 312  ? 0.2166 0.1951 0.2133 0.0181  0.0232  0.0281  310  ALA A O   
2203  C CB  . ALA A 312  ? 0.2133 0.1886 0.2112 0.0166  0.0223  0.0322  310  ALA A CB  
2204  N N   . ASP A 313  ? 0.2107 0.1847 0.2023 0.0187  0.0218  0.0236  311  ASP A N   
2205  C CA  . ASP A 313  ? 0.2149 0.1919 0.2046 0.0203  0.0221  0.0211  311  ASP A CA  
2206  C C   . ASP A 313  ? 0.2076 0.1817 0.1986 0.0200  0.0214  0.0192  311  ASP A C   
2207  O O   . ASP A 313  ? 0.2418 0.2177 0.2320 0.0214  0.0214  0.0168  311  ASP A O   
2208  C CB  . ASP A 313  ? 0.2429 0.2204 0.2290 0.0216  0.0216  0.0184  311  ASP A CB  
2209  C CG  . ASP A 313  ? 0.3124 0.2839 0.2975 0.0207  0.0201  0.0160  311  ASP A CG  
2210  O OD1 . ASP A 313  ? 0.2681 0.2353 0.2549 0.0192  0.0195  0.0163  311  ASP A OD1 
2211  O OD2 . ASP A 313  ? 0.3370 0.3084 0.3197 0.0216  0.0196  0.0138  311  ASP A OD2 
2212  N N   . ARG A 314  ? 0.2027 0.1727 0.1960 0.0183  0.0208  0.0200  312  ARG A N   
2213  C CA  . ARG A 314  ? 0.1922 0.1600 0.1870 0.0179  0.0201  0.0187  312  ARG A CA  
2214  C C   . ARG A 314  ? 0.2098 0.1793 0.2081 0.0172  0.0208  0.0211  312  ARG A C   
2215  O O   . ARG A 314  ? 0.2242 0.1930 0.2240 0.0171  0.0204  0.0203  312  ARG A O   
2216  C CB  . ARG A 314  ? 0.2181 0.1804 0.2127 0.0164  0.0186  0.0173  312  ARG A CB  
2217  C CG  . ARG A 314  ? 0.2457 0.2063 0.2374 0.0170  0.0177  0.0146  312  ARG A CG  
2218  C CD  . ARG A 314  ? 0.2695 0.2260 0.2605 0.0156  0.0165  0.0139  312  ARG A CD  
2219  N NE  . ARG A 314  ? 0.2673 0.2220 0.2566 0.0158  0.0153  0.0116  312  ARG A NE  
2220  C CZ  . ARG A 314  ? 0.2516 0.2035 0.2399 0.0147  0.0143  0.0108  312  ARG A CZ  
2221  N NH1 . ARG A 314  ? 0.2725 0.2232 0.2609 0.0135  0.0143  0.0117  312  ARG A NH1 
2222  N NH2 . ARG A 314  ? 0.2783 0.2287 0.2659 0.0148  0.0130  0.0091  312  ARG A NH2 
2223  N N   . LEU A 315  ? 0.2047 0.1769 0.2048 0.0168  0.0218  0.0244  313  LEU A N   
2224  C CA  . LEU A 315  ? 0.2076 0.1812 0.2116 0.0159  0.0223  0.0271  313  LEU A CA  
2225  C C   . LEU A 315  ? 0.2179 0.1956 0.2225 0.0170  0.0231  0.0267  313  LEU A C   
2226  O O   . LEU A 315  ? 0.2175 0.1938 0.2243 0.0165  0.0226  0.0262  313  LEU A O   
2227  C CB  . LEU A 315  ? 0.2137 0.1903 0.2197 0.0155  0.0231  0.0310  313  LEU A CB  
2228  C CG  . LEU A 315  ? 0.2085 0.1847 0.2198 0.0139  0.0230  0.0342  313  LEU A CG  
2229  C CD1 . LEU A 315  ? 0.2220 0.2009 0.2353 0.0135  0.0236  0.0383  313  LEU A CD1 
2230  C CD2 . LEU A 315  ? 0.2523 0.2317 0.2659 0.0140  0.0237  0.0350  313  LEU A CD2 
2231  N N   . GLU A 316  ? 0.2121 0.1952 0.2148 0.0187  0.0242  0.0267  314  GLU A N   
2232  C CA  . GLU A 316  ? 0.2124 0.2005 0.2162 0.0199  0.0251  0.0264  314  GLU A CA  
2233  C C   . GLU A 316  ? 0.2449 0.2303 0.2482 0.0207  0.0241  0.0225  314  GLU A C   
2234  O O   . GLU A 316  ? 0.2286 0.2152 0.2343 0.0208  0.0242  0.0223  314  GLU A O   
2235  C CB  . GLU A 316  ? 0.2312 0.2270 0.2333 0.0216  0.0266  0.0272  314  GLU A CB  
2236  C CG  . GLU A 316  ? 0.2281 0.2276 0.2322 0.0206  0.0277  0.0323  314  GLU A CG  
2237  C CD  . GLU A 316  ? 0.2298 0.2380 0.2322 0.0221  0.0292  0.0337  314  GLU A CD  
2238  O OE1 . GLU A 316  ? 0.2622 0.2759 0.2637 0.0238  0.0301  0.0318  314  GLU A OE1 
2239  O OE2 . GLU A 316  ? 0.2453 0.2551 0.2472 0.0216  0.0295  0.0368  314  GLU A OE2 
2240  N N   . LEU A 317  ? 0.2286 0.2101 0.2292 0.0210  0.0229  0.0195  315  LEU A N   
2241  C CA  . LEU A 317  ? 0.2347 0.2129 0.2355 0.0215  0.0215  0.0163  315  LEU A CA  
2242  C C   . LEU A 317  ? 0.2292 0.2035 0.2326 0.0197  0.0206  0.0172  315  LEU A C   
2243  O O   . LEU A 317  ? 0.2269 0.2012 0.2321 0.0201  0.0201  0.0161  315  LEU A O   
2244  C CB  . LEU A 317  ? 0.2526 0.2271 0.2506 0.0217  0.0202  0.0137  315  LEU A CB  
2245  C CG  . LEU A 317  ? 0.2634 0.2342 0.2621 0.0218  0.0184  0.0110  315  LEU A CG  
2246  C CD1 . LEU A 317  ? 0.3033 0.2778 0.3035 0.0239  0.0185  0.0088  315  LEU A CD1 
2247  C CD2 . LEU A 317  ? 0.3108 0.2781 0.3071 0.0218  0.0172  0.0090  315  LEU A CD2 
2248  N N   . SER A 318  ? 0.1981 0.1693 0.2020 0.0179  0.0203  0.0191  316  SER A N   
2249  C CA  . SER A 318  ? 0.2009 0.1689 0.2073 0.0162  0.0194  0.0196  316  SER A CA  
2250  C C   . SER A 318  ? 0.2222 0.1934 0.2321 0.0162  0.0202  0.0213  316  SER A C   
2251  O O   . SER A 318  ? 0.2141 0.1835 0.2259 0.0155  0.0194  0.0209  316  SER A O   
2252  C CB  . SER A 318  ? 0.1951 0.1599 0.2018 0.0145  0.0190  0.0208  316  SER A CB  
2253  O OG  . SER A 318  ? 0.2199 0.1873 0.2287 0.0141  0.0201  0.0238  316  SER A OG  
2254  N N   . LEU A 319  ? 0.2119 0.1881 0.2225 0.0169  0.0218  0.0234  317  LEU A N   
2255  C CA  . LEU A 319  ? 0.2042 0.1843 0.2184 0.0168  0.0227  0.0254  317  LEU A CA  
2256  C C   . LEU A 319  ? 0.2176 0.1994 0.2321 0.0183  0.0225  0.0230  317  LEU A C   
2257  O O   . LEU A 319  ? 0.2144 0.1972 0.2320 0.0179  0.0225  0.0237  317  LEU A O   
2258  C CB  . LEU A 319  ? 0.2214 0.2076 0.2362 0.0173  0.0245  0.0284  317  LEU A CB  
2259  C CG  . LEU A 319  ? 0.2377 0.2225 0.2535 0.0158  0.0246  0.0315  317  LEU A CG  
2260  C CD1 . LEU A 319  ? 0.2357 0.2275 0.2521 0.0164  0.0263  0.0349  317  LEU A CD1 
2261  C CD2 . LEU A 319  ? 0.2373 0.2188 0.2574 0.0138  0.0237  0.0330  317  LEU A CD2 
2262  N N   . ASP A 320  ? 0.2159 0.1982 0.2277 0.0200  0.0223  0.0201  318  ASP A N   
2263  C CA  . ASP A 320  ? 0.2558 0.2393 0.2687 0.0215  0.0218  0.0175  318  ASP A CA  
2264  C C   . ASP A 320  ? 0.2485 0.2265 0.2627 0.0204  0.0199  0.0166  318  ASP A C   
2265  O O   . ASP A 320  ? 0.2654 0.2445 0.2823 0.0208  0.0195  0.0160  318  ASP A O   
2266  C CB  . ASP A 320  ? 0.2492 0.2342 0.2595 0.0237  0.0216  0.0143  318  ASP A CB  
2267  C CG  . ASP A 320  ? 0.2972 0.2898 0.3068 0.0253  0.0235  0.0147  318  ASP A CG  
2268  O OD1 . ASP A 320  ? 0.3100 0.3079 0.3219 0.0259  0.0247  0.0158  318  ASP A OD1 
2269  O OD2 . ASP A 320  ? 0.3308 0.3243 0.3374 0.0260  0.0238  0.0142  318  ASP A OD2 
2270  N N   . LEU A 321  ? 0.2128 0.1856 0.2255 0.0189  0.0187  0.0166  319  LEU A N   
2271  C CA  . LEU A 321  ? 0.2226 0.1912 0.2366 0.0175  0.0170  0.0162  319  LEU A CA  
2272  C C   . LEU A 321  ? 0.2199 0.1889 0.2369 0.0161  0.0172  0.0184  319  LEU A C   
2273  O O   . LEU A 321  ? 0.2312 0.1998 0.2505 0.0158  0.0163  0.0181  319  LEU A O   
2274  C CB  . LEU A 321  ? 0.2260 0.1900 0.2375 0.0163  0.0157  0.0156  319  LEU A CB  
2275  C CG  . LEU A 321  ? 0.2681 0.2305 0.2774 0.0174  0.0147  0.0132  319  LEU A CG  
2276  C CD1 . LEU A 321  ? 0.3206 0.2846 0.3273 0.0184  0.0159  0.0129  319  LEU A CD1 
2277  C CD2 . LEU A 321  ? 0.3295 0.2874 0.3378 0.0158  0.0129  0.0129  319  LEU A CD2 
2278  N N   . LEU A 322  ? 0.2079 0.1778 0.2254 0.0151  0.0182  0.0206  320  LEU A N   
2279  C CA  . LEU A 322  ? 0.2130 0.1835 0.2342 0.0136  0.0183  0.0227  320  LEU A CA  
2280  C C   . LEU A 322  ? 0.2184 0.1931 0.2425 0.0145  0.0191  0.0233  320  LEU A C   
2281  O O   . LEU A 322  ? 0.2263 0.2005 0.2533 0.0137  0.0184  0.0237  320  LEU A O   
2282  C CB  . LEU A 322  ? 0.2188 0.1899 0.2407 0.0127  0.0192  0.0251  320  LEU A CB  
2283  C CG  . LEU A 322  ? 0.2392 0.2106 0.2657 0.0111  0.0191  0.0273  320  LEU A CG  
2284  C CD1 . LEU A 322  ? 0.2213 0.1884 0.2486 0.0096  0.0173  0.0259  320  LEU A CD1 
2285  C CD2 . LEU A 322  ? 0.2141 0.1872 0.2425 0.0105  0.0201  0.0302  320  LEU A CD2 
2286  N N   . GLU A 323  ? 0.1998 0.1792 0.2231 0.0163  0.0206  0.0233  321  GLU A N   
2287  C CA  . GLU A 323  ? 0.2292 0.2135 0.2553 0.0174  0.0215  0.0237  321  GLU A CA  
2288  C C   . GLU A 323  ? 0.2692 0.2517 0.2963 0.0180  0.0200  0.0213  321  GLU A C   
2289  O O   . GLU A 323  ? 0.2342 0.2177 0.2647 0.0175  0.0198  0.0221  321  GLU A O   
2290  C CB  . GLU A 323  ? 0.2418 0.2321 0.2663 0.0195  0.0232  0.0233  321  GLU A CB  
2291  C CG  . GLU A 323  ? 0.3112 0.3074 0.3382 0.0211  0.0241  0.0227  321  GLU A CG  
2292  C CD  . GLU A 323  ? 0.3390 0.3421 0.3680 0.0210  0.0261  0.0262  321  GLU A CD  
2293  O OE1 . GLU A 323  ? 0.3792 0.3825 0.4077 0.0197  0.0268  0.0291  321  GLU A OE1 
2294  O OE2 . GLU A 323  ? 0.3389 0.3474 0.3703 0.0220  0.0270  0.0261  321  GLU A OE2 
2295  N N   . VAL A 324  ? 0.2175 0.1973 0.2422 0.0190  0.0189  0.0185  322  VAL A N   
2296  C CA  . VAL A 324  ? 0.2025 0.1806 0.2289 0.0197  0.0173  0.0166  322  VAL A CA  
2297  C C   . VAL A 324  ? 0.2230 0.1974 0.2510 0.0176  0.0158  0.0177  322  VAL A C   
2298  O O   . VAL A 324  ? 0.2231 0.1981 0.2540 0.0176  0.0151  0.0176  322  VAL A O   
2299  C CB  . VAL A 324  ? 0.2693 0.2448 0.2934 0.0209  0.0160  0.0137  322  VAL A CB  
2300  C CG1 . VAL A 324  ? 0.2749 0.2482 0.3014 0.0213  0.0140  0.0122  322  VAL A CG1 
2301  C CG2 . VAL A 324  ? 0.2753 0.2551 0.2982 0.0232  0.0173  0.0120  322  VAL A CG2 
2302  N N   . LEU A 325  ? 0.1945 0.1654 0.2207 0.0158  0.0153  0.0185  323  LEU A N   
2303  C CA  . LEU A 325  ? 0.2107 0.1787 0.2381 0.0139  0.0138  0.0191  323  LEU A CA  
2304  C C   . LEU A 325  ? 0.2087 0.1791 0.2399 0.0130  0.0144  0.0209  323  LEU A C   
2305  O O   . LEU A 325  ? 0.2015 0.1714 0.2349 0.0124  0.0132  0.0209  323  LEU A O   
2306  C CB  . LEU A 325  ? 0.2316 0.1962 0.2563 0.0124  0.0133  0.0192  323  LEU A CB  
2307  C CG  . LEU A 325  ? 0.2339 0.1959 0.2553 0.0128  0.0123  0.0176  323  LEU A CG  
2308  C CD1 . LEU A 325  ? 0.2565 0.2165 0.2753 0.0117  0.0125  0.0178  323  LEU A CD1 
2309  C CD2 . LEU A 325  ? 0.2398 0.1997 0.2617 0.0122  0.0102  0.0170  323  LEU A CD2 
2310  N N   . CYS A 326  ? 0.2049 0.1780 0.2370 0.0129  0.0161  0.0226  324  CYS A N   
2311  C CA  . CYS A 326  ? 0.2061 0.1816 0.2425 0.0119  0.0165  0.0246  324  CYS A CA  
2312  C C   . CYS A 326  ? 0.2407 0.2200 0.2797 0.0132  0.0170  0.0246  324  CYS A C   
2313  O O   . CYS A 326  ? 0.2207 0.2012 0.2635 0.0122  0.0168  0.0258  324  CYS A O   
2314  C CB  . CYS A 326  ? 0.2187 0.1963 0.2560 0.0114  0.0181  0.0271  324  CYS A CB  
2315  S SG  . CYS A 326  ? 0.2469 0.2197 0.2828 0.0096  0.0171  0.0271  324  CYS A SG  
2316  N N   . LEU A 327  ? 0.2299 0.2113 0.2675 0.0153  0.0175  0.0230  325  LEU A N   
2317  C CA  . LEU A 327  ? 0.1995 0.1849 0.2399 0.0168  0.0179  0.0224  325  LEU A CA  
2318  C C   . LEU A 327  ? 0.2031 0.1857 0.2442 0.0172  0.0158  0.0204  325  LEU A C   
2319  O O   . LEU A 327  ? 0.2286 0.2140 0.2725 0.0185  0.0157  0.0197  325  LEU A O   
2320  C CB  . LEU A 327  ? 0.2121 0.2025 0.2513 0.0191  0.0196  0.0215  325  LEU A CB  
2321  C CG  . LEU A 327  ? 0.3015 0.2963 0.3404 0.0189  0.0217  0.0241  325  LEU A CG  
2322  C CD1 . LEU A 327  ? 0.3037 0.3042 0.3410 0.0213  0.0233  0.0227  325  LEU A CD1 
2323  C CD2 . LEU A 327  ? 0.3110 0.3091 0.3544 0.0175  0.0225  0.0272  325  LEU A CD2 
2324  N N   . ASP A 328  ? 0.2034 0.1808 0.2422 0.0162  0.0140  0.0196  326  ASP A N   
2325  C CA  . ASP A 328  ? 0.2177 0.1925 0.2571 0.0165  0.0119  0.0182  326  ASP A CA  
2326  C C   . ASP A 328  ? 0.2372 0.2117 0.2796 0.0150  0.0107  0.0194  326  ASP A C   
2327  O O   . ASP A 328  ? 0.2180 0.1905 0.2598 0.0130  0.0102  0.0204  326  ASP A O   
2328  C CB  . ASP A 328  ? 0.2257 0.1959 0.2615 0.0158  0.0105  0.0174  326  ASP A CB  
2329  C CG  . ASP A 328  ? 0.2915 0.2593 0.3281 0.0163  0.0082  0.0163  326  ASP A CG  
2330  O OD1 . ASP A 328  ? 0.2735 0.2418 0.3131 0.0160  0.0071  0.0168  326  ASP A OD1 
2331  O OD2 . ASP A 328  ? 0.3194 0.2850 0.3540 0.0169  0.0075  0.0151  326  ASP A OD2 
2332  N N   . GLY A 329  ? 0.2216 0.1982 0.2674 0.0161  0.0102  0.0190  327  GLY A N   
2333  C CA  . GLY A 329  ? 0.2294 0.2063 0.2784 0.0148  0.0091  0.0201  327  GLY A CA  
2334  C C   . GLY A 329  ? 0.2303 0.2034 0.2780 0.0131  0.0068  0.0202  327  GLY A C   
2335  O O   . GLY A 329  ? 0.2209 0.1941 0.2702 0.0115  0.0060  0.0212  327  GLY A O   
2336  N N   . ASP A 330  ? 0.2189 0.1890 0.2639 0.0134  0.0056  0.0193  328  ASP A N   
2337  C CA  . ASP A 330  ? 0.2240 0.1913 0.2676 0.0117  0.0035  0.0198  328  ASP A CA  
2338  C C   . ASP A 330  ? 0.2159 0.1824 0.2574 0.0097  0.0038  0.0204  328  ASP A C   
2339  O O   . ASP A 330  ? 0.2300 0.1959 0.2711 0.0081  0.0022  0.0207  328  ASP A O   
2340  C CB  . ASP A 330  ? 0.2258 0.1903 0.2671 0.0122  0.0022  0.0191  328  ASP A CB  
2341  C CG  . ASP A 330  ? 0.3203 0.2849 0.3646 0.0140  0.0009  0.0184  328  ASP A CG  
2342  O OD1 . ASP A 330  ? 0.3320 0.2985 0.3800 0.0145  0.0004  0.0187  328  ASP A OD1 
2343  O OD2 . ASP A 330  ? 0.2769 0.2396 0.3203 0.0150  0.0003  0.0174  328  ASP A OD2 
2344  N N   . LEU A 331  ? 0.1963 0.1634 0.2368 0.0097  0.0058  0.0204  329  LEU A N   
2345  C CA  . LEU A 331  ? 0.2062 0.1725 0.2455 0.0080  0.0061  0.0207  329  LEU A CA  
2346  C C   . LEU A 331  ? 0.2225 0.1909 0.2654 0.0072  0.0067  0.0215  329  LEU A C   
2347  O O   . LEU A 331  ? 0.2288 0.1966 0.2719 0.0059  0.0069  0.0216  329  LEU A O   
2348  C CB  . LEU A 331  ? 0.2001 0.1653 0.2364 0.0084  0.0075  0.0204  329  LEU A CB  
2349  C CG  . LEU A 331  ? 0.1983 0.1609 0.2308 0.0086  0.0066  0.0195  329  LEU A CG  
2350  C CD1 . LEU A 331  ? 0.2158 0.1778 0.2456 0.0094  0.0082  0.0191  329  LEU A CD1 
2351  C CD2 . LEU A 331  ? 0.2362 0.1974 0.2671 0.0067  0.0050  0.0193  329  LEU A CD2 
2352  N N   . SER A 332  ? 0.2154 0.1863 0.2618 0.0079  0.0069  0.0221  330  SER A N   
2353  C CA  . SER A 332  ? 0.2387 0.2119 0.2892 0.0071  0.0076  0.0233  330  SER A CA  
2354  C C   . SER A 332  ? 0.2187 0.1912 0.2707 0.0052  0.0059  0.0229  330  SER A C   
2355  O O   . SER A 332  ? 0.2673 0.2387 0.3178 0.0047  0.0040  0.0221  330  SER A O   
2356  C CB  . SER A 332  ? 0.2374 0.2140 0.2914 0.0083  0.0083  0.0239  330  SER A CB  
2357  O OG  . SER A 332  ? 0.2775 0.2540 0.3327 0.0085  0.0065  0.0234  330  SER A OG  
2358  N N   . GLY A 333  ? 0.2033 0.1767 0.2584 0.0040  0.0063  0.0236  331  GLY A N   
2359  C CA  . GLY A 333  ? 0.2339 0.2070 0.2911 0.0023  0.0046  0.0228  331  GLY A CA  
2360  C C   . GLY A 333  ? 0.2250 0.1958 0.2799 0.0013  0.0041  0.0215  331  GLY A C   
2361  O O   . GLY A 333  ? 0.2574 0.2284 0.3143 -0.0001 0.0026  0.0203  331  GLY A O   
2362  N N   . TRP A 334  ? 0.2196 0.1887 0.2707 0.0019  0.0051  0.0214  332  TRP A N   
2363  C CA  . TRP A 334  ? 0.2188 0.1859 0.2675 0.0011  0.0046  0.0200  332  TRP A CA  
2364  C C   . TRP A 334  ? 0.2078 0.1742 0.2572 0.0014  0.0063  0.0211  332  TRP A C   
2365  O O   . TRP A 334  ? 0.2181 0.1850 0.2660 0.0027  0.0079  0.0224  332  TRP A O   
2366  C CB  . TRP A 334  ? 0.2171 0.1829 0.2605 0.0017  0.0041  0.0191  332  TRP A CB  
2367  C CG  . TRP A 334  ? 0.1949 0.1589 0.2351 0.0013  0.0041  0.0179  332  TRP A CG  
2368  C CD1 . TRP A 334  ? 0.2019 0.1659 0.2421 0.0001  0.0029  0.0161  332  TRP A CD1 
2369  C CD2 . TRP A 334  ? 0.1883 0.1507 0.2248 0.0022  0.0052  0.0181  332  TRP A CD2 
2370  N NE1 . TRP A 334  ? 0.2060 0.1685 0.2427 0.0002  0.0032  0.0153  332  TRP A NE1 
2371  C CE2 . TRP A 334  ? 0.1922 0.1535 0.2265 0.0014  0.0046  0.0166  332  TRP A CE2 
2372  C CE3 . TRP A 334  ? 0.2265 0.1887 0.2615 0.0036  0.0065  0.0192  332  TRP A CE3 
2373  C CZ2 . TRP A 334  ? 0.2128 0.1726 0.2435 0.0019  0.0054  0.0164  332  TRP A CZ2 
2374  C CZ3 . TRP A 334  ? 0.2235 0.1840 0.2548 0.0042  0.0072  0.0188  332  TRP A CZ3 
2375  C CH2 . TRP A 334  ? 0.2255 0.1847 0.2547 0.0033  0.0067  0.0176  332  TRP A CH2 
2376  N N   . ASN A 335  ? 0.1934 0.1590 0.2453 0.0003  0.0058  0.0205  333  ASN A N   
2377  C CA  . ASN A 335  ? 0.1845 0.1495 0.2379 0.0004  0.0071  0.0219  333  ASN A CA  
2378  C C   . ASN A 335  ? 0.1933 0.1560 0.2433 0.0003  0.0069  0.0203  333  ASN A C   
2379  O O   . ASN A 335  ? 0.2027 0.1645 0.2545 0.0001  0.0074  0.0210  333  ASN A O   
2380  C CB  . ASN A 335  ? 0.2074 0.1730 0.2675 -0.0008 0.0066  0.0227  333  ASN A CB  
2381  C CG  . ASN A 335  ? 0.2346 0.2030 0.2985 -0.0007 0.0075  0.0253  333  ASN A CG  
2382  O OD1 . ASN A 335  ? 0.2176 0.1877 0.2794 0.0005  0.0091  0.0269  333  ASN A OD1 
2383  N ND2 . ASN A 335  ? 0.2795 0.2488 0.3494 -0.0019 0.0065  0.0256  333  ASN A ND2 
2384  N N   . GLY A 336  ? 0.2066 0.1686 0.2519 0.0005  0.0061  0.0184  334  GLY A N   
2385  C CA  . GLY A 336  ? 0.1928 0.1530 0.2349 0.0004  0.0058  0.0168  334  GLY A CA  
2386  C C   . GLY A 336  ? 0.2040 0.1631 0.2424 0.0015  0.0074  0.0178  334  GLY A C   
2387  O O   . GLY A 336  ? 0.2047 0.1624 0.2408 0.0014  0.0072  0.0166  334  GLY A O   
2388  N N   . MET A 337  ? 0.2016 0.1616 0.2392 0.0026  0.0087  0.0197  335  MET A N   
2389  C CA  A MET A 337  ? 0.2141 0.1734 0.2482 0.0037  0.0101  0.0203  335  MET A CA  
2390  C CA  B MET A 337  ? 0.2142 0.1736 0.2483 0.0037  0.0101  0.0203  335  MET A CA  
2391  C C   . MET A 337  ? 0.1924 0.1512 0.2284 0.0034  0.0108  0.0214  335  MET A C   
2392  O O   . MET A 337  ? 0.2054 0.1655 0.2459 0.0031  0.0113  0.0232  335  MET A O   
2393  C CB  A MET A 337  ? 0.2184 0.1796 0.2519 0.0051  0.0113  0.0217  335  MET A CB  
2394  C CB  B MET A 337  ? 0.2186 0.1799 0.2523 0.0051  0.0113  0.0217  335  MET A CB  
2395  C CG  A MET A 337  ? 0.2613 0.2222 0.2909 0.0064  0.0124  0.0217  335  MET A CG  
2396  C CG  B MET A 337  ? 0.2828 0.2442 0.3136 0.0063  0.0128  0.0224  335  MET A CG  
2397  S SD  A MET A 337  ? 0.3456 0.3040 0.3703 0.0065  0.0112  0.0196  335  MET A SD  
2398  S SD  B MET A 337  ? 0.2810 0.2425 0.3080 0.0079  0.0128  0.0212  335  MET A SD  
2399  C CE  A MET A 337  ? 0.2829 0.2423 0.3080 0.0073  0.0105  0.0194  335  MET A CE  
2400  C CE  B MET A 337  ? 0.2056 0.1642 0.2301 0.0068  0.0107  0.0193  335  MET A CE  
2401  N N   . GLY A 338  ? 0.1976 0.1548 0.2305 0.0036  0.0109  0.0204  336  GLY A N   
2402  C CA  . GLY A 338  ? 0.2041 0.1606 0.2388 0.0034  0.0114  0.0214  336  GLY A CA  
2403  C C   . GLY A 338  ? 0.1944 0.1509 0.2252 0.0046  0.0127  0.0221  336  GLY A C   
2404  O O   . GLY A 338  ? 0.1945 0.1508 0.2210 0.0054  0.0128  0.0211  336  GLY A O   
2405  N N   . PHE A 339  ? 0.1962 0.1531 0.2290 0.0046  0.0134  0.0241  337  PHE A N   
2406  C CA  . PHE A 339  ? 0.2005 0.1582 0.2300 0.0058  0.0147  0.0252  337  PHE A CA  
2407  C C   . PHE A 339  ? 0.2004 0.1574 0.2323 0.0054  0.0148  0.0266  337  PHE A C   
2408  O O   . PHE A 339  ? 0.2074 0.1649 0.2447 0.0045  0.0146  0.0286  337  PHE A O   
2409  C CB  . PHE A 339  ? 0.2148 0.1760 0.2444 0.0067  0.0162  0.0274  337  PHE A CB  
2410  C CG  . PHE A 339  ? 0.2025 0.1653 0.2281 0.0082  0.0175  0.0278  337  PHE A CG  
2411  C CD1 . PHE A 339  ? 0.2307 0.1932 0.2519 0.0093  0.0175  0.0256  337  PHE A CD1 
2412  C CD2 . PHE A 339  ? 0.2077 0.1727 0.2344 0.0084  0.0186  0.0306  337  PHE A CD2 
2413  C CE1 . PHE A 339  ? 0.2176 0.1819 0.2355 0.0107  0.0185  0.0257  337  PHE A CE1 
2414  C CE2 . PHE A 339  ? 0.2380 0.2053 0.2610 0.0098  0.0197  0.0308  337  PHE A CE2 
2415  C CZ  . PHE A 339  ? 0.2351 0.2020 0.2536 0.0110  0.0197  0.0281  337  PHE A CZ  
2416  N N   . VAL A 340  ? 0.1982 0.1540 0.2265 0.0059  0.0149  0.0257  338  VAL A N   
2417  C CA  . VAL A 340  ? 0.1929 0.1479 0.2233 0.0057  0.0148  0.0269  338  VAL A CA  
2418  C C   . VAL A 340  ? 0.2098 0.1677 0.2398 0.0065  0.0163  0.0303  338  VAL A C   
2419  O O   . VAL A 340  ? 0.2123 0.1722 0.2381 0.0077  0.0174  0.0302  338  VAL A O   
2420  C CB  . VAL A 340  ? 0.1974 0.1500 0.2241 0.0059  0.0141  0.0241  338  VAL A CB  
2421  C CG1 . VAL A 340  ? 0.2068 0.1585 0.2359 0.0058  0.0139  0.0252  338  VAL A CG1 
2422  C CG2 . VAL A 340  ? 0.2066 0.1574 0.2336 0.0050  0.0126  0.0208  338  VAL A CG2 
2423  N N   . VAL A 341  ? 0.1998 0.1583 0.2346 0.0059  0.0162  0.0332  339  VAL A N   
2424  C CA  . VAL A 341  ? 0.1949 0.1566 0.2294 0.0066  0.0175  0.0368  339  VAL A CA  
2425  C C   . VAL A 341  ? 0.2011 0.1607 0.2377 0.0062  0.0167  0.0376  339  VAL A C   
2426  O O   . VAL A 341  ? 0.2265 0.1834 0.2682 0.0052  0.0152  0.0371  339  VAL A O   
2427  C CB  . VAL A 341  ? 0.2241 0.1899 0.2629 0.0062  0.0184  0.0410  339  VAL A CB  
2428  C CG1 . VAL A 341  ? 0.3055 0.2760 0.3421 0.0072  0.0200  0.0442  339  VAL A CG1 
2429  C CG2 . VAL A 341  ? 0.2567 0.2240 0.2944 0.0064  0.0189  0.0398  339  VAL A CG2 
2430  N N   . GLN A 342  ? 0.2004 0.1617 0.2335 0.0072  0.0175  0.0386  340  GLN A N   
2431  C CA  . GLN A 342  ? 0.2115 0.1708 0.2456 0.0071  0.0167  0.0389  340  GLN A CA  
2432  C C   . GLN A 342  ? 0.2016 0.1640 0.2400 0.0068  0.0171  0.0443  340  GLN A C   
2433  O O   . GLN A 342  ? 0.2149 0.1818 0.2506 0.0077  0.0186  0.0469  340  GLN A O   
2434  C CB  . GLN A 342  ? 0.2098 0.1689 0.2370 0.0084  0.0173  0.0366  340  GLN A CB  
2435  C CG  . GLN A 342  ? 0.1927 0.1491 0.2160 0.0085  0.0167  0.0318  340  GLN A CG  
2436  C CD  . GLN A 342  ? 0.2140 0.1715 0.2308 0.0097  0.0176  0.0303  340  GLN A CD  
2437  O OE1 . GLN A 342  ? 0.2187 0.1797 0.2335 0.0106  0.0188  0.0317  340  GLN A OE1 
2438  N NE2 . GLN A 342  ? 0.1958 0.1507 0.2096 0.0098  0.0169  0.0271  340  GLN A NE2 
2439  N N   . ALA A 343  ? 0.1847 0.1449 0.2302 0.0057  0.0156  0.0458  341  ALA A N   
2440  C CA  . ALA A 343  ? 0.2166 0.1794 0.2676 0.0051  0.0156  0.0515  341  ALA A CA  
2441  C C   . ALA A 343  ? 0.2254 0.1896 0.2741 0.0059  0.0159  0.0534  341  ALA A C   
2442  O O   . ALA A 343  ? 0.2306 0.1986 0.2822 0.0056  0.0163  0.0588  341  ALA A O   
2443  C CB  . ALA A 343  ? 0.2599 0.2195 0.3199 0.0037  0.0136  0.0524  341  ALA A CB  
2444  N N   . TYR A 344  ? 0.2194 0.1811 0.2630 0.0068  0.0157  0.0494  342  TYR A N   
2445  C CA  . TYR A 344  ? 0.2284 0.1920 0.2691 0.0077  0.0162  0.0513  342  TYR A CA  
2446  C C   . TYR A 344  ? 0.2488 0.2182 0.2836 0.0088  0.0182  0.0529  342  TYR A C   
2447  O O   . TYR A 344  ? 0.2443 0.2166 0.2769 0.0095  0.0187  0.0549  342  TYR A O   
2448  C CB  . TYR A 344  ? 0.2123 0.1719 0.2501 0.0083  0.0153  0.0469  342  TYR A CB  
2449  C CG  . TYR A 344  ? 0.2002 0.1589 0.2304 0.0092  0.0159  0.0420  342  TYR A CG  
2450  C CD1 . TYR A 344  ? 0.2136 0.1741 0.2398 0.0096  0.0171  0.0407  342  TYR A CD1 
2451  C CD2 . TYR A 344  ? 0.2062 0.1621 0.2338 0.0096  0.0152  0.0386  342  TYR A CD2 
2452  C CE1 . TYR A 344  ? 0.2140 0.1733 0.2342 0.0103  0.0174  0.0365  342  TYR A CE1 
2453  C CE2 . TYR A 344  ? 0.2335 0.1885 0.2550 0.0102  0.0156  0.0346  342  TYR A CE2 
2454  C CZ  . TYR A 344  ? 0.2349 0.1914 0.2528 0.0105  0.0166  0.0336  342  TYR A CZ  
2455  O OH  . TYR A 344  ? 0.2122 0.1676 0.2247 0.0110  0.0167  0.0299  342  TYR A OH  
2456  N N   . GLY A 345  ? 0.2105 0.1819 0.2431 0.0090  0.0193  0.0518  343  GLY A N   
2457  C CA  . GLY A 345  ? 0.2290 0.2061 0.2563 0.0102  0.0211  0.0524  343  GLY A CA  
2458  C C   . GLY A 345  ? 0.2212 0.2046 0.2519 0.0098  0.0222  0.0581  343  GLY A C   
2459  O O   . GLY A 345  ? 0.2308 0.2139 0.2673 0.0086  0.0218  0.0604  343  GLY A O   
2460  N N   . LYS A 346  ? 0.2223 0.2120 0.2494 0.0110  0.0235  0.0602  344  LYS A N   
2461  C CA  . LYS A 346  ? 0.2346 0.2318 0.2643 0.0106  0.0247  0.0660  344  LYS A CA  
2462  C C   . LYS A 346  ? 0.2431 0.2438 0.2731 0.0107  0.0258  0.0657  344  LYS A C   
2463  O O   . LYS A 346  ? 0.2516 0.2577 0.2857 0.0099  0.0265  0.0707  344  LYS A O   
2464  C CB  . LYS A 346  ? 0.2367 0.2406 0.2616 0.0120  0.0258  0.0676  344  LYS A CB  
2465  C CG  . LYS A 346  ? 0.2180 0.2194 0.2434 0.0119  0.0246  0.0687  344  LYS A CG  
2466  C CD  . LYS A 346  ? 0.2412 0.2493 0.2613 0.0134  0.0257  0.0698  344  LYS A CD  
2467  C CE  . LYS A 346  ? 0.2439 0.2504 0.2658 0.0131  0.0244  0.0723  344  LYS A CE  
2468  N NZ  . LYS A 346  ? 0.2668 0.2792 0.2830 0.0146  0.0253  0.0724  344  LYS A NZ  
2469  N N   . ARG A 347  ? 0.2196 0.2176 0.2456 0.0116  0.0260  0.0602  345  ARG A N   
2470  C CA  . ARG A 347  ? 0.2180 0.2189 0.2443 0.0118  0.0270  0.0595  345  ARG A CA  
2471  C C   . ARG A 347  ? 0.2343 0.2304 0.2663 0.0101  0.0259  0.0596  345  ARG A C   
2472  O O   . ARG A 347  ? 0.2256 0.2245 0.2591 0.0100  0.0266  0.0599  345  ARG A O   
2473  C CB  . ARG A 347  ? 0.2250 0.2255 0.2450 0.0136  0.0275  0.0538  345  ARG A CB  
2474  C CG  . ARG A 347  ? 0.2185 0.2252 0.2333 0.0155  0.0287  0.0534  345  ARG A CG  
2475  C CD  . ARG A 347  ? 0.2099 0.2144 0.2193 0.0171  0.0285  0.0473  345  ARG A CD  
2476  N NE  . ARG A 347  ? 0.2342 0.2312 0.2420 0.0167  0.0270  0.0446  345  ARG A NE  
2477  C CZ  . ARG A 347  ? 0.2138 0.2068 0.2180 0.0176  0.0263  0.0396  345  ARG A CZ  
2478  N NH1 . ARG A 347  ? 0.2228 0.2181 0.2248 0.0189  0.0268  0.0365  345  ARG A NH1 
2479  N NH2 . ARG A 347  ? 0.2075 0.1944 0.2108 0.0170  0.0251  0.0377  345  ARG A NH2 
2480  N N   . CYS A 348  ? 0.2173 0.2069 0.2527 0.0089  0.0241  0.0592  346  CYS A N   
2481  C CA  . CYS A 348  ? 0.2254 0.2100 0.2656 0.0075  0.0228  0.0579  346  CYS A CA  
2482  C C   . CYS A 348  ? 0.2108 0.1991 0.2564 0.0065  0.0233  0.0616  346  CYS A C   
2483  O O   . CYS A 348  ? 0.2279 0.2151 0.2739 0.0063  0.0233  0.0592  346  CYS A O   
2484  C CB  . CYS A 348  ? 0.2472 0.2258 0.2916 0.0064  0.0208  0.0578  346  CYS A CB  
2485  S SG  . CYS A 348  ? 0.2869 0.2590 0.3355 0.0052  0.0190  0.0540  346  CYS A SG  
2486  N N   . PRO A 349  ? 0.2253 0.2182 0.2757 0.0056  0.0236  0.0677  347  PRO A N   
2487  C CA  . PRO A 349  ? 0.2370 0.2335 0.2930 0.0044  0.0240  0.0713  347  PRO A CA  
2488  C C   . PRO A 349  ? 0.2172 0.2196 0.2692 0.0056  0.0260  0.0702  347  PRO A C   
2489  O O   . PRO A 349  ? 0.2468 0.2496 0.3019 0.0050  0.0260  0.0701  347  PRO A O   
2490  C CB  . PRO A 349  ? 0.2390 0.2400 0.3004 0.0033  0.0240  0.0784  347  PRO A CB  
2491  C CG  . PRO A 349  ? 0.2626 0.2650 0.3191 0.0044  0.0245  0.0786  347  PRO A CG  
2492  C CD  . PRO A 349  ? 0.2375 0.2330 0.2885 0.0056  0.0237  0.0718  347  PRO A CD  
2493  N N   . PHE A 350  ? 0.2287 0.2355 0.2740 0.0075  0.0275  0.0689  348  PHE A N   
2494  C CA  . PHE A 350  ? 0.2385 0.2511 0.2801 0.0090  0.0292  0.0671  348  PHE A CA  
2495  C C   . PHE A 350  ? 0.2238 0.2310 0.2624 0.0098  0.0286  0.0609  348  PHE A C   
2496  O O   . PHE A 350  ? 0.2117 0.2214 0.2506 0.0102  0.0293  0.0597  348  PHE A O   
2497  C CB  . PHE A 350  ? 0.2358 0.2550 0.2718 0.0108  0.0307  0.0674  348  PHE A CB  
2498  C CG  . PHE A 350  ? 0.2469 0.2713 0.2855 0.0100  0.0311  0.0737  348  PHE A CG  
2499  C CD1 . PHE A 350  ? 0.2631 0.2957 0.3057 0.0092  0.0323  0.0794  348  PHE A CD1 
2500  C CD2 . PHE A 350  ? 0.2363 0.2574 0.2739 0.0098  0.0301  0.0743  348  PHE A CD2 
2501  C CE1 . PHE A 350  ? 0.3046 0.3422 0.3502 0.0082  0.0325  0.0859  348  PHE A CE1 
2502  C CE2 . PHE A 350  ? 0.2737 0.2995 0.3143 0.0090  0.0302  0.0806  348  PHE A CE2 
2503  C CZ  . PHE A 350  ? 0.3004 0.3345 0.3451 0.0081  0.0314  0.0866  348  PHE A CZ  
2504  N N   . VAL A 351  ? 0.2163 0.2162 0.2524 0.0099  0.0272  0.0571  349  VAL A N   
2505  C CA  . VAL A 351  ? 0.2192 0.2136 0.2533 0.0102  0.0263  0.0519  349  VAL A CA  
2506  C C   . VAL A 351  ? 0.2280 0.2199 0.2679 0.0085  0.0253  0.0526  349  VAL A C   
2507  O O   . VAL A 351  ? 0.2125 0.2043 0.2521 0.0089  0.0254  0.0502  349  VAL A O   
2508  C CB  . VAL A 351  ? 0.1936 0.1814 0.2244 0.0103  0.0250  0.0484  349  VAL A CB  
2509  C CG1 . VAL A 351  ? 0.2053 0.1879 0.2347 0.0103  0.0238  0.0438  349  VAL A CG1 
2510  C CG2 . VAL A 351  ? 0.2376 0.2282 0.2627 0.0120  0.0258  0.0473  349  VAL A CG2 
2511  N N   . LEU A 352  ? 0.2382 0.2281 0.2838 0.0068  0.0243  0.0558  350  LEU A N   
2512  C CA  . LEU A 352  ? 0.2207 0.2085 0.2725 0.0052  0.0232  0.0564  350  LEU A CA  
2513  C C   . LEU A 352  ? 0.2259 0.2200 0.2801 0.0052  0.0246  0.0592  350  LEU A C   
2514  O O   . LEU A 352  ? 0.2321 0.2251 0.2882 0.0048  0.0241  0.0575  350  LEU A O   
2515  C CB  . LEU A 352  ? 0.2367 0.2217 0.2951 0.0034  0.0217  0.0595  350  LEU A CB  
2516  C CG  . LEU A 352  ? 0.2295 0.2076 0.2866 0.0033  0.0200  0.0559  350  LEU A CG  
2517  C CD1 . LEU A 352  ? 0.2551 0.2312 0.3193 0.0019  0.0186  0.0591  350  LEU A CD1 
2518  C CD2 . LEU A 352  ? 0.2493 0.2228 0.3057 0.0031  0.0188  0.0508  350  LEU A CD2 
2519  N N   . ASP A 353  ? 0.2294 0.2308 0.2836 0.0056  0.0263  0.0635  351  ASP A N   
2520  C CA  . ASP A 353  ? 0.2272 0.2358 0.2833 0.0057  0.0278  0.0659  351  ASP A CA  
2521  C C   . ASP A 353  ? 0.1918 0.2009 0.2432 0.0075  0.0284  0.0610  351  ASP A C   
2522  O O   . ASP A 353  ? 0.2263 0.2370 0.2803 0.0072  0.0286  0.0608  351  ASP A O   
2523  C CB  . ASP A 353  ? 0.2351 0.2526 0.2905 0.0063  0.0297  0.0706  351  ASP A CB  
2524  C CG  . ASP A 353  ? 0.2775 0.2958 0.3389 0.0043  0.0291  0.0768  351  ASP A CG  
2525  O OD1 . ASP A 353  ? 0.3064 0.3202 0.3745 0.0024  0.0274  0.0782  351  ASP A OD1 
2526  O OD2 . ASP A 353  ? 0.3286 0.3526 0.3886 0.0047  0.0301  0.0804  351  ASP A OD2 
2527  N N   . PHE A 354  ? 0.2075 0.2152 0.2523 0.0093  0.0286  0.0570  352  PHE A N   
2528  C CA  . PHE A 354  ? 0.1972 0.2048 0.2380 0.0110  0.0289  0.0523  352  PHE A CA  
2529  C C   . PHE A 354  ? 0.2014 0.2024 0.2441 0.0101  0.0272  0.0493  352  PHE A C   
2530  O O   . PHE A 354  ? 0.2125 0.2147 0.2558 0.0106  0.0273  0.0477  352  PHE A O   
2531  C CB  . PHE A 354  ? 0.2103 0.2169 0.2446 0.0128  0.0290  0.0487  352  PHE A CB  
2532  C CG  . PHE A 354  ? 0.2292 0.2335 0.2602 0.0143  0.0286  0.0436  352  PHE A CG  
2533  C CD1 . PHE A 354  ? 0.2334 0.2439 0.2631 0.0162  0.0298  0.0422  352  PHE A CD1 
2534  C CD2 . PHE A 354  ? 0.2455 0.2420 0.2751 0.0138  0.0268  0.0402  352  PHE A CD2 
2535  C CE1 . PHE A 354  ? 0.2577 0.2659 0.2853 0.0176  0.0291  0.0375  352  PHE A CE1 
2536  C CE2 . PHE A 354  ? 0.2475 0.2422 0.2748 0.0150  0.0262  0.0360  352  PHE A CE2 
2537  C CZ  . PHE A 354  ? 0.2338 0.2339 0.2603 0.0169  0.0272  0.0347  352  PHE A CZ  
2538  N N   . ILE A 355  ? 0.1870 0.1811 0.2305 0.0088  0.0255  0.0484  353  ILE A N   
2539  C CA  . ILE A 355  ? 0.1914 0.1796 0.2359 0.0080  0.0238  0.0453  353  ILE A CA  
2540  C C   . ILE A 355  ? 0.2150 0.2044 0.2659 0.0065  0.0234  0.0475  353  ILE A C   
2541  O O   . ILE A 355  ? 0.2183 0.2066 0.2698 0.0065  0.0228  0.0453  353  ILE A O   
2542  C CB  . ILE A 355  ? 0.2140 0.1958 0.2580 0.0071  0.0222  0.0437  353  ILE A CB  
2543  C CG1 . ILE A 355  ? 0.2191 0.1994 0.2566 0.0085  0.0223  0.0408  353  ILE A CG1 
2544  C CG2 . ILE A 355  ? 0.2347 0.2117 0.2809 0.0059  0.0203  0.0412  353  ILE A CG2 
2545  C CD1 . ILE A 355  ? 0.2444 0.2194 0.2812 0.0077  0.0210  0.0396  353  ILE A CD1 
2546  N N   . ILE A 356  ? 0.2220 0.2136 0.2781 0.0052  0.0236  0.0520  354  ILE A N   
2547  C CA  . ILE A 356  ? 0.2104 0.2035 0.2733 0.0037  0.0232  0.0544  354  ILE A CA  
2548  C C   . ILE A 356  ? 0.2248 0.2239 0.2872 0.0047  0.0247  0.0548  354  ILE A C   
2549  O O   . ILE A 356  ? 0.2167 0.2153 0.2818 0.0042  0.0241  0.0537  354  ILE A O   
2550  C CB  . ILE A 356  ? 0.2377 0.2325 0.3066 0.0020  0.0231  0.0598  354  ILE A CB  
2551  C CG1 . ILE A 356  ? 0.2390 0.2270 0.3094 0.0010  0.0211  0.0585  354  ILE A CG1 
2552  C CG2 . ILE A 356  ? 0.2621 0.2598 0.3385 0.0005  0.0229  0.0630  354  ILE A CG2 
2553  C CD1 . ILE A 356  ? 0.2416 0.2307 0.3173 -0.0002 0.0208  0.0635  354  ILE A CD1 
2554  N N   . ASP A 357  ? 0.2109 0.2161 0.2698 0.0063  0.0267  0.0559  355  ASP A N   
2555  C CA  . ASP A 357  ? 0.2100 0.2214 0.2684 0.0076  0.0281  0.0555  355  ASP A CA  
2556  C C   . ASP A 357  ? 0.1935 0.2013 0.2486 0.0089  0.0273  0.0502  355  ASP A C   
2557  O O   . ASP A 357  ? 0.2262 0.2360 0.2835 0.0091  0.0273  0.0495  355  ASP A O   
2558  C CB  . ASP A 357  ? 0.2425 0.2616 0.2976 0.0093  0.0303  0.0571  355  ASP A CB  
2559  C CG  . ASP A 357  ? 0.2455 0.2713 0.2998 0.0110  0.0317  0.0558  355  ASP A CG  
2560  O OD1 . ASP A 357  ? 0.2921 0.3234 0.3510 0.0102  0.0326  0.0591  355  ASP A OD1 
2561  O OD2 . ASP A 357  ? 0.2529 0.2785 0.3023 0.0132  0.0319  0.0513  355  ASP A OD2 
2562  N N   . LEU A 358  ? 0.2123 0.2149 0.2623 0.0097  0.0265  0.0466  356  LEU A N   
2563  C CA  . LEU A 358  ? 0.2072 0.2062 0.2545 0.0107  0.0254  0.0420  356  LEU A CA  
2564  C C   . LEU A 358  ? 0.1900 0.1848 0.2411 0.0091  0.0237  0.0414  356  LEU A C   
2565  O O   . LEU A 358  ? 0.2127 0.2075 0.2643 0.0096  0.0232  0.0395  356  LEU A O   
2566  C CB  . LEU A 358  ? 0.1920 0.1863 0.2339 0.0115  0.0247  0.0389  356  LEU A CB  
2567  C CG  . LEU A 358  ? 0.1887 0.1784 0.2281 0.0121  0.0232  0.0347  356  LEU A CG  
2568  C CD1 . LEU A 358  ? 0.2340 0.2275 0.2727 0.0141  0.0238  0.0329  356  LEU A CD1 
2569  C CD2 . LEU A 358  ? 0.2035 0.1886 0.2381 0.0124  0.0224  0.0324  356  LEU A CD2 
2570  N N   . ALA A 359  ? 0.2101 0.2013 0.2642 0.0071  0.0226  0.0429  357  ALA A N   
2571  C CA  . ALA A 359  ? 0.2335 0.2213 0.2917 0.0055  0.0209  0.0422  357  ALA A CA  
2572  C C   . ALA A 359  ? 0.2119 0.2044 0.2751 0.0051  0.0214  0.0444  357  ALA A C   
2573  O O   . ALA A 359  ? 0.2181 0.2095 0.2828 0.0049  0.0204  0.0426  357  ALA A O   
2574  C CB  . ALA A 359  ? 0.2378 0.2219 0.2993 0.0037  0.0196  0.0434  357  ALA A CB  
2575  N N   . ARG A 360  ? 0.2051 0.2033 0.2709 0.0051  0.0231  0.0484  358  ARG A N   
2576  C CA  . ARG A 360  ? 0.2158 0.2194 0.2863 0.0047  0.0239  0.0508  358  ARG A CA  
2577  C C   . ARG A 360  ? 0.2466 0.2532 0.3143 0.0068  0.0246  0.0480  358  ARG A C   
2578  O O   . ARG A 360  ? 0.2721 0.2792 0.3427 0.0065  0.0240  0.0473  358  ARG A O   
2579  C CB  . ARG A 360  ? 0.2525 0.2627 0.3260 0.0043  0.0257  0.0560  358  ARG A CB  
2580  C CG  . ARG A 360  ? 0.2947 0.3025 0.3733 0.0020  0.0247  0.0595  358  ARG A CG  
2581  C CD  . ARG A 360  ? 0.3736 0.3888 0.4567 0.0012  0.0262  0.0656  358  ARG A CD  
2582  N NE  . ARG A 360  ? 0.4090 0.4221 0.4961 -0.0006 0.0254  0.0692  358  ARG A NE  
2583  C CZ  . ARG A 360  ? 0.4954 0.5051 0.5898 -0.0028 0.0235  0.0710  358  ARG A CZ  
2584  N NH1 . ARG A 360  ? 0.4967 0.5056 0.5954 -0.0037 0.0225  0.0700  358  ARG A NH1 
2585  N NH2 . ARG A 360  ? 0.4883 0.4956 0.5862 -0.0041 0.0225  0.0739  358  ARG A NH2 
2586  N N   . ARG A 361  ? 0.2375 0.2462 0.2998 0.0089  0.0258  0.0463  359  ARG A N   
2587  C CA  . ARG A 361  ? 0.2346 0.2464 0.2949 0.0110  0.0264  0.0435  359  ARG A CA  
2588  C C   . ARG A 361  ? 0.2326 0.2384 0.2919 0.0111  0.0243  0.0397  359  ARG A C   
2589  O O   . ARG A 361  ? 0.2573 0.2649 0.3185 0.0118  0.0241  0.0385  359  ARG A O   
2590  C CB  . ARG A 361  ? 0.2680 0.2823 0.3229 0.0133  0.0276  0.0417  359  ARG A CB  
2591  C CG  . ARG A 361  ? 0.2966 0.3189 0.3518 0.0138  0.0299  0.0451  359  ARG A CG  
2592  C CD  . ARG A 361  ? 0.3073 0.3324 0.3571 0.0163  0.0308  0.0424  359  ARG A CD  
2593  N NE  . ARG A 361  ? 0.2930 0.3129 0.3388 0.0160  0.0301  0.0416  359  ARG A NE  
2594  C CZ  . ARG A 361  ? 0.2612 0.2769 0.3025 0.0174  0.0292  0.0375  359  ARG A CZ  
2595  N NH1 . ARG A 361  ? 0.2607 0.2757 0.3014 0.0190  0.0286  0.0336  359  ARG A NH1 
2596  N NH2 . ARG A 361  ? 0.2493 0.2617 0.2872 0.0172  0.0289  0.0373  359  ARG A NH2 
2597  N N   . SER A 362  ? 0.2189 0.2181 0.2755 0.0104  0.0228  0.0379  360  SER A N   
2598  C CA  . SER A 362  ? 0.2133 0.2074 0.2684 0.0105  0.0209  0.0346  360  SER A CA  
2599  C C   . SER A 362  ? 0.2216 0.2134 0.2811 0.0085  0.0193  0.0352  360  SER A C   
2600  O O   . SER A 362  ? 0.2494 0.2387 0.3086 0.0085  0.0178  0.0330  360  SER A O   
2601  C CB  . SER A 362  ? 0.2369 0.2256 0.2873 0.0104  0.0200  0.0327  360  SER A CB  
2602  O OG  . SER A 362  ? 0.2209 0.2068 0.2725 0.0086  0.0195  0.0342  360  SER A OG  
2603  N N   . GLY A 363  ? 0.2152 0.2077 0.2787 0.0068  0.0195  0.0381  361  GLY A N   
2604  C CA  . GLY A 363  ? 0.2457 0.2355 0.3134 0.0048  0.0177  0.0381  361  GLY A CA  
2605  C C   . GLY A 363  ? 0.2477 0.2315 0.3132 0.0039  0.0158  0.0356  361  GLY A C   
2606  O O   . GLY A 363  ? 0.2830 0.2647 0.3513 0.0026  0.0141  0.0346  361  GLY A O   
2607  N N   . ARG A 364  ? 0.2369 0.2183 0.2973 0.0047  0.0161  0.0344  362  ARG A N   
2608  C CA  . ARG A 364  ? 0.2385 0.2149 0.2965 0.0039  0.0144  0.0321  362  ARG A CA  
2609  C C   . ARG A 364  ? 0.2325 0.2077 0.2930 0.0027  0.0145  0.0337  362  ARG A C   
2610  O O   . ARG A 364  ? 0.2280 0.2051 0.2882 0.0031  0.0160  0.0360  362  ARG A O   
2611  C CB  . ARG A 364  ? 0.2632 0.2378 0.3149 0.0053  0.0147  0.0301  362  ARG A CB  
2612  C CG  . ARG A 364  ? 0.3220 0.2979 0.3713 0.0069  0.0148  0.0287  362  ARG A CG  
2613  C CD  . ARG A 364  ? 0.2305 0.2037 0.2787 0.0064  0.0128  0.0264  362  ARG A CD  
2614  N NE  . ARG A 364  ? 0.2211 0.1960 0.2692 0.0078  0.0127  0.0258  362  ARG A NE  
2615  C CZ  . ARG A 364  ? 0.2299 0.2039 0.2747 0.0092  0.0125  0.0243  362  ARG A CZ  
2616  N NH1 . ARG A 364  ? 0.2171 0.1882 0.2577 0.0093  0.0122  0.0233  362  ARG A NH1 
2617  N NH2 . ARG A 364  ? 0.2212 0.1970 0.2671 0.0106  0.0123  0.0237  362  ARG A NH2 
2618  N N   . ARG A 365  ? 0.2104 0.1828 0.2737 0.0012  0.0126  0.0324  363  ARG A N   
2619  C CA  . ARG A 365  ? 0.1901 0.1609 0.2568 0.0001  0.0122  0.0335  363  ARG A CA  
2620  C C   . ARG A 365  ? 0.2273 0.1950 0.2887 0.0006  0.0121  0.0315  363  ARG A C   
2621  O O   . ARG A 365  ? 0.2429 0.2078 0.3033 0.0001  0.0105  0.0286  363  ARG A O   
2622  C CB  . ARG A 365  ? 0.2218 0.1911 0.2941 -0.0016 0.0102  0.0324  363  ARG A CB  
2623  C CG  . ARG A 365  ? 0.2293 0.1969 0.3065 -0.0027 0.0095  0.0335  363  ARG A CG  
2624  C CD  . ARG A 365  ? 0.2889 0.2564 0.3739 -0.0043 0.0077  0.0336  363  ARG A CD  
2625  N NE  . ARG A 365  ? 0.2694 0.2353 0.3599 -0.0052 0.0069  0.0350  363  ARG A NE  
2626  C CZ  . ARG A 365  ? 0.2347 0.1974 0.3274 -0.0058 0.0049  0.0319  363  ARG A CZ  
2627  N NH1 . ARG A 365  ? 0.2837 0.2451 0.3737 -0.0057 0.0035  0.0273  363  ARG A NH1 
2628  N NH2 . ARG A 365  ? 0.2380 0.1991 0.3359 -0.0065 0.0042  0.0334  363  ARG A NH2 
2629  N N   . ILE A 366  ? 0.2040 0.1730 0.2622 0.0017  0.0138  0.0331  364  ILE A N   
2630  C CA  . ILE A 366  ? 0.2121 0.1786 0.2649 0.0025  0.0138  0.0313  364  ILE A CA  
2631  C C   . ILE A 366  ? 0.2274 0.1910 0.2826 0.0014  0.0126  0.0307  364  ILE A C   
2632  O O   . ILE A 366  ? 0.2122 0.1763 0.2726 0.0006  0.0126  0.0332  364  ILE A O   
2633  C CB  . ILE A 366  ? 0.2074 0.1764 0.2568 0.0039  0.0158  0.0332  364  ILE A CB  
2634  C CG1 . ILE A 366  ? 0.2341 0.2062 0.2814 0.0052  0.0168  0.0329  364  ILE A CG1 
2635  C CG2 . ILE A 366  ? 0.2385 0.2050 0.2828 0.0045  0.0158  0.0315  364  ILE A CG2 
2636  C CD1 . ILE A 366  ? 0.2393 0.2151 0.2840 0.0068  0.0188  0.0345  364  ILE A CD1 
2637  N N   . MET A 367  ? 0.2071 0.1678 0.2588 0.0014  0.0115  0.0274  365  MET A N   
2638  C CA  . MET A 367  ? 0.2089 0.1672 0.2626 0.0007  0.0103  0.0260  365  MET A CA  
2639  C C   . MET A 367  ? 0.2095 0.1674 0.2603 0.0015  0.0115  0.0274  365  MET A C   
2640  O O   . MET A 367  ? 0.2514 0.2091 0.2962 0.0025  0.0122  0.0264  365  MET A O   
2641  C CB  . MET A 367  ? 0.2048 0.1613 0.2558 0.0004  0.0087  0.0219  365  MET A CB  
2642  C CG  . MET A 367  ? 0.2239 0.1814 0.2766 -0.0002 0.0076  0.0206  365  MET A CG  
2643  S SD  . MET A 367  ? 0.2464 0.2033 0.2958 -0.0006 0.0058  0.0161  365  MET A SD  
2644  C CE  . MET A 367  ? 0.2895 0.2455 0.3453 -0.0017 0.0038  0.0136  365  MET A CE  
2645  N N   . VAL A 368  ? 0.1894 0.1473 0.2446 0.0010  0.0116  0.0299  366  VAL A N   
2646  C CA  . VAL A 368  ? 0.1965 0.1548 0.2495 0.0018  0.0128  0.0319  366  VAL A CA  
2647  C C   . VAL A 368  ? 0.1978 0.1530 0.2526 0.0013  0.0114  0.0303  366  VAL A C   
2648  O O   . VAL A 368  ? 0.2119 0.1661 0.2734 0.0003  0.0102  0.0311  366  VAL A O   
2649  C CB  . VAL A 368  ? 0.2218 0.1834 0.2783 0.0017  0.0140  0.0368  366  VAL A CB  
2650  C CG1 . VAL A 368  ? 0.2449 0.2073 0.2991 0.0024  0.0151  0.0389  366  VAL A CG1 
2651  C CG2 . VAL A 368  ? 0.2397 0.2050 0.2945 0.0023  0.0154  0.0380  366  VAL A CG2 
2652  N N   . ARG A 369  ? 0.1959 0.1497 0.2452 0.0021  0.0115  0.0280  367  ARG A N   
2653  C CA  . ARG A 369  ? 0.1984 0.1497 0.2491 0.0019  0.0104  0.0264  367  ARG A CA  
2654  C C   . ARG A 369  ? 0.2079 0.1599 0.2587 0.0025  0.0114  0.0297  367  ARG A C   
2655  O O   . ARG A 369  ? 0.2234 0.1767 0.2685 0.0035  0.0128  0.0304  367  ARG A O   
2656  C CB  . ARG A 369  ? 0.2049 0.1549 0.2500 0.0024  0.0099  0.0222  367  ARG A CB  
2657  C CG  . ARG A 369  ? 0.2257 0.1737 0.2727 0.0023  0.0087  0.0201  367  ARG A CG  
2658  C CD  . ARG A 369  ? 0.2377 0.1852 0.2783 0.0029  0.0088  0.0172  367  ARG A CD  
2659  N NE  . ARG A 369  ? 0.2256 0.1736 0.2639 0.0025  0.0080  0.0141  367  ARG A NE  
2660  C CZ  . ARG A 369  ? 0.2592 0.2076 0.2913 0.0028  0.0084  0.0126  367  ARG A CZ  
2661  N NH1 . ARG A 369  ? 0.2445 0.1926 0.2724 0.0036  0.0094  0.0133  367  ARG A NH1 
2662  N NH2 . ARG A 369  ? 0.2352 0.1847 0.2659 0.0023  0.0076  0.0104  367  ARG A NH2 
2663  N N   . LEU A 370  ? 0.2068 0.1581 0.2643 0.0017  0.0105  0.0318  368  LEU A N   
2664  C CA  . LEU A 370  ? 0.1998 0.1519 0.2583 0.0021  0.0111  0.0353  368  LEU A CA  
2665  C C   . LEU A 370  ? 0.2050 0.1541 0.2626 0.0024  0.0100  0.0324  368  LEU A C   
2666  O O   . LEU A 370  ? 0.2038 0.1505 0.2659 0.0019  0.0081  0.0296  368  LEU A O   
2667  C CB  . LEU A 370  ? 0.2034 0.1562 0.2705 0.0010  0.0104  0.0396  368  LEU A CB  
2668  C CG  . LEU A 370  ? 0.2207 0.1753 0.2893 0.0011  0.0111  0.0444  368  LEU A CG  
2669  C CD1 . LEU A 370  ? 0.2616 0.2207 0.3241 0.0021  0.0135  0.0471  368  LEU A CD1 
2670  C CD2 . LEU A 370  ? 0.2512 0.2061 0.3297 -0.0003 0.0099  0.0486  368  LEU A CD2 
2671  N N   . VAL A 371  ? 0.1985 0.1483 0.2504 0.0035  0.0111  0.0326  369  VAL A N   
2672  C CA  . VAL A 371  ? 0.2023 0.1498 0.2531 0.0039  0.0103  0.0302  369  VAL A CA  
2673  C C   . VAL A 371  ? 0.2121 0.1609 0.2633 0.0044  0.0110  0.0343  369  VAL A C   
2674  O O   . VAL A 371  ? 0.2242 0.1761 0.2751 0.0045  0.0123  0.0384  369  VAL A O   
2675  C CB  . VAL A 371  ? 0.1985 0.1456 0.2415 0.0047  0.0108  0.0263  369  VAL A CB  
2676  C CG1 . VAL A 371  ? 0.2265 0.1732 0.2687 0.0041  0.0102  0.0231  369  VAL A CG1 
2677  C CG2 . VAL A 371  ? 0.2179 0.1674 0.2547 0.0056  0.0127  0.0283  369  VAL A CG2 
2678  N N   . LYS A 372  ? 0.2215 0.1685 0.2731 0.0048  0.0101  0.0330  370  LYS A N   
2679  C CA  . LYS A 372  ? 0.2352 0.1837 0.2859 0.0054  0.0109  0.0367  370  LYS A CA  
2680  C C   . LYS A 372  ? 0.2300 0.1803 0.2719 0.0065  0.0125  0.0357  370  LYS A C   
2681  O O   . LYS A 372  ? 0.2726 0.2264 0.3118 0.0070  0.0140  0.0388  370  LYS A O   
2682  C CB  . LYS A 372  ? 0.2385 0.1846 0.2949 0.0053  0.0091  0.0366  370  LYS A CB  
2683  C CG  . LYS A 372  ? 0.2572 0.2024 0.3234 0.0041  0.0076  0.0391  370  LYS A CG  
2684  C CD  . LYS A 372  ? 0.2577 0.2002 0.3313 0.0040  0.0054  0.0392  370  LYS A CD  
2685  C CE  . LYS A 372  ? 0.2563 0.1974 0.3402 0.0027  0.0035  0.0406  370  LYS A CE  
2686  N NZ  . LYS A 372  ? 0.2511 0.1891 0.3432 0.0027  0.0010  0.0396  370  LYS A NZ  
2687  N N   . GLY A 373  ? 0.2180 0.1664 0.2556 0.0070  0.0122  0.0313  371  GLY A N   
2688  C CA  . GLY A 373  ? 0.2216 0.1713 0.2514 0.0079  0.0135  0.0300  371  GLY A CA  
2689  C C   . GLY A 373  ? 0.2193 0.1671 0.2462 0.0083  0.0128  0.0267  371  GLY A C   
2690  O O   . GLY A 373  ? 0.2258 0.1724 0.2559 0.0083  0.0119  0.0269  371  GLY A O   
2691  N N   . ALA A 374  ? 0.2228 0.1706 0.2439 0.0086  0.0133  0.0238  372  ALA A N   
2692  C CA  . ALA A 374  ? 0.2074 0.1536 0.2259 0.0088  0.0126  0.0204  372  ALA A CA  
2693  C C   . ALA A 374  ? 0.2427 0.1899 0.2562 0.0097  0.0133  0.0205  372  ALA A C   
2694  O O   . ALA A 374  ? 0.2590 0.2052 0.2706 0.0098  0.0128  0.0180  372  ALA A O   
2695  C CB  . ALA A 374  ? 0.2355 0.1811 0.2515 0.0082  0.0122  0.0170  372  ALA A CB  
2696  N N   . TYR A 375  ? 0.2269 0.1762 0.2383 0.0104  0.0145  0.0233  373  TYR A N   
2697  C CA  . TYR A 375  ? 0.2261 0.1767 0.2323 0.0113  0.0151  0.0229  373  TYR A CA  
2698  C C   . TYR A 375  ? 0.2136 0.1662 0.2206 0.0120  0.0155  0.0260  373  TYR A C   
2699  O O   . TYR A 375  ? 0.2321 0.1871 0.2353 0.0130  0.0163  0.0266  373  TYR A O   
2700  C CB  . TYR A 375  ? 0.2380 0.1902 0.2403 0.0118  0.0161  0.0226  373  TYR A CB  
2701  C CG  . TYR A 375  ? 0.2205 0.1712 0.2220 0.0112  0.0156  0.0201  373  TYR A CG  
2702  C CD1 . TYR A 375  ? 0.2165 0.1669 0.2214 0.0104  0.0155  0.0206  373  TYR A CD1 
2703  C CD2 . TYR A 375  ? 0.2708 0.2205 0.2685 0.0112  0.0152  0.0174  373  TYR A CD2 
2704  C CE1 . TYR A 375  ? 0.2366 0.1859 0.2406 0.0098  0.0150  0.0185  373  TYR A CE1 
2705  C CE2 . TYR A 375  ? 0.2765 0.2252 0.2736 0.0104  0.0147  0.0156  373  TYR A CE2 
2706  C CZ  . TYR A 375  ? 0.2876 0.2362 0.2878 0.0098  0.0146  0.0162  373  TYR A CZ  
2707  O OH  . TYR A 375  ? 0.3218 0.2697 0.3215 0.0091  0.0140  0.0146  373  TYR A OH  
2708  N N   . TRP A 376  ? 0.2069 0.1588 0.2192 0.0116  0.0148  0.0280  374  TRP A N   
2709  C CA  . TRP A 376  ? 0.2225 0.1769 0.2365 0.0121  0.0151  0.0321  374  TRP A CA  
2710  C C   . TRP A 376  ? 0.2328 0.1883 0.2424 0.0131  0.0153  0.0315  374  TRP A C   
2711  O O   . TRP A 376  ? 0.2469 0.2061 0.2538 0.0139  0.0163  0.0337  374  TRP A O   
2712  C CB  . TRP A 376  ? 0.2422 0.1950 0.2635 0.0114  0.0139  0.0342  374  TRP A CB  
2713  C CG  . TRP A 376  ? 0.2495 0.2052 0.2732 0.0117  0.0141  0.0391  374  TRP A CG  
2714  C CD1 . TRP A 376  ? 0.2351 0.1945 0.2604 0.0116  0.0149  0.0437  374  TRP A CD1 
2715  C CD2 . TRP A 376  ? 0.2419 0.1977 0.2664 0.0123  0.0134  0.0404  374  TRP A CD2 
2716  N NE1 . TRP A 376  ? 0.2485 0.2105 0.2756 0.0119  0.0148  0.0479  374  TRP A NE1 
2717  C CE2 . TRP A 376  ? 0.2435 0.2032 0.2701 0.0123  0.0138  0.0459  374  TRP A CE2 
2718  C CE3 . TRP A 376  ? 0.2651 0.2185 0.2888 0.0127  0.0125  0.0374  374  TRP A CE3 
2719  C CZ2 . TRP A 376  ? 0.2787 0.2397 0.3068 0.0127  0.0132  0.0488  374  TRP A CZ2 
2720  C CZ3 . TRP A 376  ? 0.3001 0.2545 0.3254 0.0132  0.0119  0.0399  374  TRP A CZ3 
2721  C CH2 . TRP A 376  ? 0.2941 0.2523 0.3216 0.0132  0.0122  0.0456  374  TRP A CH2 
2722  N N   . ASP A 377  ? 0.2464 0.1993 0.2555 0.0131  0.0144  0.0285  375  ASP A N   
2723  C CA  . ASP A 377  ? 0.2688 0.2226 0.2742 0.0140  0.0145  0.0279  375  ASP A CA  
2724  C C   . ASP A 377  ? 0.2520 0.2081 0.2514 0.0147  0.0155  0.0268  375  ASP A C   
2725  O O   . ASP A 377  ? 0.2422 0.2011 0.2389 0.0156  0.0160  0.0281  375  ASP A O   
2726  C CB  . ASP A 377  ? 0.3624 0.3135 0.3673 0.0137  0.0135  0.0240  375  ASP A CB  
2727  C CG  . ASP A 377  ? 0.5066 0.4556 0.5174 0.0134  0.0123  0.0239  375  ASP A CG  
2728  O OD1 . ASP A 377  ? 0.5299 0.4796 0.5449 0.0135  0.0119  0.0274  375  ASP A OD1 
2729  O OD2 . ASP A 377  ? 0.5517 0.4987 0.5631 0.0130  0.0115  0.0203  375  ASP A OD2 
2730  N N   . ALA A 378  ? 0.2275 0.1825 0.2249 0.0143  0.0157  0.0244  376  ALA A N   
2731  C CA  . ALA A 378  ? 0.2381 0.1945 0.2305 0.0150  0.0164  0.0228  376  ALA A CA  
2732  C C   . ALA A 378  ? 0.2187 0.1792 0.2104 0.0159  0.0175  0.0254  376  ALA A C   
2733  O O   . ALA A 378  ? 0.2237 0.1869 0.2118 0.0169  0.0179  0.0247  376  ALA A O   
2734  C CB  . ALA A 378  ? 0.2324 0.1866 0.2238 0.0143  0.0161  0.0200  376  ALA A CB  
2735  N N   . GLU A 379  ? 0.2174 0.1790 0.2129 0.0154  0.0178  0.0282  377  GLU A N   
2736  C CA  . GLU A 379  ? 0.2231 0.1897 0.2181 0.0162  0.0190  0.0310  377  GLU A CA  
2737  C C   . GLU A 379  ? 0.2186 0.1890 0.2129 0.0170  0.0193  0.0337  377  GLU A C   
2738  O O   . GLU A 379  ? 0.2410 0.2163 0.2323 0.0181  0.0202  0.0344  377  GLU A O   
2739  C CB  . GLU A 379  ? 0.2227 0.1897 0.2223 0.0153  0.0193  0.0339  377  GLU A CB  
2740  C CG  . GLU A 379  ? 0.2434 0.2074 0.2440 0.0145  0.0190  0.0314  377  GLU A CG  
2741  C CD  . GLU A 379  ? 0.2417 0.2072 0.2385 0.0153  0.0197  0.0292  377  GLU A CD  
2742  O OE1 . GLU A 379  ? 0.2466 0.2159 0.2402 0.0166  0.0204  0.0292  377  GLU A OE1 
2743  O OE2 . GLU A 379  ? 0.2479 0.2108 0.2452 0.0147  0.0193  0.0273  377  GLU A OE2 
2744  N N   . ILE A 380  ? 0.2191 0.1877 0.2162 0.0165  0.0184  0.0351  378  ILE A N   
2745  C CA  . ILE A 380  ? 0.2282 0.2004 0.2248 0.0172  0.0185  0.0380  378  ILE A CA  
2746  C C   . ILE A 380  ? 0.2345 0.2079 0.2255 0.0184  0.0186  0.0350  378  ILE A C   
2747  O O   . ILE A 380  ? 0.2373 0.2160 0.2256 0.0195  0.0192  0.0362  378  ILE A O   
2748  C CB  . ILE A 380  ? 0.2332 0.2026 0.2346 0.0165  0.0172  0.0399  378  ILE A CB  
2749  C CG1 . ILE A 380  ? 0.2397 0.2075 0.2476 0.0153  0.0168  0.0426  378  ILE A CG1 
2750  C CG2 . ILE A 380  ? 0.2616 0.2348 0.2627 0.0172  0.0171  0.0432  378  ILE A CG2 
2751  C CD1 . ILE A 380  ? 0.2512 0.2243 0.2609 0.0152  0.0178  0.0476  378  ILE A CD1 
2752  N N   . LYS A 381  ? 0.2130 0.1820 0.2023 0.0181  0.0178  0.0309  379  LYS A N   
2753  C CA  . LYS A 381  ? 0.2161 0.1858 0.2008 0.0190  0.0177  0.0280  379  LYS A CA  
2754  C C   . LYS A 381  ? 0.2272 0.2003 0.2084 0.0201  0.0185  0.0264  379  LYS A C   
2755  O O   . LYS A 381  ? 0.2220 0.1990 0.2002 0.0213  0.0187  0.0259  379  LYS A O   
2756  C CB  . LYS A 381  ? 0.2212 0.1858 0.2053 0.0183  0.0167  0.0242  379  LYS A CB  
2757  C CG  . LYS A 381  ? 0.2322 0.1973 0.2121 0.0190  0.0164  0.0213  379  LYS A CG  
2758  C CD  . LYS A 381  ? 0.2460 0.2068 0.2258 0.0181  0.0155  0.0183  379  LYS A CD  
2759  C CE  . LYS A 381  ? 0.2791 0.2404 0.2553 0.0187  0.0150  0.0157  379  LYS A CE  
2760  N NZ  . LYS A 381  ? 0.2404 0.1983 0.2167 0.0177  0.0141  0.0133  379  LYS A NZ  
2761  N N   . ARG A 382  ? 0.2254 0.1973 0.2073 0.0197  0.0188  0.0254  380  ARG A N   
2762  C CA  . ARG A 382  ? 0.2168 0.1914 0.1959 0.0207  0.0194  0.0234  380  ARG A CA  
2763  C C   . ARG A 382  ? 0.2312 0.2128 0.2095 0.0220  0.0205  0.0258  380  ARG A C   
2764  O O   . ARG A 382  ? 0.2465 0.2319 0.2217 0.0234  0.0206  0.0238  380  ARG A O   
2765  C CB  . ARG A 382  ? 0.2388 0.2109 0.2195 0.0201  0.0195  0.0223  380  ARG A CB  
2766  C CG  . ARG A 382  ? 0.3080 0.2824 0.2865 0.0212  0.0197  0.0197  380  ARG A CG  
2767  C CD  . ARG A 382  ? 0.4126 0.3850 0.3884 0.0217  0.0187  0.0158  380  ARG A CD  
2768  N NE  . ARG A 382  ? 0.5499 0.5249 0.5244 0.0231  0.0188  0.0132  380  ARG A NE  
2769  C CZ  . ARG A 382  ? 0.6491 0.6221 0.6246 0.0230  0.0185  0.0116  380  ARG A CZ  
2770  N NH1 . ARG A 382  ? 0.6211 0.5896 0.5986 0.0214  0.0181  0.0122  380  ARG A NH1 
2771  N NH2 . ARG A 382  ? 0.6312 0.6072 0.6061 0.0245  0.0185  0.0091  380  ARG A NH2 
2772  N N   . ALA A 383  ? 0.2152 0.1992 0.1966 0.0214  0.0211  0.0302  381  ALA A N   
2773  C CA  . ALA A 383  ? 0.2274 0.2190 0.2081 0.0225  0.0222  0.0332  381  ALA A CA  
2774  C C   . ALA A 383  ? 0.2339 0.2292 0.2119 0.0234  0.0220  0.0336  381  ALA A C   
2775  O O   . ALA A 383  ? 0.2445 0.2464 0.2196 0.0249  0.0227  0.0332  381  ALA A O   
2776  C CB  . ALA A 383  ? 0.2528 0.2460 0.2380 0.0214  0.0227  0.0385  381  ALA A CB  
2777  N N   . GLN A 384  ? 0.2262 0.2177 0.2052 0.0228  0.0210  0.0341  382  GLN A N   
2778  C CA  . GLN A 384  ? 0.2328 0.2274 0.2093 0.0237  0.0206  0.0344  382  GLN A CA  
2779  C C   . GLN A 384  ? 0.2545 0.2496 0.2266 0.0249  0.0203  0.0292  382  GLN A C   
2780  O O   . GLN A 384  ? 0.2659 0.2671 0.2350 0.0264  0.0206  0.0288  382  GLN A O   
2781  C CB  . GLN A 384  ? 0.2189 0.2088 0.1980 0.0227  0.0195  0.0357  382  GLN A CB  
2782  C CG  . GLN A 384  ? 0.2387 0.2291 0.2228 0.0217  0.0194  0.0411  382  GLN A CG  
2783  C CD  . GLN A 384  ? 0.2744 0.2609 0.2613 0.0211  0.0181  0.0421  382  GLN A CD  
2784  O OE1 . GLN A 384  ? 0.2835 0.2660 0.2688 0.0211  0.0174  0.0383  382  GLN A OE1 
2785  N NE2 . GLN A 384  ? 0.2575 0.2453 0.2489 0.0205  0.0178  0.0471  382  GLN A NE2 
2786  N N   . LEU A 385  ? 0.2356 0.2246 0.2073 0.0244  0.0196  0.0252  383  LEU A N   
2787  C CA  . LEU A 385  ? 0.2435 0.2324 0.2120 0.0255  0.0190  0.0204  383  LEU A CA  
2788  C C   . LEU A 385  ? 0.2646 0.2593 0.2313 0.0270  0.0197  0.0189  383  LEU A C   
2789  O O   . LEU A 385  ? 0.2769 0.2752 0.2409 0.0285  0.0194  0.0160  383  LEU A O   
2790  C CB  . LEU A 385  ? 0.2345 0.2163 0.2037 0.0244  0.0181  0.0173  383  LEU A CB  
2791  C CG  . LEU A 385  ? 0.2827 0.2592 0.2530 0.0231  0.0172  0.0170  383  LEU A CG  
2792  C CD1 . LEU A 385  ? 0.3000 0.2710 0.2709 0.0220  0.0165  0.0144  383  LEU A CD1 
2793  C CD2 . LEU A 385  ? 0.3189 0.2966 0.2868 0.0238  0.0164  0.0154  383  LEU A CD2 
2794  N N   . ASP A 386  ? 0.2494 0.2455 0.2178 0.0268  0.0207  0.0204  384  ASP A N   
2795  C CA  . ASP A 386  ? 0.2565 0.2581 0.2237 0.0284  0.0214  0.0185  384  ASP A CA  
2796  C C   . ASP A 386  ? 0.2630 0.2740 0.2290 0.0296  0.0226  0.0214  384  ASP A C   
2797  O O   . ASP A 386  ? 0.2587 0.2758 0.2234 0.0312  0.0233  0.0197  384  ASP A O   
2798  C CB  . ASP A 386  ? 0.2764 0.2753 0.2460 0.0277  0.0219  0.0185  384  ASP A CB  
2799  C CG  . ASP A 386  ? 0.3768 0.3682 0.3470 0.0269  0.0206  0.0149  384  ASP A CG  
2800  O OD1 . ASP A 386  ? 0.3663 0.3550 0.3349 0.0271  0.0195  0.0120  384  ASP A OD1 
2801  O OD2 . ASP A 386  ? 0.3798 0.3681 0.3521 0.0261  0.0208  0.0151  384  ASP A OD2 
2802  N N   . GLY A 387  ? 0.2469 0.2595 0.2134 0.0290  0.0227  0.0258  385  GLY A N   
2803  C CA  . GLY A 387  ? 0.2449 0.2671 0.2102 0.0300  0.0237  0.0291  385  GLY A CA  
2804  C C   . GLY A 387  ? 0.2547 0.2822 0.2217 0.0300  0.0251  0.0321  385  GLY A C   
2805  O O   . GLY A 387  ? 0.2628 0.2997 0.2279 0.0314  0.0261  0.0324  385  GLY A O   
2806  N N   . LEU A 388  ? 0.2610 0.2834 0.2317 0.0283  0.0253  0.0343  386  LEU A N   
2807  C CA  . LEU A 388  ? 0.2830 0.3102 0.2556 0.0283  0.0266  0.0368  386  LEU A CA  
2808  C C   . LEU A 388  ? 0.2893 0.3217 0.2645 0.0273  0.0274  0.0440  386  LEU A C   
2809  O O   . LEU A 388  ? 0.2853 0.3166 0.2615 0.0266  0.0266  0.0471  386  LEU A O   
2810  C CB  . LEU A 388  ? 0.2464 0.2662 0.2218 0.0271  0.0264  0.0353  386  LEU A CB  
2811  C CG  . LEU A 388  ? 0.2812 0.2965 0.2544 0.0280  0.0256  0.0287  386  LEU A CG  
2812  C CD1 . LEU A 388  ? 0.2909 0.2991 0.2667 0.0268  0.0252  0.0274  386  LEU A CD1 
2813  C CD2 . LEU A 388  ? 0.2777 0.3005 0.2480 0.0303  0.0262  0.0252  386  LEU A CD2 
2814  N N   . ALA A 389  ? 0.2986 0.3375 0.2753 0.0274  0.0287  0.0468  387  ALA A N   
2815  C CA  . ALA A 389  ? 0.3153 0.3614 0.2942 0.0266  0.0295  0.0540  387  ALA A CA  
2816  C C   . ALA A 389  ? 0.3211 0.3605 0.3054 0.0243  0.0285  0.0588  387  ALA A C   
2817  O O   . ALA A 389  ? 0.3210 0.3637 0.3073 0.0236  0.0283  0.0644  387  ALA A O   
2818  C CB  . ALA A 389  ? 0.3308 0.3853 0.3106 0.0270  0.0311  0.0559  387  ALA A CB  
2819  N N   . ASP A 390  ? 0.2598 0.2900 0.2469 0.0232  0.0278  0.0567  388  ASP A N   
2820  C CA  . ASP A 390  ? 0.2752 0.2994 0.2682 0.0211  0.0268  0.0607  388  ASP A CA  
2821  C C   . ASP A 390  ? 0.2456 0.2599 0.2394 0.0205  0.0259  0.0559  388  ASP A C   
2822  O O   . ASP A 390  ? 0.2576 0.2701 0.2476 0.0215  0.0261  0.0504  388  ASP A O   
2823  C CB  . ASP A 390  ? 0.2742 0.3037 0.2719 0.0200  0.0277  0.0669  388  ASP A CB  
2824  C CG  . ASP A 390  ? 0.3084 0.3347 0.3126 0.0181  0.0264  0.0727  388  ASP A CG  
2825  O OD1 . ASP A 390  ? 0.3135 0.3309 0.3201 0.0173  0.0250  0.0708  388  ASP A OD1 
2826  O OD2 . ASP A 390  ? 0.3529 0.3860 0.3602 0.0174  0.0269  0.0793  388  ASP A OD2 
2827  N N   . PHE A 391  ? 0.2399 0.2481 0.2388 0.0188  0.0249  0.0579  389  PHE A N   
2828  C CA  . PHE A 391  ? 0.2263 0.2259 0.2264 0.0181  0.0240  0.0538  389  PHE A CA  
2829  C C   . PHE A 391  ? 0.2609 0.2604 0.2637 0.0174  0.0246  0.0541  389  PHE A C   
2830  O O   . PHE A 391  ? 0.2488 0.2535 0.2546 0.0169  0.0254  0.0588  389  PHE A O   
2831  C CB  . PHE A 391  ? 0.2407 0.2341 0.2453 0.0168  0.0224  0.0552  389  PHE A CB  
2832  C CG  . PHE A 391  ? 0.2400 0.2334 0.2425 0.0174  0.0217  0.0551  389  PHE A CG  
2833  C CD1 . PHE A 391  ? 0.2544 0.2447 0.2524 0.0182  0.0213  0.0498  389  PHE A CD1 
2834  C CD2 . PHE A 391  ? 0.2524 0.2497 0.2576 0.0172  0.0214  0.0605  389  PHE A CD2 
2835  C CE1 . PHE A 391  ? 0.2694 0.2599 0.2653 0.0189  0.0207  0.0495  389  PHE A CE1 
2836  C CE2 . PHE A 391  ? 0.2601 0.2577 0.2632 0.0179  0.0207  0.0603  389  PHE A CE2 
2837  C CZ  . PHE A 391  ? 0.2520 0.2462 0.2504 0.0187  0.0204  0.0547  389  PHE A CZ  
2838  N N   . PRO A 392  ? 0.2268 0.2209 0.2285 0.0173  0.0243  0.0494  390  PRO A N   
2839  C CA  . PRO A 392  ? 0.2264 0.2197 0.2311 0.0165  0.0246  0.0496  390  PRO A CA  
2840  C C   . PRO A 392  ? 0.2104 0.1980 0.2210 0.0147  0.0234  0.0511  390  PRO A C   
2841  O O   . PRO A 392  ? 0.2580 0.2440 0.2714 0.0139  0.0234  0.0509  390  PRO A O   
2842  C CB  . PRO A 392  ? 0.2146 0.2048 0.2151 0.0174  0.0245  0.0437  390  PRO A CB  
2843  C CG  . PRO A 392  ? 0.2096 0.1948 0.2077 0.0175  0.0234  0.0407  390  PRO A CG  
2844  C CD  . PRO A 392  ? 0.2301 0.2191 0.2279 0.0179  0.0235  0.0440  390  PRO A CD  
2845  N N   . VAL A 393  ? 0.2224 0.2070 0.2353 0.0141  0.0222  0.0524  391  VAL A N   
2846  C CA  . VAL A 393  ? 0.2126 0.1919 0.2318 0.0126  0.0207  0.0535  391  VAL A CA  
2847  C C   . VAL A 393  ? 0.2392 0.2208 0.2629 0.0121  0.0202  0.0589  391  VAL A C   
2848  O O   . VAL A 393  ? 0.2549 0.2409 0.2757 0.0129  0.0207  0.0609  391  VAL A O   
2849  C CB  . VAL A 393  ? 0.2200 0.1924 0.2381 0.0124  0.0194  0.0485  391  VAL A CB  
2850  C CG1 . VAL A 393  ? 0.2379 0.2082 0.2525 0.0127  0.0197  0.0437  391  VAL A CG1 
2851  C CG2 . VAL A 393  ? 0.2381 0.2106 0.2525 0.0134  0.0192  0.0473  391  VAL A CG2 
2852  N N   . PHE A 394  ? 0.2362 0.2147 0.2672 0.0106  0.0189  0.0613  392  PHE A N   
2853  C CA  . PHE A 394  ? 0.2303 0.2097 0.2667 0.0100  0.0179  0.0663  392  PHE A CA  
2854  C C   . PHE A 394  ? 0.2256 0.2014 0.2605 0.0107  0.0167  0.0638  392  PHE A C   
2855  O O   . PHE A 394  ? 0.2594 0.2310 0.2905 0.0112  0.0165  0.0582  392  PHE A O   
2856  C CB  . PHE A 394  ? 0.2442 0.2207 0.2897 0.0084  0.0164  0.0690  392  PHE A CB  
2857  C CG  . PHE A 394  ? 0.2380 0.2186 0.2855 0.0076  0.0175  0.0719  392  PHE A CG  
2858  C CD1 . PHE A 394  ? 0.2735 0.2619 0.3206 0.0077  0.0189  0.0776  392  PHE A CD1 
2859  C CD2 . PHE A 394  ? 0.2293 0.2065 0.2784 0.0070  0.0173  0.0688  392  PHE A CD2 
2860  C CE1 . PHE A 394  ? 0.2498 0.2426 0.2985 0.0071  0.0200  0.0803  392  PHE A CE1 
2861  C CE2 . PHE A 394  ? 0.2382 0.2195 0.2891 0.0064  0.0184  0.0715  392  PHE A CE2 
2862  C CZ  . PHE A 394  ? 0.2469 0.2360 0.2977 0.0064  0.0198  0.0772  392  PHE A CZ  
2863  N N   . THR A 395  ? 0.2430 0.2209 0.2809 0.0106  0.0160  0.0684  393  THR A N   
2864  C CA  . THR A 395  ? 0.2788 0.2538 0.3160 0.0112  0.0149  0.0665  393  THR A CA  
2865  C C   . THR A 395  ? 0.2682 0.2389 0.3143 0.0103  0.0126  0.0684  393  THR A C   
2866  O O   . THR A 395  ? 0.2702 0.2376 0.3165 0.0108  0.0114  0.0661  393  THR A O   
2867  C CB  . THR A 395  ? 0.2611 0.2420 0.2937 0.0123  0.0157  0.0694  393  THR A CB  
2868  O OG1 . THR A 395  ? 0.2792 0.2656 0.3165 0.0116  0.0158  0.0768  393  THR A OG1 
2869  C CG2 . THR A 395  ? 0.2805 0.2652 0.3044 0.0135  0.0177  0.0661  393  THR A CG2 
2870  N N   . ARG A 396  ? 0.2660 0.2366 0.3197 0.0090  0.0118  0.0724  394  ARG A N   
2871  C CA  . ARG A 396  ? 0.2783 0.2439 0.3415 0.0081  0.0093  0.0732  394  ARG A CA  
2872  C C   . ARG A 396  ? 0.2662 0.2272 0.3326 0.0073  0.0087  0.0691  394  ARG A C   
2873  O O   . ARG A 396  ? 0.2714 0.2344 0.3372 0.0067  0.0098  0.0700  394  ARG A O   
2874  C CB  . ARG A 396  ? 0.2928 0.2617 0.3639 0.0070  0.0084  0.0814  394  ARG A CB  
2875  C CG  . ARG A 396  ? 0.3169 0.2909 0.3857 0.0076  0.0088  0.0860  394  ARG A CG  
2876  C CD  . ARG A 396  ? 0.3737 0.3503 0.4518 0.0063  0.0073  0.0944  394  ARG A CD  
2877  N NE  . ARG A 396  ? 0.3679 0.3511 0.4428 0.0069  0.0080  0.0995  394  ARG A NE  
2878  C CZ  . ARG A 396  ? 0.4566 0.4398 0.5372 0.0067  0.0061  0.1039  394  ARG A CZ  
2879  N NH1 . ARG A 396  ? 0.4423 0.4193 0.5328 0.0060  0.0033  0.1042  394  ARG A NH1 
2880  N NH2 . ARG A 396  ? 0.3749 0.3647 0.4512 0.0074  0.0069  0.1080  394  ARG A NH2 
2881  N N   . LYS A 397  ? 0.2847 0.2400 0.3542 0.0075  0.0069  0.0644  395  LYS A N   
2882  C CA  . LYS A 397  ? 0.2825 0.2338 0.3548 0.0069  0.0062  0.0598  395  LYS A CA  
2883  C C   . LYS A 397  ? 0.2882 0.2398 0.3690 0.0054  0.0053  0.0640  395  LYS A C   
2884  O O   . LYS A 397  ? 0.2566 0.2078 0.3372 0.0048  0.0058  0.0621  395  LYS A O   
2885  C CB  . LYS A 397  ? 0.2863 0.2325 0.3618 0.0074  0.0041  0.0544  395  LYS A CB  
2886  C CG  . LYS A 397  ? 0.3298 0.2728 0.4047 0.0072  0.0038  0.0481  395  LYS A CG  
2887  C CD  . LYS A 397  ? 0.2835 0.2238 0.3689 0.0061  0.0016  0.0483  395  LYS A CD  
2888  C CE  . LYS A 397  ? 0.2955 0.2336 0.3800 0.0060  0.0013  0.0421  395  LYS A CE  
2889  N NZ  . LYS A 397  ? 0.3282 0.2636 0.4234 0.0051  -0.0012 0.0415  395  LYS A NZ  
2890  N N   . ILE A 398  ? 0.2525 0.2051 0.3411 0.0047  0.0039  0.0701  396  ILE A N   
2891  C CA  . ILE A 398  ? 0.2766 0.2294 0.3744 0.0031  0.0028  0.0745  396  ILE A CA  
2892  C C   . ILE A 398  ? 0.2434 0.2017 0.3371 0.0025  0.0052  0.0780  396  ILE A C   
2893  O O   . ILE A 398  ? 0.2836 0.2417 0.3824 0.0013  0.0048  0.0793  396  ILE A O   
2894  C CB  . ILE A 398  ? 0.3132 0.2660 0.4206 0.0024  0.0007  0.0808  396  ILE A CB  
2895  C CG1 . ILE A 398  ? 0.3310 0.2822 0.4501 0.0007  -0.0013 0.0841  396  ILE A CG1 
2896  C CG2 . ILE A 398  ? 0.3000 0.2595 0.4034 0.0026  0.0023  0.0876  396  ILE A CG2 
2897  C CD1 . ILE A 398  ? 0.3898 0.3388 0.5206 0.0000  -0.0044 0.0885  396  ILE A CD1 
2898  N N   . HIS A 399  ? 0.2746 0.2380 0.3592 0.0035  0.0076  0.0791  397  HIS A N   
2899  C CA  . HIS A 399  ? 0.2709 0.2399 0.3510 0.0033  0.0099  0.0815  397  HIS A CA  
2900  C C   . HIS A 399  ? 0.2304 0.1967 0.3070 0.0034  0.0106  0.0755  397  HIS A C   
2901  O O   . HIS A 399  ? 0.2630 0.2314 0.3418 0.0025  0.0112  0.0772  397  HIS A O   
2902  C CB  . HIS A 399  ? 0.2792 0.2541 0.3502 0.0046  0.0121  0.0827  397  HIS A CB  
2903  C CG  . HIS A 399  ? 0.2544 0.2337 0.3285 0.0044  0.0117  0.0896  397  HIS A CG  
2904  N ND1 . HIS A 399  ? 0.2755 0.2601 0.3423 0.0056  0.0132  0.0908  397  HIS A ND1 
2905  C CD2 . HIS A 399  ? 0.3470 0.3262 0.4308 0.0031  0.0098  0.0957  397  HIS A CD2 
2906  C CE1 . HIS A 399  ? 0.2986 0.2866 0.3703 0.0051  0.0123  0.0976  397  HIS A CE1 
2907  N NE2 . HIS A 399  ? 0.3060 0.2907 0.3881 0.0035  0.0102  0.1008  397  HIS A NE2 
2908  N N   . THR A 400  ? 0.2594 0.2216 0.3309 0.0044  0.0105  0.0687  398  THR A N   
2909  C CA  . THR A 400  ? 0.2390 0.1987 0.3076 0.0044  0.0108  0.0632  398  THR A CA  
2910  C C   . THR A 400  ? 0.2481 0.2044 0.3257 0.0031  0.0089  0.0629  398  THR A C   
2911  O O   . THR A 400  ? 0.2438 0.2005 0.3214 0.0025  0.0095  0.0618  398  THR A O   
2912  C CB  . THR A 400  ? 0.2387 0.1949 0.3012 0.0056  0.0107  0.0567  398  THR A CB  
2913  O OG1 . THR A 400  ? 0.2391 0.1987 0.2931 0.0068  0.0125  0.0568  398  THR A OG1 
2914  C CG2 . THR A 400  ? 0.2343 0.1876 0.2949 0.0054  0.0106  0.0510  398  THR A CG2 
2915  N N   . ASP A 401  ? 0.2423 0.1953 0.3282 0.0025  0.0066  0.0639  399  ASP A N   
2916  C CA  . ASP A 401  ? 0.2531 0.2029 0.3485 0.0013  0.0044  0.0633  399  ASP A CA  
2917  C C   . ASP A 401  ? 0.2400 0.1934 0.3403 -0.0001 0.0049  0.0694  399  ASP A C   
2918  O O   . ASP A 401  ? 0.2576 0.2100 0.3610 -0.0010 0.0045  0.0680  399  ASP A O   
2919  C CB  . ASP A 401  ? 0.2865 0.2322 0.3906 0.0011  0.0016  0.0632  399  ASP A CB  
2920  C CG  . ASP A 401  ? 0.3240 0.2660 0.4247 0.0024  0.0008  0.0561  399  ASP A CG  
2921  O OD1 . ASP A 401  ? 0.3161 0.2576 0.4098 0.0029  0.0019  0.0506  399  ASP A OD1 
2922  O OD2 . ASP A 401  ? 0.3299 0.2697 0.4351 0.0028  -0.0009 0.0561  399  ASP A OD2 
2923  N N   . VAL A 402  ? 0.2509 0.2089 0.3521 -0.0004 0.0057  0.0764  400  VAL A N   
2924  C CA  . VAL A 402  ? 0.2589 0.2216 0.3645 -0.0018 0.0064  0.0828  400  VAL A CA  
2925  C C   . VAL A 402  ? 0.2467 0.2130 0.3447 -0.0014 0.0089  0.0810  400  VAL A C   
2926  O O   . VAL A 402  ? 0.2518 0.2192 0.3538 -0.0025 0.0090  0.0823  400  VAL A O   
2927  C CB  . VAL A 402  ? 0.2635 0.2316 0.3710 -0.0022 0.0068  0.0909  400  VAL A CB  
2928  C CG1 . VAL A 402  ? 0.2521 0.2266 0.3628 -0.0036 0.0080  0.0976  400  VAL A CG1 
2929  C CG2 . VAL A 402  ? 0.3075 0.2716 0.4245 -0.0028 0.0039  0.0932  400  VAL A CG2 
2930  N N   . SER A 403  ? 0.2495 0.2178 0.3370 0.0002  0.0110  0.0780  401  SER A N   
2931  C CA  . SER A 403  ? 0.2275 0.1985 0.3078 0.0008  0.0131  0.0755  401  SER A CA  
2932  C C   . SER A 403  ? 0.2656 0.2321 0.3479 0.0003  0.0121  0.0704  401  SER A C   
2933  O O   . SER A 403  ? 0.2409 0.2095 0.3239 -0.0003 0.0129  0.0711  401  SER A O   
2934  C CB  . SER A 403  ? 0.2487 0.2209 0.3185 0.0027  0.0147  0.0719  401  SER A CB  
2935  O OG  . SER A 403  ? 0.2497 0.2239 0.3133 0.0034  0.0165  0.0689  401  SER A OG  
2936  N N   . TYR A 404  ? 0.2487 0.2092 0.3320 0.0005  0.0103  0.0653  402  TYR A N   
2937  C CA  . TYR A 404  ? 0.2453 0.2020 0.3302 0.0001  0.0093  0.0601  402  TYR A CA  
2938  C C   . TYR A 404  ? 0.2263 0.1829 0.3208 -0.0016 0.0080  0.0632  402  TYR A C   
2939  O O   . TYR A 404  ? 0.2322 0.1896 0.3265 -0.0020 0.0084  0.0619  402  TYR A O   
2940  C CB  . TYR A 404  ? 0.2288 0.1801 0.3140 0.0006  0.0074  0.0545  402  TYR A CB  
2941  C CG  . TYR A 404  ? 0.2401 0.1884 0.3243 0.0006  0.0066  0.0483  402  TYR A CG  
2942  C CD1 . TYR A 404  ? 0.2236 0.1699 0.3162 -0.0006 0.0047  0.0475  402  TYR A CD1 
2943  C CD2 . TYR A 404  ? 0.2251 0.1729 0.3006 0.0016  0.0076  0.0434  402  TYR A CD2 
2944  C CE1 . TYR A 404  ? 0.2290 0.1734 0.3206 -0.0006 0.0039  0.0418  402  TYR A CE1 
2945  C CE2 . TYR A 404  ? 0.2247 0.1705 0.2994 0.0015  0.0068  0.0382  402  TYR A CE2 
2946  C CZ  . TYR A 404  ? 0.2194 0.1637 0.3019 0.0004  0.0050  0.0373  402  TYR A CZ  
2947  O OH  . TYR A 404  ? 0.2481 0.1912 0.3297 0.0003  0.0041  0.0321  402  TYR A OH  
2948  N N   . ILE A 405  ? 0.2495 0.2054 0.3530 -0.0025 0.0062  0.0675  403  ILE A N   
2949  C CA  . ILE A 405  ? 0.2472 0.2027 0.3610 -0.0043 0.0046  0.0704  403  ILE A CA  
2950  C C   . ILE A 405  ? 0.2286 0.1902 0.3419 -0.0050 0.0066  0.0759  403  ILE A C   
2951  O O   . ILE A 405  ? 0.2625 0.2243 0.3798 -0.0061 0.0063  0.0759  403  ILE A O   
2952  C CB  . ILE A 405  ? 0.2661 0.2191 0.3903 -0.0052 0.0020  0.0739  403  ILE A CB  
2953  C CG1 . ILE A 405  ? 0.3120 0.2591 0.4368 -0.0042 0.0000  0.0672  403  ILE A CG1 
2954  C CG2 . ILE A 405  ? 0.2916 0.2443 0.4273 -0.0071 0.0002  0.0774  403  ILE A CG2 
2955  C CD1 . ILE A 405  ? 0.3327 0.2774 0.4659 -0.0045 -0.0024 0.0699  403  ILE A CD1 
2956  N N   . ALA A 406  ? 0.2528 0.2198 0.3609 -0.0045 0.0088  0.0804  404  ALA A N   
2957  C CA  . ALA A 406  ? 0.2555 0.2295 0.3623 -0.0049 0.0109  0.0852  404  ALA A CA  
2958  C C   . ALA A 406  ? 0.2391 0.2137 0.3393 -0.0041 0.0125  0.0803  404  ALA A C   
2959  O O   . ALA A 406  ? 0.2614 0.2391 0.3643 -0.0050 0.0131  0.0822  404  ALA A O   
2960  C CB  . ALA A 406  ? 0.2752 0.2556 0.3765 -0.0040 0.0130  0.0896  404  ALA A CB  
2961  N N   . CYS A 407  ? 0.2359 0.2079 0.3278 -0.0025 0.0130  0.0741  405  CYS A N   
2962  C CA  . CYS A 407  ? 0.2154 0.1877 0.3012 -0.0018 0.0143  0.0697  405  CYS A CA  
2963  C C   . CYS A 407  ? 0.2359 0.2039 0.3270 -0.0028 0.0124  0.0663  405  CYS A C   
2964  O O   . CYS A 407  ? 0.2560 0.2256 0.3458 -0.0029 0.0132  0.0652  405  CYS A O   
2965  C CB  . CYS A 407  ? 0.2604 0.2309 0.3365 0.0000  0.0151  0.0646  405  CYS A CB  
2966  S SG  . CYS A 407  ? 0.3150 0.2921 0.3839 0.0015  0.0176  0.0678  405  CYS A SG  
2967  N N   . ALA A 408  ? 0.2464 0.2092 0.3436 -0.0035 0.0099  0.0646  406  ALA A N   
2968  C CA  . ALA A 408  ? 0.2483 0.2076 0.3516 -0.0046 0.0079  0.0615  406  ALA A CA  
2969  C C   . ALA A 408  ? 0.2216 0.1839 0.3328 -0.0062 0.0077  0.0667  406  ALA A C   
2970  O O   . ALA A 408  ? 0.2503 0.2123 0.3637 -0.0068 0.0072  0.0647  406  ALA A O   
2971  C CB  . ALA A 408  ? 0.2643 0.2182 0.3733 -0.0048 0.0051  0.0586  406  ALA A CB  
2972  N N   . ALA A 409  ? 0.2605 0.2260 0.3765 -0.0070 0.0080  0.0735  407  ALA A N   
2973  C CA  . ALA A 409  ? 0.2469 0.2163 0.3705 -0.0087 0.0079  0.0792  407  ALA A CA  
2974  C C   . ALA A 409  ? 0.2527 0.2275 0.3704 -0.0082 0.0105  0.0796  407  ALA A C   
2975  O O   . ALA A 409  ? 0.2762 0.2522 0.3985 -0.0093 0.0102  0.0804  407  ALA A O   
2976  C CB  . ALA A 409  ? 0.3102 0.2831 0.4390 -0.0096 0.0079  0.0871  407  ALA A CB  
2977  N N   . LYS A 410  ? 0.2353 0.2133 0.3430 -0.0065 0.0130  0.0787  408  LYS A N   
2978  C CA  . LYS A 410  ? 0.2360 0.2190 0.3379 -0.0057 0.0153  0.0782  408  LYS A CA  
2979  C C   . LYS A 410  ? 0.2299 0.2090 0.3301 -0.0054 0.0146  0.0719  408  LYS A C   
2980  O O   . LYS A 410  ? 0.2457 0.2275 0.3473 -0.0058 0.0152  0.0724  408  LYS A O   
2981  C CB  . LYS A 410  ? 0.2406 0.2270 0.3326 -0.0037 0.0176  0.0774  408  LYS A CB  
2982  C CG  . LYS A 410  ? 0.2720 0.2638 0.3580 -0.0025 0.0200  0.0764  408  LYS A CG  
2983  C CD  . LYS A 410  ? 0.2770 0.2719 0.3540 -0.0004 0.0218  0.0752  408  LYS A CD  
2984  C CE  . LYS A 410  ? 0.3279 0.3282 0.4061 -0.0006 0.0227  0.0812  408  LYS A CE  
2985  N NZ  . LYS A 410  ? 0.3183 0.3275 0.3984 -0.0009 0.0245  0.0863  408  LYS A NZ  
2986  N N   . LEU A 411  ? 0.2212 0.1944 0.3183 -0.0047 0.0133  0.0662  409  LEU A N   
2987  C CA  . LEU A 411  ? 0.2129 0.1828 0.3079 -0.0045 0.0125  0.0605  409  LEU A CA  
2988  C C   . LEU A 411  ? 0.2203 0.1885 0.3247 -0.0063 0.0104  0.0606  409  LEU A C   
2989  O O   . LEU A 411  ? 0.2263 0.1951 0.3305 -0.0064 0.0104  0.0586  409  LEU A O   
2990  C CB  . LEU A 411  ? 0.2070 0.1720 0.2971 -0.0035 0.0115  0.0547  409  LEU A CB  
2991  C CG  . LEU A 411  ? 0.2215 0.1878 0.3015 -0.0017 0.0134  0.0530  409  LEU A CG  
2992  C CD1 . LEU A 411  ? 0.2300 0.1918 0.3064 -0.0010 0.0124  0.0488  409  LEU A CD1 
2993  C CD2 . LEU A 411  ? 0.2258 0.1938 0.3009 -0.0010 0.0145  0.0505  409  LEU A CD2 
2994  N N   . LEU A 412  ? 0.2446 0.2106 0.3576 -0.0075 0.0084  0.0630  410  LEU A N   
2995  C CA  . LEU A 412  ? 0.2316 0.1955 0.3541 -0.0092 0.0061  0.0627  410  LEU A CA  
2996  C C   . LEU A 412  ? 0.2645 0.2334 0.3917 -0.0104 0.0070  0.0678  410  LEU A C   
2997  O O   . LEU A 412  ? 0.2859 0.2538 0.4193 -0.0116 0.0054  0.0667  410  LEU A O   
2998  C CB  . LEU A 412  ? 0.2647 0.2246 0.3959 -0.0101 0.0034  0.0635  410  LEU A CB  
2999  C CG  . LEU A 412  ? 0.2364 0.1910 0.3649 -0.0091 0.0018  0.0568  410  LEU A CG  
3000  C CD1 . LEU A 412  ? 0.2965 0.2478 0.4338 -0.0098 -0.0006 0.0580  410  LEU A CD1 
3001  C CD2 . LEU A 412  ? 0.2730 0.2255 0.4016 -0.0092 0.0004  0.0505  410  LEU A CD2 
3002  N N   . ALA A 413  ? 0.2335 0.2082 0.3578 -0.0101 0.0094  0.0730  411  ALA A N   
3003  C CA  . ALA A 413  ? 0.2507 0.2312 0.3782 -0.0110 0.0107  0.0777  411  ALA A CA  
3004  C C   . ALA A 413  ? 0.2674 0.2501 0.3881 -0.0098 0.0124  0.0741  411  ALA A C   
3005  O O   . ALA A 413  ? 0.2928 0.2805 0.4159 -0.0104 0.0134  0.0770  411  ALA A O   
3006  C CB  . ALA A 413  ? 0.2516 0.2387 0.3789 -0.0111 0.0128  0.0847  411  ALA A CB  
3007  N N   . ALA A 414  ? 0.2481 0.2276 0.3607 -0.0082 0.0125  0.0680  412  ALA A N   
3008  C CA  . ALA A 414  ? 0.2918 0.2731 0.3975 -0.0069 0.0140  0.0648  412  ALA A CA  
3009  C C   . ALA A 414  ? 0.2540 0.2302 0.3583 -0.0068 0.0122  0.0584  412  ALA A C   
3010  O O   . ALA A 414  ? 0.2243 0.2007 0.3215 -0.0054 0.0130  0.0549  412  ALA A O   
3011  C CB  . ALA A 414  ? 0.2828 0.2669 0.3791 -0.0049 0.0163  0.0643  412  ALA A CB  
3012  N N   . THR A 415  ? 0.2668 0.2388 0.3779 -0.0081 0.0096  0.0568  413  THR A N   
3013  C CA  . THR A 415  ? 0.2541 0.2221 0.3637 -0.0079 0.0078  0.0506  413  THR A CA  
3014  C C   . THR A 415  ? 0.2447 0.2148 0.3534 -0.0079 0.0081  0.0492  413  THR A C   
3015  O O   . THR A 415  ? 0.2828 0.2508 0.3879 -0.0074 0.0071  0.0443  413  THR A O   
3016  C CB  . THR A 415  ? 0.2722 0.2359 0.3898 -0.0092 0.0048  0.0487  413  THR A CB  
3017  O OG1 . THR A 415  ? 0.3109 0.2760 0.4384 -0.0110 0.0038  0.0524  413  THR A OG1 
3018  C CG2 . THR A 415  ? 0.2782 0.2393 0.3964 -0.0090 0.0043  0.0493  413  THR A CG2 
3019  N N   . ASP A 416  ? 0.2666 0.2414 0.3787 -0.0085 0.0093  0.0535  414  ASP A N   
3020  C CA  . ASP A 416  ? 0.2597 0.2367 0.3705 -0.0082 0.0097  0.0521  414  ASP A CA  
3021  C C   . ASP A 416  ? 0.2898 0.2682 0.3908 -0.0062 0.0115  0.0499  414  ASP A C   
3022  O O   . ASP A 416  ? 0.3482 0.3267 0.4469 -0.0057 0.0112  0.0470  414  ASP A O   
3023  C CB  . ASP A 416  ? 0.2934 0.2754 0.4108 -0.0094 0.0104  0.0571  414  ASP A CB  
3024  C CG  . ASP A 416  ? 0.4203 0.4075 0.5359 -0.0088 0.0131  0.0623  414  ASP A CG  
3025  O OD1 . ASP A 416  ? 0.4063 0.3926 0.5201 -0.0085 0.0134  0.0637  414  ASP A OD1 
3026  O OD2 . ASP A 416  ? 0.5981 0.5910 0.7140 -0.0086 0.0147  0.0649  414  ASP A OD2 
3027  N N   . VAL A 417  ? 0.2685 0.2478 0.3641 -0.0050 0.0132  0.0511  415  VAL A N   
3028  C CA  . VAL A 417  ? 0.2882 0.2692 0.3755 -0.0030 0.0149  0.0491  415  VAL A CA  
3029  C C   . VAL A 417  ? 0.2345 0.2114 0.3151 -0.0020 0.0146  0.0456  415  VAL A C   
3030  O O   . VAL A 417  ? 0.2527 0.2297 0.3270 -0.0006 0.0152  0.0429  415  VAL A O   
3031  C CB  . VAL A 417  ? 0.3441 0.3313 0.4299 -0.0021 0.0175  0.0531  415  VAL A CB  
3032  C CG1 . VAL A 417  ? 0.3852 0.3772 0.4775 -0.0031 0.0179  0.0566  415  VAL A CG1 
3033  C CG2 . VAL A 417  ? 0.3038 0.2918 0.3895 -0.0022 0.0183  0.0562  415  VAL A CG2 
3034  N N   . VAL A 418  ? 0.2320 0.2057 0.3140 -0.0026 0.0136  0.0455  416  VAL A N   
3035  C CA  . VAL A 418  ? 0.2173 0.1871 0.2936 -0.0018 0.0130  0.0418  416  VAL A CA  
3036  C C   . VAL A 418  ? 0.2135 0.1791 0.2941 -0.0030 0.0106  0.0393  416  VAL A C   
3037  O O   . VAL A 418  ? 0.2236 0.1889 0.3119 -0.0044 0.0094  0.0410  416  VAL A O   
3038  C CB  . VAL A 418  ? 0.2290 0.1996 0.3016 -0.0008 0.0144  0.0437  416  VAL A CB  
3039  C CG1 . VAL A 418  ? 0.2349 0.2100 0.3025 0.0007  0.0167  0.0450  416  VAL A CG1 
3040  C CG2 . VAL A 418  ? 0.2380 0.2091 0.3169 -0.0020 0.0142  0.0478  416  VAL A CG2 
3041  N N   . PHE A 419  ? 0.1975 0.1600 0.2734 -0.0024 0.0098  0.0352  417  PHE A N   
3042  C CA  . PHE A 419  ? 0.2225 0.1815 0.3016 -0.0032 0.0075  0.0320  417  PHE A CA  
3043  C C   . PHE A 419  ? 0.1894 0.1466 0.2666 -0.0027 0.0077  0.0320  417  PHE A C   
3044  O O   . PHE A 419  ? 0.2067 0.1630 0.2769 -0.0017 0.0083  0.0297  417  PHE A O   
3045  C CB  . PHE A 419  ? 0.1949 0.1530 0.2701 -0.0030 0.0064  0.0272  417  PHE A CB  
3046  C CG  . PHE A 419  ? 0.2178 0.1733 0.2952 -0.0035 0.0042  0.0232  417  PHE A CG  
3047  C CD1 . PHE A 419  ? 0.2399 0.1947 0.3256 -0.0047 0.0023  0.0226  417  PHE A CD1 
3048  C CD2 . PHE A 419  ? 0.2130 0.1673 0.2845 -0.0028 0.0040  0.0197  417  PHE A CD2 
3049  C CE1 . PHE A 419  ? 0.2137 0.1666 0.3017 -0.0050 0.0002  0.0182  417  PHE A CE1 
3050  C CE2 . PHE A 419  ? 0.2200 0.1730 0.2935 -0.0032 0.0020  0.0157  417  PHE A CE2 
3051  C CZ  . PHE A 419  ? 0.2068 0.1591 0.2885 -0.0041 0.0001  0.0147  417  PHE A CZ  
3052  N N   . PRO A 420  ? 0.1909 0.1473 0.2743 -0.0034 0.0071  0.0346  418  PRO A N   
3053  C CA  . PRO A 420  ? 0.1952 0.1498 0.2770 -0.0029 0.0072  0.0348  418  PRO A CA  
3054  C C   . PRO A 420  ? 0.2211 0.1725 0.3025 -0.0027 0.0054  0.0296  418  PRO A C   
3055  O O   . PRO A 420  ? 0.2176 0.1678 0.3040 -0.0035 0.0033  0.0268  418  PRO A O   
3056  C CB  . PRO A 420  ? 0.1903 0.1453 0.2805 -0.0039 0.0067  0.0394  418  PRO A CB  
3057  C CG  . PRO A 420  ? 0.1957 0.1538 0.2900 -0.0048 0.0072  0.0426  418  PRO A CG  
3058  C CD  . PRO A 420  ? 0.2140 0.1716 0.3063 -0.0047 0.0065  0.0382  418  PRO A CD  
3059  N N   . GLN A 421  ? 0.2015 0.1520 0.2768 -0.0017 0.0060  0.0282  419  GLN A N   
3060  C CA  . GLN A 421  ? 0.1926 0.1408 0.2667 -0.0015 0.0046  0.0234  419  GLN A CA  
3061  C C   . GLN A 421  ? 0.2030 0.1498 0.2774 -0.0010 0.0047  0.0247  419  GLN A C   
3062  O O   . GLN A 421  ? 0.2200 0.1676 0.2885 -0.0001 0.0064  0.0263  419  GLN A O   
3063  C CB  . GLN A 421  ? 0.1862 0.1350 0.2518 -0.0007 0.0053  0.0203  419  GLN A CB  
3064  C CG  . GLN A 421  ? 0.2153 0.1658 0.2804 -0.0012 0.0052  0.0195  419  GLN A CG  
3065  C CD  . GLN A 421  ? 0.2005 0.1519 0.2575 -0.0004 0.0061  0.0180  419  GLN A CD  
3066  O OE1 . GLN A 421  ? 0.2257 0.1777 0.2781 0.0004  0.0078  0.0201  419  GLN A OE1 
3067  N NE2 . GLN A 421  ? 0.2230 0.1747 0.2787 -0.0008 0.0048  0.0144  419  GLN A NE2 
3068  N N   . PHE A 422  ? 0.1995 0.1443 0.2813 -0.0015 0.0028  0.0239  420  PHE A N   
3069  C CA  . PHE A 422  ? 0.1971 0.1407 0.2810 -0.0011 0.0027  0.0259  420  PHE A CA  
3070  C C   . PHE A 422  ? 0.1978 0.1397 0.2785 -0.0003 0.0019  0.0210  420  PHE A C   
3071  O O   . PHE A 422  ? 0.2256 0.1660 0.3113 -0.0004 -0.0003 0.0171  420  PHE A O   
3072  C CB  . PHE A 422  ? 0.2282 0.1706 0.3230 -0.0021 0.0009  0.0286  420  PHE A CB  
3073  C CG  . PHE A 422  ? 0.2213 0.1659 0.3193 -0.0031 0.0018  0.0339  420  PHE A CG  
3074  C CD1 . PHE A 422  ? 0.2433 0.1907 0.3376 -0.0028 0.0041  0.0391  420  PHE A CD1 
3075  C CD2 . PHE A 422  ? 0.2191 0.1637 0.3238 -0.0042 0.0004  0.0335  420  PHE A CD2 
3076  C CE1 . PHE A 422  ? 0.2598 0.2103 0.3570 -0.0036 0.0051  0.0440  420  PHE A CE1 
3077  C CE2 . PHE A 422  ? 0.2452 0.1923 0.3529 -0.0051 0.0013  0.0385  420  PHE A CE2 
3078  C CZ  . PHE A 422  ? 0.2393 0.1896 0.3432 -0.0048 0.0037  0.0438  420  PHE A CZ  
3079  N N   . ALA A 423  ? 0.2088 0.1514 0.2813 0.0007  0.0035  0.0210  421  ALA A N   
3080  C CA  . ALA A 423  ? 0.1923 0.1341 0.2609 0.0014  0.0031  0.0168  421  ALA A CA  
3081  C C   . ALA A 423  ? 0.2269 0.1672 0.2989 0.0019  0.0026  0.0183  421  ALA A C   
3082  O O   . ALA A 423  ? 0.2504 0.1913 0.3200 0.0022  0.0040  0.0225  421  ALA A O   
3083  C CB  . ALA A 423  ? 0.2081 0.1513 0.2669 0.0021  0.0050  0.0163  421  ALA A CB  
3084  N N   . THR A 424  ? 0.2237 0.1622 0.3014 0.0019  0.0005  0.0149  422  THR A N   
3085  C CA  . THR A 424  ? 0.2272 0.1641 0.3086 0.0024  -0.0003 0.0160  422  THR A CA  
3086  C C   . THR A 424  ? 0.2316 0.1672 0.3179 0.0028  -0.0026 0.0103  422  THR A C   
3087  O O   . THR A 424  ? 0.2525 0.1881 0.3428 0.0023  -0.0042 0.0067  422  THR A O   
3088  C CB  . THR A 424  ? 0.2609 0.1972 0.3499 0.0017  -0.0007 0.0219  422  THR A CB  
3089  O OG1 . THR A 424  ? 0.2571 0.1920 0.3492 0.0023  -0.0015 0.0232  422  THR A OG1 
3090  C CG2 . THR A 424  ? 0.2713 0.2064 0.3700 0.0007  -0.0029 0.0211  422  THR A CG2 
3091  N N   . HIS A 425  ? 0.2289 0.1637 0.3147 0.0037  -0.0029 0.0092  423  HIS A N   
3092  C CA  . HIS A 425  ? 0.2420 0.1757 0.3335 0.0042  -0.0053 0.0040  423  HIS A CA  
3093  C C   . HIS A 425  ? 0.2641 0.1952 0.3657 0.0042  -0.0071 0.0066  423  HIS A C   
3094  O O   . HIS A 425  ? 0.2896 0.2195 0.3971 0.0049  -0.0093 0.0024  423  HIS A O   
3095  C CB  . HIS A 425  ? 0.2393 0.1742 0.3238 0.0053  -0.0045 0.0003  423  HIS A CB  
3096  C CG  . HIS A 425  ? 0.2394 0.1769 0.3150 0.0052  -0.0031 -0.0023 423  HIS A CG  
3097  N ND1 . HIS A 425  ? 0.2696 0.2085 0.3362 0.0056  -0.0012 -0.0016 423  HIS A ND1 
3098  C CD2 . HIS A 425  ? 0.2667 0.2059 0.3414 0.0046  -0.0035 -0.0052 423  HIS A CD2 
3099  C CE1 . HIS A 425  ? 0.2877 0.2288 0.3485 0.0053  -0.0005 -0.0038 423  HIS A CE1 
3100  N NE2 . HIS A 425  ? 0.2537 0.1952 0.3190 0.0047  -0.0018 -0.0059 423  HIS A NE2 
3101  N N   . ASN A 426  ? 0.2560 0.1866 0.3599 0.0035  -0.0064 0.0133  424  ASN A N   
3102  C CA  . ASN A 426  ? 0.2696 0.1981 0.3829 0.0034  -0.0081 0.0172  424  ASN A CA  
3103  C C   . ASN A 426  ? 0.2791 0.2060 0.4033 0.0023  -0.0105 0.0174  424  ASN A C   
3104  O O   . ASN A 426  ? 0.2762 0.2042 0.4009 0.0012  -0.0097 0.0208  424  ASN A O   
3105  C CB  . ASN A 426  ? 0.2502 0.1801 0.3597 0.0031  -0.0060 0.0246  424  ASN A CB  
3106  C CG  . ASN A 426  ? 0.2794 0.2078 0.3977 0.0029  -0.0076 0.0296  424  ASN A CG  
3107  O OD1 . ASN A 426  ? 0.3097 0.2360 0.4388 0.0022  -0.0101 0.0301  424  ASN A OD1 
3108  N ND2 . ASN A 426  ? 0.2851 0.2147 0.3988 0.0034  -0.0062 0.0336  424  ASN A ND2 
3109  N N   . ALA A 427  ? 0.2546 0.1792 0.3882 0.0027  -0.0135 0.0135  425  ALA A N   
3110  C CA  . ALA A 427  ? 0.2653 0.1881 0.4102 0.0018  -0.0162 0.0127  425  ALA A CA  
3111  C C   . ALA A 427  ? 0.2323 0.1543 0.3846 0.0003  -0.0166 0.0211  425  ALA A C   
3112  O O   . ALA A 427  ? 0.2734 0.1950 0.4325 -0.0009 -0.0178 0.0223  425  ALA A O   
3113  C CB  . ALA A 427  ? 0.3057 0.2263 0.4598 0.0027  -0.0196 0.0066  425  ALA A CB  
3114  N N   . GLN A 428  ? 0.2641 0.1862 0.4155 0.0005  -0.0157 0.0269  426  GLN A N   
3115  C CA  . GLN A 428  ? 0.2974 0.2200 0.4549 -0.0010 -0.0157 0.0356  426  GLN A CA  
3116  C C   . GLN A 428  ? 0.2925 0.2185 0.4430 -0.0019 -0.0129 0.0393  426  GLN A C   
3117  O O   . GLN A 428  ? 0.2806 0.2071 0.4375 -0.0034 -0.0135 0.0432  426  GLN A O   
3118  C CB  . GLN A 428  ? 0.2600 0.1829 0.4169 -0.0005 -0.0152 0.0409  426  GLN A CB  
3119  C CG  . GLN A 428  ? 0.3189 0.2420 0.4857 -0.0020 -0.0164 0.0496  426  GLN A CG  
3120  C CD  . GLN A 428  ? 0.3500 0.2773 0.5121 -0.0033 -0.0137 0.0564  426  GLN A CD  
3121  O OE1 . GLN A 428  ? 0.3605 0.2910 0.5106 -0.0027 -0.0105 0.0564  426  GLN A OE1 
3122  N NE2 . GLN A 428  ? 0.3291 0.2567 0.5011 -0.0050 -0.0151 0.0621  426  GLN A NE2 
3123  N N   . THR A 429  ? 0.2776 0.2060 0.4152 -0.0011 -0.0099 0.0382  427  THR A N   
3124  C CA  . THR A 429  ? 0.2565 0.1883 0.3871 -0.0017 -0.0072 0.0407  427  THR A CA  
3125  C C   . THR A 429  ? 0.2545 0.1858 0.3885 -0.0025 -0.0082 0.0373  427  THR A C   
3126  O O   . THR A 429  ? 0.2730 0.2059 0.4096 -0.0037 -0.0077 0.0414  427  THR A O   
3127  C CB  . THR A 429  ? 0.2556 0.1892 0.3728 -0.0004 -0.0045 0.0380  427  THR A CB  
3128  O OG1 . THR A 429  ? 0.2704 0.2042 0.3847 0.0005  -0.0039 0.0401  427  THR A OG1 
3129  C CG2 . THR A 429  ? 0.2839 0.2211 0.3942 -0.0008 -0.0018 0.0412  427  THR A CG2 
3130  N N   . LEU A 430  ? 0.2514 0.1808 0.3855 -0.0018 -0.0097 0.0296  428  LEU A N   
3131  C CA  . LEU A 430  ? 0.2510 0.1803 0.3877 -0.0024 -0.0108 0.0256  428  LEU A CA  
3132  C C   . LEU A 430  ? 0.2638 0.1916 0.4135 -0.0039 -0.0133 0.0286  428  LEU A C   
3133  O O   . LEU A 430  ? 0.2608 0.1899 0.4122 -0.0050 -0.0129 0.0306  428  LEU A O   
3134  C CB  . LEU A 430  ? 0.2250 0.1532 0.3608 -0.0013 -0.0124 0.0169  428  LEU A CB  
3135  C CG  . LEU A 430  ? 0.2913 0.2205 0.4265 -0.0015 -0.0132 0.0109  428  LEU A CG  
3136  C CD1 . LEU A 430  ? 0.3539 0.2834 0.4855 -0.0001 -0.0140 0.0034  428  LEU A CD1 
3137  C CD2 . LEU A 430  ? 0.3162 0.2438 0.4636 -0.0026 -0.0161 0.0103  428  LEU A CD2 
3138  N N   . ALA A 431  ? 0.2928 0.2178 0.4525 -0.0038 -0.0159 0.0290  429  ALA A N   
3139  C CA  . ALA A 431  ? 0.2799 0.2030 0.4535 -0.0053 -0.0188 0.0316  429  ALA A CA  
3140  C C   . ALA A 431  ? 0.2776 0.2030 0.4528 -0.0069 -0.0173 0.0408  429  ALA A C   
3141  O O   . ALA A 431  ? 0.2623 0.1879 0.4448 -0.0084 -0.0184 0.0429  429  ALA A O   
3142  C CB  . ALA A 431  ? 0.2772 0.1968 0.4608 -0.0048 -0.0219 0.0310  429  ALA A CB  
3143  N N   . ALA A 432  ? 0.2915 0.2192 0.4601 -0.0066 -0.0148 0.0464  430  ALA A N   
3144  C CA  . ALA A 432  ? 0.2943 0.2255 0.4634 -0.0080 -0.0131 0.0551  430  ALA A CA  
3145  C C   . ALA A 432  ? 0.3076 0.2418 0.4716 -0.0086 -0.0111 0.0548  430  ALA A C   
3146  O O   . ALA A 432  ? 0.2989 0.2349 0.4689 -0.0102 -0.0113 0.0599  430  ALA A O   
3147  C CB  . ALA A 432  ? 0.2789 0.2129 0.4399 -0.0072 -0.0105 0.0597  430  ALA A CB  
3148  N N   . ILE A 433  ? 0.2931 0.2278 0.4465 -0.0073 -0.0095 0.0490  431  ILE A N   
3149  C CA  . ILE A 433  ? 0.2355 0.1731 0.3836 -0.0077 -0.0076 0.0486  431  ILE A CA  
3150  C C   . ILE A 433  ? 0.2633 0.1990 0.4190 -0.0086 -0.0101 0.0447  431  ILE A C   
3151  O O   . ILE A 433  ? 0.2779 0.2158 0.4359 -0.0098 -0.0096 0.0474  431  ILE A O   
3152  C CB  . ILE A 433  ? 0.2566 0.1953 0.3911 -0.0061 -0.0052 0.0442  431  ILE A CB  
3153  C CG1 . ILE A 433  ? 0.3254 0.2667 0.4527 -0.0054 -0.0026 0.0488  431  ILE A CG1 
3154  C CG2 . ILE A 433  ? 0.2677 0.2085 0.3976 -0.0063 -0.0040 0.0421  431  ILE A CG2 
3155  C CD1 . ILE A 433  ? 0.3263 0.2683 0.4416 -0.0038 -0.0006 0.0447  431  ILE A CD1 
3156  N N   . TYR A 434  ? 0.2511 0.1833 0.4111 -0.0081 -0.0127 0.0383  432  TYR A N   
3157  C CA  . TYR A 434  ? 0.2642 0.1949 0.4322 -0.0088 -0.0154 0.0339  432  TYR A CA  
3158  C C   . TYR A 434  ? 0.2735 0.2040 0.4538 -0.0108 -0.0171 0.0398  432  TYR A C   
3159  O O   . TYR A 434  ? 0.3164 0.2479 0.5002 -0.0119 -0.0176 0.0397  432  TYR A O   
3160  C CB  . TYR A 434  ? 0.2945 0.2219 0.4668 -0.0078 -0.0183 0.0266  432  TYR A CB  
3161  C CG  . TYR A 434  ? 0.3183 0.2440 0.5013 -0.0084 -0.0217 0.0221  432  TYR A CG  
3162  C CD1 . TYR A 434  ? 0.3186 0.2460 0.4987 -0.0086 -0.0217 0.0176  432  TYR A CD1 
3163  C CD2 . TYR A 434  ? 0.3323 0.2546 0.5288 -0.0089 -0.0253 0.0221  432  TYR A CD2 
3164  C CE1 . TYR A 434  ? 0.2902 0.2164 0.4802 -0.0092 -0.0250 0.0131  432  TYR A CE1 
3165  C CE2 . TYR A 434  ? 0.3559 0.2767 0.5629 -0.0094 -0.0287 0.0174  432  TYR A CE2 
3166  C CZ  . TYR A 434  ? 0.3663 0.2891 0.5698 -0.0096 -0.0285 0.0129  432  TYR A CZ  
3167  O OH  . TYR A 434  ? 0.4023 0.3239 0.6162 -0.0100 -0.0320 0.0079  432  TYR A OH  
3168  N N   . HIS A 435  ? 0.2884 0.2178 0.4757 -0.0113 -0.0180 0.0454  433  HIS A N   
3169  C CA  . HIS A 435  ? 0.3345 0.2639 0.5341 -0.0133 -0.0197 0.0520  433  HIS A CA  
3170  C C   . HIS A 435  ? 0.3313 0.2658 0.5266 -0.0144 -0.0166 0.0597  433  HIS A C   
3171  O O   . HIS A 435  ? 0.3118 0.2477 0.5147 -0.0162 -0.0174 0.0635  433  HIS A O   
3172  C CB  . HIS A 435  ? 0.3314 0.2580 0.5409 -0.0136 -0.0222 0.0554  433  HIS A CB  
3173  C CG  . HIS A 435  ? 0.3793 0.3011 0.5973 -0.0129 -0.0260 0.0480  433  HIS A CG  
3174  N ND1 . HIS A 435  ? 0.3643 0.2848 0.5943 -0.0139 -0.0295 0.0458  433  HIS A ND1 
3175  C CD2 . HIS A 435  ? 0.3109 0.2303 0.5260 -0.0110 -0.0269 0.0415  433  HIS A CD2 
3176  C CE1 . HIS A 435  ? 0.3598 0.2777 0.5940 -0.0126 -0.0324 0.0381  433  HIS A CE1 
3177  N NE2 . HIS A 435  ? 0.3341 0.2502 0.5604 -0.0110 -0.0309 0.0357  433  HIS A NE2 
3178  N N   . MET A 436  ? 0.2938 0.2314 0.4772 -0.0133 -0.0132 0.0618  434  MET A N   
3179  C CA  . MET A 436  ? 0.2916 0.2348 0.4700 -0.0140 -0.0100 0.0682  434  MET A CA  
3180  C C   . MET A 436  ? 0.2998 0.2446 0.4757 -0.0144 -0.0093 0.0652  434  MET A C   
3181  O O   . MET A 436  ? 0.3316 0.2801 0.5106 -0.0157 -0.0084 0.0704  434  MET A O   
3182  C CB  . MET A 436  ? 0.3105 0.2565 0.4761 -0.0124 -0.0068 0.0691  434  MET A CB  
3183  C CG  . MET A 436  ? 0.3114 0.2638 0.4718 -0.0128 -0.0036 0.0753  434  MET A CG  
3184  S SD  . MET A 436  ? 0.3343 0.2896 0.4792 -0.0106 0.0000  0.0742  434  MET A SD  
3185  C CE  . MET A 436  ? 0.3268 0.2815 0.4749 -0.0105 -0.0008 0.0788  434  MET A CE  
3186  N N   . ALA A 437  ? 0.2785 0.2210 0.4491 -0.0132 -0.0097 0.0571  435  ALA A N   
3187  C CA  . ALA A 437  ? 0.3011 0.2451 0.4684 -0.0134 -0.0090 0.0540  435  ALA A CA  
3188  C C   . ALA A 437  ? 0.3396 0.2825 0.5191 -0.0151 -0.0119 0.0540  435  ALA A C   
3189  O O   . ALA A 437  ? 0.3282 0.2735 0.5071 -0.0158 -0.0112 0.0541  435  ALA A O   
3190  C CB  . ALA A 437  ? 0.3145 0.2569 0.4730 -0.0117 -0.0089 0.0457  435  ALA A CB  
3191  N N   . GLY A 438  ? 0.4057 0.3449 0.5965 -0.0158 -0.0152 0.0536  436  GLY A N   
3192  C CA  . GLY A 438  ? 0.4372 0.3752 0.6409 -0.0176 -0.0181 0.0542  436  GLY A CA  
3193  C C   . GLY A 438  ? 0.3874 0.3232 0.5927 -0.0172 -0.0204 0.0454  436  GLY A C   
3194  O O   . GLY A 438  ? 0.3883 0.3235 0.5849 -0.0155 -0.0199 0.0387  436  GLY A O   
3195  N N   . LYS A 439  ? 0.4789 0.4140 0.6956 -0.0188 -0.0230 0.0458  437  LYS A N   
3196  C CA  . LYS A 439  ? 0.4668 0.3997 0.6881 -0.0186 -0.0260 0.0375  437  LYS A CA  
3197  C C   . LYS A 439  ? 0.4251 0.3611 0.6378 -0.0182 -0.0244 0.0339  437  LYS A C   
3198  O O   . LYS A 439  ? 0.5043 0.4395 0.7152 -0.0173 -0.0259 0.0258  437  LYS A O   
3199  C CB  . LYS A 439  ? 0.5357 0.4665 0.7737 -0.0205 -0.0299 0.0392  437  LYS A CB  
3200  N N   . ASP A 440  ? 0.3835 0.3233 0.5911 -0.0189 -0.0215 0.0395  438  ASP A N   
3201  C CA  . ASP A 440  ? 0.4185 0.3612 0.6185 -0.0185 -0.0200 0.0364  438  ASP A CA  
3202  C C   . ASP A 440  ? 0.4377 0.3810 0.6235 -0.0164 -0.0177 0.0322  438  ASP A C   
3203  O O   . ASP A 440  ? 0.4370 0.3814 0.6152 -0.0157 -0.0149 0.0359  438  ASP A O   
3204  C CB  . ASP A 440  ? 0.4120 0.3588 0.6111 -0.0197 -0.0175 0.0437  438  ASP A CB  
3205  C CG  . ASP A 440  ? 0.5166 0.4636 0.7295 -0.0219 -0.0198 0.0473  438  ASP A CG  
3206  O OD1 . ASP A 440  ? 0.5305 0.4739 0.7538 -0.0226 -0.0235 0.0439  438  ASP A OD1 
3207  O OD2 . ASP A 440  ? 0.5241 0.4750 0.7377 -0.0230 -0.0180 0.0535  438  ASP A OD2 
3208  N N   . PHE A 441  ? 0.3481 0.2909 0.5306 -0.0156 -0.0190 0.0245  439  PHE A N   
3209  C CA  . PHE A 441  ? 0.3050 0.2487 0.4746 -0.0138 -0.0170 0.0206  439  PHE A CA  
3210  C C   . PHE A 441  ? 0.3507 0.2965 0.5161 -0.0136 -0.0175 0.0153  439  PHE A C   
3211  O O   . PHE A 441  ? 0.3369 0.2825 0.5098 -0.0143 -0.0202 0.0116  439  PHE A O   
3212  C CB  . PHE A 441  ? 0.2913 0.2323 0.4597 -0.0126 -0.0181 0.0161  439  PHE A CB  
3213  C CG  . PHE A 441  ? 0.2823 0.2246 0.4376 -0.0109 -0.0160 0.0130  439  PHE A CG  
3214  C CD1 . PHE A 441  ? 0.2873 0.2304 0.4343 -0.0103 -0.0129 0.0174  439  PHE A CD1 
3215  C CD2 . PHE A 441  ? 0.3117 0.2551 0.4629 -0.0102 -0.0171 0.0058  439  PHE A CD2 
3216  C CE1 . PHE A 441  ? 0.2764 0.2206 0.4120 -0.0089 -0.0111 0.0148  439  PHE A CE1 
3217  C CE2 . PHE A 441  ? 0.2881 0.2330 0.4277 -0.0089 -0.0151 0.0036  439  PHE A CE2 
3218  C CZ  . PHE A 441  ? 0.2918 0.2369 0.4239 -0.0083 -0.0122 0.0082  439  PHE A CZ  
3219  N N   . HIS A 442  ? 0.2665 0.2144 0.4202 -0.0125 -0.0149 0.0150  440  HIS A N   
3220  C CA  . HIS A 442  ? 0.3137 0.2638 0.4618 -0.0120 -0.0152 0.0099  440  HIS A CA  
3221  C C   . HIS A 442  ? 0.3619 0.3127 0.4977 -0.0106 -0.0129 0.0087  440  HIS A C   
3222  O O   . HIS A 442  ? 0.2882 0.2386 0.4195 -0.0101 -0.0106 0.0130  440  HIS A O   
3223  C CB  . HIS A 442  ? 0.3157 0.2685 0.4642 -0.0129 -0.0144 0.0127  440  HIS A CB  
3224  C CG  . HIS A 442  ? 0.2774 0.2318 0.4199 -0.0127 -0.0110 0.0189  440  HIS A CG  
3225  N ND1 . HIS A 442  ? 0.3366 0.2912 0.4842 -0.0135 -0.0100 0.0253  440  HIS A ND1 
3226  C CD2 . HIS A 442  ? 0.3099 0.2663 0.4422 -0.0116 -0.0086 0.0194  440  HIS A CD2 
3227  C CE1 . HIS A 442  ? 0.3125 0.2695 0.4530 -0.0129 -0.0070 0.0292  440  HIS A CE1 
3228  N NE2 . HIS A 442  ? 0.3131 0.2709 0.4444 -0.0117 -0.0062 0.0256  440  HIS A NE2 
3229  N N   . VAL A 443  ? 0.3266 0.2789 0.4574 -0.0099 -0.0138 0.0030  441  VAL A N   
3230  C CA  . VAL A 443  ? 0.3825 0.3357 0.5020 -0.0087 -0.0118 0.0020  441  VAL A CA  
3231  C C   . VAL A 443  ? 0.3464 0.3012 0.4598 -0.0086 -0.0091 0.0068  441  VAL A C   
3232  O O   . VAL A 443  ? 0.3300 0.2866 0.4448 -0.0092 -0.0092 0.0079  441  VAL A O   
3233  C CB  . VAL A 443  ? 0.3755 0.3310 0.4912 -0.0082 -0.0133 -0.0046 441  VAL A CB  
3234  C CG1 . VAL A 443  ? 0.3839 0.3410 0.4882 -0.0073 -0.0112 -0.0045 441  VAL A CG1 
3235  C CG2 . VAL A 443  ? 0.4474 0.4017 0.5680 -0.0078 -0.0156 -0.0097 441  VAL A CG2 
3236  N N   . GLY A 444  ? 0.2968 0.2510 0.4038 -0.0077 -0.0068 0.0097  442  GLY A N   
3237  C CA  . GLY A 444  ? 0.2648 0.2204 0.3669 -0.0074 -0.0042 0.0142  442  GLY A CA  
3238  C C   . GLY A 444  ? 0.2550 0.2102 0.3609 -0.0078 -0.0028 0.0200  442  GLY A C   
3239  O O   . GLY A 444  ? 0.2553 0.2120 0.3564 -0.0072 -0.0005 0.0235  442  GLY A O   
3240  N N   . LYS A 445  ? 0.2457 0.1991 0.3601 -0.0086 -0.0043 0.0210  443  LYS A N   
3241  C CA  . LYS A 445  ? 0.2349 0.1887 0.3530 -0.0090 -0.0030 0.0271  443  LYS A CA  
3242  C C   . LYS A 445  ? 0.2769 0.2298 0.3890 -0.0079 -0.0013 0.0284  443  LYS A C   
3243  O O   . LYS A 445  ? 0.2458 0.2007 0.3538 -0.0074 0.0011  0.0326  443  LYS A O   
3244  C CB  . LYS A 445  ? 0.2647 0.2168 0.3946 -0.0104 -0.0053 0.0283  443  LYS A CB  
3245  C CG  . LYS A 445  ? 0.3167 0.2703 0.4509 -0.0111 -0.0039 0.0355  443  LYS A CG  
3246  C CD  . LYS A 445  ? 0.3653 0.3173 0.5120 -0.0128 -0.0064 0.0376  443  LYS A CD  
3247  C CE  . LYS A 445  ? 0.4163 0.3714 0.5672 -0.0138 -0.0048 0.0454  443  LYS A CE  
3248  N NZ  . LYS A 445  ? 0.4725 0.4262 0.6365 -0.0156 -0.0073 0.0484  443  LYS A NZ  
3249  N N   . TYR A 446  ? 0.2545 0.2048 0.3662 -0.0074 -0.0026 0.0247  444  TYR A N   
3250  C CA  A TYR A 446  ? 0.2398 0.1892 0.3454 -0.0063 -0.0013 0.0248  444  TYR A CA  
3251  C CA  B TYR A 446  ? 0.2399 0.1892 0.3452 -0.0063 -0.0013 0.0248  444  TYR A CA  
3252  C C   . TYR A 446  ? 0.2299 0.1772 0.3345 -0.0058 -0.0031 0.0187  444  TYR A C   
3253  O O   . TYR A 446  ? 0.2379 0.1848 0.3473 -0.0063 -0.0054 0.0147  444  TYR A O   
3254  C CB  A TYR A 446  ? 0.2286 0.1773 0.3389 -0.0066 -0.0009 0.0300  444  TYR A CB  
3255  C CB  B TYR A 446  ? 0.2284 0.1772 0.3382 -0.0066 -0.0008 0.0299  444  TYR A CB  
3256  C CG  A TYR A 446  ? 0.2387 0.1845 0.3582 -0.0072 -0.0036 0.0288  444  TYR A CG  
3257  C CG  B TYR A 446  ? 0.2500 0.1963 0.3707 -0.0076 -0.0035 0.0296  444  TYR A CG  
3258  C CD1 A TYR A 446  ? 0.2817 0.2269 0.4119 -0.0086 -0.0056 0.0302  444  TYR A CD1 
3259  C CD1 B TYR A 446  ? 0.2381 0.1850 0.3680 -0.0090 -0.0046 0.0326  444  TYR A CD1 
3260  C CD2 A TYR A 446  ? 0.2473 0.1908 0.3654 -0.0063 -0.0042 0.0263  444  TYR A CD2 
3261  C CD2 B TYR A 446  ? 0.2217 0.1652 0.3442 -0.0070 -0.0051 0.0262  444  TYR A CD2 
3262  C CE1 A TYR A 446  ? 0.2266 0.1689 0.3661 -0.0091 -0.0083 0.0289  444  TYR A CE1 
3263  C CE1 B TYR A 446  ? 0.2476 0.1921 0.3884 -0.0100 -0.0074 0.0323  444  TYR A CE1 
3264  C CE2 A TYR A 446  ? 0.2410 0.1817 0.3681 -0.0067 -0.0068 0.0249  444  TYR A CE2 
3265  C CE2 B TYR A 446  ? 0.2574 0.1985 0.3908 -0.0078 -0.0079 0.0256  444  TYR A CE2 
3266  C CZ  A TYR A 446  ? 0.2517 0.1917 0.3897 -0.0081 -0.0089 0.0262  444  TYR A CZ  
3267  C CZ  B TYR A 446  ? 0.2361 0.1775 0.3787 -0.0093 -0.0091 0.0286  444  TYR A CZ  
3268  O OH  A TYR A 446  ? 0.2832 0.2203 0.4311 -0.0084 -0.0118 0.0247  444  TYR A OH  
3269  O OH  B TYR A 446  ? 0.2856 0.2244 0.4399 -0.0101 -0.0122 0.0280  444  TYR A OH  
3270  N N   . GLU A 447  ? 0.2058 0.1524 0.3044 -0.0047 -0.0022 0.0178  445  GLU A N   
3271  C CA  . GLU A 447  ? 0.2206 0.1658 0.3187 -0.0042 -0.0038 0.0123  445  GLU A CA  
3272  C C   . GLU A 447  ? 0.2368 0.1805 0.3329 -0.0034 -0.0031 0.0136  445  GLU A C   
3273  O O   . GLU A 447  ? 0.2324 0.1765 0.3256 -0.0031 -0.0011 0.0183  445  GLU A O   
3274  C CB  . GLU A 447  ? 0.2161 0.1631 0.3062 -0.0036 -0.0035 0.0081  445  GLU A CB  
3275  C CG  . GLU A 447  ? 0.2247 0.1726 0.3051 -0.0028 -0.0010 0.0100  445  GLU A CG  
3276  C CD  . GLU A 447  ? 0.2322 0.1819 0.3055 -0.0025 -0.0008 0.0068  445  GLU A CD  
3277  O OE1 . GLU A 447  ? 0.2592 0.2104 0.3345 -0.0030 -0.0024 0.0036  445  GLU A OE1 
3278  O OE2 . GLU A 447  ? 0.2246 0.1748 0.2905 -0.0018 0.0007  0.0076  445  GLU A OE2 
3279  N N   . PHE A 448  ? 0.2150 0.1574 0.3127 -0.0029 -0.0047 0.0091  446  PHE A N   
3280  C CA  . PHE A 448  ? 0.2325 0.1738 0.3268 -0.0019 -0.0040 0.0091  446  PHE A CA  
3281  C C   . PHE A 448  ? 0.1904 0.1333 0.2750 -0.0011 -0.0030 0.0056  446  PHE A C   
3282  O O   . PHE A 448  ? 0.2141 0.1589 0.2958 -0.0013 -0.0032 0.0027  446  PHE A O   
3283  C CB  . PHE A 448  ? 0.2422 0.1814 0.3446 -0.0018 -0.0065 0.0062  446  PHE A CB  
3284  C CG  . PHE A 448  ? 0.2411 0.1784 0.3537 -0.0027 -0.0077 0.0103  446  PHE A CG  
3285  C CD1 . PHE A 448  ? 0.2387 0.1752 0.3521 -0.0027 -0.0066 0.0161  446  PHE A CD1 
3286  C CD2 . PHE A 448  ? 0.2456 0.1823 0.3673 -0.0036 -0.0101 0.0085  446  PHE A CD2 
3287  C CE1 . PHE A 448  ? 0.2884 0.2237 0.4117 -0.0037 -0.0078 0.0206  446  PHE A CE1 
3288  C CE2 . PHE A 448  ? 0.2918 0.2268 0.4238 -0.0046 -0.0114 0.0127  446  PHE A CE2 
3289  C CZ  . PHE A 448  ? 0.2677 0.2021 0.4004 -0.0047 -0.0102 0.0191  446  PHE A CZ  
3290  N N   . GLN A 449  ? 0.2021 0.1444 0.2820 -0.0003 -0.0019 0.0061  447  GLN A N   
3291  C CA  . GLN A 449  ? 0.2065 0.1502 0.2779 0.0004  -0.0011 0.0030  447  GLN A CA  
3292  C C   . GLN A 449  ? 0.2234 0.1662 0.2946 0.0012  -0.0014 0.0012  447  GLN A C   
3293  O O   . GLN A 449  ? 0.2321 0.1730 0.3073 0.0014  -0.0015 0.0039  447  GLN A O   
3294  C CB  . GLN A 449  ? 0.2078 0.1526 0.2711 0.0006  0.0013  0.0062  447  GLN A CB  
3295  C CG  . GLN A 449  ? 0.2043 0.1504 0.2674 0.0000  0.0017  0.0078  447  GLN A CG  
3296  C CD  . GLN A 449  ? 0.2248 0.1722 0.2797 0.0004  0.0035  0.0091  447  GLN A CD  
3297  O OE1 . GLN A 449  ? 0.2380 0.1853 0.2876 0.0011  0.0046  0.0097  447  GLN A OE1 
3298  N NE2 . GLN A 449  ? 0.2295 0.1783 0.2837 -0.0001 0.0036  0.0096  447  GLN A NE2 
3299  N N   . CYS A 450  ? 0.2111 0.1555 0.2776 0.0017  -0.0017 -0.0032 448  CYS A N   
3300  C CA  . CYS A 450  ? 0.2129 0.1569 0.2785 0.0025  -0.0019 -0.0053 448  CYS A CA  
3301  C C   . CYS A 450  ? 0.2219 0.1684 0.2788 0.0028  -0.0009 -0.0075 448  CYS A C   
3302  O O   . CYS A 450  ? 0.2460 0.1946 0.2985 0.0023  -0.0004 -0.0079 448  CYS A O   
3303  C CB  . CYS A 450  ? 0.2410 0.1847 0.3146 0.0028  -0.0044 -0.0099 448  CYS A CB  
3304  S SG  . CYS A 450  ? 0.2689 0.2167 0.3417 0.0027  -0.0059 -0.0169 448  CYS A SG  
3305  N N   . LEU A 451  ? 0.2089 0.1555 0.2639 0.0036  -0.0007 -0.0088 449  LEU A N   
3306  C CA  . LEU A 451  ? 0.2360 0.1851 0.2833 0.0038  0.0001  -0.0108 449  LEU A CA  
3307  C C   . LEU A 451  ? 0.2362 0.1886 0.2848 0.0039  -0.0014 -0.0167 449  LEU A C   
3308  O O   . LEU A 451  ? 0.2566 0.2086 0.3117 0.0044  -0.0030 -0.0198 449  LEU A O   
3309  C CB  . LEU A 451  ? 0.2613 0.2092 0.3055 0.0045  0.0012  -0.0089 449  LEU A CB  
3310  C CG  . LEU A 451  ? 0.3092 0.2596 0.3461 0.0047  0.0020  -0.0106 449  LEU A CG  
3311  C CD1 . LEU A 451  ? 0.3021 0.2536 0.3326 0.0040  0.0033  -0.0083 449  LEU A CD1 
3312  C CD2 . LEU A 451  ? 0.3244 0.2732 0.3602 0.0055  0.0027  -0.0091 449  LEU A CD2 
3313  N N   . HIS A 452  ? 0.2346 0.1907 0.2775 0.0035  -0.0011 -0.0183 450  HIS A N   
3314  C CA  . HIS A 452  ? 0.2481 0.2087 0.2907 0.0036  -0.0022 -0.0238 450  HIS A CA  
3315  C C   . HIS A 452  ? 0.2581 0.2192 0.3016 0.0046  -0.0025 -0.0263 450  HIS A C   
3316  O O   . HIS A 452  ? 0.2897 0.2490 0.3296 0.0049  -0.0012 -0.0236 450  HIS A O   
3317  C CB  . HIS A 452  ? 0.2395 0.2042 0.2745 0.0029  -0.0014 -0.0236 450  HIS A CB  
3318  C CG  . HIS A 452  ? 0.2286 0.1992 0.2622 0.0030  -0.0023 -0.0286 450  HIS A CG  
3319  N ND1 . HIS A 452  ? 0.2488 0.2237 0.2849 0.0028  -0.0038 -0.0327 450  HIS A ND1 
3320  C CD2 . HIS A 452  ? 0.2634 0.2370 0.2936 0.0034  -0.0019 -0.0304 450  HIS A CD2 
3321  C CE1 . HIS A 452  ? 0.2680 0.2486 0.3020 0.0031  -0.0042 -0.0368 450  HIS A CE1 
3322  N NE2 . HIS A 452  ? 0.2622 0.2421 0.2926 0.0034  -0.0030 -0.0354 450  HIS A NE2 
3323  N N   . GLY A 453  ? 0.3248 0.2884 0.3730 0.0052  -0.0042 -0.0318 451  GLY A N   
3324  C CA  . GLY A 453  ? 0.3211 0.2860 0.3702 0.0063  -0.0045 -0.0350 451  GLY A CA  
3325  C C   . GLY A 453  ? 0.4700 0.4297 0.5236 0.0070  -0.0045 -0.0324 451  GLY A C   
3326  O O   . GLY A 453  ? 0.4533 0.4132 0.5057 0.0078  -0.0042 -0.0332 451  GLY A O   
3327  N N   . MET A 454  ? 0.3134 0.2687 0.3721 0.0067  -0.0049 -0.0292 452  MET A N   
3328  C CA  . MET A 454  ? 0.3099 0.2606 0.3735 0.0072  -0.0051 -0.0262 452  MET A CA  
3329  C C   . MET A 454  ? 0.3206 0.2683 0.3932 0.0069  -0.0068 -0.0254 452  MET A C   
3330  O O   . MET A 454  ? 0.3307 0.2764 0.4116 0.0075  -0.0086 -0.0269 452  MET A O   
3331  C CB  . MET A 454  ? 0.3201 0.2686 0.3776 0.0069  -0.0029 -0.0200 452  MET A CB  
3332  C CG  . MET A 454  ? 0.3340 0.2784 0.3963 0.0072  -0.0030 -0.0159 452  MET A CG  
3333  S SD  . MET A 454  ? 0.4259 0.3700 0.4929 0.0086  -0.0043 -0.0191 452  MET A SD  
3334  C CE  . MET A 454  ? 0.4499 0.3967 0.5064 0.0089  -0.0023 -0.0193 452  MET A CE  
3335  N N   . GLY A 455  ? 0.2945 0.2421 0.3662 0.0059  -0.0063 -0.0231 453  GLY A N   
3336  C CA  . GLY A 455  ? 0.2794 0.2241 0.3594 0.0053  -0.0077 -0.0213 453  GLY A CA  
3337  C C   . GLY A 455  ? 0.3019 0.2482 0.3887 0.0053  -0.0101 -0.0267 453  GLY A C   
3338  O O   . GLY A 455  ? 0.3062 0.2499 0.4016 0.0049  -0.0117 -0.0257 453  GLY A O   
3339  N N   . GLU A 456  ? 0.3043 0.2552 0.3878 0.0057  -0.0106 -0.0324 454  GLU A N   
3340  C CA  . GLU A 456  ? 0.3171 0.2703 0.4065 0.0056  -0.0129 -0.0380 454  GLU A CA  
3341  C C   . GLU A 456  ? 0.3252 0.2763 0.4260 0.0065  -0.0157 -0.0416 454  GLU A C   
3342  O O   . GLU A 456  ? 0.3330 0.2834 0.4414 0.0061  -0.0177 -0.0433 454  GLU A O   
3343  C CB  . GLU A 456  ? 0.3437 0.3034 0.4268 0.0059  -0.0128 -0.0432 454  GLU A CB  
3344  C CG  . GLU A 456  ? 0.4176 0.3796 0.4910 0.0049  -0.0106 -0.0399 454  GLU A CG  
3345  C CD  . GLU A 456  ? 0.4186 0.3818 0.4835 0.0052  -0.0086 -0.0382 454  GLU A CD  
3346  O OE1 . GLU A 456  ? 0.3926 0.3531 0.4590 0.0059  -0.0083 -0.0371 454  GLU A OE1 
3347  O OE2 . GLU A 456  ? 0.3923 0.3594 0.4497 0.0046  -0.0075 -0.0379 454  GLU A OE2 
3348  N N   . PRO A 457  ? 0.3193 0.2695 0.4223 0.0076  -0.0161 -0.0431 455  PRO A N   
3349  C CA  . PRO A 457  ? 0.3406 0.2882 0.4557 0.0085  -0.0191 -0.0463 455  PRO A CA  
3350  C C   . PRO A 457  ? 0.3435 0.2857 0.4668 0.0075  -0.0201 -0.0410 455  PRO A C   
3351  O O   . PRO A 457  ? 0.3485 0.2896 0.4821 0.0075  -0.0229 -0.0440 455  PRO A O   
3352  C CB  . PRO A 457  ? 0.3615 0.3084 0.4760 0.0097  -0.0188 -0.0467 455  PRO A CB  
3353  C CG  . PRO A 457  ? 0.3482 0.2998 0.4510 0.0098  -0.0164 -0.0476 455  PRO A CG  
3354  C CD  . PRO A 457  ? 0.3423 0.2940 0.4376 0.0083  -0.0143 -0.0427 455  PRO A CD  
3355  N N   . LEU A 458  ? 0.3100 0.2495 0.4294 0.0066  -0.0179 -0.0332 456  LEU A N   
3356  C CA  . LEU A 458  ? 0.3009 0.2363 0.4274 0.0055  -0.0185 -0.0275 456  LEU A CA  
3357  C C   . LEU A 458  ? 0.2884 0.2250 0.4162 0.0044  -0.0190 -0.0278 456  LEU A C   
3358  O O   . LEU A 458  ? 0.2906 0.2251 0.4287 0.0038  -0.0213 -0.0280 456  LEU A O   
3359  C CB  . LEU A 458  ? 0.2965 0.2302 0.4172 0.0050  -0.0159 -0.0194 456  LEU A CB  
3360  C CG  . LEU A 458  ? 0.2920 0.2228 0.4185 0.0037  -0.0160 -0.0125 456  LEU A CG  
3361  C CD1 . LEU A 458  ? 0.2647 0.1923 0.4051 0.0037  -0.0192 -0.0128 456  LEU A CD1 
3362  C CD2 . LEU A 458  ? 0.3193 0.2497 0.4391 0.0034  -0.0132 -0.0054 456  LEU A CD2 
3363  N N   . TYR A 459  ? 0.2842 0.2240 0.4021 0.0039  -0.0169 -0.0279 457  TYR A N   
3364  C CA  . TYR A 459  ? 0.2954 0.2361 0.4138 0.0028  -0.0170 -0.0270 457  TYR A CA  
3365  C C   . TYR A 459  ? 0.2897 0.2331 0.4131 0.0030  -0.0196 -0.0344 457  TYR A C   
3366  O O   . TYR A 459  ? 0.3127 0.2562 0.4398 0.0020  -0.0205 -0.0341 457  TYR A O   
3367  C CB  . TYR A 459  ? 0.2601 0.2028 0.3673 0.0022  -0.0140 -0.0232 457  TYR A CB  
3368  C CG  . TYR A 459  ? 0.2494 0.1891 0.3552 0.0017  -0.0121 -0.0154 457  TYR A CG  
3369  C CD1 . TYR A 459  ? 0.2753 0.2133 0.3864 0.0006  -0.0123 -0.0108 457  TYR A CD1 
3370  C CD2 . TYR A 459  ? 0.2826 0.2218 0.3824 0.0023  -0.0102 -0.0127 457  TYR A CD2 
3371  C CE1 . TYR A 459  ? 0.2693 0.2057 0.3794 0.0001  -0.0105 -0.0038 457  TYR A CE1 
3372  C CE2 . TYR A 459  ? 0.2386 0.1759 0.3373 0.0019  -0.0085 -0.0058 457  TYR A CE2 
3373  C CZ  . TYR A 459  ? 0.2759 0.2121 0.3797 0.0008  -0.0087 -0.0014 457  TYR A CZ  
3374  O OH  . TYR A 459  ? 0.2854 0.2208 0.3880 0.0005  -0.0069 0.0054  457  TYR A OH  
3375  N N   . GLU A 460  ? 0.2880 0.2340 0.4120 0.0043  -0.0209 -0.0411 458  GLU A N   
3376  C CA  . GLU A 460  ? 0.3444 0.2929 0.4754 0.0047  -0.0239 -0.0486 458  GLU A CA  
3377  C C   . GLU A 460  ? 0.3402 0.2844 0.4854 0.0046  -0.0269 -0.0489 458  GLU A C   
3378  O O   . GLU A 460  ? 0.3639 0.3095 0.5164 0.0048  -0.0297 -0.0545 458  GLU A O   
3379  C CB  . GLU A 460  ? 0.3929 0.3464 0.5208 0.0062  -0.0244 -0.0561 458  GLU A CB  
3380  C CG  . GLU A 460  ? 0.4608 0.4204 0.5775 0.0060  -0.0226 -0.0578 458  GLU A CG  
3381  C CD  . GLU A 460  ? 0.6354 0.6009 0.7483 0.0073  -0.0228 -0.0644 458  GLU A CD  
3382  O OE1 . GLU A 460  ? 0.6505 0.6149 0.7683 0.0086  -0.0240 -0.0674 458  GLU A OE1 
3383  O OE2 . GLU A 460  ? 0.6643 0.6358 0.7694 0.0071  -0.0219 -0.0666 458  GLU A OE2 
3384  N N   . GLU A 461  ? 0.3169 0.2561 0.4663 0.0043  -0.0266 -0.0428 459  GLU A N   
3385  C CA  . GLU A 461  ? 0.3452 0.2798 0.5080 0.0037  -0.0293 -0.0408 459  GLU A CA  
3386  C C   . GLU A 461  ? 0.3216 0.2543 0.4856 0.0019  -0.0284 -0.0337 459  GLU A C   
3387  O O   . GLU A 461  ? 0.3571 0.2864 0.5323 0.0010  -0.0305 -0.0309 459  GLU A O   
3388  C CB  . GLU A 461  ? 0.3116 0.2424 0.4792 0.0044  -0.0298 -0.0378 459  GLU A CB  
3389  C CG  . GLU A 461  ? 0.3687 0.3014 0.5352 0.0063  -0.0305 -0.0444 459  GLU A CG  
3390  C CD  . GLU A 461  ? 0.4428 0.3773 0.6182 0.0074  -0.0341 -0.0538 459  GLU A CD  
3391  O OE1 . GLU A 461  ? 0.4044 0.3366 0.5910 0.0067  -0.0369 -0.0543 459  GLU A OE1 
3392  O OE2 . GLU A 461  ? 0.4329 0.3717 0.6044 0.0089  -0.0342 -0.0607 459  GLU A OE2 
3393  N N   . VAL A 462  ? 0.3023 0.2375 0.4555 0.0012  -0.0255 -0.0307 460  VAL A N   
3394  C CA  . VAL A 462  ? 0.2752 0.2093 0.4280 -0.0004 -0.0241 -0.0239 460  VAL A CA  
3395  C C   . VAL A 462  ? 0.3074 0.2447 0.4577 -0.0011 -0.0243 -0.0267 460  VAL A C   
3396  O O   . VAL A 462  ? 0.3309 0.2673 0.4887 -0.0022 -0.0257 -0.0254 460  VAL A O   
3397  C CB  . VAL A 462  ? 0.3015 0.2355 0.4443 -0.0006 -0.0205 -0.0169 460  VAL A CB  
3398  C CG1 . VAL A 462  ? 0.2736 0.2076 0.4153 -0.0021 -0.0189 -0.0106 460  VAL A CG1 
3399  C CG2 . VAL A 462  ? 0.2985 0.2294 0.4446 -0.0001 -0.0205 -0.0133 460  VAL A CG2 
3400  N N   . VAL A 463  ? 0.2879 0.2293 0.4281 -0.0004 -0.0229 -0.0305 461  VAL A N   
3401  C CA  . VAL A 463  ? 0.3099 0.2549 0.4465 -0.0010 -0.0228 -0.0327 461  VAL A CA  
3402  C C   . VAL A 463  ? 0.3785 0.3250 0.5241 -0.0008 -0.0264 -0.0399 461  VAL A C   
3403  O O   . VAL A 463  ? 0.3904 0.3375 0.5403 0.0004  -0.0284 -0.0458 461  VAL A O   
3404  C CB  . VAL A 463  ? 0.3193 0.2685 0.4431 -0.0004 -0.0206 -0.0346 461  VAL A CB  
3405  C CG1 . VAL A 463  ? 0.3463 0.2997 0.4664 -0.0010 -0.0208 -0.0367 461  VAL A CG1 
3406  C CG2 . VAL A 463  ? 0.3021 0.2497 0.4176 -0.0005 -0.0174 -0.0279 461  VAL A CG2 
3407  N N   . GLY A 464  ? 0.3771 0.3245 0.5257 -0.0019 -0.0272 -0.0397 462  GLY A N   
3408  C CA  . GLY A 464  ? 0.4072 0.3570 0.5631 -0.0017 -0.0305 -0.0471 462  GLY A CA  
3409  C C   . GLY A 464  ? 0.4016 0.3474 0.5715 -0.0025 -0.0334 -0.0460 462  GLY A C   
3410  O O   . GLY A 464  ? 0.3723 0.3134 0.5484 -0.0029 -0.0335 -0.0413 462  GLY A O   
3411  N N   . ARG A 465  ? 0.3950 0.3430 0.5705 -0.0030 -0.0358 -0.0504 463  ARG A N   
3412  C CA  . ARG A 465  ? 0.4199 0.3644 0.6095 -0.0040 -0.0387 -0.0496 463  ARG A CA  
3413  C C   . ARG A 465  ? 0.4757 0.4168 0.6766 -0.0031 -0.0417 -0.0530 463  ARG A C   
3414  O O   . ARG A 465  ? 0.5152 0.4517 0.7276 -0.0041 -0.0435 -0.0493 463  ARG A O   
3415  C CB  . ARG A 465  ? 0.4594 0.4075 0.6524 -0.0045 -0.0410 -0.0549 463  ARG A CB  
3416  N N   . GLY A 466  ? 0.3923 0.3357 0.5906 -0.0013 -0.0423 -0.0597 464  GLY A N   
3417  C CA  . GLY A 466  ? 0.3907 0.3310 0.5995 -0.0002 -0.0452 -0.0632 464  GLY A CA  
3418  C C   . GLY A 466  ? 0.4497 0.3856 0.6578 -0.0002 -0.0435 -0.0566 464  GLY A C   
3419  O O   . GLY A 466  ? 0.4219 0.3548 0.6392 0.0007  -0.0458 -0.0586 464  GLY A O   
3420  N N   . LYS A 467  ? 0.4055 0.3411 0.6031 -0.0010 -0.0395 -0.0488 465  LYS A N   
3421  C CA  . LYS A 467  ? 0.3535 0.2856 0.5494 -0.0010 -0.0377 -0.0421 465  LYS A CA  
3422  C C   . LYS A 467  ? 0.3872 0.3165 0.5852 -0.0029 -0.0364 -0.0325 465  LYS A C   
3423  O O   . LYS A 467  ? 0.4235 0.3507 0.6327 -0.0041 -0.0388 -0.0313 465  LYS A O   
3424  C CB  . LYS A 467  ? 0.3757 0.3106 0.5575 0.0002  -0.0345 -0.0425 465  LYS A CB  
3425  C CG  . LYS A 467  ? 0.3630 0.3015 0.5433 0.0021  -0.0358 -0.0520 465  LYS A CG  
3426  C CD  . LYS A 467  ? 0.3904 0.3258 0.5812 0.0032  -0.0385 -0.0548 465  LYS A CD  
3427  C CE  . LYS A 467  ? 0.4483 0.3881 0.6364 0.0053  -0.0394 -0.0641 465  LYS A CE  
3428  N NZ  . LYS A 467  ? 0.4152 0.3521 0.6135 0.0066  -0.0420 -0.0671 465  LYS A NZ  
3429  N N   . LEU A 468  ? 0.3638 0.2933 0.5514 -0.0033 -0.0326 -0.0257 466  LEU A N   
3430  C CA  . LEU A 468  ? 0.3342 0.2623 0.5225 -0.0050 -0.0309 -0.0167 466  LEU A CA  
3431  C C   . LEU A 468  ? 0.3592 0.2905 0.5413 -0.0059 -0.0293 -0.0158 466  LEU A C   
3432  O O   . LEU A 468  ? 0.3436 0.2743 0.5269 -0.0073 -0.0281 -0.0090 466  LEU A O   
3433  C CB  . LEU A 468  ? 0.3376 0.2649 0.5188 -0.0048 -0.0279 -0.0100 466  LEU A CB  
3434  C CG  . LEU A 468  ? 0.3537 0.2778 0.5409 -0.0040 -0.0293 -0.0095 466  LEU A CG  
3435  C CD1 . LEU A 468  ? 0.3592 0.2828 0.5404 -0.0041 -0.0264 -0.0017 466  LEU A CD1 
3436  C CD2 . LEU A 468  ? 0.4297 0.3504 0.6334 -0.0048 -0.0333 -0.0093 466  LEU A CD2 
3437  N N   . ASP A 469  ? 0.3558 0.2906 0.5313 -0.0051 -0.0293 -0.0224 467  ASP A N   
3438  C CA  . ASP A 469  ? 0.3181 0.2561 0.4879 -0.0058 -0.0280 -0.0222 467  ASP A CA  
3439  C C   . ASP A 469  ? 0.3108 0.2492 0.4713 -0.0064 -0.0242 -0.0146 467  ASP A C   
3440  O O   . ASP A 469  ? 0.2936 0.2326 0.4548 -0.0076 -0.0235 -0.0104 467  ASP A O   
3441  C CB  . ASP A 469  ? 0.3505 0.2879 0.5311 -0.0071 -0.0308 -0.0230 467  ASP A CB  
3442  C CG  . ASP A 469  ? 0.4074 0.3490 0.5829 -0.0074 -0.0305 -0.0259 467  ASP A CG  
3443  O OD1 . ASP A 469  ? 0.4307 0.3757 0.5961 -0.0064 -0.0292 -0.0298 467  ASP A OD1 
3444  O OD2 . ASP A 469  ? 0.5096 0.4511 0.6912 -0.0088 -0.0315 -0.0239 467  ASP A OD2 
3445  N N   . ARG A 470  ? 0.3218 0.2601 0.4740 -0.0054 -0.0220 -0.0130 468  ARG A N   
3446  C CA  . ARG A 470  ? 0.2778 0.2170 0.4200 -0.0056 -0.0184 -0.0072 468  ARG A CA  
3447  C C   . ARG A 470  ? 0.2875 0.2293 0.4179 -0.0044 -0.0167 -0.0107 468  ARG A C   
3448  O O   . ARG A 470  ? 0.2846 0.2266 0.4140 -0.0034 -0.0175 -0.0153 468  ARG A O   
3449  C CB  . ARG A 470  ? 0.2698 0.2065 0.4134 -0.0057 -0.0171 -0.0007 468  ARG A CB  
3450  C CG  . ARG A 470  ? 0.2442 0.1788 0.3995 -0.0070 -0.0185 0.0042  468  ARG A CG  
3451  C CD  . ARG A 470  ? 0.2867 0.2232 0.4418 -0.0083 -0.0174 0.0084  468  ARG A CD  
3452  N NE  . ARG A 470  ? 0.3249 0.2598 0.4919 -0.0098 -0.0190 0.0130  468  ARG A NE  
3453  C CZ  . ARG A 470  ? 0.3188 0.2529 0.4962 -0.0107 -0.0220 0.0104  468  ARG A CZ  
3454  N NH1 . ARG A 470  ? 0.3349 0.2699 0.5120 -0.0102 -0.0238 0.0029  468  ARG A NH1 
3455  N NH2 . ARG A 470  ? 0.3659 0.2985 0.5543 -0.0122 -0.0234 0.0156  468  ARG A NH2 
3456  N N   . PRO A 471  ? 0.2664 0.2105 0.3882 -0.0046 -0.0145 -0.0086 469  PRO A N   
3457  C CA  . PRO A 471  ? 0.2507 0.1974 0.3617 -0.0037 -0.0131 -0.0116 469  PRO A CA  
3458  C C   . PRO A 471  ? 0.2707 0.2163 0.3753 -0.0029 -0.0109 -0.0088 469  PRO A C   
3459  O O   . PRO A 471  ? 0.2405 0.1839 0.3463 -0.0031 -0.0097 -0.0033 469  PRO A O   
3460  C CB  . PRO A 471  ? 0.2656 0.2146 0.3714 -0.0044 -0.0117 -0.0093 469  PRO A CB  
3461  C CG  . PRO A 471  ? 0.2909 0.2380 0.4017 -0.0052 -0.0109 -0.0031 469  PRO A CG  
3462  C CD  . PRO A 471  ? 0.2519 0.1966 0.3741 -0.0057 -0.0134 -0.0037 469  PRO A CD  
3463  N N   . CYS A 472  ? 0.2477 0.1953 0.3453 -0.0021 -0.0105 -0.0125 470  CYS A N   
3464  C CA  . CYS A 472  ? 0.2288 0.1758 0.3194 -0.0013 -0.0085 -0.0105 470  CYS A CA  
3465  C C   . CYS A 472  ? 0.2396 0.1897 0.3202 -0.0011 -0.0071 -0.0118 470  CYS A C   
3466  O O   . CYS A 472  ? 0.2559 0.2091 0.3353 -0.0011 -0.0084 -0.0167 470  CYS A O   
3467  C CB  . CYS A 472  ? 0.2538 0.1998 0.3475 -0.0005 -0.0098 -0.0140 470  CYS A CB  
3468  S SG  . CYS A 472  ? 0.2702 0.2153 0.3560 0.0005  -0.0075 -0.0115 470  CYS A SG  
3469  N N   . ARG A 473  ? 0.2185 0.1681 0.2923 -0.0009 -0.0048 -0.0076 471  ARG A N   
3470  C CA  . ARG A 473  ? 0.2079 0.1600 0.2726 -0.0007 -0.0036 -0.0082 471  ARG A CA  
3471  C C   . ARG A 473  ? 0.2409 0.1928 0.3011 0.0001  -0.0028 -0.0091 471  ARG A C   
3472  O O   . ARG A 473  ? 0.2362 0.1856 0.2967 0.0005  -0.0018 -0.0060 471  ARG A O   
3473  C CB  . ARG A 473  ? 0.2322 0.1840 0.2927 -0.0010 -0.0017 -0.0033 471  ARG A CB  
3474  C CG  . ARG A 473  ? 0.2356 0.1897 0.2878 -0.0009 -0.0008 -0.0038 471  ARG A CG  
3475  C CD  . ARG A 473  ? 0.2172 0.1710 0.2666 -0.0010 0.0007  0.0004  471  ARG A CD  
3476  N NE  . ARG A 473  ? 0.2212 0.1751 0.2761 -0.0016 0.0000  0.0015  471  ARG A NE  
3477  C CZ  . ARG A 473  ? 0.2649 0.2210 0.3207 -0.0022 -0.0011 -0.0004 471  ARG A CZ  
3478  N NH1 . ARG A 473  ? 0.2471 0.2058 0.2980 -0.0023 -0.0017 -0.0029 471  ARG A NH1 
3479  N NH2 . ARG A 473  ? 0.2396 0.1956 0.3013 -0.0028 -0.0019 0.0004  471  ARG A NH2 
3480  N N   . ILE A 474  ? 0.2141 0.1691 0.2703 0.0002  -0.0033 -0.0130 472  ILE A N   
3481  C CA  . ILE A 474  ? 0.2098 0.1652 0.2619 0.0009  -0.0028 -0.0145 472  ILE A CA  
3482  C C   . ILE A 474  ? 0.2182 0.1742 0.2621 0.0009  -0.0009 -0.0115 472  ILE A C   
3483  O O   . ILE A 474  ? 0.2289 0.1874 0.2687 0.0004  -0.0008 -0.0115 472  ILE A O   
3484  C CB  . ILE A 474  ? 0.2190 0.1785 0.2715 0.0011  -0.0043 -0.0205 472  ILE A CB  
3485  C CG1 . ILE A 474  ? 0.2754 0.2341 0.3370 0.0014  -0.0065 -0.0241 472  ILE A CG1 
3486  C CG2 . ILE A 474  ? 0.2457 0.2065 0.2935 0.0018  -0.0036 -0.0218 472  ILE A CG2 
3487  C CD1 . ILE A 474  ? 0.2862 0.2499 0.3487 0.0016  -0.0082 -0.0306 472  ILE A CD1 
3488  N N   . TYR A 475  ? 0.2233 0.1769 0.2650 0.0014  0.0005  -0.0088 473  TYR A N   
3489  C CA  . TYR A 475  ? 0.2442 0.1981 0.2786 0.0015  0.0020  -0.0064 473  TYR A CA  
3490  C C   . TYR A 475  ? 0.2416 0.1984 0.2720 0.0016  0.0018  -0.0096 473  TYR A C   
3491  O O   . TYR A 475  ? 0.2312 0.1878 0.2630 0.0022  0.0014  -0.0116 473  TYR A O   
3492  C CB  . TYR A 475  ? 0.2547 0.2055 0.2888 0.0022  0.0034  -0.0027 473  TYR A CB  
3493  C CG  . TYR A 475  ? 0.2444 0.1950 0.2719 0.0024  0.0050  0.0000  473  TYR A CG  
3494  C CD1 . TYR A 475  ? 0.2651 0.2153 0.2911 0.0024  0.0059  0.0031  473  TYR A CD1 
3495  C CD2 . TYR A 475  ? 0.3233 0.2744 0.3465 0.0028  0.0054  -0.0009 473  TYR A CD2 
3496  C CE1 . TYR A 475  ? 0.2504 0.2003 0.2711 0.0028  0.0071  0.0050  473  TYR A CE1 
3497  C CE2 . TYR A 475  ? 0.3403 0.2911 0.3582 0.0030  0.0066  0.0013  473  TYR A CE2 
3498  C CZ  . TYR A 475  ? 0.3348 0.2849 0.3516 0.0031  0.0073  0.0041  473  TYR A CZ  
3499  O OH  . TYR A 475  ? 0.3836 0.3334 0.3957 0.0034  0.0083  0.0058  473  TYR A OH  
3500  N N   . ALA A 476  ? 0.2401 0.1999 0.2659 0.0010  0.0017  -0.0099 474  ALA A N   
3501  C CA  . ALA A 476  ? 0.2267 0.1908 0.2496 0.0008  0.0011  -0.0133 474  ALA A CA  
3502  C C   . ALA A 476  ? 0.2199 0.1846 0.2362 0.0006  0.0022  -0.0110 474  ALA A C   
3503  O O   . ALA A 476  ? 0.2213 0.1870 0.2345 0.0000  0.0024  -0.0089 474  ALA A O   
3504  C CB  . ALA A 476  ? 0.2646 0.2328 0.2882 0.0001  -0.0002 -0.0155 474  ALA A CB  
3505  N N   . PRO A 477  ? 0.2355 0.1998 0.2501 0.0011  0.0028  -0.0113 475  PRO A N   
3506  C CA  . PRO A 477  ? 0.2323 0.1973 0.2412 0.0008  0.0036  -0.0093 475  PRO A CA  
3507  C C   . PRO A 477  ? 0.2134 0.1840 0.2193 -0.0002 0.0029  -0.0109 475  PRO A C   
3508  O O   . PRO A 477  ? 0.2297 0.2044 0.2373 -0.0002 0.0019  -0.0146 475  PRO A O   
3509  C CB  . PRO A 477  ? 0.2416 0.2055 0.2503 0.0016  0.0042  -0.0101 475  PRO A CB  
3510  C CG  . PRO A 477  ? 0.2746 0.2357 0.2891 0.0024  0.0038  -0.0111 475  PRO A CG  
3511  C CD  . PRO A 477  ? 0.2339 0.1969 0.2521 0.0020  0.0026  -0.0134 475  PRO A CD  
3512  N N   . VAL A 478  ? 0.2052 0.1764 0.2071 -0.0009 0.0032  -0.0080 476  VAL A N   
3513  C CA  . VAL A 478  ? 0.2349 0.2117 0.2338 -0.0020 0.0025  -0.0083 476  VAL A CA  
3514  C C   . VAL A 478  ? 0.2545 0.2314 0.2494 -0.0025 0.0030  -0.0058 476  VAL A C   
3515  O O   . VAL A 478  ? 0.2820 0.2549 0.2758 -0.0023 0.0036  -0.0027 476  VAL A O   
3516  C CB  . VAL A 478  ? 0.2244 0.2019 0.2235 -0.0028 0.0018  -0.0066 476  VAL A CB  
3517  C CG1 . VAL A 478  ? 0.2364 0.2203 0.2326 -0.0041 0.0009  -0.0064 476  VAL A CG1 
3518  C CG2 . VAL A 478  ? 0.2581 0.2353 0.2618 -0.0024 0.0011  -0.0090 476  VAL A CG2 
3519  N N   . GLY A 479  ? 0.2520 0.2338 0.2449 -0.0030 0.0028  -0.0074 477  GLY A N   
3520  C CA  . GLY A 479  ? 0.2896 0.2717 0.2791 -0.0036 0.0032  -0.0047 477  GLY A CA  
3521  C C   . GLY A 479  ? 0.2861 0.2735 0.2739 -0.0040 0.0032  -0.0069 477  GLY A C   
3522  O O   . GLY A 479  ? 0.2843 0.2748 0.2739 -0.0034 0.0030  -0.0108 477  GLY A O   
3523  N N   . THR A 480  ? 0.3257 0.3144 0.3107 -0.0049 0.0033  -0.0042 478  THR A N   
3524  C CA  . THR A 480  ? 0.3429 0.3371 0.3261 -0.0054 0.0034  -0.0054 478  THR A CA  
3525  C C   . THR A 480  ? 0.3839 0.3749 0.3679 -0.0041 0.0043  -0.0074 478  THR A C   
3526  O O   . THR A 480  ? 0.3908 0.3755 0.3765 -0.0029 0.0048  -0.0072 478  THR A O   
3527  C CB  . THR A 480  ? 0.3632 0.3589 0.3436 -0.0069 0.0031  -0.0013 478  THR A CB  
3528  O OG1 . THR A 480  ? 0.4200 0.4085 0.4005 -0.0064 0.0035  0.0013  478  THR A OG1 
3529  C CG2 . THR A 480  ? 0.3852 0.3844 0.3651 -0.0083 0.0021  0.0011  478  THR A CG2 
3530  N N   . HIS A 481  ? 0.4053 0.4015 0.3882 -0.0043 0.0044  -0.0091 479  HIS A N   
3531  C CA  . HIS A 481  ? 0.4564 0.4503 0.4400 -0.0032 0.0051  -0.0109 479  HIS A CA  
3532  C C   . HIS A 481  ? 0.4596 0.4471 0.4422 -0.0030 0.0057  -0.0075 479  HIS A C   
3533  O O   . HIS A 481  ? 0.4323 0.4149 0.4165 -0.0016 0.0062  -0.0082 479  HIS A O   
3534  C CB  . HIS A 481  ? 0.3850 0.3861 0.3672 -0.0036 0.0052  -0.0128 479  HIS A CB  
3535  C CG  . HIS A 481  ? 0.4283 0.4366 0.4116 -0.0035 0.0047  -0.0169 479  HIS A CG  
3536  N ND1 . HIS A 481  ? 0.4178 0.4344 0.4000 -0.0039 0.0048  -0.0192 479  HIS A ND1 
3537  C CD2 . HIS A 481  ? 0.4228 0.4320 0.4084 -0.0030 0.0041  -0.0195 479  HIS A CD2 
3538  C CE1 . HIS A 481  ? 0.4492 0.4715 0.4328 -0.0035 0.0042  -0.0233 479  HIS A CE1 
3539  N NE2 . HIS A 481  ? 0.4540 0.4717 0.4398 -0.0030 0.0036  -0.0236 479  HIS A NE2 
3540  N N   . GLU A 482  ? 0.4763 0.4640 0.4566 -0.0043 0.0054  -0.0039 480  GLU A N   
3541  C CA  . GLU A 482  ? 0.4875 0.4696 0.4672 -0.0040 0.0057  -0.0012 480  GLU A CA  
3542  C C   . GLU A 482  ? 0.5132 0.4889 0.4945 -0.0028 0.0060  -0.0006 480  GLU A C   
3543  O O   . GLU A 482  ? 0.4966 0.4678 0.4782 -0.0017 0.0066  -0.0003 480  GLU A O   
3544  C CB  . GLU A 482  ? 0.5307 0.5143 0.5087 -0.0057 0.0050  0.0026  480  GLU A CB  
3545  N N   . THR A 483  ? 0.4354 0.4110 0.4176 -0.0030 0.0056  -0.0003 481  THR A N   
3546  C CA  . THR A 483  ? 0.4405 0.4108 0.4244 -0.0020 0.0059  0.0006  481  THR A CA  
3547  C C   . THR A 483  ? 0.4827 0.4507 0.4690 -0.0006 0.0065  -0.0018 481  THR A C   
3548  O O   . THR A 483  ? 0.4506 0.4140 0.4377 0.0005  0.0071  -0.0008 481  THR A O   
3549  C CB  . THR A 483  ? 0.4335 0.4048 0.4181 -0.0027 0.0052  0.0015  481  THR A CB  
3550  O OG1 . THR A 483  ? 0.5323 0.5061 0.5152 -0.0042 0.0044  0.0040  481  THR A OG1 
3551  C CG2 . THR A 483  ? 0.5529 0.5191 0.5392 -0.0017 0.0055  0.0027  481  THR A CG2 
3552  N N   . LEU A 484  ? 0.4146 0.3859 0.4023 -0.0005 0.0063  -0.0049 482  LEU A N   
3553  C CA  . LEU A 484  ? 0.4147 0.3836 0.4058 0.0008  0.0065  -0.0070 482  LEU A CA  
3554  C C   . LEU A 484  ? 0.4204 0.3873 0.4115 0.0018  0.0071  -0.0072 482  LEU A C   
3555  O O   . LEU A 484  ? 0.4402 0.4034 0.4336 0.0029  0.0074  -0.0070 482  LEU A O   
3556  C CB  . LEU A 484  ? 0.4226 0.3957 0.4162 0.0008  0.0058  -0.0108 482  LEU A CB  
3557  C CG  . LEU A 484  ? 0.4501 0.4290 0.4426 0.0006  0.0055  -0.0136 482  LEU A CG  
3558  C CD1 . LEU A 484  ? 0.4747 0.4524 0.4697 0.0019  0.0057  -0.0161 482  LEU A CD1 
3559  C CD2 . LEU A 484  ? 0.4453 0.4300 0.4386 0.0000  0.0047  -0.0164 482  LEU A CD2 
3560  N N   . LEU A 485  ? 0.4534 0.4229 0.4419 0.0013  0.0072  -0.0073 483  LEU A N   
3561  C CA  . LEU A 485  ? 0.4246 0.3926 0.4131 0.0022  0.0077  -0.0077 483  LEU A CA  
3562  C C   . LEU A 485  ? 0.4571 0.4202 0.4444 0.0027  0.0083  -0.0047 483  LEU A C   
3563  O O   . LEU A 485  ? 0.4843 0.4455 0.4724 0.0037  0.0087  -0.0047 483  LEU A O   
3564  C CB  . LEU A 485  ? 0.4370 0.4096 0.4233 0.0014  0.0076  -0.0085 483  LEU A CB  
3565  C CG  . LEU A 485  ? 0.4402 0.4184 0.4278 0.0014  0.0072  -0.0123 483  LEU A CG  
3566  C CD1 . LEU A 485  ? 0.4442 0.4278 0.4291 0.0003  0.0073  -0.0124 483  LEU A CD1 
3567  C CD2 . LEU A 485  ? 0.4156 0.3924 0.4070 0.0029  0.0071  -0.0153 483  LEU A CD2 
3568  N N   . ALA A 486  ? 0.4805 0.4422 0.4665 0.0022  0.0082  -0.0023 484  ALA A N   
3569  C CA  . ALA A 486  ? 0.4774 0.4354 0.4620 0.0027  0.0086  0.0000  484  ALA A CA  
3570  C C   . ALA A 486  ? 0.4870 0.4419 0.4737 0.0041  0.0093  0.0003  484  ALA A C   
3571  O O   . ALA A 486  ? 0.5077 0.4609 0.4935 0.0049  0.0097  0.0011  484  ALA A O   
3572  C CB  . ALA A 486  ? 0.4836 0.4409 0.4674 0.0020  0.0083  0.0021  484  ALA A CB  
3573  N N   . TYR A 487  ? 0.4998 0.4540 0.4893 0.0044  0.0092  -0.0001 485  TYR A N   
3574  C CA  . TYR A 487  ? 0.5263 0.4779 0.5182 0.0055  0.0097  0.0008  485  TYR A CA  
3575  C C   . TYR A 487  ? 0.4912 0.4433 0.4874 0.0058  0.0093  -0.0011 485  TYR A C   
3576  O O   . TYR A 487  ? 0.4192 0.3695 0.4186 0.0063  0.0094  -0.0001 485  TYR A O   
3577  C CB  . TYR A 487  ? 0.5828 0.5327 0.5750 0.0058  0.0101  0.0030  485  TYR A CB  
3578  C CG  . TYR A 487  ? 0.6068 0.5561 0.5957 0.0058  0.0103  0.0044  485  TYR A CG  
3579  C CD1 . TYR A 487  ? 0.6302 0.5784 0.6176 0.0067  0.0109  0.0054  485  TYR A CD1 
3580  C CD2 . TYR A 487  ? 0.5705 0.5206 0.5581 0.0048  0.0098  0.0047  485  TYR A CD2 
3581  C CE1 . TYR A 487  ? 0.6796 0.6274 0.6646 0.0068  0.0108  0.0061  485  TYR A CE1 
3582  C CE2 . TYR A 487  ? 0.6213 0.5705 0.6067 0.0049  0.0097  0.0059  485  TYR A CE2 
3583  C CZ  . TYR A 487  ? 0.7205 0.6686 0.7048 0.0059  0.0101  0.0063  485  TYR A CZ  
3584  O OH  . TYR A 487  ? 0.7011 0.6484 0.6840 0.0061  0.0098  0.0070  485  TYR A OH  
3585  N N   . LEU A 488  ? 0.4854 0.4401 0.4819 0.0055  0.0087  -0.0038 486  LEU A N   
3586  C CA  . LEU A 488  ? 0.4083 0.3634 0.4094 0.0060  0.0081  -0.0063 486  LEU A CA  
3587  C C   . LEU A 488  ? 0.3839 0.3365 0.3877 0.0071  0.0082  -0.0055 486  LEU A C   
3588  O O   . LEU A 488  ? 0.3622 0.3137 0.3711 0.0076  0.0076  -0.0061 486  LEU A O   
3589  C CB  . LEU A 488  ? 0.4212 0.3806 0.4220 0.0056  0.0075  -0.0098 486  LEU A CB  
3590  C CG  . LEU A 488  ? 0.4964 0.4569 0.5024 0.0061  0.0065  -0.0134 486  LEU A CG  
3591  C CD1 . LEU A 488  ? 0.4624 0.4216 0.4717 0.0059  0.0060  -0.0132 486  LEU A CD1 
3592  C CD2 . LEU A 488  ? 0.3686 0.3345 0.3737 0.0058  0.0060  -0.0171 486  LEU A CD2 
3593  N N   . VAL A 489  ? 0.4579 0.4098 0.4589 0.0075  0.0088  -0.0039 487  VAL A N   
3594  C CA  . VAL A 489  ? 0.3983 0.3484 0.4016 0.0086  0.0089  -0.0028 487  VAL A CA  
3595  C C   . VAL A 489  ? 0.4109 0.3587 0.4171 0.0089  0.0091  0.0001  487  VAL A C   
3596  O O   . VAL A 489  ? 0.3851 0.3317 0.3963 0.0094  0.0086  0.0004  487  VAL A O   
3597  C CB  . VAL A 489  ? 0.4667 0.4168 0.4659 0.0089  0.0095  -0.0016 487  VAL A CB  
3598  C CG1 . VAL A 489  ? 0.4702 0.4186 0.4715 0.0100  0.0097  0.0005  487  VAL A CG1 
3599  C CG2 . VAL A 489  ? 0.4528 0.4056 0.4506 0.0086  0.0092  -0.0043 487  VAL A CG2 
3600  N N   . ARG A 490  ? 0.4355 0.3827 0.4390 0.0086  0.0099  0.0023  488  ARG A N   
3601  C CA  . ARG A 490  ? 0.4798 0.4256 0.4859 0.0088  0.0102  0.0051  488  ARG A CA  
3602  C C   . ARG A 490  ? 0.4495 0.3949 0.4610 0.0084  0.0093  0.0041  488  ARG A C   
3603  O O   . ARG A 490  ? 0.4600 0.4043 0.4761 0.0087  0.0091  0.0060  488  ARG A O   
3604  C CB  . ARG A 490  ? 0.5144 0.4603 0.5168 0.0087  0.0111  0.0070  488  ARG A CB  
3605  C CG  . ARG A 490  ? 0.4664 0.4119 0.4711 0.0091  0.0117  0.0101  488  ARG A CG  
3606  C CD  . ARG A 490  ? 0.4718 0.4178 0.4733 0.0091  0.0125  0.0113  488  ARG A CD  
3607  N NE  . ARG A 490  ? 0.5431 0.4891 0.5448 0.0082  0.0120  0.0100  488  ARG A NE  
3608  C CZ  . ARG A 490  ? 0.4891 0.4356 0.4875 0.0078  0.0120  0.0091  488  ARG A CZ  
3609  N NH1 . ARG A 490  ? 0.4577 0.4043 0.4523 0.0082  0.0123  0.0093  488  ARG A NH1 
3610  N NH2 . ARG A 490  ? 0.4943 0.4411 0.4933 0.0070  0.0114  0.0082  488  ARG A NH2 
3611  N N   . ARG A 491  ? 0.4531 0.3998 0.4643 0.0077  0.0087  0.0013  489  ARG A N   
3612  C CA  . ARG A 491  ? 0.4583 0.4050 0.4747 0.0073  0.0078  -0.0001 489  ARG A CA  
3613  C C   . ARG A 491  ? 0.5686 0.5148 0.5905 0.0079  0.0066  -0.0021 489  ARG A C   
3614  O O   . ARG A 491  ? 0.4867 0.4317 0.5146 0.0079  0.0057  -0.0020 489  ARG A O   
3615  C CB  . ARG A 491  ? 0.5566 0.5055 0.5709 0.0065  0.0073  -0.0028 489  ARG A CB  
3616  N N   . LEU A 492  ? 0.4739 0.4210 0.4945 0.0084  0.0065  -0.0040 490  LEU A N   
3617  C CA  . LEU A 492  ? 0.5046 0.4513 0.5309 0.0091  0.0052  -0.0062 490  LEU A CA  
3618  C C   . LEU A 492  ? 0.5583 0.5023 0.5886 0.0097  0.0051  -0.0026 490  LEU A C   
3619  O O   . LEU A 492  ? 0.4693 0.4120 0.5067 0.0100  0.0037  -0.0031 490  LEU A O   
3620  C CB  . LEU A 492  ? 0.4842 0.4332 0.5080 0.0095  0.0051  -0.0093 490  LEU A CB  
3621  C CG  . LEU A 492  ? 0.4873 0.4402 0.5085 0.0089  0.0049  -0.0133 490  LEU A CG  
3622  C CD1 . LEU A 492  ? 0.4908 0.4464 0.5086 0.0092  0.0052  -0.0153 490  LEU A CD1 
3623  C CD2 . LEU A 492  ? 0.5334 0.4874 0.5605 0.0090  0.0034  -0.0171 490  LEU A CD2 
3624  N N   . LEU A 493  ? 0.4690 0.4125 0.4951 0.0099  0.0064  0.0011  491  LEU A N   
3625  C CA  . LEU A 493  ? 0.3987 0.3407 0.4282 0.0104  0.0063  0.0050  491  LEU A CA  
3626  C C   . LEU A 493  ? 0.5141 0.4549 0.5485 0.0099  0.0060  0.0078  491  LEU A C   
3627  O O   . LEU A 493  ? 0.5262 0.4660 0.5658 0.0102  0.0055  0.0107  491  LEU A O   
3628  C CB  . LEU A 493  ? 0.4931 0.4358 0.5167 0.0108  0.0078  0.0079  491  LEU A CB  
3629  C CG  . LEU A 493  ? 0.5220 0.4656 0.5417 0.0113  0.0080  0.0061  491  LEU A CG  
3630  C CD1 . LEU A 493  ? 0.5559 0.5001 0.5705 0.0117  0.0092  0.0092  491  LEU A CD1 
3631  C CD2 . LEU A 493  ? 0.5314 0.4744 0.5564 0.0120  0.0067  0.0049  491  LEU A CD2 
3632  N N   . GLU A 494  ? 0.5501 0.4913 0.5832 0.0092  0.0064  0.0072  492  GLU A N   
3633  C CA  . GLU A 494  ? 0.5835 0.5240 0.6215 0.0086  0.0061  0.0098  492  GLU A CA  
3634  C C   . GLU A 494  ? 0.5578 0.4966 0.6047 0.0086  0.0042  0.0089  492  GLU A C   
3635  O O   . GLU A 494  ? 0.4835 0.4213 0.5359 0.0084  0.0037  0.0126  492  GLU A O   
3636  C CB  . GLU A 494  ? 0.4755 0.4167 0.5112 0.0079  0.0065  0.0084  492  GLU A CB  
3637  C CG  . GLU A 494  ? 0.4682 0.4107 0.4963 0.0078  0.0081  0.0096  492  GLU A CG  
3638  C CD  . GLU A 494  ? 0.4897 0.4330 0.5158 0.0071  0.0081  0.0075  492  GLU A CD  
3639  O OE1 . GLU A 494  ? 0.5293 0.4726 0.5598 0.0066  0.0069  0.0055  492  GLU A OE1 
3640  O OE2 . GLU A 494  ? 0.6135 0.5577 0.6338 0.0071  0.0091  0.0079  492  GLU A OE2 
3641  N N   . ASN A 495  ? 0.5308 0.4698 0.5796 0.0089  0.0029  0.0039  493  ASN A N   
3642  C CA  . ASN A 495  ? 0.5208 0.4584 0.5787 0.0091  0.0007  0.0018  493  ASN A CA  
3643  C C   . ASN A 495  ? 0.5181 0.4556 0.5781 0.0101  -0.0003 -0.0007 493  ASN A C   
3644  O O   . ASN A 495  ? 0.5306 0.4672 0.5981 0.0105  -0.0023 -0.0038 493  ASN A O   
3645  C CB  . ASN A 495  ? 0.4763 0.4148 0.5364 0.0086  -0.0003 -0.0028 493  ASN A CB  
3646  C CG  . ASN A 495  ? 0.4541 0.3930 0.5121 0.0076  0.0006  -0.0006 493  ASN A CG  
3647  O OD1 . ASN A 495  ? 0.4239 0.3613 0.4867 0.0071  0.0003  0.0030  493  ASN A OD1 
3648  N ND2 . ASN A 495  ? 0.4004 0.3413 0.4514 0.0073  0.0016  -0.0025 493  ASN A ND2 
3649  N N   . GLY A 496  ? 0.5977 0.5360 0.6517 0.0106  0.0010  0.0004  494  GLY A N   
3650  C CA  . GLY A 496  ? 0.5464 0.4849 0.6018 0.0116  0.0001  -0.0021 494  GLY A CA  
3651  C C   . GLY A 496  ? 0.6119 0.5494 0.6679 0.0122  0.0004  0.0021  494  GLY A C   
3652  O O   . GLY A 496  ? 0.5964 0.5338 0.6543 0.0131  -0.0005 0.0003  494  GLY A O   
3653  N N   . ALA A 497  ? 0.5542 0.4912 0.6083 0.0118  0.0015  0.0076  495  ALA A N   
3654  C CA  . ALA A 497  ? 0.5577 0.4945 0.6126 0.0123  0.0016  0.0121  495  ALA A CA  
3655  C C   . ALA A 497  ? 0.5030 0.4377 0.5683 0.0124  -0.0005 0.0140  495  ALA A C   
3656  O O   . ALA A 497  ? 0.5037 0.4370 0.5756 0.0119  -0.0019 0.0130  495  ALA A O   
3657  C CB  . ALA A 497  ? 0.4926 0.4306 0.5425 0.0118  0.0035  0.0173  495  ALA A CB  
3658  N N   . ASN A 498  ? 0.5242 0.4588 0.5915 0.0131  -0.0010 0.0169  496  ASN A N   
3659  C CA  . ASN A 498  ? 0.5163 0.4488 0.5942 0.0133  -0.0034 0.0188  496  ASN A CA  
3660  C C   . ASN A 498  ? 0.4529 0.3846 0.5367 0.0122  -0.0039 0.0235  496  ASN A C   
3661  O O   . ASN A 498  ? 0.4671 0.3965 0.5609 0.0120  -0.0062 0.0237  496  ASN A O   
3662  C CB  . ASN A 498  ? 0.5521 0.4851 0.6305 0.0141  -0.0036 0.0221  496  ASN A CB  
3663  N N   . SER A 499  ? 0.4698 0.4035 0.5478 0.0115  -0.0018 0.0274  497  SER A N   
3664  C CA  . SER A 499  ? 0.4753 0.4089 0.5580 0.0103  -0.0020 0.0320  497  SER A CA  
3665  C C   . SER A 499  ? 0.3667 0.2994 0.4508 0.0096  -0.0022 0.0284  497  SER A C   
3666  O O   . SER A 499  ? 0.4062 0.3384 0.4960 0.0086  -0.0028 0.0315  497  SER A O   
3667  C CB  . SER A 499  ? 0.4543 0.3913 0.5304 0.0100  0.0004  0.0375  497  SER A CB  
3668  O OG  . SER A 499  ? 0.5403 0.4789 0.6060 0.0104  0.0024  0.0345  497  SER A OG  
3669  N N   . SER A 500  ? 0.3712 0.3038 0.4504 0.0100  -0.0018 0.0221  498  SER A N   
3670  C CA  . SER A 500  ? 0.3384 0.2709 0.4178 0.0093  -0.0019 0.0187  498  SER A CA  
3671  C C   . SER A 500  ? 0.3963 0.3263 0.4863 0.0092  -0.0047 0.0160  498  SER A C   
3672  O O   . SER A 500  ? 0.3881 0.3169 0.4833 0.0100  -0.0065 0.0131  498  SER A O   
3673  C CB  . SER A 500  ? 0.4151 0.3489 0.4863 0.0097  -0.0008 0.0131  498  SER A CB  
3674  O OG  . SER A 500  ? 0.4607 0.3963 0.5225 0.0097  0.0016  0.0154  498  SER A OG  
3675  N N   . PHE A 501  ? 0.3266 0.2563 0.4205 0.0081  -0.0051 0.0166  499  PHE A N   
3676  C CA  . PHE A 501  ? 0.3266 0.2541 0.4311 0.0079  -0.0079 0.0138  499  PHE A CA  
3677  C C   . PHE A 501  ? 0.4032 0.3309 0.5078 0.0089  -0.0091 0.0057  499  PHE A C   
3678  O O   . PHE A 501  ? 0.3728 0.2988 0.4863 0.0095  -0.0117 0.0027  499  PHE A O   
3679  C CB  . PHE A 501  ? 0.3195 0.2472 0.4260 0.0066  -0.0079 0.0148  499  PHE A CB  
3680  C CG  . PHE A 501  ? 0.3163 0.2420 0.4336 0.0064  -0.0109 0.0111  499  PHE A CG  
3681  C CD1 . PHE A 501  ? 0.3239 0.2472 0.4525 0.0058  -0.0130 0.0151  499  PHE A CD1 
3682  C CD2 . PHE A 501  ? 0.3398 0.2662 0.4564 0.0068  -0.0116 0.0038  499  PHE A CD2 
3683  C CE1 . PHE A 501  ? 0.3256 0.2468 0.4649 0.0056  -0.0160 0.0114  499  PHE A CE1 
3684  C CE2 . PHE A 501  ? 0.3349 0.2597 0.4616 0.0067  -0.0146 -0.0001 499  PHE A CE2 
3685  C CZ  . PHE A 501  ? 0.3628 0.2849 0.5012 0.0061  -0.0168 0.0036  499  PHE A CZ  
3686  N N   . VAL A 502  ? 0.3878 0.3178 0.4830 0.0091  -0.0074 0.0020  500  VAL A N   
3687  C CA  . VAL A 502  ? 0.4149 0.3463 0.5100 0.0099  -0.0084 -0.0056 500  VAL A CA  
3688  C C   . VAL A 502  ? 0.3928 0.3241 0.4890 0.0112  -0.0091 -0.0077 500  VAL A C   
3689  O O   . VAL A 502  ? 0.5074 0.4389 0.6091 0.0121  -0.0111 -0.0134 500  VAL A O   
3690  C CB  . VAL A 502  ? 0.4044 0.3388 0.4893 0.0095  -0.0064 -0.0081 500  VAL A CB  
3691  C CG1 . VAL A 502  ? 0.5892 0.5263 0.6726 0.0104  -0.0072 -0.0153 500  VAL A CG1 
3692  C CG2 . VAL A 502  ? 0.4006 0.3352 0.4863 0.0084  -0.0064 -0.0072 500  VAL A CG2 
3693  N N   . HIS A 503  ? 0.3628 0.2940 0.4539 0.0114  -0.0076 -0.0034 501  HIS A N   
3694  C CA  . HIS A 503  ? 0.3792 0.3101 0.4724 0.0127  -0.0085 -0.0046 501  HIS A CA  
3695  C C   . HIS A 503  ? 0.4375 0.3654 0.5432 0.0130  -0.0113 -0.0036 501  HIS A C   
3696  O O   . HIS A 503  ? 0.4200 0.3476 0.5316 0.0142  -0.0133 -0.0083 501  HIS A O   
3697  C CB  . HIS A 503  ? 0.4293 0.3608 0.5151 0.0127  -0.0064 0.0003  501  HIS A CB  
3698  C CG  . HIS A 503  ? 0.5310 0.4622 0.6187 0.0140  -0.0072 -0.0002 501  HIS A CG  
3699  N ND1 . HIS A 503  ? 0.4961 0.4253 0.5910 0.0142  -0.0086 0.0041  501  HIS A ND1 
3700  C CD2 . HIS A 503  ? 0.5265 0.4596 0.6102 0.0149  -0.0068 -0.0044 501  HIS A CD2 
3701  C CE1 . HIS A 503  ? 0.5008 0.4303 0.5959 0.0154  -0.0091 0.0025  501  HIS A CE1 
3702  N NE2 . HIS A 503  ? 0.4973 0.4292 0.5856 0.0159  -0.0080 -0.0028 501  HIS A NE2 
3703  N N   . ARG A 504  ? 0.3630 0.2890 0.4735 0.0120  -0.0117 0.0025  502  ARG A N   
3704  C CA  . ARG A 504  ? 0.4054 0.3284 0.5282 0.0121  -0.0145 0.0048  502  ARG A CA  
3705  C C   . ARG A 504  ? 0.4218 0.3434 0.5546 0.0124  -0.0174 -0.0011 502  ARG A C   
3706  O O   . ARG A 504  ? 0.4057 0.3252 0.5485 0.0132  -0.0202 -0.0028 502  ARG A O   
3707  C CB  . ARG A 504  ? 0.3977 0.3199 0.5227 0.0108  -0.0140 0.0134  502  ARG A CB  
3708  C CG  . ARG A 504  ? 0.4354 0.3595 0.5526 0.0109  -0.0117 0.0191  502  ARG A CG  
3709  C CD  . ARG A 504  ? 0.4378 0.3630 0.5532 0.0095  -0.0101 0.0265  502  ARG A CD  
3710  N NE  . ARG A 504  ? 0.4610 0.3843 0.5881 0.0085  -0.0124 0.0305  502  ARG A NE  
3711  C CZ  . ARG A 504  ? 0.4880 0.4101 0.6236 0.0085  -0.0143 0.0352  502  ARG A CZ  
3712  N NH1 . ARG A 504  ? 0.5092 0.4316 0.6430 0.0095  -0.0143 0.0363  502  ARG A NH1 
3713  N NH2 . ARG A 504  ? 0.4893 0.4098 0.6358 0.0073  -0.0164 0.0392  502  ARG A NH2 
3714  N N   . ILE A 505  ? 0.4240 0.3467 0.5545 0.0117  -0.0170 -0.0044 503  ILE A N   
3715  C CA  . ILE A 505  ? 0.3968 0.3188 0.5365 0.0121  -0.0198 -0.0107 503  ILE A CA  
3716  C C   . ILE A 505  ? 0.4736 0.3971 0.6145 0.0139  -0.0211 -0.0184 503  ILE A C   
3717  O O   . ILE A 505  ? 0.4854 0.4075 0.6370 0.0147  -0.0242 -0.0230 503  ILE A O   
3718  C CB  . ILE A 505  ? 0.4954 0.4190 0.6315 0.0110  -0.0190 -0.0128 503  ILE A CB  
3719  C CG1 . ILE A 505  ? 0.5482 0.4713 0.6946 0.0114  -0.0222 -0.0192 503  ILE A CG1 
3720  C CG2 . ILE A 505  ? 0.4732 0.4008 0.5969 0.0113  -0.0165 -0.0164 503  ILE A CG2 
3721  C CD1 . ILE A 505  ? 0.4135 0.3339 0.5686 0.0100  -0.0238 -0.0155 503  ILE A CD1 
3722  N N   . ASN A 506  ? 0.4459 0.3723 0.5763 0.0145  -0.0188 -0.0200 504  ASN A N   
3723  C CA  . ASN A 506  ? 0.4473 0.3760 0.5777 0.0162  -0.0196 -0.0270 504  ASN A CA  
3724  C C   . ASN A 506  ? 0.4866 0.4134 0.6217 0.0173  -0.0207 -0.0252 504  ASN A C   
3725  O O   . ASN A 506  ? 0.5644 0.4931 0.7000 0.0188  -0.0214 -0.0307 504  ASN A O   
3726  C CB  . ASN A 506  ? 0.5029 0.4361 0.6203 0.0162  -0.0167 -0.0295 504  ASN A CB  
3727  C CG  . ASN A 506  ? 0.5055 0.4414 0.6189 0.0154  -0.0161 -0.0326 504  ASN A CG  
3728  O OD1 . ASN A 506  ? 0.6066 0.5425 0.7273 0.0155  -0.0182 -0.0369 504  ASN A OD1 
3729  N ND2 . ASN A 506  ? 0.6136 0.5518 0.7157 0.0145  -0.0132 -0.0305 504  ASN A ND2 
3730  N N   . ASP A 507  ? 0.4489 0.3725 0.5873 0.0166  -0.0208 -0.0174 505  ASP A N   
3731  C CA  . ASP A 507  ? 0.4734 0.3953 0.6164 0.0176  -0.0220 -0.0150 505  ASP A CA  
3732  C C   . ASP A 507  ? 0.5142 0.4325 0.6726 0.0181  -0.0259 -0.0159 505  ASP A C   
3733  O O   . ASP A 507  ? 0.4631 0.3787 0.6281 0.0168  -0.0270 -0.0106 505  ASP A O   
3734  C CB  . ASP A 507  ? 0.4542 0.3753 0.5920 0.0166  -0.0200 -0.0059 505  ASP A CB  
3735  C CG  . ASP A 507  ? 0.5605 0.4807 0.7012 0.0177  -0.0209 -0.0032 505  ASP A CG  
3736  O OD1 . ASP A 507  ? 0.5659 0.4847 0.7161 0.0190  -0.0237 -0.0072 505  ASP A OD1 
3737  O OD2 . ASP A 507  ? 0.5112 0.4323 0.6452 0.0173  -0.0189 0.0027  505  ASP A OD2 
3738  N N   . PRO A 508  ? 0.5554 0.4738 0.7208 0.0199  -0.0283 -0.0223 506  PRO A N   
3739  C CA  . PRO A 508  ? 0.5582 0.4730 0.7396 0.0205  -0.0325 -0.0236 506  PRO A CA  
3740  C C   . PRO A 508  ? 0.5017 0.4128 0.6902 0.0199  -0.0338 -0.0148 506  PRO A C   
3741  O O   . PRO A 508  ? 0.5901 0.4976 0.7919 0.0196  -0.0371 -0.0133 506  PRO A O   
3742  C CB  . PRO A 508  ? 0.5778 0.4944 0.7630 0.0228  -0.0343 -0.0326 506  PRO A CB  
3743  C CG  . PRO A 508  ? 0.6268 0.5487 0.7977 0.0232  -0.0309 -0.0366 506  PRO A CG  
3744  C CD  . PRO A 508  ? 0.5227 0.4447 0.6821 0.0215  -0.0274 -0.0286 506  PRO A CD  
3745  N N   . LYS A 509  ? 0.4737 0.3856 0.6540 0.0196  -0.0314 -0.0088 507  LYS A N   
3746  C CA  . LYS A 509  ? 0.5045 0.4140 0.6906 0.0189  -0.0324 0.0002  507  LYS A CA  
3747  C C   . LYS A 509  ? 0.5143 0.4228 0.7008 0.0167  -0.0317 0.0081  507  LYS A C   
3748  O O   . LYS A 509  ? 0.5319 0.4387 0.7252 0.0159  -0.0330 0.0159  507  LYS A O   
3749  C CB  . LYS A 509  ? 0.5798 0.4913 0.7564 0.0195  -0.0301 0.0037  507  LYS A CB  
3750  N N   . VAL A 510  ? 0.4813 0.3914 0.6611 0.0157  -0.0297 0.0064  508  VAL A N   
3751  C CA  . VAL A 510  ? 0.4468 0.3566 0.6266 0.0136  -0.0288 0.0134  508  VAL A CA  
3752  C C   . VAL A 510  ? 0.3720 0.2792 0.5640 0.0130  -0.0319 0.0107  508  VAL A C   
3753  O O   . VAL A 510  ? 0.4334 0.3412 0.6249 0.0136  -0.0323 0.0027  508  VAL A O   
3754  C CB  . VAL A 510  ? 0.4594 0.3726 0.6243 0.0128  -0.0247 0.0137  508  VAL A CB  
3755  C CG1 . VAL A 510  ? 0.4234 0.3368 0.5887 0.0108  -0.0238 0.0208  508  VAL A CG1 
3756  C CG2 . VAL A 510  ? 0.4327 0.3485 0.5861 0.0135  -0.0219 0.0156  508  VAL A CG2 
3757  N N   . SER A 511  ? 0.3763 0.2811 0.5793 0.0118  -0.0341 0.0174  509  SER A N   
3758  C CA  . SER A 511  ? 0.3719 0.2769 0.5851 0.0108  -0.0370 0.0150  509  SER A CA  
3759  C C   . SER A 511  ? 0.3771 0.2822 0.5870 0.0093  -0.0354 0.0165  509  SER A C   
3760  O O   . SER A 511  ? 0.4170 0.3230 0.6175 0.0086  -0.0321 0.0214  509  SER A O   
3761  C CB  . SER A 511  ? 0.4607 0.3665 0.6846 0.0095  -0.0396 0.0216  509  SER A CB  
3762  O OG  . SER A 511  ? 0.4446 0.3517 0.6654 0.0077  -0.0377 0.0317  509  SER A OG  
3763  N N   . ILE A 512  ? 0.3903 0.2956 0.6080 0.0087  -0.0377 0.0122  510  ILE A N   
3764  C CA  . ILE A 512  ? 0.3768 0.2823 0.5929 0.0071  -0.0366 0.0138  510  ILE A CA  
3765  C C   . ILE A 512  ? 0.4336 0.3403 0.6512 0.0050  -0.0358 0.0247  510  ILE A C   
3766  O O   . ILE A 512  ? 0.4185 0.3258 0.6296 0.0039  -0.0331 0.0288  510  ILE A O   
3767  C CB  . ILE A 512  ? 0.3923 0.2981 0.6172 0.0071  -0.0397 0.0067  510  ILE A CB  
3768  C CG1 . ILE A 512  ? 0.3990 0.3049 0.6205 0.0092  -0.0399 -0.0043 510  ILE A CG1 
3769  C CG2 . ILE A 512  ? 0.4181 0.3242 0.6426 0.0053  -0.0388 0.0090  510  ILE A CG2 
3770  C CD1 . ILE A 512  ? 0.4978 0.4048 0.7277 0.0095  -0.0430 -0.0121 510  ILE A CD1 
3771  N N   . ASP A 513  ? 0.4347 0.3422 0.6608 0.0044  -0.0380 0.0296  511  ASP A N   
3772  C CA  . ASP A 513  ? 0.4182 0.3279 0.6457 0.0024  -0.0372 0.0402  511  ASP A CA  
3773  C C   . ASP A 513  ? 0.4169 0.3277 0.6321 0.0024  -0.0332 0.0458  511  ASP A C   
3774  O O   . ASP A 513  ? 0.4199 0.3328 0.6317 0.0009  -0.0312 0.0526  511  ASP A O   
3775  C CB  . ASP A 513  ? 0.4982 0.4089 0.7366 0.0019  -0.0402 0.0442  511  ASP A CB  
3776  C CG  . ASP A 513  ? 0.5317 0.4421 0.7836 0.0014  -0.0443 0.0401  511  ASP A CG  
3777  O OD1 . ASP A 513  ? 0.5737 0.4842 0.8276 0.0004  -0.0445 0.0390  511  ASP A OD1 
3778  O OD2 . ASP A 513  ? 0.6680 0.5780 0.9286 0.0022  -0.0474 0.0380  511  ASP A OD2 
3779  N N   . GLU A 514  ? 0.3811 0.2907 0.5897 0.0043  -0.0321 0.0430  512  GLU A N   
3780  C CA  . GLU A 514  ? 0.4235 0.3340 0.6203 0.0046  -0.0284 0.0475  512  GLU A CA  
3781  C C   . GLU A 514  ? 0.4038 0.3166 0.5895 0.0043  -0.0253 0.0444  512  GLU A C   
3782  O O   . GLU A 514  ? 0.4129 0.3292 0.5899 0.0034  -0.0222 0.0497  512  GLU A O   
3783  C CB  . GLU A 514  ? 0.4535 0.3639 0.6448 0.0066  -0.0279 0.0439  512  GLU A CB  
3784  C CG  . GLU A 514  ? 0.5378 0.4483 0.7366 0.0068  -0.0301 0.0486  512  GLU A CG  
3785  C CD  . GLU A 514  ? 0.5895 0.4983 0.7864 0.0091  -0.0307 0.0433  512  GLU A CD  
3786  O OE1 . GLU A 514  ? 0.5707 0.4775 0.7686 0.0104  -0.0316 0.0342  512  GLU A OE1 
3787  O OE2 . GLU A 514  ? 0.6948 0.6049 0.8894 0.0095  -0.0301 0.0482  512  GLU A OE2 
3788  N N   . LEU A 515  ? 0.4083 0.3196 0.5943 0.0049  -0.0261 0.0357  513  LEU A N   
3789  C CA  . LEU A 515  ? 0.3498 0.2635 0.5250 0.0046  -0.0233 0.0324  513  LEU A CA  
3790  C C   . LEU A 515  ? 0.3597 0.2740 0.5384 0.0027  -0.0231 0.0369  513  LEU A C   
3791  O O   . LEU A 515  ? 0.3561 0.2733 0.5252 0.0022  -0.0201 0.0376  513  LEU A O   
3792  C CB  . LEU A 515  ? 0.3793 0.2921 0.5536 0.0059  -0.0242 0.0219  513  LEU A CB  
3793  C CG  . LEU A 515  ? 0.3935 0.3071 0.5613 0.0078  -0.0236 0.0166  513  LEU A CG  
3794  C CD1 . LEU A 515  ? 0.4337 0.3471 0.6034 0.0090  -0.0252 0.0065  513  LEU A CD1 
3795  C CD2 . LEU A 515  ? 0.4083 0.3253 0.5608 0.0079  -0.0195 0.0185  513  LEU A CD2 
3796  N N   . ILE A 516  ? 0.3787 0.2905 0.5715 0.0016  -0.0263 0.0398  514  ILE A N   
3797  C CA  . ILE A 516  ? 0.3371 0.2495 0.5344 -0.0003 -0.0263 0.0444  514  ILE A CA  
3798  C C   . ILE A 516  ? 0.3682 0.2833 0.5665 -0.0018 -0.0252 0.0553  514  ILE A C   
3799  O O   . ILE A 516  ? 0.3744 0.2918 0.5764 -0.0036 -0.0252 0.0599  514  ILE A O   
3800  C CB  . ILE A 516  ? 0.3612 0.2720 0.5714 -0.0009 -0.0302 0.0404  514  ILE A CB  
3801  C CG1 . ILE A 516  ? 0.4265 0.3379 0.6471 -0.0011 -0.0333 0.0431  514  ILE A CG1 
3802  C CG2 . ILE A 516  ? 0.3620 0.2704 0.5713 0.0006  -0.0312 0.0296  514  ILE A CG2 
3803  C CD1 . ILE A 516  ? 0.4147 0.3261 0.6483 -0.0019 -0.0371 0.0401  514  ILE A CD1 
3804  N N   . ALA A 517  ? 0.3339 0.2503 0.5279 -0.0011 -0.0241 0.0592  515  ALA A N   
3805  C CA  . ALA A 517  ? 0.3831 0.3038 0.5759 -0.0023 -0.0226 0.0693  515  ALA A CA  
3806  C C   . ALA A 517  ? 0.3783 0.3029 0.5622 -0.0032 -0.0192 0.0720  515  ALA A C   
3807  O O   . ALA A 517  ? 0.3744 0.3002 0.5468 -0.0023 -0.0166 0.0666  515  ALA A O   
3808  C CB  . ALA A 517  ? 0.3877 0.3096 0.5742 -0.0011 -0.0214 0.0718  515  ALA A CB  
3809  N N   . ASP A 518  ? 0.3409 0.2685 0.5299 -0.0051 -0.0191 0.0802  516  ASP A N   
3810  C CA  . ASP A 518  ? 0.3500 0.2821 0.5322 -0.0061 -0.0160 0.0833  516  ASP A CA  
3811  C C   . ASP A 518  ? 0.3247 0.2625 0.4953 -0.0055 -0.0126 0.0879  516  ASP A C   
3812  O O   . ASP A 518  ? 0.3431 0.2840 0.5170 -0.0062 -0.0127 0.0959  516  ASP A O   
3813  C CB  . ASP A 518  ? 0.3710 0.3056 0.5634 -0.0083 -0.0175 0.0895  516  ASP A CB  
3814  C CG  . ASP A 518  ? 0.3806 0.3193 0.5680 -0.0094 -0.0146 0.0935  516  ASP A CG  
3815  O OD1 . ASP A 518  ? 0.3735 0.3140 0.5485 -0.0083 -0.0116 0.0895  516  ASP A OD1 
3816  O OD2 . ASP A 518  ? 0.4617 0.4046 0.6557 -0.0112 -0.0153 0.0989  516  ASP A OD2 
3817  N N   . PRO A 519  ? 0.3414 0.2810 0.4987 -0.0042 -0.0096 0.0831  517  PRO A N   
3818  C CA  . PRO A 519  ? 0.3371 0.2822 0.4838 -0.0035 -0.0065 0.0867  517  PRO A CA  
3819  C C   . PRO A 519  ? 0.2853 0.2369 0.4325 -0.0049 -0.0049 0.0955  517  PRO A C   
3820  O O   . PRO A 519  ? 0.3345 0.2911 0.4776 -0.0046 -0.0034 0.1009  517  PRO A O   
3821  C CB  . PRO A 519  ? 0.3296 0.2747 0.4637 -0.0021 -0.0040 0.0793  517  PRO A CB  
3822  C CG  . PRO A 519  ? 0.3816 0.3233 0.5194 -0.0027 -0.0051 0.0743  517  PRO A CG  
3823  C CD  . PRO A 519  ? 0.3186 0.2559 0.4704 -0.0035 -0.0089 0.0745  517  PRO A CD  
3824  N N   . VAL A 520  ? 0.3170 0.2692 0.4692 -0.0064 -0.0051 0.0970  518  VAL A N   
3825  C CA  . VAL A 520  ? 0.2986 0.2577 0.4517 -0.0078 -0.0034 0.1053  518  VAL A CA  
3826  C C   . VAL A 520  ? 0.3842 0.3455 0.5466 -0.0090 -0.0052 0.1142  518  VAL A C   
3827  O O   . VAL A 520  ? 0.3521 0.3202 0.5105 -0.0091 -0.0034 0.1208  518  VAL A O   
3828  C CB  . VAL A 520  ? 0.3395 0.2983 0.4974 -0.0092 -0.0037 0.1048  518  VAL A CB  
3829  C CG1 . VAL A 520  ? 0.3642 0.3309 0.5229 -0.0106 -0.0019 0.1134  518  VAL A CG1 
3830  C CG2 . VAL A 520  ? 0.3165 0.2734 0.4651 -0.0079 -0.0021 0.0962  518  VAL A CG2 
3831  N N   . GLU A 521  ? 0.3745 0.3305 0.5492 -0.0099 -0.0089 0.1141  519  GLU A N   
3832  C CA  . GLU A 521  ? 0.3773 0.3375 0.5598 -0.0109 -0.0109 0.1203  519  GLU A CA  
3833  C C   . GLU A 521  ? 0.3836 0.3445 0.5620 -0.0096 -0.0108 0.1216  519  GLU A C   
3834  O O   . GLU A 521  ? 0.4026 0.3697 0.5829 -0.0102 -0.0109 0.1285  519  GLU A O   
3835  C CB  . GLU A 521  ? 0.4094 0.3657 0.6053 -0.0119 -0.0151 0.1178  519  GLU A CB  
3836  C CG  . GLU A 521  ? 0.4624 0.4200 0.6639 -0.0136 -0.0155 0.1186  519  GLU A CG  
3837  C CD  . GLU A 521  ? 0.5132 0.4799 0.7127 -0.0149 -0.0131 0.1271  519  GLU A CD  
3838  O OE1 . GLU A 521  ? 0.5498 0.5223 0.7502 -0.0154 -0.0130 0.1338  519  GLU A OE1 
3839  O OE2 . GLU A 521  ? 0.5455 0.5137 0.7424 -0.0156 -0.0113 0.1271  519  GLU A OE2 
3840  N N   . VAL A 522  ? 0.3615 0.3164 0.5344 -0.0077 -0.0106 0.1151  520  VAL A N   
3841  C CA  . VAL A 522  ? 0.3536 0.3089 0.5222 -0.0063 -0.0104 0.1161  520  VAL A CA  
3842  C C   . VAL A 522  ? 0.4394 0.4025 0.5969 -0.0058 -0.0068 0.1210  520  VAL A C   
3843  O O   . VAL A 522  ? 0.4428 0.4106 0.6004 -0.0059 -0.0067 0.1272  520  VAL A O   
3844  C CB  . VAL A 522  ? 0.3979 0.3463 0.5626 -0.0043 -0.0110 0.1066  520  VAL A CB  
3845  C CG1 . VAL A 522  ? 0.4297 0.3797 0.5886 -0.0028 -0.0105 0.1073  520  VAL A CG1 
3846  C CG2 . VAL A 522  ? 0.4208 0.3625 0.5975 -0.0046 -0.0149 0.1020  520  VAL A CG2 
3847  N N   . VAL A 523  ? 0.3578 0.3236 0.5051 -0.0053 -0.0037 0.1171  521  VAL A N   
3848  C CA  . VAL A 523  ? 0.3675 0.3417 0.5041 -0.0047 -0.0003 0.1204  521  VAL A CA  
3849  C C   . VAL A 523  ? 0.3710 0.3529 0.5131 -0.0065 0.0000  0.1309  521  VAL A C   
3850  O O   . VAL A 523  ? 0.4067 0.3959 0.5444 -0.0062 0.0014  0.1364  521  VAL A O   
3851  C CB  . VAL A 523  ? 0.3232 0.2982 0.4491 -0.0037 0.0025  0.1138  521  VAL A CB  
3852  C CG1 . VAL A 523  ? 0.3832 0.3676 0.4997 -0.0032 0.0058  0.1174  521  VAL A CG1 
3853  C CG2 . VAL A 523  ? 0.3542 0.3232 0.4735 -0.0019 0.0025  0.1044  521  VAL A CG2 
3854  N N   . ARG A 524  ? 0.3691 0.3499 0.5210 -0.0085 -0.0014 0.1340  522  ARG A N   
3855  C CA  . ARG A 524  ? 0.3988 0.3885 0.5552 -0.0102 -0.0011 0.1424  522  ARG A CA  
3856  C C   . ARG A 524  ? 0.4452 0.4389 0.6070 -0.0107 -0.0031 0.1477  522  ARG A C   
3857  O O   . ARG A 524  ? 0.4701 0.4734 0.6306 -0.0114 -0.0019 0.1546  522  ARG A O   
3858  C CB  . ARG A 524  ? 0.4579 0.4461 0.6239 -0.0121 -0.0028 0.1422  522  ARG A CB  
3859  C CG  . ARG A 524  ? 0.5221 0.5153 0.6992 -0.0140 -0.0053 0.1487  522  ARG A CG  
3860  C CD  . ARG A 524  ? 0.5026 0.4996 0.6855 -0.0158 -0.0053 0.1516  522  ARG A CD  
3861  N NE  . ARG A 524  ? 0.4770 0.4666 0.6608 -0.0157 -0.0056 0.1449  522  ARG A NE  
3862  C CZ  . ARG A 524  ? 0.4270 0.4187 0.6057 -0.0159 -0.0030 0.1442  522  ARG A CZ  
3863  N NH1 . ARG A 524  ? 0.4459 0.4469 0.6183 -0.0160 0.0002  0.1495  522  ARG A NH1 
3864  N NH2 . ARG A 524  ? 0.4708 0.4554 0.6509 -0.0159 -0.0036 0.1379  522  ARG A NH2 
3865  N N   . ALA A 525  ? 0.4388 0.4255 0.6064 -0.0103 -0.0061 0.1443  523  ALA A N   
3866  C CA  . ALA A 525  ? 0.4382 0.4277 0.6123 -0.0108 -0.0085 0.1490  523  ALA A CA  
3867  C C   . ALA A 525  ? 0.4348 0.4266 0.6004 -0.0091 -0.0071 0.1500  523  ALA A C   
3868  O O   . ALA A 525  ? 0.5200 0.5148 0.6900 -0.0094 -0.0088 0.1542  523  ALA A O   
3869  C CB  . ALA A 525  ? 0.4507 0.4321 0.6363 -0.0111 -0.0126 0.1449  523  ALA A CB  
3870  N N   . MET A 526  ? 0.4423 0.4328 0.5962 -0.0074 -0.0043 0.1462  524  MET A N   
3871  C CA  A MET A 526  ? 0.4507 0.4434 0.5962 -0.0057 -0.0030 0.1468  524  MET A CA  
3872  C CA  B MET A 526  ? 0.4506 0.4433 0.5963 -0.0057 -0.0031 0.1468  524  MET A CA  
3873  C C   . MET A 526  ? 0.4895 0.4943 0.6322 -0.0063 -0.0015 0.1549  524  MET A C   
3874  O O   . MET A 526  ? 0.4748 0.4867 0.6172 -0.0074 0.0001  0.1589  524  MET A O   
3875  C CB  A MET A 526  ? 0.4996 0.4903 0.6325 -0.0037 -0.0002 0.1397  524  MET A CB  
3876  C CB  B MET A 526  ? 0.4996 0.4898 0.6328 -0.0037 -0.0003 0.1395  524  MET A CB  
3877  C CG  A MET A 526  ? 0.4892 0.4696 0.6227 -0.0027 -0.0015 0.1298  524  MET A CG  
3878  C CG  B MET A 526  ? 0.4874 0.4685 0.6198 -0.0021 -0.0019 0.1308  524  MET A CG  
3879  S SD  A MET A 526  ? 0.5337 0.5076 0.6723 -0.0017 -0.0047 0.1276  524  MET A SD  
3880  S SD  B MET A 526  ? 0.5076 0.4854 0.6276 -0.0004 0.0006  0.1192  524  MET A SD  
3881  C CE  A MET A 526  ? 0.4889 0.4697 0.6146 0.0001  -0.0021 0.1286  524  MET A CE  
3882  C CE  B MET A 526  ? 0.4567 0.4271 0.5753 0.0014  -0.0011 0.1120  524  MET A CE  
3883  N N   . PRO A 527  ? 0.5318 0.5397 0.6724 -0.0054 -0.0020 0.1574  525  PRO A N   
3884  C CA  . PRO A 527  ? 0.5579 0.5781 0.6956 -0.0059 -0.0006 0.1650  525  PRO A CA  
3885  C C   . PRO A 527  ? 0.5324 0.5603 0.6587 -0.0051 0.0034  0.1656  525  PRO A C   
3886  O O   . PRO A 527  ? 0.4121 0.4501 0.5386 -0.0062 0.0047  0.1710  525  PRO A O   
3887  C CB  . PRO A 527  ? 0.5076 0.5279 0.6438 -0.0048 -0.0018 0.1657  525  PRO A CB  
3888  C CG  . PRO A 527  ? 0.5374 0.5463 0.6712 -0.0031 -0.0025 0.1579  525  PRO A CG  
3889  C CD  . PRO A 527  ? 0.5031 0.5039 0.6441 -0.0040 -0.0039 0.1535  525  PRO A CD  
3890  N N   . VAL A 528  ? 0.5236 0.5474 0.6401 -0.0032 0.0054  0.1600  526  VAL A N   
3891  C CA  . VAL A 528  ? 0.4379 0.4682 0.5431 -0.0021 0.0090  0.1565  526  VAL A CA  
3892  C C   . VAL A 528  ? 0.3951 0.4170 0.4988 -0.0017 0.0094  0.1476  526  VAL A C   
3893  O O   . VAL A 528  ? 0.4750 0.4886 0.5758 -0.0004 0.0087  0.1397  526  VAL A O   
3894  C CB  . VAL A 528  ? 0.4529 0.4879 0.5463 0.0002  0.0108  0.1531  526  VAL A CB  
3895  C CG1 . VAL A 528  ? 0.4996 0.5407 0.5823 0.0015  0.0142  0.1487  526  VAL A CG1 
3896  C CG2 . VAL A 528  ? 0.5110 0.5548 0.6061 -0.0002 0.0103  0.1621  526  VAL A CG2 
3897  N N   . VAL A 529  ? 0.3922 0.4167 0.4980 -0.0029 0.0105  0.1491  527  VAL A N   
3898  C CA  . VAL A 529  ? 0.3845 0.4017 0.4891 -0.0026 0.0108  0.1411  527  VAL A CA  
3899  C C   . VAL A 529  ? 0.4478 0.4659 0.5392 -0.0003 0.0133  0.1330  527  VAL A C   
3900  O O   . VAL A 529  ? 0.4057 0.4329 0.4896 0.0006  0.0159  0.1344  527  VAL A O   
3901  C CB  . VAL A 529  ? 0.3798 0.4002 0.4900 -0.0044 0.0113  0.1451  527  VAL A CB  
3902  C CG1 . VAL A 529  ? 0.3552 0.3694 0.4625 -0.0039 0.0120  0.1366  527  VAL A CG1 
3903  C CG2 . VAL A 529  ? 0.4603 0.4781 0.5848 -0.0068 0.0082  0.1523  527  VAL A CG2 
3904  N N   . GLY A 530  ? 0.3523 0.3612 0.4413 0.0007  0.0126  0.1245  528  GLY A N   
3905  C CA  . GLY A 530  ? 0.3493 0.3578 0.4270 0.0027  0.0146  0.1167  528  GLY A CA  
3906  C C   . GLY A 530  ? 0.3046 0.3159 0.3741 0.0045  0.0154  0.1149  528  GLY A C   
3907  O O   . GLY A 530  ? 0.3671 0.3807 0.4273 0.0061  0.0174  0.1099  528  GLY A O   
3908  N N   . ALA A 531  ? 0.3515 0.3628 0.4245 0.0044  0.0138  0.1188  529  ALA A N   
3909  C CA  . ALA A 531  ? 0.3252 0.3393 0.3906 0.0061  0.0144  0.1170  529  ALA A CA  
3910  C C   . ALA A 531  ? 0.3162 0.3227 0.3756 0.0076  0.0144  0.1075  529  ALA A C   
3911  O O   . ALA A 531  ? 0.3506 0.3485 0.4142 0.0071  0.0129  0.1034  529  ALA A O   
3912  C CB  . ALA A 531  ? 0.3529 0.3675 0.4242 0.0056  0.0123  0.1230  529  ALA A CB  
3913  N N   . LYS A 532  ? 0.3203 0.3306 0.3700 0.0093  0.0161  0.1039  530  LYS A N   
3914  C CA  . LYS A 532  ? 0.3250 0.3291 0.3686 0.0107  0.0160  0.0956  530  LYS A CA  
3915  C C   . LYS A 532  ? 0.3411 0.3384 0.3894 0.0106  0.0136  0.0947  530  LYS A C   
3916  O O   . LYS A 532  ? 0.3088 0.3077 0.3627 0.0100  0.0122  0.1005  530  LYS A O   
3917  C CB  . LYS A 532  ? 0.3509 0.3614 0.3849 0.0125  0.0178  0.0935  530  LYS A CB  
3918  C CG  . LYS A 532  ? 0.3966 0.4016 0.4243 0.0138  0.0177  0.0855  530  LYS A CG  
3919  C CD  . LYS A 532  ? 0.3479 0.3594 0.3671 0.0155  0.0190  0.0838  530  LYS A CD  
3920  C CE  . LYS A 532  ? 0.3714 0.3884 0.3914 0.0158  0.0184  0.0893  530  LYS A CE  
3921  N NZ  . LYS A 532  ? 0.3424 0.3528 0.3654 0.0157  0.0163  0.0882  530  LYS A NZ  
3922  N N   . HIS A 533  ? 0.3247 0.3146 0.3710 0.0111  0.0131  0.0874  531  HIS A N   
3923  C CA  . HIS A 533  ? 0.3155 0.2995 0.3651 0.0113  0.0111  0.0854  531  HIS A CA  
3924  C C   . HIS A 533  ? 0.3427 0.3311 0.3885 0.0124  0.0111  0.0875  531  HIS A C   
3925  O O   . HIS A 533  ? 0.3383 0.3314 0.3757 0.0135  0.0128  0.0858  531  HIS A O   
3926  C CB  . HIS A 533  ? 0.3112 0.2886 0.3573 0.0119  0.0110  0.0770  531  HIS A CB  
3927  C CG  . HIS A 533  ? 0.3576 0.3286 0.4088 0.0120  0.0088  0.0745  531  HIS A CG  
3928  N ND1 . HIS A 533  ? 0.3442 0.3154 0.3945 0.0128  0.0079  0.0747  531  HIS A ND1 
3929  C CD2 . HIS A 533  ? 0.4161 0.3808 0.4737 0.0113  0.0071  0.0716  531  HIS A CD2 
3930  C CE1 . HIS A 533  ? 0.4544 0.4196 0.5104 0.0128  0.0059  0.0719  531  HIS A CE1 
3931  N NE2 . HIS A 533  ? 0.4881 0.4495 0.5486 0.0119  0.0054  0.0698  531  HIS A NE2 
3932  N N   . ASP A 534  ? 0.3113 0.2982 0.3637 0.0121  0.0090  0.0912  532  ASP A N   
3933  C CA  . ASP A 534  ? 0.3580 0.3493 0.4079 0.0130  0.0088  0.0940  532  ASP A CA  
3934  C C   . ASP A 534  ? 0.3657 0.3548 0.4078 0.0145  0.0093  0.0871  532  ASP A C   
3935  O O   . ASP A 534  ? 0.4422 0.4365 0.4788 0.0155  0.0099  0.0880  532  ASP A O   
3936  C CB  . ASP A 534  ? 0.3979 0.3867 0.4576 0.0123  0.0061  0.0988  532  ASP A CB  
3937  C CG  . ASP A 534  ? 0.6049 0.5962 0.6733 0.0106  0.0053  0.1065  532  ASP A CG  
3938  O OD1 . ASP A 534  ? 0.6602 0.6592 0.7257 0.0102  0.0070  0.1111  532  ASP A OD1 
3939  O OD2 . ASP A 534  ? 0.8065 0.7922 0.8848 0.0097  0.0029  0.1078  532  ASP A OD2 
3940  N N   . ARG A 535  ? 0.3184 0.3003 0.3602 0.0146  0.0089  0.0803  533  ARG A N   
3941  C CA  . ARG A 535  ? 0.3366 0.3159 0.3726 0.0158  0.0089  0.0742  533  ARG A CA  
3942  C C   . ARG A 535  ? 0.3198 0.2998 0.3471 0.0164  0.0109  0.0687  533  ARG A C   
3943  O O   . ARG A 535  ? 0.3509 0.3282 0.3736 0.0172  0.0110  0.0633  533  ARG A O   
3944  C CB  . ARG A 535  ? 0.3961 0.3678 0.4375 0.0157  0.0070  0.0702  533  ARG A CB  
3945  N N   . ILE A 536  ? 0.3224 0.3060 0.3476 0.0161  0.0125  0.0702  534  ILE A N   
3946  C CA  . ILE A 536  ? 0.3373 0.3219 0.3549 0.0168  0.0142  0.0654  534  ILE A CA  
3947  C C   . ILE A 536  ? 0.3311 0.3243 0.3436 0.0176  0.0157  0.0682  534  ILE A C   
3948  O O   . ILE A 536  ? 0.3422 0.3405 0.3573 0.0171  0.0162  0.0736  534  ILE A O   
3949  C CB  . ILE A 536  ? 0.3107 0.2921 0.3301 0.0159  0.0147  0.0635  534  ILE A CB  
3950  C CG1 . ILE A 536  ? 0.3642 0.3379 0.3884 0.0152  0.0131  0.0601  534  ILE A CG1 
3951  C CG2 . ILE A 536  ? 0.3323 0.3153 0.3444 0.0166  0.0163  0.0591  534  ILE A CG2 
3952  C CD1 . ILE A 536  ? 0.3713 0.3420 0.3977 0.0143  0.0133  0.0582  534  ILE A CD1 
3953  N N   . ALA A 537  ? 0.2738 0.2689 0.2794 0.0189  0.0163  0.0646  535  ALA A N   
3954  C CA  . ALA A 537  ? 0.2710 0.2748 0.2716 0.0200  0.0175  0.0663  535  ALA A CA  
3955  C C   . ALA A 537  ? 0.3260 0.3323 0.3232 0.0203  0.0192  0.0640  535  ALA A C   
3956  O O   . ALA A 537  ? 0.2737 0.2751 0.2688 0.0204  0.0193  0.0586  535  ALA A O   
3957  C CB  . ALA A 537  ? 0.3092 0.3139 0.3043 0.0213  0.0173  0.0627  535  ALA A CB  
3958  N N   . LEU A 538  ? 0.2981 0.3126 0.2949 0.0205  0.0203  0.0683  536  LEU A N   
3959  C CA  . LEU A 538  ? 0.2703 0.2889 0.2627 0.0213  0.0219  0.0655  536  LEU A CA  
3960  C C   . LEU A 538  ? 0.3059 0.3254 0.2916 0.0230  0.0221  0.0595  536  LEU A C   
3961  O O   . LEU A 538  ? 0.2795 0.3000 0.2634 0.0236  0.0213  0.0594  536  LEU A O   
3962  C CB  . LEU A 538  ? 0.2790 0.3081 0.2717 0.0215  0.0232  0.0711  536  LEU A CB  
3963  C CG  . LEU A 538  ? 0.3058 0.3353 0.3053 0.0198  0.0233  0.0771  536  LEU A CG  
3964  C CD1 . LEU A 538  ? 0.3741 0.4153 0.3734 0.0200  0.0245  0.0831  536  LEU A CD1 
3965  C CD2 . LEU A 538  ? 0.3103 0.3347 0.3112 0.0192  0.0237  0.0738  536  LEU A CD2 
3966  N N   . PRO A 539  ? 0.2491 0.2679 0.2314 0.0238  0.0229  0.0544  537  PRO A N   
3967  C CA  . PRO A 539  ? 0.2623 0.2812 0.2391 0.0253  0.0227  0.0486  537  PRO A CA  
3968  C C   . PRO A 539  ? 0.2600 0.2879 0.2331 0.0268  0.0230  0.0496  537  PRO A C   
3969  O O   . PRO A 539  ? 0.2843 0.3111 0.2545 0.0275  0.0221  0.0467  537  PRO A O   
3970  C CB  . PRO A 539  ? 0.2643 0.2823 0.2395 0.0258  0.0235  0.0443  537  PRO A CB  
3971  C CG  . PRO A 539  ? 0.2671 0.2798 0.2472 0.0240  0.0235  0.0464  537  PRO A CG  
3972  C CD  . PRO A 539  ? 0.2773 0.2934 0.2616 0.0231  0.0235  0.0534  537  PRO A CD  
3973  N N   . ALA A 540  ? 0.2612 0.2983 0.2345 0.0271  0.0241  0.0540  538  ALA A N   
3974  C CA  . ALA A 540  ? 0.2895 0.3363 0.2591 0.0285  0.0244  0.0553  538  ALA A CA  
3975  C C   . ALA A 540  ? 0.3303 0.3764 0.3012 0.0281  0.0232  0.0588  538  ALA A C   
3976  O O   . ALA A 540  ? 0.3219 0.3743 0.2892 0.0293  0.0230  0.0585  538  ALA A O   
3977  C CB  . ALA A 540  ? 0.3165 0.3740 0.2866 0.0288  0.0259  0.0602  538  ALA A CB  
3978  N N   . GLU A 541  ? 0.2902 0.3289 0.2662 0.0264  0.0222  0.0619  539  GLU A N   
3979  C CA  . GLU A 541  ? 0.2879 0.3264 0.2663 0.0259  0.0209  0.0660  539  GLU A CA  
3980  C C   . GLU A 541  ? 0.3167 0.3460 0.2952 0.0257  0.0195  0.0618  539  GLU A C   
3981  O O   . GLU A 541  ? 0.2939 0.3209 0.2758 0.0251  0.0182  0.0648  539  GLU A O   
3982  C CB  . GLU A 541  ? 0.3773 0.4161 0.3624 0.0242  0.0206  0.0736  539  GLU A CB  
3983  C CG  . GLU A 541  ? 0.4163 0.4654 0.4015 0.0243  0.0221  0.0785  539  GLU A CG  
3984  C CD  . GLU A 541  ? 0.5093 0.5589 0.5018 0.0224  0.0216  0.0866  539  GLU A CD  
3985  O OE1 . GLU A 541  ? 0.6600 0.7071 0.6567 0.0217  0.0201  0.0904  539  GLU A OE1 
3986  O OE2 . GLU A 541  ? 0.6512 0.7037 0.6458 0.0217  0.0227  0.0892  539  GLU A OE2 
3987  N N   . LEU A 542  ? 0.2755 0.3001 0.2508 0.0263  0.0195  0.0549  540  LEU A N   
3988  C CA  . LEU A 542  ? 0.3034 0.3197 0.2788 0.0260  0.0183  0.0509  540  LEU A CA  
3989  C C   . LEU A 542  ? 0.3047 0.3233 0.2787 0.0267  0.0172  0.0517  540  LEU A C   
3990  O O   . LEU A 542  ? 0.3352 0.3479 0.3114 0.0261  0.0160  0.0510  540  LEU A O   
3991  C CB  . LEU A 542  ? 0.3437 0.3567 0.3152 0.0266  0.0185  0.0439  540  LEU A CB  
3992  C CG  . LEU A 542  ? 0.3913 0.3985 0.3644 0.0257  0.0189  0.0416  540  LEU A CG  
3993  C CD1 . LEU A 542  ? 0.3429 0.3461 0.3127 0.0262  0.0185  0.0350  540  LEU A CD1 
3994  C CD2 . LEU A 542  ? 0.3748 0.3752 0.3533 0.0241  0.0182  0.0439  540  LEU A CD2 
3995  N N   . PHE A 543  ? 0.2851 0.3127 0.2555 0.0280  0.0177  0.0527  541  PHE A N   
3996  C CA  . PHE A 543  ? 0.3180 0.3482 0.2866 0.0288  0.0166  0.0530  541  PHE A CA  
3997  C C   . PHE A 543  ? 0.3027 0.3389 0.2742 0.0285  0.0163  0.0606  541  PHE A C   
3998  O O   . PHE A 543  ? 0.3025 0.3426 0.2726 0.0292  0.0155  0.0618  541  PHE A O   
3999  C CB  . PHE A 543  ? 0.3005 0.3361 0.2630 0.0305  0.0169  0.0481  541  PHE A CB  
4000  C CG  . PHE A 543  ? 0.2983 0.3284 0.2587 0.0307  0.0171  0.0413  541  PHE A CG  
4001  C CD1 . PHE A 543  ? 0.3275 0.3483 0.2894 0.0298  0.0161  0.0380  541  PHE A CD1 
4002  C CD2 . PHE A 543  ? 0.2775 0.3120 0.2351 0.0318  0.0181  0.0383  541  PHE A CD2 
4003  C CE1 . PHE A 543  ? 0.3157 0.3317 0.2761 0.0299  0.0162  0.0324  541  PHE A CE1 
4004  C CE2 . PHE A 543  ? 0.2606 0.2898 0.2171 0.0319  0.0180  0.0324  541  PHE A CE2 
4005  C CZ  . PHE A 543  ? 0.3046 0.3246 0.2625 0.0309  0.0170  0.0297  541  PHE A CZ  
4006  N N   . GLY A 544  ? 0.3030 0.3399 0.2790 0.0273  0.0168  0.0659  542  GLY A N   
4007  C CA  . GLY A 544  ? 0.3405 0.3821 0.3205 0.0267  0.0162  0.0738  542  GLY A CA  
4008  C C   . GLY A 544  ? 0.3599 0.4135 0.3356 0.0280  0.0167  0.0763  542  GLY A C   
4009  O O   . GLY A 544  ? 0.3325 0.3929 0.3035 0.0290  0.0181  0.0741  542  GLY A O   
4010  N N   . ASP A 545  ? 0.3518 0.4083 0.3292 0.0280  0.0154  0.0807  543  ASP A N   
4011  C CA  . ASP A 545  ? 0.3810 0.4497 0.3547 0.0290  0.0157  0.0841  543  ASP A CA  
4012  C C   . ASP A 545  ? 0.3753 0.4477 0.3417 0.0310  0.0159  0.0773  543  ASP A C   
4013  O O   . ASP A 545  ? 0.4171 0.5008 0.3795 0.0321  0.0163  0.0788  543  ASP A O   
4014  C CB  . ASP A 545  ? 0.4288 0.4993 0.4070 0.0284  0.0140  0.0911  543  ASP A CB  
4015  C CG  . ASP A 545  ? 0.6074 0.6763 0.5936 0.0266  0.0136  0.0989  543  ASP A CG  
4016  O OD1 . ASP A 545  ? 0.6055 0.6742 0.5931 0.0258  0.0148  0.0995  543  ASP A OD1 
4017  O OD2 . ASP A 545  ? 0.7463 0.8142 0.7378 0.0259  0.0118  0.1044  543  ASP A OD2 
4018  N N   . ALA A 546  ? 0.3102 0.3740 0.2750 0.0313  0.0154  0.0700  544  ALA A N   
4019  C CA  . ALA A 546  ? 0.3499 0.4165 0.3087 0.0330  0.0152  0.0636  544  ALA A CA  
4020  C C   . ALA A 546  ? 0.3769 0.4512 0.3309 0.0344  0.0167  0.0602  544  ALA A C   
4021  O O   . ALA A 546  ? 0.3616 0.4450 0.3110 0.0360  0.0167  0.0585  544  ALA A O   
4022  C CB  . ALA A 546  ? 0.3433 0.3987 0.3021 0.0328  0.0144  0.0571  544  ALA A CB  
4023  N N   . ARG A 547  ? 0.3221 0.3932 0.2771 0.0338  0.0179  0.0588  545  ARG A N   
4024  C CA  . ARG A 547  ? 0.3359 0.4141 0.2871 0.0352  0.0193  0.0553  545  ARG A CA  
4025  C C   . ARG A 547  ? 0.2886 0.3619 0.2427 0.0341  0.0204  0.0555  545  ARG A C   
4026  O O   . ARG A 547  ? 0.2886 0.3521 0.2470 0.0325  0.0199  0.0568  545  ARG A O   
4027  C CB  . ARG A 547  ? 0.3205 0.3977 0.2673 0.0368  0.0188  0.0466  545  ARG A CB  
4028  C CG  . ARG A 547  ? 0.3555 0.4199 0.3038 0.0360  0.0180  0.0417  545  ARG A CG  
4029  C CD  . ARG A 547  ? 0.3522 0.4158 0.2969 0.0375  0.0172  0.0338  545  ARG A CD  
4030  N NE  . ARG A 547  ? 0.3040 0.3562 0.2504 0.0364  0.0160  0.0309  545  ARG A NE  
4031  C CZ  . ARG A 547  ? 0.3004 0.3447 0.2478 0.0358  0.0160  0.0267  545  ARG A CZ  
4032  N NH1 . ARG A 547  ? 0.3032 0.3490 0.2500 0.0364  0.0170  0.0243  545  ARG A NH1 
4033  N NH2 . ARG A 547  ? 0.3169 0.3520 0.2660 0.0347  0.0150  0.0248  545  ARG A NH2 
4034  N N   . THR A 548  ? 0.2728 0.3532 0.2245 0.0352  0.0218  0.0539  546  THR A N   
4035  C CA  . THR A 548  ? 0.2582 0.3355 0.2122 0.0344  0.0229  0.0538  546  THR A CA  
4036  C C   . THR A 548  ? 0.2515 0.3209 0.2040 0.0350  0.0226  0.0456  546  THR A C   
4037  O O   . THR A 548  ? 0.2543 0.3272 0.2029 0.0368  0.0224  0.0398  546  THR A O   
4038  C CB  . THR A 548  ? 0.3106 0.4005 0.2629 0.0354  0.0246  0.0560  546  THR A CB  
4039  O OG1 . THR A 548  ? 0.3576 0.4558 0.3112 0.0348  0.0247  0.0641  546  THR A OG1 
4040  C CG2 . THR A 548  ? 0.3172 0.4042 0.2722 0.0345  0.0258  0.0564  546  THR A CG2 
4041  N N   . ASN A 549  ? 0.2393 0.2985 0.1953 0.0335  0.0225  0.0453  547  ASN A N   
4042  C CA  . ASN A 549  ? 0.2377 0.2895 0.1928 0.0338  0.0222  0.0384  547  ASN A CA  
4043  C C   . ASN A 549  ? 0.2584 0.3165 0.2115 0.0352  0.0233  0.0352  547  ASN A C   
4044  O O   . ASN A 549  ? 0.2637 0.3288 0.2177 0.0352  0.0247  0.0392  547  ASN A O   
4045  C CB  . ASN A 549  ? 0.2440 0.2852 0.2034 0.0317  0.0219  0.0396  547  ASN A CB  
4046  C CG  . ASN A 549  ? 0.2440 0.2767 0.2029 0.0317  0.0212  0.0332  547  ASN A CG  
4047  O OD1 . ASN A 549  ? 0.2515 0.2847 0.2072 0.0330  0.0206  0.0280  547  ASN A OD1 
4048  N ND2 . ASN A 549  ? 0.2702 0.2950 0.2324 0.0301  0.0212  0.0337  547  ASN A ND2 
4049  N N   . SER A 550  ? 0.2529 0.3090 0.2038 0.0365  0.0227  0.0281  548  SER A N   
4050  C CA  . SER A 550  ? 0.2480 0.3084 0.1979 0.0379  0.0236  0.0243  548  SER A CA  
4051  C C   . SER A 550  ? 0.2547 0.3092 0.2080 0.0364  0.0243  0.0260  548  SER A C   
4052  O O   . SER A 550  ? 0.2665 0.3115 0.2225 0.0346  0.0238  0.0275  548  SER A O   
4053  C CB  . SER A 550  ? 0.2269 0.2844 0.1749 0.0393  0.0223  0.0164  548  SER A CB  
4054  O OG  . SER A 550  ? 0.2569 0.3025 0.2069 0.0379  0.0212  0.0145  548  SER A OG  
4055  N N   . ALA A 551  ? 0.2648 0.3256 0.2181 0.0374  0.0256  0.0255  549  ALA A N   
4056  C CA  . ALA A 551  ? 0.2718 0.3284 0.2282 0.0362  0.0264  0.0269  549  ALA A CA  
4057  C C   . ALA A 551  ? 0.2756 0.3285 0.2319 0.0373  0.0259  0.0201  549  ALA A C   
4058  O O   . ALA A 551  ? 0.2620 0.3205 0.2160 0.0395  0.0257  0.0151  549  ALA A O   
4059  C CB  . ALA A 551  ? 0.2883 0.3547 0.2456 0.0363  0.0282  0.0319  549  ALA A CB  
4060  N N   . GLY A 552  ? 0.2582 0.3018 0.2172 0.0358  0.0256  0.0199  550  GLY A N   
4061  C CA  . GLY A 552  ? 0.2757 0.3154 0.2354 0.0365  0.0251  0.0146  550  GLY A CA  
4062  C C   . GLY A 552  ? 0.2666 0.3100 0.2283 0.0366  0.0265  0.0160  550  GLY A C   
4063  O O   . GLY A 552  ? 0.2867 0.3384 0.2485 0.0368  0.0280  0.0202  550  GLY A O   
4064  N N   . LEU A 553  ? 0.2786 0.3163 0.2421 0.0365  0.0259  0.0125  551  LEU A N   
4065  C CA  . LEU A 553  ? 0.2709 0.3112 0.2365 0.0367  0.0270  0.0131  551  LEU A CA  
4066  C C   . LEU A 553  ? 0.2786 0.3084 0.2471 0.0349  0.0263  0.0131  551  LEU A C   
4067  O O   . LEU A 553  ? 0.2921 0.3143 0.2605 0.0345  0.0247  0.0100  551  LEU A O   
4068  C CB  . LEU A 553  ? 0.3008 0.3467 0.2655 0.0394  0.0269  0.0071  551  LEU A CB  
4069  C CG  . LEU A 553  ? 0.2845 0.3427 0.2464 0.0416  0.0279  0.0065  551  LEU A CG  
4070  C CD1 . LEU A 553  ? 0.3795 0.4424 0.3410 0.0444  0.0273  -0.0006 551  LEU A CD1 
4071  C CD2 . LEU A 553  ? 0.3032 0.3700 0.2655 0.0410  0.0300  0.0128  551  LEU A CD2 
4072  N N   . ASP A 554  ? 0.2632 0.2931 0.2343 0.0338  0.0273  0.0167  552  ASP A N   
4073  C CA  . ASP A 554  ? 0.2662 0.2871 0.2402 0.0319  0.0266  0.0171  552  ASP A CA  
4074  C C   . ASP A 554  ? 0.2570 0.2773 0.2321 0.0330  0.0263  0.0129  552  ASP A C   
4075  O O   . ASP A 554  ? 0.2509 0.2764 0.2275 0.0336  0.0275  0.0139  552  ASP A O   
4076  C CB  . ASP A 554  ? 0.2621 0.2832 0.2390 0.0300  0.0277  0.0232  552  ASP A CB  
4077  C CG  . ASP A 554  ? 0.2680 0.2801 0.2477 0.0281  0.0269  0.0235  552  ASP A CG  
4078  O OD1 . ASP A 554  ? 0.2810 0.2871 0.2603 0.0282  0.0256  0.0194  552  ASP A OD1 
4079  O OD2 . ASP A 554  ? 0.2936 0.3049 0.2763 0.0265  0.0274  0.0279  552  ASP A OD2 
4080  N N   . LEU A 555  ? 0.2444 0.2583 0.2193 0.0332  0.0247  0.0085  553  LEU A N   
4081  C CA  . LEU A 555  ? 0.2552 0.2681 0.2319 0.0343  0.0240  0.0044  553  LEU A CA  
4082  C C   . LEU A 555  ? 0.2482 0.2556 0.2279 0.0326  0.0239  0.0063  553  LEU A C   
4083  O O   . LEU A 555  ? 0.2905 0.2958 0.2721 0.0332  0.0231  0.0033  553  LEU A O   
4084  C CB  . LEU A 555  ? 0.2657 0.2744 0.2418 0.0352  0.0220  -0.0008 553  LEU A CB  
4085  C CG  . LEU A 555  ? 0.2753 0.2900 0.2486 0.0372  0.0219  -0.0036 553  LEU A CG  
4086  C CD1 . LEU A 555  ? 0.3386 0.3486 0.3122 0.0380  0.0196  -0.0088 553  LEU A CD1 
4087  C CD2 . LEU A 555  ? 0.3197 0.3449 0.2925 0.0395  0.0233  -0.0047 553  LEU A CD2 
4088  N N   . SER A 556  ? 0.2437 0.2488 0.2243 0.0305  0.0246  0.0111  554  SER A N   
4089  C CA  . SER A 556  ? 0.2503 0.2520 0.2340 0.0291  0.0248  0.0131  554  SER A CA  
4090  C C   . SER A 556  ? 0.2637 0.2723 0.2491 0.0292  0.0266  0.0167  554  SER A C   
4091  O O   . SER A 556  ? 0.2663 0.2730 0.2546 0.0280  0.0268  0.0185  554  SER A O   
4092  C CB  . SER A 556  ? 0.2822 0.2765 0.2668 0.0266  0.0240  0.0155  554  SER A CB  
4093  O OG  . SER A 556  ? 0.3017 0.2984 0.2865 0.0257  0.0250  0.0199  554  SER A OG  
4094  N N   . ASN A 557  ? 0.2319 0.2488 0.2157 0.0304  0.0278  0.0179  555  ASN A N   
4095  C CA  . ASN A 557  ? 0.2303 0.2548 0.2156 0.0304  0.0296  0.0220  555  ASN A CA  
4096  C C   . ASN A 557  ? 0.2604 0.2918 0.2459 0.0326  0.0303  0.0187  555  ASN A C   
4097  O O   . ASN A 557  ? 0.2472 0.2833 0.2302 0.0348  0.0302  0.0148  555  ASN A O   
4098  C CB  . ASN A 557  ? 0.2613 0.2920 0.2447 0.0305  0.0305  0.0255  555  ASN A CB  
4099  C CG  . ASN A 557  ? 0.2438 0.2832 0.2290 0.0302  0.0323  0.0306  555  ASN A CG  
4100  O OD1 . ASN A 557  ? 0.2782 0.3245 0.2638 0.0316  0.0334  0.0295  555  ASN A OD1 
4101  N ND2 . ASN A 557  ? 0.2703 0.3096 0.2570 0.0284  0.0326  0.0363  555  ASN A ND2 
4102  N N   . GLU A 558  ? 0.2473 0.2793 0.2359 0.0321  0.0309  0.0199  556  GLU A N   
4103  C CA  . GLU A 558  ? 0.2731 0.3111 0.2623 0.0343  0.0315  0.0164  556  GLU A CA  
4104  C C   . GLU A 558  ? 0.2510 0.3014 0.2384 0.0362  0.0332  0.0170  556  GLU A C   
4105  O O   . GLU A 558  ? 0.2676 0.3236 0.2542 0.0388  0.0333  0.0122  556  GLU A O   
4106  C CB  . GLU A 558  ? 0.3023 0.3393 0.2954 0.0334  0.0319  0.0181  556  GLU A CB  
4107  C CG  . GLU A 558  ? 0.2851 0.3114 0.2801 0.0320  0.0302  0.0167  556  GLU A CG  
4108  C CD  . GLU A 558  ? 0.2725 0.2949 0.2669 0.0336  0.0285  0.0106  556  GLU A CD  
4109  O OE1 . GLU A 558  ? 0.2586 0.2864 0.2519 0.0362  0.0285  0.0065  556  GLU A OE1 
4110  O OE2 . GLU A 558  ? 0.2748 0.2886 0.2703 0.0323  0.0269  0.0099  556  GLU A OE2 
4111  N N   . GLU A 559  ? 0.2347 0.2900 0.2219 0.0350  0.0345  0.0228  557  GLU A N   
4112  C CA  . GLU A 559  ? 0.2419 0.3099 0.2270 0.0367  0.0361  0.0237  557  GLU A CA  
4113  C C   . GLU A 559  ? 0.2617 0.3314 0.2429 0.0387  0.0353  0.0190  557  GLU A C   
4114  O O   . GLU A 559  ? 0.2806 0.3591 0.2601 0.0413  0.0358  0.0151  557  GLU A O   
4115  C CB  . GLU A 559  ? 0.3146 0.3870 0.3005 0.0348  0.0373  0.0315  557  GLU A CB  
4116  C CG  . GLU A 559  ? 0.3417 0.4145 0.3322 0.0328  0.0382  0.0367  557  GLU A CG  
4117  C CD  . GLU A 559  ? 0.4512 0.5275 0.4432 0.0308  0.0390  0.0446  557  GLU A CD  
4118  O OE1 . GLU A 559  ? 0.5416 0.6212 0.5307 0.0311  0.0390  0.0459  557  GLU A OE1 
4119  O OE2 . GLU A 559  ? 0.4738 0.5493 0.4701 0.0287  0.0394  0.0495  557  GLU A OE2 
4120  N N   . THR A 560  ? 0.2383 0.2995 0.2180 0.0376  0.0339  0.0189  558  THR A N   
4121  C CA  . THR A 560  ? 0.2710 0.3329 0.2473 0.0393  0.0329  0.0144  558  THR A CA  
4122  C C   . THR A 560  ? 0.2534 0.3134 0.2300 0.0415  0.0316  0.0069  558  THR A C   
4123  O O   . THR A 560  ? 0.2693 0.3359 0.2439 0.0440  0.0315  0.0024  558  THR A O   
4124  C CB  . THR A 560  ? 0.2597 0.3122 0.2352 0.0374  0.0315  0.0159  558  THR A CB  
4125  O OG1 . THR A 560  ? 0.2869 0.3409 0.2629 0.0355  0.0324  0.0228  558  THR A OG1 
4126  C CG2 . THR A 560  ? 0.2821 0.3354 0.2541 0.0390  0.0304  0.0115  558  THR A CG2 
4127  N N   . LEU A 561  ? 0.2338 0.2850 0.2132 0.0406  0.0305  0.0055  559  LEU A N   
4128  C CA  . LEU A 561  ? 0.2321 0.2811 0.2126 0.0425  0.0291  -0.0013 559  LEU A CA  
4129  C C   . LEU A 561  ? 0.2616 0.3213 0.2428 0.0452  0.0302  -0.0042 559  LEU A C   
4130  O O   . LEU A 561  ? 0.2647 0.3274 0.2458 0.0478  0.0292  -0.0104 559  LEU A O   
4131  C CB  . LEU A 561  ? 0.2242 0.2626 0.2078 0.0409  0.0277  -0.0014 559  LEU A CB  
4132  C CG  . LEU A 561  ? 0.2271 0.2551 0.2099 0.0386  0.0263  0.0000  559  LEU A CG  
4133  C CD1 . LEU A 561  ? 0.2333 0.2526 0.2192 0.0370  0.0252  0.0003  559  LEU A CD1 
4134  C CD2 . LEU A 561  ? 0.2560 0.2820 0.2370 0.0399  0.0246  -0.0048 559  LEU A CD2 
4135  N N   . ALA A 562  ? 0.2512 0.3173 0.2337 0.0446  0.0322  0.0002  560  ALA A N   
4136  C CA  . ALA A 562  ? 0.2407 0.3178 0.2240 0.0472  0.0334  -0.0025 560  ALA A CA  
4137  C C   . ALA A 562  ? 0.2442 0.3329 0.2241 0.0494  0.0343  -0.0043 560  ALA A C   
4138  O O   . ALA A 562  ? 0.2643 0.3596 0.2441 0.0524  0.0341  -0.0104 560  ALA A O   
4139  C CB  . ALA A 562  ? 0.2869 0.3682 0.2726 0.0458  0.0354  0.0030  560  ALA A CB  
4140  N N   . SER A 563  ? 0.2554 0.3469 0.2326 0.0480  0.0352  0.0009  561  SER A N   
4141  C CA  A SER A 563  ? 0.2785 0.3813 0.2521 0.0500  0.0360  -0.0003 561  SER A CA  
4142  C CA  B SER A 563  ? 0.2784 0.3813 0.2520 0.0500  0.0360  -0.0004 561  SER A CA  
4143  C C   . SER A 563  ? 0.2648 0.3642 0.2366 0.0519  0.0339  -0.0074 561  SER A C   
4144  O O   . SER A 563  ? 0.3057 0.4145 0.2761 0.0548  0.0339  -0.0126 561  SER A O   
4145  C CB  A SER A 563  ? 0.2839 0.3893 0.2555 0.0478  0.0371  0.0074  561  SER A CB  
4146  C CB  B SER A 563  ? 0.2837 0.3901 0.2553 0.0479  0.0373  0.0073  561  SER A CB  
4147  O OG  A SER A 563  ? 0.2890 0.4055 0.2570 0.0496  0.0377  0.0065  561  SER A OG  
4148  O OG  B SER A 563  ? 0.3323 0.4280 0.3031 0.0460  0.0358  0.0089  561  SER A OG  
4149  N N   . LEU A 564  ? 0.2793 0.3657 0.2516 0.0502  0.0320  -0.0078 562  LEU A N   
4150  C CA  . LEU A 564  ? 0.2681 0.3505 0.2393 0.0517  0.0298  -0.0141 562  LEU A CA  
4151  C C   . LEU A 564  ? 0.2866 0.3695 0.2606 0.0543  0.0285  -0.0218 562  LEU A C   
4152  O O   . LEU A 564  ? 0.2904 0.3777 0.2636 0.0569  0.0273  -0.0280 562  LEU A O   
4153  C CB  . LEU A 564  ? 0.2717 0.3403 0.2433 0.0491  0.0281  -0.0123 562  LEU A CB  
4154  C CG  . LEU A 564  ? 0.3835 0.4481 0.3533 0.0497  0.0261  -0.0164 562  LEU A CG  
4155  C CD1 . LEU A 564  ? 0.3537 0.4276 0.3196 0.0505  0.0271  -0.0148 562  LEU A CD1 
4156  C CD2 . LEU A 564  ? 0.3401 0.3917 0.3106 0.0469  0.0248  -0.0139 562  LEU A CD2 
4157  N N   . THR A 565  ? 0.2768 0.3555 0.2544 0.0538  0.0284  -0.0216 563  THR A N   
4158  C CA  . THR A 565  ? 0.2796 0.3591 0.2606 0.0564  0.0271  -0.0286 563  THR A CA  
4159  C C   . THR A 565  ? 0.2531 0.3472 0.2331 0.0599  0.0282  -0.0330 563  THR A C   
4160  O O   . THR A 565  ? 0.2927 0.3888 0.2737 0.0626  0.0264  -0.0405 563  THR A O   
4161  C CB  . THR A 565  ? 0.2704 0.3458 0.2552 0.0554  0.0275  -0.0267 563  THR A CB  
4162  O OG1 . THR A 565  ? 0.2758 0.3379 0.2619 0.0525  0.0261  -0.0238 563  THR A OG1 
4163  C CG2 . THR A 565  ? 0.3247 0.4020 0.3135 0.0583  0.0261  -0.0340 563  THR A CG2 
4164  N N   . GLU A 566  ? 0.2655 0.3704 0.2435 0.0598  0.0309  -0.0285 564  GLU A N   
4165  C CA  . GLU A 566  ? 0.2865 0.4067 0.2633 0.0631  0.0321  -0.0325 564  GLU A CA  
4166  C C   . GLU A 566  ? 0.2863 0.4116 0.2594 0.0646  0.0314  -0.0357 564  GLU A C   
4167  O O   . GLU A 566  ? 0.2877 0.4202 0.2611 0.0680  0.0305  -0.0433 564  GLU A O   
4168  C CB  . GLU A 566  ? 0.3242 0.4552 0.3000 0.0623  0.0352  -0.0260 564  GLU A CB  
4169  C CG  . GLU A 566  ? 0.4406 0.5683 0.4204 0.0612  0.0359  -0.0238 564  GLU A CG  
4170  C CD  . GLU A 566  ? 0.4816 0.6082 0.4655 0.0640  0.0344  -0.0318 564  GLU A CD  
4171  O OE1 . GLU A 566  ? 0.5168 0.6537 0.5006 0.0675  0.0343  -0.0384 564  GLU A OE1 
4172  O OE2 . GLU A 566  ? 0.4504 0.5661 0.4380 0.0627  0.0331  -0.0317 564  GLU A OE2 
4173  N N   . ALA A 567  ? 0.2798 0.4011 0.2497 0.0622  0.0315  -0.0305 565  ALA A N   
4174  C CA  . ALA A 567  ? 0.2856 0.4115 0.2520 0.0635  0.0307  -0.0332 565  ALA A CA  
4175  C C   . ALA A 567  ? 0.2570 0.3751 0.2253 0.0651  0.0276  -0.0413 565  ALA A C   
4176  O O   . ALA A 567  ? 0.2914 0.4166 0.2584 0.0678  0.0267  -0.0474 565  ALA A O   
4177  C CB  . ALA A 567  ? 0.3256 0.4476 0.2889 0.0605  0.0313  -0.0255 565  ALA A CB  
4178  N N   . LEU A 568  ? 0.2592 0.3632 0.2308 0.0633  0.0259  -0.0413 566  LEU A N   
4179  C CA  . LEU A 568  ? 0.2418 0.3379 0.2160 0.0645  0.0227  -0.0483 566  LEU A CA  
4180  C C   . LEU A 568  ? 0.2642 0.3663 0.2420 0.0682  0.0217  -0.0566 566  LEU A C   
4181  O O   . LEU A 568  ? 0.2915 0.3958 0.2701 0.0706  0.0196  -0.0638 566  LEU A O   
4182  C CB  . LEU A 568  ? 0.2601 0.3405 0.2372 0.0616  0.0212  -0.0457 566  LEU A CB  
4183  C CG  . LEU A 568  ? 0.2584 0.3313 0.2326 0.0581  0.0216  -0.0388 566  LEU A CG  
4184  C CD1 . LEU A 568  ? 0.2621 0.3213 0.2394 0.0556  0.0203  -0.0367 566  LEU A CD1 
4185  C CD2 . LEU A 568  ? 0.2708 0.3434 0.2424 0.0585  0.0203  -0.0409 566  LEU A CD2 
4186  N N   . ARG A 569  ? 0.2757 0.3807 0.2560 0.0686  0.0229  -0.0560 567  ARG A N   
4187  C CA  . ARG A 569  ? 0.2699 0.3821 0.2539 0.0724  0.0221  -0.0639 567  ARG A CA  
4188  C C   . ARG A 569  ? 0.2970 0.4247 0.2780 0.0756  0.0230  -0.0684 567  ARG A C   
4189  O O   . ARG A 569  ? 0.3427 0.4739 0.3260 0.0788  0.0209  -0.0771 567  ARG A O   
4190  C CB  . ARG A 569  ? 0.2948 0.4096 0.2813 0.0722  0.0239  -0.0613 567  ARG A CB  
4191  C CG  . ARG A 569  ? 0.3141 0.4145 0.3047 0.0698  0.0225  -0.0589 567  ARG A CG  
4192  C CD  . ARG A 569  ? 0.4094 0.5129 0.4022 0.0695  0.0244  -0.0559 567  ARG A CD  
4193  N NE  . ARG A 569  ? 0.4511 0.5414 0.4475 0.0671  0.0231  -0.0532 567  ARG A NE  
4194  C CZ  . ARG A 569  ? 0.5303 0.6201 0.5287 0.0661  0.0244  -0.0496 567  ARG A CZ  
4195  N NH1 . ARG A 569  ? 0.6054 0.7071 0.6030 0.0671  0.0271  -0.0479 567  ARG A NH1 
4196  N NH2 . ARG A 569  ? 0.5732 0.6510 0.5748 0.0639  0.0229  -0.0475 567  ARG A NH2 
4197  N N   . GLU A 570  ? 0.2819 0.4192 0.2578 0.0747  0.0259  -0.0624 568  GLU A N   
4198  C CA  . GLU A 570  ? 0.3059 0.4592 0.2783 0.0775  0.0269  -0.0659 568  GLU A CA  
4199  C C   . GLU A 570  ? 0.3392 0.4906 0.3102 0.0785  0.0245  -0.0708 568  GLU A C   
4200  O O   . GLU A 570  ? 0.3633 0.5252 0.3339 0.0820  0.0238  -0.0781 568  GLU A O   
4201  C CB  . GLU A 570  ? 0.3273 0.4905 0.2950 0.0758  0.0303  -0.0571 568  GLU A CB  
4202  C CG  . GLU A 570  ? 0.3709 0.5408 0.3402 0.0757  0.0328  -0.0536 568  GLU A CG  
4203  C CD  . GLU A 570  ? 0.5051 0.6802 0.4710 0.0728  0.0357  -0.0431 568  GLU A CD  
4204  O OE1 . GLU A 570  ? 0.6305 0.8014 0.5934 0.0705  0.0356  -0.0380 568  GLU A OE1 
4205  O OE2 . GLU A 570  ? 0.6493 0.8327 0.6161 0.0728  0.0380  -0.0398 568  GLU A OE2 
4206  N N   . SER A 571  ? 0.3126 0.4508 0.2828 0.0756  0.0232  -0.0671 569  SER A N   
4207  C CA  . SER A 571  ? 0.3254 0.4610 0.2946 0.0764  0.0208  -0.0716 569  SER A CA  
4208  C C   . SER A 571  ? 0.3183 0.4500 0.2930 0.0791  0.0175  -0.0816 569  SER A C   
4209  O O   . SER A 571  ? 0.3269 0.4630 0.3014 0.0814  0.0157  -0.0882 569  SER A O   
4210  C CB  . SER A 571  ? 0.2934 0.4157 0.2612 0.0725  0.0201  -0.0654 569  SER A CB  
4211  O OG  . SER A 571  ? 0.3194 0.4270 0.2919 0.0711  0.0180  -0.0663 569  SER A OG  
4212  N N   . ALA A 572  ? 0.3354 0.4591 0.3154 0.0789  0.0165  -0.0829 570  ALA A N   
4213  C CA  . ALA A 572  ? 0.3321 0.4515 0.3185 0.0814  0.0130  -0.0920 570  ALA A CA  
4214  C C   . ALA A 572  ? 0.3766 0.5102 0.3648 0.0859  0.0131  -0.1004 570  ALA A C   
4215  O O   . ALA A 572  ? 0.4573 0.5894 0.4507 0.0886  0.0100  -0.1091 570  ALA A O   
4216  C CB  . ALA A 572  ? 0.3867 0.4929 0.3785 0.0795  0.0118  -0.0902 570  ALA A CB  
4217  N N   . ALA A 573  ? 0.3316 0.4791 0.3158 0.0869  0.0164  -0.0978 571  ALA A N   
4218  C CA  . ALA A 573  ? 0.4096 0.5730 0.3946 0.0913  0.0169  -0.1054 571  ALA A CA  
4219  C C   . ALA A 573  ? 0.4843 0.6601 0.4647 0.0933  0.0170  -0.1089 571  ALA A C   
4220  O O   . ALA A 573  ? 0.4731 0.6636 0.4537 0.0971  0.0173  -0.1158 571  ALA A O   
4221  C CB  . ALA A 573  ? 0.3868 0.5600 0.3705 0.0913  0.0204  -0.1008 571  ALA A CB  
4222  N N   . MET A 574  ? 0.3671 0.5379 0.3433 0.0909  0.0168  -0.1044 572  MET A N   
4223  C CA  . MET A 574  ? 0.4153 0.5974 0.3868 0.0925  0.0169  -0.1070 572  MET A CA  
4224  C C   . MET A 574  ? 0.3890 0.5682 0.3645 0.0951  0.0129  -0.1175 572  MET A C   
4225  O O   . MET A 574  ? 0.3835 0.5481 0.3644 0.0942  0.0099  -0.1198 572  MET A O   
4226  C CB  . MET A 574  ? 0.4238 0.6021 0.3894 0.0888  0.0183  -0.0975 572  MET A CB  
4227  C CG  . MET A 574  ? 0.3932 0.5778 0.3548 0.0866  0.0223  -0.0874 572  MET A CG  
4228  S SD  . MET A 574  ? 0.4389 0.6155 0.3954 0.0819  0.0235  -0.0759 572  MET A SD  
4229  C CE  . MET A 574  ? 0.5523 0.7386 0.5059 0.0801  0.0277  -0.0658 572  MET A CE  
4230  N N   . LYS A 575  ? 0.4244 0.6164 0.3982 0.0972  0.0121  -0.1222 573  LYS A N   
4231  C CA  . LYS A 575  ? 0.4390 0.6287 0.4175 0.0987  0.0075  -0.1309 573  LYS A CA  
4232  C C   . LYS A 575  ? 0.4019 0.5879 0.3762 0.0974  0.0067  -0.1292 573  LYS A C   
4233  O O   . LYS A 575  ? 0.4200 0.6162 0.3912 0.0980  0.0063  -0.1302 573  LYS A O   
4234  C CB  . LYS A 575  ? 0.4596 0.6643 0.4396 0.1010  0.0063  -0.1364 573  LYS A CB  
4235  N N   . TRP A 576  ? 0.3594 0.5309 0.3341 0.0957  0.0065  -0.1267 574  TRP A N   
4236  C CA  . TRP A 576  ? 0.3145 0.4800 0.2859 0.0935  0.0056  -0.1234 574  TRP A CA  
4237  C C   . TRP A 576  ? 0.2756 0.4414 0.2507 0.0955  0.0015  -0.1325 574  TRP A C   
4238  O O   . TRP A 576  ? 0.3194 0.4780 0.3022 0.0964  -0.0020 -0.1389 574  TRP A O   
4239  C CB  . TRP A 576  ? 0.3010 0.4476 0.2746 0.0892  0.0048  -0.1167 574  TRP A CB  
4240  C CG  . TRP A 576  ? 0.2827 0.4264 0.2535 0.0862  0.0082  -0.1064 574  TRP A CG  
4241  C CD1 . TRP A 576  ? 0.2996 0.4357 0.2742 0.0851  0.0087  -0.1041 574  TRP A CD1 
4242  C CD2 . TRP A 576  ? 0.2960 0.4443 0.2600 0.0839  0.0114  -0.0972 574  TRP A CD2 
4243  N NE1 . TRP A 576  ? 0.3133 0.4490 0.2839 0.0822  0.0119  -0.0943 574  TRP A NE1 
4244  C CE2 . TRP A 576  ? 0.3006 0.4435 0.2650 0.0814  0.0136  -0.0898 574  TRP A CE2 
4245  C CE3 . TRP A 576  ? 0.2741 0.4306 0.2322 0.0837  0.0124  -0.0944 574  TRP A CE3 
4246  C CZ2 . TRP A 576  ? 0.3224 0.4676 0.2819 0.0787  0.0167  -0.0799 574  TRP A CZ2 
4247  C CZ3 . TRP A 576  ? 0.2837 0.4423 0.2369 0.0810  0.0155  -0.0843 574  TRP A CZ3 
4248  C CH2 . TRP A 576  ? 0.3361 0.4890 0.2903 0.0785  0.0175  -0.0772 574  TRP A CH2 
4249  N N   . THR A 577  ? 0.2899 0.4633 0.2604 0.0954  0.0014  -0.1319 575  THR A N   
4250  C CA  . THR A 577  ? 0.2656 0.4383 0.2398 0.0963  -0.0027 -0.1389 575  THR A CA  
4251  C C   . THR A 577  ? 0.3366 0.5066 0.3055 0.0947  -0.0025 -0.1352 575  THR A C   
4252  O O   . THR A 577  ? 0.3082 0.4811 0.2699 0.0933  0.0009  -0.1275 575  THR A O   
4253  C CB  . THR A 577  ? 0.3168 0.5052 0.2920 0.0987  -0.0039 -0.1441 575  THR A CB  
4254  O OG1 . THR A 577  ? 0.3516 0.5530 0.3189 0.0983  -0.0009 -0.1384 575  THR A OG1 
4255  C CG2 . THR A 577  ? 0.3557 0.5483 0.3357 0.1004  -0.0040 -0.1476 575  THR A CG2 
4256  N N   . ALA A 578  ? 0.3019 0.4663 0.2748 0.0949  -0.0064 -0.1408 576  ALA A N   
4257  C CA  . ALA A 578  ? 0.2971 0.4605 0.2661 0.0938  -0.0070 -0.1390 576  ALA A CA  
4258  C C   . ALA A 578  ? 0.3319 0.5020 0.3047 0.0955  -0.0107 -0.1466 576  ALA A C   
4259  O O   . ALA A 578  ? 0.3314 0.4965 0.3124 0.0965  -0.0143 -0.1536 576  ALA A O   
4260  C CB  . ALA A 578  ? 0.2991 0.4453 0.2698 0.0917  -0.0083 -0.1376 576  ALA A CB  
4261  N N   . LEU A 579  ? 0.3053 0.4871 0.2728 0.0959  -0.0098 -0.1451 577  LEU A N   
4262  C CA  . LEU A 579  ? 0.3404 0.5311 0.3110 0.0978  -0.0130 -0.1520 577  LEU A CA  
4263  C C   . LEU A 579  ? 0.3250 0.5149 0.2917 0.0967  -0.0137 -0.1502 577  LEU A C   
4264  O O   . LEU A 579  ? 0.2983 0.4858 0.2584 0.0948  -0.0110 -0.1427 577  LEU A O   
4265  C CB  . LEU A 579  ? 0.3106 0.5197 0.2785 0.0998  -0.0114 -0.1523 577  LEU A CB  
4266  C CG  . LEU A 579  ? 0.3832 0.5961 0.3538 0.1009  -0.0101 -0.1532 577  LEU A CG  
4267  C CD1 . LEU A 579  ? 0.3800 0.6121 0.3478 0.1028  -0.0088 -0.1535 577  LEU A CD1 
4268  C CD2 . LEU A 579  ? 0.4409 0.6456 0.4212 0.1022  -0.0139 -0.1615 577  LEU A CD2 
4269  N N   . PRO A 580  ? 0.3037 0.4960 0.2749 0.0979  -0.0174 -0.1570 578  PRO A N   
4270  C CA  . PRO A 580  ? 0.3219 0.5168 0.2890 0.0972  -0.0180 -0.1555 578  PRO A CA  
4271  C C   . PRO A 580  ? 0.3688 0.5803 0.3287 0.0979  -0.0151 -0.1510 578  PRO A C   
4272  O O   . PRO A 580  ? 0.4021 0.6271 0.3635 0.1001  -0.0160 -0.1553 578  PRO A O   
4273  C CB  . PRO A 580  ? 0.3463 0.5413 0.3212 0.0988  -0.0228 -0.1648 578  PRO A CB  
4274  C CG  . PRO A 580  ? 0.3695 0.5585 0.3531 0.0999  -0.0250 -0.1705 578  PRO A CG  
4275  C CD  . PRO A 580  ? 0.3294 0.5232 0.3096 0.1001  -0.0214 -0.1664 578  PRO A CD  
4276  N N   . GLN A 581  ? 0.3287 0.5394 0.2811 0.0959  -0.0116 -0.1420 579  GLN A N   
4277  C CA  . GLN A 581  ? 0.3408 0.5662 0.2863 0.0959  -0.0086 -0.1358 579  GLN A CA  
4278  C C   . GLN A 581  ? 0.3271 0.5565 0.2695 0.0956  -0.0097 -0.1348 579  GLN A C   
4279  O O   . GLN A 581  ? 0.3388 0.5628 0.2761 0.0935  -0.0082 -0.1283 579  GLN A O   
4280  C CB  . GLN A 581  ? 0.3202 0.5425 0.2602 0.0939  -0.0044 -0.1262 579  GLN A CB  
4281  C CG  . GLN A 581  ? 0.3489 0.5679 0.2918 0.0943  -0.0031 -0.1267 579  GLN A CG  
4282  C CD  . GLN A 581  ? 0.3673 0.6019 0.3112 0.0963  -0.0024 -0.1288 579  GLN A CD  
4283  O OE1 . GLN A 581  ? 0.3407 0.5892 0.2824 0.0974  -0.0026 -0.1289 579  GLN A OE1 
4284  N NE2 . GLN A 581  ? 0.3556 0.5883 0.3027 0.0970  -0.0017 -0.1304 579  GLN A NE2 
4285  N N   . LEU A 582  ? 0.3573 0.5964 0.3028 0.0977  -0.0123 -0.1415 580  LEU A N   
4286  C CA  . LEU A 582  ? 0.3496 0.5944 0.2924 0.0977  -0.0135 -0.1411 580  LEU A CA  
4287  C C   . LEU A 582  ? 0.3660 0.6256 0.3020 0.0975  -0.0104 -0.1336 580  LEU A C   
4288  O O   . LEU A 582  ? 0.3911 0.6582 0.3253 0.0977  -0.0078 -0.1298 580  LEU A O   
4289  C CB  . LEU A 582  ? 0.3697 0.6196 0.3191 0.1001  -0.0176 -0.1513 580  LEU A CB  
4290  C CG  . LEU A 582  ? 0.4810 0.7162 0.4364 0.0996  -0.0213 -0.1572 580  LEU A CG  
4291  C CD1 . LEU A 582  ? 0.4384 0.6595 0.3986 0.0989  -0.0217 -0.1589 580  LEU A CD1 
4292  C CD2 . LEU A 582  ? 0.4924 0.7346 0.4541 0.1021  -0.0252 -0.1666 580  LEU A CD2 
4293  N N   . ALA A 583  ? 0.3519 0.6158 0.2844 0.0969  -0.0108 -0.1310 581  ALA A N   
4294  C CA  . ALA A 583  ? 0.3516 0.6297 0.2783 0.0966  -0.0082 -0.1234 581  ALA A CA  
4295  C C   . ALA A 583  ? 0.3776 0.6730 0.3062 0.0991  -0.0083 -0.1271 581  ALA A C   
4296  O O   . ALA A 583  ? 0.4774 0.7844 0.4022 0.0988  -0.0056 -0.1205 581  ALA A O   
4297  C CB  . ALA A 583  ? 0.3777 0.6579 0.3015 0.0959  -0.0093 -0.1213 581  ALA A CB  
4298  N N   . THR A 584  ? 0.3834 0.6807 0.3182 0.1016  -0.0115 -0.1375 582  THR A N   
4299  C CA  . THR A 584  ? 0.3966 0.7105 0.3340 0.1043  -0.0121 -0.1425 582  THR A CA  
4300  C C   . THR A 584  ? 0.4327 0.7472 0.3722 0.1050  -0.0107 -0.1433 582  THR A C   
4301  O O   . THR A 584  ? 0.4674 0.7967 0.4082 0.1070  -0.0106 -0.1459 582  THR A O   
4302  C CB  . THR A 584  ? 0.4316 0.7471 0.3754 0.1068  -0.0164 -0.1537 582  THR A CB  
4303  O OG1 . THR A 584  ? 0.4905 0.7892 0.4399 0.1065  -0.0187 -0.1591 582  THR A OG1 
4304  C CG2 . THR A 584  ? 0.4855 0.8045 0.4273 0.1066  -0.0177 -0.1532 582  THR A CG2 
4305  N N   . GLY A 585  ? 0.4138 0.7131 0.3539 0.1033  -0.0098 -0.1412 583  GLY A N   
4306  C CA  . GLY A 585  ? 0.4177 0.7159 0.3604 0.1039  -0.0087 -0.1425 583  GLY A CA  
4307  C C   . GLY A 585  ? 0.4542 0.7361 0.4030 0.1040  -0.0110 -0.1488 583  GLY A C   
4308  O O   . GLY A 585  ? 0.4401 0.7119 0.3917 0.1036  -0.0137 -0.1525 583  GLY A O   
4309  N N   . PRO A 586  ? 0.4194 0.6986 0.3710 0.1044  -0.0102 -0.1500 584  PRO A N   
4310  C CA  . PRO A 586  ? 0.3961 0.6600 0.3543 0.1044  -0.0125 -0.1557 584  PRO A CA  
4311  C C   . PRO A 586  ? 0.4788 0.7438 0.4445 0.1067  -0.0172 -0.1663 584  PRO A C   
4312  O O   . PRO A 586  ? 0.4202 0.6998 0.3877 0.1091  -0.0184 -0.1712 584  PRO A O   
4313  C CB  . PRO A 586  ? 0.5027 0.7685 0.4623 0.1050  -0.0107 -0.1552 584  PRO A CB  
4314  C CG  . PRO A 586  ? 0.5115 0.7911 0.4642 0.1045  -0.0068 -0.1472 584  PRO A CG  
4315  C CD  . PRO A 586  ? 0.4684 0.7598 0.4181 0.1051  -0.0075 -0.1469 584  PRO A CD  
4316  N N   . ALA A 587  ? 0.4138 0.6634 0.3842 0.1058  -0.0199 -0.1698 585  ALA A N   
4317  C CA  . ALA A 587  ? 0.4178 0.6662 0.3965 0.1076  -0.0246 -0.1794 585  ALA A CA  
4318  C C   . ALA A 587  ? 0.4487 0.6879 0.4358 0.1083  -0.0268 -0.1851 585  ALA A C   
4319  O O   . ALA A 587  ? 0.4117 0.6409 0.3984 0.1068  -0.0251 -0.1811 585  ALA A O   
4320  C CB  . ALA A 587  ? 0.4693 0.7075 0.4482 0.1060  -0.0266 -0.1793 585  ALA A CB  
4321  N N   . ALA A 588  ? 0.4258 0.6692 0.4210 0.1107  -0.0309 -0.1943 586  ALA A N   
4322  C CA  . ALA A 588  ? 0.3928 0.6275 0.3973 0.1115  -0.0337 -0.2001 586  ALA A CA  
4323  C C   . ALA A 588  ? 0.4186 0.6350 0.4281 0.1095  -0.0364 -0.2007 586  ALA A C   
4324  O O   . ALA A 588  ? 0.4522 0.6647 0.4594 0.1081  -0.0370 -0.1989 586  ALA A O   
4325  C CB  . ALA A 588  ? 0.3809 0.6272 0.3928 0.1149  -0.0373 -0.2099 586  ALA A CB  
4326  N N   . GLY A 589  ? 0.4149 0.6205 0.4317 0.1092  -0.0382 -0.2031 587  GLY A N   
4327  C CA  . GLY A 589  ? 0.4080 0.5965 0.4308 0.1073  -0.0410 -0.2036 587  GLY A CA  
4328  C C   . GLY A 589  ? 0.4338 0.6122 0.4643 0.1071  -0.0425 -0.2053 587  GLY A C   
4329  O O   . GLY A 589  ? 0.4548 0.6397 0.4866 0.1088  -0.0417 -0.2073 587  GLY A O   
4330  N N   . GLU A 590  ? 0.4549 0.6172 0.4906 0.1049  -0.0448 -0.2044 588  GLU A N   
4331  C CA  . GLU A 590  ? 0.4121 0.5633 0.4556 0.1044  -0.0464 -0.2052 588  GLU A CA  
4332  C C   . GLU A 590  ? 0.3913 0.5383 0.4282 0.1029  -0.0420 -0.1978 588  GLU A C   
4333  O O   . GLU A 590  ? 0.3764 0.5180 0.4059 0.1007  -0.0390 -0.1909 588  GLU A O   
4334  C CB  . GLU A 590  ? 0.4817 0.6174 0.5327 0.1022  -0.0502 -0.2055 588  GLU A CB  
4335  N N   . THR A 591  ? 0.3866 0.5363 0.4266 0.1043  -0.0415 -0.1995 589  THR A N   
4336  C CA  . THR A 591  ? 0.3772 0.5252 0.4114 0.1034  -0.0372 -0.1932 589  THR A CA  
4337  C C   . THR A 591  ? 0.4027 0.5364 0.4443 0.1021  -0.0389 -0.1925 589  THR A C   
4338  O O   . THR A 591  ? 0.4028 0.5337 0.4546 0.1031  -0.0430 -0.1984 589  THR A O   
4339  C CB  . THR A 591  ? 0.4306 0.5945 0.4617 0.1059  -0.0350 -0.1951 589  THR A CB  
4340  O OG1 . THR A 591  ? 0.4238 0.6014 0.4477 0.1068  -0.0333 -0.1946 589  THR A OG1 
4341  C CG2 . THR A 591  ? 0.4110 0.5734 0.4372 0.1051  -0.0307 -0.1888 589  THR A CG2 
4342  N N   . ARG A 592  ? 0.3236 0.4483 0.3605 0.0999  -0.0358 -0.1852 590  ARG A N   
4343  C CA  . ARG A 592  ? 0.3999 0.5115 0.4430 0.0986  -0.0369 -0.1835 590  ARG A CA  
4344  C C   . ARG A 592  ? 0.3831 0.4933 0.4188 0.0976  -0.0320 -0.1763 590  ARG A C   
4345  O O   . ARG A 592  ? 0.3520 0.4684 0.3780 0.0972  -0.0281 -0.1717 590  ARG A O   
4346  C CB  . ARG A 592  ? 0.3948 0.4912 0.4434 0.0961  -0.0401 -0.1823 590  ARG A CB  
4347  C CG  . ARG A 592  ? 0.4228 0.5138 0.4632 0.0937  -0.0375 -0.1757 590  ARG A CG  
4348  C CD  . ARG A 592  ? 0.4785 0.5532 0.5245 0.0908  -0.0402 -0.1733 590  ARG A CD  
4349  N NE  . ARG A 592  ? 0.4798 0.5503 0.5184 0.0887  -0.0382 -0.1679 590  ARG A NE  
4350  C CZ  . ARG A 592  ? 0.4407 0.5079 0.4720 0.0874  -0.0342 -0.1613 590  ARG A CZ  
4351  N NH1 . ARG A 592  ? 0.4609 0.5280 0.4911 0.0878  -0.0318 -0.1588 590  ARG A NH1 
4352  N NH2 . ARG A 592  ? 0.4674 0.5314 0.4923 0.0856  -0.0328 -0.1570 590  ARG A NH2 
4353  N N   . THR A 593  ? 0.3733 0.4756 0.4141 0.0971  -0.0323 -0.1752 591  THR A N   
4354  C CA  . THR A 593  ? 0.3314 0.4313 0.3662 0.0962  -0.0280 -0.1685 591  THR A CA  
4355  C C   . THR A 593  ? 0.3524 0.4399 0.3840 0.0932  -0.0270 -0.1622 591  THR A C   
4356  O O   . THR A 593  ? 0.3727 0.4505 0.4089 0.0917  -0.0303 -0.1630 591  THR A O   
4357  C CB  . THR A 593  ? 0.4000 0.4954 0.4416 0.0967  -0.0288 -0.1694 591  THR A CB  
4358  O OG1 . THR A 593  ? 0.4186 0.5007 0.4698 0.0953  -0.0333 -0.1709 591  THR A OG1 
4359  C CG2 . THR A 593  ? 0.4377 0.5462 0.4821 0.0996  -0.0294 -0.1755 591  THR A CG2 
4360  N N   . VAL A 594  ? 0.3320 0.4203 0.3558 0.0925  -0.0225 -0.1558 592  VAL A N   
4361  C CA  . VAL A 594  ? 0.3217 0.3983 0.3424 0.0886  -0.0212 -0.1472 592  VAL A CA  
4362  C C   . VAL A 594  ? 0.3537 0.4231 0.3773 0.0871  -0.0203 -0.1424 592  VAL A C   
4363  O O   . VAL A 594  ? 0.3217 0.3986 0.3423 0.0882  -0.0172 -0.1409 592  VAL A O   
4364  C CB  . VAL A 594  ? 0.3082 0.3911 0.3182 0.0869  -0.0171 -0.1399 592  VAL A CB  
4365  C CG1 . VAL A 594  ? 0.3179 0.3885 0.3253 0.0820  -0.0160 -0.1296 592  VAL A CG1 
4366  C CG2 . VAL A 594  ? 0.3456 0.4368 0.3526 0.0887  -0.0181 -0.1449 592  VAL A CG2 
4367  N N   . LEU A 595  ? 0.3291 0.3844 0.3587 0.0844  -0.0229 -0.1399 593  LEU A N   
4368  C CA  . LEU A 595  ? 0.3360 0.3838 0.3698 0.0831  -0.0228 -0.1361 593  LEU A CA  
4369  C C   . LEU A 595  ? 0.3267 0.3659 0.3555 0.0784  -0.0203 -0.1250 593  LEU A C   
4370  O O   . LEU A 595  ? 0.3433 0.3772 0.3695 0.0757  -0.0207 -0.1213 593  LEU A O   
4371  C CB  . LEU A 595  ? 0.3405 0.3789 0.3858 0.0836  -0.0279 -0.1413 593  LEU A CB  
4372  C CG  . LEU A 595  ? 0.3621 0.4071 0.4145 0.0882  -0.0312 -0.1530 593  LEU A CG  
4373  C CD1 . LEU A 595  ? 0.3975 0.4321 0.4618 0.0871  -0.0363 -0.1549 593  LEU A CD1 
4374  C CD2 . LEU A 595  ? 0.3683 0.4260 0.4183 0.0910  -0.0287 -0.1556 593  LEU A CD2 
4375  N N   . ASN A 596  ? 0.2996 0.3378 0.3271 0.0774  -0.0179 -0.1200 594  ASN A N   
4376  C CA  . ASN A 596  ? 0.3004 0.3306 0.3240 0.0731  -0.0158 -0.1100 594  ASN A CA  
4377  C C   . ASN A 596  ? 0.2881 0.3049 0.3178 0.0704  -0.0192 -0.1082 594  ASN A C   
4378  O O   . ASN A 596  ? 0.2937 0.3056 0.3317 0.0712  -0.0222 -0.1116 594  ASN A O   
4379  C CB  . ASN A 596  ? 0.2917 0.3235 0.3150 0.0732  -0.0134 -0.1070 594  ASN A CB  
4380  C CG  . ASN A 596  ? 0.3092 0.3347 0.3280 0.0692  -0.0108 -0.0970 594  ASN A CG  
4381  O OD1 . ASN A 596  ? 0.3069 0.3231 0.3258 0.0660  -0.0118 -0.0926 594  ASN A OD1 
4382  N ND2 . ASN A 596  ? 0.3231 0.3541 0.3382 0.0693  -0.0074 -0.0935 594  ASN A ND2 
4383  N N   . PRO A 597  ? 0.2804 0.2913 0.3067 0.0671  -0.0190 -0.1028 595  PRO A N   
4384  C CA  . PRO A 597  ? 0.2811 0.2802 0.3134 0.0644  -0.0223 -0.1008 595  PRO A CA  
4385  C C   . PRO A 597  ? 0.2850 0.2766 0.3207 0.0623  -0.0224 -0.0960 595  PRO A C   
4386  O O   . PRO A 597  ? 0.3044 0.2873 0.3472 0.0609  -0.0258 -0.0958 595  PRO A O   
4387  C CB  . PRO A 597  ? 0.2844 0.2809 0.3107 0.0614  -0.0210 -0.0954 595  PRO A CB  
4388  C CG  . PRO A 597  ? 0.2906 0.2951 0.3078 0.0616  -0.0165 -0.0918 595  PRO A CG  
4389  C CD  . PRO A 597  ? 0.2760 0.2912 0.2934 0.0658  -0.0159 -0.0982 595  PRO A CD  
4390  N N   . GLY A 598  ? 0.2682 0.2630 0.2995 0.0621  -0.0189 -0.0920 596  GLY A N   
4391  C CA  . GLY A 598  ? 0.2779 0.2663 0.3122 0.0604  -0.0190 -0.0876 596  GLY A CA  
4392  C C   . GLY A 598  ? 0.3231 0.3131 0.3645 0.0632  -0.0208 -0.0929 596  GLY A C   
4393  O O   . GLY A 598  ? 0.3057 0.2901 0.3509 0.0619  -0.0215 -0.0898 596  GLY A O   
4394  N N   . ASP A 599  ? 0.3007 0.2985 0.3442 0.0671  -0.0217 -0.1010 597  ASP A N   
4395  C CA  . ASP A 599  ? 0.2939 0.2944 0.3444 0.0704  -0.0235 -0.1072 597  ASP A CA  
4396  C C   . ASP A 599  ? 0.2893 0.2988 0.3413 0.0745  -0.0247 -0.1166 597  ASP A C   
4397  O O   . ASP A 599  ? 0.2918 0.3122 0.3377 0.0767  -0.0217 -0.1184 597  ASP A O   
4398  C CB  . ASP A 599  ? 0.3108 0.3165 0.3577 0.0709  -0.0199 -0.1042 597  ASP A CB  
4399  C CG  . ASP A 599  ? 0.3397 0.3475 0.3941 0.0740  -0.0217 -0.1099 597  ASP A CG  
4400  O OD1 . ASP A 599  ? 0.3367 0.3450 0.3984 0.0767  -0.0253 -0.1177 597  ASP A OD1 
4401  O OD2 . ASP A 599  ? 0.3600 0.3691 0.4134 0.0737  -0.0195 -0.1066 597  ASP A OD2 
4402  N N   . HIS A 600  ? 0.2814 0.2867 0.3416 0.0756  -0.0293 -0.1225 598  HIS A N   
4403  C CA  . HIS A 600  ? 0.3264 0.3396 0.3885 0.0794  -0.0310 -0.1319 598  HIS A CA  
4404  C C   . HIS A 600  ? 0.3236 0.3474 0.3874 0.0839  -0.0303 -0.1390 598  HIS A C   
4405  O O   . HIS A 600  ? 0.3739 0.4071 0.4373 0.0874  -0.0307 -0.1467 598  HIS A O   
4406  C CB  . HIS A 600  ? 0.3562 0.3617 0.4281 0.0795  -0.0365 -0.1366 598  HIS A CB  
4407  C CG  . HIS A 600  ? 0.4044 0.4025 0.4738 0.0757  -0.0371 -0.1312 598  HIS A CG  
4408  N ND1 . HIS A 600  ? 0.4284 0.4186 0.5060 0.0747  -0.0418 -0.1334 598  HIS A ND1 
4409  C CD2 . HIS A 600  ? 0.3780 0.3759 0.4380 0.0727  -0.0337 -0.1238 598  HIS A CD2 
4410  C CE1 . HIS A 600  ? 0.4890 0.4747 0.5620 0.0713  -0.0411 -0.1275 598  HIS A CE1 
4411  N NE2 . HIS A 600  ? 0.4199 0.4101 0.4823 0.0700  -0.0362 -0.1218 598  HIS A NE2 
4412  N N   . ARG A 601  ? 0.3279 0.3510 0.3936 0.0840  -0.0291 -0.1367 599  ARG A N   
4413  C CA  . ARG A 601  ? 0.3390 0.3729 0.4056 0.0882  -0.0279 -0.1427 599  ARG A CA  
4414  C C   . ARG A 601  ? 0.3908 0.4371 0.4467 0.0888  -0.0228 -0.1404 599  ARG A C   
4415  O O   . ARG A 601  ? 0.3868 0.4449 0.4424 0.0926  -0.0216 -0.1465 599  ARG A O   
4416  C CB  . ARG A 601  ? 0.3326 0.3618 0.4041 0.0877  -0.0280 -0.1400 599  ARG A CB  
4417  C CG  . ARG A 601  ? 0.3547 0.3719 0.4374 0.0869  -0.0331 -0.1411 599  ARG A CG  
4418  C CD  . ARG A 601  ? 0.3936 0.4053 0.4795 0.0855  -0.0328 -0.1362 599  ARG A CD  
4419  N NE  . ARG A 601  ? 0.3731 0.3810 0.4508 0.0813  -0.0291 -0.1256 599  ARG A NE  
4420  C CZ  . ARG A 601  ? 0.4116 0.4156 0.4901 0.0796  -0.0280 -0.1200 599  ARG A CZ  
4421  N NH1 . ARG A 601  ? 0.4098 0.4125 0.4967 0.0816  -0.0303 -0.1234 599  ARG A NH1 
4422  N NH2 . ARG A 601  ? 0.3836 0.3847 0.4544 0.0759  -0.0247 -0.1109 599  ARG A NH2 
4423  N N   . ASP A 602  ? 0.3280 0.3720 0.3754 0.0852  -0.0198 -0.1319 600  ASP A N   
4424  C CA  . ASP A 602  ? 0.3536 0.4084 0.3911 0.0853  -0.0150 -0.1284 600  ASP A CA  
4425  C C   . ASP A 602  ? 0.3625 0.4245 0.3962 0.0867  -0.0152 -0.1325 600  ASP A C   
4426  O O   . ASP A 602  ? 0.3522 0.4086 0.3826 0.0840  -0.0155 -0.1285 600  ASP A O   
4427  C CB  . ASP A 602  ? 0.3703 0.4188 0.4017 0.0808  -0.0120 -0.1172 600  ASP A CB  
4428  C CG  . ASP A 602  ? 0.3874 0.4465 0.4094 0.0806  -0.0074 -0.1129 600  ASP A CG  
4429  O OD1 . ASP A 602  ? 0.3857 0.4575 0.4063 0.0840  -0.0060 -0.1176 600  ASP A OD1 
4430  O OD2 . ASP A 602  ? 0.3663 0.4212 0.3825 0.0771  -0.0052 -0.1047 600  ASP A OD2 
4431  N N   . VAL A 603  ? 0.3293 0.4040 0.3632 0.0910  -0.0151 -0.1405 601  VAL A N   
4432  C CA  . VAL A 603  ? 0.3226 0.4062 0.3526 0.0927  -0.0152 -0.1449 601  VAL A CA  
4433  C C   . VAL A 603  ? 0.3387 0.4302 0.3579 0.0911  -0.0105 -0.1376 601  VAL A C   
4434  O O   . VAL A 603  ? 0.3586 0.4591 0.3743 0.0921  -0.0072 -0.1355 601  VAL A O   
4435  C CB  . VAL A 603  ? 0.3530 0.4476 0.3872 0.0966  -0.0172 -0.1543 601  VAL A CB  
4436  C CG1 . VAL A 603  ? 0.3899 0.4942 0.4196 0.0973  -0.0173 -0.1570 601  VAL A CG1 
4437  C CG2 . VAL A 603  ? 0.3528 0.4385 0.3984 0.0966  -0.0224 -0.1592 601  VAL A CG2 
4438  N N   . VAL A 604  ? 0.3359 0.4240 0.3503 0.0887  -0.0102 -0.1333 602  VAL A N   
4439  C CA  . VAL A 604  ? 0.3205 0.4147 0.3253 0.0868  -0.0061 -0.1257 602  VAL A CA  
4440  C C   . VAL A 604  ? 0.3041 0.4140 0.3042 0.0899  -0.0050 -0.1304 602  VAL A C   
4441  O O   . VAL A 604  ? 0.3415 0.4621 0.3353 0.0901  -0.0013 -0.1264 602  VAL A O   
4442  C CB  . VAL A 604  ? 0.2895 0.3723 0.2914 0.0825  -0.0062 -0.1181 602  VAL A CB  
4443  C CG1 . VAL A 604  ? 0.3072 0.3957 0.3003 0.0806  -0.0021 -0.1099 602  VAL A CG1 
4444  C CG2 . VAL A 604  ? 0.3036 0.3718 0.3104 0.0796  -0.0074 -0.1138 602  VAL A CG2 
4445  N N   . GLY A 605  ? 0.3082 0.4202 0.3117 0.0924  -0.0082 -0.1390 603  GLY A N   
4446  C CA  . GLY A 605  ? 0.3188 0.4463 0.3180 0.0954  -0.0075 -0.1440 603  GLY A CA  
4447  C C   . GLY A 605  ? 0.3169 0.4428 0.3219 0.0961  -0.0122 -0.1512 603  GLY A C   
4448  O O   . GLY A 605  ? 0.3389 0.4544 0.3523 0.0959  -0.0160 -0.1549 603  GLY A O   
4449  N N   . SER A 606  ? 0.3022 0.4389 0.3031 0.0969  -0.0122 -0.1528 604  SER A N   
4450  C CA  A SER A 606  ? 0.2935 0.4313 0.2997 0.0979  -0.0165 -0.1599 604  SER A CA  
4451  C CA  B SER A 606  ? 0.2937 0.4318 0.2998 0.0980  -0.0165 -0.1599 604  SER A CA  
4452  C C   . SER A 606  ? 0.3398 0.4805 0.3400 0.0971  -0.0162 -0.1580 604  SER A C   
4453  O O   . SER A 606  ? 0.3366 0.4861 0.3283 0.0968  -0.0125 -0.1529 604  SER A O   
4454  C CB  A SER A 606  ? 0.3360 0.4875 0.3452 0.1007  -0.0177 -0.1661 604  SER A CB  
4455  C CB  B SER A 606  ? 0.3357 0.4882 0.3442 0.1008  -0.0173 -0.1658 604  SER A CB  
4456  O OG  A SER A 606  ? 0.3361 0.4843 0.3519 0.1016  -0.0186 -0.1686 604  SER A OG  
4457  O OG  B SER A 606  ? 0.3118 0.4680 0.3244 0.1020  -0.0212 -0.1724 604  SER A OG  
4458  N N   . VAL A 607  ? 0.2947 0.4278 0.2996 0.0965  -0.0200 -0.1617 605  VAL A N   
4459  C CA  . VAL A 607  ? 0.2851 0.4202 0.2853 0.0957  -0.0202 -0.1606 605  VAL A CA  
4460  C C   . VAL A 607  ? 0.3112 0.4526 0.3169 0.0975  -0.0243 -0.1685 605  VAL A C   
4461  O O   . VAL A 607  ? 0.3232 0.4590 0.3383 0.0982  -0.0282 -0.1742 605  VAL A O   
4462  C CB  . VAL A 607  ? 0.2981 0.4180 0.2980 0.0930  -0.0208 -0.1568 605  VAL A CB  
4463  C CG1 . VAL A 607  ? 0.3526 0.4594 0.3631 0.0924  -0.0253 -0.1609 605  VAL A CG1 
4464  C CG2 . VAL A 607  ? 0.3019 0.4249 0.2969 0.0923  -0.0211 -0.1558 605  VAL A CG2 
4465  N N   . THR A 608  ? 0.3172 0.4708 0.3174 0.0984  -0.0234 -0.1687 606  THR A N   
4466  C CA  . THR A 608  ? 0.3414 0.5010 0.3459 0.0999  -0.0271 -0.1756 606  THR A CA  
4467  C C   . THR A 608  ? 0.3389 0.4922 0.3407 0.0981  -0.0279 -0.1735 606  THR A C   
4468  O O   . THR A 608  ? 0.3210 0.4777 0.3140 0.0970  -0.0247 -0.1674 606  THR A O   
4469  C CB  . THR A 608  ? 0.3442 0.5226 0.3444 0.1022  -0.0256 -0.1772 606  THR A CB  
4470  O OG1 . THR A 608  ? 0.3394 0.5236 0.3423 0.1039  -0.0249 -0.1794 606  THR A OG1 
4471  C CG2 . THR A 608  ? 0.3725 0.5577 0.3769 0.1039  -0.0294 -0.1844 606  THR A CG2 
4472  N N   . GLU A 609  ? 0.3319 0.4760 0.3415 0.0977  -0.0322 -0.1781 607  GLU A N   
4473  C CA  . GLU A 609  ? 0.3602 0.4966 0.3682 0.0957  -0.0333 -0.1760 607  GLU A CA  
4474  C C   . GLU A 609  ? 0.3245 0.4714 0.3316 0.0970  -0.0350 -0.1799 607  GLU A C   
4475  O O   . GLU A 609  ? 0.3352 0.4928 0.3461 0.0995  -0.0368 -0.1861 607  GLU A O   
4476  C CB  . GLU A 609  ? 0.3808 0.5007 0.3975 0.0939  -0.0368 -0.1773 607  GLU A CB  
4477  C CG  . GLU A 609  ? 0.4309 0.5402 0.4467 0.0921  -0.0345 -0.1716 607  GLU A CG  
4478  C CD  . GLU A 609  ? 0.5147 0.6077 0.5388 0.0901  -0.0378 -0.1717 607  GLU A CD  
4479  O OE1 . GLU A 609  ? 0.5963 0.6870 0.6300 0.0906  -0.0423 -0.1775 607  GLU A OE1 
4480  O OE2 . GLU A 609  ? 0.4846 0.5675 0.5061 0.0878  -0.0360 -0.1658 607  GLU A OE2 
4481  N N   . THR A 610  ? 0.3280 0.4723 0.3298 0.0953  -0.0343 -0.1762 608  THR A N   
4482  C CA  . THR A 610  ? 0.3323 0.4871 0.3313 0.0963  -0.0350 -0.1782 608  THR A CA  
4483  C C   . THR A 610  ? 0.3713 0.5211 0.3792 0.0966  -0.0401 -0.1849 608  THR A C   
4484  O O   . THR A 610  ? 0.4211 0.5569 0.4335 0.0945  -0.0421 -0.1842 608  THR A O   
4485  C CB  . THR A 610  ? 0.3703 0.5238 0.3598 0.0943  -0.0321 -0.1708 608  THR A CB  
4486  O OG1 . THR A 610  ? 0.3381 0.4942 0.3201 0.0937  -0.0275 -0.1639 608  THR A OG1 
4487  C CG2 . THR A 610  ? 0.3482 0.5139 0.3339 0.0954  -0.0324 -0.1720 608  THR A CG2 
4488  N N   . SER A 611  ? 0.3669 0.5287 0.3779 0.0991  -0.0422 -0.1912 609  SER A N   
4489  C CA  . SER A 611  ? 0.3863 0.5448 0.4053 0.0994  -0.0469 -0.1972 609  SER A CA  
4490  C C   . SER A 611  ? 0.4376 0.5932 0.4513 0.0975  -0.0466 -0.1936 609  SER A C   
4491  O O   . SER A 611  ? 0.3937 0.5554 0.3976 0.0970  -0.0431 -0.1881 609  SER A O   
4492  C CB  . SER A 611  ? 0.4106 0.5839 0.4336 0.1027  -0.0491 -0.2049 609  SER A CB  
4493  O OG  . SER A 611  ? 0.4174 0.6040 0.4323 0.1036  -0.0470 -0.2033 609  SER A OG  
4494  N N   . GLU A 612  ? 0.4475 0.5936 0.4683 0.0964  -0.0504 -0.1965 610  GLU A N   
4495  C CA  . GLU A 612  ? 0.4556 0.5992 0.4724 0.0947  -0.0505 -0.1937 610  GLU A CA  
4496  C C   . GLU A 612  ? 0.4425 0.6018 0.4543 0.0967  -0.0500 -0.1956 610  GLU A C   
4497  O O   . GLU A 612  ? 0.4476 0.6089 0.4515 0.0956  -0.0480 -0.1909 610  GLU A O   
4498  C CB  . GLU A 612  ? 0.5280 0.6593 0.5542 0.0932  -0.0551 -0.1968 610  GLU A CB  
4499  C CG  . GLU A 612  ? 0.5420 0.6568 0.5695 0.0900  -0.0547 -0.1915 610  GLU A CG  
4500  C CD  . GLU A 612  ? 0.6064 0.7103 0.6466 0.0892  -0.0593 -0.1954 610  GLU A CD  
4501  O OE1 . GLU A 612  ? 0.6836 0.7875 0.7298 0.0905  -0.0603 -0.1984 610  GLU A OE1 
4502  O OE2 . GLU A 612  ? 0.6686 0.7640 0.7131 0.0872  -0.0620 -0.1952 610  GLU A OE2 
4503  N N   . GLU A 613  ? 0.4070 0.5779 0.4232 0.0998  -0.0516 -0.2023 611  GLU A N   
4504  C CA  . GLU A 613  ? 0.4987 0.6860 0.5103 0.1019  -0.0509 -0.2040 611  GLU A CA  
4505  C C   . GLU A 613  ? 0.4079 0.6042 0.4081 0.1017  -0.0458 -0.1969 611  GLU A C   
4506  O O   . GLU A 613  ? 0.3681 0.5720 0.3613 0.1016  -0.0442 -0.1935 611  GLU A O   
4507  C CB  . GLU A 613  ? 0.4843 0.6825 0.5036 0.1053  -0.0537 -0.2129 611  GLU A CB  
4508  N N   . ASP A 614  ? 0.3878 0.5835 0.3863 0.1018  -0.0433 -0.1942 612  ASP A N   
4509  C CA  . ASP A 614  ? 0.3412 0.5452 0.3295 0.1015  -0.0385 -0.1870 612  ASP A CA  
4510  C C   . ASP A 614  ? 0.3568 0.5517 0.3377 0.0984  -0.0359 -0.1784 612  ASP A C   
4511  O O   . ASP A 614  ? 0.3432 0.5461 0.3155 0.0980  -0.0326 -0.1722 612  ASP A O   
4512  C CB  . ASP A 614  ? 0.3746 0.5801 0.3636 0.1023  -0.0366 -0.1865 612  ASP A CB  
4513  C CG  . ASP A 614  ? 0.4033 0.6225 0.3971 0.1056  -0.0382 -0.1938 612  ASP A CG  
4514  O OD1 . ASP A 614  ? 0.4433 0.6751 0.4365 0.1073  -0.0392 -0.1969 612  ASP A OD1 
4515  O OD2 . ASP A 614  ? 0.4498 0.6674 0.4481 0.1065  -0.0385 -0.1963 612  ASP A OD2 
4516  N N   . ALA A 615  ? 0.3209 0.4995 0.3053 0.0963  -0.0374 -0.1778 613  ALA A N   
4517  C CA  . ALA A 615  ? 0.3253 0.4954 0.3033 0.0935  -0.0353 -0.1704 613  ALA A CA  
4518  C C   . ALA A 615  ? 0.3471 0.5233 0.3210 0.0933  -0.0359 -0.1695 613  ALA A C   
4519  O O   . ALA A 615  ? 0.3279 0.5075 0.2933 0.0922  -0.0329 -0.1626 613  ALA A O   
4520  C CB  . ALA A 615  ? 0.3447 0.4968 0.3284 0.0913  -0.0374 -0.1707 613  ALA A CB  
4521  N N   . ARG A 616  ? 0.3824 0.5602 0.3628 0.0944  -0.0398 -0.1764 614  ARG A N   
4522  C CA  . ARG A 616  ? 0.3793 0.5639 0.3564 0.0946  -0.0405 -0.1763 614  ARG A CA  
4523  C C   . ARG A 616  ? 0.3566 0.5589 0.3269 0.0963  -0.0378 -0.1739 614  ARG A C   
4524  O O   . ARG A 616  ? 0.3650 0.5722 0.3283 0.0955  -0.0361 -0.1687 614  ARG A O   
4525  C CB  . ARG A 616  ? 0.4095 0.5931 0.3957 0.0957  -0.0453 -0.1847 614  ARG A CB  
4526  C CG  . ARG A 616  ? 0.5096 0.6761 0.5020 0.0933  -0.0481 -0.1855 614  ARG A CG  
4527  C CD  . ARG A 616  ? 0.6060 0.7718 0.6081 0.0943  -0.0529 -0.1935 614  ARG A CD  
4528  N NE  . ARG A 616  ? 0.6412 0.7981 0.6537 0.0944  -0.0559 -0.1981 614  ARG A NE  
4529  C CZ  . ARG A 616  ? 0.5894 0.7528 0.6090 0.0971  -0.0580 -0.2051 614  ARG A CZ  
4530  N NH1 . ARG A 616  ? 0.6618 0.8411 0.6795 0.1000  -0.0577 -0.2087 614  ARG A NH1 
4531  N NH2 . ARG A 616  ? 0.5929 0.7468 0.6221 0.0968  -0.0607 -0.2084 614  ARG A NH2 
4532  N N   . ARG A 617  ? 0.3268 0.5390 0.2993 0.0987  -0.0375 -0.1775 615  ARG A N   
4533  C CA  . ARG A 617  ? 0.3700 0.5994 0.3363 0.1003  -0.0349 -0.1748 615  ARG A CA  
4534  C C   . ARG A 617  ? 0.3657 0.5950 0.3227 0.0983  -0.0303 -0.1644 615  ARG A C   
4535  O O   . ARG A 617  ? 0.3388 0.5783 0.2894 0.0982  -0.0284 -0.1593 615  ARG A O   
4536  C CB  . ARG A 617  ? 0.3980 0.6375 0.3688 0.1030  -0.0354 -0.1805 615  ARG A CB  
4537  C CG  . ARG A 617  ? 0.4676 0.7263 0.4331 0.1048  -0.0332 -0.1785 615  ARG A CG  
4538  C CD  . ARG A 617  ? 0.5352 0.8055 0.5072 0.1081  -0.0353 -0.1871 615  ARG A CD  
4539  N NE  . ARG A 617  ? 0.5102 0.7759 0.4860 0.1085  -0.0349 -0.1889 615  ARG A NE  
4540  C CZ  . ARG A 617  ? 0.6029 0.8764 0.5748 0.1089  -0.0318 -0.1851 615  ARG A CZ  
4541  N NH1 . ARG A 617  ? 0.5517 0.8378 0.5159 0.1088  -0.0287 -0.1788 615  ARG A NH1 
4542  N NH2 . ARG A 617  ? 0.5294 0.7980 0.5055 0.1094  -0.0318 -0.1874 615  ARG A NH2 
4543  N N   . ALA A 618  ? 0.3350 0.5527 0.2917 0.0967  -0.0287 -0.1610 616  ALA A N   
4544  C CA  . ALA A 618  ? 0.3358 0.5529 0.2844 0.0948  -0.0245 -0.1512 616  ALA A CA  
4545  C C   . ALA A 618  ? 0.3050 0.5186 0.2481 0.0928  -0.0239 -0.1454 616  ALA A C   
4546  O O   . ALA A 618  ? 0.3223 0.5431 0.2582 0.0921  -0.0210 -0.1378 616  ALA A O   
4547  C CB  . ALA A 618  ? 0.3382 0.5424 0.2884 0.0935  -0.0233 -0.1494 616  ALA A CB  
4548  N N   . VAL A 619  ? 0.3020 0.5049 0.2487 0.0918  -0.0269 -0.1487 617  VAL A N   
4549  C CA  . VAL A 619  ? 0.3093 0.5090 0.2511 0.0900  -0.0266 -0.1437 617  VAL A CA  
4550  C C   . VAL A 619  ? 0.3227 0.5376 0.2610 0.0912  -0.0265 -0.1429 617  VAL A C   
4551  O O   . VAL A 619  ? 0.3259 0.5445 0.2573 0.0901  -0.0244 -0.1354 617  VAL A O   
4552  C CB  . VAL A 619  ? 0.3236 0.5091 0.2706 0.0887  -0.0300 -0.1478 617  VAL A CB  
4553  C CG1 . VAL A 619  ? 0.3429 0.5263 0.2849 0.0869  -0.0299 -0.1430 617  VAL A CG1 
4554  C CG2 . VAL A 619  ? 0.3237 0.4943 0.2737 0.0872  -0.0298 -0.1473 617  VAL A CG2 
4555  N N   . ARG A 620  ? 0.3217 0.5457 0.2648 0.0937  -0.0290 -0.1505 618  ARG A N   
4556  C CA  . ARG A 620  ? 0.3363 0.5756 0.2765 0.0950  -0.0290 -0.1501 618  ARG A CA  
4557  C C   . ARG A 620  ? 0.3511 0.6029 0.2848 0.0953  -0.0251 -0.1429 618  ARG A C   
4558  O O   . ARG A 620  ? 0.3904 0.6501 0.3186 0.0947  -0.0237 -0.1370 618  ARG A O   
4559  C CB  . ARG A 620  ? 0.3851 0.6321 0.3323 0.0978  -0.0323 -0.1602 618  ARG A CB  
4560  C CG  . ARG A 620  ? 0.4664 0.7031 0.4201 0.0975  -0.0364 -0.1666 618  ARG A CG  
4561  C CD  . ARG A 620  ? 0.5544 0.7999 0.5154 0.1004  -0.0398 -0.1764 618  ARG A CD  
4562  N NE  . ARG A 620  ? 0.6512 0.8872 0.6212 0.1009  -0.0426 -0.1834 618  ARG A NE  
4563  C CZ  . ARG A 620  ? 0.5390 0.7810 0.5137 0.1032  -0.0431 -0.1886 618  ARG A CZ  
4564  N NH1 . ARG A 620  ? 0.5909 0.8490 0.5624 0.1052  -0.0412 -0.1883 618  ARG A NH1 
4565  N NH2 . ARG A 620  ? 0.5755 0.8074 0.5587 0.1033  -0.0458 -0.1943 618  ARG A NH2 
4566  N N   . LEU A 621  ? 0.3025 0.5560 0.2372 0.0959  -0.0235 -0.1430 619  LEU A N   
4567  C CA  . LEU A 621  ? 0.3772 0.6418 0.3062 0.0959  -0.0198 -0.1355 619  LEU A CA  
4568  C C   . LEU A 621  ? 0.3317 0.5899 0.2541 0.0930  -0.0169 -0.1249 619  LEU A C   
4569  O O   . LEU A 621  ? 0.3535 0.6217 0.2707 0.0925  -0.0147 -0.1175 619  LEU A O   
4570  C CB  . LEU A 621  ? 0.3472 0.6132 0.2790 0.0969  -0.0187 -0.1377 619  LEU A CB  
4571  C CG  . LEU A 621  ? 0.3453 0.6195 0.2837 0.1000  -0.0213 -0.1477 619  LEU A CG  
4572  C CD1 . LEU A 621  ? 0.3270 0.5992 0.2685 0.1007  -0.0204 -0.1497 619  LEU A CD1 
4573  C CD2 . LEU A 621  ? 0.4012 0.6950 0.3376 0.1019  -0.0210 -0.1478 619  LEU A CD2 
4574  N N   . ALA A 622  ? 0.3159 0.5576 0.2389 0.0912  -0.0171 -0.1240 620  ALA A N   
4575  C CA  . ALA A 622  ? 0.3383 0.5731 0.2555 0.0886  -0.0148 -0.1146 620  ALA A CA  
4576  C C   . ALA A 622  ? 0.3049 0.5436 0.2187 0.0879  -0.0156 -0.1112 620  ALA A C   
4577  O O   . ALA A 622  ? 0.3497 0.5929 0.2581 0.0866  -0.0132 -0.1022 620  ALA A O   
4578  C CB  . ALA A 622  ? 0.3078 0.5245 0.2271 0.0870  -0.0154 -0.1156 620  ALA A CB  
4579  N N   . ALA A 623  ? 0.3151 0.5523 0.2325 0.0887  -0.0190 -0.1182 621  ALA A N   
4580  C CA  . ALA A 623  ? 0.3258 0.5673 0.2404 0.0882  -0.0199 -0.1157 621  ALA A CA  
4581  C C   . ALA A 623  ? 0.3140 0.5735 0.2254 0.0894  -0.0184 -0.1119 621  ALA A C   
4582  O O   . ALA A 623  ? 0.3479 0.6115 0.2545 0.0882  -0.0172 -0.1042 621  ALA A O   
4583  C CB  . ALA A 623  ? 0.3645 0.6021 0.2845 0.0891  -0.0240 -0.1248 621  ALA A CB  
4584  N N   . ASP A 624  ? 0.3056 0.5761 0.2198 0.0917  -0.0186 -0.1170 622  ASP A N   
4585  C CA  . ASP A 624  ? 0.3877 0.6764 0.2994 0.0929  -0.0173 -0.1138 622  ASP A CA  
4586  C C   . ASP A 624  ? 0.3816 0.6736 0.2880 0.0912  -0.0135 -0.1025 622  ASP A C   
4587  O O   . ASP A 624  ? 0.4454 0.7480 0.3483 0.0908  -0.0124 -0.0958 622  ASP A O   
4588  C CB  . ASP A 624  ? 0.4295 0.7287 0.3456 0.0958  -0.0181 -0.1216 622  ASP A CB  
4589  C CG  . ASP A 624  ? 0.5339 0.8327 0.4561 0.0978  -0.0220 -0.1327 622  ASP A CG  
4590  O OD1 . ASP A 624  ? 0.5958 0.8905 0.5180 0.0972  -0.0240 -0.1338 622  ASP A OD1 
4591  O OD2 . ASP A 624  ? 0.5757 0.8784 0.5029 0.0999  -0.0233 -0.1402 622  ASP A OD2 
4592  N N   . ALA A 625  ? 0.4248 0.7080 0.3310 0.0901  -0.0117 -0.1000 623  ALA A N   
4593  C CA  . ALA A 625  ? 0.4487 0.7340 0.3508 0.0884  -0.0082 -0.0896 623  ALA A CA  
4594  C C   . ALA A 625  ? 0.4184 0.6933 0.3167 0.0857  -0.0072 -0.0811 623  ALA A C   
4595  O O   . ALA A 625  ? 0.4793 0.7558 0.3745 0.0841  -0.0044 -0.0716 623  ALA A O   
4596  C CB  . ALA A 625  ? 0.4862 0.7666 0.3903 0.0886  -0.0068 -0.0912 623  ALA A CB  
4597  N N   . ALA A 626  ? 0.3859 0.6502 0.2846 0.0851  -0.0094 -0.0842 624  ALA A N   
4598  C CA  . ALA A 626  ? 0.3632 0.6173 0.2586 0.0826  -0.0086 -0.0765 624  ALA A CA  
4599  C C   . ALA A 626  ? 0.3735 0.6368 0.2649 0.0814  -0.0070 -0.0660 624  ALA A C   
4600  O O   . ALA A 626  ? 0.3763 0.6350 0.2651 0.0795  -0.0048 -0.0571 624  ALA A O   
4601  C CB  . ALA A 626  ? 0.3738 0.6167 0.2708 0.0823  -0.0116 -0.0822 624  ALA A CB  
4602  N N   . PRO A 627  ? 0.3628 0.6389 0.2538 0.0825  -0.0080 -0.0663 625  PRO A N   
4603  C CA  . PRO A 627  ? 0.3820 0.6662 0.2698 0.0811  -0.0065 -0.0556 625  PRO A CA  
4604  C C   . PRO A 627  ? 0.3558 0.6463 0.2426 0.0803  -0.0034 -0.0474 625  PRO A C   
4605  O O   . PRO A 627  ? 0.3907 0.6797 0.2756 0.0782  -0.0019 -0.0370 625  PRO A O   
4606  C CB  . PRO A 627  ? 0.3648 0.6629 0.2533 0.0829  -0.0082 -0.0593 625  PRO A CB  
4607  C CG  . PRO A 627  ? 0.3724 0.6644 0.2640 0.0845  -0.0112 -0.0711 625  PRO A CG  
4608  C CD  . PRO A 627  ? 0.4014 0.6847 0.2953 0.0848  -0.0106 -0.0759 625  PRO A CD  
4609  N N   . ASP A 628  ? 0.3617 0.6593 0.2504 0.0818  -0.0026 -0.0517 626  ASP A N   
4610  C CA  . ASP A 628  ? 0.3648 0.6695 0.2529 0.0810  0.0003  -0.0440 626  ASP A CA  
4611  C C   . ASP A 628  ? 0.4134 0.7048 0.3006 0.0789  0.0022  -0.0382 626  ASP A C   
4612  O O   . ASP A 628  ? 0.3950 0.6891 0.2813 0.0771  0.0044  -0.0282 626  ASP A O   
4613  C CB  . ASP A 628  ? 0.3813 0.6962 0.2719 0.0833  0.0006  -0.0507 626  ASP A CB  
4614  C CG  . ASP A 628  ? 0.4359 0.7669 0.3273 0.0854  -0.0008 -0.0550 626  ASP A CG  
4615  O OD1 . ASP A 628  ? 0.5208 0.8575 0.4106 0.0848  -0.0013 -0.0502 626  ASP A OD1 
4616  O OD2 . ASP A 628  ? 0.5533 0.8914 0.4474 0.0878  -0.0015 -0.0631 626  ASP A OD2 
4617  N N   . TRP A 629  ? 0.3494 0.6265 0.2374 0.0789  0.0013  -0.0443 627  TRP A N   
4618  C CA  . TRP A 629  ? 0.3498 0.6145 0.2371 0.0771  0.0030  -0.0393 627  TRP A CA  
4619  C C   . TRP A 629  ? 0.3246 0.5816 0.2096 0.0749  0.0029  -0.0313 627  TRP A C   
4620  O O   . TRP A 629  ? 0.3438 0.5962 0.2288 0.0727  0.0049  -0.0221 627  TRP A O   
4621  C CB  . TRP A 629  ? 0.3329 0.5856 0.2223 0.0779  0.0021  -0.0485 627  TRP A CB  
4622  C CG  . TRP A 629  ? 0.3084 0.5468 0.1991 0.0756  0.0038  -0.0432 627  TRP A CG  
4623  C CD1 . TRP A 629  ? 0.2730 0.4930 0.1678 0.0734  0.0026  -0.0437 627  TRP A CD1 
4624  C CD2 . TRP A 629  ? 0.2849 0.5246 0.1757 0.0743  0.0067  -0.0357 627  TRP A CD2 
4625  N NE1 . TRP A 629  ? 0.2985 0.5086 0.1957 0.0711  0.0045  -0.0374 627  TRP A NE1 
4626  C CE2 . TRP A 629  ? 0.2843 0.5057 0.1793 0.0715  0.0070  -0.0324 627  TRP A CE2 
4627  C CE3 . TRP A 629  ? 0.3143 0.5686 0.2028 0.0750  0.0089  -0.0313 627  TRP A CE3 
4628  C CZ2 . TRP A 629  ? 0.2993 0.5168 0.1957 0.0697  0.0094  -0.0254 627  TRP A CZ2 
4629  C CZ3 . TRP A 629  ? 0.3028 0.5536 0.1923 0.0732  0.0115  -0.0240 627  TRP A CZ3 
4630  C CH2 . TRP A 629  ? 0.3326 0.5648 0.2265 0.0705  0.0116  -0.0212 627  TRP A CH2 
4631  N N   . ALA A 630  ? 0.3216 0.5765 0.2060 0.0752  0.0005  -0.0345 628  ALA A N   
4632  C CA  . ALA A 630  ? 0.3633 0.6103 0.2479 0.0728  0.0000  -0.0267 628  ALA A CA  
4633  C C   . ALA A 630  ? 0.3573 0.6155 0.2391 0.0720  0.0016  -0.0156 628  ALA A C   
4634  O O   . ALA A 630  ? 0.3758 0.6259 0.2597 0.0693  0.0020  -0.0067 628  ALA A O   
4635  C CB  . ALA A 630  ? 0.3482 0.5934 0.2327 0.0736  -0.0030 -0.0326 628  ALA A CB  
4636  N N   . ALA A 631  ? 0.3476 0.6208 0.2301 0.0730  0.0021  -0.0155 629  ALA A N   
4637  C CA  . ALA A 631  ? 0.3836 0.6673 0.2661 0.0718  0.0034  -0.0049 629  ALA A CA  
4638  C C   . ALA A 631  ? 0.3824 0.6653 0.2659 0.0701  0.0061  0.0033  629  ALA A C   
4639  O O   . ALA A 631  ? 0.3584 0.6473 0.2428 0.0685  0.0070  0.0135  629  ALA A O   
4640  C CB  . ALA A 631  ? 0.3693 0.6703 0.2524 0.0736  0.0029  -0.0081 629  ALA A CB  
4641  N N   . VAL A 632  ? 0.3279 0.6038 0.2118 0.0704  0.0072  -0.0007 630  VAL A N   
4642  C CA  . VAL A 632  ? 0.3236 0.5972 0.2087 0.0686  0.0098  0.0073  630  VAL A CA  
4643  C C   . VAL A 632  ? 0.3363 0.5968 0.2217 0.0662  0.0096  0.0148  630  VAL A C   
4644  O O   . VAL A 632  ? 0.3472 0.5925 0.2352 0.0656  0.0082  0.0099  630  VAL A O   
4645  C CB  . VAL A 632  ? 0.3375 0.6067 0.2231 0.0697  0.0109  0.0005  630  VAL A CB  
4646  C CG1 . VAL A 632  ? 0.3265 0.5929 0.2135 0.0677  0.0135  0.0089  630  VAL A CG1 
4647  C CG2 . VAL A 632  ? 0.3492 0.6313 0.2357 0.0721  0.0106  -0.0074 630  VAL A CG2 
4648  N N   . PRO A 633  ? 0.3078 0.5711 0.1942 0.0642  0.0106  0.0265  631  PRO A N   
4649  C CA  . PRO A 633  ? 0.2907 0.5394 0.1812 0.0615  0.0098  0.0330  631  PRO A CA  
4650  C C   . PRO A 633  ? 0.3280 0.5584 0.2228 0.0599  0.0103  0.0304  631  PRO A C   
4651  O O   . PRO A 633  ? 0.3180 0.5483 0.2133 0.0603  0.0120  0.0280  631  PRO A O   
4652  C CB  . PRO A 633  ? 0.3461 0.6030 0.2376 0.0598  0.0110  0.0457  631  PRO A CB  
4653  C CG  . PRO A 633  ? 0.3729 0.6478 0.2635 0.0612  0.0115  0.0448  631  PRO A CG  
4654  C CD  . PRO A 633  ? 0.3529 0.6298 0.2414 0.0635  0.0119  0.0335  631  PRO A CD  
4655  N N   . PRO A 634  ? 0.2823 0.4977 0.1805 0.0583  0.0090  0.0307  632  PRO A N   
4656  C CA  . PRO A 634  ? 0.2733 0.4716 0.1755 0.0568  0.0094  0.0283  632  PRO A CA  
4657  C C   . PRO A 634  ? 0.2814 0.4781 0.1862 0.0553  0.0116  0.0347  632  PRO A C   
4658  O O   . PRO A 634  ? 0.2702 0.4597 0.1764 0.0551  0.0125  0.0305  632  PRO A O   
4659  C CB  . PRO A 634  ? 0.3001 0.4858 0.2054 0.0551  0.0078  0.0304  632  PRO A CB  
4660  C CG  . PRO A 634  ? 0.2932 0.4879 0.1953 0.0565  0.0060  0.0293  632  PRO A CG  
4661  C CD  . PRO A 634  ? 0.3022 0.5159 0.2004 0.0580  0.0069  0.0324  632  PRO A CD  
4662  N N   . SER A 635  ? 0.3057 0.5091 0.2114 0.0540  0.0123  0.0449  633  SER A N   
4663  C CA  . SER A 635  ? 0.3019 0.5039 0.2107 0.0524  0.0142  0.0515  633  SER A CA  
4664  C C   . SER A 635  ? 0.2939 0.5053 0.2000 0.0540  0.0161  0.0474  633  SER A C   
4665  O O   . SER A 635  ? 0.3053 0.5104 0.2139 0.0531  0.0174  0.0474  633  SER A O   
4666  C CB  . SER A 635  ? 0.3964 0.6057 0.3070 0.0509  0.0144  0.0633  633  SER A CB  
4667  N N   . GLU A 636  ? 0.2935 0.5205 0.1948 0.0565  0.0160  0.0437  634  GLU A N   
4668  C CA  . GLU A 636  ? 0.3008 0.5379 0.1995 0.0583  0.0177  0.0392  634  GLU A CA  
4669  C C   . GLU A 636  ? 0.2964 0.5240 0.1953 0.0596  0.0172  0.0277  634  GLU A C   
4670  O O   . GLU A 636  ? 0.3121 0.5395 0.2118 0.0601  0.0186  0.0250  634  GLU A O   
4671  C CB  . GLU A 636  ? 0.3199 0.5778 0.2135 0.0606  0.0178  0.0388  634  GLU A CB  
4672  C CG  . GLU A 636  ? 0.3804 0.6488 0.2730 0.0625  0.0192  0.0331  634  GLU A CG  
4673  C CD  . GLU A 636  ? 0.5092 0.7765 0.4044 0.0610  0.0216  0.0387  634  GLU A CD  
4674  O OE1 . GLU A 636  ? 0.5287 0.7967 0.4268 0.0586  0.0223  0.0495  634  GLU A OE1 
4675  O OE2 . GLU A 636  ? 0.4410 0.7063 0.3359 0.0623  0.0226  0.0322  634  GLU A OE2 
4676  N N   . ARG A 637  ? 0.2840 0.5035 0.1827 0.0602  0.0151  0.0212  635  ARG A N   
4677  C CA  . ARG A 637  ? 0.2625 0.4712 0.1626 0.0610  0.0143  0.0114  635  ARG A CA  
4678  C C   . ARG A 637  ? 0.2632 0.4568 0.1679 0.0586  0.0153  0.0141  635  ARG A C   
4679  O O   . ARG A 637  ? 0.2721 0.4619 0.1779 0.0592  0.0160  0.0091  635  ARG A O   
4680  C CB  . ARG A 637  ? 0.2742 0.4762 0.1741 0.0615  0.0118  0.0052  635  ARG A CB  
4681  C CG  . ARG A 637  ? 0.2808 0.4979 0.1764 0.0639  0.0106  0.0022  635  ARG A CG  
4682  C CD  . ARG A 637  ? 0.2913 0.5027 0.1868 0.0649  0.0080  -0.0064 635  ARG A CD  
4683  N NE  . ARG A 637  ? 0.3054 0.5029 0.2037 0.0627  0.0068  -0.0032 635  ARG A NE  
4684  C CZ  . ARG A 637  ? 0.2926 0.4920 0.1899 0.0624  0.0054  -0.0007 635  ARG A CZ  
4685  N NH1 . ARG A 637  ? 0.3203 0.5352 0.2137 0.0641  0.0049  -0.0002 635  ARG A NH1 
4686  N NH2 . ARG A 637  ? 0.2967 0.4826 0.1970 0.0604  0.0043  0.0011  635  ARG A NH2 
4687  N N   . ALA A 638  ? 0.2634 0.4485 0.1709 0.0561  0.0152  0.0220  636  ALA A N   
4688  C CA  . ALA A 638  ? 0.2543 0.4257 0.1661 0.0538  0.0160  0.0250  636  ALA A CA  
4689  C C   . ALA A 638  ? 0.2626 0.4400 0.1751 0.0535  0.0183  0.0289  636  ALA A C   
4690  O O   . ALA A 638  ? 0.2549 0.4237 0.1700 0.0528  0.0191  0.0272  636  ALA A O   
4691  C CB  . ALA A 638  ? 0.2637 0.4269 0.1786 0.0513  0.0154  0.0328  636  ALA A CB  
4692  N N   . ALA A 639  ? 0.2567 0.4495 0.1670 0.0541  0.0194  0.0344  637  ALA A N   
4693  C CA  . ALA A 639  ? 0.2581 0.4584 0.1689 0.0540  0.0216  0.0381  637  ALA A CA  
4694  C C   . ALA A 639  ? 0.2744 0.4774 0.1837 0.0562  0.0223  0.0289  637  ALA A C   
4695  O O   . ALA A 639  ? 0.2784 0.4794 0.1898 0.0557  0.0238  0.0295  637  ALA A O   
4696  C CB  . ALA A 639  ? 0.2878 0.5055 0.1964 0.0542  0.0225  0.0457  637  ALA A CB  
4697  N N   . CYS A 640  ? 0.2589 0.4665 0.1650 0.0587  0.0210  0.0200  638  CYS A N   
4698  C CA  . CYS A 640  ? 0.2683 0.4768 0.1739 0.0609  0.0211  0.0103  638  CYS A CA  
4699  C C   . CYS A 640  ? 0.2722 0.4628 0.1818 0.0596  0.0207  0.0071  638  CYS A C   
4700  O O   . CYS A 640  ? 0.2646 0.4540 0.1757 0.0600  0.0218  0.0043  638  CYS A O   
4701  C CB  . CYS A 640  ? 0.2744 0.4888 0.1769 0.0637  0.0192  0.0010  638  CYS A CB  
4702  S SG  . CYS A 640  ? 0.3034 0.5413 0.2006 0.0661  0.0196  0.0020  638  CYS A SG  
4703  N N   . LEU A 641  ? 0.2516 0.4288 0.1632 0.0579  0.0191  0.0075  639  LEU A N   
4704  C CA  . LEU A 641  ? 0.2537 0.4143 0.1690 0.0565  0.0187  0.0049  639  LEU A CA  
4705  C C   . LEU A 641  ? 0.2519 0.4086 0.1701 0.0544  0.0206  0.0118  639  LEU A C   
4706  O O   . LEU A 641  ? 0.2480 0.3982 0.1684 0.0543  0.0211  0.0086  639  LEU A O   
4707  C CB  . LEU A 641  ? 0.2589 0.4074 0.1756 0.0549  0.0169  0.0052  639  LEU A CB  
4708  C CG  . LEU A 641  ? 0.2744 0.4193 0.1904 0.0564  0.0146  -0.0039 639  LEU A CG  
4709  C CD1 . LEU A 641  ? 0.3046 0.4639 0.2166 0.0590  0.0139  -0.0077 639  LEU A CD1 
4710  C CD2 . LEU A 641  ? 0.2473 0.3798 0.1652 0.0544  0.0132  -0.0023 639  LEU A CD2 
4711  N N   . ASP A 642  ? 0.2443 0.4047 0.1630 0.0528  0.0215  0.0212  640  ASP A N   
4712  C CA  . ASP A 642  ? 0.2665 0.4232 0.1885 0.0507  0.0231  0.0279  640  ASP A CA  
4713  C C   . ASP A 642  ? 0.2613 0.4279 0.1826 0.0521  0.0250  0.0267  640  ASP A C   
4714  O O   . ASP A 642  ? 0.2634 0.4237 0.1875 0.0511  0.0260  0.0272  640  ASP A O   
4715  C CB  . ASP A 642  ? 0.2661 0.4256 0.1895 0.0488  0.0234  0.0384  640  ASP A CB  
4716  C CG  . ASP A 642  ? 0.2813 0.4272 0.2075 0.0469  0.0219  0.0405  640  ASP A CG  
4717  O OD1 . ASP A 642  ? 0.3041 0.4372 0.2320 0.0464  0.0211  0.0355  640  ASP A OD1 
4718  O OD2 . ASP A 642  ? 0.3003 0.4488 0.2273 0.0458  0.0214  0.0475  640  ASP A OD2 
4719  N N   . ARG A 643  ? 0.2591 0.4417 0.1766 0.0543  0.0255  0.0250  641  ARG A N   
4720  C CA  . ARG A 643  ? 0.2411 0.4340 0.1577 0.0559  0.0273  0.0228  641  ARG A CA  
4721  C C   . ARG A 643  ? 0.2851 0.4704 0.2028 0.0573  0.0267  0.0131  641  ARG A C   
4722  O O   . ARG A 643  ? 0.2902 0.4753 0.2097 0.0574  0.0280  0.0125  641  ARG A O   
4723  C CB  . ARG A 643  ? 0.2843 0.4967 0.1964 0.0583  0.0278  0.0220  641  ARG A CB  
4724  C CG  . ARG A 643  ? 0.2787 0.5019 0.1903 0.0569  0.0290  0.0330  641  ARG A CG  
4725  C CD  . ARG A 643  ? 0.2845 0.5287 0.1915 0.0594  0.0298  0.0321  641  ARG A CD  
4726  N NE  . ARG A 643  ? 0.3024 0.5503 0.2058 0.0615  0.0279  0.0254  641  ARG A NE  
4727  C CZ  . ARG A 643  ? 0.3016 0.5538 0.2031 0.0611  0.0269  0.0298  641  ARG A CZ  
4728  N NH1 . ARG A 643  ? 0.3384 0.5908 0.2418 0.0585  0.0273  0.0410  641  ARG A NH1 
4729  N NH2 . ARG A 643  ? 0.3425 0.5990 0.2407 0.0632  0.0252  0.0229  641  ARG A NH2 
4730  N N   . ALA A 644  ? 0.2324 0.4116 0.1494 0.0585  0.0246  0.0055  642  ALA A N   
4731  C CA  . ALA A 644  ? 0.2472 0.4183 0.1660 0.0596  0.0237  -0.0034 642  ALA A CA  
4732  C C   . ALA A 644  ? 0.2341 0.3898 0.1571 0.0571  0.0240  -0.0007 642  ALA A C   
4733  O O   . ALA A 644  ? 0.2661 0.4184 0.1912 0.0576  0.0243  -0.0047 642  ALA A O   
4734  C CB  . ALA A 644  ? 0.2711 0.4381 0.1890 0.0610  0.0212  -0.0113 642  ALA A CB  
4735  N N   . ALA A 645  ? 0.2386 0.3852 0.1631 0.0544  0.0237  0.0058  643  ALA A N   
4736  C CA  . ALA A 645  ? 0.2530 0.3859 0.1814 0.0520  0.0240  0.0086  643  ALA A CA  
4737  C C   . ALA A 645  ? 0.2833 0.4205 0.2133 0.0514  0.0261  0.0131  643  ALA A C   
4738  O O   . ALA A 645  ? 0.2725 0.4022 0.2052 0.0509  0.0264  0.0111  643  ALA A O   
4739  C CB  . ALA A 645  ? 0.2553 0.3796 0.1850 0.0495  0.0233  0.0147  643  ALA A CB  
4740  N N   . GLU A 646  ? 0.2619 0.4112 0.1907 0.0513  0.0276  0.0196  644  GLU A N   
4741  C CA  . GLU A 646  ? 0.2757 0.4306 0.2061 0.0507  0.0296  0.0240  644  GLU A CA  
4742  C C   . GLU A 646  ? 0.2997 0.4601 0.2295 0.0532  0.0303  0.0167  644  GLU A C   
4743  O O   . GLU A 646  ? 0.2778 0.4349 0.2103 0.0526  0.0313  0.0171  644  GLU A O   
4744  C CB  . GLU A 646  ? 0.3257 0.4948 0.2546 0.0505  0.0309  0.0319  644  GLU A CB  
4745  C CG  . GLU A 646  ? 0.4454 0.6098 0.3763 0.0479  0.0304  0.0407  644  GLU A CG  
4746  C CD  . GLU A 646  ? 0.5759 0.7288 0.5119 0.0451  0.0308  0.0458  644  GLU A CD  
4747  O OE1 . GLU A 646  ? 0.5913 0.7446 0.5290 0.0450  0.0321  0.0454  644  GLU A OE1 
4748  O OE2 . GLU A 646  ? 0.5492 0.6927 0.4876 0.0431  0.0297  0.0501  644  GLU A OE2 
4749  N N   . LEU A 647  ? 0.2610 0.4298 0.1875 0.0560  0.0295  0.0096  645  LEU A N   
4750  C CA  . LEU A 647  ? 0.2459 0.4205 0.1723 0.0587  0.0299  0.0019  645  LEU A CA  
4751  C C   . LEU A 647  ? 0.3202 0.4800 0.2499 0.0584  0.0286  -0.0041 645  LEU A C   
4752  O O   . LEU A 647  ? 0.2942 0.4539 0.2259 0.0591  0.0294  -0.0066 645  LEU A O   
4753  C CB  . LEU A 647  ? 0.2924 0.4792 0.2150 0.0619  0.0290  -0.0049 645  LEU A CB  
4754  C CG  . LEU A 647  ? 0.2751 0.4801 0.1941 0.0627  0.0305  -0.0002 645  LEU A CG  
4755  C CD1 . LEU A 647  ? 0.2904 0.5056 0.2058 0.0659  0.0292  -0.0078 645  LEU A CD1 
4756  C CD2 . LEU A 647  ? 0.3498 0.5662 0.2693 0.0633  0.0330  0.0026  645  LEU A CD2 
4757  N N   . MET A 648  ? 0.2661 0.4135 0.1965 0.0574  0.0266  -0.0061 646  MET A N   
4758  C CA  . MET A 648  ? 0.2708 0.4042 0.2045 0.0569  0.0253  -0.0108 646  MET A CA  
4759  C C   . MET A 648  ? 0.2678 0.3931 0.2047 0.0543  0.0265  -0.0050 646  MET A C   
4760  O O   . MET A 648  ? 0.2914 0.4111 0.2310 0.0545  0.0264  -0.0084 646  MET A O   
4761  C CB  . MET A 648  ? 0.2569 0.3796 0.1908 0.0561  0.0230  -0.0134 646  MET A CB  
4762  C CG  . MET A 648  ? 0.2886 0.4167 0.2207 0.0588  0.0213  -0.0214 646  MET A CG  
4763  S SD  . MET A 648  ? 0.3229 0.4363 0.2566 0.0576  0.0184  -0.0252 646  MET A SD  
4764  C CE  . MET A 648  ? 0.3446 0.4680 0.2762 0.0610  0.0166  -0.0340 646  MET A CE  
4765  N N   . GLN A 649  ? 0.2798 0.4041 0.2168 0.0520  0.0275  0.0036  647  GLN A N   
4766  C CA  . GLN A 649  ? 0.2754 0.3924 0.2158 0.0495  0.0285  0.0091  647  GLN A CA  
4767  C C   . GLN A 649  ? 0.2704 0.3955 0.2117 0.0505  0.0303  0.0093  647  GLN A C   
4768  O O   . GLN A 649  ? 0.3038 0.4220 0.2482 0.0497  0.0306  0.0086  647  GLN A O   
4769  C CB  . GLN A 649  ? 0.2978 0.4139 0.2387 0.0471  0.0291  0.0181  647  GLN A CB  
4770  C CG  . GLN A 649  ? 0.2864 0.3944 0.2314 0.0445  0.0298  0.0235  647  GLN A CG  
4771  C CD  . GLN A 649  ? 0.2764 0.3688 0.2235 0.0431  0.0283  0.0210  647  GLN A CD  
4772  O OE1 . GLN A 649  ? 0.2624 0.3486 0.2096 0.0419  0.0272  0.0227  647  GLN A OE1 
4773  N NE2 . GLN A 649  ? 0.3115 0.3982 0.2606 0.0432  0.0282  0.0170  647  GLN A NE2 
4774  N N   . ALA A 650  ? 0.2736 0.4141 0.2125 0.0521  0.0316  0.0104  648  ALA A N   
4775  C CA  . ALA A 650  ? 0.3097 0.4597 0.2494 0.0531  0.0335  0.0108  648  ALA A CA  
4776  C C   . ALA A 650  ? 0.3517 0.5004 0.2922 0.0555  0.0329  0.0015  648  ALA A C   
4777  O O   . ALA A 650  ? 0.3483 0.4977 0.2913 0.0556  0.0339  0.0012  648  ALA A O   
4778  C CB  . ALA A 650  ? 0.3281 0.4961 0.2645 0.0545  0.0350  0.0137  648  ALA A CB  
4779  N N   . ARG A 651  ? 0.2811 0.4282 0.2202 0.0574  0.0310  -0.0061 649  ARG A N   
4780  C CA  . ARG A 651  ? 0.2815 0.4280 0.2220 0.0600  0.0299  -0.0155 649  ARG A CA  
4781  C C   . ARG A 651  ? 0.2865 0.4161 0.2304 0.0587  0.0280  -0.0184 649  ARG A C   
4782  O O   . ARG A 651  ? 0.2989 0.4259 0.2448 0.0606  0.0266  -0.0260 649  ARG A O   
4783  C CB  . ARG A 651  ? 0.3224 0.4776 0.2600 0.0630  0.0286  -0.0225 649  ARG A CB  
4784  C CG  . ARG A 651  ? 0.3437 0.5031 0.2830 0.0663  0.0276  -0.0325 649  ARG A CG  
4785  C CD  . ARG A 651  ? 0.3519 0.5271 0.2878 0.0696  0.0275  -0.0377 649  ARG A CD  
4786  N NE  . ARG A 651  ? 0.4264 0.6050 0.3645 0.0730  0.0263  -0.0479 649  ARG A NE  
4787  C CZ  . ARG A 651  ? 0.4235 0.6099 0.3633 0.0748  0.0276  -0.0503 649  ARG A CZ  
4788  N NH1 . ARG A 651  ? 0.4193 0.6099 0.3589 0.0732  0.0302  -0.0430 649  ARG A NH1 
4789  N NH2 . ARG A 651  ? 0.4608 0.6507 0.4029 0.0781  0.0261  -0.0603 649  ARG A NH2 
4790  N N   . MET A 652  ? 0.2911 0.4095 0.2361 0.0556  0.0279  -0.0125 650  MET A N   
4791  C CA  . MET A 652  ? 0.3035 0.4066 0.2514 0.0542  0.0261  -0.0148 650  MET A CA  
4792  C C   . MET A 652  ? 0.2747 0.3746 0.2261 0.0551  0.0258  -0.0195 650  MET A C   
4793  O O   . MET A 652  ? 0.2937 0.3866 0.2469 0.0559  0.0237  -0.0257 650  MET A O   
4794  C CB  . MET A 652  ? 0.3028 0.3960 0.2518 0.0507  0.0264  -0.0075 650  MET A CB  
4795  C CG  . MET A 652  ? 0.2929 0.3716 0.2448 0.0492  0.0249  -0.0095 650  MET A CG  
4796  S SD  . MET A 652  ? 0.3235 0.3915 0.2766 0.0454  0.0251  -0.0016 650  MET A SD  
4797  C CE  . MET A 652  ? 0.3024 0.3698 0.2527 0.0452  0.0239  -0.0014 650  MET A CE  
4798  N N   . PRO A 653  ? 0.2972 0.4018 0.2499 0.0551  0.0277  -0.0169 651  PRO A N   
4799  C CA  . PRO A 653  ? 0.3272 0.4277 0.2836 0.0560  0.0271  -0.0214 651  PRO A CA  
4800  C C   . PRO A 653  ? 0.3070 0.4121 0.2640 0.0594  0.0256  -0.0307 651  PRO A C   
4801  O O   . PRO A 653  ? 0.2911 0.3877 0.2514 0.0598  0.0236  -0.0356 651  PRO A O   
4802  C CB  . PRO A 653  ? 0.2757 0.3835 0.2329 0.0556  0.0296  -0.0165 651  PRO A CB  
4803  C CG  . PRO A 653  ? 0.3305 0.4387 0.2860 0.0530  0.0310  -0.0078 651  PRO A CG  
4804  C CD  . PRO A 653  ? 0.3086 0.4204 0.2604 0.0538  0.0301  -0.0089 651  PRO A CD  
4805  N N   . THR A 654  ? 0.2643 0.3830 0.2184 0.0618  0.0263  -0.0331 652  THR A N   
4806  C CA  . THR A 654  ? 0.2801 0.4040 0.2351 0.0653  0.0246  -0.0426 652  THR A CA  
4807  C C   . THR A 654  ? 0.2939 0.4085 0.2494 0.0652  0.0217  -0.0469 652  THR A C   
4808  O O   . THR A 654  ? 0.3047 0.4147 0.2637 0.0667  0.0194  -0.0541 652  THR A O   
4809  C CB  . THR A 654  ? 0.3002 0.4417 0.2516 0.0679  0.0261  -0.0440 652  THR A CB  
4810  O OG1 . THR A 654  ? 0.3289 0.4792 0.2804 0.0679  0.0288  -0.0398 652  THR A OG1 
4811  C CG2 . THR A 654  ? 0.3466 0.4939 0.2992 0.0717  0.0242  -0.0546 652  THR A CG2 
4812  N N   . LEU A 655  ? 0.2750 0.3868 0.2275 0.0633  0.0217  -0.0425 653  LEU A N   
4813  C CA  . LEU A 655  ? 0.2558 0.3586 0.2089 0.0629  0.0190  -0.0459 653  LEU A CA  
4814  C C   . LEU A 655  ? 0.3004 0.3881 0.2578 0.0610  0.0174  -0.0463 653  LEU A C   
4815  O O   . LEU A 655  ? 0.3021 0.3836 0.2621 0.0617  0.0148  -0.0521 653  LEU A O   
4816  C CB  . LEU A 655  ? 0.2870 0.3894 0.2364 0.0609  0.0195  -0.0401 653  LEU A CB  
4817  C CG  . LEU A 655  ? 0.2777 0.3950 0.2227 0.0626  0.0209  -0.0390 653  LEU A CG  
4818  C CD1 . LEU A 655  ? 0.2854 0.4008 0.2274 0.0605  0.0211  -0.0329 653  LEU A CD1 
4819  C CD2 . LEU A 655  ? 0.3427 0.4677 0.2875 0.0660  0.0192  -0.0481 653  LEU A CD2 
4820  N N   . LEU A 656  ? 0.3181 0.4000 0.2765 0.0586  0.0188  -0.0402 654  LEU A N   
4821  C CA  . LEU A 656  ? 0.2876 0.3563 0.2500 0.0568  0.0174  -0.0404 654  LEU A CA  
4822  C C   . LEU A 656  ? 0.3015 0.3698 0.2681 0.0591  0.0156  -0.0479 654  LEU A C   
4823  O O   . LEU A 656  ? 0.3049 0.3640 0.2748 0.0587  0.0131  -0.0513 654  LEU A O   
4824  C CB  . LEU A 656  ? 0.2961 0.3612 0.2591 0.0544  0.0194  -0.0336 654  LEU A CB  
4825  C CG  . LEU A 656  ? 0.3202 0.3844 0.2804 0.0518  0.0210  -0.0256 654  LEU A CG  
4826  C CD1 . LEU A 656  ? 0.3472 0.4058 0.3093 0.0495  0.0222  -0.0202 654  LEU A CD1 
4827  C CD2 . LEU A 656  ? 0.3192 0.3758 0.2784 0.0504  0.0194  -0.0253 654  LEU A CD2 
4828  N N   . GLY A 657  ? 0.2863 0.3645 0.2533 0.0615  0.0169  -0.0503 655  GLY A N   
4829  C CA  . GLY A 657  ? 0.3252 0.4032 0.2968 0.0639  0.0152  -0.0574 655  GLY A CA  
4830  C C   . GLY A 657  ? 0.2938 0.3717 0.2672 0.0660  0.0122  -0.0652 655  GLY A C   
4831  O O   . GLY A 657  ? 0.3162 0.3870 0.2947 0.0666  0.0096  -0.0701 655  GLY A O   
4832  N N   . LEU A 658  ? 0.2733 0.3590 0.2428 0.0671  0.0125  -0.0665 656  LEU A N   
4833  C CA  . LEU A 658  ? 0.2835 0.3695 0.2548 0.0692  0.0095  -0.0742 656  LEU A CA  
4834  C C   . LEU A 658  ? 0.2599 0.3320 0.2333 0.0667  0.0071  -0.0732 656  LEU A C   
4835  O O   . LEU A 658  ? 0.2787 0.3450 0.2572 0.0675  0.0041  -0.0790 656  LEU A O   
4836  C CB  . LEU A 658  ? 0.2650 0.3634 0.2313 0.0709  0.0104  -0.0754 656  LEU A CB  
4837  C CG  . LEU A 658  ? 0.2846 0.3851 0.2526 0.0733  0.0074  -0.0839 656  LEU A CG  
4838  C CD1 . LEU A 658  ? 0.2912 0.3931 0.2651 0.0764  0.0053  -0.0927 656  LEU A CD1 
4839  C CD2 . LEU A 658  ? 0.3043 0.4185 0.2668 0.0751  0.0086  -0.0846 656  LEU A CD2 
4840  N N   . ILE A 659  ? 0.2658 0.3327 0.2359 0.0636  0.0084  -0.0659 657  ILE A N   
4841  C CA  . ILE A 659  ? 0.2877 0.3423 0.2595 0.0610  0.0063  -0.0645 657  ILE A CA  
4842  C C   . ILE A 659  ? 0.2883 0.3325 0.2655 0.0598  0.0048  -0.0648 657  ILE A C   
4843  O O   . ILE A 659  ? 0.2773 0.3137 0.2586 0.0594  0.0019  -0.0680 657  ILE A O   
4844  C CB  . ILE A 659  ? 0.2774 0.3294 0.2446 0.0581  0.0082  -0.0564 657  ILE A CB  
4845  C CG1 . ILE A 659  ? 0.2769 0.3386 0.2395 0.0593  0.0090  -0.0567 657  ILE A CG1 
4846  C CG2 . ILE A 659  ? 0.2916 0.3311 0.2608 0.0553  0.0065  -0.0545 657  ILE A CG2 
4847  C CD1 . ILE A 659  ? 0.3115 0.3742 0.2697 0.0571  0.0113  -0.0486 657  ILE A CD1 
4848  N N   . ILE A 660  ? 0.2747 0.3189 0.2524 0.0593  0.0067  -0.0615 658  ILE A N   
4849  C CA  . ILE A 660  ? 0.2923 0.3273 0.2751 0.0581  0.0053  -0.0614 658  ILE A CA  
4850  C C   . ILE A 660  ? 0.2938 0.3282 0.2825 0.0606  0.0022  -0.0695 658  ILE A C   
4851  O O   . ILE A 660  ? 0.3109 0.3358 0.3042 0.0595  -0.0005 -0.0706 658  ILE A O   
4852  C CB  . ILE A 660  ? 0.2671 0.3043 0.2494 0.0576  0.0079  -0.0571 658  ILE A CB  
4853  C CG1 . ILE A 660  ? 0.2823 0.3159 0.2607 0.0544  0.0101  -0.0488 658  ILE A CG1 
4854  C CG2 . ILE A 660  ? 0.2976 0.3284 0.2857 0.0576  0.0063  -0.0590 658  ILE A CG2 
4855  C CD1 . ILE A 660  ? 0.3442 0.3823 0.3215 0.0540  0.0129  -0.0444 658  ILE A CD1 
4856  N N   . ARG A 661  ? 0.2883 0.3331 0.2771 0.0641  0.0024  -0.0752 659  ARG A N   
4857  C CA  . ARG A 661  ? 0.3183 0.3632 0.3136 0.0669  -0.0006 -0.0834 659  ARG A CA  
4858  C C   . ARG A 661  ? 0.3187 0.3624 0.3159 0.0680  -0.0037 -0.0891 659  ARG A C   
4859  O O   . ARG A 661  ? 0.3120 0.3502 0.3160 0.0688  -0.0071 -0.0942 659  ARG A O   
4860  C CB  . ARG A 661  ? 0.3273 0.3844 0.3226 0.0704  0.0008  -0.0878 659  ARG A CB  
4861  C CG  . ARG A 661  ? 0.2875 0.3443 0.2835 0.0697  0.0029  -0.0837 659  ARG A CG  
4862  C CD  . ARG A 661  ? 0.3194 0.3896 0.3145 0.0729  0.0048  -0.0871 659  ARG A CD  
4863  N NE  . ARG A 661  ? 0.3144 0.3888 0.3149 0.0767  0.0022  -0.0968 659  ARG A NE  
4864  C CZ  . ARG A 661  ? 0.3306 0.4173 0.3296 0.0801  0.0023  -0.1029 659  ARG A CZ  
4865  N NH1 . ARG A 661  ? 0.3470 0.4433 0.3391 0.0801  0.0050  -0.1000 659  ARG A NH1 
4866  N NH2 . ARG A 661  ? 0.3306 0.4204 0.3355 0.0836  -0.0003 -0.1122 659  ARG A NH2 
4867  N N   . GLU A 662  ? 0.3045 0.3534 0.2964 0.0679  -0.0027 -0.0883 660  GLU A N   
4868  C CA  . GLU A 662  ? 0.3092 0.3578 0.3030 0.0690  -0.0057 -0.0940 660  GLU A CA  
4869  C C   . GLU A 662  ? 0.2877 0.3239 0.2833 0.0657  -0.0076 -0.0907 660  GLU A C   
4870  O O   . GLU A 662  ? 0.3173 0.3487 0.3182 0.0662  -0.0112 -0.0956 660  GLU A O   
4871  C CB  . GLU A 662  ? 0.3243 0.3844 0.3118 0.0706  -0.0041 -0.0950 660  GLU A CB  
4872  C CG  . GLU A 662  ? 0.3089 0.3700 0.2984 0.0721  -0.0072 -0.1016 660  GLU A CG  
4873  C CD  . GLU A 662  ? 0.3143 0.3875 0.2976 0.0737  -0.0058 -0.1028 660  GLU A CD  
4874  O OE1 . GLU A 662  ? 0.3300 0.4076 0.3069 0.0724  -0.0025 -0.0960 660  GLU A OE1 
4875  O OE2 . GLU A 662  ? 0.3184 0.3969 0.3037 0.0764  -0.0081 -0.1106 660  GLU A OE2 
4876  N N   . ALA A 663  ? 0.2829 0.3139 0.2745 0.0624  -0.0055 -0.0825 661  ALA A N   
4877  C CA  . ALA A 663  ? 0.2724 0.2940 0.2643 0.0593  -0.0069 -0.0791 661  ALA A CA  
4878  C C   . ALA A 663  ? 0.2935 0.3042 0.2883 0.0563  -0.0072 -0.0740 661  ALA A C   
4879  O O   . ALA A 663  ? 0.3597 0.3631 0.3541 0.0534  -0.0078 -0.0701 661  ALA A O   
4880  C CB  . ALA A 663  ? 0.2962 0.3212 0.2811 0.0580  -0.0046 -0.0743 661  ALA A CB  
4881  N N   . GLY A 664  ? 0.3180 0.3280 0.3156 0.0568  -0.0068 -0.0740 662  GLY A N   
4882  C CA  . GLY A 664  ? 0.3214 0.3219 0.3219 0.0540  -0.0073 -0.0694 662  GLY A CA  
4883  C C   . GLY A 664  ? 0.3312 0.3290 0.3265 0.0510  -0.0044 -0.0613 662  GLY A C   
4884  O O   . GLY A 664  ? 0.3679 0.3574 0.3648 0.0482  -0.0051 -0.0573 662  GLY A O   
4885  N N   . LYS A 665  ? 0.3183 0.3234 0.3078 0.0515  -0.0013 -0.0588 663  LYS A N   
4886  C CA  . LYS A 665  ? 0.2871 0.2899 0.2722 0.0487  0.0012  -0.0515 663  LYS A CA  
4887  C C   . LYS A 665  ? 0.2745 0.2777 0.2597 0.0483  0.0032  -0.0481 663  LYS A C   
4888  O O   . LYS A 665  ? 0.2741 0.2834 0.2602 0.0505  0.0039  -0.0507 663  LYS A O   
4889  C CB  . LYS A 665  ? 0.2935 0.3039 0.2729 0.0493  0.0032  -0.0499 663  LYS A CB  
4890  C CG  . LYS A 665  ? 0.3047 0.3159 0.2833 0.0499  0.0015  -0.0531 663  LYS A CG  
4891  C CD  . LYS A 665  ? 0.3366 0.3379 0.3170 0.0472  -0.0003 -0.0512 663  LYS A CD  
4892  C CE  . LYS A 665  ? 0.3802 0.3829 0.3596 0.0476  -0.0018 -0.0538 663  LYS A CE  
4893  N NZ  . LYS A 665  ? 0.3932 0.3868 0.3753 0.0451  -0.0040 -0.0527 663  LYS A NZ  
4894  N N   . SER A 666  ? 0.2836 0.2805 0.2679 0.0453  0.0041  -0.0423 664  SER A N   
4895  C CA  . SER A 666  ? 0.2970 0.2947 0.2806 0.0445  0.0063  -0.0382 664  SER A CA  
4896  C C   . SER A 666  ? 0.3129 0.3187 0.2917 0.0451  0.0092  -0.0353 664  SER A C   
4897  O O   . SER A 666  ? 0.3197 0.3293 0.2953 0.0455  0.0095  -0.0354 664  SER A O   
4898  C CB  . SER A 666  ? 0.3004 0.2897 0.2841 0.0412  0.0064  -0.0330 664  SER A CB  
4899  O OG  . SER A 666  ? 0.3393 0.3282 0.3192 0.0397  0.0074  -0.0295 664  SER A OG  
4900  N N   . ALA A 667  ? 0.2935 0.3022 0.2721 0.0450  0.0112  -0.0324 665  ALA A N   
4901  C CA  . ALA A 667  ? 0.2785 0.2949 0.2532 0.0453  0.0139  -0.0288 665  ALA A CA  
4902  C C   . ALA A 667  ? 0.2994 0.3127 0.2711 0.0429  0.0147  -0.0238 665  ALA A C   
4903  O O   . ALA A 667  ? 0.2827 0.3021 0.2512 0.0435  0.0157  -0.0226 665  ALA A O   
4904  C CB  . ALA A 667  ? 0.3192 0.3383 0.2949 0.0451  0.0158  -0.0261 665  ALA A CB  
4905  N N   . LEU A 668  ? 0.2944 0.2989 0.2673 0.0403  0.0141  -0.0209 666  LEU A N   
4906  C CA  . LEU A 668  ? 0.2677 0.2689 0.2383 0.0382  0.0146  -0.0167 666  LEU A CA  
4907  C C   . LEU A 668  ? 0.3178 0.3202 0.2865 0.0389  0.0135  -0.0190 666  LEU A C   
4908  O O   . LEU A 668  ? 0.3083 0.3140 0.2742 0.0386  0.0145  -0.0163 666  LEU A O   
4909  C CB  . LEU A 668  ? 0.3355 0.3273 0.3080 0.0356  0.0137  -0.0146 666  LEU A CB  
4910  C CG  . LEU A 668  ? 0.5007 0.4908 0.4741 0.0340  0.0151  -0.0102 666  LEU A CG  
4911  C CD1 . LEU A 668  ? 0.3685 0.3500 0.3437 0.0317  0.0139  -0.0091 666  LEU A CD1 
4912  C CD2 . LEU A 668  ? 0.4758 0.4696 0.4468 0.0334  0.0170  -0.0058 666  LEU A CD2 
4913  N N   . ASN A 669  ? 0.2817 0.2816 0.2523 0.0398  0.0112  -0.0239 667  ASN A N   
4914  C CA  . ASN A 669  ? 0.2930 0.2936 0.2623 0.0403  0.0099  -0.0264 667  ASN A CA  
4915  C C   . ASN A 669  ? 0.2851 0.2957 0.2520 0.0429  0.0107  -0.0289 667  ASN A C   
4916  O O   . ASN A 669  ? 0.3074 0.3207 0.2716 0.0431  0.0106  -0.0286 667  ASN A O   
4917  C CB  . ASN A 669  ? 0.3455 0.3402 0.3184 0.0403  0.0071  -0.0307 667  ASN A CB  
4918  C CG  . ASN A 669  ? 0.3919 0.3774 0.3666 0.0374  0.0064  -0.0277 667  ASN A CG  
4919  O OD1 . ASN A 669  ? 0.4901 0.4734 0.4627 0.0354  0.0075  -0.0233 667  ASN A OD1 
4920  N ND2 . ASN A 669  ? 0.4568 0.4376 0.4357 0.0372  0.0043  -0.0301 667  ASN A ND2 
4921  N N   . ALA A 670  ? 0.2755 0.2922 0.2431 0.0450  0.0114  -0.0312 668  ALA A N   
4922  C CA  . ALA A 670  ? 0.2912 0.3190 0.2562 0.0475  0.0123  -0.0332 668  ALA A CA  
4923  C C   . ALA A 670  ? 0.2696 0.3025 0.2309 0.0466  0.0148  -0.0271 668  ALA A C   
4924  O O   . ALA A 670  ? 0.2737 0.3136 0.2320 0.0477  0.0152  -0.0271 668  ALA A O   
4925  C CB  . ALA A 670  ? 0.2664 0.3002 0.2334 0.0500  0.0126  -0.0371 668  ALA A CB  
4926  N N   . ILE A 671  ? 0.2870 0.3167 0.2488 0.0447  0.0163  -0.0217 669  ILE A N   
4927  C CA  . ILE A 671  ? 0.2563 0.2895 0.2156 0.0435  0.0183  -0.0154 669  ILE A CA  
4928  C C   . ILE A 671  ? 0.2763 0.3064 0.2338 0.0424  0.0175  -0.0138 669  ILE A C   
4929  O O   . ILE A 671  ? 0.2916 0.3283 0.2464 0.0428  0.0183  -0.0116 669  ILE A O   
4930  C CB  . ILE A 671  ? 0.2916 0.3201 0.2528 0.0414  0.0195  -0.0104 669  ILE A CB  
4931  C CG1 . ILE A 671  ? 0.2609 0.2945 0.2236 0.0426  0.0206  -0.0112 669  ILE A CG1 
4932  C CG2 . ILE A 671  ? 0.3125 0.3422 0.2723 0.0397  0.0208  -0.0039 669  ILE A CG2 
4933  C CD1 . ILE A 671  ? 0.3001 0.3279 0.2654 0.0406  0.0213  -0.0076 669  ILE A CD1 
4934  N N   . ALA A 672  ? 0.2573 0.2778 0.2163 0.0408  0.0159  -0.0147 670  ALA A N   
4935  C CA  . ALA A 672  ? 0.2642 0.2815 0.2219 0.0396  0.0151  -0.0135 670  ALA A CA  
4936  C C   . ALA A 672  ? 0.2642 0.2874 0.2199 0.0417  0.0141  -0.0175 670  ALA A C   
4937  O O   . ALA A 672  ? 0.2710 0.2969 0.2243 0.0415  0.0143  -0.0154 670  ALA A O   
4938  C CB  . ALA A 672  ? 0.2759 0.2828 0.2358 0.0377  0.0136  -0.0143 670  ALA A CB  
4939  N N   . GLU A 673  ? 0.2551 0.2805 0.2119 0.0437  0.0129  -0.0234 671  GLU A N   
4940  C CA  . GLU A 673  ? 0.2659 0.2974 0.2213 0.0458  0.0117  -0.0282 671  GLU A CA  
4941  C C   . GLU A 673  ? 0.2801 0.3230 0.2319 0.0473  0.0134  -0.0261 671  GLU A C   
4942  O O   . GLU A 673  ? 0.2682 0.3151 0.2176 0.0477  0.0131  -0.0261 671  GLU A O   
4943  C CB  . GLU A 673  ? 0.3090 0.3412 0.2673 0.0479  0.0101  -0.0350 671  GLU A CB  
4944  C CG  . GLU A 673  ? 0.3499 0.3887 0.3074 0.0504  0.0086  -0.0411 671  GLU A CG  
4945  C CD  . GLU A 673  ? 0.3602 0.3922 0.3191 0.0495  0.0061  -0.0434 671  GLU A CD  
4946  O OE1 . GLU A 673  ? 0.3769 0.3991 0.3379 0.0471  0.0054  -0.0413 671  GLU A OE1 
4947  O OE2 . GLU A 673  ? 0.3223 0.3593 0.2801 0.0511  0.0049  -0.0475 671  GLU A OE2 
4948  N N   . VAL A 674  ? 0.2359 0.2847 0.1875 0.0479  0.0153  -0.0240 672  VAL A N   
4949  C CA  . VAL A 674  ? 0.2411 0.3016 0.1894 0.0492  0.0171  -0.0215 672  VAL A CA  
4950  C C   . VAL A 674  ? 0.2508 0.3104 0.1975 0.0471  0.0181  -0.0142 672  VAL A C   
4951  O O   . VAL A 674  ? 0.2343 0.3014 0.1782 0.0478  0.0184  -0.0126 672  VAL A O   
4952  C CB  . VAL A 674  ? 0.2506 0.3181 0.1996 0.0504  0.0188  -0.0211 672  VAL A CB  
4953  C CG1 . VAL A 674  ? 0.2604 0.3411 0.2061 0.0515  0.0206  -0.0180 672  VAL A CG1 
4954  C CG2 . VAL A 674  ? 0.2573 0.3258 0.2084 0.0527  0.0175  -0.0289 672  VAL A CG2 
4955  N N   . ARG A 675  ? 0.2486 0.2992 0.1973 0.0446  0.0185  -0.0099 673  ARG A N   
4956  C CA  . ARG A 675  ? 0.2282 0.2771 0.1762 0.0427  0.0191  -0.0035 673  ARG A CA  
4957  C C   . ARG A 675  ? 0.2330 0.2806 0.1795 0.0427  0.0177  -0.0048 673  ARG A C   
4958  O O   . ARG A 675  ? 0.2355 0.2877 0.1801 0.0425  0.0181  -0.0009 673  ARG A O   
4959  C CB  . ARG A 675  ? 0.2322 0.2710 0.1831 0.0401  0.0193  -0.0001 673  ARG A CB  
4960  C CG  . ARG A 675  ? 0.2364 0.2771 0.1889 0.0397  0.0210  0.0031  673  ARG A CG  
4961  C CD  . ARG A 675  ? 0.2680 0.2992 0.2232 0.0371  0.0210  0.0067  673  ARG A CD  
4962  N NE  . ARG A 675  ? 0.2550 0.2859 0.2102 0.0358  0.0213  0.0121  673  ARG A NE  
4963  C CZ  . ARG A 675  ? 0.2520 0.2749 0.2094 0.0337  0.0210  0.0148  673  ARG A CZ  
4964  N NH1 . ARG A 675  ? 0.2569 0.2716 0.2162 0.0326  0.0204  0.0130  673  ARG A NH1 
4965  N NH2 . ARG A 675  ? 0.2505 0.2739 0.2083 0.0328  0.0211  0.0195  673  ARG A NH2 
4966  N N   . GLU A 676  ? 0.2237 0.2649 0.1711 0.0428  0.0158  -0.0100 674  GLU A N   
4967  C CA  . GLU A 676  ? 0.2292 0.2688 0.1754 0.0427  0.0143  -0.0114 674  GLU A CA  
4968  C C   . GLU A 676  ? 0.2381 0.2887 0.1813 0.0450  0.0142  -0.0135 674  GLU A C   
4969  O O   . GLU A 676  ? 0.2400 0.2929 0.1813 0.0448  0.0139  -0.0114 674  GLU A O   
4970  C CB  . GLU A 676  ? 0.2535 0.2848 0.2018 0.0423  0.0122  -0.0165 674  GLU A CB  
4971  C CG  . GLU A 676  ? 0.2872 0.3164 0.2346 0.0419  0.0107  -0.0176 674  GLU A CG  
4972  C CD  . GLU A 676  ? 0.4912 0.5101 0.4412 0.0401  0.0092  -0.0190 674  GLU A CD  
4973  O OE1 . GLU A 676  ? 0.6868 0.7013 0.6393 0.0400  0.0083  -0.0223 674  GLU A OE1 
4974  O OE2 . GLU A 676  ? 0.4892 0.5045 0.4388 0.0387  0.0088  -0.0166 674  GLU A OE2 
4975  N N   . ALA A 677  ? 0.2328 0.2905 0.1755 0.0472  0.0143  -0.0177 675  ALA A N   
4976  C CA  . ALA A 677  ? 0.2158 0.2853 0.1554 0.0496  0.0143  -0.0199 675  ALA A CA  
4977  C C   . ALA A 677  ? 0.2448 0.3221 0.1820 0.0492  0.0161  -0.0129 675  ALA A C   
4978  O O   . ALA A 677  ? 0.2373 0.3205 0.1720 0.0497  0.0158  -0.0118 675  ALA A O   
4979  C CB  . ALA A 677  ? 0.2224 0.2988 0.1624 0.0522  0.0143  -0.0259 675  ALA A CB  
4980  N N   . ILE A 678  ? 0.2348 0.3126 0.1731 0.0481  0.0180  -0.0078 676  ILE A N   
4981  C CA  . ILE A 678  ? 0.2408 0.3252 0.1779 0.0474  0.0196  -0.0003 676  ILE A CA  
4982  C C   . ILE A 678  ? 0.2461 0.3249 0.1833 0.0456  0.0189  0.0041  676  ILE A C   
4983  O O   . ILE A 678  ? 0.2411 0.3271 0.1764 0.0458  0.0191  0.0079  676  ILE A O   
4984  C CB  . ILE A 678  ? 0.2187 0.3019 0.1580 0.0462  0.0214  0.0042  676  ILE A CB  
4985  C CG1 . ILE A 678  ? 0.2633 0.3542 0.2023 0.0482  0.0223  0.0002  676  ILE A CG1 
4986  C CG2 . ILE A 678  ? 0.2601 0.3475 0.1995 0.0447  0.0227  0.0129  676  ILE A CG2 
4987  C CD1 . ILE A 678  ? 0.2530 0.3409 0.1948 0.0471  0.0237  0.0032  676  ILE A CD1 
4988  N N   . ASP A 679  ? 0.2229 0.2894 0.1626 0.0438  0.0180  0.0036  677  ASP A N   
4989  C CA  . ASP A 679  ? 0.2162 0.2768 0.1565 0.0420  0.0173  0.0074  677  ASP A CA  
4990  C C   . ASP A 679  ? 0.2377 0.3014 0.1757 0.0431  0.0158  0.0044  677  ASP A C   
4991  O O   . ASP A 679  ? 0.2324 0.2982 0.1697 0.0426  0.0157  0.0087  677  ASP A O   
4992  C CB  . ASP A 679  ? 0.2344 0.2822 0.1776 0.0401  0.0167  0.0067  677  ASP A CB  
4993  C CG  . ASP A 679  ? 0.2897 0.3340 0.2355 0.0387  0.0180  0.0104  677  ASP A CG  
4994  O OD1 . ASP A 679  ? 0.2911 0.3414 0.2372 0.0385  0.0194  0.0156  677  ASP A OD1 
4995  O OD2 . ASP A 679  ? 0.3071 0.3429 0.2551 0.0376  0.0176  0.0085  677  ASP A OD2 
4996  N N   . PHE A 680  ? 0.2265 0.2902 0.1637 0.0446  0.0145  -0.0028 678  PHE A N   
4997  C CA  . PHE A 680  ? 0.2472 0.3151 0.1822 0.0459  0.0130  -0.0060 678  PHE A CA  
4998  C C   . PHE A 680  ? 0.2401 0.3210 0.1720 0.0473  0.0138  -0.0031 678  PHE A C   
4999  O O   . PHE A 680  ? 0.2359 0.3194 0.1663 0.0472  0.0132  -0.0007 678  PHE A O   
5000  C CB  . PHE A 680  ? 0.2440 0.3116 0.1791 0.0476  0.0115  -0.0145 678  PHE A CB  
5001  C CG  . PHE A 680  ? 0.2282 0.2841 0.1661 0.0462  0.0098  -0.0176 678  PHE A CG  
5002  C CD1 . PHE A 680  ? 0.2280 0.2780 0.1663 0.0446  0.0089  -0.0156 678  PHE A CD1 
5003  C CD2 . PHE A 680  ? 0.2458 0.2970 0.1861 0.0466  0.0091  -0.0226 678  PHE A CD2 
5004  C CE1 . PHE A 680  ? 0.2492 0.2895 0.1900 0.0433  0.0074  -0.0183 678  PHE A CE1 
5005  C CE2 . PHE A 680  ? 0.2442 0.2853 0.1872 0.0452  0.0075  -0.0249 678  PHE A CE2 
5006  C CZ  . PHE A 680  ? 0.2518 0.2876 0.1950 0.0435  0.0067  -0.0227 678  PHE A CZ  
5007  N N   . LEU A 681  ? 0.2222 0.3119 0.1529 0.0487  0.0152  -0.0033 679  LEU A N   
5008  C CA  . LEU A 681  ? 0.2108 0.3144 0.1384 0.0501  0.0160  -0.0006 679  LEU A CA  
5009  C C   . LEU A 681  ? 0.2434 0.3474 0.1714 0.0483  0.0168  0.0085  679  LEU A C   
5010  O O   . LEU A 681  ? 0.2329 0.3435 0.1589 0.0487  0.0163  0.0109  679  LEU A O   
5011  C CB  . LEU A 681  ? 0.2468 0.3595 0.1737 0.0517  0.0176  -0.0016 679  LEU A CB  
5012  C CG  . LEU A 681  ? 0.2712 0.3864 0.1978 0.0541  0.0166  -0.0110 679  LEU A CG  
5013  C CD1 . LEU A 681  ? 0.2509 0.3703 0.1784 0.0550  0.0182  -0.0119 679  LEU A CD1 
5014  C CD2 . LEU A 681  ? 0.2539 0.3808 0.1769 0.0566  0.0157  -0.0151 679  LEU A CD2 
5015  N N   . ARG A 682  ? 0.2243 0.3212 0.1554 0.0462  0.0178  0.0134  680  ARG A N   
5016  C CA  . ARG A 682  ? 0.2254 0.3228 0.1579 0.0445  0.0183  0.0221  680  ARG A CA  
5017  C C   . ARG A 682  ? 0.2394 0.3291 0.1730 0.0434  0.0168  0.0230  680  ARG A C   
5018  O O   . ARG A 682  ? 0.2368 0.3303 0.1704 0.0429  0.0166  0.0286  680  ARG A O   
5019  C CB  . ARG A 682  ? 0.2098 0.3021 0.1458 0.0428  0.0197  0.0266  680  ARG A CB  
5020  C CG  . ARG A 682  ? 0.2269 0.3287 0.1620 0.0438  0.0214  0.0273  680  ARG A CG  
5021  C CD  . ARG A 682  ? 0.2399 0.3360 0.1789 0.0420  0.0226  0.0315  680  ARG A CD  
5022  N NE  . ARG A 682  ? 0.2616 0.3680 0.1999 0.0428  0.0243  0.0332  680  ARG A NE  
5023  C CZ  . ARG A 682  ? 0.2534 0.3569 0.1945 0.0419  0.0255  0.0348  680  ARG A CZ  
5024  N NH1 . ARG A 682  ? 0.2713 0.3621 0.2158 0.0401  0.0251  0.0349  680  ARG A NH1 
5025  N NH2 . ARG A 682  ? 0.2909 0.4049 0.2312 0.0428  0.0271  0.0362  680  ARG A NH2 
5026  N N   . TYR A 683  ? 0.2299 0.3092 0.1645 0.0429  0.0156  0.0178  681  TYR A N   
5027  C CA  . TYR A 683  ? 0.2097 0.2819 0.1454 0.0419  0.0142  0.0184  681  TYR A CA  
5028  C C   . TYR A 683  ? 0.2644 0.3438 0.1970 0.0434  0.0130  0.0164  681  TYR A C   
5029  O O   . TYR A 683  ? 0.2411 0.3215 0.1741 0.0428  0.0124  0.0207  681  TYR A O   
5030  C CB  . TYR A 683  ? 0.2412 0.3017 0.1788 0.0410  0.0133  0.0134  681  TYR A CB  
5031  C CG  . TYR A 683  ? 0.2526 0.3064 0.1912 0.0399  0.0119  0.0132  681  TYR A CG  
5032  C CD1 . TYR A 683  ? 0.2447 0.2928 0.1863 0.0382  0.0120  0.0184  681  TYR A CD1 
5033  C CD2 . TYR A 683  ? 0.2440 0.2974 0.1810 0.0408  0.0103  0.0077  681  TYR A CD2 
5034  C CE1 . TYR A 683  ? 0.2351 0.2775 0.1778 0.0374  0.0107  0.0180  681  TYR A CE1 
5035  C CE2 . TYR A 683  ? 0.2566 0.3044 0.1948 0.0399  0.0090  0.0077  681  TYR A CE2 
5036  C CZ  . TYR A 683  ? 0.2536 0.2960 0.1944 0.0382  0.0093  0.0128  681  TYR A CZ  
5037  O OH  . TYR A 683  ? 0.2576 0.2949 0.1997 0.0374  0.0081  0.0125  681  TYR A OH  
5038  N N   . TYR A 684  ? 0.2363 0.3210 0.1663 0.0453  0.0124  0.0099  682  TYR A N   
5039  C CA  . TYR A 684  ? 0.2533 0.3453 0.1804 0.0468  0.0111  0.0076  682  TYR A CA  
5040  C C   . TYR A 684  ? 0.2577 0.3622 0.1826 0.0476  0.0120  0.0134  682  TYR A C   
5041  O O   . TYR A 684  ? 0.2357 0.3445 0.1593 0.0479  0.0110  0.0151  682  TYR A O   
5042  C CB  . TYR A 684  ? 0.2356 0.3306 0.1610 0.0489  0.0101  -0.0012 682  TYR A CB  
5043  C CG  . TYR A 684  ? 0.2120 0.2950 0.1399 0.0481  0.0088  -0.0065 682  TYR A CG  
5044  C CD1 . TYR A 684  ? 0.2346 0.3082 0.1645 0.0463  0.0078  -0.0052 682  TYR A CD1 
5045  C CD2 . TYR A 684  ? 0.2378 0.3194 0.1665 0.0491  0.0085  -0.0128 682  TYR A CD2 
5046  C CE1 . TYR A 684  ? 0.2625 0.3259 0.1947 0.0454  0.0067  -0.0096 682  TYR A CE1 
5047  C CE2 . TYR A 684  ? 0.2220 0.2930 0.1534 0.0482  0.0072  -0.0171 682  TYR A CE2 
5048  C CZ  . TYR A 684  ? 0.2419 0.3040 0.1750 0.0462  0.0063  -0.0153 682  TYR A CZ  
5049  O OH  . TYR A 684  ? 0.2521 0.3044 0.1879 0.0452  0.0051  -0.0191 682  TYR A OH  
5050  N N   . ALA A 685  ? 0.2274 0.3383 0.1522 0.0477  0.0137  0.0169  683  ALA A N   
5051  C CA  . ALA A 685  ? 0.2326 0.3552 0.1560 0.0479  0.0146  0.0238  683  ALA A CA  
5052  C C   . ALA A 685  ? 0.2506 0.3682 0.1768 0.0459  0.0142  0.0315  683  ALA A C   
5053  O O   . ALA A 685  ? 0.2497 0.3744 0.1747 0.0462  0.0135  0.0354  683  ALA A O   
5054  C CB  . ALA A 685  ? 0.2484 0.3775 0.1719 0.0481  0.0167  0.0266  683  ALA A CB  
5055  N N   . GLU A 686  ? 0.2409 0.3466 0.1712 0.0439  0.0144  0.0338  684  GLU A N   
5056  C CA  . GLU A 686  ? 0.2653 0.3661 0.1991 0.0421  0.0139  0.0406  684  GLU A CA  
5057  C C   . GLU A 686  ? 0.2573 0.3542 0.1908 0.0422  0.0120  0.0384  684  GLU A C   
5058  O O   . GLU A 686  ? 0.2503 0.3503 0.1847 0.0419  0.0112  0.0437  684  GLU A O   
5059  C CB  . GLU A 686  ? 0.2822 0.3716 0.2206 0.0401  0.0145  0.0427  684  GLU A CB  
5060  C CG  . GLU A 686  ? 0.3429 0.4258 0.2859 0.0384  0.0136  0.0485  684  GLU A CG  
5061  C CD  . GLU A 686  ? 0.3987 0.4903 0.3431 0.0381  0.0137  0.0573  684  GLU A CD  
5062  O OE1 . GLU A 686  ? 0.3828 0.4852 0.3252 0.0387  0.0148  0.0600  684  GLU A OE1 
5063  O OE2 . GLU A 686  ? 0.4447 0.5326 0.3926 0.0371  0.0125  0.0617  684  GLU A OE2 
5064  N N   . GLN A 687  ? 0.2244 0.3148 0.1569 0.0427  0.0111  0.0308  685  GLN A N   
5065  C CA  . GLN A 687  ? 0.2138 0.3008 0.1460 0.0428  0.0094  0.0285  685  GLN A CA  
5066  C C   . GLN A 687  ? 0.2304 0.3294 0.1591 0.0444  0.0086  0.0289  685  GLN A C   
5067  O O   . GLN A 687  ? 0.2653 0.3646 0.1944 0.0443  0.0073  0.0312  685  GLN A O   
5068  C CB  . GLN A 687  ? 0.2269 0.3062 0.1589 0.0430  0.0085  0.0203  685  GLN A CB  
5069  C CG  . GLN A 687  ? 0.2259 0.2928 0.1614 0.0411  0.0090  0.0201  685  GLN A CG  
5070  C CD  . GLN A 687  ? 0.2749 0.3354 0.2140 0.0395  0.0085  0.0250  685  GLN A CD  
5071  O OE1 . GLN A 687  ? 0.2882 0.3474 0.2273 0.0395  0.0072  0.0244  685  GLN A OE1 
5072  N NE2 . GLN A 687  ? 0.3286 0.3853 0.2709 0.0381  0.0095  0.0297  685  GLN A NE2 
5073  N N   . THR A 688  ? 0.2127 0.3221 0.1379 0.0462  0.0093  0.0265  686  THR A N   
5074  C CA  . THR A 688  ? 0.2162 0.3387 0.1378 0.0478  0.0087  0.0271  686  THR A CA  
5075  C C   . THR A 688  ? 0.2429 0.3713 0.1657 0.0470  0.0090  0.0368  686  THR A C   
5076  O O   . THR A 688  ? 0.2576 0.3904 0.1795 0.0473  0.0077  0.0390  686  THR A O   
5077  C CB  . THR A 688  ? 0.2222 0.3555 0.1402 0.0499  0.0097  0.0229  686  THR A CB  
5078  O OG1 . THR A 688  ? 0.2496 0.3784 0.1669 0.0510  0.0087  0.0134  686  THR A OG1 
5079  C CG2 . THR A 688  ? 0.2548 0.4038 0.1690 0.0515  0.0094  0.0248  686  THR A CG2 
5080  N N   . ARG A 689  ? 0.2432 0.3715 0.1684 0.0458  0.0105  0.0428  687  ARG A N   
5081  C CA  . ARG A 689  ? 0.2537 0.3873 0.1810 0.0448  0.0106  0.0526  687  ARG A CA  
5082  C C   . ARG A 689  ? 0.2693 0.3937 0.2007 0.0434  0.0091  0.0560  687  ARG A C   
5083  O O   . ARG A 689  ? 0.2883 0.4178 0.2211 0.0430  0.0084  0.0629  687  ARG A O   
5084  C CB  . ARG A 689  ? 0.2593 0.3933 0.1893 0.0436  0.0124  0.0581  687  ARG A CB  
5085  C CG  . ARG A 689  ? 0.2703 0.4173 0.1966 0.0450  0.0140  0.0571  687  ARG A CG  
5086  C CD  . ARG A 689  ? 0.3186 0.4664 0.2482 0.0436  0.0156  0.0638  687  ARG A CD  
5087  N NE  . ARG A 689  ? 0.3193 0.4538 0.2520 0.0424  0.0161  0.0608  687  ARG A NE  
5088  C CZ  . ARG A 689  ? 0.3275 0.4617 0.2590 0.0430  0.0175  0.0560  687  ARG A CZ  
5089  N NH1 . ARG A 689  ? 0.3525 0.4989 0.2798 0.0449  0.0184  0.0530  687  ARG A NH1 
5090  N NH2 . ARG A 689  ? 0.3321 0.4540 0.2667 0.0418  0.0177  0.0539  687  ARG A NH2 
5091  N N   . ARG A 690  ? 0.2407 0.3520 0.1741 0.0426  0.0085  0.0512  688  ARG A N   
5092  C CA  . ARG A 690  ? 0.2673 0.3700 0.2046 0.0415  0.0071  0.0534  688  ARG A CA  
5093  C C   . ARG A 690  ? 0.2795 0.3847 0.2143 0.0426  0.0054  0.0501  688  ARG A C   
5094  O O   . ARG A 690  ? 0.2738 0.3753 0.2116 0.0419  0.0040  0.0533  688  ARG A O   
5095  C CB  . ARG A 690  ? 0.2611 0.3497 0.2015 0.0402  0.0072  0.0496  688  ARG A CB  
5096  C CG  . ARG A 690  ? 0.3009 0.3852 0.2449 0.0388  0.0086  0.0534  688  ARG A CG  
5097  C CD  . ARG A 690  ? 0.3134 0.3961 0.2629 0.0374  0.0081  0.0617  688  ARG A CD  
5098  N NE  . ARG A 690  ? 0.3072 0.3808 0.2601 0.0367  0.0066  0.0611  688  ARG A NE  
5099  C CZ  . ARG A 690  ? 0.3894 0.4654 0.3438 0.0369  0.0050  0.0646  688  ARG A CZ  
5100  N NH1 . ARG A 690  ? 0.3235 0.4107 0.2763 0.0376  0.0048  0.0696  688  ARG A NH1 
5101  N NH2 . ARG A 690  ? 0.3400 0.4075 0.2978 0.0364  0.0038  0.0633  688  ARG A NH2 
5102  N N   . THR A 691  ? 0.2329 0.3440 0.1629 0.0443  0.0052  0.0435  689  THR A N   
5103  C CA  . THR A 691  ? 0.2446 0.3552 0.1729 0.0451  0.0034  0.0389  689  THR A CA  
5104  C C   . THR A 691  ? 0.2892 0.4132 0.2127 0.0471  0.0027  0.0373  689  THR A C   
5105  O O   . THR A 691  ? 0.3419 0.4691 0.2652 0.0474  0.0012  0.0391  689  THR A O   
5106  C CB  . THR A 691  ? 0.2492 0.3501 0.1776 0.0450  0.0030  0.0305  689  THR A CB  
5107  O OG1 . THR A 691  ? 0.2813 0.3858 0.2068 0.0461  0.0039  0.0253  689  THR A OG1 
5108  C CG2 . THR A 691  ? 0.2614 0.3490 0.1944 0.0430  0.0033  0.0317  689  THR A CG2 
5109  N N   . LEU A 692  ? 0.2594 0.3919 0.1793 0.0485  0.0036  0.0337  690  LEU A N   
5110  C CA  . LEU A 692  ? 0.2807 0.4239 0.1960 0.0507  0.0026  0.0287  690  LEU A CA  
5111  C C   . LEU A 692  ? 0.2988 0.4557 0.2120 0.0514  0.0023  0.0353  690  LEU A C   
5112  O O   . LEU A 692  ? 0.3121 0.4756 0.2256 0.0510  0.0037  0.0421  690  LEU A O   
5113  C CB  . LEU A 692  ? 0.2704 0.4180 0.1829 0.0523  0.0035  0.0218  690  LEU A CB  
5114  C CG  . LEU A 692  ? 0.3136 0.4489 0.2278 0.0519  0.0031  0.0140  690  LEU A CG  
5115  C CD1 . LEU A 692  ? 0.3131 0.4547 0.2247 0.0539  0.0034  0.0066  690  LEU A CD1 
5116  C CD2 . LEU A 692  ? 0.3389 0.4670 0.2543 0.0516  0.0010  0.0102  690  LEU A CD2 
5117  N N   . GLY A 693  ? 0.2734 0.4348 0.1848 0.0524  0.0005  0.0333  691  GLY A N   
5118  C CA  . GLY A 693  ? 0.3244 0.4991 0.2336 0.0532  -0.0001 0.0389  691  GLY A CA  
5119  C C   . GLY A 693  ? 0.3092 0.4941 0.2137 0.0555  -0.0015 0.0320  691  GLY A C   
5120  O O   . GLY A 693  ? 0.3313 0.5126 0.2346 0.0565  -0.0020 0.0228  691  GLY A O   
5121  N N   . PRO A 694  ? 0.3308 0.5285 0.2329 0.0563  -0.0023 0.0364  692  PRO A N   
5122  C CA  . PRO A 694  ? 0.3666 0.5763 0.2639 0.0587  -0.0036 0.0299  692  PRO A CA  
5123  C C   . PRO A 694  ? 0.3997 0.6013 0.2974 0.0592  -0.0057 0.0215  692  PRO A C   
5124  O O   . PRO A 694  ? 0.4196 0.6269 0.3143 0.0612  -0.0066 0.0130  692  PRO A O   
5125  C CB  . PRO A 694  ? 0.4133 0.6362 0.3089 0.0590  -0.0042 0.0381  692  PRO A CB  
5126  C CG  . PRO A 694  ? 0.3432 0.5644 0.2421 0.0570  -0.0027 0.0488  692  PRO A CG  
5127  C CD  . PRO A 694  ? 0.3524 0.5551 0.2563 0.0551  -0.0022 0.0478  692  PRO A CD  
5128  N N   . GLY A 695  ? 0.3188 0.5077 0.2206 0.0575  -0.0066 0.0236  693  GLY A N   
5129  C CA  . GLY A 695  ? 0.3749 0.5563 0.2776 0.0577  -0.0085 0.0165  693  GLY A CA  
5130  C C   . GLY A 695  ? 0.4000 0.5699 0.3043 0.0573  -0.0083 0.0086  693  GLY A C   
5131  O O   . GLY A 695  ? 0.3618 0.5259 0.2672 0.0574  -0.0100 0.0023  693  GLY A O   
5132  N N   . HIS A 696  ? 0.3337 0.5003 0.2387 0.0569  -0.0063 0.0088  694  HIS A N   
5133  C CA  . HIS A 696  ? 0.3299 0.4859 0.2367 0.0565  -0.0061 0.0016  694  HIS A CA  
5134  C C   . HIS A 696  ? 0.3430 0.5084 0.2466 0.0589  -0.0061 -0.0057 694  HIS A C   
5135  O O   . HIS A 696  ? 0.3966 0.5647 0.2995 0.0592  -0.0044 -0.0056 694  HIS A O   
5136  C CB  . HIS A 696  ? 0.3309 0.4765 0.2410 0.0545  -0.0042 0.0062  694  HIS A CB  
5137  C CG  . HIS A 696  ? 0.2900 0.4290 0.2034 0.0526  -0.0042 0.0140  694  HIS A CG  
5138  N ND1 . HIS A 696  ? 0.3077 0.4494 0.2222 0.0517  -0.0028 0.0228  694  HIS A ND1 
5139  C CD2 . HIS A 696  ? 0.3091 0.4397 0.2253 0.0515  -0.0055 0.0142  694  HIS A CD2 
5140  C CE1 . HIS A 696  ? 0.2773 0.4119 0.1954 0.0502  -0.0034 0.0278  694  HIS A CE1 
5141  N NE2 . HIS A 696  ? 0.3290 0.4570 0.2480 0.0501  -0.0050 0.0227  694  HIS A NE2 
5142  N N   . GLY A 697  ? 0.3397 0.5108 0.2416 0.0605  -0.0082 -0.0122 695  GLY A N   
5143  C CA  . GLY A 697  ? 0.3308 0.5124 0.2297 0.0631  -0.0086 -0.0196 695  GLY A CA  
5144  C C   . GLY A 697  ? 0.3079 0.4807 0.2094 0.0632  -0.0086 -0.0272 695  GLY A C   
5145  O O   . GLY A 697  ? 0.3154 0.4747 0.2205 0.0616  -0.0094 -0.0294 695  GLY A O   
5146  N N   . PRO A 698  ? 0.3025 0.4829 0.2023 0.0650  -0.0077 -0.0312 696  PRO A N   
5147  C CA  . PRO A 698  ? 0.3100 0.4824 0.2126 0.0653  -0.0080 -0.0387 696  PRO A CA  
5148  C C   . PRO A 698  ? 0.2976 0.4669 0.2021 0.0662  -0.0110 -0.0479 696  PRO A C   
5149  O O   . PRO A 698  ? 0.3225 0.4997 0.2252 0.0675  -0.0128 -0.0504 696  PRO A O   
5150  C CB  . PRO A 698  ? 0.3315 0.5160 0.2314 0.0675  -0.0066 -0.0410 696  PRO A CB  
5151  C CG  . PRO A 698  ? 0.4214 0.6222 0.3168 0.0690  -0.0065 -0.0379 696  PRO A CG  
5152  C CD  . PRO A 698  ? 0.3952 0.5922 0.2907 0.0668  -0.0064 -0.0289 696  PRO A CD  
5153  N N   . LEU A 699  ? 0.2876 0.4449 0.1963 0.0654  -0.0117 -0.0528 697  LEU A N   
5154  C CA  . LEU A 699  ? 0.2922 0.4464 0.2037 0.0663  -0.0147 -0.0619 697  LEU A CA  
5155  C C   . LEU A 699  ? 0.3109 0.4780 0.2207 0.0696  -0.0159 -0.0702 697  LEU A C   
5156  O O   . LEU A 699  ? 0.3229 0.4948 0.2328 0.0710  -0.0184 -0.0762 697  LEU A O   
5157  C CB  . LEU A 699  ? 0.2740 0.4133 0.1906 0.0646  -0.0151 -0.0647 697  LEU A CB  
5158  C CG  . LEU A 699  ? 0.3262 0.4519 0.2454 0.0614  -0.0145 -0.0585 697  LEU A CG  
5159  C CD1 . LEU A 699  ? 0.2854 0.3986 0.2095 0.0601  -0.0149 -0.0619 697  LEU A CD1 
5160  C CD2 . LEU A 699  ? 0.3282 0.4526 0.2477 0.0606  -0.0164 -0.0581 697  LEU A CD2 
5161  N N   . GLY A 700  ? 0.2915 0.4647 0.1998 0.0710  -0.0141 -0.0708 698  GLY A N   
5162  C CA  . GLY A 700  ? 0.2780 0.4623 0.1856 0.0742  -0.0152 -0.0797 698  GLY A CA  
5163  C C   . GLY A 700  ? 0.3213 0.4992 0.2324 0.0745  -0.0146 -0.0835 698  GLY A C   
5164  O O   . GLY A 700  ? 0.3012 0.4697 0.2136 0.0723  -0.0125 -0.0776 698  GLY A O   
5165  N N   . PRO A 701  ? 0.2851 0.4677 0.1982 0.0771  -0.0165 -0.0936 699  PRO A N   
5166  C CA  . PRO A 701  ? 0.2834 0.4607 0.2002 0.0776  -0.0161 -0.0976 699  PRO A CA  
5167  C C   . PRO A 701  ? 0.2744 0.4330 0.1966 0.0747  -0.0167 -0.0960 699  PRO A C   
5168  O O   . PRO A 701  ? 0.2838 0.4347 0.2094 0.0737  -0.0193 -0.0989 699  PRO A O   
5169  C CB  . PRO A 701  ? 0.3074 0.4926 0.2263 0.0811  -0.0189 -0.1097 699  PRO A CB  
5170  C CG  . PRO A 701  ? 0.3334 0.5343 0.2473 0.0830  -0.0193 -0.1101 699  PRO A CG  
5171  C CD  . PRO A 701  ? 0.3075 0.5028 0.2193 0.0802  -0.0189 -0.1018 699  PRO A CD  
5172  N N   . ILE A 702  ? 0.2800 0.4320 0.2029 0.0731  -0.0144 -0.0910 700  ILE A N   
5173  C CA  A ILE A 702  ? 0.2621 0.3974 0.1898 0.0703  -0.0146 -0.0889 700  ILE A CA  
5174  C CA  B ILE A 702  ? 0.2623 0.3976 0.1899 0.0703  -0.0146 -0.0888 700  ILE A CA  
5175  C C   . ILE A 702  ? 0.2638 0.3956 0.1959 0.0714  -0.0152 -0.0948 700  ILE A C   
5176  O O   . ILE A 702  ? 0.2690 0.4081 0.1992 0.0730  -0.0133 -0.0950 700  ILE A O   
5177  C CB  A ILE A 702  ? 0.2529 0.3821 0.1785 0.0674  -0.0117 -0.0781 700  ILE A CB  
5178  C CB  B ILE A 702  ? 0.2530 0.3827 0.1785 0.0675  -0.0115 -0.0780 700  ILE A CB  
5179  C CG1 A ILE A 702  ? 0.2738 0.4035 0.1969 0.0660  -0.0120 -0.0730 700  ILE A CG1 
5180  C CG1 B ILE A 702  ? 0.2718 0.4055 0.1935 0.0665  -0.0111 -0.0718 700  ILE A CG1 
5181  C CG2 A ILE A 702  ? 0.2548 0.3685 0.1851 0.0648  -0.0116 -0.0764 700  ILE A CG2 
5182  C CG2 B ILE A 702  ? 0.2553 0.3685 0.1855 0.0646  -0.0118 -0.0760 700  ILE A CG2 
5183  C CD1 A ILE A 702  ? 0.2546 0.3786 0.1763 0.0633  -0.0095 -0.0629 700  ILE A CD1 
5184  C CD1 B ILE A 702  ? 0.2875 0.4139 0.2115 0.0653  -0.0136 -0.0736 700  ILE A CD1 
5185  N N   . VAL A 703  ? 0.2629 0.3837 0.2009 0.0705  -0.0178 -0.0994 701  VAL A N   
5186  C CA  . VAL A 703  ? 0.2585 0.3738 0.2018 0.0712  -0.0188 -0.1045 701  VAL A CA  
5187  C C   . VAL A 703  ? 0.2441 0.3469 0.1889 0.0680  -0.0169 -0.0973 701  VAL A C   
5188  O O   . VAL A 703  ? 0.2719 0.3646 0.2182 0.0652  -0.0174 -0.0933 701  VAL A O   
5189  C CB  . VAL A 703  ? 0.2832 0.3937 0.2330 0.0719  -0.0230 -0.1133 701  VAL A CB  
5190  C CG1 . VAL A 703  ? 0.2999 0.4020 0.2562 0.0719  -0.0242 -0.1172 701  VAL A CG1 
5191  C CG2 . VAL A 703  ? 0.2904 0.4145 0.2388 0.0755  -0.0248 -0.1214 701  VAL A CG2 
5192  N N   . CYS A 704  ? 0.2408 0.3450 0.1850 0.0685  -0.0147 -0.0956 702  CYS A N   
5193  C CA  . CYS A 704  ? 0.2545 0.3479 0.2000 0.0657  -0.0128 -0.0891 702  CYS A CA  
5194  C C   . CYS A 704  ? 0.2597 0.3465 0.2114 0.0662  -0.0145 -0.0945 702  CYS A C   
5195  O O   . CYS A 704  ? 0.2542 0.3477 0.2066 0.0687  -0.0143 -0.0991 702  CYS A O   
5196  C CB  . CYS A 704  ? 0.2696 0.3690 0.2102 0.0656  -0.0091 -0.0822 702  CYS A CB  
5197  S SG  . CYS A 704  ? 0.2708 0.3779 0.2049 0.0649  -0.0073 -0.0748 702  CYS A SG  
5198  N N   . ILE A 705  ? 0.2411 0.3150 0.1976 0.0637  -0.0161 -0.0937 703  ILE A N   
5199  C CA  . ILE A 705  ? 0.2706 0.3368 0.2338 0.0637  -0.0181 -0.0981 703  ILE A CA  
5200  C C   . ILE A 705  ? 0.2524 0.3085 0.2163 0.0607  -0.0162 -0.0909 703  ILE A C   
5201  O O   . ILE A 705  ? 0.2560 0.3055 0.2187 0.0578  -0.0155 -0.0850 703  ILE A O   
5202  C CB  . ILE A 705  ? 0.2600 0.3205 0.2291 0.0634  -0.0222 -0.1037 703  ILE A CB  
5203  C CG1 . ILE A 705  ? 0.2714 0.3425 0.2404 0.0667  -0.0243 -0.1120 703  ILE A CG1 
5204  C CG2 . ILE A 705  ? 0.2719 0.3229 0.2487 0.0627  -0.0243 -0.1065 703  ILE A CG2 
5205  C CD1 . ILE A 705  ? 0.2911 0.3576 0.2649 0.0660  -0.0280 -0.1161 703  ILE A CD1 
5206  N N   . SER A 706  ? 0.2673 0.3227 0.2330 0.0614  -0.0153 -0.0915 704  SER A N   
5207  C CA  . SER A 706  ? 0.2560 0.3042 0.2212 0.0589  -0.0130 -0.0845 704  SER A CA  
5208  C C   . SER A 706  ? 0.2451 0.2845 0.2169 0.0583  -0.0148 -0.0870 704  SER A C   
5209  O O   . SER A 706  ? 0.2697 0.3107 0.2462 0.0605  -0.0173 -0.0943 704  SER A O   
5210  C CB  . SER A 706  ? 0.2784 0.3349 0.2385 0.0599  -0.0095 -0.0808 704  SER A CB  
5211  O OG  . SER A 706  ? 0.2766 0.3419 0.2374 0.0633  -0.0099 -0.0872 704  SER A OG  
5212  N N   . PRO A 707  ? 0.2479 0.2784 0.2206 0.0554  -0.0137 -0.0810 705  PRO A N   
5213  C CA  . PRO A 707  ? 0.2650 0.2868 0.2440 0.0544  -0.0154 -0.0823 705  PRO A CA  
5214  C C   . PRO A 707  ? 0.2493 0.2738 0.2284 0.0558  -0.0137 -0.0824 705  PRO A C   
5215  O O   . PRO A 707  ? 0.2570 0.2888 0.2310 0.0568  -0.0108 -0.0799 705  PRO A O   
5216  C CB  . PRO A 707  ? 0.2584 0.2708 0.2371 0.0506  -0.0145 -0.0750 705  PRO A CB  
5217  C CG  . PRO A 707  ? 0.2387 0.2558 0.2105 0.0501  -0.0111 -0.0692 705  PRO A CG  
5218  C CD  . PRO A 707  ? 0.2607 0.2881 0.2290 0.0527  -0.0111 -0.0727 705  PRO A CD  
5219  N N   . TRP A 708  ? 0.2592 0.2778 0.2447 0.0558  -0.0157 -0.0851 706  TRP A N   
5220  C CA  . TRP A 708  ? 0.2434 0.2644 0.2296 0.0572  -0.0143 -0.0857 706  TRP A CA  
5221  C C   . TRP A 708  ? 0.2615 0.2783 0.2447 0.0547  -0.0113 -0.0777 706  TRP A C   
5222  O O   . TRP A 708  ? 0.2809 0.3023 0.2624 0.0558  -0.0092 -0.0767 706  TRP A O   
5223  C CB  . TRP A 708  ? 0.2561 0.2723 0.2506 0.0582  -0.0176 -0.0914 706  TRP A CB  
5224  C CG  . TRP A 708  ? 0.2515 0.2558 0.2502 0.0549  -0.0188 -0.0870 706  TRP A CG  
5225  C CD1 . TRP A 708  ? 0.2839 0.2808 0.2870 0.0529  -0.0217 -0.0871 706  TRP A CD1 
5226  C CD2 . TRP A 708  ? 0.2740 0.2732 0.2727 0.0530  -0.0171 -0.0815 706  TRP A CD2 
5227  N NE1 . TRP A 708  ? 0.2852 0.2731 0.2908 0.0499  -0.0217 -0.0818 706  TRP A NE1 
5228  C CE2 . TRP A 708  ? 0.2635 0.2527 0.2664 0.0500  -0.0190 -0.0785 706  TRP A CE2 
5229  C CE3 . TRP A 708  ? 0.2840 0.2866 0.2797 0.0536  -0.0141 -0.0789 706  TRP A CE3 
5230  C CZ2 . TRP A 708  ? 0.2575 0.2402 0.2614 0.0476  -0.0181 -0.0731 706  TRP A CZ2 
5231  C CZ3 . TRP A 708  ? 0.2898 0.2855 0.2867 0.0512  -0.0133 -0.0736 706  TRP A CZ3 
5232  C CH2 . TRP A 708  ? 0.2848 0.2708 0.2858 0.0483  -0.0153 -0.0709 706  TRP A CH2 
5233  N N   . ASN A 709  ? 0.2625 0.2715 0.2451 0.0514  -0.0111 -0.0721 707  ASN A N   
5234  C CA  . ASN A 709  ? 0.2846 0.2877 0.2669 0.0490  -0.0093 -0.0659 707  ASN A CA  
5235  C C   . ASN A 709  ? 0.2962 0.3038 0.2722 0.0485  -0.0056 -0.0601 707  ASN A C   
5236  O O   . ASN A 709  ? 0.2946 0.2997 0.2702 0.0474  -0.0038 -0.0561 707  ASN A O   
5237  C CB  . ASN A 709  ? 0.2677 0.2609 0.2525 0.0457  -0.0107 -0.0625 707  ASN A CB  
5238  C CG  . ASN A 709  ? 0.3051 0.2984 0.2857 0.0442  -0.0098 -0.0590 707  ASN A CG  
5239  O OD1 . ASN A 709  ? 0.3103 0.3073 0.2902 0.0453  -0.0109 -0.0622 707  ASN A OD1 
5240  N ND2 . ASN A 709  ? 0.3047 0.2943 0.2828 0.0417  -0.0077 -0.0526 707  ASN A ND2 
5241  N N   . PHE A 710  ? 0.2852 0.2991 0.2565 0.0492  -0.0045 -0.0595 708  PHE A N   
5242  C CA  . PHE A 710  ? 0.2932 0.3132 0.2591 0.0493  -0.0013 -0.0546 708  PHE A CA  
5243  C C   . PHE A 710  ? 0.2848 0.3164 0.2485 0.0525  -0.0011 -0.0591 708  PHE A C   
5244  O O   . PHE A 710  ? 0.2782 0.3153 0.2383 0.0531  -0.0008 -0.0587 708  PHE A O   
5245  C CB  . PHE A 710  ? 0.2812 0.2987 0.2439 0.0470  -0.0004 -0.0492 708  PHE A CB  
5246  C CG  . PHE A 710  ? 0.3483 0.3554 0.3129 0.0439  -0.0005 -0.0450 708  PHE A CG  
5247  C CD1 . PHE A 710  ? 0.3413 0.3440 0.3079 0.0428  0.0002  -0.0429 708  PHE A CD1 
5248  C CD2 . PHE A 710  ? 0.3105 0.3130 0.2750 0.0420  -0.0014 -0.0433 708  PHE A CD2 
5249  C CE1 . PHE A 710  ? 0.3527 0.3469 0.3210 0.0400  0.0001  -0.0392 708  PHE A CE1 
5250  C CE2 . PHE A 710  ? 0.3271 0.3213 0.2933 0.0391  -0.0015 -0.0396 708  PHE A CE2 
5251  C CZ  . PHE A 710  ? 0.3721 0.3622 0.3400 0.0382  -0.0007 -0.0376 708  PHE A CZ  
5252  N N   . PRO A 711  ? 0.2796 0.3156 0.2453 0.0549  -0.0013 -0.0635 709  PRO A N   
5253  C CA  . PRO A 711  ? 0.2749 0.3216 0.2398 0.0583  -0.0020 -0.0699 709  PRO A CA  
5254  C C   . PRO A 711  ? 0.2667 0.3250 0.2258 0.0595  0.0008  -0.0671 709  PRO A C   
5255  O O   . PRO A 711  ? 0.2777 0.3461 0.2352 0.0622  0.0003  -0.0719 709  PRO A O   
5256  C CB  . PRO A 711  ? 0.2903 0.3374 0.2598 0.0602  -0.0028 -0.0748 709  PRO A CB  
5257  C CG  . PRO A 711  ? 0.2704 0.3119 0.2399 0.0580  -0.0008 -0.0685 709  PRO A CG  
5258  C CD  . PRO A 711  ? 0.2811 0.3127 0.2501 0.0545  -0.0009 -0.0630 709  PRO A CD  
5259  N N   . LEU A 712  ? 0.2756 0.3334 0.2318 0.0576  0.0035  -0.0595 710  LEU A N   
5260  C CA  . LEU A 712  ? 0.2476 0.3157 0.1986 0.0583  0.0059  -0.0555 710  LEU A CA  
5261  C C   . LEU A 712  ? 0.2676 0.3327 0.2157 0.0559  0.0066  -0.0493 710  LEU A C   
5262  O O   . LEU A 712  ? 0.2565 0.3297 0.2010 0.0568  0.0070  -0.0486 710  LEU A O   
5263  C CB  . LEU A 712  ? 0.2741 0.3460 0.2244 0.0582  0.0086  -0.0515 710  LEU A CB  
5264  C CG  . LEU A 712  ? 0.2661 0.3496 0.2116 0.0588  0.0111  -0.0468 710  LEU A CG  
5265  C CD1 . LEU A 712  ? 0.2531 0.3496 0.1966 0.0621  0.0105  -0.0528 710  LEU A CD1 
5266  C CD2 . LEU A 712  ? 0.2890 0.3747 0.2343 0.0581  0.0137  -0.0416 710  LEU A CD2 
5267  N N   . ALA A 713  ? 0.2656 0.3196 0.2153 0.0530  0.0066  -0.0451 711  ALA A N   
5268  C CA  . ALA A 713  ? 0.2374 0.2888 0.1847 0.0509  0.0074  -0.0388 711  ALA A CA  
5269  C C   . ALA A 713  ? 0.2674 0.3189 0.2138 0.0511  0.0055  -0.0414 711  ALA A C   
5270  O O   . ALA A 713  ? 0.2594 0.3171 0.2024 0.0514  0.0062  -0.0387 711  ALA A O   
5271  C CB  . ALA A 713  ? 0.2366 0.2765 0.1862 0.0479  0.0078  -0.0345 711  ALA A CB  
5272  N N   . ILE A 714  ? 0.2411 0.2857 0.1909 0.0508  0.0030  -0.0461 712  ILE A N   
5273  C CA  . ILE A 714  ? 0.2394 0.2838 0.1889 0.0509  0.0011  -0.0485 712  ILE A CA  
5274  C C   . ILE A 714  ? 0.2625 0.3183 0.2099 0.0540  0.0004  -0.0536 712  ILE A C   
5275  O O   . ILE A 714  ? 0.2680 0.3286 0.2127 0.0543  0.0001  -0.0531 712  ILE A O   
5276  C CB  . ILE A 714  ? 0.2638 0.2982 0.2179 0.0497  -0.0015 -0.0520 712  ILE A CB  
5277  C CG1 . ILE A 714  ? 0.2875 0.3120 0.2426 0.0465  -0.0007 -0.0461 712  ILE A CG1 
5278  C CG2 . ILE A 714  ? 0.2600 0.2956 0.2145 0.0503  -0.0040 -0.0561 712  ILE A CG2 
5279  C CD1 . ILE A 714  ? 0.3718 0.3877 0.3303 0.0446  -0.0029 -0.0473 712  ILE A CD1 
5280  N N   . PHE A 715  ? 0.2581 0.3188 0.2070 0.0563  0.0001  -0.0587 713  PHE A N   
5281  C CA  . PHE A 715  ? 0.2497 0.3229 0.1965 0.0595  -0.0003 -0.0638 713  PHE A CA  
5282  C C   . PHE A 715  ? 0.2800 0.3629 0.2212 0.0597  0.0021  -0.0584 713  PHE A C   
5283  O O   . PHE A 715  ? 0.2461 0.3359 0.1847 0.0608  0.0014  -0.0596 713  PHE A O   
5284  C CB  . PHE A 715  ? 0.2656 0.3429 0.2146 0.0617  -0.0001 -0.0686 713  PHE A CB  
5285  C CG  . PHE A 715  ? 0.2472 0.3382 0.1942 0.0652  -0.0003 -0.0742 713  PHE A CG  
5286  C CD1 . PHE A 715  ? 0.2727 0.3657 0.2221 0.0672  -0.0033 -0.0825 713  PHE A CD1 
5287  C CD2 . PHE A 715  ? 0.2614 0.3639 0.2043 0.0665  0.0024  -0.0714 713  PHE A CD2 
5288  C CE1 . PHE A 715  ? 0.3113 0.4178 0.2589 0.0706  -0.0036 -0.0883 713  PHE A CE1 
5289  C CE2 . PHE A 715  ? 0.2766 0.3931 0.2175 0.0697  0.0022  -0.0767 713  PHE A CE2 
5290  C CZ  . PHE A 715  ? 0.3105 0.4291 0.2536 0.0719  -0.0008 -0.0854 713  PHE A CZ  
5291  N N   . THR A 716  ? 0.2438 0.3273 0.1835 0.0586  0.0048  -0.0519 714  THR A N   
5292  C CA  . THR A 716  ? 0.2553 0.3483 0.1905 0.0586  0.0070  -0.0459 714  THR A CA  
5293  C C   . THR A 716  ? 0.2691 0.3583 0.2027 0.0567  0.0067  -0.0410 714  THR A C   
5294  O O   . THR A 716  ? 0.2518 0.3500 0.1820 0.0575  0.0070  -0.0393 714  THR A O   
5295  C CB  . THR A 716  ? 0.2655 0.3585 0.2006 0.0575  0.0096  -0.0399 714  THR A CB  
5296  O OG1 . THR A 716  ? 0.2627 0.3608 0.1992 0.0596  0.0100  -0.0446 714  THR A OG1 
5297  C CG2 . THR A 716  ? 0.2945 0.3966 0.2258 0.0572  0.0117  -0.0328 714  THR A CG2 
5298  N N   . GLY A 717  ? 0.2285 0.3051 0.1647 0.0541  0.0061  -0.0388 715  GLY A N   
5299  C CA  . GLY A 717  ? 0.2509 0.3237 0.1860 0.0523  0.0059  -0.0342 715  GLY A CA  
5300  C C   . GLY A 717  ? 0.2572 0.3345 0.1909 0.0535  0.0039  -0.0382 715  GLY A C   
5301  O O   . GLY A 717  ? 0.2631 0.3462 0.1938 0.0536  0.0044  -0.0345 715  GLY A O   
5302  N N   . GLN A 718  ? 0.2400 0.3149 0.1760 0.0546  0.0016  -0.0456 716  GLN A N   
5303  C CA  . GLN A 718  ? 0.2543 0.3330 0.1896 0.0557  -0.0005 -0.0498 716  GLN A CA  
5304  C C   . GLN A 718  ? 0.2600 0.3535 0.1912 0.0583  0.0001  -0.0509 716  GLN A C   
5305  O O   . GLN A 718  ? 0.2554 0.3540 0.1839 0.0585  -0.0003 -0.0492 716  GLN A O   
5306  C CB  . GLN A 718  ? 0.2357 0.3096 0.1752 0.0565  -0.0033 -0.0579 716  GLN A CB  
5307  C CG  . GLN A 718  ? 0.2563 0.3164 0.1999 0.0539  -0.0042 -0.0567 716  GLN A CG  
5308  C CD  . GLN A 718  ? 0.2616 0.3170 0.2100 0.0544  -0.0074 -0.0640 716  GLN A CD  
5309  O OE1 . GLN A 718  ? 0.2564 0.3037 0.2072 0.0524  -0.0089 -0.0635 716  GLN A OE1 
5310  N NE2 . GLN A 718  ? 0.2679 0.3285 0.2179 0.0570  -0.0085 -0.0707 716  GLN A NE2 
5311  N N   . ILE A 719  ? 0.2554 0.3563 0.1862 0.0604  0.0009  -0.0539 717  ILE A N   
5312  C CA  . ILE A 719  ? 0.2513 0.3676 0.1783 0.0631  0.0015  -0.0556 717  ILE A CA  
5313  C C   . ILE A 719  ? 0.2605 0.3830 0.1835 0.0621  0.0038  -0.0467 717  ILE A C   
5314  O O   . ILE A 719  ? 0.2541 0.3866 0.1737 0.0632  0.0036  -0.0460 717  ILE A O   
5315  C CB  . ILE A 719  ? 0.2869 0.4095 0.2148 0.0654  0.0021  -0.0604 717  ILE A CB  
5316  C CG1 . ILE A 719  ? 0.2756 0.3936 0.2078 0.0668  -0.0008 -0.0700 717  ILE A CG1 
5317  C CG2 . ILE A 719  ? 0.3551 0.4947 0.2785 0.0678  0.0034  -0.0604 717  ILE A CG2 
5318  C CD1 . ILE A 719  ? 0.3295 0.4493 0.2641 0.0684  -0.0003 -0.0740 717  ILE A CD1 
5319  N N   . ALA A 720  ? 0.2662 0.3832 0.1899 0.0600  0.0058  -0.0398 718  ALA A N   
5320  C CA  . ALA A 720  ? 0.2634 0.3859 0.1844 0.0589  0.0079  -0.0309 718  ALA A CA  
5321  C C   . ALA A 720  ? 0.2349 0.3548 0.1549 0.0576  0.0068  -0.0275 718  ALA A C   
5322  O O   . ALA A 720  ? 0.2470 0.3765 0.1640 0.0581  0.0074  -0.0234 718  ALA A O   
5323  C CB  . ALA A 720  ? 0.2671 0.3821 0.1900 0.0567  0.0098  -0.0247 718  ALA A CB  
5324  N N   . ALA A 721  ? 0.2329 0.3403 0.1556 0.0560  0.0054  -0.0290 719  ALA A N   
5325  C CA  . ALA A 721  ? 0.2204 0.3250 0.1427 0.0549  0.0043  -0.0262 719  ALA A CA  
5326  C C   . ALA A 721  ? 0.2643 0.3791 0.1839 0.0570  0.0027  -0.0306 719  ALA A C   
5327  O O   . ALA A 721  ? 0.2343 0.3554 0.1515 0.0570  0.0028  -0.0262 719  ALA A O   
5328  C CB  . ALA A 721  ? 0.2426 0.3330 0.1685 0.0530  0.0029  -0.0283 719  ALA A CB  
5329  N N   . ALA A 722  ? 0.2331 0.3497 0.1536 0.0590  0.0010  -0.0393 720  ALA A N   
5330  C CA  . ALA A 722  ? 0.2294 0.3556 0.1477 0.0612  -0.0008 -0.0444 720  ALA A CA  
5331  C C   . ALA A 722  ? 0.2696 0.4118 0.1834 0.0630  0.0007  -0.0415 720  ALA A C   
5332  O O   . ALA A 722  ? 0.2613 0.4110 0.1722 0.0635  0.0001  -0.0397 720  ALA A O   
5333  C CB  . ALA A 722  ? 0.2722 0.3974 0.1930 0.0630  -0.0029 -0.0545 720  ALA A CB  
5334  N N   . LEU A 723  ? 0.2446 0.3923 0.1576 0.0638  0.0026  -0.0408 721  LEU A N   
5335  C CA  . LEU A 723  ? 0.2350 0.3989 0.1440 0.0655  0.0042  -0.0379 721  LEU A CA  
5336  C C   . LEU A 723  ? 0.2484 0.4145 0.1555 0.0636  0.0054  -0.0276 721  LEU A C   
5337  O O   . LEU A 723  ? 0.2426 0.4209 0.1463 0.0647  0.0054  -0.0253 721  LEU A O   
5338  C CB  . LEU A 723  ? 0.2768 0.4444 0.1861 0.0662  0.0062  -0.0381 721  LEU A CB  
5339  C CG  . LEU A 723  ? 0.2450 0.4157 0.1557 0.0689  0.0051  -0.0483 721  LEU A CG  
5340  C CD1 . LEU A 723  ? 0.2559 0.4280 0.1674 0.0690  0.0074  -0.0467 721  LEU A CD1 
5341  C CD2 . LEU A 723  ? 0.2630 0.4496 0.1703 0.0720  0.0041  -0.0538 721  LEU A CD2 
5342  N N   . VAL A 724  ? 0.2648 0.4194 0.1744 0.0609  0.0065  -0.0211 722  VAL A N   
5343  C CA  . VAL A 724  ? 0.2643 0.4214 0.1731 0.0592  0.0077  -0.0111 722  VAL A CA  
5344  C C   . VAL A 724  ? 0.2593 0.4154 0.1674 0.0588  0.0059  -0.0099 722  VAL A C   
5345  O O   . VAL A 724  ? 0.2707 0.4338 0.1771 0.0584  0.0063  -0.0031 722  VAL A O   
5346  C CB  . VAL A 724  ? 0.2308 0.3766 0.1429 0.0566  0.0092  -0.0049 722  VAL A CB  
5347  C CG1 . VAL A 724  ? 0.2483 0.3786 0.1637 0.0546  0.0079  -0.0054 722  VAL A CG1 
5348  C CG2 . VAL A 724  ? 0.2674 0.4199 0.1789 0.0555  0.0109  0.0052  722  VAL A CG2 
5349  N N   . ALA A 725  ? 0.2529 0.4007 0.1625 0.0589  0.0038  -0.0164 723  ALA A N   
5350  C CA  . ALA A 725  ? 0.2581 0.4058 0.1671 0.0588  0.0019  -0.0167 723  ALA A CA  
5351  C C   . ALA A 725  ? 0.3073 0.4700 0.2125 0.0614  0.0009  -0.0205 723  ALA A C   
5352  O O   . ALA A 725  ? 0.2972 0.4613 0.2015 0.0616  -0.0009 -0.0213 723  ALA A O   
5353  C CB  . ALA A 725  ? 0.2504 0.3849 0.1626 0.0579  0.0000  -0.0224 723  ALA A CB  
5354  N N   . GLY A 726  ? 0.2665 0.4407 0.1693 0.0635  0.0018  -0.0232 724  GLY A N   
5355  C CA  . GLY A 726  ? 0.2635 0.4536 0.1624 0.0661  0.0010  -0.0268 724  GLY A CA  
5356  C C   . GLY A 726  ? 0.2882 0.4804 0.1874 0.0685  -0.0011 -0.0384 724  GLY A C   
5357  O O   . GLY A 726  ? 0.3075 0.5126 0.2036 0.0708  -0.0022 -0.0423 724  GLY A O   
5358  N N   . ASN A 727  ? 0.2785 0.4589 0.1815 0.0682  -0.0018 -0.0440 725  ASN A N   
5359  C CA  . ASN A 727  ? 0.2671 0.4477 0.1717 0.0703  -0.0042 -0.0551 725  ASN A CA  
5360  C C   . ASN A 727  ? 0.2573 0.4443 0.1621 0.0724  -0.0033 -0.0604 725  ASN A C   
5361  O O   . ASN A 727  ? 0.2636 0.4452 0.1699 0.0713  -0.0014 -0.0572 725  ASN A O   
5362  C CB  . ASN A 727  ? 0.2768 0.4401 0.1864 0.0684  -0.0058 -0.0579 725  ASN A CB  
5363  C CG  . ASN A 727  ? 0.2841 0.4396 0.1942 0.0660  -0.0064 -0.0526 725  ASN A CG  
5364  O OD1 . ASN A 727  ? 0.3046 0.4637 0.2138 0.0667  -0.0084 -0.0550 725  ASN A OD1 
5365  N ND2 . ASN A 727  ? 0.2672 0.4122 0.1790 0.0633  -0.0049 -0.0456 725  ASN A ND2 
5366  N N   . PRO A 728  ? 0.2653 0.4632 0.1691 0.0755  -0.0048 -0.0691 726  PRO A N   
5367  C CA  . PRO A 728  ? 0.2784 0.4799 0.1837 0.0777  -0.0046 -0.0760 726  PRO A CA  
5368  C C   . PRO A 728  ? 0.2792 0.4651 0.1906 0.0769  -0.0064 -0.0817 726  PRO A C   
5369  O O   . PRO A 728  ? 0.2950 0.4712 0.2090 0.0757  -0.0087 -0.0837 726  PRO A O   
5370  C CB  . PRO A 728  ? 0.2811 0.4987 0.1840 0.0813  -0.0062 -0.0842 726  PRO A CB  
5371  C CG  . PRO A 728  ? 0.2762 0.4917 0.1787 0.0808  -0.0086 -0.0849 726  PRO A CG  
5372  C CD  . PRO A 728  ? 0.2790 0.4851 0.1809 0.0773  -0.0072 -0.0739 726  PRO A CD  
5373  N N   . VAL A 729  ? 0.2872 0.4709 0.2010 0.0775  -0.0054 -0.0841 727  VAL A N   
5374  C CA  . VAL A 729  ? 0.2716 0.4395 0.1912 0.0762  -0.0066 -0.0869 727  VAL A CA  
5375  C C   . VAL A 729  ? 0.2849 0.4559 0.2081 0.0791  -0.0084 -0.0977 727  VAL A C   
5376  O O   . VAL A 729  ? 0.2858 0.4690 0.2072 0.0817  -0.0072 -0.1004 727  VAL A O   
5377  C CB  . VAL A 729  ? 0.2386 0.3979 0.1587 0.0735  -0.0038 -0.0786 727  VAL A CB  
5378  C CG1 . VAL A 729  ? 0.2836 0.4295 0.2096 0.0727  -0.0049 -0.0824 727  VAL A CG1 
5379  C CG2 . VAL A 729  ? 0.2754 0.4281 0.1939 0.0704  -0.0029 -0.0694 727  VAL A CG2 
5380  N N   . LEU A 730  ? 0.2702 0.4302 0.1990 0.0788  -0.0114 -0.1037 728  LEU A N   
5381  C CA  . LEU A 730  ? 0.2678 0.4259 0.2021 0.0808  -0.0134 -0.1130 728  LEU A CA  
5382  C C   . LEU A 730  ? 0.2645 0.4071 0.2031 0.0782  -0.0128 -0.1093 728  LEU A C   
5383  O O   . LEU A 730  ? 0.2757 0.4055 0.2170 0.0754  -0.0140 -0.1066 728  LEU A O   
5384  C CB  . LEU A 730  ? 0.3028 0.4592 0.2413 0.0821  -0.0176 -0.1220 728  LEU A CB  
5385  C CG  . LEU A 730  ? 0.2644 0.4358 0.1993 0.0849  -0.0188 -0.1271 728  LEU A CG  
5386  C CD1 . LEU A 730  ? 0.2920 0.4788 0.2250 0.0870  -0.0169 -0.1270 728  LEU A CD1 
5387  C CD2 . LEU A 730  ? 0.2925 0.4643 0.2228 0.0829  -0.0182 -0.1200 728  LEU A CD2 
5388  N N   . ALA A 731  ? 0.2865 0.4310 0.2257 0.0789  -0.0110 -0.1088 729  ALA A N   
5389  C CA  . ALA A 731  ? 0.2776 0.4088 0.2200 0.0764  -0.0100 -0.1043 729  ALA A CA  
5390  C C   . ALA A 731  ? 0.3121 0.4373 0.2618 0.0777  -0.0127 -0.1128 729  ALA A C   
5391  O O   . ALA A 731  ? 0.2979 0.4314 0.2488 0.0807  -0.0129 -0.1190 729  ALA A O   
5392  C CB  . ALA A 731  ? 0.2929 0.4294 0.2316 0.0761  -0.0062 -0.0978 729  ALA A CB  
5393  N N   . LYS A 732  ? 0.2670 0.3780 0.2217 0.0754  -0.0149 -0.1128 730  LYS A N   
5394  C CA  . LYS A 732  ? 0.2774 0.3812 0.2400 0.0763  -0.0180 -0.1200 730  LYS A CA  
5395  C C   . LYS A 732  ? 0.2708 0.3620 0.2362 0.0734  -0.0169 -0.1142 730  LYS A C   
5396  O O   . LYS A 732  ? 0.2725 0.3521 0.2398 0.0703  -0.0176 -0.1100 730  LYS A O   
5397  C CB  . LYS A 732  ? 0.3019 0.4002 0.2690 0.0759  -0.0219 -0.1249 730  LYS A CB  
5398  C CG  . LYS A 732  ? 0.2908 0.3898 0.2653 0.0787  -0.0258 -0.1359 730  LYS A CG  
5399  C CD  . LYS A 732  ? 0.2875 0.3773 0.2684 0.0782  -0.0265 -0.1368 730  LYS A CD  
5400  C CE  . LYS A 732  ? 0.3077 0.3817 0.2931 0.0742  -0.0278 -0.1318 730  LYS A CE  
5401  N NZ  . LYS A 732  ? 0.2991 0.3647 0.2903 0.0736  -0.0282 -0.1316 730  LYS A NZ  
5402  N N   . PRO A 733  ? 0.2449 0.3383 0.2106 0.0743  -0.0151 -0.1138 731  PRO A N   
5403  C CA  . PRO A 733  ? 0.2627 0.3444 0.2311 0.0717  -0.0142 -0.1085 731  PRO A CA  
5404  C C   . PRO A 733  ? 0.2496 0.3213 0.2266 0.0715  -0.0178 -0.1138 731  PRO A C   
5405  O O   . PRO A 733  ? 0.2817 0.3565 0.2633 0.0741  -0.0209 -0.1226 731  PRO A O   
5406  C CB  . PRO A 733  ? 0.2588 0.3483 0.2249 0.0733  -0.0113 -0.1075 731  PRO A CB  
5407  C CG  . PRO A 733  ? 0.2830 0.3854 0.2495 0.0775  -0.0126 -0.1166 731  PRO A CG  
5408  C CD  . PRO A 733  ? 0.2615 0.3687 0.2251 0.0779  -0.0139 -0.1183 731  PRO A CD  
5409  N N   . ALA A 734  ? 0.2565 0.3160 0.2359 0.0684  -0.0175 -0.1083 732  ALA A N   
5410  C CA  . ALA A 734  ? 0.2829 0.3324 0.2708 0.0678  -0.0209 -0.1120 732  ALA A CA  
5411  C C   . ALA A 734  ? 0.2776 0.3318 0.2701 0.0711  -0.0221 -0.1195 732  ALA A C   
5412  O O   . ALA A 734  ? 0.2864 0.3482 0.2757 0.0728  -0.0195 -0.1190 732  ALA A O   
5413  C CB  . ALA A 734  ? 0.2656 0.3038 0.2544 0.0642  -0.0196 -0.1042 732  ALA A CB  
5414  N N   . GLU A 735  ? 0.2719 0.3216 0.2727 0.0721  -0.0263 -0.1264 733  GLU A N   
5415  C CA  . GLU A 735  ? 0.3052 0.3592 0.3114 0.0756  -0.0280 -0.1346 733  GLU A CA  
5416  C C   . GLU A 735  ? 0.3178 0.3679 0.3257 0.0750  -0.0264 -0.1312 733  GLU A C   
5417  O O   . GLU A 735  ? 0.3239 0.3804 0.3340 0.0781  -0.0265 -0.1366 733  GLU A O   
5418  C CB  . GLU A 735  ? 0.3232 0.3719 0.3390 0.0765  -0.0332 -0.1424 733  GLU A CB  
5419  C CG  . GLU A 735  ? 0.3157 0.3496 0.3376 0.0728  -0.0355 -0.1380 733  GLU A CG  
5420  C CD  . GLU A 735  ? 0.3785 0.4082 0.3985 0.0700  -0.0362 -0.1345 733  GLU A CD  
5421  O OE1 . GLU A 735  ? 0.3566 0.3932 0.3685 0.0701  -0.0336 -0.1319 733  GLU A OE1 
5422  O OE2 . GLU A 735  ? 0.3694 0.3892 0.3962 0.0678  -0.0393 -0.1340 733  GLU A OE2 
5423  N N   . GLU A 736  ? 0.3092 0.3495 0.3162 0.0713  -0.0250 -0.1227 734  GLU A N   
5424  C CA  . GLU A 736  ? 0.2869 0.3230 0.2958 0.0706  -0.0237 -0.1195 734  GLU A CA  
5425  C C   . GLU A 736  ? 0.2983 0.3431 0.2998 0.0714  -0.0192 -0.1156 734  GLU A C   
5426  O O   . GLU A 736  ? 0.3253 0.3713 0.3286 0.0725  -0.0183 -0.1161 734  GLU A O   
5427  C CB  . GLU A 736  ? 0.2824 0.3055 0.2929 0.0663  -0.0238 -0.1118 734  GLU A CB  
5428  C CG  . GLU A 736  ? 0.3348 0.3484 0.3534 0.0649  -0.0282 -0.1143 734  GLU A CG  
5429  C CD  . GLU A 736  ? 0.4096 0.4214 0.4259 0.0631  -0.0290 -0.1126 734  GLU A CD  
5430  O OE1 . GLU A 736  ? 0.3104 0.3299 0.3195 0.0638  -0.0268 -0.1119 734  GLU A OE1 
5431  O OE2 . GLU A 736  ? 0.3425 0.3452 0.3643 0.0607  -0.0318 -0.1116 734  GLU A OE2 
5432  N N   . THR A 737  ? 0.2850 0.3362 0.2787 0.0709  -0.0166 -0.1117 735  THR A N   
5433  C CA  . THR A 737  ? 0.2829 0.3409 0.2697 0.0707  -0.0123 -0.1059 735  THR A CA  
5434  C C   . THR A 737  ? 0.2757 0.3480 0.2565 0.0732  -0.0106 -0.1081 735  THR A C   
5435  O O   . THR A 737  ? 0.2935 0.3693 0.2678 0.0718  -0.0079 -0.1017 735  THR A O   
5436  C CB  . THR A 737  ? 0.2919 0.3418 0.2752 0.0666  -0.0101 -0.0960 735  THR A CB  
5437  O OG1 . THR A 737  ? 0.2765 0.3232 0.2580 0.0650  -0.0112 -0.0946 735  THR A OG1 
5438  C CG2 . THR A 737  ? 0.2846 0.3225 0.2731 0.0644  -0.0111 -0.0935 735  THR A CG2 
5439  N N   . PRO A 738  ? 0.2766 0.3581 0.2597 0.0771  -0.0123 -0.1170 736  PRO A N   
5440  C CA  . PRO A 738  ? 0.2676 0.3641 0.2448 0.0795  -0.0107 -0.1191 736  PRO A CA  
5441  C C   . PRO A 738  ? 0.2998 0.4065 0.2717 0.0803  -0.0067 -0.1150 736  PRO A C   
5442  O O   . PRO A 738  ? 0.2785 0.3963 0.2441 0.0811  -0.0047 -0.1130 736  PRO A O   
5443  C CB  . PRO A 738  ? 0.3139 0.4164 0.2963 0.0835  -0.0140 -0.1308 736  PRO A CB  
5444  C CG  . PRO A 738  ? 0.2946 0.3897 0.2843 0.0839  -0.0156 -0.1337 736  PRO A CG  
5445  C CD  . PRO A 738  ? 0.3048 0.3845 0.2961 0.0795  -0.0155 -0.1257 736  PRO A CD  
5446  N N   . LEU A 739  ? 0.2695 0.3733 0.2439 0.0802  -0.0056 -0.1135 737  LEU A N   
5447  C CA  . LEU A 739  ? 0.2653 0.3806 0.2357 0.0814  -0.0021 -0.1109 737  LEU A CA  
5448  C C   . LEU A 739  ? 0.2446 0.3606 0.2082 0.0785  0.0014  -0.1003 737  LEU A C   
5449  O O   . LEU A 739  ? 0.2740 0.4029 0.2323 0.0796  0.0038  -0.0982 737  LEU A O   
5450  C CB  . LEU A 739  ? 0.2439 0.3556 0.2190 0.0819  -0.0019 -0.1121 737  LEU A CB  
5451  C CG  . LEU A 739  ? 0.2878 0.3995 0.2704 0.0851  -0.0053 -0.1227 737  LEU A CG  
5452  C CD1 . LEU A 739  ? 0.2891 0.3959 0.2763 0.0851  -0.0050 -0.1222 737  LEU A CD1 
5453  C CD2 . LEU A 739  ? 0.2774 0.4056 0.2584 0.0895  -0.0055 -0.1307 737  LEU A CD2 
5454  N N   . ILE A 740  ? 0.2624 0.3653 0.2266 0.0748  0.0016  -0.0935 738  ILE A N   
5455  C CA  . ILE A 740  ? 0.2569 0.3598 0.2156 0.0720  0.0046  -0.0837 738  ILE A CA  
5456  C C   . ILE A 740  ? 0.2427 0.3513 0.1967 0.0720  0.0045  -0.0827 738  ILE A C   
5457  O O   . ILE A 740  ? 0.2753 0.3913 0.2243 0.0714  0.0071  -0.0765 738  ILE A O   
5458  C CB  . ILE A 740  ? 0.2666 0.3545 0.2273 0.0682  0.0047  -0.0773 738  ILE A CB  
5459  C CG1 . ILE A 740  ? 0.2883 0.3767 0.2442 0.0656  0.0078  -0.0675 738  ILE A CG1 
5460  C CG2 . ILE A 740  ? 0.2974 0.3747 0.2607 0.0668  0.0018  -0.0790 738  ILE A CG2 
5461  C CD1 . ILE A 740  ? 0.2950 0.3932 0.2486 0.0665  0.0108  -0.0643 738  ILE A CD1 
5462  N N   . ALA A 741  ? 0.2730 0.3790 0.2291 0.0729  0.0015  -0.0886 739  ALA A N   
5463  C CA  . ALA A 741  ? 0.2942 0.4064 0.2462 0.0732  0.0011  -0.0886 739  ALA A CA  
5464  C C   . ALA A 741  ? 0.2680 0.3978 0.2161 0.0765  0.0024  -0.0916 739  ALA A C   
5465  O O   . ALA A 741  ? 0.2895 0.4273 0.2321 0.0761  0.0042  -0.0866 739  ALA A O   
5466  C CB  . ALA A 741  ? 0.3107 0.4166 0.2667 0.0736  -0.0027 -0.0952 739  ALA A CB  
5467  N N   . ALA A 742  ? 0.2719 0.4084 0.2229 0.0797  0.0016  -0.0995 740  ALA A N   
5468  C CA  . ALA A 742  ? 0.2618 0.4162 0.2091 0.0829  0.0030  -0.1026 740  ALA A CA  
5469  C C   . ALA A 742  ? 0.2940 0.4554 0.2365 0.0817  0.0070  -0.0936 740  ALA A C   
5470  O O   . ALA A 742  ? 0.3024 0.4774 0.2398 0.0827  0.0087  -0.0914 740  ALA A O   
5471  C CB  . ALA A 742  ? 0.2742 0.4338 0.2263 0.0866  0.0014  -0.1128 740  ALA A CB  
5472  N N   . GLU A 743  ? 0.2695 0.4220 0.2140 0.0795  0.0084  -0.0882 741  GLU A N   
5473  C CA  . GLU A 743  ? 0.3030 0.4613 0.2438 0.0780  0.0120  -0.0794 741  GLU A CA  
5474  C C   . GLU A 743  ? 0.2642 0.4209 0.2007 0.0752  0.0132  -0.0706 741  GLU A C   
5475  O O   . GLU A 743  ? 0.2814 0.4491 0.2136 0.0751  0.0156  -0.0649 741  GLU A O   
5476  C CB  . GLU A 743  ? 0.2869 0.4356 0.2315 0.0764  0.0129  -0.0765 741  GLU A CB  
5477  C CG  . GLU A 743  ? 0.3491 0.5011 0.2911 0.0744  0.0164  -0.0670 741  GLU A CG  
5478  C CD  . GLU A 743  ? 0.3030 0.4727 0.2423 0.0768  0.0187  -0.0673 741  GLU A CD  
5479  O OE1 . GLU A 743  ? 0.3085 0.4885 0.2481 0.0804  0.0177  -0.0758 741  GLU A OE1 
5480  O OE2 . GLU A 743  ? 0.3525 0.5261 0.2896 0.0751  0.0214  -0.0590 741  GLU A OE2 
5481  N N   . GLY A 744  ? 0.2874 0.4309 0.2253 0.0730  0.0114  -0.0693 742  GLY A N   
5482  C CA  . GLY A 744  ? 0.2790 0.4210 0.2133 0.0706  0.0121  -0.0619 742  GLY A CA  
5483  C C   . GLY A 744  ? 0.2666 0.4222 0.1965 0.0725  0.0119  -0.0635 742  GLY A C   
5484  O O   . GLY A 744  ? 0.2825 0.4446 0.2085 0.0715  0.0137  -0.0563 742  GLY A O   
5485  N N   . VAL A 745  ? 0.2817 0.4421 0.2126 0.0754  0.0096  -0.0730 743  VAL A N   
5486  C CA  . VAL A 745  ? 0.2748 0.4497 0.2016 0.0777  0.0093  -0.0756 743  VAL A CA  
5487  C C   . VAL A 745  ? 0.3020 0.4938 0.2252 0.0793  0.0121  -0.0732 743  VAL A C   
5488  O O   . VAL A 745  ? 0.3063 0.5092 0.2248 0.0793  0.0134  -0.0684 743  VAL A O   
5489  C CB  . VAL A 745  ? 0.2977 0.4739 0.2271 0.0806  0.0060  -0.0871 743  VAL A CB  
5490  C CG1 . VAL A 745  ? 0.3213 0.5154 0.2464 0.0836  0.0059  -0.0910 743  VAL A CG1 
5491  C CG2 . VAL A 745  ? 0.3113 0.4730 0.2433 0.0785  0.0034  -0.0878 743  VAL A CG2 
5492  N N   . ARG A 746  ? 0.2901 0.4845 0.2156 0.0807  0.0131  -0.0760 744  ARG A N   
5493  C CA  . ARG A 746  ? 0.3022 0.5129 0.2247 0.0821  0.0159  -0.0734 744  ARG A CA  
5494  C C   . ARG A 746  ? 0.2827 0.4939 0.2021 0.0790  0.0186  -0.0609 744  ARG A C   
5495  O O   . ARG A 746  ? 0.3070 0.5328 0.2222 0.0795  0.0204  -0.0566 744  ARG A O   
5496  C CB  . ARG A 746  ? 0.3101 0.5211 0.2362 0.0837  0.0165  -0.0778 744  ARG A CB  
5497  C CG  . ARG A 746  ? 0.3218 0.5512 0.2452 0.0856  0.0192  -0.0767 744  ARG A CG  
5498  C CD  . ARG A 746  ? 0.3114 0.5391 0.2385 0.0861  0.0204  -0.0779 744  ARG A CD  
5499  N NE  . ARG A 746  ? 0.3436 0.5584 0.2722 0.0823  0.0218  -0.0687 744  ARG A NE  
5500  C CZ  . ARG A 746  ? 0.3706 0.5894 0.2965 0.0800  0.0246  -0.0584 744  ARG A CZ  
5501  N NH1 . ARG A 746  ? 0.3795 0.6151 0.3008 0.0809  0.0263  -0.0550 744  ARG A NH1 
5502  N NH2 . ARG A 746  ? 0.3390 0.5449 0.2669 0.0766  0.0254  -0.0512 744  ARG A NH2 
5503  N N   . ILE A 747  ? 0.2737 0.4693 0.1956 0.0756  0.0189  -0.0550 745  ILE A N   
5504  C CA  . ILE A 747  ? 0.2878 0.4823 0.2079 0.0726  0.0211  -0.0434 745  ILE A CA  
5505  C C   . ILE A 747  ? 0.2995 0.4977 0.2160 0.0717  0.0206  -0.0391 745  ILE A C   
5506  O O   . ILE A 747  ? 0.2793 0.4872 0.1929 0.0709  0.0225  -0.0313 745  ILE A O   
5507  C CB  . ILE A 747  ? 0.2666 0.4431 0.1905 0.0694  0.0211  -0.0393 745  ILE A CB  
5508  C CG1 . ILE A 747  ? 0.2920 0.4680 0.2190 0.0701  0.0222  -0.0414 745  ILE A CG1 
5509  C CG2 . ILE A 747  ? 0.3011 0.4739 0.2239 0.0661  0.0225  -0.0282 745  ILE A CG2 
5510  C CD1 . ILE A 747  ? 0.2988 0.4572 0.2301 0.0677  0.0216  -0.0402 745  ILE A CD1 
5511  N N   . LEU A 748  ? 0.2822 0.4728 0.1991 0.0718  0.0181  -0.0436 746  LEU A N   
5512  C CA  . LEU A 748  ? 0.2721 0.4661 0.1858 0.0711  0.0174  -0.0399 746  LEU A CA  
5513  C C   . LEU A 748  ? 0.2794 0.4932 0.1887 0.0738  0.0180  -0.0416 746  LEU A C   
5514  O O   . LEU A 748  ? 0.2709 0.4929 0.1769 0.0730  0.0190  -0.0344 746  LEU A O   
5515  C CB  . LEU A 748  ? 0.2640 0.4467 0.1793 0.0709  0.0145  -0.0455 746  LEU A CB  
5516  C CG  . LEU A 748  ? 0.3099 0.4747 0.2281 0.0675  0.0140  -0.0407 746  LEU A CG  
5517  C CD1 . LEU A 748  ? 0.3455 0.4992 0.2667 0.0677  0.0111  -0.0481 746  LEU A CD1 
5518  C CD2 . LEU A 748  ? 0.3179 0.4831 0.2338 0.0654  0.0147  -0.0318 746  LEU A CD2 
5519  N N   . ARG A 749  ? 0.2409 0.4633 0.1504 0.0772  0.0173  -0.0511 747  ARG A N   
5520  C CA  . ARG A 749  ? 0.2726 0.5153 0.1779 0.0800  0.0179  -0.0533 747  ARG A CA  
5521  C C   . ARG A 749  ? 0.2840 0.5374 0.1883 0.0789  0.0208  -0.0445 747  ARG A C   
5522  O O   . ARG A 749  ? 0.3127 0.5778 0.2153 0.0784  0.0211  -0.0391 747  ARG A O   
5523  C CB  . ARG A 749  ? 0.3042 0.5504 0.2132 0.0829  0.0156  -0.0649 747  ARG A CB  
5524  C CG  . ARG A 749  ? 0.3636 0.6036 0.2740 0.0840  0.0122  -0.0730 747  ARG A CG  
5525  C CD  . ARG A 749  ? 0.4534 0.6977 0.3686 0.0868  0.0097  -0.0840 747  ARG A CD  
5526  N NE  . ARG A 749  ? 0.3675 0.6079 0.2845 0.0878  0.0062  -0.0914 747  ARG A NE  
5527  C CZ  . ARG A 749  ? 0.4084 0.6547 0.3295 0.0902  0.0035  -0.1004 747  ARG A CZ  
5528  N NH1 . ARG A 749  ? 0.3779 0.6344 0.3015 0.0919  0.0038  -0.1036 747  ARG A NH1 
5529  N NH2 . ARG A 749  ? 0.4291 0.6715 0.3523 0.0908  0.0003  -0.1065 747  ARG A NH2 
5530  N N   . GLU A 750  ? 0.2699 0.5190 0.1759 0.0783  0.0228  -0.0426 748  GLU A N   
5531  C CA  . GLU A 750  ? 0.3057 0.5639 0.2111 0.0770  0.0256  -0.0336 748  GLU A CA  
5532  C C   . GLU A 750  ? 0.3176 0.5744 0.2209 0.0740  0.0267  -0.0219 748  GLU A C   
5533  O O   . GLU A 750  ? 0.3009 0.5694 0.2034 0.0730  0.0279  -0.0144 748  GLU A O   
5534  C CB  . GLU A 750  ? 0.2903 0.5417 0.1990 0.0764  0.0271  -0.0334 748  GLU A CB  
5535  C CG  . GLU A 750  ? 0.3299 0.5915 0.2381 0.0752  0.0301  -0.0246 748  GLU A CG  
5536  C CD  . GLU A 750  ? 0.3643 0.6180 0.2763 0.0743  0.0314  -0.0238 748  GLU A CD  
5537  O OE1 . GLU A 750  ? 0.4838 0.7273 0.3989 0.0754  0.0300  -0.0317 748  GLU A OE1 
5538  O OE2 . GLU A 750  ? 0.3742 0.6313 0.2866 0.0723  0.0337  -0.0148 748  GLU A OE2 
5539  N N   . ALA A 751  ? 0.2866 0.5264 0.1920 0.0716  0.0252  -0.0198 749  ALA A N   
5540  C CA  . ALA A 751  ? 0.2879 0.5235 0.1929 0.0685  0.0256  -0.0091 749  ALA A CA  
5541  C C   . ALA A 751  ? 0.3108 0.5577 0.2118 0.0692  0.0248  -0.0074 749  ALA A C   
5542  O O   . ALA A 751  ? 0.3391 0.5850 0.2397 0.0669  0.0250  0.0018  749  ALA A O   
5543  C CB  . ALA A 751  ? 0.2567 0.4714 0.1652 0.0660  0.0240  -0.0087 749  ALA A CB  
5544  N N   . GLY A 752  ? 0.2868 0.5441 0.1850 0.0725  0.0236  -0.0161 750  GLY A N   
5545  C CA  . GLY A 752  ? 0.3187 0.5864 0.2151 0.0729  0.0223  -0.0147 750  GLY A CA  
5546  C C   . GLY A 752  ? 0.3188 0.5816 0.2141 0.0743  0.0195  -0.0226 750  GLY A C   
5547  O O   . GLY A 752  ? 0.3191 0.5901 0.2133 0.0746  0.0182  -0.0218 750  GLY A O   
5548  N N   . ILE A 753  ? 0.2956 0.5448 0.1925 0.0747  0.0183  -0.0298 751  ILE A N   
5549  C CA  . ILE A 753  ? 0.3024 0.5473 0.1993 0.0760  0.0153  -0.0377 751  ILE A CA  
5550  C C   . ILE A 753  ? 0.2941 0.5514 0.1919 0.0790  0.0139  -0.0466 751  ILE A C   
5551  O O   . ILE A 753  ? 0.3013 0.5596 0.2019 0.0805  0.0140  -0.0525 751  ILE A O   
5552  C CB  . ILE A 753  ? 0.2597 0.4847 0.1613 0.0748  0.0136  -0.0424 751  ILE A CB  
5553  C CG1 . ILE A 753  ? 0.2567 0.4667 0.1607 0.0710  0.0144  -0.0333 751  ILE A CG1 
5554  C CG2 . ILE A 753  ? 0.3138 0.5353 0.2158 0.0760  0.0105  -0.0502 751  ILE A CG2 
5555  C CD1 . ILE A 753  ? 0.2606 0.4686 0.1629 0.0692  0.0137  -0.0269 751  ILE A CD1 
5556  N N   . PRO A 754  ? 0.3193 0.5854 0.2163 0.0798  0.0121  -0.0479 752  PRO A N   
5557  C CA  . PRO A 754  ? 0.3283 0.6060 0.2276 0.0825  0.0104  -0.0563 752  PRO A CA  
5558  C C   . PRO A 754  ? 0.2957 0.5646 0.1985 0.0843  0.0080  -0.0681 752  PRO A C   
5559  O O   . PRO A 754  ? 0.2971 0.5522 0.2001 0.0836  0.0068  -0.0705 752  PRO A O   
5560  C CB  . PRO A 754  ? 0.3947 0.6809 0.2922 0.0826  0.0090  -0.0546 752  PRO A CB  
5561  C CG  . PRO A 754  ? 0.3195 0.6017 0.2138 0.0798  0.0105  -0.0434 752  PRO A CG  
5562  C CD  . PRO A 754  ? 0.2820 0.5481 0.1762 0.0784  0.0116  -0.0418 752  PRO A CD  
5563  N N   . ALA A 755  ? 0.3109 0.5884 0.2169 0.0867  0.0071  -0.0754 753  ALA A N   
5564  C CA  . ALA A 755  ? 0.3157 0.5862 0.2264 0.0886  0.0043  -0.0868 753  ALA A CA  
5565  C C   . ALA A 755  ? 0.2968 0.5625 0.2082 0.0890  0.0013  -0.0919 753  ALA A C   
5566  O O   . ALA A 755  ? 0.3415 0.5949 0.2562 0.0892  -0.0008 -0.0984 753  ALA A O   
5567  C CB  . ALA A 755  ? 0.3673 0.6506 0.2814 0.0912  0.0036  -0.0933 753  ALA A CB  
5568  N N   . SER A 756  ? 0.3040 0.5794 0.2128 0.0890  0.0008  -0.0891 754  SER A N   
5569  C CA  . SER A 756  ? 0.3178 0.5892 0.2272 0.0893  -0.0021 -0.0937 754  SER A CA  
5570  C C   . SER A 756  ? 0.3117 0.5676 0.2190 0.0869  -0.0020 -0.0897 754  SER A C   
5571  O O   . SER A 756  ? 0.3395 0.5874 0.2487 0.0871  -0.0047 -0.0952 754  SER A O   
5572  C CB  . SER A 756  ? 0.3406 0.6269 0.2477 0.0899  -0.0024 -0.0910 754  SER A CB  
5573  O OG  . SER A 756  ? 0.3526 0.6420 0.2549 0.0877  0.0002  -0.0795 754  SER A OG  
5574  N N   . ALA A 757  ? 0.3112 0.5629 0.2149 0.0848  0.0009  -0.0803 755  ALA A N   
5575  C CA  . ALA A 757  ? 0.2700 0.5078 0.1716 0.0827  0.0012  -0.0760 755  ALA A CA  
5576  C C   . ALA A 757  ? 0.3255 0.5481 0.2300 0.0822  0.0010  -0.0797 755  ALA A C   
5577  O O   . ALA A 757  ? 0.3080 0.5154 0.2151 0.0797  -0.0001 -0.0773 755  ALA A O   
5578  C CB  . ALA A 757  ? 0.3111 0.5513 0.2082 0.0805  0.0041  -0.0637 755  ALA A CB  
5579  N N   . LEU A 758  ? 0.2795 0.5035 0.1869 0.0835  0.0016  -0.0840 756  LEU A N   
5580  C CA  . LEU A 758  ? 0.2805 0.4893 0.1926 0.0825  0.0013  -0.0862 756  LEU A CA  
5581  C C   . LEU A 758  ? 0.3086 0.5211 0.2247 0.0855  -0.0003 -0.0968 756  LEU A C   
5582  O O   . LEU A 758  ? 0.3297 0.5514 0.2466 0.0865  0.0011  -0.0966 756  LEU A O   
5583  C CB  . LEU A 758  ? 0.2763 0.4803 0.1881 0.0800  0.0044  -0.0767 756  LEU A CB  
5584  C CG  . LEU A 758  ? 0.2915 0.4800 0.2087 0.0786  0.0041  -0.0780 756  LEU A CG  
5585  C CD1 . LEU A 758  ? 0.2926 0.4651 0.2135 0.0768  0.0015  -0.0800 756  LEU A CD1 
5586  C CD2 . LEU A 758  ? 0.3094 0.4939 0.2261 0.0761  0.0072  -0.0682 756  LEU A CD2 
5587  N N   . GLN A 759  ? 0.2781 0.4823 0.1988 0.0862  -0.0036 -0.1049 757  GLN A N   
5588  C CA  . GLN A 759  ? 0.3054 0.5101 0.2328 0.0883  -0.0061 -0.1144 757  GLN A CA  
5589  C C   . GLN A 759  ? 0.3218 0.5105 0.2537 0.0876  -0.0070 -0.1175 757  GLN A C   
5590  O O   . GLN A 759  ? 0.3454 0.5209 0.2788 0.0853  -0.0083 -0.1155 757  GLN A O   
5591  C CB  . GLN A 759  ? 0.2868 0.4959 0.2174 0.0897  -0.0097 -0.1215 757  GLN A CB  
5592  C CG  . GLN A 759  ? 0.2925 0.5186 0.2197 0.0907  -0.0091 -0.1196 757  GLN A CG  
5593  C CD  . GLN A 759  ? 0.3005 0.5304 0.2308 0.0921  -0.0127 -0.1266 757  GLN A CD  
5594  O OE1 . GLN A 759  ? 0.3038 0.5402 0.2391 0.0944  -0.0148 -0.1343 757  GLN A OE1 
5595  N NE2 . GLN A 759  ? 0.3091 0.5351 0.2367 0.0908  -0.0135 -0.1241 757  GLN A NE2 
5596  N N   . LEU A 760  ? 0.3077 0.4965 0.2435 0.0886  -0.0067 -0.1204 758  LEU A N   
5597  C CA  . LEU A 760  ? 0.2973 0.4717 0.2383 0.0881  -0.0077 -0.1233 758  LEU A CA  
5598  C C   . LEU A 760  ? 0.2914 0.4629 0.2405 0.0897  -0.0120 -0.1333 758  LEU A C   
5599  O O   . LEU A 760  ? 0.2997 0.4816 0.2517 0.0918  -0.0131 -0.1383 758  LEU A O   
5600  C CB  . LEU A 760  ? 0.2847 0.4604 0.2260 0.0883  -0.0050 -0.1206 758  LEU A CB  
5601  C CG  . LEU A 760  ? 0.2990 0.4592 0.2473 0.0869  -0.0063 -0.1218 758  LEU A CG  
5602  C CD1 . LEU A 760  ? 0.3000 0.4450 0.2481 0.0824  -0.0054 -0.1123 758  LEU A CD1 
5603  C CD2 . LEU A 760  ? 0.3253 0.4904 0.2750 0.0886  -0.0046 -0.1232 758  LEU A CD2 
5604  N N   . LEU A 761  ? 0.2928 0.4502 0.2461 0.0885  -0.0146 -0.1360 759  LEU A N   
5605  C CA  A LEU A 761  ? 0.3110 0.4642 0.2731 0.0895  -0.0191 -0.1447 759  LEU A CA  
5606  C CA  B LEU A 761  ? 0.3110 0.4642 0.2731 0.0895  -0.0191 -0.1447 759  LEU A CA  
5607  C C   . LEU A 761  ? 0.2976 0.4357 0.2660 0.0885  -0.0204 -0.1461 759  LEU A C   
5608  O O   . LEU A 761  ? 0.3054 0.4307 0.2764 0.0862  -0.0221 -0.1447 759  LEU A O   
5609  C CB  A LEU A 761  ? 0.3106 0.4625 0.2728 0.0890  -0.0217 -0.1466 759  LEU A CB  
5610  C CB  B LEU A 761  ? 0.3107 0.4621 0.2731 0.0889  -0.0218 -0.1466 759  LEU A CB  
5611  C CG  A LEU A 761  ? 0.3036 0.4705 0.2594 0.0899  -0.0204 -0.1444 759  LEU A CG  
5612  C CG  B LEU A 761  ? 0.2977 0.4629 0.2548 0.0898  -0.0212 -0.1456 759  LEU A CG  
5613  C CD1 A LEU A 761  ? 0.2819 0.4463 0.2363 0.0888  -0.0222 -0.1443 759  LEU A CD1 
5614  C CD1 B LEU A 761  ? 0.3007 0.4814 0.2585 0.0924  -0.0209 -0.1490 759  LEU A CD1 
5615  C CD2 A LEU A 761  ? 0.3015 0.4819 0.2608 0.0926  -0.0217 -0.1506 759  LEU A CD2 
5616  C CD2 B LEU A 761  ? 0.3101 0.4769 0.2579 0.0881  -0.0176 -0.1364 759  LEU A CD2 
5617  N N   . PRO A 762  ? 0.2804 0.4194 0.2521 0.0896  -0.0198 -0.1478 760  PRO A N   
5618  C CA  . PRO A 762  ? 0.3097 0.4348 0.2881 0.0887  -0.0214 -0.1491 760  PRO A CA  
5619  C C   . PRO A 762  ? 0.3417 0.4598 0.3295 0.0888  -0.0265 -0.1560 760  PRO A C   
5620  O O   . PRO A 762  ? 0.3458 0.4717 0.3363 0.0903  -0.0289 -0.1614 760  PRO A O   
5621  C CB  . PRO A 762  ? 0.3030 0.4339 0.2831 0.0904  -0.0199 -0.1502 760  PRO A CB  
5622  C CG  . PRO A 762  ? 0.3161 0.4628 0.2885 0.0914  -0.0165 -0.1469 760  PRO A CG  
5623  C CD  . PRO A 762  ? 0.2714 0.4246 0.2412 0.0916  -0.0178 -0.1482 760  PRO A CD  
5624  N N   . GLY A 763  ? 0.3080 0.4114 0.3012 0.0871  -0.0282 -0.1556 761  GLY A N   
5625  C CA  . GLY A 763  ? 0.3388 0.4344 0.3421 0.0867  -0.0331 -0.1612 761  GLY A CA  
5626  C C   . GLY A 763  ? 0.3293 0.4094 0.3347 0.0835  -0.0343 -0.1571 761  GLY A C   
5627  O O   . GLY A 763  ? 0.3209 0.3960 0.3213 0.0802  -0.0312 -0.1473 761  GLY A O   
5628  N N   . ASP A 764  ? 0.3572 0.4299 0.3714 0.0830  -0.0388 -0.1617 762  ASP A N   
5629  C CA  . ASP A 764  ? 0.3581 0.4160 0.3766 0.0792  -0.0404 -0.1568 762  ASP A CA  
5630  C C   . ASP A 764  ? 0.3382 0.3948 0.3535 0.0772  -0.0409 -0.1542 762  ASP A C   
5631  O O   . ASP A 764  ? 0.3181 0.3848 0.3261 0.0784  -0.0391 -0.1542 762  ASP A O   
5632  C CB  . ASP A 764  ? 0.4085 0.4580 0.4392 0.0795  -0.0450 -0.1624 762  ASP A CB  
5633  C CG  . ASP A 764  ? 0.4114 0.4662 0.4492 0.0810  -0.0491 -0.1695 762  ASP A CG  
5634  O OD1 . ASP A 764  ? 0.4410 0.5022 0.4750 0.0815  -0.0492 -0.1710 762  ASP A OD1 
5635  O OD2 . ASP A 764  ? 0.5582 0.6111 0.6057 0.0817  -0.0523 -0.1736 762  ASP A OD2 
5636  N N   . GLY A 765  ? 0.3107 0.3555 0.3317 0.0741  -0.0435 -0.1517 763  GLY A N   
5637  C CA  . GLY A 765  ? 0.3261 0.3688 0.3448 0.0719  -0.0441 -0.1489 763  GLY A CA  
5638  C C   . GLY A 765  ? 0.3482 0.3997 0.3677 0.0747  -0.0467 -0.1574 763  GLY A C   
5639  O O   . GLY A 765  ? 0.3644 0.4189 0.3787 0.0738  -0.0459 -0.1550 763  GLY A O   
5640  N N   . ARG A 766  ? 0.3423 0.3983 0.3685 0.0778  -0.0497 -0.1663 764  ARG A N   
5641  C CA  . ARG A 766  ? 0.3775 0.4432 0.4053 0.0797  -0.0518 -0.1720 764  ARG A CA  
5642  C C   . ARG A 766  ? 0.3614 0.4408 0.3783 0.0816  -0.0482 -0.1709 764  ARG A C   
5643  O O   . ARG A 766  ? 0.3492 0.4349 0.3638 0.0821  -0.0489 -0.1726 764  ARG A O   
5644  C CB  . ARG A 766  ? 0.4573 0.5270 0.4945 0.0820  -0.0548 -0.1787 764  ARG A CB  
5645  C CG  . ARG A 766  ? 0.5365 0.5951 0.5863 0.0805  -0.0595 -0.1808 764  ARG A CG  
5646  C CD  . ARG A 766  ? 0.4554 0.5196 0.5135 0.0832  -0.0620 -0.1874 764  ARG A CD  
5647  N NE  . ARG A 766  ? 0.4782 0.5441 0.5340 0.0842  -0.0593 -0.1860 764  ARG A NE  
5648  C CZ  . ARG A 766  ? 0.4999 0.5764 0.5567 0.0873  -0.0590 -0.1906 764  ARG A CZ  
5649  N NH1 . ARG A 766  ? 0.5713 0.6584 0.6307 0.0898  -0.0611 -0.1971 764  ARG A NH1 
5650  N NH2 . ARG A 766  ? 0.5297 0.6063 0.5849 0.0879  -0.0567 -0.1888 764  ARG A NH2 
5651  N N   . VAL A 767  ? 0.3291 0.4137 0.3399 0.0826  -0.0443 -0.1681 765  VAL A N   
5652  C CA  . VAL A 767  ? 0.3349 0.4328 0.3355 0.0841  -0.0407 -0.1659 765  VAL A CA  
5653  C C   . VAL A 767  ? 0.3182 0.4131 0.3107 0.0821  -0.0386 -0.1598 765  VAL A C   
5654  O O   . VAL A 767  ? 0.3285 0.4324 0.3154 0.0827  -0.0378 -0.1592 765  VAL A O   
5655  C CB  . VAL A 767  ? 0.3250 0.4291 0.3219 0.0856  -0.0373 -0.1640 765  VAL A CB  
5656  C CG1 . VAL A 767  ? 0.3419 0.4606 0.3290 0.0869  -0.0337 -0.1612 765  VAL A CG1 
5657  C CG2 . VAL A 767  ? 0.3506 0.4572 0.3562 0.0876  -0.0397 -0.1704 765  VAL A CG2 
5658  N N   . GLY A 768  ? 0.3070 0.3892 0.3005 0.0782  -0.0375 -0.1515 766  GLY A N   
5659  C CA  . GLY A 768  ? 0.2896 0.3677 0.2779 0.0749  -0.0356 -0.1428 766  GLY A CA  
5660  C C   . GLY A 768  ? 0.3081 0.3856 0.2985 0.0745  -0.0387 -0.1461 766  GLY A C   
5661  O O   . GLY A 768  ? 0.3098 0.3928 0.2940 0.0741  -0.0374 -0.1431 766  GLY A O   
5662  N N   . ALA A 769  ? 0.3261 0.3970 0.3257 0.0746  -0.0431 -0.1525 767  ALA A N   
5663  C CA  . ALA A 769  ? 0.3179 0.3873 0.3207 0.0740  -0.0464 -0.1556 767  ALA A CA  
5664  C C   . ALA A 769  ? 0.3130 0.3965 0.3123 0.0776  -0.0472 -0.1628 767  ALA A C   
5665  O O   . ALA A 769  ? 0.3435 0.4298 0.3398 0.0769  -0.0477 -0.1617 767  ALA A O   
5666  C CB  . ALA A 769  ? 0.3138 0.3733 0.3283 0.0733  -0.0511 -0.1609 767  ALA A CB  
5667  N N   . ALA A 770  ? 0.3374 0.4302 0.3381 0.0805  -0.0472 -0.1676 768  ALA A N   
5668  C CA  . ALA A 770  ? 0.3448 0.4521 0.3435 0.0830  -0.0475 -0.1714 768  ALA A CA  
5669  C C   . ALA A 770  ? 0.3494 0.4655 0.3364 0.0831  -0.0436 -0.1659 768  ALA A C   
5670  O O   . ALA A 770  ? 0.3360 0.4603 0.3203 0.0839  -0.0442 -0.1669 768  ALA A O   
5671  C CB  . ALA A 770  ? 0.3382 0.4539 0.3408 0.0859  -0.0478 -0.1763 768  ALA A CB  
5672  N N   . LEU A 771  ? 0.3256 0.4401 0.3059 0.0824  -0.0397 -0.1596 769  LEU A N   
5673  C CA  . LEU A 771  ? 0.3571 0.4790 0.3270 0.0820  -0.0360 -0.1528 769  LEU A CA  
5674  C C   . LEU A 771  ? 0.3325 0.4475 0.3011 0.0788  -0.0364 -0.1470 769  LEU A C   
5675  O O   . LEU A 771  ? 0.3389 0.4624 0.3019 0.0793  -0.0357 -0.1454 769  LEU A O   
5676  C CB  . LEU A 771  ? 0.3066 0.4263 0.2726 0.0807  -0.0318 -0.1447 769  LEU A CB  
5677  C CG  . LEU A 771  ? 0.2998 0.4288 0.2654 0.0839  -0.0306 -0.1493 769  LEU A CG  
5678  C CD1 . LEU A 771  ? 0.3210 0.4458 0.2840 0.0821  -0.0268 -0.1408 769  LEU A CD1 
5679  C CD2 . LEU A 771  ? 0.3187 0.4647 0.2800 0.0861  -0.0297 -0.1503 769  LEU A CD2 
5680  N N   . VAL A 772  ? 0.2898 0.3902 0.2638 0.0756  -0.0375 -0.1437 770  VAL A N   
5681  C CA  . VAL A 772  ? 0.2916 0.3850 0.2649 0.0725  -0.0379 -0.1383 770  VAL A CA  
5682  C C   . VAL A 772  ? 0.3150 0.4138 0.2902 0.0739  -0.0414 -0.1451 770  VAL A C   
5683  O O   . VAL A 772  ? 0.3749 0.4760 0.3459 0.0728  -0.0409 -0.1414 770  VAL A O   
5684  C CB  . VAL A 772  ? 0.3130 0.3907 0.2926 0.0689  -0.0388 -0.1346 770  VAL A CB  
5685  C CG1 . VAL A 772  ? 0.3259 0.3972 0.3062 0.0660  -0.0399 -0.1307 770  VAL A CG1 
5686  C CG2 . VAL A 772  ? 0.3127 0.3857 0.2891 0.0672  -0.0350 -0.1265 770  VAL A CG2 
5687  N N   . ALA A 773  ? 0.3388 0.4394 0.3205 0.0763  -0.0450 -0.1552 771  ALA A N   
5688  C CA  . ALA A 773  ? 0.3303 0.4348 0.3153 0.0776  -0.0489 -0.1626 771  ALA A CA  
5689  C C   . ALA A 773  ? 0.4066 0.5273 0.3863 0.0803  -0.0479 -0.1643 771  ALA A C   
5690  O O   . ALA A 773  ? 0.4169 0.5417 0.3987 0.0807  -0.0504 -0.1675 771  ALA A O   
5691  C CB  . ALA A 773  ? 0.3565 0.4560 0.3532 0.0782  -0.0530 -0.1697 771  ALA A CB  
5692  N N   . ALA A 774  ? 0.3634 0.4935 0.3368 0.0819  -0.0445 -0.1616 772  ALA A N   
5693  C CA  . ALA A 774  ? 0.3802 0.5264 0.3496 0.0843  -0.0436 -0.1627 772  ALA A CA  
5694  C C   . ALA A 774  ? 0.3511 0.5016 0.3134 0.0834  -0.0427 -0.1583 772  ALA A C   
5695  O O   . ALA A 774  ? 0.3880 0.5333 0.3444 0.0814  -0.0406 -0.1516 772  ALA A O   
5696  C CB  . ALA A 774  ? 0.3720 0.5269 0.3365 0.0857  -0.0399 -0.1598 772  ALA A CB  
5697  N N   . ALA A 775  ? 0.4338 0.5946 0.3972 0.0850  -0.0445 -0.1621 773  ALA A N   
5698  C CA  . ALA A 775  ? 0.4628 0.6266 0.4212 0.0841  -0.0445 -0.1588 773  ALA A CA  
5699  C C   . ALA A 775  ? 0.3597 0.5301 0.3077 0.0837  -0.0404 -0.1501 773  ALA A C   
5700  O O   . ALA A 775  ? 0.3952 0.5629 0.3385 0.0820  -0.0399 -0.1450 773  ALA A O   
5701  C CB  . ALA A 775  ? 0.4190 0.5934 0.3807 0.0862  -0.0471 -0.1648 773  ALA A CB  
5702  N N   . GLU A 776  ? 0.3534 0.5324 0.2982 0.0851  -0.0376 -0.1479 774  GLU A N   
5703  C CA  . GLU A 776  ? 0.3135 0.4994 0.2491 0.0846  -0.0337 -0.1392 774  GLU A CA  
5704  C C   . GLU A 776  ? 0.3302 0.5055 0.2622 0.0825  -0.0312 -0.1326 774  GLU A C   
5705  O O   . GLU A 776  ? 0.3610 0.5399 0.2870 0.0814  -0.0280 -0.1236 774  GLU A O   
5706  C CB  . GLU A 776  ? 0.3664 0.5675 0.3002 0.0869  -0.0318 -0.1391 774  GLU A CB  
5707  C CG  . GLU A 776  ? 0.4114 0.6247 0.3485 0.0892  -0.0341 -0.1455 774  GLU A CG  
5708  C CD  . GLU A 776  ? 0.5061 0.7178 0.4521 0.0910  -0.0370 -0.1553 774  GLU A CD  
5709  O OE1 . GLU A 776  ? 0.4160 0.6158 0.3663 0.0902  -0.0377 -0.1572 774  GLU A OE1 
5710  O OE2 . GLU A 776  ? 0.5638 0.7865 0.5129 0.0933  -0.0388 -0.1610 774  GLU A OE2 
5711  N N   . THR A 777  ? 0.3119 0.4730 0.2501 0.0809  -0.0323 -0.1342 775  THR A N   
5712  C CA  . THR A 777  ? 0.3078 0.4568 0.2463 0.0776  -0.0296 -0.1252 775  THR A CA  
5713  C C   . THR A 777  ? 0.3198 0.4624 0.2563 0.0746  -0.0290 -0.1172 775  THR A C   
5714  O O   . THR A 777  ? 0.3484 0.4853 0.2884 0.0735  -0.0317 -0.1197 775  THR A O   
5715  C CB  . THR A 777  ? 0.2922 0.4282 0.2384 0.0766  -0.0314 -0.1291 775  THR A CB  
5716  O OG1 . THR A 777  ? 0.3092 0.4511 0.2567 0.0794  -0.0312 -0.1350 775  THR A OG1 
5717  C CG2 . THR A 777  ? 0.3039 0.4264 0.2508 0.0729  -0.0291 -0.1199 775  THR A CG2 
5718  N N   . ALA A 778  ? 0.2909 0.4350 0.2222 0.0732  -0.0256 -0.1077 776  ALA A N   
5719  C CA  . ALA A 778  ? 0.2698 0.4102 0.1988 0.0707  -0.0248 -0.1000 776  ALA A CA  
5720  C C   . ALA A 778  ? 0.2956 0.4213 0.2270 0.0673  -0.0233 -0.0930 776  ALA A C   
5721  O O   . ALA A 778  ? 0.2987 0.4194 0.2295 0.0651  -0.0230 -0.0873 776  ALA A O   
5722  C CB  . ALA A 778  ? 0.2959 0.4491 0.2178 0.0716  -0.0224 -0.0939 776  ALA A CB  
5723  N N   . GLY A 779  ? 0.2703 0.3895 0.2044 0.0668  -0.0224 -0.0934 777  GLY A N   
5724  C CA  . GLY A 779  ? 0.2487 0.3546 0.1850 0.0636  -0.0210 -0.0872 777  GLY A CA  
5725  C C   . GLY A 779  ? 0.2510 0.3514 0.1912 0.0638  -0.0209 -0.0902 777  GLY A C   
5726  O O   . GLY A 779  ? 0.2627 0.3710 0.2022 0.0664  -0.0207 -0.0949 777  GLY A O   
5727  N N   . VAL A 780  ? 0.2526 0.3399 0.1968 0.0611  -0.0210 -0.0878 778  VAL A N   
5728  C CA  . VAL A 780  ? 0.2505 0.3313 0.1991 0.0609  -0.0212 -0.0903 778  VAL A CA  
5729  C C   . VAL A 780  ? 0.2324 0.3042 0.1805 0.0581  -0.0186 -0.0822 778  VAL A C   
5730  O O   . VAL A 780  ? 0.2447 0.3094 0.1933 0.0555  -0.0184 -0.0775 778  VAL A O   
5731  C CB  . VAL A 780  ? 0.2628 0.3364 0.2186 0.0606  -0.0249 -0.0970 778  VAL A CB  
5732  C CG1 . VAL A 780  ? 0.2696 0.3362 0.2301 0.0603  -0.0252 -0.0989 778  VAL A CG1 
5733  C CG2 . VAL A 780  ? 0.2682 0.3510 0.2247 0.0637  -0.0277 -0.1058 778  VAL A CG2 
5734  N N   . MET A 781  ? 0.2375 0.3103 0.1848 0.0586  -0.0165 -0.0806 779  MET A N   
5735  C CA  . MET A 781  ? 0.2198 0.2840 0.1674 0.0560  -0.0143 -0.0739 779  MET A CA  
5736  C C   . MET A 781  ? 0.2552 0.3127 0.2081 0.0560  -0.0155 -0.0779 779  MET A C   
5737  O O   . MET A 781  ? 0.2427 0.3057 0.1960 0.0583  -0.0154 -0.0821 779  MET A O   
5738  C CB  . MET A 781  ? 0.2657 0.3365 0.2082 0.0565  -0.0109 -0.0682 779  MET A CB  
5739  C CG  . MET A 781  ? 0.2469 0.3254 0.1846 0.0568  -0.0100 -0.0641 779  MET A CG  
5740  S SD  . MET A 781  ? 0.2696 0.3574 0.2022 0.0575  -0.0065 -0.0577 779  MET A SD  
5741  C CE  . MET A 781  ? 0.2635 0.3392 0.1975 0.0541  -0.0044 -0.0494 779  MET A CE  
5742  N N   . PHE A 782  ? 0.2666 0.3129 0.2238 0.0534  -0.0166 -0.0767 780  PHE A N   
5743  C CA  . PHE A 782  ? 0.2643 0.3033 0.2273 0.0530  -0.0182 -0.0799 780  PHE A CA  
5744  C C   . PHE A 782  ? 0.2607 0.2909 0.2242 0.0502  -0.0163 -0.0733 780  PHE A C   
5745  O O   . PHE A 782  ? 0.2418 0.2668 0.2045 0.0477  -0.0157 -0.0683 780  PHE A O   
5746  C CB  . PHE A 782  ? 0.2635 0.2971 0.2324 0.0523  -0.0219 -0.0845 780  PHE A CB  
5747  C CG  . PHE A 782  ? 0.2658 0.2912 0.2415 0.0514  -0.0238 -0.0870 780  PHE A CG  
5748  C CD1 . PHE A 782  ? 0.2488 0.2774 0.2279 0.0540  -0.0253 -0.0936 780  PHE A CD1 
5749  C CD2 . PHE A 782  ? 0.2614 0.2766 0.2401 0.0482  -0.0240 -0.0825 780  PHE A CD2 
5750  C CE1 . PHE A 782  ? 0.2705 0.2915 0.2564 0.0533  -0.0273 -0.0957 780  PHE A CE1 
5751  C CE2 . PHE A 782  ? 0.2713 0.2795 0.2565 0.0473  -0.0259 -0.0843 780  PHE A CE2 
5752  C CZ  . PHE A 782  ? 0.2467 0.2575 0.2357 0.0499  -0.0276 -0.0908 780  PHE A CZ  
5753  N N   . THR A 783  ? 0.2239 0.2526 0.1891 0.0507  -0.0155 -0.0738 781  THR A N   
5754  C CA  . THR A 783  ? 0.2393 0.2588 0.2066 0.0480  -0.0146 -0.0691 781  THR A CA  
5755  C C   . THR A 783  ? 0.2498 0.2647 0.2234 0.0485  -0.0169 -0.0739 781  THR A C   
5756  O O   . THR A 783  ? 0.2521 0.2722 0.2266 0.0511  -0.0174 -0.0789 781  THR A O   
5757  C CB  . THR A 783  ? 0.2690 0.2906 0.2318 0.0478  -0.0110 -0.0634 781  THR A CB  
5758  O OG1 . THR A 783  ? 0.2586 0.2847 0.2164 0.0475  -0.0093 -0.0591 781  THR A OG1 
5759  C CG2 . THR A 783  ? 0.2576 0.2698 0.2225 0.0450  -0.0102 -0.0586 781  THR A CG2 
5760  N N   . GLY A 784  ? 0.2496 0.2552 0.2279 0.0459  -0.0186 -0.0725 782  GLY A N   
5761  C CA  . GLY A 784  ? 0.2519 0.2528 0.2372 0.0462  -0.0214 -0.0770 782  GLY A CA  
5762  C C   . GLY A 784  ? 0.2301 0.2219 0.2202 0.0430  -0.0234 -0.0747 782  GLY A C   
5763  O O   . GLY A 784  ? 0.2541 0.2428 0.2415 0.0405  -0.0219 -0.0691 782  GLY A O   
5764  N N   . SER A 785  ? 0.2529 0.2408 0.2503 0.0431  -0.0268 -0.0792 783  SER A N   
5765  C CA  . SER A 785  ? 0.2687 0.2482 0.2714 0.0400  -0.0289 -0.0767 783  SER A CA  
5766  C C   . SER A 785  ? 0.2781 0.2581 0.2806 0.0389  -0.0302 -0.0768 783  SER A C   
5767  O O   . SER A 785  ? 0.2738 0.2599 0.2745 0.0411  -0.0309 -0.0812 783  SER A O   
5768  C CB  . SER A 785  ? 0.3190 0.2942 0.3305 0.0404  -0.0326 -0.0812 783  SER A CB  
5769  O OG  . SER A 785  ? 0.3054 0.2847 0.3202 0.0430  -0.0354 -0.0888 783  SER A OG  
5770  N N   . THR A 786  ? 0.2734 0.2472 0.2775 0.0356  -0.0304 -0.0719 784  THR A N   
5771  C CA  . THR A 786  ? 0.2896 0.2633 0.2942 0.0343  -0.0317 -0.0717 784  THR A CA  
5772  C C   . THR A 786  ? 0.2701 0.2442 0.2815 0.0354  -0.0359 -0.0785 784  THR A C   
5773  O O   . THR A 786  ? 0.2685 0.2465 0.2787 0.0363  -0.0369 -0.0812 784  THR A O   
5774  C CB  . THR A 786  ? 0.2821 0.2494 0.2883 0.0304  -0.0314 -0.0654 784  THR A CB  
5775  O OG1 . THR A 786  ? 0.2954 0.2630 0.2955 0.0296  -0.0275 -0.0598 784  THR A OG1 
5776  C CG2 . THR A 786  ? 0.3091 0.2768 0.3159 0.0290  -0.0326 -0.0650 784  THR A CG2 
5777  N N   . GLU A 787  ? 0.3189 0.2889 0.3376 0.0356  -0.0386 -0.0813 785  GLU A N   
5778  C CA  . GLU A 787  ? 0.2848 0.2544 0.3112 0.0366  -0.0430 -0.0880 785  GLU A CA  
5779  C C   . GLU A 787  ? 0.2913 0.2693 0.3153 0.0406  -0.0434 -0.0952 785  GLU A C   
5780  O O   . GLU A 787  ? 0.2935 0.2738 0.3203 0.0415  -0.0461 -0.1000 785  GLU A O   
5781  C CB  . GLU A 787  ? 0.3554 0.3191 0.3906 0.0361  -0.0459 -0.0894 785  GLU A CB  
5782  N N   . VAL A 788  ? 0.2748 0.2578 0.2935 0.0431  -0.0408 -0.0961 786  VAL A N   
5783  C CA  . VAL A 788  ? 0.2655 0.2579 0.2813 0.0469  -0.0409 -0.1027 786  VAL A CA  
5784  C C   . VAL A 788  ? 0.2831 0.2811 0.2917 0.0469  -0.0391 -0.1008 786  VAL A C   
5785  O O   . VAL A 788  ? 0.2656 0.2695 0.2742 0.0489  -0.0408 -0.1063 786  VAL A O   
5786  C CB  . VAL A 788  ? 0.2574 0.2543 0.2699 0.0494  -0.0386 -0.1039 786  VAL A CB  
5787  C CG1 . VAL A 788  ? 0.2853 0.2935 0.2930 0.0531  -0.0379 -0.1094 786  VAL A CG1 
5788  C CG2 . VAL A 788  ? 0.2890 0.2815 0.3099 0.0501  -0.0414 -0.1079 786  VAL A CG2 
5789  N N   . ALA A 789  ? 0.2653 0.2618 0.2680 0.0447  -0.0357 -0.0931 787  ALA A N   
5790  C CA  . ALA A 789  ? 0.2442 0.2455 0.2408 0.0446  -0.0341 -0.0908 787  ALA A CA  
5791  C C   . ALA A 789  ? 0.2574 0.2571 0.2583 0.0436  -0.0374 -0.0934 787  ALA A C   
5792  O O   . ALA A 789  ? 0.2615 0.2676 0.2594 0.0451  -0.0377 -0.0959 787  ALA A O   
5793  C CB  . ALA A 789  ? 0.2462 0.2442 0.2378 0.0420  -0.0306 -0.0822 787  ALA A CB  
5794  N N   . ARG A 790  ? 0.2668 0.2584 0.2750 0.0412  -0.0399 -0.0928 788  ARG A N   
5795  C CA  . ARG A 790  ? 0.2710 0.2608 0.2843 0.0399  -0.0432 -0.0949 788  ARG A CA  
5796  C C   . ARG A 790  ? 0.2684 0.2632 0.2855 0.0430  -0.0466 -0.1041 788  ARG A C   
5797  O O   . ARG A 790  ? 0.2760 0.2740 0.2934 0.0433  -0.0482 -0.1068 788  ARG A O   
5798  C CB  . ARG A 790  ? 0.2969 0.2773 0.3177 0.0365  -0.0451 -0.0918 788  ARG A CB  
5799  C CG  . ARG A 790  ? 0.3158 0.2936 0.3425 0.0347  -0.0485 -0.0930 788  ARG A CG  
5800  C CD  . ARG A 790  ? 0.3077 0.2771 0.3407 0.0308  -0.0497 -0.0879 788  ARG A CD  
5801  N NE  . ARG A 790  ? 0.2963 0.2638 0.3235 0.0284  -0.0459 -0.0798 788  ARG A NE  
5802  C CZ  . ARG A 790  ? 0.2982 0.2614 0.3255 0.0268  -0.0443 -0.0752 788  ARG A CZ  
5803  N NH1 . ARG A 790  ? 0.3428 0.3026 0.3758 0.0272  -0.0462 -0.0772 788  ARG A NH1 
5804  N NH2 . ARG A 790  ? 0.3141 0.2765 0.3360 0.0249  -0.0410 -0.0686 788  ARG A NH2 
5805  N N   . LEU A 791  ? 0.2909 0.2870 0.3109 0.0454  -0.0476 -0.1091 789  LEU A N   
5806  C CA  . LEU A 791  ? 0.2848 0.2870 0.3081 0.0488  -0.0506 -0.1185 789  LEU A CA  
5807  C C   . LEU A 791  ? 0.2821 0.2952 0.2968 0.0515  -0.0485 -0.1203 789  LEU A C   
5808  O O   . LEU A 791  ? 0.2943 0.3126 0.3100 0.0531  -0.0508 -0.1258 789  LEU A O   
5809  C CB  . LEU A 791  ? 0.2899 0.2917 0.3178 0.0510  -0.0518 -0.1233 789  LEU A CB  
5810  C CG  . LEU A 791  ? 0.3422 0.3339 0.3800 0.0488  -0.0547 -0.1225 789  LEU A CG  
5811  C CD1 . LEU A 791  ? 0.3458 0.3379 0.3870 0.0512  -0.0552 -0.1266 789  LEU A CD1 
5812  C CD2 . LEU A 791  ? 0.3675 0.3558 0.4145 0.0480  -0.0596 -0.1268 789  LEU A CD2 
5813  N N   . ILE A 792  ? 0.2754 0.2922 0.2818 0.0519  -0.0442 -0.1154 790  ILE A N   
5814  C CA  . ILE A 792  ? 0.2903 0.3176 0.2885 0.0541  -0.0420 -0.1158 790  ILE A CA  
5815  C C   . ILE A 792  ? 0.2995 0.3270 0.2953 0.0524  -0.0421 -0.1128 790  ILE A C   
5816  O O   . ILE A 792  ? 0.3124 0.3480 0.3057 0.0544  -0.0430 -0.1166 790  ILE A O   
5817  C CB  . ILE A 792  ? 0.2871 0.3175 0.2780 0.0545  -0.0375 -0.1102 790  ILE A CB  
5818  C CG1 . ILE A 792  ? 0.2786 0.3112 0.2716 0.0569  -0.0376 -0.1148 790  ILE A CG1 
5819  C CG2 . ILE A 792  ? 0.2950 0.3353 0.2774 0.0559  -0.0351 -0.1083 790  ILE A CG2 
5820  C CD1 . ILE A 792  ? 0.2743 0.3077 0.2619 0.0567  -0.0336 -0.1090 790  ILE A CD1 
5821  N N   . GLN A 793  ? 0.2706 0.2900 0.2673 0.0488  -0.0413 -0.1061 791  GLN A N   
5822  C CA  . GLN A 793  ? 0.2747 0.2937 0.2699 0.0471  -0.0416 -0.1032 791  GLN A CA  
5823  C C   . GLN A 793  ? 0.2703 0.2908 0.2714 0.0478  -0.0459 -0.1102 791  GLN A C   
5824  O O   . GLN A 793  ? 0.3023 0.3284 0.3004 0.0486  -0.0464 -0.1115 791  GLN A O   
5825  C CB  . GLN A 793  ? 0.3062 0.3157 0.3032 0.0431  -0.0406 -0.0959 791  GLN A CB  
5826  C CG  . GLN A 793  ? 0.2937 0.3022 0.2903 0.0410  -0.0410 -0.0929 791  GLN A CG  
5827  C CD  . GLN A 793  ? 0.3026 0.3019 0.3030 0.0371  -0.0409 -0.0873 791  GLN A CD  
5828  O OE1 . GLN A 793  ? 0.3506 0.3439 0.3572 0.0359  -0.0426 -0.0880 791  GLN A OE1 
5829  N NE2 . GLN A 793  ? 0.3313 0.3300 0.3283 0.0352  -0.0390 -0.0817 791  GLN A NE2 
5830  N N   . ALA A 794  ? 0.2849 0.3003 0.2946 0.0478  -0.0493 -0.1150 792  ALA A N   
5831  C CA  . ALA A 794  ? 0.3277 0.3440 0.3441 0.0485  -0.0538 -0.1220 792  ALA A CA  
5832  C C   . ALA A 794  ? 0.3280 0.3553 0.3415 0.0526  -0.0547 -0.1297 792  ALA A C   
5833  O O   . ALA A 794  ? 0.3644 0.3962 0.3784 0.0534  -0.0568 -0.1334 792  ALA A O   
5834  C CB  . ALA A 794  ? 0.3278 0.3361 0.3549 0.0474  -0.0574 -0.1250 792  ALA A CB  
5835  N N   . GLN A 795  ? 0.3013 0.3338 0.3119 0.0554  -0.0531 -0.1322 793  GLN A N   
5836  C CA  . GLN A 795  ? 0.3083 0.3528 0.3155 0.0595  -0.0536 -0.1393 793  GLN A CA  
5837  C C   . GLN A 795  ? 0.3264 0.3787 0.3250 0.0598  -0.0514 -0.1361 793  GLN A C   
5838  O O   . GLN A 795  ? 0.3514 0.4117 0.3494 0.0619  -0.0534 -0.1418 793  GLN A O   
5839  C CB  . GLN A 795  ? 0.3501 0.3991 0.3538 0.0619  -0.0511 -0.1402 793  GLN A CB  
5840  C CG  . GLN A 795  ? 0.3897 0.4358 0.4014 0.0634  -0.0538 -0.1469 793  GLN A CG  
5841  C CD  . GLN A 795  ? 0.4305 0.4840 0.4376 0.0663  -0.0512 -0.1484 793  GLN A CD  
5842  O OE1 . GLN A 795  ? 0.4366 0.4870 0.4402 0.0651  -0.0478 -0.1418 793  GLN A OE1 
5843  N NE2 . GLN A 795  ? 0.3636 0.4277 0.3705 0.0703  -0.0526 -0.1570 793  GLN A NE2 
5844  N N   . LEU A 796  ? 0.2912 0.3419 0.2832 0.0579  -0.0474 -0.1271 794  LEU A N   
5845  C CA  . LEU A 796  ? 0.3224 0.3807 0.3064 0.0583  -0.0452 -0.1234 794  LEU A CA  
5846  C C   . LEU A 796  ? 0.3339 0.3899 0.3197 0.0564  -0.0471 -0.1224 794  LEU A C   
5847  O O   . LEU A 796  ? 0.3880 0.4517 0.3686 0.0574  -0.0465 -0.1218 794  LEU A O   
5848  C CB  . LEU A 796  ? 0.3017 0.3586 0.2791 0.0568  -0.0406 -0.1141 794  LEU A CB  
5849  C CG  . LEU A 796  ? 0.2735 0.3355 0.2471 0.0589  -0.0380 -0.1139 794  LEU A CG  
5850  C CD1 . LEU A 796  ? 0.3030 0.3625 0.2711 0.0570  -0.0337 -0.1044 794  LEU A CD1 
5851  C CD2 . LEU A 796  ? 0.2834 0.3592 0.2527 0.0626  -0.0381 -0.1192 794  LEU A CD2 
5852  N N   . ALA A 797  ? 0.3162 0.3622 0.3093 0.0537  -0.0493 -0.1220 795  ALA A N   
5853  C CA  . ALA A 797  ? 0.3454 0.3894 0.3404 0.0518  -0.0511 -0.1211 795  ALA A CA  
5854  C C   . ALA A 797  ? 0.3602 0.4118 0.3574 0.0543  -0.0547 -0.1295 795  ALA A C   
5855  O O   . ALA A 797  ? 0.4709 0.5246 0.4673 0.0536  -0.0556 -0.1290 795  ALA A O   
5856  C CB  . ALA A 797  ? 0.3465 0.3787 0.3492 0.0482  -0.0528 -0.1185 795  ALA A CB  
5857  N N   . ASP A 798  ? 0.3917 0.4478 0.3916 0.0573  -0.0567 -0.1376 796  ASP A N   
5858  C CA  . ASP A 798  ? 0.4289 0.4939 0.4302 0.0602  -0.0599 -0.1464 796  ASP A CA  
5859  C C   . ASP A 798  ? 0.4698 0.5475 0.4616 0.0627  -0.0576 -0.1460 796  ASP A C   
5860  O O   . ASP A 798  ? 0.4140 0.4999 0.4058 0.0648  -0.0600 -0.1521 796  ASP A O   
5861  C CB  . ASP A 798  ? 0.3587 0.4257 0.3656 0.0631  -0.0624 -0.1554 796  ASP A CB  
5862  C CG  . ASP A 798  ? 0.5695 0.6252 0.5875 0.0612  -0.0659 -0.1578 796  ASP A CG  
5863  O OD1 . ASP A 798  ? 0.5832 0.6314 0.6053 0.0579  -0.0673 -0.1542 796  ASP A OD1 
5864  O OD2 . ASP A 798  ? 0.5483 0.6032 0.5714 0.0629  -0.0675 -0.1633 796  ASP A OD2 
5865  N N   . ARG A 799  ? 0.3458 0.4257 0.3299 0.0626  -0.0532 -0.1388 797  ARG A N   
5866  C CA  A ARG A 799  ? 0.3603 0.4532 0.3359 0.0653  -0.0509 -0.1386 797  ARG A CA  
5867  C CA  B ARG A 799  ? 0.3599 0.4530 0.3356 0.0653  -0.0510 -0.1387 797  ARG A CA  
5868  C C   . ARG A 799  ? 0.3252 0.4200 0.2942 0.0637  -0.0483 -0.1302 797  ARG A C   
5869  O O   . ARG A 799  ? 0.3466 0.4323 0.3157 0.0606  -0.0465 -0.1227 797  ARG A O   
5870  C CB  A ARG A 799  ? 0.4223 0.5175 0.3947 0.0666  -0.0479 -0.1371 797  ARG A CB  
5871  C CB  B ARG A 799  ? 0.4234 0.5198 0.3957 0.0670  -0.0482 -0.1380 797  ARG A CB  
5872  C CG  A ARG A 799  ? 0.4074 0.4991 0.3869 0.0679  -0.0503 -0.1444 797  ARG A CG  
5873  C CG  B ARG A 799  ? 0.4007 0.4973 0.3793 0.0693  -0.0508 -0.1471 797  ARG A CG  
5874  C CD  A ARG A 799  ? 0.3938 0.4982 0.3727 0.0722  -0.0520 -0.1539 797  ARG A CD  
5875  C CD  B ARG A 799  ? 0.4351 0.5381 0.4095 0.0715  -0.0480 -0.1471 797  ARG A CD  
5876  N NE  A ARG A 799  ? 0.4392 0.5555 0.4088 0.0741  -0.0484 -0.1508 797  ARG A NE  
5877  N NE  B ARG A 799  ? 0.4531 0.5697 0.4186 0.0735  -0.0455 -0.1451 797  ARG A NE  
5878  C CZ  A ARG A 799  ? 0.4098 0.5268 0.3760 0.0744  -0.0451 -0.1468 797  ARG A CZ  
5879  C CZ  B ARG A 799  ? 0.3785 0.4983 0.3372 0.0732  -0.0414 -0.1377 797  ARG A CZ  
5880  N NH1 A ARG A 799  ? 0.4379 0.5446 0.4088 0.0730  -0.0448 -0.1456 797  ARG A NH1 
5881  N NH1 B ARG A 799  ? 0.3194 0.4309 0.2789 0.0714  -0.0391 -0.1326 797  ARG A NH1 
5882  N NH2 A ARG A 799  ? 0.4482 0.5768 0.4063 0.0760  -0.0420 -0.1435 797  ARG A NH2 
5883  N NH2 B ARG A 799  ? 0.3914 0.5236 0.3427 0.0747  -0.0396 -0.1354 797  ARG A NH2 
5884  N N   . LEU A 800  ? 0.3330 0.4400 0.2963 0.0660  -0.0481 -0.1315 798  LEU A N   
5885  C CA  . LEU A 800  ? 0.3710 0.4821 0.3275 0.0651  -0.0455 -0.1237 798  LEU A CA  
5886  C C   . LEU A 800  ? 0.2943 0.4192 0.2434 0.0681  -0.0434 -0.1235 798  LEU A C   
5887  O O   . LEU A 800  ? 0.3554 0.4890 0.3047 0.0711  -0.0448 -0.1312 798  LEU A O   
5888  C CB  . LEU A 800  ? 0.3571 0.4702 0.3144 0.0647  -0.0480 -0.1250 798  LEU A CB  
5889  C CG  . LEU A 800  ? 0.3510 0.4520 0.3150 0.0615  -0.0500 -0.1241 798  LEU A CG  
5890  C CD1 . LEU A 800  ? 0.3694 0.4747 0.3342 0.0617  -0.0527 -0.1268 798  LEU A CD1 
5891  C CD2 . LEU A 800  ? 0.3781 0.4700 0.3406 0.0583  -0.0468 -0.1142 798  LEU A CD2 
5892  N N   . SER A 801  ? 0.3433 0.4702 0.2864 0.0671  -0.0400 -0.1145 799  SER A N   
5893  C CA  . SER A 801  ? 0.3385 0.4790 0.2745 0.0695  -0.0379 -0.1126 799  SER A CA  
5894  C C   . SER A 801  ? 0.4301 0.5827 0.3638 0.0716  -0.0402 -0.1171 799  SER A C   
5895  O O   . SER A 801  ? 0.3966 0.5459 0.3339 0.0709  -0.0430 -0.1202 799  SER A O   
5896  C CB  . SER A 801  ? 0.3827 0.5214 0.3140 0.0675  -0.0343 -0.1015 799  SER A CB  
5897  O OG  . SER A 801  ? 0.3923 0.5302 0.3229 0.0662  -0.0350 -0.0976 799  SER A OG  
5898  N N   . PRO A 802  ? 0.3798 0.5471 0.3076 0.0743  -0.0390 -0.1175 800  PRO A N   
5899  C CA  . PRO A 802  ? 0.4240 0.6038 0.3490 0.0763  -0.0410 -0.1208 800  PRO A CA  
5900  C C   . PRO A 802  ? 0.4311 0.6081 0.3548 0.0742  -0.0411 -0.1143 800  PRO A C   
5901  O O   . PRO A 802  ? 0.4973 0.6802 0.4211 0.0751  -0.0438 -0.1182 800  PRO A O   
5902  C CB  . PRO A 802  ? 0.4667 0.6622 0.3848 0.0789  -0.0388 -0.1195 800  PRO A CB  
5903  C CG  . PRO A 802  ? 0.4708 0.6630 0.3905 0.0793  -0.0372 -0.1210 800  PRO A CG  
5904  C CD  . PRO A 802  ? 0.3941 0.5683 0.3182 0.0759  -0.0363 -0.1161 800  PRO A CD  
5905  N N   . ALA A 803  ? 0.4343 0.6029 0.3570 0.0715  -0.0385 -0.1046 801  ALA A N   
5906  C CA  . ALA A 803  ? 0.4634 0.6276 0.3860 0.0693  -0.0386 -0.0984 801  ALA A CA  
5907  C C   . ALA A 803  ? 0.4951 0.6459 0.4243 0.0670  -0.0407 -0.1008 801  ALA A C   
5908  O O   . ALA A 803  ? 0.4797 0.6260 0.4094 0.0651  -0.0409 -0.0960 801  ALA A O   
5909  C CB  . ALA A 803  ? 0.4936 0.6546 0.4130 0.0675  -0.0350 -0.0874 801  ALA A CB  
5910  N N   . GLY A 804  ? 0.4686 0.6130 0.4031 0.0671  -0.0424 -0.1077 802  GLY A N   
5911  C CA  . GLY A 804  ? 0.3719 0.5041 0.3132 0.0647  -0.0446 -0.1097 802  GLY A CA  
5912  C C   . GLY A 804  ? 0.4196 0.5384 0.3630 0.0614  -0.0424 -0.1026 802  GLY A C   
5913  O O   . GLY A 804  ? 0.3993 0.5099 0.3465 0.0591  -0.0435 -0.1009 802  GLY A O   
5914  N N   . ARG A 805  ? 0.3945 0.5112 0.3358 0.0612  -0.0394 -0.0986 803  ARG A N   
5915  C CA  . ARG A 805  ? 0.4033 0.5081 0.3463 0.0583  -0.0373 -0.0919 803  ARG A CA  
5916  C C   . ARG A 805  ? 0.2898 0.3885 0.2360 0.0581  -0.0368 -0.0945 803  ARG A C   
5917  O O   . ARG A 805  ? 0.3329 0.4379 0.2785 0.0606  -0.0373 -0.1000 803  ARG A O   
5918  C CB  . ARG A 805  ? 0.4185 0.5260 0.3560 0.0578  -0.0338 -0.0827 803  ARG A CB  
5919  C CG  . ARG A 805  ? 0.4373 0.5500 0.3721 0.0577  -0.0343 -0.0793 803  ARG A CG  
5920  C CD  . ARG A 805  ? 0.4232 0.5278 0.3629 0.0556  -0.0363 -0.0799 803  ARG A CD  
5921  N NE  . ARG A 805  ? 0.4127 0.5226 0.3502 0.0557  -0.0370 -0.0770 803  ARG A NE  
5922  C CZ  . ARG A 805  ? 0.4646 0.5810 0.4026 0.0570  -0.0398 -0.0821 803  ARG A CZ  
5923  N NH1 . ARG A 805  ? 0.4254 0.5437 0.3662 0.0583  -0.0425 -0.0907 803  ARG A NH1 
5924  N NH2 . ARG A 805  ? 0.5789 0.7000 0.5147 0.0570  -0.0402 -0.0786 803  ARG A NH2 
5925  N N   . PRO A 806  ? 0.3268 0.4134 0.2765 0.0553  -0.0360 -0.0910 804  PRO A N   
5926  C CA  . PRO A 806  ? 0.3279 0.4083 0.2812 0.0550  -0.0358 -0.0933 804  PRO A CA  
5927  C C   . PRO A 806  ? 0.3205 0.4062 0.2691 0.0566  -0.0329 -0.0912 804  PRO A C   
5928  O O   . PRO A 806  ? 0.3044 0.3939 0.2478 0.0566  -0.0302 -0.0847 804  PRO A O   
5929  C CB  . PRO A 806  ? 0.3449 0.4129 0.3015 0.0515  -0.0349 -0.0880 804  PRO A CB  
5930  C CG  . PRO A 806  ? 0.3702 0.4373 0.3275 0.0502  -0.0361 -0.0862 804  PRO A CG  
5931  C CD  . PRO A 806  ? 0.3660 0.4445 0.3175 0.0523  -0.0356 -0.0855 804  PRO A CD  
5932  N N   . ILE A 807  ? 0.2884 0.3742 0.2395 0.0580  -0.0336 -0.0966 805  ILE A N   
5933  C CA  . ILE A 807  ? 0.2864 0.3763 0.2340 0.0594  -0.0310 -0.0950 805  ILE A CA  
5934  C C   . ILE A 807  ? 0.2637 0.3436 0.2118 0.0567  -0.0284 -0.0879 805  ILE A C   
5935  O O   . ILE A 807  ? 0.3055 0.3752 0.2588 0.0549  -0.0294 -0.0888 805  ILE A O   
5936  C CB  . ILE A 807  ? 0.2915 0.3842 0.2424 0.0618  -0.0328 -0.1036 805  ILE A CB  
5937  C CG1 . ILE A 807  ? 0.3342 0.4368 0.2853 0.0645  -0.0358 -0.1115 805  ILE A CG1 
5938  C CG2 . ILE A 807  ? 0.3120 0.4096 0.2595 0.0632  -0.0300 -0.1020 805  ILE A CG2 
5939  C CD1 . ILE A 807  ? 0.3683 0.4844 0.3121 0.0664  -0.0343 -0.1095 805  ILE A CD1 
5940  N N   . PRO A 808  ? 0.2779 0.3605 0.2210 0.0564  -0.0252 -0.0807 806  PRO A N   
5941  C CA  . PRO A 808  ? 0.2808 0.3539 0.2245 0.0539  -0.0228 -0.0741 806  PRO A CA  
5942  C C   . PRO A 808  ? 0.2599 0.3282 0.2068 0.0539  -0.0226 -0.0767 806  PRO A C   
5943  O O   . PRO A 808  ? 0.2765 0.3513 0.2224 0.0563  -0.0225 -0.0808 806  PRO A O   
5944  C CB  . PRO A 808  ? 0.2819 0.3614 0.2198 0.0543  -0.0198 -0.0672 806  PRO A CB  
5945  C CG  . PRO A 808  ? 0.3350 0.4246 0.2698 0.0559  -0.0209 -0.0683 806  PRO A CG  
5946  C CD  . PRO A 808  ? 0.3032 0.3972 0.2402 0.0580  -0.0238 -0.0777 806  PRO A CD  
5947  N N   . LEU A 809  ? 0.2643 0.3212 0.2149 0.0513  -0.0225 -0.0743 807  LEU A N   
5948  C CA  . LEU A 809  ? 0.2785 0.3294 0.2325 0.0509  -0.0224 -0.0758 807  LEU A CA  
5949  C C   . LEU A 809  ? 0.2841 0.3278 0.2373 0.0484  -0.0197 -0.0683 807  LEU A C   
5950  O O   . LEU A 809  ? 0.2782 0.3156 0.2327 0.0460  -0.0197 -0.0646 807  LEU A O   
5951  C CB  . LEU A 809  ? 0.2788 0.3228 0.2397 0.0500  -0.0257 -0.0811 807  LEU A CB  
5952  C CG  . LEU A 809  ? 0.2861 0.3223 0.2514 0.0490  -0.0258 -0.0816 807  LEU A CG  
5953  C CD1 . LEU A 809  ? 0.2795 0.3218 0.2440 0.0518  -0.0253 -0.0857 807  LEU A CD1 
5954  C CD2 . LEU A 809  ? 0.3169 0.3458 0.2895 0.0476  -0.0292 -0.0854 807  LEU A CD2 
5955  N N   . ILE A 810  ? 0.2329 0.2781 0.1842 0.0490  -0.0174 -0.0662 808  ILE A N   
5956  C CA  . ILE A 810  ? 0.2582 0.2957 0.2100 0.0468  -0.0153 -0.0606 808  ILE A CA  
5957  C C   . ILE A 810  ? 0.2585 0.2901 0.2151 0.0465  -0.0166 -0.0643 808  ILE A C   
5958  O O   . ILE A 810  ? 0.2736 0.3097 0.2305 0.0487  -0.0169 -0.0687 808  ILE A O   
5959  C CB  . ILE A 810  ? 0.2269 0.2693 0.1741 0.0474  -0.0122 -0.0555 808  ILE A CB  
5960  C CG1 . ILE A 810  ? 0.2636 0.3128 0.2065 0.0479  -0.0113 -0.0518 808  ILE A CG1 
5961  C CG2 . ILE A 810  ? 0.2698 0.3037 0.2180 0.0450  -0.0103 -0.0500 808  ILE A CG2 
5962  C CD1 . ILE A 810  ? 0.2888 0.3428 0.2280 0.0483  -0.0084 -0.0460 808  ILE A CD1 
5963  N N   . ALA A 811  ? 0.2428 0.2650 0.2034 0.0439  -0.0174 -0.0628 809  ALA A N   
5964  C CA  . ALA A 811  ? 0.2506 0.2667 0.2165 0.0434  -0.0190 -0.0659 809  ALA A CA  
5965  C C   . ALA A 811  ? 0.2576 0.2660 0.2241 0.0408  -0.0171 -0.0601 809  ALA A C   
5966  O O   . ALA A 811  ? 0.2688 0.2717 0.2365 0.0383  -0.0173 -0.0568 809  ALA A O   
5967  C CB  . ALA A 811  ? 0.2801 0.2928 0.2515 0.0428  -0.0225 -0.0705 809  ALA A CB  
5968  N N   . GLU A 812  ? 0.2162 0.2249 0.1816 0.0414  -0.0154 -0.0589 810  GLU A N   
5969  C CA  . GLU A 812  ? 0.2454 0.2479 0.2109 0.0393  -0.0135 -0.0536 810  GLU A CA  
5970  C C   . GLU A 812  ? 0.2386 0.2356 0.2094 0.0388  -0.0151 -0.0562 810  GLU A C   
5971  O O   . GLU A 812  ? 0.2457 0.2458 0.2176 0.0409  -0.0155 -0.0602 810  GLU A O   
5972  C CB  . GLU A 812  ? 0.2858 0.2930 0.2466 0.0403  -0.0104 -0.0500 810  GLU A CB  
5973  C CG  . GLU A 812  ? 0.2657 0.2783 0.2220 0.0406  -0.0091 -0.0469 810  GLU A CG  
5974  C CD  . GLU A 812  ? 0.3288 0.3360 0.2856 0.0381  -0.0091 -0.0431 810  GLU A CD  
5975  O OE1 . GLU A 812  ? 0.3054 0.3083 0.2619 0.0364  -0.0074 -0.0382 810  GLU A OE1 
5976  O OE2 . GLU A 812  ? 0.3010 0.3085 0.2589 0.0379  -0.0110 -0.0452 810  GLU A OE2 
5977  N N   . THR A 813  ? 0.2470 0.2365 0.2215 0.0361  -0.0161 -0.0542 811  THR A N   
5978  C CA  . THR A 813  ? 0.2531 0.2375 0.2339 0.0355  -0.0186 -0.0572 811  THR A CA  
5979  C C   . THR A 813  ? 0.2491 0.2267 0.2316 0.0331  -0.0177 -0.0528 811  THR A C   
5980  O O   . THR A 813  ? 0.2661 0.2441 0.2449 0.0327  -0.0149 -0.0486 811  THR A O   
5981  C CB  . THR A 813  ? 0.2360 0.2186 0.2211 0.0348  -0.0219 -0.0604 811  THR A CB  
5982  O OG1 . THR A 813  ? 0.2832 0.2641 0.2666 0.0326  -0.0212 -0.0563 811  THR A OG1 
5983  C CG2 . THR A 813  ? 0.2678 0.2576 0.2521 0.0378  -0.0232 -0.0664 811  THR A CG2 
5984  N N   . GLY A 814  ? 0.2767 0.2486 0.2652 0.0315  -0.0201 -0.0536 812  GLY A N   
5985  C CA  . GLY A 814  ? 0.2684 0.2349 0.2592 0.0296  -0.0197 -0.0502 812  GLY A CA  
5986  C C   . GLY A 814  ? 0.2610 0.2242 0.2499 0.0267  -0.0179 -0.0441 812  GLY A C   
5987  O O   . GLY A 814  ? 0.2710 0.2354 0.2573 0.0259  -0.0172 -0.0424 812  GLY A O   
5988  N N   . GLY A 815  ? 0.2542 0.2134 0.2445 0.0251  -0.0173 -0.0410 813  GLY A N   
5989  C CA  . GLY A 815  ? 0.2701 0.2265 0.2588 0.0224  -0.0157 -0.0356 813  GLY A CA  
5990  C C   . GLY A 815  ? 0.2778 0.2290 0.2718 0.0200  -0.0174 -0.0338 813  GLY A C   
5991  O O   . GLY A 815  ? 0.3106 0.2599 0.3092 0.0205  -0.0194 -0.0361 813  GLY A O   
5992  N N   . GLN A 816  ? 0.2581 0.2075 0.2517 0.0173  -0.0167 -0.0296 814  GLN A N   
5993  C CA  . GLN A 816  ? 0.2583 0.2037 0.2558 0.0147  -0.0177 -0.0264 814  GLN A CA  
5994  C C   . GLN A 816  ? 0.2509 0.1966 0.2443 0.0133  -0.0148 -0.0220 814  GLN A C   
5995  O O   . GLN A 816  ? 0.2835 0.2291 0.2766 0.0111  -0.0145 -0.0190 814  GLN A O   
5996  C CB  . GLN A 816  ? 0.2759 0.2196 0.2784 0.0125  -0.0204 -0.0261 814  GLN A CB  
5997  C CG  . GLN A 816  ? 0.3053 0.2453 0.3128 0.0100  -0.0219 -0.0230 814  GLN A CG  
5998  C CD  . GLN A 816  ? 0.3242 0.2618 0.3366 0.0111  -0.0241 -0.0256 814  GLN A CD  
5999  O OE1 . GLN A 816  ? 0.3012 0.2387 0.3119 0.0124  -0.0228 -0.0257 814  GLN A OE1 
6000  N NE2 . GLN A 816  ? 0.3473 0.2830 0.3664 0.0108  -0.0276 -0.0277 814  GLN A NE2 
6001  N N   . ASN A 817  ? 0.2312 0.1777 0.2214 0.0147  -0.0128 -0.0217 815  ASN A N   
6002  C CA  . ASN A 817  ? 0.2378 0.1857 0.2233 0.0143  -0.0099 -0.0187 815  ASN A CA  
6003  C C   . ASN A 817  ? 0.2271 0.1727 0.2137 0.0119  -0.0094 -0.0149 815  ASN A C   
6004  O O   . ASN A 817  ? 0.2426 0.1860 0.2319 0.0116  -0.0103 -0.0146 815  ASN A O   
6005  C CB  . ASN A 817  ? 0.2210 0.1711 0.2032 0.0168  -0.0080 -0.0198 815  ASN A CB  
6006  C CG  . ASN A 817  ? 0.2267 0.1800 0.2080 0.0193  -0.0087 -0.0236 815  ASN A CG  
6007  O OD1 . ASN A 817  ? 0.2340 0.1893 0.2140 0.0195  -0.0088 -0.0243 815  ASN A OD1 
6008  N ND2 . ASN A 817  ? 0.2320 0.1863 0.2142 0.0213  -0.0090 -0.0264 815  ASN A ND2 
6009  N N   . ALA A 818  ? 0.2218 0.1683 0.2065 0.0104  -0.0082 -0.0123 816  ALA A N   
6010  C CA  . ALA A 818  ? 0.2349 0.1805 0.2202 0.0080  -0.0076 -0.0089 816  ALA A CA  
6011  C C   . ALA A 818  ? 0.2081 0.1548 0.1895 0.0085  -0.0049 -0.0074 816  ALA A C   
6012  O O   . ALA A 818  ? 0.2255 0.1740 0.2038 0.0101  -0.0035 -0.0082 816  ALA A O   
6013  C CB  . ALA A 818  ? 0.2446 0.1911 0.2311 0.0058  -0.0083 -0.0072 816  ALA A CB  
6014  N N   . MET A 819  ? 0.2217 0.1676 0.2037 0.0070  -0.0045 -0.0051 817  MET A N   
6015  C CA  . MET A 819  ? 0.2371 0.1841 0.2163 0.0069  -0.0023 -0.0034 817  MET A CA  
6016  C C   . MET A 819  ? 0.2326 0.1803 0.2128 0.0043  -0.0025 -0.0009 817  MET A C   
6017  O O   . MET A 819  ? 0.2474 0.1941 0.2304 0.0027  -0.0039 0.0004  817  MET A O   
6018  C CB  . MET A 819  ? 0.2302 0.1761 0.2090 0.0079  -0.0015 -0.0033 817  MET A CB  
6019  C CG  . MET A 819  ? 0.2458 0.1926 0.2225 0.0075  0.0005  -0.0016 817  MET A CG  
6020  S SD  . MET A 819  ? 0.2717 0.2173 0.2485 0.0083  0.0012  -0.0012 817  MET A SD  
6021  C CE  . MET A 819  ? 0.2995 0.2459 0.2748 0.0112  0.0019  -0.0034 817  MET A CE  
6022  N N   . ILE A 820  ? 0.2218 0.1718 0.2000 0.0039  -0.0011 -0.0003 818  ILE A N   
6023  C CA  . ILE A 820  ? 0.2350 0.1871 0.2138 0.0016  -0.0010 0.0018  818  ILE A CA  
6024  C C   . ILE A 820  ? 0.2090 0.1617 0.1862 0.0017  0.0007  0.0025  818  ILE A C   
6025  O O   . ILE A 820  ? 0.2265 0.1793 0.2018 0.0033  0.0021  0.0015  818  ILE A O   
6026  C CB  . ILE A 820  ? 0.2265 0.1812 0.2047 0.0011  -0.0007 0.0015  818  ILE A CB  
6027  C CG1 . ILE A 820  ? 0.2500 0.2041 0.2303 0.0007  -0.0025 0.0009  818  ILE A CG1 
6028  C CG2 . ILE A 820  ? 0.2320 0.1900 0.2105 -0.0011 -0.0003 0.0034  818  ILE A CG2 
6029  C CD1 . ILE A 820  ? 0.2435 0.2003 0.2235 0.0002  -0.0024 0.0006  818  ILE A CD1 
6030  N N   . VAL A 821  ? 0.2213 0.1746 0.1996 -0.0001 0.0003  0.0044  819  VAL A N   
6031  C CA  . VAL A 821  ? 0.2284 0.1826 0.2056 -0.0001 0.0015  0.0050  819  VAL A CA  
6032  C C   . VAL A 821  ? 0.2362 0.1943 0.2135 -0.0022 0.0016  0.0064  819  VAL A C   
6033  O O   . VAL A 821  ? 0.2766 0.2358 0.2557 -0.0042 0.0003  0.0084  819  VAL A O   
6034  C CB  . VAL A 821  ? 0.2358 0.1875 0.2142 -0.0001 0.0009  0.0058  819  VAL A CB  
6035  C CG1 . VAL A 821  ? 0.2581 0.2110 0.2356 -0.0003 0.0020  0.0064  819  VAL A CG1 
6036  C CG2 . VAL A 821  ? 0.2482 0.1969 0.2266 0.0021  0.0007  0.0041  819  VAL A CG2 
6037  N N   . ASP A 822  ? 0.2476 0.2081 0.2234 -0.0019 0.0031  0.0055  820  ASP A N   
6038  C CA  . ASP A 822  ? 0.2487 0.2141 0.2246 -0.0037 0.0033  0.0064  820  ASP A CA  
6039  C C   . ASP A 822  ? 0.2693 0.2358 0.2449 -0.0041 0.0038  0.0069  820  ASP A C   
6040  O O   . ASP A 822  ? 0.2691 0.2324 0.2445 -0.0030 0.0040  0.0067  820  ASP A O   
6041  C CB  . ASP A 822  ? 0.2762 0.2446 0.2513 -0.0032 0.0042  0.0048  820  ASP A CB  
6042  C CG  . ASP A 822  ? 0.2601 0.2281 0.2343 -0.0014 0.0056  0.0026  820  ASP A CG  
6043  O OD1 . ASP A 822  ? 0.2771 0.2433 0.2512 -0.0007 0.0060  0.0025  820  ASP A OD1 
6044  O OD2 . ASP A 822  ? 0.2773 0.2470 0.2514 -0.0006 0.0061  0.0011  820  ASP A OD2 
6045  N N   . SER A 823  ? 0.2641 0.2358 0.2395 -0.0056 0.0040  0.0075  821  SER A N   
6046  C CA  . SER A 823  ? 0.2977 0.2714 0.2729 -0.0062 0.0043  0.0080  821  SER A CA  
6047  C C   . SER A 823  ? 0.3110 0.2839 0.2855 -0.0044 0.0056  0.0054  821  SER A C   
6048  O O   . SER A 823  ? 0.3448 0.3191 0.3193 -0.0047 0.0057  0.0054  821  SER A O   
6049  C CB  . SER A 823  ? 0.3068 0.2872 0.2819 -0.0083 0.0041  0.0093  821  SER A CB  
6050  O OG  . SER A 823  ? 0.3384 0.3229 0.3129 -0.0079 0.0050  0.0071  821  SER A OG  
6051  N N   . SER A 824  ? 0.2634 0.2344 0.2376 -0.0026 0.0063  0.0033  822  SER A N   
6052  C CA  . SER A 824  ? 0.2736 0.2435 0.2481 -0.0010 0.0072  0.0013  822  SER A CA  
6053  C C   . SER A 824  ? 0.2735 0.2381 0.2481 0.0004  0.0073  0.0017  822  SER A C   
6054  O O   . SER A 824  ? 0.2825 0.2460 0.2578 0.0015  0.0080  0.0007  822  SER A O   
6055  C CB  . SER A 824  ? 0.2737 0.2445 0.2485 0.0002  0.0078  -0.0008 822  SER A CB  
6056  O OG  . SER A 824  ? 0.2624 0.2297 0.2369 0.0013  0.0077  -0.0005 822  SER A OG  
6057  N N   . ALA A 825  ? 0.2870 0.2488 0.2614 0.0003  0.0067  0.0032  823  ALA A N   
6058  C CA  . ALA A 825  ? 0.2836 0.2413 0.2581 0.0017  0.0068  0.0033  823  ALA A CA  
6059  C C   . ALA A 825  ? 0.2600 0.2170 0.2350 0.0014  0.0068  0.0041  823  ALA A C   
6060  O O   . ALA A 825  ? 0.3072 0.2664 0.2824 -0.0002 0.0062  0.0051  823  ALA A O   
6061  C CB  . ALA A 825  ? 0.2696 0.2251 0.2441 0.0019  0.0059  0.0040  823  ALA A CB  
6062  N N   . LEU A 826  ? 0.2851 0.2395 0.2604 0.0028  0.0073  0.0039  824  LEU A N   
6063  C CA  . LEU A 826  ? 0.3092 0.2628 0.2853 0.0026  0.0073  0.0046  824  LEU A CA  
6064  C C   . LEU A 826  ? 0.3044 0.2558 0.2808 0.0026  0.0064  0.0058  824  LEU A C   
6065  O O   . LEU A 826  ? 0.3033 0.2525 0.2795 0.0039  0.0065  0.0054  824  LEU A O   
6066  C CB  . LEU A 826  ? 0.3476 0.2998 0.3243 0.0041  0.0083  0.0040  824  LEU A CB  
6067  N N   . ALA A 827  ? 0.2848 0.2369 0.2619 0.0011  0.0054  0.0071  825  ALA A N   
6068  C CA  . ALA A 827  ? 0.2811 0.2312 0.2594 0.0009  0.0041  0.0082  825  ALA A CA  
6069  C C   . ALA A 827  ? 0.2735 0.2207 0.2523 0.0027  0.0044  0.0076  825  ALA A C   
6070  O O   . ALA A 827  ? 0.2738 0.2193 0.2532 0.0036  0.0038  0.0071  825  ALA A O   
6071  C CB  . ALA A 827  ? 0.3260 0.2777 0.3054 -0.0011 0.0030  0.0102  825  ALA A CB  
6072  N N   . GLU A 828  ? 0.2988 0.2460 0.2776 0.0032  0.0054  0.0075  826  GLU A N   
6073  C CA  . GLU A 828  ? 0.3030 0.2484 0.2825 0.0049  0.0058  0.0071  826  GLU A CA  
6074  C C   . GLU A 828  ? 0.3079 0.2528 0.2863 0.0066  0.0066  0.0059  826  GLU A C   
6075  O O   . GLU A 828  ? 0.2922 0.2360 0.2711 0.0079  0.0063  0.0053  826  GLU A O   
6076  C CB  . GLU A 828  ? 0.3365 0.2824 0.3164 0.0051  0.0068  0.0073  826  GLU A CB  
6077  C CG  . GLU A 828  ? 0.3814 0.3277 0.3624 0.0038  0.0060  0.0085  826  GLU A CG  
6078  C CD  . GLU A 828  ? 0.4562 0.4052 0.4367 0.0019  0.0056  0.0089  826  GLU A CD  
6079  O OE1 . GLU A 828  ? 0.4389 0.3892 0.4183 0.0017  0.0060  0.0081  826  GLU A OE1 
6080  O OE2 . GLU A 828  ? 0.5434 0.4935 0.5247 0.0007  0.0048  0.0101  826  GLU A OE2 
6081  N N   . GLN A 829  ? 0.3116 0.2575 0.2889 0.0067  0.0074  0.0054  827  GLN A N   
6082  C CA  . GLN A 829  ? 0.3038 0.2497 0.2801 0.0083  0.0080  0.0046  827  GLN A CA  
6083  C C   . GLN A 829  ? 0.2710 0.2165 0.2470 0.0084  0.0068  0.0039  827  GLN A C   
6084  O O   . GLN A 829  ? 0.2758 0.2210 0.2515 0.0099  0.0068  0.0030  827  GLN A O   
6085  C CB  . GLN A 829  ? 0.3373 0.2844 0.3130 0.0082  0.0088  0.0044  827  GLN A CB  
6086  C CG  . GLN A 829  ? 0.5606 0.5079 0.5366 0.0094  0.0099  0.0048  827  GLN A CG  
6087  C CD  . GLN A 829  ? 0.5501 0.4983 0.5264 0.0092  0.0103  0.0045  827  GLN A CD  
6088  O OE1 . GLN A 829  ? 0.4829 0.4320 0.4587 0.0085  0.0099  0.0037  827  GLN A OE1 
6089  N NE2 . GLN A 829  ? 0.5597 0.5080 0.5374 0.0099  0.0111  0.0051  827  GLN A NE2 
6090  N N   . VAL A 830  ? 0.2617 0.2074 0.2380 0.0067  0.0058  0.0042  828  VAL A N   
6091  C CA  . VAL A 830  ? 0.2772 0.2224 0.2541 0.0065  0.0045  0.0037  828  VAL A CA  
6092  C C   . VAL A 830  ? 0.2535 0.1970 0.2321 0.0073  0.0034  0.0032  828  VAL A C   
6093  O O   . VAL A 830  ? 0.2514 0.1943 0.2302 0.0086  0.0028  0.0017  828  VAL A O   
6094  C CB  . VAL A 830  ? 0.2526 0.1988 0.2302 0.0043  0.0035  0.0048  828  VAL A CB  
6095  C CG1 . VAL A 830  ? 0.2687 0.2140 0.2479 0.0039  0.0017  0.0047  828  VAL A CG1 
6096  C CG2 . VAL A 830  ? 0.2694 0.2178 0.2454 0.0039  0.0045  0.0046  828  VAL A CG2 
6097  N N   . VAL A 831  ? 0.2655 0.2082 0.2455 0.0066  0.0030  0.0043  829  VAL A N   
6098  C CA  . VAL A 831  ? 0.2392 0.1803 0.2216 0.0072  0.0017  0.0039  829  VAL A CA  
6099  C C   . VAL A 831  ? 0.2393 0.1804 0.2210 0.0096  0.0025  0.0020  829  VAL A C   
6100  O O   . VAL A 831  ? 0.2370 0.1776 0.2202 0.0108  0.0015  0.0002  829  VAL A O   
6101  C CB  . VAL A 831  ? 0.2373 0.1779 0.2214 0.0059  0.0010  0.0057  829  VAL A CB  
6102  C CG1 . VAL A 831  ? 0.2444 0.1833 0.2313 0.0070  -0.0002 0.0049  829  VAL A CG1 
6103  C CG2 . VAL A 831  ? 0.2915 0.2327 0.2766 0.0035  -0.0003 0.0076  829  VAL A CG2 
6104  N N   . GLY A 832  ? 0.2501 0.1924 0.2301 0.0104  0.0044  0.0023  830  GLY A N   
6105  C CA  . GLY A 832  ? 0.2465 0.1900 0.2258 0.0126  0.0054  0.0010  830  GLY A CA  
6106  C C   . GLY A 832  ? 0.2399 0.1844 0.2180 0.0138  0.0052  -0.0007 830  GLY A C   
6107  O O   . GLY A 832  ? 0.2478 0.1933 0.2264 0.0155  0.0049  -0.0026 830  GLY A O   
6108  N N   . ASP A 833  ? 0.2496 0.1945 0.2263 0.0130  0.0054  -0.0002 831  ASP A N   
6109  C CA  . ASP A 833  ? 0.2337 0.1799 0.2093 0.0141  0.0053  -0.0017 831  ASP A CA  
6110  C C   . ASP A 833  ? 0.2295 0.1745 0.2069 0.0140  0.0032  -0.0035 831  ASP A C   
6111  O O   . ASP A 833  ? 0.2521 0.1983 0.2292 0.0156  0.0028  -0.0056 831  ASP A O   
6112  C CB  . ASP A 833  ? 0.2522 0.1991 0.2262 0.0133  0.0059  -0.0008 831  ASP A CB  
6113  C CG  . ASP A 833  ? 0.2658 0.2138 0.2387 0.0137  0.0077  0.0006  831  ASP A CG  
6114  O OD1 . ASP A 833  ? 0.3175 0.2665 0.2904 0.0149  0.0085  0.0008  831  ASP A OD1 
6115  O OD2 . ASP A 833  ? 0.2753 0.2235 0.2476 0.0129  0.0081  0.0014  831  ASP A OD2 
6116  N N   . VAL A 834  ? 0.2338 0.1768 0.2134 0.0123  0.0018  -0.0026 832  VAL A N   
6117  C CA  . VAL A 834  ? 0.2297 0.1712 0.2122 0.0120  -0.0005 -0.0038 832  VAL A CA  
6118  C C   . VAL A 834  ? 0.2652 0.2061 0.2498 0.0137  -0.0013 -0.0059 832  VAL A C   
6119  O O   . VAL A 834  ? 0.2411 0.1823 0.2271 0.0150  -0.0026 -0.0086 832  VAL A O   
6120  C CB  . VAL A 834  ? 0.2375 0.1774 0.2220 0.0094  -0.0017 -0.0015 832  VAL A CB  
6121  C CG1 . VAL A 834  ? 0.2432 0.1812 0.2318 0.0090  -0.0044 -0.0023 832  VAL A CG1 
6122  C CG2 . VAL A 834  ? 0.2595 0.2008 0.2422 0.0079  -0.0011 -0.0002 832  VAL A CG2 
6123  N N   . ILE A 835  ? 0.2565 0.1970 0.2417 0.0138  -0.0007 -0.0050 833  ILE A N   
6124  C CA  . ILE A 835  ? 0.2490 0.1895 0.2365 0.0156  -0.0014 -0.0070 833  ILE A CA  
6125  C C   . ILE A 835  ? 0.2579 0.2015 0.2436 0.0182  -0.0005 -0.0098 833  ILE A C   
6126  O O   . ILE A 835  ? 0.2830 0.2271 0.2707 0.0199  -0.0018 -0.0129 833  ILE A O   
6127  C CB  . ILE A 835  ? 0.2628 0.2031 0.2508 0.0154  -0.0006 -0.0053 833  ILE A CB  
6128  C CG1 . ILE A 835  ? 0.3133 0.2510 0.3039 0.0130  -0.0021 -0.0029 833  ILE A CG1 
6129  C CG2 . ILE A 835  ? 0.3185 0.2599 0.3081 0.0177  -0.0007 -0.0077 833  ILE A CG2 
6130  C CD1 . ILE A 835  ? 0.3361 0.2716 0.3315 0.0131  -0.0048 -0.0040 833  ILE A CD1 
6131  N N   . THR A 836  ? 0.2599 0.2059 0.2419 0.0186  0.0017  -0.0087 834  THR A N   
6132  C CA  . THR A 836  ? 0.2684 0.2182 0.2483 0.0209  0.0027  -0.0107 834  THR A CA  
6133  C C   . THR A 836  ? 0.2584 0.2087 0.2383 0.0214  0.0014  -0.0130 834  THR A C   
6134  O O   . THR A 836  ? 0.2870 0.2394 0.2676 0.0233  0.0006  -0.0163 834  THR A O   
6135  C CB  . THR A 836  ? 0.3139 0.2658 0.2906 0.0208  0.0051  -0.0082 834  THR A CB  
6136  O OG1 . THR A 836  ? 0.3840 0.3359 0.3612 0.0206  0.0062  -0.0065 834  THR A OG1 
6137  C CG2 . THR A 836  ? 0.3524 0.3088 0.3268 0.0228  0.0061  -0.0094 834  THR A CG2 
6138  N N   . SER A 837  ? 0.2713 0.2200 0.2505 0.0196  0.0010  -0.0116 835  SER A N   
6139  C CA  . SER A 837  ? 0.2465 0.1961 0.2254 0.0201  0.0000  -0.0136 835  SER A CA  
6140  C C   . SER A 837  ? 0.2399 0.1876 0.2229 0.0203  -0.0027 -0.0164 835  SER A C   
6141  O O   . SER A 837  ? 0.2533 0.2028 0.2366 0.0217  -0.0038 -0.0195 835  SER A O   
6142  C CB  . SER A 837  ? 0.2408 0.1893 0.2185 0.0181  0.0002  -0.0113 835  SER A CB  
6143  O OG  . SER A 837  ? 0.2459 0.1960 0.2206 0.0180  0.0024  -0.0091 835  SER A OG  
6144  N N   . ALA A 838  ? 0.2360 0.1804 0.2224 0.0189  -0.0041 -0.0153 836  ALA A N   
6145  C CA  . ALA A 838  ? 0.2460 0.1881 0.2372 0.0188  -0.0070 -0.0175 836  ALA A CA  
6146  C C   . ALA A 838  ? 0.2534 0.1963 0.2472 0.0211  -0.0080 -0.0210 836  ALA A C   
6147  O O   . ALA A 838  ? 0.2664 0.2091 0.2637 0.0223  -0.0102 -0.0245 836  ALA A O   
6148  C CB  . ALA A 838  ? 0.2477 0.1862 0.2421 0.0160  -0.0084 -0.0144 836  ALA A CB  
6149  N N   . PHE A 839  ? 0.2478 0.1917 0.2406 0.0219  -0.0064 -0.0202 837  PHE A N   
6150  C CA  . PHE A 839  ? 0.2666 0.2109 0.2628 0.0238  -0.0075 -0.0231 837  PHE A CA  
6151  C C   . PHE A 839  ? 0.2659 0.2152 0.2593 0.0266  -0.0055 -0.0253 837  PHE A C   
6152  O O   . PHE A 839  ? 0.2841 0.2348 0.2805 0.0287  -0.0066 -0.0289 837  PHE A O   
6153  C CB  . PHE A 839  ? 0.2727 0.2137 0.2719 0.0224  -0.0081 -0.0205 837  PHE A CB  
6154  C CG  . PHE A 839  ? 0.2478 0.1847 0.2500 0.0196  -0.0101 -0.0180 837  PHE A CG  
6155  C CD1 . PHE A 839  ? 0.2827 0.2176 0.2895 0.0195  -0.0131 -0.0201 837  PHE A CD1 
6156  C CD2 . PHE A 839  ? 0.2879 0.2234 0.2886 0.0172  -0.0091 -0.0135 837  PHE A CD2 
6157  C CE1 . PHE A 839  ? 0.2779 0.2097 0.2880 0.0168  -0.0150 -0.0172 837  PHE A CE1 
6158  C CE2 . PHE A 839  ? 0.3180 0.2508 0.3214 0.0146  -0.0109 -0.0109 837  PHE A CE2 
6159  C CZ  . PHE A 839  ? 0.2910 0.2219 0.2991 0.0143  -0.0138 -0.0125 837  PHE A CZ  
6160  N N   . ASP A 840  ? 0.2792 0.2317 0.2676 0.0267  -0.0029 -0.0234 838  ASP A N   
6161  C CA  . ASP A 840  ? 0.2988 0.2570 0.2846 0.0292  -0.0012 -0.0253 838  ASP A CA  
6162  C C   . ASP A 840  ? 0.3150 0.2760 0.3023 0.0315  -0.0029 -0.0304 838  ASP A C   
6163  O O   . ASP A 840  ? 0.2842 0.2436 0.2723 0.0309  -0.0045 -0.0317 838  ASP A O   
6164  C CB  . ASP A 840  ? 0.3300 0.2909 0.3108 0.0287  0.0013  -0.0222 838  ASP A CB  
6165  C CG  . ASP A 840  ? 0.4360 0.4034 0.4140 0.0310  0.0032  -0.0230 838  ASP A CG  
6166  O OD1 . ASP A 840  ? 0.4424 0.4140 0.4194 0.0328  0.0028  -0.0260 838  ASP A OD1 
6167  O OD2 . ASP A 840  ? 0.4916 0.4604 0.4686 0.0309  0.0051  -0.0205 838  ASP A OD2 
6168  N N   . SER A 841  ? 0.2850 0.2504 0.2730 0.0341  -0.0027 -0.0338 839  SER A N   
6169  C CA  . SER A 841  ? 0.2823 0.2513 0.2721 0.0366  -0.0044 -0.0395 839  SER A CA  
6170  C C   . SER A 841  ? 0.2643 0.2280 0.2599 0.0360  -0.0079 -0.0422 839  SER A C   
6171  O O   . SER A 841  ? 0.2597 0.2248 0.2569 0.0373  -0.0098 -0.0464 839  SER A O   
6172  C CB  . SER A 841  ? 0.3527 0.3267 0.3380 0.0374  -0.0034 -0.0401 839  SER A CB  
6173  O OG  . SER A 841  ? 0.3826 0.3608 0.3631 0.0375  -0.0003 -0.0366 839  SER A OG  
6174  N N   . ALA A 842  ? 0.2840 0.2419 0.2832 0.0341  -0.0090 -0.0397 840  ALA A N   
6175  C CA  . ALA A 842  ? 0.2428 0.1954 0.2482 0.0331  -0.0125 -0.0412 840  ALA A CA  
6176  C C   . ALA A 842  ? 0.2426 0.1935 0.2475 0.0316  -0.0136 -0.0408 840  ALA A C   
6177  O O   . ALA A 842  ? 0.2731 0.2222 0.2827 0.0319  -0.0166 -0.0441 840  ALA A O   
6178  C CB  . ALA A 842  ? 0.2637 0.2174 0.2748 0.0358  -0.0150 -0.0471 840  ALA A CB  
6179  N N   . GLY A 843  ? 0.2482 0.1996 0.2478 0.0300  -0.0114 -0.0368 841  GLY A N   
6180  C CA  . GLY A 843  ? 0.2558 0.2061 0.2546 0.0286  -0.0121 -0.0361 841  GLY A CA  
6181  C C   . GLY A 843  ? 0.2455 0.2001 0.2434 0.0308  -0.0128 -0.0408 841  GLY A C   
6182  O O   . GLY A 843  ? 0.2473 0.2010 0.2456 0.0299  -0.0140 -0.0410 841  GLY A O   
6183  N N   . GLN A 844  ? 0.2490 0.2089 0.2457 0.0338  -0.0120 -0.0444 842  GLN A N   
6184  C CA  . GLN A 844  ? 0.2414 0.2065 0.2372 0.0362  -0.0128 -0.0493 842  GLN A CA  
6185  C C   . GLN A 844  ? 0.2747 0.2451 0.2636 0.0366  -0.0099 -0.0471 842  GLN A C   
6186  O O   . GLN A 844  ? 0.2754 0.2525 0.2613 0.0390  -0.0086 -0.0494 842  GLN A O   
6187  C CB  . GLN A 844  ? 0.2426 0.2113 0.2415 0.0393  -0.0139 -0.0550 842  GLN A CB  
6188  C CG  . GLN A 844  ? 0.2444 0.2074 0.2512 0.0389  -0.0174 -0.0574 842  GLN A CG  
6189  C CD  . GLN A 844  ? 0.2561 0.2218 0.2668 0.0418  -0.0184 -0.0623 842  GLN A CD  
6190  O OE1 . GLN A 844  ? 0.2723 0.2382 0.2885 0.0435  -0.0214 -0.0681 842  GLN A OE1 
6191  N NE2 . GLN A 844  ? 0.2678 0.2355 0.2761 0.0423  -0.0159 -0.0602 842  GLN A NE2 
6192  N N   . ARG A 845  ? 0.2542 0.2215 0.2408 0.0340  -0.0089 -0.0425 843  ARG A N   
6193  C CA  . ARG A 845  ? 0.2417 0.2127 0.2228 0.0339  -0.0069 -0.0402 843  ARG A CA  
6194  C C   . ARG A 845  ? 0.2412 0.2093 0.2231 0.0323  -0.0084 -0.0399 843  ARG A C   
6195  O O   . ARG A 845  ? 0.2622 0.2246 0.2475 0.0300  -0.0099 -0.0384 843  ARG A O   
6196  C CB  . ARG A 845  ? 0.2955 0.2653 0.2733 0.0323  -0.0041 -0.0344 843  ARG A CB  
6197  C CG  . ARG A 845  ? 0.2733 0.2464 0.2497 0.0336  -0.0021 -0.0337 843  ARG A CG  
6198  C CD  . ARG A 845  ? 0.3755 0.3470 0.3493 0.0318  0.0003  -0.0281 843  ARG A CD  
6199  N NE  . ARG A 845  ? 0.4202 0.3948 0.3930 0.0328  0.0022  -0.0269 843  ARG A NE  
6200  C CZ  . ARG A 845  ? 0.5131 0.4936 0.4824 0.0341  0.0042  -0.0257 843  ARG A CZ  
6201  N NH1 . ARG A 845  ? 0.4310 0.4153 0.3975 0.0346  0.0046  -0.0253 843  ARG A NH1 
6202  N NH2 . ARG A 845  ? 0.5054 0.4887 0.4745 0.0349  0.0058  -0.0245 843  ARG A NH2 
6203  N N   . CYS A 846  ? 0.2391 0.2116 0.2181 0.0334  -0.0082 -0.0412 844  CYS A N   
6204  C CA  . CYS A 846  ? 0.2494 0.2196 0.2292 0.0318  -0.0096 -0.0408 844  CYS A CA  
6205  C C   . CYS A 846  ? 0.2463 0.2125 0.2246 0.0290  -0.0082 -0.0352 844  CYS A C   
6206  O O   . CYS A 846  ? 0.2285 0.1910 0.2089 0.0270  -0.0095 -0.0342 844  CYS A O   
6207  C CB  . CYS A 846  ? 0.2471 0.2232 0.2237 0.0335  -0.0095 -0.0429 844  CYS A CB  
6208  S SG  . CYS A 846  ? 0.2752 0.2575 0.2453 0.0346  -0.0059 -0.0395 844  CYS A SG  
6209  N N   . SER A 847  ? 0.2320 0.1993 0.2069 0.0288  -0.0055 -0.0317 845  SER A N   
6210  C CA  . SER A 847  ? 0.2220 0.1863 0.1955 0.0265  -0.0040 -0.0268 845  SER A CA  
6211  C C   . SER A 847  ? 0.2316 0.1907 0.2081 0.0246  -0.0045 -0.0250 845  SER A C   
6212  O O   . SER A 847  ? 0.2362 0.1931 0.2119 0.0226  -0.0034 -0.0213 845  SER A O   
6213  C CB  . SER A 847  ? 0.2280 0.1957 0.1975 0.0273  -0.0013 -0.0241 845  SER A CB  
6214  O OG  . SER A 847  ? 0.2589 0.2286 0.2288 0.0289  -0.0007 -0.0254 845  SER A OG  
6215  N N   . ALA A 848  ? 0.2380 0.1956 0.2182 0.0251  -0.0061 -0.0275 846  ALA A N   
6216  C CA  . ALA A 848  ? 0.2308 0.1842 0.2138 0.0235  -0.0064 -0.0254 846  ALA A CA  
6217  C C   . ALA A 848  ? 0.2307 0.1801 0.2154 0.0206  -0.0074 -0.0226 846  ALA A C   
6218  O O   . ALA A 848  ? 0.2399 0.1887 0.2259 0.0199  -0.0089 -0.0235 846  ALA A O   
6219  C CB  . ALA A 848  ? 0.2497 0.2021 0.2372 0.0248  -0.0085 -0.0289 846  ALA A CB  
6220  N N   . LEU A 849  ? 0.2385 0.1856 0.2233 0.0189  -0.0064 -0.0192 847  LEU A N   
6221  C CA  . LEU A 849  ? 0.2424 0.1867 0.2287 0.0161  -0.0072 -0.0163 847  LEU A CA  
6222  C C   . LEU A 849  ? 0.2494 0.1907 0.2414 0.0151  -0.0102 -0.0173 847  LEU A C   
6223  O O   . LEU A 849  ? 0.2477 0.1875 0.2426 0.0156  -0.0112 -0.0181 847  LEU A O   
6224  C CB  . LEU A 849  ? 0.2456 0.1890 0.2305 0.0147  -0.0054 -0.0128 847  LEU A CB  
6225  C CG  . LEU A 849  ? 0.2304 0.1719 0.2170 0.0118  -0.0062 -0.0097 847  LEU A CG  
6226  C CD1 . LEU A 849  ? 0.2602 0.2031 0.2450 0.0108  -0.0058 -0.0090 847  LEU A CD1 
6227  C CD2 . LEU A 849  ? 0.2522 0.1933 0.2376 0.0108  -0.0047 -0.0069 847  LEU A CD2 
6228  N N   . ARG A 850  ? 0.2334 0.1740 0.2274 0.0138  -0.0119 -0.0173 848  ARG A N   
6229  C CA  . ARG A 850  ? 0.2539 0.1917 0.2541 0.0126  -0.0150 -0.0179 848  ARG A CA  
6230  C C   . ARG A 850  ? 0.2535 0.1895 0.2557 0.0093  -0.0157 -0.0135 848  ARG A C   
6231  O O   . ARG A 850  ? 0.2741 0.2075 0.2816 0.0080  -0.0180 -0.0125 848  ARG A O   
6232  C CB  . ARG A 850  ? 0.2722 0.2107 0.2744 0.0134  -0.0170 -0.0212 848  ARG A CB  
6233  C CG  . ARG A 850  ? 0.2700 0.2115 0.2697 0.0166  -0.0164 -0.0257 848  ARG A CG  
6234  C CD  . ARG A 850  ? 0.2823 0.2234 0.2843 0.0186  -0.0171 -0.0284 848  ARG A CD  
6235  N NE  . ARG A 850  ? 0.2773 0.2223 0.2772 0.0218  -0.0167 -0.0329 848  ARG A NE  
6236  C CZ  . ARG A 850  ? 0.2800 0.2268 0.2804 0.0241  -0.0165 -0.0358 848  ARG A CZ  
6237  N NH1 . ARG A 850  ? 0.2767 0.2210 0.2796 0.0238  -0.0167 -0.0346 848  ARG A NH1 
6238  N NH2 . ARG A 850  ? 0.2656 0.2171 0.2639 0.0269  -0.0161 -0.0399 848  ARG A NH2 
6239  N N   . VAL A 851  ? 0.2578 0.1955 0.2562 0.0079  -0.0138 -0.0108 849  VAL A N   
6240  C CA  . VAL A 851  ? 0.2515 0.1889 0.2515 0.0048  -0.0142 -0.0068 849  VAL A CA  
6241  C C   . VAL A 851  ? 0.2472 0.1865 0.2424 0.0042  -0.0114 -0.0042 849  VAL A C   
6242  O O   . VAL A 851  ? 0.2605 0.2019 0.2517 0.0049  -0.0094 -0.0047 849  VAL A O   
6243  C CB  . VAL A 851  ? 0.3142 0.2526 0.3155 0.0034  -0.0154 -0.0065 849  VAL A CB  
6244  C CG1 . VAL A 851  ? 0.3555 0.2942 0.3589 0.0001  -0.0160 -0.0021 849  VAL A CG1 
6245  C CG2 . VAL A 851  ? 0.3571 0.2939 0.3630 0.0043  -0.0182 -0.0098 849  VAL A CG2 
6246  N N   . LEU A 852  ? 0.2472 0.1857 0.2433 0.0030  -0.0112 -0.0017 850  LEU A N   
6247  C CA  . LEU A 852  ? 0.2561 0.1965 0.2486 0.0021  -0.0089 0.0007  850  LEU A CA  
6248  C C   . LEU A 852  ? 0.2358 0.1779 0.2295 -0.0008 -0.0094 0.0040  850  LEU A C   
6249  O O   . LEU A 852  ? 0.2449 0.1861 0.2428 -0.0027 -0.0116 0.0060  850  LEU A O   
6250  C CB  . LEU A 852  ? 0.2376 0.1767 0.2306 0.0024  -0.0086 0.0016  850  LEU A CB  
6251  C CG  . LEU A 852  ? 0.2546 0.1956 0.2446 0.0014  -0.0066 0.0039  850  LEU A CG  
6252  C CD1 . LEU A 852  ? 0.2350 0.1776 0.2205 0.0030  -0.0041 0.0024  850  LEU A CD1 
6253  C CD2 . LEU A 852  ? 0.2391 0.1786 0.2303 0.0016  -0.0067 0.0047  850  LEU A CD2 
6254  N N   . CYS A 853  ? 0.2359 0.1808 0.2262 -0.0013 -0.0076 0.0045  851  CYS A N   
6255  C CA  . CYS A 853  ? 0.2505 0.1983 0.2414 -0.0039 -0.0078 0.0072  851  CYS A CA  
6256  C C   . CYS A 853  ? 0.2232 0.1736 0.2113 -0.0045 -0.0059 0.0088  851  CYS A C   
6257  O O   . CYS A 853  ? 0.2435 0.1949 0.2281 -0.0032 -0.0039 0.0073  851  CYS A O   
6258  C CB  . CYS A 853  ? 0.2443 0.1940 0.2340 -0.0037 -0.0075 0.0060  851  CYS A CB  
6259  S SG  . CYS A 853  ? 0.2787 0.2258 0.2709 -0.0023 -0.0094 0.0030  851  CYS A SG  
6260  N N   . LEU A 854  ? 0.2244 0.1760 0.2144 -0.0067 -0.0067 0.0118  852  LEU A N   
6261  C CA  . LEU A 854  ? 0.2468 0.2010 0.2346 -0.0073 -0.0052 0.0132  852  LEU A CA  
6262  C C   . LEU A 854  ? 0.2466 0.2060 0.2342 -0.0097 -0.0050 0.0155  852  LEU A C   
6263  O O   . LEU A 854  ? 0.2597 0.2204 0.2504 -0.0119 -0.0068 0.0182  852  LEU A O   
6264  C CB  . LEU A 854  ? 0.2463 0.1986 0.2363 -0.0078 -0.0064 0.0149  852  LEU A CB  
6265  C CG  . LEU A 854  ? 0.2547 0.2026 0.2452 -0.0055 -0.0066 0.0126  852  LEU A CG  
6266  C CD1 . LEU A 854  ? 0.2675 0.2138 0.2608 -0.0062 -0.0079 0.0146  852  LEU A CD1 
6267  C CD2 . LEU A 854  ? 0.2772 0.2251 0.2637 -0.0033 -0.0041 0.0102  852  LEU A CD2 
6268  N N   . GLN A 855  ? 0.2380 0.2006 0.2223 -0.0093 -0.0030 0.0145  853  GLN A N   
6269  C CA  . GLN A 855  ? 0.2288 0.1974 0.2128 -0.0114 -0.0026 0.0164  853  GLN A CA  
6270  C C   . GLN A 855  ? 0.2703 0.2411 0.2559 -0.0136 -0.0037 0.0199  853  GLN A C   
6271  O O   . GLN A 855  ? 0.2643 0.2331 0.2498 -0.0130 -0.0037 0.0201  853  GLN A O   
6272  C CB  . GLN A 855  ? 0.2398 0.2115 0.2205 -0.0103 -0.0004 0.0141  853  GLN A CB  
6273  C CG  . GLN A 855  ? 0.2640 0.2426 0.2444 -0.0121 0.0000  0.0151  853  GLN A CG  
6274  C CD  . GLN A 855  ? 0.2927 0.2747 0.2706 -0.0110 0.0019  0.0125  853  GLN A CD  
6275  O OE1 . GLN A 855  ? 0.3316 0.3108 0.3083 -0.0088 0.0029  0.0097  853  GLN A OE1 
6276  N NE2 . GLN A 855  ? 0.3246 0.3131 0.3020 -0.0125 0.0023  0.0135  853  GLN A NE2 
6277  N N   . GLU A 856  ? 0.2828 0.2580 0.2704 -0.0162 -0.0047 0.0230  854  GLU A N   
6278  C CA  . GLU A 856  ? 0.3033 0.2803 0.2934 -0.0185 -0.0063 0.0273  854  GLU A CA  
6279  C C   . GLU A 856  ? 0.2875 0.2672 0.2755 -0.0185 -0.0053 0.0276  854  GLU A C   
6280  O O   . GLU A 856  ? 0.3048 0.2826 0.2946 -0.0191 -0.0065 0.0298  854  GLU A O   
6281  C CB  . GLU A 856  ? 0.3124 0.2954 0.3044 -0.0214 -0.0072 0.0307  854  GLU A CB  
6282  C CG  . GLU A 856  ? 0.3212 0.3076 0.3159 -0.0241 -0.0088 0.0359  854  GLU A CG  
6283  C CD  . GLU A 856  ? 0.4773 0.4573 0.4765 -0.0243 -0.0113 0.0377  854  GLU A CD  
6284  O OE1 . GLU A 856  ? 0.4456 0.4204 0.4474 -0.0235 -0.0125 0.0362  854  GLU A OE1 
6285  O OE2 . GLU A 856  ? 0.4768 0.4571 0.4772 -0.0251 -0.0121 0.0403  854  GLU A OE2 
6286  N N   . ASP A 857  ? 0.2978 0.2816 0.2823 -0.0178 -0.0032 0.0253  855  ASP A N   
6287  C CA  . ASP A 857  ? 0.3350 0.3223 0.3176 -0.0179 -0.0024 0.0254  855  ASP A CA  
6288  C C   . ASP A 857  ? 0.3431 0.3247 0.3254 -0.0160 -0.0022 0.0238  855  ASP A C   
6289  O O   . ASP A 857  ? 0.3727 0.3564 0.3545 -0.0165 -0.0021 0.0247  855  ASP A O   
6290  C CB  . ASP A 857  ? 0.4043 0.3972 0.3840 -0.0172 -0.0004 0.0225  855  ASP A CB  
6291  N N   . VAL A 858  ? 0.2763 0.2514 0.2589 -0.0139 -0.0021 0.0215  856  VAL A N   
6292  C CA  . VAL A 858  ? 0.3015 0.2717 0.2839 -0.0121 -0.0018 0.0200  856  VAL A CA  
6293  C C   . VAL A 858  ? 0.2585 0.2232 0.2438 -0.0118 -0.0036 0.0210  856  VAL A C   
6294  O O   . VAL A 858  ? 0.2789 0.2397 0.2644 -0.0102 -0.0035 0.0199  856  VAL A O   
6295  C CB  . VAL A 858  ? 0.2636 0.2317 0.2435 -0.0096 0.0000  0.0161  856  VAL A CB  
6296  C CG1 . VAL A 858  ? 0.3127 0.2860 0.2905 -0.0097 0.0015  0.0148  856  VAL A CG1 
6297  C CG2 . VAL A 858  ? 0.2752 0.2411 0.2551 -0.0086 0.0001  0.0145  856  VAL A CG2 
6298  N N   . ALA A 859  ? 0.2624 0.2268 0.2505 -0.0132 -0.0053 0.0230  857  ALA A N   
6299  C CA  . ALA A 859  ? 0.2593 0.2183 0.2508 -0.0125 -0.0071 0.0230  857  ALA A CA  
6300  C C   . ALA A 859  ? 0.2763 0.2332 0.2702 -0.0128 -0.0085 0.0249  857  ALA A C   
6301  O O   . ALA A 859  ? 0.2594 0.2116 0.2546 -0.0109 -0.0089 0.0230  857  ALA A O   
6302  C CB  . ALA A 859  ? 0.2807 0.2402 0.2754 -0.0142 -0.0090 0.0249  857  ALA A CB  
6303  N N   . ASP A 860  ? 0.2889 0.2497 0.2836 -0.0150 -0.0091 0.0285  858  ASP A N   
6304  C CA  . ASP A 860  ? 0.3002 0.2593 0.2978 -0.0154 -0.0106 0.0306  858  ASP A CA  
6305  C C   . ASP A 860  ? 0.2752 0.2322 0.2703 -0.0132 -0.0091 0.0279  858  ASP A C   
6306  O O   . ASP A 860  ? 0.3049 0.2576 0.3024 -0.0120 -0.0101 0.0274  858  ASP A O   
6307  C CB  . ASP A 860  ? 0.2999 0.2647 0.2985 -0.0183 -0.0116 0.0353  858  ASP A CB  
6308  C CG  . ASP A 860  ? 0.4036 0.3698 0.4062 -0.0208 -0.0137 0.0391  858  ASP A CG  
6309  O OD1 . ASP A 860  ? 0.4579 0.4191 0.4643 -0.0203 -0.0155 0.0385  858  ASP A OD1 
6310  O OD2 . ASP A 860  ? 0.6277 0.6004 0.6299 -0.0233 -0.0138 0.0425  858  ASP A OD2 
6311  N N   . ARG A 861  ? 0.2721 0.2322 0.2631 -0.0127 -0.0068 0.0262  859  ARG A N   
6312  C CA  . ARG A 861  ? 0.2971 0.2555 0.2862 -0.0108 -0.0054 0.0239  859  ARG A CA  
6313  C C   . ARG A 861  ? 0.2772 0.2303 0.2664 -0.0082 -0.0049 0.0207  859  ARG A C   
6314  O O   . ARG A 861  ? 0.2786 0.2287 0.2688 -0.0069 -0.0051 0.0200  859  ARG A O   
6315  C CB  . ARG A 861  ? 0.3583 0.3210 0.3437 -0.0107 -0.0033 0.0224  859  ARG A CB  
6316  C CG  . ARG A 861  ? 0.4763 0.4372 0.4602 -0.0089 -0.0020 0.0201  859  ARG A CG  
6317  C CD  . ARG A 861  ? 0.5923 0.5579 0.5737 -0.0091 -0.0005 0.0188  859  ARG A CD  
6318  N NE  . ARG A 861  ? 0.7177 0.6811 0.6985 -0.0074 0.0006  0.0167  859  ARG A NE  
6319  C CZ  . ARG A 861  ? 0.6904 0.6516 0.6701 -0.0055 0.0020  0.0140  859  ARG A CZ  
6320  N NH1 . ARG A 861  ? 0.6703 0.6313 0.6491 -0.0050 0.0026  0.0127  859  ARG A NH1 
6321  N NH2 . ARG A 861  ? 0.5975 0.5570 0.5773 -0.0042 0.0028  0.0127  859  ARG A NH2 
6322  N N   . ILE A 862  ? 0.2579 0.2103 0.2461 -0.0074 -0.0044 0.0189  860  ILE A N   
6323  C CA  . ILE A 862  ? 0.2820 0.2305 0.2700 -0.0050 -0.0039 0.0159  860  ILE A CA  
6324  C C   . ILE A 862  ? 0.2854 0.2301 0.2773 -0.0045 -0.0060 0.0161  860  ILE A C   
6325  O O   . ILE A 862  ? 0.2473 0.1893 0.2397 -0.0025 -0.0058 0.0142  860  ILE A O   
6326  C CB  . ILE A 862  ? 0.2639 0.2130 0.2499 -0.0043 -0.0030 0.0140  860  ILE A CB  
6327  C CG1 . ILE A 862  ? 0.2990 0.2510 0.2817 -0.0041 -0.0008 0.0130  860  ILE A CG1 
6328  C CG2 . ILE A 862  ? 0.2778 0.2233 0.2641 -0.0020 -0.0029 0.0113  860  ILE A CG2 
6329  C CD1 . ILE A 862  ? 0.3002 0.2535 0.2812 -0.0037 0.0000  0.0115  860  ILE A CD1 
6330  N N   . LEU A 863  ? 0.2491 0.1940 0.2443 -0.0064 -0.0081 0.0185  861  LEU A N   
6331  C CA  A LEU A 863  ? 0.2443 0.1856 0.2443 -0.0060 -0.0106 0.0185  861  LEU A CA  
6332  C CA  B LEU A 863  ? 0.2443 0.1855 0.2442 -0.0060 -0.0106 0.0185  861  LEU A CA  
6333  C C   . LEU A 863  ? 0.2626 0.2024 0.2644 -0.0056 -0.0112 0.0194  861  LEU A C   
6334  O O   . LEU A 863  ? 0.2500 0.1865 0.2542 -0.0038 -0.0120 0.0174  861  LEU A O   
6335  C CB  A LEU A 863  ? 0.2792 0.2210 0.2831 -0.0084 -0.0130 0.0215  861  LEU A CB  
6336  C CB  B LEU A 863  ? 0.2795 0.2216 0.2833 -0.0085 -0.0129 0.0216  861  LEU A CB  
6337  C CG  A LEU A 863  ? 0.2935 0.2347 0.2979 -0.0082 -0.0135 0.0199  861  LEU A CG  
6338  C CG  B LEU A 863  ? 0.2949 0.2331 0.3046 -0.0083 -0.0159 0.0214  861  LEU A CG  
6339  C CD1 A LEU A 863  ? 0.2856 0.2280 0.2944 -0.0110 -0.0159 0.0235  861  LEU A CD1 
6340  C CD1 B LEU A 863  ? 0.2812 0.2165 0.2902 -0.0054 -0.0154 0.0166  861  LEU A CD1 
6341  C CD2 A LEU A 863  ? 0.3295 0.2666 0.3358 -0.0056 -0.0142 0.0160  861  LEU A CD2 
6342  C CD2 B LEU A 863  ? 0.3312 0.2709 0.3441 -0.0110 -0.0178 0.0246  861  LEU A CD2 
6343  N N   . THR A 864  ? 0.2599 0.2026 0.2609 -0.0073 -0.0109 0.0222  862  THR A N   
6344  C CA  . THR A 864  ? 0.2669 0.2086 0.2694 -0.0069 -0.0114 0.0231  862  THR A CA  
6345  C C   . THR A 864  ? 0.2484 0.1883 0.2486 -0.0041 -0.0095 0.0195  862  THR A C   
6346  O O   . THR A 864  ? 0.2336 0.1709 0.2363 -0.0027 -0.0102 0.0185  862  THR A O   
6347  C CB  . THR A 864  ? 0.2787 0.2247 0.2796 -0.0090 -0.0110 0.0262  862  THR A CB  
6348  O OG1 . THR A 864  ? 0.3127 0.2608 0.3166 -0.0116 -0.0130 0.0302  862  THR A OG1 
6349  C CG2 . THR A 864  ? 0.2873 0.2326 0.2893 -0.0084 -0.0112 0.0268  862  THR A CG2 
6350  N N   . MET A 865  ? 0.2359 0.1776 0.2316 -0.0034 -0.0070 0.0177  863  MET A N   
6351  C CA  . MET A 865  ? 0.2387 0.1792 0.2323 -0.0010 -0.0052 0.0150  863  MET A CA  
6352  C C   . MET A 865  ? 0.2343 0.1720 0.2292 0.0011  -0.0056 0.0122  863  MET A C   
6353  O O   . MET A 865  ? 0.2264 0.1628 0.2221 0.0030  -0.0052 0.0106  863  MET A O   
6354  C CB  . MET A 865  ? 0.2481 0.1910 0.2375 -0.0009 -0.0028 0.0139  863  MET A CB  
6355  C CG  . MET A 865  ? 0.2920 0.2342 0.2796 0.0012  -0.0009 0.0119  863  MET A CG  
6356  S SD  . MET A 865  ? 0.3314 0.2762 0.3154 0.0012  0.0013  0.0110  863  MET A SD  
6357  C CE  . MET A 865  ? 0.3515 0.2998 0.3354 -0.0015 0.0007  0.0133  863  MET A CE  
6358  N N   . LEU A 866  ? 0.2278 0.1651 0.2232 0.0009  -0.0063 0.0115  864  LEU A N   
6359  C CA  . LEU A 866  ? 0.2230 0.1583 0.2197 0.0030  -0.0069 0.0086  864  LEU A CA  
6360  C C   . LEU A 866  ? 0.2171 0.1499 0.2187 0.0036  -0.0092 0.0082  864  LEU A C   
6361  O O   . LEU A 866  ? 0.2319 0.1637 0.2341 0.0060  -0.0090 0.0053  864  LEU A O   
6362  C CB  . LEU A 866  ? 0.2358 0.1713 0.2328 0.0022  -0.0077 0.0083  864  LEU A CB  
6363  C CG  . LEU A 866  ? 0.2925 0.2264 0.2908 0.0043  -0.0085 0.0049  864  LEU A CG  
6364  C CD1 . LEU A 866  ? 0.3046 0.2394 0.2992 0.0068  -0.0062 0.0022  864  LEU A CD1 
6365  C CD2 . LEU A 866  ? 0.2990 0.2331 0.2977 0.0033  -0.0095 0.0048  864  LEU A CD2 
6366  N N   . LYS A 867  ? 0.2362 0.1683 0.2416 0.0016  -0.0114 0.0111  865  LYS A N   
6367  C CA  . LYS A 867  ? 0.2445 0.1739 0.2553 0.0022  -0.0138 0.0109  865  LYS A CA  
6368  C C   . LYS A 867  ? 0.2567 0.1861 0.2672 0.0035  -0.0129 0.0103  865  LYS A C   
6369  O O   . LYS A 867  ? 0.2518 0.1795 0.2653 0.0056  -0.0138 0.0079  865  LYS A O   
6370  C CB  . LYS A 867  ? 0.2851 0.2141 0.3005 -0.0005 -0.0166 0.0149  865  LYS A CB  
6371  C CG  . LYS A 867  ? 0.2873 0.2159 0.3046 -0.0017 -0.0181 0.0151  865  LYS A CG  
6372  C CD  . LYS A 867  ? 0.3302 0.2593 0.3516 -0.0049 -0.0205 0.0201  865  LYS A CD  
6373  C CE  . LYS A 867  ? 0.3991 0.3284 0.4223 -0.0063 -0.0218 0.0208  865  LYS A CE  
6374  N NZ  . LYS A 867  ? 0.4167 0.3477 0.4434 -0.0097 -0.0238 0.0263  865  LYS A NZ  
6375  N N   . GLY A 868  ? 0.2466 0.1781 0.2537 0.0025  -0.0111 0.0123  866  GLY A N   
6376  C CA  . GLY A 868  ? 0.2398 0.1715 0.2465 0.0038  -0.0100 0.0118  866  GLY A CA  
6377  C C   . GLY A 868  ? 0.2417 0.1736 0.2463 0.0066  -0.0082 0.0081  866  GLY A C   
6378  O O   . GLY A 868  ? 0.2618 0.1931 0.2683 0.0083  -0.0083 0.0066  866  GLY A O   
6379  N N   . ALA A 869  ? 0.2288 0.1619 0.2296 0.0070  -0.0065 0.0068  867  ALA A N   
6380  C CA  . ALA A 869  ? 0.2205 0.1544 0.2191 0.0095  -0.0047 0.0038  867  ALA A CA  
6381  C C   . ALA A 869  ? 0.2135 0.1463 0.2154 0.0115  -0.0063 0.0006  867  ALA A C   
6382  O O   . ALA A 869  ? 0.2473 0.1811 0.2493 0.0138  -0.0055 -0.0017 867  ALA A O   
6383  C CB  . ALA A 869  ? 0.2393 0.1749 0.2337 0.0094  -0.0028 0.0034  867  ALA A CB  
6384  N N   . LEU A 870  ? 0.2396 0.1707 0.2443 0.0107  -0.0085 0.0006  868  LEU A N   
6385  C CA  . LEU A 870  ? 0.2480 0.1779 0.2567 0.0125  -0.0105 -0.0028 868  LEU A CA  
6386  C C   . LEU A 870  ? 0.2682 0.1972 0.2808 0.0139  -0.0116 -0.0038 868  LEU A C   
6387  O O   . LEU A 870  ? 0.2781 0.2079 0.2922 0.0165  -0.0118 -0.0076 868  LEU A O   
6388  C CB  . LEU A 870  ? 0.2771 0.2048 0.2896 0.0107  -0.0133 -0.0017 868  LEU A CB  
6389  C CG  . LEU A 870  ? 0.3211 0.2472 0.3383 0.0123  -0.0158 -0.0053 868  LEU A CG  
6390  C CD1 . LEU A 870  ? 0.3540 0.2819 0.3677 0.0135  -0.0146 -0.0081 868  LEU A CD1 
6391  C CD2 . LEU A 870  ? 0.3615 0.2848 0.3847 0.0101  -0.0192 -0.0031 868  LEU A CD2 
6392  N N   . HIS A 871  ? 0.2337 0.1616 0.2484 0.0122  -0.0124 -0.0006 869  HIS A N   
6393  C CA  . HIS A 871  ? 0.2733 0.2001 0.2925 0.0134  -0.0138 -0.0014 869  HIS A CA  
6394  C C   . HIS A 871  ? 0.3055 0.2347 0.3221 0.0154  -0.0114 -0.0029 869  HIS A C   
6395  O O   . HIS A 871  ? 0.2977 0.2266 0.3180 0.0168  -0.0123 -0.0042 869  HIS A O   
6396  C CB  . HIS A 871  ? 0.3128 0.2379 0.3356 0.0110  -0.0158 0.0028  869  HIS A CB  
6397  C CG  . HIS A 871  ? 0.3541 0.2767 0.3816 0.0095  -0.0190 0.0039  869  HIS A CG  
6398  N ND1 . HIS A 871  ? 0.3868 0.3070 0.4209 0.0109  -0.0219 0.0014  869  HIS A ND1 
6399  C CD2 . HIS A 871  ? 0.3401 0.2627 0.3673 0.0068  -0.0197 0.0072  869  HIS A CD2 
6400  C CE1 . HIS A 871  ? 0.4034 0.3217 0.4413 0.0089  -0.0244 0.0033  869  HIS A CE1 
6401  N NE2 . HIS A 871  ? 0.3963 0.3162 0.4298 0.0064  -0.0231 0.0071  869  HIS A NE2 
6402  N N   . GLU A 872  ? 0.2374 0.1690 0.2484 0.0156  -0.0084 -0.0028 870  GLU A N   
6403  C CA  . GLU A 872  ? 0.2539 0.1882 0.2627 0.0174  -0.0061 -0.0040 870  GLU A CA  
6404  C C   . GLU A 872  ? 0.2538 0.1906 0.2616 0.0201  -0.0053 -0.0081 870  GLU A C   
6405  O O   . GLU A 872  ? 0.2673 0.2071 0.2733 0.0217  -0.0032 -0.0090 870  GLU A O   
6406  C CB  . GLU A 872  ? 0.2518 0.1877 0.2557 0.0160  -0.0035 -0.0014 870  GLU A CB  
6407  C CG  . GLU A 872  ? 0.2729 0.2075 0.2772 0.0134  -0.0041 0.0023  870  GLU A CG  
6408  C CD  . GLU A 872  ? 0.3083 0.2424 0.3160 0.0137  -0.0050 0.0029  870  GLU A CD  
6409  O OE1 . GLU A 872  ? 0.3232 0.2587 0.3317 0.0159  -0.0042 0.0008  870  GLU A OE1 
6410  O OE2 . GLU A 872  ? 0.3142 0.2470 0.3240 0.0118  -0.0066 0.0056  870  GLU A OE2 
6411  N N   . LEU A 873  ? 0.2560 0.1921 0.2652 0.0207  -0.0067 -0.0104 871  LEU A N   
6412  C CA  . LEU A 873  ? 0.2426 0.1818 0.2506 0.0234  -0.0060 -0.0145 871  LEU A CA  
6413  C C   . LEU A 873  ? 0.2650 0.2049 0.2777 0.0259  -0.0075 -0.0182 871  LEU A C   
6414  O O   . LEU A 873  ? 0.2892 0.2259 0.3074 0.0255  -0.0103 -0.0184 871  LEU A O   
6415  C CB  . LEU A 873  ? 0.2642 0.2026 0.2719 0.0232  -0.0072 -0.0159 871  LEU A CB  
6416  C CG  . LEU A 873  ? 0.2804 0.2186 0.2836 0.0210  -0.0058 -0.0129 871  LEU A CG  
6417  C CD1 . LEU A 873  ? 0.2776 0.2148 0.2815 0.0208  -0.0074 -0.0145 871  LEU A CD1 
6418  C CD2 . LEU A 873  ? 0.3206 0.2626 0.3187 0.0219  -0.0026 -0.0125 871  LEU A CD2 
6419  N N   . HIS A 874  ? 0.2670 0.2116 0.2780 0.0285  -0.0058 -0.0211 872  HIS A N   
6420  C CA  . HIS A 874  ? 0.2703 0.2170 0.2854 0.0313  -0.0069 -0.0254 872  HIS A CA  
6421  C C   . HIS A 874  ? 0.2324 0.1814 0.2481 0.0334  -0.0079 -0.0302 872  HIS A C   
6422  O O   . HIS A 874  ? 0.2566 0.2096 0.2674 0.0342  -0.0059 -0.0309 872  HIS A O   
6423  C CB  . HIS A 874  ? 0.2889 0.2405 0.3017 0.0327  -0.0042 -0.0253 872  HIS A CB  
6424  C CG  . HIS A 874  ? 0.2876 0.2423 0.3043 0.0358  -0.0050 -0.0298 872  HIS A CG  
6425  N ND1 . HIS A 874  ? 0.4074 0.3672 0.4229 0.0373  -0.0027 -0.0301 872  HIS A ND1 
6426  C CD2 . HIS A 874  ? 0.3604 0.3143 0.3828 0.0376  -0.0078 -0.0344 872  HIS A CD2 
6427  C CE1 . HIS A 874  ? 0.3816 0.3439 0.4015 0.0400  -0.0040 -0.0348 872  HIS A CE1 
6428  N NE2 . HIS A 874  ? 0.3256 0.2842 0.3498 0.0404  -0.0072 -0.0377 872  HIS A NE2 
6429  N N   . ILE A 875  ? 0.2612 0.2075 0.2829 0.0342  -0.0112 -0.0334 873  ILE A N   
6430  C CA  . ILE A 875  ? 0.2628 0.2109 0.2864 0.0363  -0.0128 -0.0387 873  ILE A CA  
6431  C C   . ILE A 875  ? 0.2879 0.2401 0.3152 0.0398  -0.0134 -0.0442 873  ILE A C   
6432  O O   . ILE A 875  ? 0.3037 0.2536 0.3363 0.0402  -0.0151 -0.0446 873  ILE A O   
6433  C CB  . ILE A 875  ? 0.2820 0.2244 0.3108 0.0347  -0.0164 -0.0388 873  ILE A CB  
6434  C CG1 . ILE A 875  ? 0.3796 0.3194 0.4042 0.0316  -0.0156 -0.0342 873  ILE A CG1 
6435  C CG2 . ILE A 875  ? 0.3194 0.2635 0.3515 0.0372  -0.0186 -0.0451 873  ILE A CG2 
6436  C CD1 . ILE A 875  ? 0.4485 0.3855 0.4713 0.0287  -0.0145 -0.0281 873  ILE A CD1 
6437  N N   . GLY A 876  ? 0.2794 0.2378 0.3040 0.0424  -0.0122 -0.0484 874  GLY A N   
6438  C CA  . GLY A 876  ? 0.2670 0.2304 0.2950 0.0459  -0.0128 -0.0541 874  GLY A CA  
6439  C C   . GLY A 876  ? 0.2990 0.2707 0.3227 0.0486  -0.0109 -0.0581 874  GLY A C   
6440  O O   . GLY A 876  ? 0.2740 0.2471 0.2925 0.0477  -0.0096 -0.0566 874  GLY A O   
6441  N N   . ARG A 877  ? 0.2924 0.2702 0.3185 0.0519  -0.0109 -0.0632 875  ARG A N   
6442  C CA  . ARG A 877  ? 0.2725 0.2598 0.2945 0.0546  -0.0090 -0.0670 875  ARG A CA  
6443  C C   . ARG A 877  ? 0.2594 0.2508 0.2737 0.0533  -0.0049 -0.0614 875  ARG A C   
6444  O O   . ARG A 877  ? 0.2741 0.2640 0.2876 0.0519  -0.0032 -0.0570 875  ARG A O   
6445  C CB  . ARG A 877  ? 0.3436 0.3370 0.3699 0.0584  -0.0097 -0.0733 875  ARG A CB  
6446  C CG  . ARG A 877  ? 0.3521 0.3553 0.3764 0.0617  -0.0091 -0.0794 875  ARG A CG  
6447  C CD  . ARG A 877  ? 0.3381 0.3475 0.3673 0.0655  -0.0100 -0.0861 875  ARG A CD  
6448  N NE  . ARG A 877  ? 0.3267 0.3432 0.3525 0.0662  -0.0065 -0.0837 875  ARG A NE  
6449  C CZ  . ARG A 877  ? 0.4312 0.4552 0.4597 0.0695  -0.0063 -0.0888 875  ARG A CZ  
6450  N NH1 . ARG A 877  ? 0.4357 0.4612 0.4708 0.0727  -0.0094 -0.0969 875  ARG A NH1 
6451  N NH2 . ARG A 877  ? 0.3859 0.4164 0.4111 0.0698  -0.0029 -0.0858 875  ARG A NH2 
6452  N N   . THR A 878  ? 0.2748 0.2712 0.2838 0.0536  -0.0033 -0.0614 876  THR A N   
6453  C CA  . THR A 878  ? 0.2382 0.2360 0.2404 0.0515  -0.0001 -0.0551 876  THR A CA  
6454  C C   . THR A 878  ? 0.2873 0.2942 0.2862 0.0529  0.0031  -0.0539 876  THR A C   
6455  O O   . THR A 878  ? 0.2761 0.2851 0.2699 0.0514  0.0057  -0.0489 876  THR A O   
6456  C CB  . THR A 878  ? 0.2686 0.2668 0.2670 0.0508  -0.0001 -0.0547 876  THR A CB  
6457  O OG1 . THR A 878  ? 0.3047 0.3100 0.3034 0.0539  -0.0010 -0.0611 876  THR A OG1 
6458  C CG2 . THR A 878  ? 0.3113 0.3000 0.3122 0.0483  -0.0026 -0.0534 876  THR A CG2 
6459  N N   . ASP A 879  ? 0.2586 0.2709 0.2605 0.0557  0.0030  -0.0583 877  ASP A N   
6460  C CA  . ASP A 879  ? 0.2985 0.3199 0.2977 0.0569  0.0060  -0.0569 877  ASP A CA  
6461  C C   . ASP A 879  ? 0.3048 0.3226 0.3050 0.0550  0.0073  -0.0519 877  ASP A C   
6462  O O   . ASP A 879  ? 0.2837 0.3081 0.2841 0.0564  0.0091  -0.0520 877  ASP A O   
6463  C CB  . ASP A 879  ? 0.2348 0.2656 0.2363 0.0610  0.0056  -0.0641 877  ASP A CB  
6464  C CG  . ASP A 879  ? 0.3551 0.3816 0.3640 0.0624  0.0028  -0.0689 877  ASP A CG  
6465  O OD1 . ASP A 879  ? 0.3886 0.4048 0.4012 0.0606  0.0002  -0.0681 877  ASP A OD1 
6466  O OD2 . ASP A 879  ? 0.3693 0.4033 0.3805 0.0653  0.0031  -0.0733 877  ASP A OD2 
6467  N N   . ARG A 880  ? 0.2773 0.2852 0.2782 0.0519  0.0065  -0.0476 878  ARG A N   
6468  C CA  . ARG A 880  ? 0.2811 0.2852 0.2822 0.0497  0.0077  -0.0423 878  ARG A CA  
6469  C C   . ARG A 880  ? 0.2574 0.2568 0.2544 0.0465  0.0088  -0.0363 878  ARG A C   
6470  O O   . ARG A 880  ? 0.2740 0.2679 0.2708 0.0452  0.0072  -0.0364 878  ARG A O   
6471  C CB  . ARG A 880  ? 0.3176 0.3141 0.3245 0.0491  0.0051  -0.0433 878  ARG A CB  
6472  C CG  . ARG A 880  ? 0.3784 0.3787 0.3903 0.0522  0.0040  -0.0487 878  ARG A CG  
6473  C CD  . ARG A 880  ? 0.4206 0.4126 0.4386 0.0512  0.0011  -0.0489 878  ARG A CD  
6474  N NE  . ARG A 880  ? 0.6452 0.6402 0.6690 0.0543  -0.0005 -0.0545 878  ARG A NE  
6475  C CZ  . ARG A 880  ? 0.6294 0.6252 0.6561 0.0548  -0.0001 -0.0539 878  ARG A CZ  
6476  N NH1 . ARG A 880  ? 0.6754 0.6691 0.7000 0.0523  0.0017  -0.0479 878  ARG A NH1 
6477  N NH2 . ARG A 880  ? 0.6769 0.6757 0.7092 0.0579  -0.0017 -0.0596 878  ARG A NH2 
6478  N N   . LEU A 881  ? 0.2450 0.2469 0.2393 0.0452  0.0114  -0.0314 879  LEU A N   
6479  C CA  . LEU A 881  ? 0.2388 0.2364 0.2299 0.0422  0.0124  -0.0259 879  LEU A CA  
6480  C C   . LEU A 881  ? 0.2535 0.2412 0.2467 0.0398  0.0105  -0.0243 879  LEU A C   
6481  O O   . LEU A 881  ? 0.2532 0.2368 0.2442 0.0378  0.0103  -0.0217 879  LEU A O   
6482  C CB  . LEU A 881  ? 0.2493 0.2507 0.2387 0.0413  0.0152  -0.0211 879  LEU A CB  
6483  C CG  . LEU A 881  ? 0.2818 0.2798 0.2684 0.0385  0.0163  -0.0155 879  LEU A CG  
6484  C CD1 . LEU A 881  ? 0.2985 0.3001 0.2813 0.0389  0.0169  -0.0152 879  LEU A CD1 
6485  C CD2 . LEU A 881  ? 0.3141 0.3148 0.3008 0.0376  0.0184  -0.0111 879  LEU A CD2 
6486  N N   . SER A 882  ? 0.2321 0.2165 0.2297 0.0400  0.0089  -0.0258 880  SER A N   
6487  C CA  . SER A 882  ? 0.2233 0.1992 0.2230 0.0376  0.0071  -0.0238 880  SER A CA  
6488  C C   . SER A 882  ? 0.2763 0.2478 0.2774 0.0373  0.0045  -0.0262 880  SER A C   
6489  O O   . SER A 882  ? 0.2764 0.2414 0.2789 0.0351  0.0030  -0.0241 880  SER A O   
6490  C CB  . SER A 882  ? 0.2744 0.2485 0.2786 0.0379  0.0060  -0.0243 880  SER A CB  
6491  O OG  . SER A 882  ? 0.3178 0.2938 0.3259 0.0406  0.0042  -0.0297 880  SER A OG  
6492  N N   . VAL A 883  ? 0.2569 0.2320 0.2577 0.0394  0.0039  -0.0304 881  VAL A N   
6493  C CA  . VAL A 883  ? 0.2613 0.2322 0.2639 0.0392  0.0012  -0.0329 881  VAL A CA  
6494  C C   . VAL A 883  ? 0.2755 0.2447 0.2738 0.0372  0.0020  -0.0299 881  VAL A C   
6495  O O   . VAL A 883  ? 0.2989 0.2730 0.2929 0.0377  0.0041  -0.0291 881  VAL A O   
6496  C CB  . VAL A 883  ? 0.2704 0.2459 0.2753 0.0424  -0.0002 -0.0393 881  VAL A CB  
6497  C CG1 . VAL A 883  ? 0.2675 0.2392 0.2738 0.0420  -0.0027 -0.0415 881  VAL A CG1 
6498  C CG2 . VAL A 883  ? 0.2657 0.2412 0.2763 0.0442  -0.0017 -0.0425 881  VAL A CG2 
6499  N N   . ASP A 884  ? 0.2381 0.2008 0.2379 0.0349  0.0002  -0.0281 882  ASP A N   
6500  C CA  . ASP A 884  ? 0.2526 0.2132 0.2489 0.0330  0.0007  -0.0256 882  ASP A CA  
6501  C C   . ASP A 884  ? 0.2941 0.2546 0.2911 0.0338  -0.0012 -0.0291 882  ASP A C   
6502  O O   . ASP A 884  ? 0.3302 0.2927 0.3235 0.0336  -0.0002 -0.0285 882  ASP A O   
6503  C CB  . ASP A 884  ? 0.2730 0.2275 0.2704 0.0299  -0.0001 -0.0216 882  ASP A CB  
6504  C CG  . ASP A 884  ? 0.2500 0.2045 0.2469 0.0290  0.0015  -0.0183 882  ASP A CG  
6505  O OD1 . ASP A 884  ? 0.2989 0.2567 0.2921 0.0291  0.0040  -0.0165 882  ASP A OD1 
6506  O OD2 . ASP A 884  ? 0.2751 0.2263 0.2753 0.0282  0.0002  -0.0175 882  ASP A OD2 
6507  N N   . VAL A 885  ? 0.2709 0.2290 0.2732 0.0346  -0.0041 -0.0325 883  VAL A N   
6508  C CA  . VAL A 885  ? 0.2893 0.2462 0.2936 0.0350  -0.0064 -0.0358 883  VAL A CA  
6509  C C   . VAL A 885  ? 0.2709 0.2311 0.2792 0.0382  -0.0081 -0.0419 883  VAL A C   
6510  O O   . VAL A 885  ? 0.2614 0.2200 0.2745 0.0390  -0.0095 -0.0433 883  VAL A O   
6511  C CB  . VAL A 885  ? 0.2930 0.2429 0.3011 0.0324  -0.0090 -0.0336 883  VAL A CB  
6512  C CG1 . VAL A 885  ? 0.3013 0.2499 0.3124 0.0328  -0.0117 -0.0371 883  VAL A CG1 
6513  C CG2 . VAL A 885  ? 0.2983 0.2459 0.3024 0.0293  -0.0073 -0.0279 883  VAL A CG2 
6514  N N   . GLY A 886  ? 0.2714 0.2366 0.2777 0.0403  -0.0079 -0.0458 884  GLY A N   
6515  C CA  . GLY A 886  ? 0.2541 0.2233 0.2641 0.0436  -0.0095 -0.0524 884  GLY A CA  
6516  C C   . GLY A 886  ? 0.2575 0.2226 0.2733 0.0437  -0.0134 -0.0562 884  GLY A C   
6517  O O   . GLY A 886  ? 0.2627 0.2212 0.2808 0.0411  -0.0151 -0.0533 884  GLY A O   
6518  N N   . PRO A 887  ? 0.2658 0.2353 0.2844 0.0469  -0.0149 -0.0629 885  PRO A N   
6519  C CA  . PRO A 887  ? 0.2536 0.2194 0.2792 0.0474  -0.0190 -0.0674 885  PRO A CA  
6520  C C   . PRO A 887  ? 0.2665 0.2322 0.2897 0.0464  -0.0196 -0.0676 885  PRO A C   
6521  O O   . PRO A 887  ? 0.2656 0.2352 0.2818 0.0461  -0.0169 -0.0655 885  PRO A O   
6522  C CB  . PRO A 887  ? 0.2704 0.2425 0.2992 0.0515  -0.0200 -0.0750 885  PRO A CB  
6523  C CG  . PRO A 887  ? 0.2867 0.2678 0.3077 0.0530  -0.0161 -0.0748 885  PRO A CG  
6524  C CD  . PRO A 887  ? 0.2837 0.2625 0.2998 0.0502  -0.0130 -0.0670 885  PRO A CD  
6525  N N   . VAL A 888  ? 0.2652 0.2261 0.2949 0.0460  -0.0234 -0.0703 886  VAL A N   
6526  C CA  . VAL A 888  ? 0.2675 0.2296 0.2965 0.0462  -0.0247 -0.0729 886  VAL A CA  
6527  C C   . VAL A 888  ? 0.2809 0.2503 0.3111 0.0503  -0.0256 -0.0811 886  VAL A C   
6528  O O   . VAL A 888  ? 0.2760 0.2479 0.3101 0.0529  -0.0264 -0.0855 886  VAL A O   
6529  C CB  . VAL A 888  ? 0.3058 0.2600 0.3412 0.0437  -0.0283 -0.0717 886  VAL A CB  
6530  C CG1 . VAL A 888  ? 0.2965 0.2452 0.3295 0.0397  -0.0269 -0.0634 886  VAL A CG1 
6531  C CG2 . VAL A 888  ? 0.3288 0.2795 0.3741 0.0449  -0.0323 -0.0758 886  VAL A CG2 
6532  N N   . ILE A 889  ? 0.2646 0.2383 0.2912 0.0510  -0.0253 -0.0832 887  ILE A N   
6533  C CA  . ILE A 889  ? 0.2810 0.2642 0.3057 0.0548  -0.0248 -0.0899 887  ILE A CA  
6534  C C   . ILE A 889  ? 0.2769 0.2603 0.3104 0.0576  -0.0289 -0.0983 887  ILE A C   
6535  O O   . ILE A 889  ? 0.3056 0.2965 0.3395 0.0612  -0.0286 -0.1041 887  ILE A O   
6536  C CB  . ILE A 889  ? 0.2820 0.2700 0.3003 0.0547  -0.0235 -0.0896 887  ILE A CB  
6537  C CG1 . ILE A 889  ? 0.3019 0.3013 0.3170 0.0587  -0.0224 -0.0956 887  ILE A CG1 
6538  C CG2 . ILE A 889  ? 0.2846 0.2674 0.3072 0.0534  -0.0269 -0.0912 887  ILE A CG2 
6539  C CD1 . ILE A 889  ? 0.2989 0.3045 0.3096 0.0599  -0.0189 -0.0937 887  ILE A CD1 
6540  N N   . THR A 890  ? 0.2744 0.2502 0.3155 0.0561  -0.0328 -0.0991 888  THR A N   
6541  C CA  . THR A 890  ? 0.2737 0.2492 0.3241 0.0587  -0.0372 -0.1073 888  THR A CA  
6542  C C   . THR A 890  ? 0.3118 0.2768 0.3715 0.0564  -0.0409 -0.1051 888  THR A C   
6543  O O   . THR A 890  ? 0.2912 0.2498 0.3498 0.0525  -0.0403 -0.0976 888  THR A O   
6544  C CB  . THR A 890  ? 0.3265 0.3054 0.3777 0.0601  -0.0393 -0.1131 888  THR A CB  
6545  O OG1 . THR A 890  ? 0.3403 0.3128 0.3912 0.0565  -0.0402 -0.1081 888  THR A OG1 
6546  C CG2 . THR A 890  ? 0.3278 0.3181 0.3703 0.0627  -0.0361 -0.1158 888  THR A CG2 
6547  N N   . SER A 891  ? 0.3307 0.2946 0.4002 0.0587  -0.0449 -0.1119 889  SER A N   
6548  C CA  . SER A 891  ? 0.3098 0.2641 0.3896 0.0565  -0.0491 -0.1101 889  SER A CA  
6549  C C   . SER A 891  ? 0.3320 0.2812 0.4141 0.0538  -0.0515 -0.1081 889  SER A C   
6550  O O   . SER A 891  ? 0.3490 0.2902 0.4360 0.0503  -0.0534 -0.1025 889  SER A O   
6551  C CB  . SER A 891  ? 0.3592 0.3135 0.4497 0.0599  -0.0532 -0.1183 889  SER A CB  
6552  O OG  . SER A 891  ? 0.4579 0.4176 0.5506 0.0629  -0.0553 -0.1270 889  SER A OG  
6553  N N   . GLU A 892  ? 0.3211 0.2754 0.3999 0.0551  -0.0514 -0.1124 890  GLU A N   
6554  C CA  . GLU A 892  ? 0.3549 0.3050 0.4356 0.0524  -0.0534 -0.1103 890  GLU A CA  
6555  C C   . GLU A 892  ? 0.3548 0.3022 0.4274 0.0484  -0.0500 -0.1007 890  GLU A C   
6556  O O   . GLU A 892  ? 0.3502 0.2911 0.4263 0.0449  -0.0517 -0.0958 890  GLU A O   
6557  C CB  . GLU A 892  ? 0.3764 0.3331 0.4552 0.0549  -0.0541 -0.1174 890  GLU A CB  
6558  C CG  . GLU A 892  ? 0.4178 0.3789 0.5036 0.0594  -0.0573 -0.1280 890  GLU A CG  
6559  C CD  . GLU A 892  ? 0.4790 0.4505 0.5574 0.0632  -0.0537 -0.1320 890  GLU A CD  
6560  O OE1 . GLU A 892  ? 0.4568 0.4288 0.5344 0.0638  -0.0519 -0.1304 890  GLU A OE1 
6561  O OE2 . GLU A 892  ? 0.7130 0.6927 0.7863 0.0653  -0.0527 -0.1366 890  GLU A OE2 
6562  N N   . ALA A 893  ? 0.3209 0.2738 0.3832 0.0488  -0.0451 -0.0979 891  ALA A N   
6563  C CA  . ALA A 893  ? 0.3197 0.2699 0.3748 0.0452  -0.0418 -0.0890 891  ALA A CA  
6564  C C   . ALA A 893  ? 0.3672 0.3101 0.4267 0.0424  -0.0426 -0.0830 891  ALA A C   
6565  O O   . ALA A 893  ? 0.3307 0.2686 0.3904 0.0388  -0.0429 -0.0769 891  ALA A O   
6566  C CB  . ALA A 893  ? 0.2899 0.2471 0.3344 0.0464  -0.0369 -0.0873 891  ALA A CB  
6567  N N   . LYS A 894  ? 0.3234 0.2661 0.3869 0.0441  -0.0432 -0.0849 892  LYS A N   
6568  C CA  . LYS A 894  ? 0.3312 0.2672 0.3994 0.0417  -0.0443 -0.0796 892  LYS A CA  
6569  C C   . LYS A 894  ? 0.3362 0.2652 0.4140 0.0393  -0.0489 -0.0784 892  LYS A C   
6570  O O   . LYS A 894  ? 0.3685 0.2925 0.4469 0.0356  -0.0490 -0.0712 892  LYS A O   
6571  C CB  . LYS A 894  ? 0.3157 0.2531 0.3876 0.0445  -0.0447 -0.0832 892  LYS A CB  
6572  C CG  . LYS A 894  ? 0.3450 0.2758 0.4230 0.0423  -0.0463 -0.0783 892  LYS A CG  
6573  C CD  . LYS A 894  ? 0.3565 0.2893 0.4379 0.0453  -0.0466 -0.0822 892  LYS A CD  
6574  C CE  . LYS A 894  ? 0.4343 0.3608 0.5218 0.0432  -0.0483 -0.0771 892  LYS A CE  
6575  N NZ  . LYS A 894  ? 0.5844 0.5125 0.6766 0.0463  -0.0491 -0.0814 892  LYS A NZ  
6576  N N   . ASP A 895  ? 0.3343 0.2632 0.4200 0.0413  -0.0529 -0.0854 893  ASP A N   
6577  C CA  . ASP A 895  ? 0.4018 0.3240 0.4976 0.0390  -0.0577 -0.0843 893  ASP A CA  
6578  C C   . ASP A 895  ? 0.3630 0.2835 0.4550 0.0354  -0.0568 -0.0787 893  ASP A C   
6579  O O   . ASP A 895  ? 0.3708 0.2856 0.4679 0.0318  -0.0589 -0.0730 893  ASP A O   
6580  C CB  . ASP A 895  ? 0.3985 0.3216 0.5032 0.0422  -0.0620 -0.0937 893  ASP A CB  
6581  C CG  . ASP A 895  ? 0.4485 0.3719 0.5601 0.0454  -0.0641 -0.0992 893  ASP A CG  
6582  O OD1 . ASP A 895  ? 0.5313 0.4518 0.6441 0.0444  -0.0634 -0.0947 893  ASP A OD1 
6583  O OD2 . ASP A 895  ? 0.4803 0.4072 0.5966 0.0491  -0.0664 -0.1082 893  ASP A OD2 
6584  N N   . ASN A 896  ? 0.3203 0.2460 0.4036 0.0362  -0.0539 -0.0801 894  ASN A N   
6585  C CA  . ASN A 896  ? 0.3485 0.2731 0.4282 0.0330  -0.0531 -0.0752 894  ASN A CA  
6586  C C   . ASN A 896  ? 0.3375 0.2599 0.4118 0.0295  -0.0501 -0.0661 894  ASN A C   
6587  O O   . ASN A 896  ? 0.3450 0.2636 0.4215 0.0259  -0.0512 -0.0607 894  ASN A O   
6588  C CB  . ASN A 896  ? 0.3703 0.3015 0.4420 0.0349  -0.0507 -0.0789 894  ASN A CB  
6589  C CG  . ASN A 896  ? 0.4567 0.3872 0.5240 0.0319  -0.0495 -0.0740 894  ASN A CG  
6590  O OD1 . ASN A 896  ? 0.5396 0.4717 0.5983 0.0304  -0.0455 -0.0688 894  ASN A OD1 
6591  N ND2 . ASN A 896  ? 0.5550 0.4832 0.6287 0.0308  -0.0531 -0.0758 894  ASN A ND2 
6592  N N   . ILE A 897  ? 0.3589 0.2839 0.4264 0.0305  -0.0464 -0.0645 895  ILE A N   
6593  C CA  . ILE A 897  ? 0.3184 0.2417 0.3809 0.0274  -0.0435 -0.0564 895  ILE A CA  
6594  C C   . ILE A 897  ? 0.3563 0.2736 0.4269 0.0249  -0.0464 -0.0522 895  ILE A C   
6595  O O   . ILE A 897  ? 0.3731 0.2879 0.4435 0.0213  -0.0463 -0.0456 895  ILE A O   
6596  C CB  . ILE A 897  ? 0.3059 0.2334 0.3603 0.0292  -0.0393 -0.0562 895  ILE A CB  
6597  C CG1 . ILE A 897  ? 0.3381 0.2719 0.3846 0.0314  -0.0365 -0.0594 895  ILE A CG1 
6598  C CG2 . ILE A 897  ? 0.3152 0.2409 0.3650 0.0262  -0.0366 -0.0484 895  ILE A CG2 
6599  C CD1 . ILE A 897  ? 0.3166 0.2555 0.3574 0.0342  -0.0333 -0.0613 895  ILE A CD1 
6600  N N   . GLU A 898  ? 0.3399 0.2555 0.4182 0.0268  -0.0492 -0.0559 896  GLU A N   
6601  C CA  . GLU A 898  ? 0.3566 0.2666 0.4431 0.0246  -0.0522 -0.0516 896  GLU A CA  
6602  C C   . GLU A 898  ? 0.3978 0.3037 0.4923 0.0218  -0.0562 -0.0494 896  GLU A C   
6603  O O   . GLU A 898  ? 0.4158 0.3182 0.5138 0.0183  -0.0573 -0.0427 896  GLU A O   
6604  C CB  . GLU A 898  ? 0.3595 0.2687 0.4530 0.0276  -0.0545 -0.0565 896  GLU A CB  
6605  C CG  . GLU A 898  ? 0.3773 0.2903 0.4637 0.0297  -0.0506 -0.0570 896  GLU A CG  
6606  C CD  . GLU A 898  ? 0.4432 0.3559 0.5366 0.0328  -0.0528 -0.0622 896  GLU A CD  
6607  O OE1 . GLU A 898  ? 0.4952 0.4064 0.5976 0.0345  -0.0569 -0.0679 896  GLU A OE1 
6608  O OE2 . GLU A 898  ? 0.5814 0.4956 0.6716 0.0336  -0.0505 -0.0607 896  GLU A OE2 
6609  N N   . LYS A 899  ? 0.3834 0.2900 0.4811 0.0231  -0.0584 -0.0549 897  LYS A N   
6610  C CA  . LYS A 899  ? 0.3713 0.2742 0.4762 0.0202  -0.0620 -0.0526 897  LYS A CA  
6611  C C   . LYS A 899  ? 0.4509 0.3544 0.5494 0.0163  -0.0593 -0.0448 897  LYS A C   
6612  O O   . LYS A 899  ? 0.4100 0.3102 0.5141 0.0127  -0.0616 -0.0391 897  LYS A O   
6613  C CB  . LYS A 899  ? 0.4067 0.3112 0.5148 0.0225  -0.0643 -0.0602 897  LYS A CB  
6614  N N   . HIS A 900  ? 0.3536 0.2615 0.4405 0.0170  -0.0546 -0.0445 898  HIS A N   
6615  C CA  . HIS A 900  ? 0.3685 0.2774 0.4490 0.0136  -0.0519 -0.0376 898  HIS A CA  
6616  C C   . HIS A 900  ? 0.3779 0.2850 0.4582 0.0110  -0.0509 -0.0305 898  HIS A C   
6617  O O   . HIS A 900  ? 0.4286 0.3346 0.5103 0.0073  -0.0514 -0.0243 898  HIS A O   
6618  C CB  . HIS A 900  ? 0.3216 0.2356 0.3905 0.0152  -0.0472 -0.0391 898  HIS A CB  
6619  C CG  . HIS A 900  ? 0.3479 0.2632 0.4099 0.0122  -0.0441 -0.0325 898  HIS A CG  
6620  N ND1 . HIS A 900  ? 0.3861 0.3013 0.4487 0.0096  -0.0448 -0.0299 898  HIS A ND1 
6621  C CD2 . HIS A 900  ? 0.3535 0.2703 0.4085 0.0113  -0.0404 -0.0283 898  HIS A CD2 
6622  C CE1 . HIS A 900  ? 0.3833 0.3003 0.4393 0.0075  -0.0416 -0.0245 898  HIS A CE1 
6623  N NE2 . HIS A 900  ? 0.3516 0.2694 0.4030 0.0085  -0.0390 -0.0235 898  HIS A NE2 
6624  N N   . ILE A 901  ? 0.3283 0.2357 0.4068 0.0128  -0.0495 -0.0314 899  ILE A N   
6625  C CA  . ILE A 901  ? 0.3572 0.2634 0.4352 0.0106  -0.0486 -0.0249 899  ILE A CA  
6626  C C   . ILE A 901  ? 0.4276 0.3294 0.5163 0.0079  -0.0531 -0.0210 899  ILE A C   
6627  O O   . ILE A 901  ? 0.4376 0.3390 0.5263 0.0044  -0.0529 -0.0139 899  ILE A O   
6628  C CB  . ILE A 901  ? 0.3609 0.2681 0.4359 0.0133  -0.0467 -0.0272 899  ILE A CB  
6629  C CG1 . ILE A 901  ? 0.3287 0.2407 0.3929 0.0153  -0.0420 -0.0295 899  ILE A CG1 
6630  C CG2 . ILE A 901  ? 0.3993 0.3049 0.4753 0.0110  -0.0465 -0.0209 899  ILE A CG2 
6631  C CD1 . ILE A 901  ? 0.3576 0.2714 0.4194 0.0185  -0.0403 -0.0329 899  ILE A CD1 
6632  N N   . GLU A 902  ? 0.4121 0.3109 0.5105 0.0095  -0.0574 -0.0256 900  GLU A N   
6633  C CA  . GLU A 902  ? 0.4727 0.3670 0.5827 0.0070  -0.0621 -0.0218 900  GLU A CA  
6634  C C   . GLU A 902  ? 0.4402 0.3339 0.5532 0.0035  -0.0638 -0.0176 900  GLU A C   
6635  O O   . GLU A 902  ? 0.5219 0.4136 0.6406 0.0000  -0.0660 -0.0108 900  GLU A O   
6636  C CB  . GLU A 902  ? 0.4757 0.3669 0.5961 0.0099  -0.0664 -0.0283 900  GLU A CB  
6637  C CG  . GLU A 902  ? 0.5658 0.4574 0.6852 0.0128  -0.0653 -0.0310 900  GLU A CG  
6638  C CD  . GLU A 902  ? 0.6104 0.5016 0.7270 0.0104  -0.0635 -0.0233 900  GLU A CD  
6639  O OE1 . GLU A 902  ? 0.6046 0.4927 0.7289 0.0073  -0.0667 -0.0175 900  GLU A OE1 
6640  O OE2 . GLU A 902  ? 0.5609 0.4554 0.6678 0.0114  -0.0591 -0.0230 900  GLU A OE2 
6641  N N   . ARG A 903  ? 0.4473 0.3431 0.5566 0.0042  -0.0628 -0.0211 901  ARG A N   
6642  C CA  . ARG A 903  ? 0.5094 0.4054 0.6202 0.0007  -0.0638 -0.0168 901  ARG A CA  
6643  C C   . ARG A 903  ? 0.5481 0.4468 0.6518 -0.0027 -0.0605 -0.0088 901  ARG A C   
6644  O O   . ARG A 903  ? 0.5314 0.4294 0.6401 -0.0064 -0.0623 -0.0022 901  ARG A O   
6645  C CB  . ARG A 903  ? 0.4863 0.3847 0.5929 0.0025  -0.0628 -0.0225 901  ARG A CB  
6646  C CG  . ARG A 903  ? 0.6185 0.5173 0.7272 -0.0007 -0.0639 -0.0189 901  ARG A CG  
6647  C CD  . ARG A 903  ? 0.6497 0.5522 0.7510 0.0010  -0.0615 -0.0235 901  ARG A CD  
6648  N NE  . ARG A 903  ? 0.8446 0.7489 0.9439 -0.0024 -0.0607 -0.0186 901  ARG A NE  
6649  C CZ  . ARG A 903  ? 0.8236 0.7320 0.9132 -0.0022 -0.0569 -0.0186 901  ARG A CZ  
6650  N NH1 . ARG A 903  ? 0.7414 0.6524 0.8222 0.0010  -0.0534 -0.0227 901  ARG A NH1 
6651  N NH2 . ARG A 903  ? 0.8406 0.7506 0.9296 -0.0053 -0.0566 -0.0143 901  ARG A NH2 
6652  N N   . MET A 904  ? 0.4754 0.3775 0.5679 -0.0013 -0.0556 -0.0092 902  MET A N   
6653  C CA  . MET A 904  ? 0.4535 0.3585 0.5394 -0.0041 -0.0524 -0.0023 902  MET A CA  
6654  C C   . MET A 904  ? 0.5005 0.4037 0.5916 -0.0063 -0.0542 0.0035  902  MET A C   
6655  O O   . MET A 904  ? 0.5147 0.4193 0.6066 -0.0100 -0.0544 0.0104  902  MET A O   
6656  C CB  . MET A 904  ? 0.4031 0.3114 0.4775 -0.0019 -0.0474 -0.0045 902  MET A CB  
6657  C CG  . MET A 904  ? 0.4226 0.3334 0.4910 0.0000  -0.0454 -0.0093 902  MET A CG  
6658  S SD  . MET A 904  ? 0.5844 0.4977 0.6508 -0.0034 -0.0448 -0.0050 902  MET A SD  
6659  C CE  . MET A 904  ? 0.5335 0.4445 0.6082 -0.0027 -0.0490 -0.0097 902  MET A CE  
6660  N N   . ARG A 905  ? 0.4283 0.3290 0.5228 -0.0041 -0.0553 0.0009  903  ARG A N   
6661  C CA  . ARG A 905  ? 0.4905 0.3894 0.5904 -0.0059 -0.0573 0.0062  903  ARG A CA  
6662  C C   . ARG A 905  ? 0.5640 0.4603 0.6752 -0.0091 -0.0621 0.0107  903  ARG A C   
6663  O O   . ARG A 905  ? 0.4919 0.3888 0.6057 -0.0124 -0.0630 0.0181  903  ARG A O   
6664  C CB  . ARG A 905  ? 0.5185 0.4150 0.6213 -0.0026 -0.0582 0.0016  903  ARG A CB  
6665  C CG  . ARG A 905  ? 0.5494 0.4451 0.6544 -0.0039 -0.0586 0.0069  903  ARG A CG  
6666  C CD  . ARG A 905  ? 0.5738 0.4666 0.6844 -0.0007 -0.0606 0.0021  903  ARG A CD  
6667  N NE  . ARG A 905  ? 0.4414 0.3360 0.5448 0.0033  -0.0574 -0.0050 903  ARG A NE  
6668  C CZ  . ARG A 905  ? 0.4967 0.3939 0.5922 0.0046  -0.0537 -0.0050 903  ARG A CZ  
6669  N NH1 . ARG A 905  ? 0.5070 0.4053 0.5995 0.0022  -0.0522 0.0013  903  ARG A NH1 
6670  N NH2 . ARG A 905  ? 0.5278 0.4267 0.6184 0.0083  -0.0514 -0.0115 903  ARG A NH2 
6671  N N   . GLY A 906  ? 0.5354 0.4291 0.6537 -0.0082 -0.0653 0.0064  904  GLY A N   
6672  C CA  . GLY A 906  ? 0.6070 0.4980 0.7368 -0.0112 -0.0702 0.0104  904  GLY A CA  
6673  C C   . GLY A 906  ? 0.6341 0.5285 0.7614 -0.0153 -0.0692 0.0171  904  GLY A C   
6674  O O   . GLY A 906  ? 0.6881 0.5816 0.8240 -0.0188 -0.0726 0.0234  904  GLY A O   
6675  N N   . LEU A 907  ? 0.6084 0.5070 0.7247 -0.0150 -0.0647 0.0161  905  LEU A N   
6676  C CA  . LEU A 907  ? 0.5853 0.4881 0.6983 -0.0187 -0.0633 0.0220  905  LEU A CA  
6677  C C   . LEU A 907  ? 0.5796 0.4862 0.6877 -0.0213 -0.0609 0.0293  905  LEU A C   
6678  O O   . LEU A 907  ? 0.5784 0.4894 0.6834 -0.0243 -0.0595 0.0345  905  LEU A O   
6679  C CB  . LEU A 907  ? 0.5571 0.4629 0.6609 -0.0171 -0.0597 0.0176  905  LEU A CB  
6680  C CG  . LEU A 907  ? 0.6415 0.5448 0.7499 -0.0152 -0.0622 0.0111  905  LEU A CG  
6681  C CD1 . LEU A 907  ? 0.6692 0.5761 0.7685 -0.0142 -0.0587 0.0080  905  LEU A CD1 
6682  C CD2 . LEU A 907  ? 0.6852 0.5860 0.8059 -0.0181 -0.0672 0.0145  905  LEU A CD2 
6683  N N   . GLY A 908  ? 0.5106 0.4161 0.6180 -0.0201 -0.0604 0.0298  906  GLY A N   
6684  C CA  . GLY A 908  ? 0.4973 0.4065 0.6001 -0.0223 -0.0583 0.0362  906  GLY A CA  
6685  C C   . GLY A 908  ? 0.4727 0.3855 0.5631 -0.0205 -0.0530 0.0339  906  GLY A C   
6686  O O   . GLY A 908  ? 0.4737 0.3900 0.5598 -0.0221 -0.0511 0.0386  906  GLY A O   
6687  N N   . ARG A 909  ? 0.4947 0.4068 0.5794 -0.0171 -0.0508 0.0269  907  ARG A N   
6688  C CA  . ARG A 909  ? 0.4006 0.3161 0.4740 -0.0155 -0.0459 0.0250  907  ARG A CA  
6689  C C   . ARG A 909  ? 0.4502 0.3646 0.5218 -0.0137 -0.0449 0.0243  907  ARG A C   
6690  O O   . ARG A 909  ? 0.4566 0.3670 0.5341 -0.0119 -0.0473 0.0216  907  ARG A O   
6691  C CB  . ARG A 909  ? 0.4138 0.3291 0.4826 -0.0126 -0.0441 0.0182  907  ARG A CB  
6692  C CG  . ARG A 909  ? 0.4345 0.3501 0.5060 -0.0139 -0.0456 0.0179  907  ARG A CG  
6693  C CD  . ARG A 909  ? 0.4990 0.4197 0.5660 -0.0170 -0.0435 0.0231  907  ARG A CD  
6694  N NE  . ARG A 909  ? 0.5176 0.4391 0.5857 -0.0178 -0.0442 0.0219  907  ARG A NE  
6695  C CZ  . ARG A 909  ? 0.6443 0.5665 0.7190 -0.0210 -0.0469 0.0262  907  ARG A CZ  
6696  N NH1 . ARG A 909  ? 0.5820 0.5042 0.6629 -0.0239 -0.0493 0.0324  907  ARG A NH1 
6697  N NH2 . ARG A 909  ? 0.5336 0.4566 0.6090 -0.0213 -0.0474 0.0245  907  ARG A NH2 
6698  N N   . LYS A 910  ? 0.3744 0.2926 0.4380 -0.0142 -0.0413 0.0265  908  LYS A N   
6699  C CA  . LYS A 910  ? 0.3502 0.2680 0.4114 -0.0127 -0.0400 0.0261  908  LYS A CA  
6700  C C   . LYS A 910  ? 0.3824 0.2986 0.4397 -0.0086 -0.0381 0.0190  908  LYS A C   
6701  O O   . LYS A 910  ? 0.3569 0.2749 0.4076 -0.0074 -0.0354 0.0159  908  LYS A O   
6702  C CB  . LYS A 910  ? 0.4004 0.3232 0.4544 -0.0145 -0.0369 0.0302  908  LYS A CB  
6703  C CG  . LYS A 910  ? 0.5230 0.4460 0.5765 -0.0144 -0.0365 0.0324  908  LYS A CG  
6704  C CD  . LYS A 910  ? 0.5040 0.4326 0.5523 -0.0171 -0.0344 0.0374  908  LYS A CD  
6705  C CE  . LYS A 910  ? 0.6022 0.5316 0.6489 -0.0167 -0.0336 0.0389  908  LYS A CE  
6706  N NZ  . LYS A 910  ? 0.6969 0.6324 0.7390 -0.0193 -0.0318 0.0435  908  LYS A NZ  
6707  N N   . VAL A 911  ? 0.3597 0.2727 0.4212 -0.0065 -0.0397 0.0165  909  VAL A N   
6708  C CA  . VAL A 911  ? 0.3712 0.2829 0.4305 -0.0026 -0.0386 0.0096  909  VAL A CA  
6709  C C   . VAL A 911  ? 0.3403 0.2524 0.3972 -0.0011 -0.0370 0.0095  909  VAL A C   
6710  O O   . VAL A 911  ? 0.4069 0.3169 0.4697 -0.0017 -0.0394 0.0117  909  VAL A O   
6711  C CB  . VAL A 911  ? 0.3587 0.2666 0.4267 -0.0009 -0.0424 0.0054  909  VAL A CB  
6712  C CG1 . VAL A 911  ? 0.4181 0.3260 0.4840 0.0033  -0.0412 -0.0017 909  VAL A CG1 
6713  C CG2 . VAL A 911  ? 0.3654 0.2730 0.4362 -0.0023 -0.0441 0.0052  909  VAL A CG2 
6714  N N   . GLU A 912  ? 0.3319 0.2464 0.3805 0.0006  -0.0331 0.0072  910  GLU A N   
6715  C CA  . GLU A 912  ? 0.3306 0.2457 0.3765 0.0022  -0.0313 0.0065  910  GLU A CA  
6716  C C   . GLU A 912  ? 0.4050 0.3197 0.4504 0.0061  -0.0307 0.0000  910  GLU A C   
6717  O O   . GLU A 912  ? 0.3401 0.2564 0.3815 0.0075  -0.0291 -0.0034 910  GLU A O   
6718  C CB  . GLU A 912  ? 0.3282 0.2469 0.3655 0.0013  -0.0274 0.0088  910  GLU A CB  
6719  C CG  . GLU A 912  ? 0.3794 0.2989 0.4142 0.0024  -0.0256 0.0090  910  GLU A CG  
6720  C CD  . GLU A 912  ? 0.4395 0.3585 0.4782 0.0001  -0.0274 0.0139  910  GLU A CD  
6721  O OE1 . GLU A 912  ? 0.4155 0.3345 0.4575 -0.0026 -0.0294 0.0180  910  GLU A OE1 
6722  O OE2 . GLU A 912  ? 0.4371 0.3561 0.4756 0.0011  -0.0268 0.0140  910  GLU A OE2 
6723  N N   . GLN A 913  ? 0.3724 0.2855 0.4221 0.0078  -0.0320 -0.0018 911  GLN A N   
6724  C CA  . GLN A 913  ? 0.3645 0.2781 0.4143 0.0116  -0.0315 -0.0081 911  GLN A CA  
6725  C C   . GLN A 913  ? 0.4398 0.3542 0.4884 0.0131  -0.0301 -0.0084 911  GLN A C   
6726  O O   . GLN A 913  ? 0.4138 0.3267 0.4660 0.0117  -0.0315 -0.0049 911  GLN A O   
6727  C CB  . GLN A 913  ? 0.3904 0.3011 0.4491 0.0129  -0.0356 -0.0119 911  GLN A CB  
6728  C CG  . GLN A 913  ? 0.3857 0.2957 0.4458 0.0121  -0.0371 -0.0129 911  GLN A CG  
6729  C CD  . GLN A 913  ? 0.4097 0.3175 0.4782 0.0142  -0.0409 -0.0183 911  GLN A CD  
6730  O OE1 . GLN A 913  ? 0.4362 0.3407 0.5134 0.0139  -0.0444 -0.0177 911  GLN A OE1 
6731  N NE2 . GLN A 913  ? 0.3461 0.2558 0.4123 0.0164  -0.0402 -0.0237 911  GLN A NE2 
6732  N N   . ILE A 914  ? 0.4027 0.3200 0.4462 0.0158  -0.0273 -0.0123 912  ILE A N   
6733  C CA  . ILE A 914  ? 0.3633 0.2818 0.4065 0.0178  -0.0261 -0.0137 912  ILE A CA  
6734  C C   . ILE A 914  ? 0.4169 0.3333 0.4687 0.0198  -0.0295 -0.0172 912  ILE A C   
6735  O O   . ILE A 914  ? 0.3760 0.2914 0.4322 0.0210  -0.0319 -0.0211 912  ILE A O   
6736  C CB  . ILE A 914  ? 0.5101 0.4328 0.5465 0.0202  -0.0226 -0.0171 912  ILE A CB  
6737  C CG1 . ILE A 914  ? 0.4664 0.3910 0.4950 0.0183  -0.0193 -0.0134 912  ILE A CG1 
6738  C CG2 . ILE A 914  ? 0.6139 0.5385 0.6510 0.0229  -0.0217 -0.0198 912  ILE A CG2 
6739  C CD1 . ILE A 914  ? 0.4438 0.3723 0.4664 0.0204  -0.0162 -0.0163 912  ILE A CD1 
6740  N N   . GLY A 915  ? 0.4495 0.3652 0.5040 0.0201  -0.0300 -0.0160 913  GLY A N   
6741  C CA  . GLY A 915  ? 0.4153 0.3296 0.4777 0.0226  -0.0329 -0.0201 913  GLY A CA  
6742  C C   . GLY A 915  ? 0.4560 0.3744 0.5156 0.0264  -0.0308 -0.0262 913  GLY A C   
6743  O O   . GLY A 915  ? 0.5372 0.4592 0.5902 0.0269  -0.0272 -0.0256 913  GLY A O   
6744  N N   . LEU A 916  ? 0.4301 0.3486 0.4952 0.0290  -0.0331 -0.0321 914  LEU A N   
6745  C CA  . LEU A 916  ? 0.4595 0.3829 0.5222 0.0328  -0.0314 -0.0384 914  LEU A CA  
6746  C C   . LEU A 916  ? 0.4815 0.4057 0.5492 0.0352  -0.0323 -0.0411 914  LEU A C   
6747  O O   . LEU A 916  ? 0.5075 0.4278 0.5838 0.0351  -0.0359 -0.0409 914  LEU A O   
6748  C CB  . LEU A 916  ? 0.4618 0.3857 0.5276 0.0347  -0.0335 -0.0442 914  LEU A CB  
6749  C CG  . LEU A 916  ? 0.4400 0.3638 0.5011 0.0328  -0.0326 -0.0426 914  LEU A CG  
6750  C CD1 . LEU A 916  ? 0.4632 0.3879 0.5281 0.0351  -0.0350 -0.0491 914  LEU A CD1 
6751  C CD2 . LEU A 916  ? 0.5318 0.4602 0.5825 0.0326  -0.0279 -0.0407 914  LEU A CD2 
6752  N N   . ALA A 917  ? 0.3853 0.3150 0.4480 0.0375  -0.0290 -0.0434 915  ALA A N   
6753  C CA  . ALA A 917  ? 0.4298 0.3614 0.4967 0.0401  -0.0295 -0.0464 915  ALA A CA  
6754  C C   . ALA A 917  ? 0.4465 0.3786 0.5213 0.0434  -0.0328 -0.0538 915  ALA A C   
6755  O O   . ALA A 917  ? 0.4725 0.4053 0.5475 0.0443  -0.0338 -0.0576 915  ALA A O   
6756  C CB  . ALA A 917  ? 0.4474 0.3856 0.5069 0.0417  -0.0250 -0.0471 915  ALA A CB  
6757  N N   . SER A 918  ? 0.4539 0.3856 0.5356 0.0453  -0.0347 -0.0562 916  SER A N   
6758  C CA  . SER A 918  ? 0.4726 0.4051 0.5628 0.0488  -0.0381 -0.0639 916  SER A CA  
6759  C C   . SER A 918  ? 0.4290 0.3693 0.5146 0.0522  -0.0358 -0.0706 916  SER A C   
6760  O O   . SER A 918  ? 0.4181 0.3595 0.5087 0.0546  -0.0384 -0.0772 916  SER A O   
6761  C CB  . SER A 918  ? 0.4777 0.4091 0.5757 0.0504  -0.0402 -0.0652 916  SER A CB  
6762  O OG  . SER A 918  ? 0.5769 0.5137 0.6694 0.0515  -0.0364 -0.0647 916  SER A OG  
6763  N N   . GLU A 919  ? 0.4415 0.3877 0.5182 0.0525  -0.0312 -0.0691 917  GLU A N   
6764  C CA  . GLU A 919  ? 0.4174 0.3722 0.4895 0.0557  -0.0288 -0.0747 917  GLU A CA  
6765  C C   . GLU A 919  ? 0.4259 0.3815 0.4951 0.0555  -0.0291 -0.0767 917  GLU A C   
6766  O O   . GLU A 919  ? 0.3940 0.3564 0.4619 0.0586  -0.0285 -0.0829 917  GLU A O   
6767  C CB  . GLU A 919  ? 0.4695 0.4300 0.5326 0.0553  -0.0238 -0.0710 917  GLU A CB  
6768  C CG  . GLU A 919  ? 0.5341 0.4969 0.5994 0.0566  -0.0229 -0.0709 917  GLU A CG  
6769  C CD  . GLU A 919  ? 0.6217 0.5773 0.6898 0.0536  -0.0240 -0.0646 917  GLU A CD  
6770  O OE1 . GLU A 919  ? 0.5499 0.4992 0.6172 0.0503  -0.0250 -0.0597 917  GLU A OE1 
6771  O OE2 . GLU A 919  ? 0.6821 0.6386 0.7531 0.0545  -0.0238 -0.0644 917  GLU A OE2 
6772  N N   . THR A 920  ? 0.3965 0.3458 0.4648 0.0520  -0.0300 -0.0717 918  THR A N   
6773  C CA  . THR A 920  ? 0.3697 0.3195 0.4354 0.0517  -0.0304 -0.0735 918  THR A CA  
6774  C C   . THR A 920  ? 0.3634 0.3122 0.4378 0.0541  -0.0348 -0.0807 918  THR A C   
6775  O O   . THR A 920  ? 0.3518 0.3030 0.4245 0.0549  -0.0351 -0.0842 918  THR A O   
6776  C CB  . THR A 920  ? 0.3623 0.3061 0.4251 0.0473  -0.0302 -0.0662 918  THR A CB  
6777  O OG1 . THR A 920  ? 0.3677 0.3039 0.4384 0.0454  -0.0339 -0.0635 918  THR A OG1 
6778  C CG2 . THR A 920  ? 0.3455 0.2909 0.3993 0.0453  -0.0258 -0.0598 918  THR A CG2 
6779  N N   . GLY A 921  ? 0.3831 0.3286 0.4673 0.0553  -0.0383 -0.0833 919  GLY A N   
6780  C CA  . GLY A 921  ? 0.4035 0.3471 0.4973 0.0573  -0.0430 -0.0900 919  GLY A CA  
6781  C C   . GLY A 921  ? 0.3551 0.3070 0.4478 0.0616  -0.0426 -0.0990 919  GLY A C   
6782  O O   . GLY A 921  ? 0.3984 0.3497 0.4968 0.0629  -0.0460 -0.1046 919  GLY A O   
6783  N N   . VAL A 922  ? 0.3472 0.3076 0.4329 0.0637  -0.0386 -0.1004 920  VAL A N   
6784  C CA  . VAL A 922  ? 0.3412 0.3110 0.4252 0.0677  -0.0378 -0.1087 920  VAL A CA  
6785  C C   . VAL A 922  ? 0.3363 0.3097 0.4122 0.0670  -0.0358 -0.1081 920  VAL A C   
6786  O O   . VAL A 922  ? 0.3511 0.3323 0.4258 0.0701  -0.0357 -0.1150 920  VAL A O   
6787  C CB  . VAL A 922  ? 0.3303 0.3090 0.4107 0.0705  -0.0345 -0.1107 920  VAL A CB  
6788  C CG1 . VAL A 922  ? 0.3529 0.3295 0.4429 0.0724  -0.0372 -0.1138 920  VAL A CG1 
6789  C CG2 . VAL A 922  ? 0.3445 0.3239 0.4152 0.0677  -0.0298 -0.1021 920  VAL A CG2 
6790  N N   . GLY A 923  ? 0.3285 0.2969 0.3989 0.0629  -0.0343 -0.1003 921  GLY A N   
6791  C CA  . GLY A 923  ? 0.3048 0.2757 0.3684 0.0620  -0.0327 -0.0994 921  GLY A CA  
6792  C C   . GLY A 923  ? 0.2887 0.2510 0.3555 0.0588  -0.0356 -0.0963 921  GLY A C   
6793  O O   . GLY A 923  ? 0.3191 0.2743 0.3949 0.0579  -0.0394 -0.0964 921  GLY A O   
6794  N N   . THR A 924  ? 0.3070 0.2700 0.3670 0.0569  -0.0338 -0.0933 922  THR A N   
6795  C CA  . THR A 924  ? 0.2950 0.2508 0.3575 0.0538  -0.0362 -0.0902 922  THR A CA  
6796  C C   . THR A 924  ? 0.3105 0.2634 0.3656 0.0499  -0.0329 -0.0811 922  THR A C   
6797  O O   . THR A 924  ? 0.3105 0.2676 0.3573 0.0495  -0.0298 -0.0792 922  THR A O   
6798  C CB  . THR A 924  ? 0.2952 0.2543 0.3572 0.0551  -0.0374 -0.0953 922  THR A CB  
6799  O OG1 . THR A 924  ? 0.3069 0.2746 0.3593 0.0566  -0.0335 -0.0960 922  THR A OG1 
6800  C CG2 . THR A 924  ? 0.3309 0.2913 0.4023 0.0586  -0.0416 -0.1045 922  THR A CG2 
6801  N N   . PHE A 925  ? 0.2856 0.2318 0.3440 0.0472  -0.0338 -0.0756 923  PHE A N   
6802  C CA  . PHE A 925  ? 0.2651 0.2087 0.3171 0.0437  -0.0310 -0.0673 923  PHE A CA  
6803  C C   . PHE A 925  ? 0.2864 0.2227 0.3424 0.0401  -0.0336 -0.0629 923  PHE A C   
6804  O O   . PHE A 925  ? 0.3343 0.2659 0.3994 0.0399  -0.0376 -0.0643 923  PHE A O   
6805  C CB  . PHE A 925  ? 0.2571 0.2004 0.3086 0.0434  -0.0293 -0.0640 923  PHE A CB  
6806  C CG  . PHE A 925  ? 0.2914 0.2423 0.3376 0.0462  -0.0260 -0.0665 923  PHE A CG  
6807  C CD1 . PHE A 925  ? 0.2785 0.2336 0.3292 0.0499  -0.0272 -0.0733 923  PHE A CD1 
6808  C CD2 . PHE A 925  ? 0.2565 0.2106 0.2939 0.0451  -0.0217 -0.0621 923  PHE A CD2 
6809  C CE1 . PHE A 925  ? 0.3042 0.2671 0.3502 0.0524  -0.0240 -0.0753 923  PHE A CE1 
6810  C CE2 . PHE A 925  ? 0.2608 0.2223 0.2940 0.0475  -0.0188 -0.0638 923  PHE A CE2 
6811  C CZ  . PHE A 925  ? 0.2756 0.2417 0.3128 0.0511  -0.0198 -0.0703 923  PHE A CZ  
6812  N N   . VAL A 926  ? 0.3002 0.2358 0.3497 0.0373  -0.0313 -0.0574 924  VAL A N   
6813  C CA  . VAL A 926  ? 0.2776 0.2074 0.3293 0.0334  -0.0328 -0.0518 924  VAL A CA  
6814  C C   . VAL A 926  ? 0.3103 0.2395 0.3559 0.0311  -0.0295 -0.0450 924  VAL A C   
6815  O O   . VAL A 926  ? 0.2936 0.2269 0.3313 0.0314  -0.0259 -0.0440 924  VAL A O   
6816  C CB  . VAL A 926  ? 0.2840 0.2138 0.3337 0.0323  -0.0332 -0.0519 924  VAL A CB  
6817  C CG1 . VAL A 926  ? 0.3190 0.2438 0.3700 0.0281  -0.0342 -0.0454 924  VAL A CG1 
6818  C CG2 . VAL A 926  ? 0.3107 0.2407 0.3672 0.0345  -0.0368 -0.0588 924  VAL A CG2 
6819  N N   . PRO A 927  ? 0.3064 0.2312 0.3558 0.0286  -0.0308 -0.0403 925  PRO A N   
6820  C CA  . PRO A 927  ? 0.3006 0.2256 0.3444 0.0265  -0.0278 -0.0344 925  PRO A CA  
6821  C C   . PRO A 927  ? 0.3031 0.2284 0.3409 0.0240  -0.0259 -0.0305 925  PRO A C   
6822  O O   . PRO A 927  ? 0.2963 0.2197 0.3365 0.0226  -0.0279 -0.0302 925  PRO A O   
6823  C CB  . PRO A 927  ? 0.3550 0.2752 0.4054 0.0245  -0.0305 -0.0307 925  PRO A CB  
6824  C CG  . PRO A 927  ? 0.3604 0.2772 0.4190 0.0241  -0.0348 -0.0325 925  PRO A CG  
6825  C CD  . PRO A 927  ? 0.3370 0.2567 0.3962 0.0276  -0.0353 -0.0399 925  PRO A CD  
6826  N N   . PRO A 928  ? 0.3191 0.2470 0.3494 0.0235  -0.0222 -0.0278 926  PRO A N   
6827  C CA  . PRO A 928  ? 0.3151 0.2429 0.3404 0.0209  -0.0206 -0.0236 926  PRO A CA  
6828  C C   . PRO A 928  ? 0.2772 0.2010 0.3068 0.0177  -0.0229 -0.0193 926  PRO A C   
6829  O O   . PRO A 928  ? 0.3154 0.2370 0.3490 0.0167  -0.0243 -0.0169 926  PRO A O   
6830  C CB  . PRO A 928  ? 0.2779 0.2081 0.2971 0.0208  -0.0170 -0.0209 926  PRO A CB  
6831  C CG  . PRO A 928  ? 0.3407 0.2743 0.3593 0.0241  -0.0159 -0.0253 926  PRO A CG  
6832  C CD  . PRO A 928  ? 0.3416 0.2731 0.3680 0.0255  -0.0194 -0.0288 926  PRO A CD  
6833  N N   . THR A 929  ? 0.2848 0.2082 0.3137 0.0160  -0.0235 -0.0182 927  THR A N   
6834  C CA  . THR A 929  ? 0.2731 0.1935 0.3071 0.0131  -0.0262 -0.0146 927  THR A CA  
6835  C C   . THR A 929  ? 0.2822 0.2040 0.3109 0.0105  -0.0243 -0.0107 927  THR A C   
6836  O O   . THR A 929  ? 0.3097 0.2338 0.3334 0.0114  -0.0223 -0.0125 927  THR A O   
6837  C CB  . THR A 929  ? 0.3292 0.2476 0.3697 0.0138  -0.0297 -0.0183 927  THR A CB  
6838  O OG1 . THR A 929  ? 0.3129 0.2304 0.3586 0.0165  -0.0315 -0.0225 927  THR A OG1 
6839  C CG2 . THR A 929  ? 0.3433 0.2587 0.3898 0.0106  -0.0328 -0.0141 927  THR A CG2 
6840  N N   . ILE A 930  ? 0.2958 0.2166 0.3260 0.0075  -0.0249 -0.0055 928  ILE A N   
6841  C CA  . ILE A 930  ? 0.2968 0.2193 0.3233 0.0049  -0.0236 -0.0018 928  ILE A CA  
6842  C C   . ILE A 930  ? 0.3028 0.2234 0.3356 0.0023  -0.0269 0.0010  928  ILE A C   
6843  O O   . ILE A 930  ? 0.3560 0.2745 0.3946 0.0011  -0.0294 0.0034  928  ILE A O   
6844  C CB  . ILE A 930  ? 0.2690 0.1932 0.2911 0.0034  -0.0212 0.0022  928  ILE A CB  
6845  C CG1 . ILE A 930  ? 0.3458 0.2719 0.3619 0.0057  -0.0180 -0.0001 928  ILE A CG1 
6846  C CG2 . ILE A 930  ? 0.3678 0.2941 0.3874 0.0005  -0.0205 0.0060  928  ILE A CG2 
6847  C CD1 . ILE A 930  ? 0.3432 0.2705 0.3563 0.0047  -0.0161 0.0031  928  ILE A CD1 
6848  N N   . ILE A 931  ? 0.3013 0.2227 0.3335 0.0014  -0.0272 0.0008  929  ILE A N   
6849  C CA  . ILE A 931  ? 0.3041 0.2243 0.3424 -0.0012 -0.0302 0.0035  929  ILE A CA  
6850  C C   . ILE A 931  ? 0.3643 0.2878 0.3984 -0.0039 -0.0285 0.0075  929  ILE A C   
6851  O O   . ILE A 931  ? 0.3346 0.2603 0.3632 -0.0031 -0.0261 0.0057  929  ILE A O   
6852  C CB  . ILE A 931  ? 0.3603 0.2788 0.4031 0.0002  -0.0327 -0.0010 929  ILE A CB  
6853  C CG1 . ILE A 931  ? 0.3419 0.2578 0.3892 0.0032  -0.0345 -0.0056 929  ILE A CG1 
6854  C CG2 . ILE A 931  ? 0.3381 0.2552 0.3876 -0.0028 -0.0359 0.0023  929  ILE A CG2 
6855  C CD1 . ILE A 931  ? 0.3521 0.2663 0.4048 0.0046  -0.0374 -0.0105 929  ILE A CD1 
6856  N N   . GLU A 932  ? 0.3496 0.2738 0.3864 -0.0070 -0.0296 0.0130  930  GLU A N   
6857  C CA  . GLU A 932  ? 0.3520 0.2802 0.3852 -0.0096 -0.0280 0.0169  930  GLU A CA  
6858  C C   . GLU A 932  ? 0.2967 0.2248 0.3345 -0.0115 -0.0304 0.0181  930  GLU A C   
6859  O O   . GLU A 932  ? 0.3468 0.2729 0.3924 -0.0131 -0.0338 0.0205  930  GLU A O   
6860  C CB  . GLU A 932  ? 0.3359 0.2661 0.3691 -0.0120 -0.0278 0.0223  930  GLU A CB  
6861  C CG  . GLU A 932  ? 0.3562 0.2870 0.3843 -0.0102 -0.0252 0.0210  930  GLU A CG  
6862  C CD  . GLU A 932  ? 0.4250 0.3574 0.4542 -0.0122 -0.0256 0.0258  930  GLU A CD  
6863  O OE1 . GLU A 932  ? 0.3938 0.3299 0.4227 -0.0151 -0.0257 0.0302  930  GLU A OE1 
6864  O OE2 . GLU A 932  ? 0.3997 0.3300 0.4300 -0.0109 -0.0260 0.0250  930  GLU A OE2 
6865  N N   . LEU A 933  ? 0.3483 0.2787 0.3821 -0.0112 -0.0287 0.0164  931  LEU A N   
6866  C CA  . LEU A 933  ? 0.3215 0.2521 0.3592 -0.0128 -0.0307 0.0170  931  LEU A CA  
6867  C C   . LEU A 933  ? 0.4608 0.3963 0.4969 -0.0161 -0.0297 0.0221  931  LEU A C   
6868  O O   . LEU A 933  ? 0.4117 0.3507 0.4420 -0.0165 -0.0269 0.0238  931  LEU A O   
6869  C CB  . LEU A 933  ? 0.4138 0.3441 0.4485 -0.0104 -0.0297 0.0117  931  LEU A CB  
6870  C CG  . LEU A 933  ? 0.4403 0.3671 0.4765 -0.0070 -0.0307 0.0059  931  LEU A CG  
6871  C CD1 . LEU A 933  ? 0.4969 0.4247 0.5302 -0.0051 -0.0299 0.0014  931  LEU A CD1 
6872  C CD2 . LEU A 933  ? 0.4542 0.3771 0.4999 -0.0074 -0.0350 0.0059  931  LEU A CD2 
6873  N N   . GLU A 934  ? 0.3989 0.3348 0.4405 -0.0184 -0.0322 0.0245  932  GLU A N   
6874  C CA  . GLU A 934  ? 0.4888 0.4299 0.5291 -0.0215 -0.0313 0.0289  932  GLU A CA  
6875  C C   . GLU A 934  ? 0.5127 0.4564 0.5480 -0.0205 -0.0291 0.0259  932  GLU A C   
6876  O O   . GLU A 934  ? 0.5752 0.5237 0.6049 -0.0212 -0.0264 0.0272  932  GLU A O   
6877  C CB  . GLU A 934  ? 0.5324 0.4734 0.5816 -0.0247 -0.0351 0.0336  932  GLU A CB  
6878  N N   . LYS A 935  ? 0.5203 0.4609 0.5576 -0.0187 -0.0304 0.0216  933  LYS A N   
6879  C CA  . LYS A 935  ? 0.5187 0.4612 0.5518 -0.0176 -0.0287 0.0185  933  LYS A CA  
6880  C C   . LYS A 935  ? 0.5629 0.5021 0.5939 -0.0139 -0.0284 0.0123  933  LYS A C   
6881  O O   . LYS A 935  ? 0.5325 0.4676 0.5675 -0.0125 -0.0304 0.0100  933  LYS A O   
6882  C CB  . LYS A 935  ? 0.4929 0.4365 0.5314 -0.0199 -0.0311 0.0202  933  LYS A CB  
6883  N N   . LEU A 936  ? 0.5457 0.4870 0.5705 -0.0122 -0.0258 0.0095  934  LEU A N   
6884  C CA  . LEU A 936  ? 0.5529 0.4921 0.5755 -0.0087 -0.0254 0.0039  934  LEU A CA  
6885  C C   . LEU A 936  ? 0.5660 0.5030 0.5946 -0.0084 -0.0287 0.0011  934  LEU A C   
6886  O O   . LEU A 936  ? 0.5720 0.5068 0.6009 -0.0056 -0.0294 -0.0036 934  LEU A O   
6887  C CB  . LEU A 936  ? 0.5177 0.4600 0.5330 -0.0072 -0.0222 0.0022  934  LEU A CB  
6888  C CG  . LEU A 936  ? 0.5828 0.5245 0.5930 -0.0039 -0.0201 -0.0014 934  LEU A CG  
6889  C CD1 . LEU A 936  ? 0.5122 0.4572 0.5160 -0.0032 -0.0169 -0.0016 934  LEU A CD1 
6890  C CD2 . LEU A 936  ? 0.5544 0.4939 0.5664 -0.0014 -0.0217 -0.0062 934  LEU A CD2 
6891  N N   . SER A 937  ? 0.5922 0.5300 0.6256 -0.0111 -0.0307 0.0038  935  SER A N   
6892  C CA  . SER A 937  ? 0.5921 0.5275 0.6324 -0.0112 -0.0343 0.0015  935  SER A CA  
6893  C C   . SER A 937  ? 0.5490 0.4800 0.5964 -0.0107 -0.0375 0.0005  935  SER A C   
6894  O O   . SER A 937  ? 0.5810 0.5095 0.6343 -0.0100 -0.0406 -0.0028 935  SER A O   
6895  C CB  . SER A 937  ? 0.6092 0.5468 0.6538 -0.0147 -0.0358 0.0056  935  SER A CB  
6896  O OG  . SER A 937  ? 0.6498 0.5879 0.6979 -0.0178 -0.0366 0.0115  935  SER A OG  
6897  N N   . ASP A 938  ? 0.5889 0.5188 0.6361 -0.0111 -0.0370 0.0030  936  ASP A N   
6898  C CA  . ASP A 938  ? 0.5523 0.4779 0.6060 -0.0103 -0.0399 0.0017  936  ASP A CA  
6899  C C   . ASP A 938  ? 0.5928 0.5166 0.6453 -0.0062 -0.0400 -0.0053 936  ASP A C   
6900  O O   . ASP A 938  ? 0.5930 0.5133 0.6522 -0.0051 -0.0431 -0.0080 936  ASP A O   
6901  C CB  . ASP A 938  ? 0.6301 0.5554 0.6828 -0.0112 -0.0389 0.0057  936  ASP A CB  
6902  C CG  . ASP A 938  ? 0.6557 0.5832 0.7112 -0.0153 -0.0395 0.0129  936  ASP A CG  
6903  O OD1 . ASP A 938  ? 0.6485 0.5773 0.7077 -0.0176 -0.0411 0.0149  936  ASP A OD1 
6904  O OD2 . ASP A 938  ? 0.6265 0.5549 0.6803 -0.0163 -0.0384 0.0166  936  ASP A OD2 
6905  N N   . LEU A 939  ? 0.5391 0.4654 0.5834 -0.0039 -0.0367 -0.0083 937  LEU A N   
6906  C CA  . LEU A 939  ? 0.5485 0.4745 0.5910 -0.0001 -0.0366 -0.0148 937  LEU A CA  
6907  C C   . LEU A 939  ? 0.6002 0.5270 0.6446 0.0008  -0.0382 -0.0187 937  LEU A C   
6908  O O   . LEU A 939  ? 0.5785 0.5075 0.6208 -0.0008 -0.0374 -0.0169 937  LEU A O   
6909  C CB  . LEU A 939  ? 0.5217 0.4505 0.5548 0.0020  -0.0323 -0.0155 937  LEU A CB  
6910  C CG  . LEU A 939  ? 0.4988 0.4270 0.5295 0.0017  -0.0305 -0.0126 937  LEU A CG  
6911  C CD1 . LEU A 939  ? 0.4968 0.4274 0.5196 0.0043  -0.0269 -0.0147 937  LEU A CD1 
6912  C CD2 . LEU A 939  ? 0.5413 0.4660 0.5788 0.0021  -0.0333 -0.0135 937  LEU A CD2 
6913  N N   . GLN A 940  ? 0.5270 0.4523 0.5753 0.0033  -0.0406 -0.0244 938  GLN A N   
6914  C CA  . GLN A 940  ? 0.5993 0.5255 0.6498 0.0045  -0.0425 -0.0291 938  GLN A CA  
6915  C C   . GLN A 940  ? 0.6009 0.5307 0.6443 0.0082  -0.0402 -0.0342 938  GLN A C   
6916  O O   . GLN A 940  ? 0.6879 0.6207 0.7263 0.0084  -0.0385 -0.0345 938  GLN A O   
6917  C CB  . GLN A 940  ? 0.5632 0.4858 0.6243 0.0047  -0.0474 -0.0322 938  GLN A CB  
6918  N N   . ARG A 941  ? 0.5623 0.4921 0.6053 0.0111  -0.0401 -0.0381 939  ARG A N   
6919  C CA  . ARG A 941  ? 0.4357 0.3695 0.4723 0.0146  -0.0379 -0.0428 939  ARG A CA  
6920  C C   . ARG A 941  ? 0.3832 0.3179 0.4147 0.0160  -0.0350 -0.0417 939  ARG A C   
6921  O O   . ARG A 941  ? 0.4357 0.3675 0.4694 0.0145  -0.0350 -0.0383 939  ARG A O   
6922  C CB  . ARG A 941  ? 0.5016 0.4362 0.5431 0.0174  -0.0411 -0.0502 939  ARG A CB  
6923  N N   . GLU A 942  ? 0.3728 0.3118 0.3976 0.0187  -0.0324 -0.0444 940  GLU A N   
6924  C CA  . GLU A 942  ? 0.3351 0.2757 0.3552 0.0203  -0.0296 -0.0439 940  GLU A CA  
6925  C C   . GLU A 942  ? 0.3152 0.2535 0.3411 0.0216  -0.0317 -0.0467 940  GLU A C   
6926  O O   . GLU A 942  ? 0.3428 0.2813 0.3738 0.0234  -0.0346 -0.0521 940  GLU A O   
6927  C CB  . GLU A 942  ? 0.3158 0.2621 0.3296 0.0233  -0.0275 -0.0473 940  GLU A CB  
6928  C CG  . GLU A 942  ? 0.2951 0.2439 0.3042 0.0252  -0.0247 -0.0472 940  GLU A CG  
6929  C CD  . GLU A 942  ? 0.2916 0.2468 0.2955 0.0282  -0.0231 -0.0507 940  GLU A CD  
6930  O OE1 . GLU A 942  ? 0.3508 0.3083 0.3574 0.0302  -0.0253 -0.0563 940  GLU A OE1 
6931  O OE2 . GLU A 942  ? 0.2799 0.2380 0.2775 0.0286  -0.0199 -0.0480 940  GLU A OE2 
6932  N N   . VAL A 943  ? 0.3167 0.2531 0.3421 0.0208  -0.0304 -0.0432 941  VAL A N   
6933  C CA  . VAL A 943  ? 0.3013 0.2360 0.3314 0.0222  -0.0319 -0.0454 941  VAL A CA  
6934  C C   . VAL A 943  ? 0.3343 0.2727 0.3579 0.0245  -0.0285 -0.0461 941  VAL A C   
6935  O O   . VAL A 943  ? 0.3007 0.2390 0.3198 0.0232  -0.0257 -0.0415 941  VAL A O   
6936  C CB  . VAL A 943  ? 0.3250 0.2546 0.3603 0.0193  -0.0334 -0.0406 941  VAL A CB  
6937  C CG1 . VAL A 943  ? 0.3253 0.2531 0.3655 0.0209  -0.0349 -0.0429 941  VAL A CG1 
6938  C CG2 . VAL A 943  ? 0.3567 0.2831 0.3986 0.0168  -0.0367 -0.0394 941  VAL A CG2 
6939  N N   . PHE A 944  ? 0.3220 0.2643 0.3455 0.0279  -0.0288 -0.0520 942  PHE A N   
6940  C CA  . PHE A 944  ? 0.2675 0.2150 0.2844 0.0302  -0.0255 -0.0529 942  PHE A CA  
6941  C C   . PHE A 944  ? 0.3051 0.2517 0.3243 0.0312  -0.0253 -0.0532 942  PHE A C   
6942  O O   . PHE A 944  ? 0.3024 0.2515 0.3239 0.0341  -0.0263 -0.0584 942  PHE A O   
6943  C CB  . PHE A 944  ? 0.2800 0.2334 0.2951 0.0334  -0.0257 -0.0589 942  PHE A CB  
6944  C CG  . PHE A 944  ? 0.2687 0.2284 0.2757 0.0351  -0.0220 -0.0583 942  PHE A CG  
6945  C CD1 . PHE A 944  ? 0.2596 0.2203 0.2606 0.0335  -0.0194 -0.0537 942  PHE A CD1 
6946  C CD2 . PHE A 944  ? 0.2497 0.2148 0.2557 0.0383  -0.0213 -0.0624 942  PHE A CD2 
6947  C CE1 . PHE A 944  ? 0.2479 0.2144 0.2423 0.0350  -0.0163 -0.0527 942  PHE A CE1 
6948  C CE2 . PHE A 944  ? 0.2642 0.2357 0.2631 0.0396  -0.0179 -0.0613 942  PHE A CE2 
6949  C CZ  . PHE A 944  ? 0.2436 0.2155 0.2369 0.0379  -0.0155 -0.0563 942  PHE A CZ  
6950  N N   . GLY A 945  ? 0.2896 0.2326 0.3083 0.0288  -0.0242 -0.0476 943  GLY A N   
6951  C CA  . GLY A 945  ? 0.2907 0.2322 0.3118 0.0293  -0.0241 -0.0471 943  GLY A CA  
6952  C C   . GLY A 945  ? 0.2835 0.2226 0.3015 0.0266  -0.0219 -0.0406 943  GLY A C   
6953  O O   . GLY A 945  ? 0.2819 0.2211 0.2956 0.0247  -0.0202 -0.0368 943  GLY A O   
6954  N N   . PRO A 946  ? 0.2771 0.2143 0.2976 0.0266  -0.0220 -0.0393 944  PRO A N   
6955  C CA  . PRO A 946  ? 0.2816 0.2174 0.2988 0.0244  -0.0198 -0.0335 944  PRO A CA  
6956  C C   . PRO A 946  ? 0.2692 0.2003 0.2901 0.0210  -0.0216 -0.0291 944  PRO A C   
6957  O O   . PRO A 946  ? 0.2946 0.2230 0.3189 0.0198  -0.0226 -0.0265 944  PRO A O   
6958  C CB  . PRO A 946  ? 0.2832 0.2197 0.3021 0.0262  -0.0194 -0.0348 944  PRO A CB  
6959  C CG  . PRO A 946  ? 0.3132 0.2482 0.3396 0.0278  -0.0231 -0.0397 944  PRO A CG  
6960  C CD  . PRO A 946  ? 0.2881 0.2248 0.3146 0.0288  -0.0243 -0.0435 944  PRO A CD  
6961  N N   . VAL A 947  ? 0.2923 0.2230 0.3126 0.0193  -0.0222 -0.0279 945  VAL A N   
6962  C CA  . VAL A 947  ? 0.2859 0.2131 0.3103 0.0161  -0.0242 -0.0240 945  VAL A CA  
6963  C C   . VAL A 947  ? 0.2924 0.2209 0.3111 0.0139  -0.0219 -0.0200 945  VAL A C   
6964  O O   . VAL A 947  ? 0.2960 0.2262 0.3125 0.0141  -0.0216 -0.0214 945  VAL A O   
6965  C CB  . VAL A 947  ? 0.3332 0.2582 0.3647 0.0160  -0.0281 -0.0267 945  VAL A CB  
6966  C CG1 . VAL A 947  ? 0.3086 0.2303 0.3446 0.0124  -0.0302 -0.0217 945  VAL A CG1 
6967  C CG2 . VAL A 947  ? 0.2972 0.2211 0.3345 0.0186  -0.0305 -0.0316 945  VAL A CG2 
6968  N N   . LEU A 948  ? 0.2679 0.1960 0.2846 0.0119  -0.0204 -0.0154 946  LEU A N   
6969  C CA  . LEU A 948  ? 0.2462 0.1757 0.2582 0.0098  -0.0183 -0.0117 946  LEU A CA  
6970  C C   . LEU A 948  ? 0.2770 0.2048 0.2931 0.0066  -0.0205 -0.0080 946  LEU A C   
6971  O O   . LEU A 948  ? 0.3270 0.2527 0.3477 0.0053  -0.0223 -0.0057 946  LEU A O   
6972  C CB  . LEU A 948  ? 0.2734 0.2040 0.2811 0.0096  -0.0156 -0.0091 946  LEU A CB  
6973  C CG  . LEU A 948  ? 0.2669 0.1993 0.2703 0.0075  -0.0136 -0.0057 946  LEU A CG  
6974  C CD1 . LEU A 948  ? 0.2828 0.2175 0.2821 0.0086  -0.0121 -0.0077 946  LEU A CD1 
6975  C CD2 . LEU A 948  ? 0.3060 0.2393 0.3063 0.0073  -0.0114 -0.0036 946  LEU A CD2 
6976  N N   . HIS A 949  ? 0.2751 0.2042 0.2898 0.0053  -0.0203 -0.0072 947  HIS A N   
6977  C CA  . HIS A 949  ? 0.2937 0.2223 0.3116 0.0021  -0.0219 -0.0031 947  HIS A CA  
6978  C C   . HIS A 949  ? 0.2990 0.2304 0.3117 0.0003  -0.0191 0.0005  947  HIS A C   
6979  O O   . HIS A 949  ? 0.2969 0.2304 0.3038 0.0016  -0.0164 -0.0007 947  HIS A O   
6980  C CB  . HIS A 949  ? 0.3019 0.2303 0.3228 0.0017  -0.0238 -0.0047 947  HIS A CB  
6981  C CG  . HIS A 949  ? 0.3323 0.2585 0.3582 0.0038  -0.0265 -0.0093 947  HIS A CG  
6982  N ND1 . HIS A 949  ? 0.3031 0.2306 0.3261 0.0070  -0.0255 -0.0144 947  HIS A ND1 
6983  C CD2 . HIS A 949  ? 0.3690 0.2921 0.4030 0.0033  -0.0301 -0.0098 947  HIS A CD2 
6984  C CE1 . HIS A 949  ? 0.3332 0.2587 0.3620 0.0085  -0.0284 -0.0182 947  HIS A CE1 
6985  N NE2 . HIS A 949  ? 0.3427 0.2652 0.3785 0.0063  -0.0314 -0.0156 947  HIS A NE2 
6986  N N   . VAL A 950  ? 0.2807 0.2125 0.2956 -0.0025 -0.0200 0.0050  948  VAL A N   
6987  C CA  . VAL A 950  ? 0.2912 0.2262 0.3017 -0.0042 -0.0176 0.0083  948  VAL A CA  
6988  C C   . VAL A 950  ? 0.3371 0.2742 0.3497 -0.0072 -0.0187 0.0117  948  VAL A C   
6989  O O   . VAL A 950  ? 0.3495 0.2854 0.3679 -0.0091 -0.0215 0.0143  948  VAL A O   
6990  C CB  . VAL A 950  ? 0.3062 0.2411 0.3164 -0.0047 -0.0171 0.0107  948  VAL A CB  
6991  C CG1 . VAL A 950  ? 0.3267 0.2656 0.3326 -0.0064 -0.0148 0.0136  948  VAL A CG1 
6992  C CG2 . VAL A 950  ? 0.2831 0.2165 0.2913 -0.0017 -0.0158 0.0074  948  VAL A CG2 
6993  N N   . ILE A 951  ? 0.2916 0.2320 0.2999 -0.0076 -0.0167 0.0118  949  ILE A N   
6994  C CA  . ILE A 951  ? 0.3071 0.2507 0.3166 -0.0105 -0.0172 0.0153  949  ILE A CA  
6995  C C   . ILE A 951  ? 0.2985 0.2465 0.3030 -0.0114 -0.0145 0.0171  949  ILE A C   
6996  O O   . ILE A 951  ? 0.2870 0.2353 0.2869 -0.0095 -0.0122 0.0149  949  ILE A O   
6997  C CB  . ILE A 951  ? 0.3608 0.3048 0.3711 -0.0105 -0.0179 0.0136  949  ILE A CB  
6998  C CG1 . ILE A 951  ? 0.3639 0.3093 0.3682 -0.0083 -0.0151 0.0103  949  ILE A CG1 
6999  C CG2 . ILE A 951  ? 0.4274 0.3673 0.4431 -0.0095 -0.0208 0.0112  949  ILE A CG2 
7000  C CD1 . ILE A 951  ? 0.5312 0.4771 0.5361 -0.0080 -0.0158 0.0083  949  ILE A CD1 
7001  N N   . ARG A 952  ? 0.2965 0.2483 0.3024 -0.0143 -0.0150 0.0211  950  ARG A N   
7002  C CA  . ARG A 952  ? 0.2842 0.2412 0.2860 -0.0153 -0.0127 0.0228  950  ARG A CA  
7003  C C   . ARG A 952  ? 0.2684 0.2298 0.2691 -0.0164 -0.0120 0.0231  950  ARG A C   
7004  O O   . ARG A 952  ? 0.3254 0.2866 0.3298 -0.0177 -0.0139 0.0241  950  ARG A O   
7005  C CB  . ARG A 952  ? 0.3170 0.2766 0.3211 -0.0178 -0.0138 0.0274  950  ARG A CB  
7006  C CG  . ARG A 952  ? 0.3195 0.2747 0.3260 -0.0171 -0.0151 0.0277  950  ARG A CG  
7007  C CD  . ARG A 952  ? 0.3762 0.3333 0.3870 -0.0200 -0.0172 0.0329  950  ARG A CD  
7008  N NE  . ARG A 952  ? 0.4202 0.3827 0.4277 -0.0211 -0.0156 0.0352  950  ARG A NE  
7009  C CZ  . ARG A 952  ? 0.3953 0.3572 0.4022 -0.0207 -0.0154 0.0359  950  ARG A CZ  
7010  N NH1 . ARG A 952  ? 0.3860 0.3422 0.3955 -0.0192 -0.0167 0.0346  950  ARG A NH1 
7011  N NH2 . ARG A 952  ? 0.3627 0.3301 0.3664 -0.0218 -0.0140 0.0377  950  ARG A NH2 
7012  N N   . TYR A 953  ? 0.2682 0.2334 0.2643 -0.0159 -0.0095 0.0220  951  TYR A N   
7013  C CA  . TYR A 953  ? 0.2754 0.2452 0.2704 -0.0168 -0.0087 0.0220  951  TYR A CA  
7014  C C   . TYR A 953  ? 0.2640 0.2402 0.2559 -0.0177 -0.0067 0.0229  951  TYR A C   
7015  O O   . TYR A 953  ? 0.2743 0.2504 0.2635 -0.0165 -0.0054 0.0217  951  TYR A O   
7016  C CB  . TYR A 953  ? 0.2834 0.2510 0.2764 -0.0144 -0.0078 0.0179  951  TYR A CB  
7017  C CG  . TYR A 953  ? 0.2602 0.2275 0.2487 -0.0119 -0.0054 0.0149  951  TYR A CG  
7018  C CD1 . TYR A 953  ? 0.2522 0.2150 0.2397 -0.0099 -0.0051 0.0132  951  TYR A CD1 
7019  C CD2 . TYR A 953  ? 0.2678 0.2394 0.2535 -0.0117 -0.0035 0.0139  951  TYR A CD2 
7020  C CE1 . TYR A 953  ? 0.2440 0.2066 0.2280 -0.0079 -0.0030 0.0110  951  TYR A CE1 
7021  C CE2 . TYR A 953  ? 0.2432 0.2143 0.2256 -0.0096 -0.0016 0.0114  951  TYR A CE2 
7022  C CZ  . TYR A 953  ? 0.2498 0.2163 0.2315 -0.0078 -0.0014 0.0101  951  TYR A CZ  
7023  O OH  . TYR A 953  ? 0.2822 0.2484 0.2614 -0.0059 0.0004  0.0080  951  TYR A OH  
7024  N N   . ARG A 954  ? 0.3030 0.2851 0.2955 -0.0197 -0.0067 0.0248  952  ARG A N   
7025  C CA  . ARG A 954  ? 0.3032 0.2924 0.2928 -0.0203 -0.0048 0.0249  952  ARG A CA  
7026  C C   . ARG A 954  ? 0.2624 0.2518 0.2489 -0.0179 -0.0028 0.0205  952  ARG A C   
7027  O O   . ARG A 954  ? 0.2683 0.2551 0.2553 -0.0170 -0.0032 0.0189  952  ARG A O   
7028  C CB  . ARG A 954  ? 0.3539 0.3503 0.3456 -0.0234 -0.0055 0.0287  952  ARG A CB  
7029  N N   . ARG A 955  ? 0.3048 0.2973 0.2882 -0.0169 -0.0010 0.0187  953  ARG A N   
7030  C CA  . ARG A 955  ? 0.2958 0.2877 0.2768 -0.0144 0.0007  0.0145  953  ARG A CA  
7031  C C   . ARG A 955  ? 0.2852 0.2801 0.2668 -0.0147 0.0008  0.0138  953  ARG A C   
7032  O O   . ARG A 955  ? 0.3183 0.3099 0.2993 -0.0127 0.0011  0.0112  953  ARG A O   
7033  C CB  . ARG A 955  ? 0.3758 0.3720 0.3546 -0.0138 0.0023  0.0128  953  ARG A CB  
7034  C CG  . ARG A 955  ? 0.4589 0.4552 0.4362 -0.0114 0.0038  0.0087  953  ARG A CG  
7035  C CD  . ARG A 955  ? 0.5333 0.5220 0.5103 -0.0092 0.0037  0.0071  953  ARG A CD  
7036  N NE  . ARG A 955  ? 0.5986 0.5867 0.5748 -0.0069 0.0048  0.0038  953  ARG A NE  
7037  C CZ  . ARG A 955  ? 0.5464 0.5350 0.5229 -0.0062 0.0048  0.0026  953  ARG A CZ  
7038  N NH1 . ARG A 955  ? 0.4378 0.4280 0.4155 -0.0078 0.0039  0.0042  953  ARG A NH1 
7039  N NH2 . ARG A 955  ? 0.5154 0.5028 0.4915 -0.0040 0.0057  -0.0001 953  ARG A NH2 
7040  N N   . ASP A 956  ? 0.2946 0.2961 0.2775 -0.0171 0.0004  0.0163  954  ASP A N   
7041  C CA  . ASP A 956  ? 0.2951 0.3000 0.2787 -0.0174 0.0006  0.0156  954  ASP A CA  
7042  C C   . ASP A 956  ? 0.3347 0.3343 0.3206 -0.0174 -0.0010 0.0160  954  ASP A C   
7043  O O   . ASP A 956  ? 0.3263 0.3270 0.3126 -0.0169 -0.0009 0.0147  954  ASP A O   
7044  C CB  . ASP A 956  ? 0.3111 0.3251 0.2959 -0.0202 0.0005  0.0186  954  ASP A CB  
7045  C CG  . ASP A 956  ? 0.3997 0.4208 0.3822 -0.0200 0.0023  0.0172  954  ASP A CG  
7046  O OD1 . ASP A 956  ? 0.4080 0.4272 0.3885 -0.0174 0.0035  0.0132  954  ASP A OD1 
7047  O OD2 . ASP A 956  ? 0.4542 0.4832 0.4372 -0.0223 0.0023  0.0200  954  ASP A OD2 
7048  N N   . ASP A 957  ? 0.2892 0.2832 0.2769 -0.0177 -0.0026 0.0177  955  ASP A N   
7049  C CA  . ASP A 957  ? 0.3014 0.2902 0.2916 -0.0176 -0.0044 0.0175  955  ASP A CA  
7050  C C   . ASP A 957  ? 0.2838 0.2662 0.2722 -0.0144 -0.0041 0.0139  955  ASP A C   
7051  O O   . ASP A 957  ? 0.2928 0.2706 0.2832 -0.0139 -0.0057 0.0133  955  ASP A O   
7052  C CB  . ASP A 957  ? 0.3462 0.3329 0.3403 -0.0197 -0.0067 0.0212  955  ASP A CB  
7053  C CG  . ASP A 957  ? 0.4309 0.4243 0.4277 -0.0231 -0.0075 0.0256  955  ASP A CG  
7054  O OD1 . ASP A 957  ? 0.4128 0.4116 0.4093 -0.0238 -0.0067 0.0255  955  ASP A OD1 
7055  O OD2 . ASP A 957  ? 0.4405 0.4340 0.4398 -0.0251 -0.0089 0.0293  955  ASP A OD2 
7056  N N   . LEU A 958  ? 0.2846 0.2670 0.2697 -0.0124 -0.0022 0.0114  956  LEU A N   
7057  C CA  . LEU A 958  ? 0.2846 0.2616 0.2680 -0.0095 -0.0018 0.0085  956  LEU A CA  
7058  C C   . LEU A 958  ? 0.2704 0.2460 0.2544 -0.0085 -0.0024 0.0067  956  LEU A C   
7059  O O   . LEU A 958  ? 0.2660 0.2370 0.2503 -0.0071 -0.0033 0.0054  956  LEU A O   
7060  C CB  . LEU A 958  ? 0.2784 0.2563 0.2589 -0.0078 0.0003  0.0065  956  LEU A CB  
7061  C CG  . LEU A 958  ? 0.2855 0.2588 0.2643 -0.0049 0.0009  0.0040  956  LEU A CG  
7062  C CD1 . LEU A 958  ? 0.2975 0.2657 0.2768 -0.0044 0.0000  0.0043  956  LEU A CD1 
7063  C CD2 . LEU A 958  ? 0.3183 0.2928 0.2953 -0.0035 0.0027  0.0024  956  LEU A CD2 
7064  N N   . ASP A 959  ? 0.2391 0.2190 0.2232 -0.0091 -0.0019 0.0065  957  ASP A N   
7065  C CA  . ASP A 959  ? 0.2716 0.2506 0.2562 -0.0081 -0.0026 0.0048  957  ASP A CA  
7066  C C   . ASP A 959  ? 0.2651 0.2417 0.2530 -0.0093 -0.0049 0.0059  957  ASP A C   
7067  O O   . ASP A 959  ? 0.2791 0.2523 0.2673 -0.0078 -0.0058 0.0040  957  ASP A O   
7068  C CB  . ASP A 959  ? 0.2980 0.2825 0.2826 -0.0085 -0.0017 0.0043  957  ASP A CB  
7069  C CG  . ASP A 959  ? 0.3292 0.3126 0.3135 -0.0068 -0.0019 0.0021  957  ASP A CG  
7070  O OD1 . ASP A 959  ? 0.3128 0.2930 0.2951 -0.0043 -0.0013 0.0001  957  ASP A OD1 
7071  O OD2 . ASP A 959  ? 0.4023 0.3880 0.3885 -0.0079 -0.0028 0.0025  957  ASP A OD2 
7072  N N   . ARG A 960  ? 0.2697 0.2482 0.2604 -0.0121 -0.0060 0.0090  958  ARG A N   
7073  C CA  . ARG A 960  ? 0.3040 0.2799 0.2989 -0.0134 -0.0086 0.0103  958  ARG A CA  
7074  C C   . ARG A 960  ? 0.2879 0.2577 0.2831 -0.0118 -0.0096 0.0088  958  ARG A C   
7075  O O   . ARG A 960  ? 0.3067 0.2732 0.3042 -0.0111 -0.0114 0.0073  958  ARG A O   
7076  C CB  . ARG A 960  ? 0.3117 0.2911 0.3100 -0.0168 -0.0097 0.0146  958  ARG A CB  
7077  C CG  . ARG A 960  ? 0.3499 0.3269 0.3539 -0.0187 -0.0127 0.0166  958  ARG A CG  
7078  C CD  . ARG A 960  ? 0.4907 0.4624 0.4967 -0.0185 -0.0142 0.0171  958  ARG A CD  
7079  N NE  . ARG A 960  ? 0.5048 0.4784 0.5096 -0.0195 -0.0133 0.0198  958  ARG A NE  
7080  C CZ  . ARG A 960  ? 0.5499 0.5197 0.5542 -0.0185 -0.0134 0.0195  958  ARG A CZ  
7081  N NH1 . ARG A 960  ? 0.5260 0.4901 0.5308 -0.0163 -0.0143 0.0165  958  ARG A NH1 
7082  N NH2 . ARG A 960  ? 0.5835 0.5558 0.5868 -0.0197 -0.0126 0.0221  958  ARG A NH2 
7083  N N   . LEU A 961  ? 0.2748 0.2434 0.2678 -0.0111 -0.0084 0.0091  959  LEU A N   
7084  C CA  . LEU A 961  ? 0.2751 0.2386 0.2683 -0.0094 -0.0091 0.0077  959  LEU A CA  
7085  C C   . LEU A 961  ? 0.2915 0.2526 0.2825 -0.0065 -0.0087 0.0039  959  LEU A C   
7086  O O   . LEU A 961  ? 0.2810 0.2387 0.2739 -0.0054 -0.0103 0.0022  959  LEU A O   
7087  C CB  . LEU A 961  ? 0.2738 0.2371 0.2646 -0.0091 -0.0076 0.0085  959  LEU A CB  
7088  C CG  . LEU A 961  ? 0.2561 0.2146 0.2464 -0.0070 -0.0078 0.0067  959  LEU A CG  
7089  C CD1 . LEU A 961  ? 0.3591 0.3145 0.3541 -0.0079 -0.0105 0.0075  959  LEU A CD1 
7090  C CD2 . LEU A 961  ? 0.3029 0.2619 0.2907 -0.0066 -0.0061 0.0074  959  LEU A CD2 
7091  N N   . VAL A 962  ? 0.2518 0.2149 0.2392 -0.0051 -0.0067 0.0026  960  VAL A N   
7092  C CA  . VAL A 962  ? 0.2600 0.2217 0.2454 -0.0024 -0.0063 -0.0004 960  VAL A CA  
7093  C C   . VAL A 962  ? 0.2977 0.2591 0.2857 -0.0026 -0.0083 -0.0016 960  VAL A C   
7094  O O   . VAL A 962  ? 0.2794 0.2387 0.2674 -0.0008 -0.0092 -0.0041 960  VAL A O   
7095  C CB  . VAL A 962  ? 0.2850 0.2492 0.2671 -0.0012 -0.0041 -0.0012 960  VAL A CB  
7096  C CG1 . VAL A 962  ? 0.3078 0.2712 0.2883 0.0013  -0.0040 -0.0037 960  VAL A CG1 
7097  C CG2 . VAL A 962  ? 0.2894 0.2532 0.2694 -0.0007 -0.0024 -0.0006 960  VAL A CG2 
7098  N N   . ASP A 963  ? 0.2918 0.2559 0.2823 -0.0049 -0.0091 0.0000  961  ASP A N   
7099  C CA  . ASP A 963  ? 0.3010 0.2647 0.2948 -0.0054 -0.0114 -0.0009 961  ASP A CA  
7100  C C   . ASP A 963  ? 0.2957 0.2554 0.2931 -0.0055 -0.0137 -0.0014 961  ASP A C   
7101  O O   . ASP A 963  ? 0.3347 0.2926 0.3335 -0.0042 -0.0153 -0.0042 961  ASP A O   
7102  C CB  . ASP A 963  ? 0.3164 0.2838 0.3129 -0.0083 -0.0119 0.0017  961  ASP A CB  
7103  C CG  . ASP A 963  ? 0.4213 0.3929 0.4152 -0.0079 -0.0101 0.0013  961  ASP A CG  
7104  O OD1 . ASP A 963  ? 0.5241 0.4952 0.5148 -0.0054 -0.0090 -0.0012 961  ASP A OD1 
7105  O OD2 . ASP A 963  ? 0.5536 0.5294 0.5489 -0.0101 -0.0099 0.0036  961  ASP A OD2 
7106  N N   . ASP A 964  ? 0.2917 0.2503 0.2910 -0.0071 -0.0142 0.0011  962  ASP A N   
7107  C CA  . ASP A 964  ? 0.3208 0.2755 0.3243 -0.0071 -0.0166 0.0006  962  ASP A CA  
7108  C C   . ASP A 964  ? 0.3559 0.3078 0.3573 -0.0039 -0.0163 -0.0031 962  ASP A C   
7109  O O   . ASP A 964  ? 0.3402 0.2896 0.3447 -0.0030 -0.0186 -0.0056 962  ASP A O   
7110  C CB  . ASP A 964  ? 0.3494 0.3037 0.3549 -0.0092 -0.0169 0.0043  962  ASP A CB  
7111  C CG  . ASP A 964  ? 0.4053 0.3627 0.4142 -0.0126 -0.0178 0.0083  962  ASP A CG  
7112  O OD1 . ASP A 964  ? 0.4707 0.4298 0.4815 -0.0135 -0.0188 0.0082  962  ASP A OD1 
7113  O OD2 . ASP A 964  ? 0.5367 0.4953 0.5465 -0.0145 -0.0177 0.0118  962  ASP A OD2 
7114  N N   . VAL A 965  ? 0.2837 0.2362 0.2800 -0.0022 -0.0137 -0.0037 963  VAL A N   
7115  C CA  . VAL A 965  ? 0.2985 0.2493 0.2924 0.0008  -0.0133 -0.0069 963  VAL A CA  
7116  C C   . VAL A 965  ? 0.3163 0.2681 0.3098 0.0025  -0.0140 -0.0101 963  VAL A C   
7117  O O   . VAL A 965  ? 0.3221 0.2725 0.3168 0.0042  -0.0154 -0.0131 963  VAL A O   
7118  C CB  . VAL A 965  ? 0.2530 0.2047 0.2420 0.0020  -0.0104 -0.0063 963  VAL A CB  
7119  C CG1 . VAL A 965  ? 0.2996 0.2506 0.2862 0.0050  -0.0098 -0.0092 963  VAL A CG1 
7120  C CG2 . VAL A 965  ? 0.2846 0.2353 0.2743 0.0006  -0.0099 -0.0036 963  VAL A CG2 
7121  N N   . ASN A 966  ? 0.2698 0.2244 0.2615 0.0021  -0.0131 -0.0096 964  ASN A N   
7122  C CA  . ASN A 966  ? 0.2615 0.2174 0.2525 0.0036  -0.0137 -0.0124 964  ASN A CA  
7123  C C   . ASN A 966  ? 0.3055 0.2602 0.3017 0.0028  -0.0169 -0.0139 964  ASN A C   
7124  O O   . ASN A 966  ? 0.3119 0.2669 0.3084 0.0046  -0.0181 -0.0173 964  ASN A O   
7125  C CB  . ASN A 966  ? 0.2954 0.2545 0.2842 0.0031  -0.0123 -0.0112 964  ASN A CB  
7126  C CG  . ASN A 966  ? 0.2974 0.2578 0.2816 0.0045  -0.0095 -0.0106 964  ASN A CG  
7127  O OD1 . ASN A 966  ? 0.2778 0.2371 0.2598 0.0064  -0.0087 -0.0115 964  ASN A OD1 
7128  N ND2 . ASN A 966  ? 0.3023 0.2652 0.2853 0.0037  -0.0082 -0.0091 964  ASN A ND2 
7129  N N   . ALA A 967  ? 0.3156 0.2692 0.3163 0.0000  -0.0183 -0.0114 965  ALA A N   
7130  C CA  . ALA A 967  ? 0.3688 0.3213 0.3755 -0.0013 -0.0215 -0.0121 965  ALA A CA  
7131  C C   . ALA A 967  ? 0.3504 0.2998 0.3604 0.0003  -0.0239 -0.0155 965  ALA A C   
7132  O O   . ALA A 967  ? 0.3829 0.3314 0.3979 -0.0001 -0.0267 -0.0174 965  ALA A O   
7133  C CB  . ALA A 967  ? 0.4210 0.3736 0.4319 -0.0049 -0.0225 -0.0077 965  ALA A CB  
7134  N N   . THR A 968  ? 0.3258 0.2738 0.3335 0.0021  -0.0228 -0.0166 966  THR A N   
7135  C CA  . THR A 968  ? 0.3045 0.2503 0.3152 0.0040  -0.0249 -0.0205 966  THR A CA  
7136  C C   . THR A 968  ? 0.3090 0.2568 0.3184 0.0066  -0.0256 -0.0252 966  THR A C   
7137  O O   . THR A 968  ? 0.3415 0.2882 0.3549 0.0078  -0.0282 -0.0291 966  THR A O   
7138  C CB  . THR A 968  ? 0.2948 0.2395 0.3028 0.0057  -0.0234 -0.0208 966  THR A CB  
7139  O OG1 . THR A 968  ? 0.3071 0.2546 0.3084 0.0079  -0.0205 -0.0218 966  THR A OG1 
7140  C CG2 . THR A 968  ? 0.3003 0.2436 0.3088 0.0034  -0.0224 -0.0162 966  THR A CG2 
7141  N N   . GLY A 969  ? 0.2953 0.2464 0.2994 0.0075  -0.0234 -0.0251 967  GLY A N   
7142  C CA  . GLY A 969  ? 0.2936 0.2474 0.2955 0.0100  -0.0237 -0.0292 967  GLY A CA  
7143  C C   . GLY A 969  ? 0.2973 0.2529 0.2941 0.0130  -0.0218 -0.0311 967  GLY A C   
7144  O O   . GLY A 969  ? 0.2789 0.2379 0.2724 0.0151  -0.0212 -0.0335 967  GLY A O   
7145  N N   . TYR A 970  ? 0.2670 0.2208 0.2632 0.0132  -0.0207 -0.0299 968  TYR A N   
7146  C CA  . TYR A 970  ? 0.2615 0.2173 0.2530 0.0157  -0.0185 -0.0309 968  TYR A CA  
7147  C C   . TYR A 970  ? 0.2544 0.2119 0.2406 0.0154  -0.0154 -0.0274 968  TYR A C   
7148  O O   . TYR A 970  ? 0.3140 0.2711 0.3003 0.0133  -0.0149 -0.0244 968  TYR A O   
7149  C CB  . TYR A 970  ? 0.2730 0.2262 0.2663 0.0160  -0.0186 -0.0309 968  TYR A CB  
7150  C CG  . TYR A 970  ? 0.2603 0.2119 0.2592 0.0167  -0.0218 -0.0349 968  TYR A CG  
7151  C CD1 . TYR A 970  ? 0.3109 0.2652 0.3091 0.0198  -0.0224 -0.0398 968  TYR A CD1 
7152  C CD2 . TYR A 970  ? 0.3237 0.2714 0.3289 0.0145  -0.0244 -0.0339 968  TYR A CD2 
7153  C CE1 . TYR A 970  ? 0.3102 0.2633 0.3142 0.0208  -0.0255 -0.0441 968  TYR A CE1 
7154  C CE2 . TYR A 970  ? 0.3413 0.2872 0.3527 0.0152  -0.0276 -0.0377 968  TYR A CE2 
7155  C CZ  . TYR A 970  ? 0.3509 0.2993 0.3617 0.0185  -0.0282 -0.0431 968  TYR A CZ  
7156  O OH  . TYR A 970  ? 0.4634 0.4102 0.4809 0.0194  -0.0316 -0.0475 968  TYR A OH  
7157  N N   . GLY A 971  ? 0.2289 0.1888 0.2109 0.0176  -0.0135 -0.0277 969  GLY A N   
7158  C CA  . GLY A 971  ? 0.2486 0.2101 0.2263 0.0175  -0.0108 -0.0246 969  GLY A CA  
7159  C C   . GLY A 971  ? 0.2288 0.1927 0.2028 0.0198  -0.0089 -0.0248 969  GLY A C   
7160  O O   . GLY A 971  ? 0.2307 0.1981 0.2014 0.0211  -0.0077 -0.0243 969  GLY A O   
7161  N N   . LEU A 972  ? 0.2260 0.1884 0.2008 0.0202  -0.0087 -0.0251 970  LEU A N   
7162  C CA  . LEU A 972  ? 0.2276 0.1929 0.1993 0.0224  -0.0071 -0.0254 970  LEU A CA  
7163  C C   . LEU A 972  ? 0.2289 0.1931 0.1987 0.0216  -0.0047 -0.0215 970  LEU A C   
7164  O O   . LEU A 972  ? 0.2377 0.2037 0.2049 0.0217  -0.0032 -0.0192 970  LEU A O   
7165  C CB  . LEU A 972  ? 0.2364 0.2018 0.2101 0.0239  -0.0084 -0.0289 970  LEU A CB  
7166  C CG  . LEU A 972  ? 0.2464 0.2163 0.2171 0.0264  -0.0069 -0.0299 970  LEU A CG  
7167  C CD1 . LEU A 972  ? 0.2386 0.2140 0.2057 0.0280  -0.0062 -0.0303 970  LEU A CD1 
7168  C CD2 . LEU A 972  ? 0.2596 0.2301 0.2331 0.0280  -0.0086 -0.0343 970  LEU A CD2 
7169  N N   . THR A 973  ? 0.2192 0.1805 0.1905 0.0208  -0.0045 -0.0206 971  THR A N   
7170  C CA  . THR A 973  ? 0.2292 0.1893 0.1990 0.0199  -0.0024 -0.0171 971  THR A CA  
7171  C C   . THR A 973  ? 0.2325 0.1891 0.2044 0.0173  -0.0028 -0.0151 971  THR A C   
7172  O O   . THR A 973  ? 0.2369 0.1914 0.2119 0.0161  -0.0047 -0.0160 971  THR A O   
7173  C CB  . THR A 973  ? 0.2054 0.1656 0.1750 0.0210  -0.0015 -0.0172 971  THR A CB  
7174  O OG1 . THR A 973  ? 0.2367 0.1943 0.2097 0.0206  -0.0033 -0.0190 971  THR A OG1 
7175  C CG2 . THR A 973  ? 0.2323 0.1973 0.1995 0.0236  -0.0008 -0.0188 971  THR A CG2 
7176  N N   . PHE A 974  ? 0.2216 0.1779 0.1921 0.0164  -0.0010 -0.0122 972  PHE A N   
7177  C CA  . PHE A 974  ? 0.2156 0.1698 0.1876 0.0140  -0.0011 -0.0102 972  PHE A CA  
7178  C C   . PHE A 974  ? 0.2050 0.1589 0.1756 0.0138  0.0008  -0.0079 972  PHE A C   
7179  O O   . PHE A 974  ? 0.2393 0.1949 0.2079 0.0149  0.0022  -0.0072 972  PHE A O   
7180  C CB  . PHE A 974  ? 0.2270 0.1823 0.1990 0.0130  -0.0014 -0.0098 972  PHE A CB  
7181  C CG  . PHE A 974  ? 0.2142 0.1687 0.1873 0.0107  -0.0011 -0.0077 972  PHE A CG  
7182  C CD1 . PHE A 974  ? 0.2181 0.1711 0.1940 0.0088  -0.0026 -0.0073 972  PHE A CD1 
7183  C CD2 . PHE A 974  ? 0.2220 0.1774 0.1936 0.0105  0.0006  -0.0062 972  PHE A CD2 
7184  C CE1 . PHE A 974  ? 0.2462 0.1995 0.2229 0.0066  -0.0023 -0.0052 972  PHE A CE1 
7185  C CE2 . PHE A 974  ? 0.2230 0.1785 0.1955 0.0085  0.0008  -0.0047 972  PHE A CE2 
7186  C CZ  . PHE A 974  ? 0.2390 0.1939 0.2138 0.0066  -0.0005 -0.0041 972  PHE A CZ  
7187  N N   . GLY A 975  ? 0.2169 0.1688 0.1890 0.0122  0.0008  -0.0067 973  GLY A N   
7188  C CA  . GLY A 975  ? 0.2125 0.1642 0.1837 0.0118  0.0024  -0.0048 973  GLY A CA  
7189  C C   . GLY A 975  ? 0.1976 0.1492 0.1697 0.0097  0.0025  -0.0033 973  GLY A C   
7190  O O   . GLY A 975  ? 0.2168 0.1681 0.1906 0.0081  0.0012  -0.0031 973  GLY A O   
7191  N N   . LEU A 976  ? 0.2150 0.1674 0.1862 0.0097  0.0039  -0.0022 974  LEU A N   
7192  C CA  . LEU A 976  ? 0.2133 0.1664 0.1850 0.0079  0.0042  -0.0012 974  LEU A CA  
7193  C C   . LEU A 976  ? 0.2294 0.1821 0.2010 0.0079  0.0053  -0.0003 974  LEU A C   
7194  O O   . LEU A 976  ? 0.2356 0.1884 0.2065 0.0093  0.0064  -0.0003 974  LEU A O   
7195  C CB  . LEU A 976  ? 0.2293 0.1845 0.2006 0.0079  0.0046  -0.0015 974  LEU A CB  
7196  C CG  . LEU A 976  ? 0.2245 0.1816 0.1964 0.0064  0.0050  -0.0010 974  LEU A CG  
7197  C CD1 . LEU A 976  ? 0.2620 0.2200 0.2351 0.0043  0.0040  -0.0003 974  LEU A CD1 
7198  C CD2 . LEU A 976  ? 0.2809 0.2399 0.2527 0.0071  0.0055  -0.0017 974  LEU A CD2 
7199  N N   . HIS A 977  ? 0.2223 0.1749 0.1948 0.0064  0.0051  0.0005  975  HIS A N   
7200  C CA  . HIS A 977  ? 0.2279 0.1805 0.2005 0.0062  0.0060  0.0012  975  HIS A CA  
7201  C C   . HIS A 977  ? 0.2086 0.1638 0.1816 0.0047  0.0062  0.0013  975  HIS A C   
7202  O O   . HIS A 977  ? 0.2327 0.1892 0.2062 0.0030  0.0054  0.0021  975  HIS A O   
7203  C CB  . HIS A 977  ? 0.2417 0.1927 0.2150 0.0057  0.0055  0.0020  975  HIS A CB  
7204  C CG  . HIS A 977  ? 0.2754 0.2248 0.2484 0.0074  0.0060  0.0017  975  HIS A CG  
7205  N ND1 . HIS A 977  ? 0.3272 0.2764 0.3003 0.0078  0.0070  0.0022  975  HIS A ND1 
7206  C CD2 . HIS A 977  ? 0.3531 0.3017 0.3258 0.0089  0.0057  0.0009  975  HIS A CD2 
7207  C CE1 . HIS A 977  ? 0.3083 0.2566 0.2812 0.0093  0.0074  0.0021  975  HIS A CE1 
7208  N NE2 . HIS A 977  ? 0.3029 0.2511 0.2755 0.0101  0.0067  0.0012  975  HIS A NE2 
7209  N N   . THR A 978  ? 0.2063 0.1626 0.1792 0.0055  0.0072  0.0006  976  THR A N   
7210  C CA  . THR A 978  ? 0.2293 0.1886 0.2027 0.0045  0.0075  0.0001  976  THR A CA  
7211  C C   . THR A 978  ? 0.2250 0.1842 0.1993 0.0057  0.0083  -0.0009 976  THR A C   
7212  O O   . THR A 978  ? 0.2585 0.2159 0.2329 0.0073  0.0087  -0.0008 976  THR A O   
7213  C CB  . THR A 978  ? 0.2499 0.2116 0.2233 0.0039  0.0071  -0.0005 976  THR A CB  
7214  O OG1 . THR A 978  ? 0.2504 0.2158 0.2244 0.0031  0.0075  -0.0013 976  THR A OG1 
7215  C CG2 . THR A 978  ? 0.2668 0.2276 0.2400 0.0056  0.0073  -0.0013 976  THR A CG2 
7216  N N   . ARG A 979  ? 0.2351 0.1968 0.2104 0.0051  0.0086  -0.0018 977  ARG A N   
7217  C CA  . ARG A 979  ? 0.2575 0.2193 0.2345 0.0062  0.0091  -0.0031 977  ARG A CA  
7218  C C   . ARG A 979  ? 0.2315 0.1961 0.2095 0.0065  0.0091  -0.0048 977  ARG A C   
7219  O O   . ARG A 979  ? 0.2933 0.2581 0.2735 0.0076  0.0093  -0.0061 977  ARG A O   
7220  C CB  . ARG A 979  ? 0.2674 0.2303 0.2455 0.0056  0.0093  -0.0037 977  ARG A CB  
7221  C CG  . ARG A 979  ? 0.3212 0.2812 0.2989 0.0057  0.0093  -0.0022 977  ARG A CG  
7222  C CD  . ARG A 979  ? 0.4605 0.4220 0.4392 0.0049  0.0093  -0.0028 977  ARG A CD  
7223  N NE  . ARG A 979  ? 0.5036 0.4623 0.4823 0.0051  0.0094  -0.0014 977  ARG A NE  
7224  C CZ  . ARG A 979  ? 0.6220 0.5814 0.6016 0.0045  0.0094  -0.0016 977  ARG A CZ  
7225  N NH1 . ARG A 979  ? 0.4326 0.3956 0.4129 0.0038  0.0092  -0.0033 977  ARG A NH1 
7226  N NH2 . ARG A 979  ? 0.5634 0.5202 0.5432 0.0048  0.0095  -0.0003 977  ARG A NH2 
7227  N N   . LEU A 980  ? 0.2204 0.1871 0.1973 0.0057  0.0088  -0.0047 978  LEU A N   
7228  C CA  . LEU A 980  ? 0.2257 0.1962 0.2035 0.0056  0.0088  -0.0065 978  LEU A CA  
7229  C C   . LEU A 980  ? 0.2431 0.2126 0.2211 0.0068  0.0086  -0.0065 978  LEU A C   
7230  O O   . LEU A 980  ? 0.2378 0.2064 0.2143 0.0064  0.0082  -0.0053 978  LEU A O   
7231  C CB  . LEU A 980  ? 0.2270 0.2017 0.2038 0.0036  0.0085  -0.0061 978  LEU A CB  
7232  C CG  . LEU A 980  ? 0.2367 0.2129 0.2130 0.0023  0.0085  -0.0055 978  LEU A CG  
7233  C CD1 . LEU A 980  ? 0.2625 0.2431 0.2379 0.0002  0.0081  -0.0043 978  LEU A CD1 
7234  C CD2 . LEU A 980  ? 0.2719 0.2505 0.2499 0.0029  0.0089  -0.0080 978  LEU A CD2 
7235  N N   . ASP A 981  ? 0.2296 0.1996 0.2098 0.0081  0.0087  -0.0081 979  ASP A N   
7236  C CA  . ASP A 981  ? 0.2329 0.2022 0.2136 0.0093  0.0085  -0.0080 979  ASP A CA  
7237  C C   . ASP A 981  ? 0.2370 0.2091 0.2165 0.0085  0.0082  -0.0083 979  ASP A C   
7238  O O   . ASP A 981  ? 0.2386 0.2095 0.2173 0.0090  0.0078  -0.0075 979  ASP A O   
7239  C CB  . ASP A 981  ? 0.2396 0.2093 0.2236 0.0108  0.0084  -0.0097 979  ASP A CB  
7240  C CG  . ASP A 981  ? 0.2695 0.2359 0.2554 0.0119  0.0085  -0.0088 979  ASP A CG  
7241  O OD1 . ASP A 981  ? 0.3092 0.2729 0.2933 0.0118  0.0087  -0.0067 979  ASP A OD1 
7242  O OD2 . ASP A 981  ? 0.3224 0.2890 0.3119 0.0129  0.0082  -0.0102 979  ASP A OD2 
7243  N N   . GLU A 982  ? 0.2182 0.1946 0.1979 0.0071  0.0083  -0.0094 980  GLU A N   
7244  C CA  . GLU A 982  ? 0.2245 0.2040 0.2035 0.0061  0.0080  -0.0093 980  GLU A CA  
7245  C C   . GLU A 982  ? 0.2243 0.2015 0.2013 0.0050  0.0074  -0.0070 980  GLU A C   
7246  O O   . GLU A 982  ? 0.2358 0.2129 0.2125 0.0050  0.0069  -0.0066 980  GLU A O   
7247  C CB  . GLU A 982  ? 0.2491 0.2345 0.2286 0.0047  0.0082  -0.0105 980  GLU A CB  
7248  C CG  . GLU A 982  ? 0.2545 0.2437 0.2335 0.0034  0.0079  -0.0099 980  GLU A CG  
7249  C CD  . GLU A 982  ? 0.3501 0.3456 0.3290 0.0015  0.0082  -0.0100 980  GLU A CD  
7250  O OE1 . GLU A 982  ? 0.3790 0.3747 0.3570 0.0003  0.0082  -0.0087 980  GLU A OE1 
7251  O OE2 . GLU A 982  ? 0.3151 0.3160 0.2950 0.0011  0.0083  -0.0112 980  GLU A OE2 
7252  N N   . THR A 983  ? 0.2144 0.1896 0.1905 0.0043  0.0074  -0.0057 981  THR A N   
7253  C CA  . THR A 983  ? 0.2213 0.1942 0.1962 0.0033  0.0067  -0.0039 981  THR A CA  
7254  C C   . THR A 983  ? 0.2247 0.1937 0.1990 0.0050  0.0064  -0.0037 981  THR A C   
7255  O O   . THR A 983  ? 0.2368 0.2049 0.2107 0.0048  0.0056  -0.0033 981  THR A O   
7256  C CB  . THR A 983  ? 0.2313 0.2033 0.2058 0.0022  0.0066  -0.0026 981  THR A CB  
7257  O OG1 . THR A 983  ? 0.2598 0.2366 0.2347 0.0005  0.0067  -0.0025 981  THR A OG1 
7258  C CG2 . THR A 983  ? 0.2482 0.2173 0.2223 0.0015  0.0056  -0.0010 981  THR A CG2 
7259  N N   . ILE A 984  ? 0.2172 0.1842 0.1917 0.0067  0.0070  -0.0041 982  ILE A N   
7260  C CA  . ILE A 984  ? 0.2361 0.2005 0.2099 0.0083  0.0069  -0.0037 982  ILE A CA  
7261  C C   . ILE A 984  ? 0.2439 0.2098 0.2179 0.0089  0.0065  -0.0043 982  ILE A C   
7262  O O   . ILE A 984  ? 0.2417 0.2067 0.2147 0.0093  0.0058  -0.0041 982  ILE A O   
7263  C CB  . ILE A 984  ? 0.2355 0.1983 0.2101 0.0098  0.0076  -0.0035 982  ILE A CB  
7264  C CG1 . ILE A 984  ? 0.2439 0.2049 0.2182 0.0093  0.0079  -0.0027 982  ILE A CG1 
7265  C CG2 . ILE A 984  ? 0.2537 0.2151 0.2276 0.0114  0.0075  -0.0027 982  ILE A CG2 
7266  C CD1 . ILE A 984  ? 0.2744 0.2341 0.2500 0.0104  0.0086  -0.0024 982  ILE A CD1 
7267  N N   . ALA A 985  ? 0.2151 0.1836 0.1906 0.0090  0.0067  -0.0054 983  ALA A N   
7268  C CA  . ALA A 985  ? 0.2433 0.2133 0.2193 0.0097  0.0063  -0.0061 983  ALA A CA  
7269  C C   . ALA A 985  ? 0.2382 0.2096 0.2135 0.0083  0.0055  -0.0059 983  ALA A C   
7270  O O   . ALA A 985  ? 0.2456 0.2167 0.2204 0.0088  0.0048  -0.0059 983  ALA A O   
7271  C CB  . ALA A 985  ? 0.2562 0.2290 0.2345 0.0101  0.0066  -0.0076 983  ALA A CB  
7272  N N   . HIS A 986  ? 0.2317 0.2050 0.2072 0.0064  0.0055  -0.0057 984  HIS A N   
7273  C CA  . HIS A 986  ? 0.2527 0.2274 0.2282 0.0047  0.0046  -0.0051 984  HIS A CA  
7274  C C   . HIS A 986  ? 0.2429 0.2142 0.2177 0.0048  0.0036  -0.0044 984  HIS A C   
7275  O O   . HIS A 986  ? 0.2434 0.2146 0.2183 0.0051  0.0027  -0.0048 984  HIS A O   
7276  C CB  . HIS A 986  ? 0.2485 0.2260 0.2246 0.0025  0.0048  -0.0044 984  HIS A CB  
7277  C CG  . HIS A 986  ? 0.2818 0.2607 0.2586 0.0004  0.0037  -0.0030 984  HIS A CG  
7278  N ND1 . HIS A 986  ? 0.3538 0.3352 0.3311 -0.0018 0.0035  -0.0014 984  HIS A ND1 
7279  C CD2 . HIS A 986  ? 0.2647 0.2428 0.2421 0.0001  0.0025  -0.0027 984  HIS A CD2 
7280  C CE1 . HIS A 986  ? 0.3745 0.3565 0.3531 -0.0034 0.0023  0.0000  984  HIS A CE1 
7281  N NE2 . HIS A 986  ? 0.2815 0.2613 0.2603 -0.0023 0.0016  -0.0009 984  HIS A NE2 
7282  N N   . VAL A 987  ? 0.2352 0.2038 0.2093 0.0048  0.0038  -0.0037 985  VAL A N   
7283  C CA  . VAL A 987  ? 0.2551 0.2209 0.2289 0.0049  0.0027  -0.0034 985  VAL A CA  
7284  C C   . VAL A 987  ? 0.2516 0.2162 0.2244 0.0070  0.0025  -0.0044 985  VAL A C   
7285  O O   . VAL A 987  ? 0.2523 0.2164 0.2253 0.0071  0.0013  -0.0050 985  VAL A O   
7286  C CB  . VAL A 987  ? 0.2100 0.1735 0.1835 0.0046  0.0030  -0.0025 985  VAL A CB  
7287  C CG1 . VAL A 987  ? 0.2503 0.2110 0.2239 0.0051  0.0019  -0.0028 985  VAL A CG1 
7288  C CG2 . VAL A 987  ? 0.2798 0.2452 0.2545 0.0022  0.0028  -0.0012 985  VAL A CG2 
7289  N N   . THR A 988  ? 0.2300 0.1944 0.2019 0.0087  0.0036  -0.0045 986  THR A N   
7290  C CA  . THR A 988  ? 0.2497 0.2136 0.2206 0.0106  0.0034  -0.0049 986  THR A CA  
7291  C C   . THR A 988  ? 0.3243 0.2903 0.2955 0.0109  0.0027  -0.0057 986  THR A C   
7292  O O   . THR A 988  ? 0.2983 0.2645 0.2687 0.0121  0.0021  -0.0063 986  THR A O   
7293  C CB  . THR A 988  ? 0.2793 0.2426 0.2496 0.0122  0.0045  -0.0041 986  THR A CB  
7294  O OG1 . THR A 988  ? 0.2913 0.2560 0.2630 0.0122  0.0051  -0.0041 986  THR A OG1 
7295  C CG2 . THR A 988  ? 0.3011 0.2625 0.2712 0.0119  0.0051  -0.0034 986  THR A CG2 
7296  N N   . SER A 989  ? 0.2716 0.2397 0.2441 0.0099  0.0029  -0.0058 987  SER A N   
7297  C CA  . SER A 989  ? 0.3133 0.2835 0.2863 0.0101  0.0022  -0.0065 987  SER A CA  
7298  C C   . SER A 989  ? 0.3147 0.2851 0.2883 0.0088  0.0008  -0.0070 987  SER A C   
7299  O O   . SER A 989  ? 0.3924 0.3639 0.3661 0.0094  -0.0001 -0.0078 987  SER A O   
7300  C CB  . SER A 989  ? 0.2965 0.2693 0.2710 0.0097  0.0028  -0.0068 987  SER A CB  
7301  O OG  . SER A 989  ? 0.3864 0.3608 0.3618 0.0076  0.0028  -0.0066 987  SER A OG  
7302  N N   . ARG A 990  ? 0.2436 0.2128 0.2178 0.0072  0.0004  -0.0064 988  ARG A N   
7303  C CA  . ARG A 990  ? 0.2717 0.2410 0.2476 0.0056  -0.0012 -0.0065 988  ARG A CA  
7304  C C   . ARG A 990  ? 0.2666 0.2332 0.2426 0.0062  -0.0024 -0.0072 988  ARG A C   
7305  O O   . ARG A 990  ? 0.2764 0.2430 0.2539 0.0057  -0.0041 -0.0081 988  ARG A O   
7306  C CB  . ARG A 990  ? 0.2984 0.2691 0.2759 0.0031  -0.0012 -0.0050 988  ARG A CB  
7307  C CG  . ARG A 990  ? 0.4076 0.3820 0.3853 0.0026  0.0000  -0.0048 988  ARG A CG  
7308  C CD  . ARG A 990  ? 0.4249 0.4023 0.4039 0.0020  -0.0007 -0.0053 988  ARG A CD  
7309  N NE  . ARG A 990  ? 0.3850 0.3647 0.3662 -0.0007 -0.0015 -0.0038 988  ARG A NE  
7310  C CZ  . ARG A 990  ? 0.3586 0.3413 0.3416 -0.0018 -0.0023 -0.0036 988  ARG A CZ  
7311  N NH1 . ARG A 990  ? 0.3898 0.3734 0.3727 -0.0005 -0.0025 -0.0051 988  ARG A NH1 
7312  N NH2 . ARG A 990  ? 0.3770 0.3623 0.3622 -0.0045 -0.0029 -0.0017 988  ARG A NH2 
7313  N N   . ILE A 991  ? 0.2560 0.2205 0.2306 0.0072  -0.0017 -0.0071 989  ILE A N   
7314  C CA  . ILE A 991  ? 0.2376 0.2000 0.2124 0.0080  -0.0028 -0.0083 989  ILE A CA  
7315  C C   . ILE A 991  ? 0.2524 0.2159 0.2259 0.0100  -0.0034 -0.0101 989  ILE A C   
7316  O O   . ILE A 991  ? 0.2831 0.2484 0.2550 0.0113  -0.0024 -0.0099 989  ILE A O   
7317  C CB  . ILE A 991  ? 0.2434 0.2039 0.2169 0.0087  -0.0017 -0.0076 989  ILE A CB  
7318  C CG1 . ILE A 991  ? 0.2704 0.2289 0.2449 0.0093  -0.0030 -0.0089 989  ILE A CG1 
7319  C CG2 . ILE A 991  ? 0.2626 0.2239 0.2336 0.0107  -0.0002 -0.0075 989  ILE A CG2 
7320  C CD1 . ILE A 991  ? 0.3191 0.2760 0.2968 0.0071  -0.0047 -0.0083 989  ILE A CD1 
7321  N N   . LYS A 992  ? 0.2504 0.2131 0.2251 0.0104  -0.0051 -0.0119 990  LYS A N   
7322  C CA  . LYS A 992  ? 0.2590 0.2233 0.2326 0.0124  -0.0059 -0.0141 990  LYS A CA  
7323  C C   . LYS A 992  ? 0.2503 0.2137 0.2234 0.0139  -0.0062 -0.0157 990  LYS A C   
7324  O O   . LYS A 992  ? 0.2757 0.2380 0.2511 0.0138  -0.0081 -0.0177 990  LYS A O   
7325  C CB  . LYS A 992  ? 0.2685 0.2335 0.2446 0.0115  -0.0079 -0.0156 990  LYS A CB  
7326  C CG  . LYS A 992  ? 0.2958 0.2625 0.2728 0.0100  -0.0076 -0.0141 990  LYS A CG  
7327  C CD  . LYS A 992  ? 0.4358 0.4029 0.4160 0.0087  -0.0099 -0.0153 990  LYS A CD  
7328  C CE  . LYS A 992  ? 0.6236 0.5931 0.6046 0.0074  -0.0096 -0.0141 990  LYS A CE  
7329  N NZ  . LYS A 992  ? 0.7477 0.7176 0.7324 0.0058  -0.0119 -0.0149 990  LYS A NZ  
7330  N N   . ALA A 993  ? 0.2566 0.2206 0.2270 0.0154  -0.0045 -0.0149 991  ALA A N   
7331  C CA  . ALA A 993  ? 0.2370 0.2012 0.2066 0.0171  -0.0045 -0.0163 991  ALA A CA  
7332  C C   . ALA A 993  ? 0.2421 0.2093 0.2084 0.0191  -0.0029 -0.0155 991  ALA A C   
7333  O O   . ALA A 993  ? 0.2661 0.2340 0.2313 0.0189  -0.0016 -0.0133 991  ALA A O   
7334  C CB  . ALA A 993  ? 0.2553 0.2166 0.2259 0.0162  -0.0040 -0.0152 991  ALA A CB  
7335  N N   . GLY A 994  ? 0.2235 0.1928 0.1886 0.0210  -0.0032 -0.0174 992  GLY A N   
7336  C CA  . GLY A 994  ? 0.2287 0.2020 0.1909 0.0229  -0.0019 -0.0164 992  GLY A CA  
7337  C C   . GLY A 994  ? 0.2077 0.1805 0.1688 0.0231  0.0001  -0.0137 992  GLY A C   
7338  O O   . GLY A 994  ? 0.2214 0.1968 0.1809 0.0240  0.0012  -0.0115 992  GLY A O   
7339  N N   . ASN A 995  ? 0.2119 0.1817 0.1743 0.0223  0.0003  -0.0136 993  ASN A N   
7340  C CA  . ASN A 995  ? 0.2305 0.1998 0.1922 0.0224  0.0020  -0.0113 993  ASN A CA  
7341  C C   . ASN A 995  ? 0.2186 0.1837 0.1821 0.0203  0.0023  -0.0099 993  ASN A C   
7342  O O   . ASN A 995  ? 0.2274 0.1900 0.1927 0.0194  0.0013  -0.0112 993  ASN A O   
7343  C CB  . ASN A 995  ? 0.2245 0.1957 0.1855 0.0240  0.0022  -0.0127 993  ASN A CB  
7344  C CG  . ASN A 995  ? 0.2287 0.2055 0.1873 0.0261  0.0026  -0.0129 993  ASN A CG  
7345  O OD1 . ASN A 995  ? 0.2397 0.2192 0.1978 0.0271  0.0013  -0.0157 993  ASN A OD1 
7346  N ND2 . ASN A 995  ? 0.2380 0.2170 0.1953 0.0267  0.0043  -0.0100 993  ASN A ND2 
7347  N N   . LEU A 996  ? 0.2166 0.1811 0.1800 0.0196  0.0035  -0.0074 994  LEU A N   
7348  C CA  . LEU A 996  ? 0.2127 0.1741 0.1776 0.0178  0.0039  -0.0062 994  LEU A CA  
7349  C C   . LEU A 996  ? 0.2083 0.1691 0.1731 0.0180  0.0053  -0.0043 994  LEU A C   
7350  O O   . LEU A 996  ? 0.2130 0.1758 0.1768 0.0193  0.0062  -0.0030 994  LEU A O   
7351  C CB  . LEU A 996  ? 0.2352 0.1967 0.2006 0.0169  0.0040  -0.0052 994  LEU A CB  
7352  C CG  . LEU A 996  ? 0.2355 0.1985 0.2009 0.0169  0.0028  -0.0066 994  LEU A CG  
7353  C CD1 . LEU A 996  ? 0.2678 0.2312 0.2341 0.0160  0.0032  -0.0056 994  LEU A CD1 
7354  C CD2 . LEU A 996  ? 0.2579 0.2196 0.2246 0.0159  0.0013  -0.0084 994  LEU A CD2 
7355  N N   . TYR A 997  ? 0.2121 0.1704 0.1781 0.0167  0.0054  -0.0040 995  TYR A N   
7356  C CA  . TYR A 997  ? 0.2011 0.1586 0.1673 0.0167  0.0065  -0.0025 995  TYR A CA  
7357  C C   . TYR A 997  ? 0.2229 0.1784 0.1904 0.0149  0.0067  -0.0017 995  TYR A C   
7358  O O   . TYR A 997  ? 0.2443 0.1985 0.2127 0.0135  0.0058  -0.0023 995  TYR A O   
7359  C CB  . TYR A 997  ? 0.2157 0.1728 0.1819 0.0174  0.0063  -0.0035 995  TYR A CB  
7360  C CG  . TYR A 997  ? 0.2225 0.1824 0.1874 0.0193  0.0060  -0.0050 995  TYR A CG  
7361  C CD1 . TYR A 997  ? 0.2270 0.1872 0.1923 0.0195  0.0044  -0.0075 995  TYR A CD1 
7362  C CD2 . TYR A 997  ? 0.2449 0.2077 0.2085 0.0208  0.0071  -0.0039 995  TYR A CD2 
7363  C CE1 . TYR A 997  ? 0.2577 0.2210 0.2219 0.0214  0.0040  -0.0095 995  TYR A CE1 
7364  C CE2 . TYR A 997  ? 0.2432 0.2097 0.2054 0.0227  0.0068  -0.0055 995  TYR A CE2 
7365  C CZ  . TYR A 997  ? 0.2602 0.2270 0.2226 0.0230  0.0053  -0.0085 995  TYR A CZ  
7366  O OH  . TYR A 997  ? 0.3004 0.2713 0.2614 0.0249  0.0049  -0.0105 995  TYR A OH  
7367  N N   . ILE A 998  ? 0.2122 0.1677 0.1803 0.0149  0.0078  -0.0002 996  ILE A N   
7368  C CA  A ILE A 998  ? 0.2113 0.1658 0.1807 0.0134  0.0080  0.0002  996  ILE A CA  
7369  C CA  B ILE A 998  ? 0.2114 0.1659 0.1807 0.0134  0.0080  0.0002  996  ILE A CA  
7370  C C   . ILE A 998  ? 0.2157 0.1691 0.1858 0.0133  0.0088  0.0012  996  ILE A C   
7371  O O   . ILE A 998  ? 0.2238 0.1776 0.1942 0.0143  0.0096  0.0024  996  ILE A O   
7372  C CB  A ILE A 998  ? 0.2257 0.1812 0.1959 0.0135  0.0084  0.0005  996  ILE A CB  
7373  C CB  B ILE A 998  ? 0.2259 0.1815 0.1961 0.0135  0.0083  0.0005  996  ILE A CB  
7374  C CG1 A ILE A 998  ? 0.2540 0.2110 0.2235 0.0138  0.0076  -0.0003 996  ILE A CG1 
7375  C CG1 B ILE A 998  ? 0.2481 0.2049 0.2176 0.0135  0.0075  -0.0005 996  ILE A CG1 
7376  C CG2 A ILE A 998  ? 0.2372 0.1925 0.2087 0.0121  0.0085  0.0003  996  ILE A CG2 
7377  C CG2 B ILE A 998  ? 0.2366 0.1918 0.2082 0.0122  0.0086  0.0004  996  ILE A CG2 
7378  C CD1 A ILE A 998  ? 0.2487 0.2055 0.2181 0.0124  0.0067  -0.0015 996  ILE A CD1 
7379  C CD1 B ILE A 998  ? 0.2708 0.2289 0.2413 0.0138  0.0077  -0.0004 996  ILE A CD1 
7380  N N   . ASN A 999  ? 0.2267 0.1789 0.1972 0.0120  0.0084  0.0010  997  ASN A N   
7381  C CA  . ASN A 999  ? 0.2265 0.1777 0.1979 0.0116  0.0090  0.0018  997  ASN A CA  
7382  C C   . ASN A 999  ? 0.2126 0.1636 0.1836 0.0129  0.0094  0.0023  997  ASN A C   
7383  O O   . ASN A 999  ? 0.2255 0.1763 0.1973 0.0132  0.0102  0.0034  997  ASN A O   
7384  C CB  . ASN A 999  ? 0.2235 0.1751 0.1962 0.0113  0.0096  0.0023  997  ASN A CB  
7385  C CG  . ASN A 999  ? 0.2246 0.1772 0.1978 0.0100  0.0092  0.0014  997  ASN A CG  
7386  O OD1 . ASN A 999  ? 0.2383 0.1910 0.2111 0.0088  0.0085  0.0011  997  ASN A OD1 
7387  N ND2 . ASN A 999  ? 0.2402 0.1937 0.2145 0.0102  0.0095  0.0010  997  ASN A ND2 
7388  N N   . ARG A 1000 ? 0.2308 0.1821 0.2009 0.0137  0.0088  0.0014  998  ARG A N   
7389  C CA  . ARG A 1000 ? 0.2334 0.1855 0.2031 0.0151  0.0092  0.0013  998  ARG A CA  
7390  C C   . ARG A 1000 ? 0.2206 0.1725 0.1901 0.0155  0.0079  -0.0006 998  ARG A C   
7391  O O   . ARG A 1000 ? 0.2499 0.2009 0.2197 0.0146  0.0068  -0.0015 998  ARG A O   
7392  C CB  . ARG A 1000 ? 0.2200 0.1745 0.1889 0.0166  0.0101  0.0023  998  ARG A CB  
7393  C CG  . ARG A 1000 ? 0.2286 0.1844 0.1964 0.0171  0.0096  0.0017  998  ARG A CG  
7394  C CD  . ARG A 1000 ? 0.2376 0.1967 0.2041 0.0189  0.0102  0.0023  998  ARG A CD  
7395  N NE  . ARG A 1000 ? 0.2151 0.1757 0.1808 0.0200  0.0099  0.0007  998  ARG A NE  
7396  C CZ  . ARG A 1000 ? 0.2556 0.2200 0.2200 0.0217  0.0104  0.0008  998  ARG A CZ  
7397  N NH1 . ARG A 1000 ? 0.2511 0.2181 0.2149 0.0223  0.0111  0.0030  998  ARG A NH1 
7398  N NH2 . ARG A 1000 ? 0.2540 0.2199 0.2178 0.0228  0.0100  -0.0013 998  ARG A NH2 
7399  N N   . ASN A 1001 ? 0.2189 0.1719 0.1883 0.0169  0.0081  -0.0014 999  ASN A N   
7400  C CA  . ASN A 1001 ? 0.2253 0.1783 0.1951 0.0176  0.0067  -0.0038 999  ASN A CA  
7401  C C   . ASN A 1001 ? 0.2412 0.1962 0.2097 0.0185  0.0062  -0.0051 999  ASN A C   
7402  O O   . ASN A 1001 ? 0.2317 0.1884 0.1987 0.0188  0.0071  -0.0039 999  ASN A O   
7403  C CB  . ASN A 1001 ? 0.2620 0.2161 0.2323 0.0190  0.0069  -0.0048 999  ASN A CB  
7404  C CG  . ASN A 1001 ? 0.2793 0.2375 0.2477 0.0210  0.0082  -0.0045 999  ASN A CG  
7405  O OD1 . ASN A 1001 ? 0.2792 0.2399 0.2462 0.0218  0.0082  -0.0050 999  ASN A OD1 
7406  N ND2 . ASN A 1001 ? 0.3683 0.3277 0.3370 0.0216  0.0093  -0.0035 999  ASN A ND2 
7407  N N   A ILE A 1002 ? 0.2200 0.1747 0.1894 0.0189  0.0046  -0.0075 1000 ILE A N   
7408  N N   B ILE A 1002 ? 0.2199 0.1747 0.1892 0.0189  0.0046  -0.0076 1000 ILE A N   
7409  C CA  A ILE A 1002 ? 0.2398 0.1962 0.2084 0.0195  0.0038  -0.0091 1000 ILE A CA  
7410  C CA  B ILE A 1002 ? 0.2415 0.1982 0.2099 0.0197  0.0039  -0.0092 1000 ILE A CA  
7411  C C   A ILE A 1002 ? 0.2380 0.1978 0.2058 0.0218  0.0035  -0.0117 1000 ILE A C   
7412  C C   B ILE A 1002 ? 0.2377 0.1980 0.2053 0.0221  0.0037  -0.0116 1000 ILE A C   
7413  O O   A ILE A 1002 ? 0.2514 0.2124 0.2192 0.0224  0.0022  -0.0140 1000 ILE A O   
7414  O O   B ILE A 1002 ? 0.2642 0.2261 0.2315 0.0229  0.0026  -0.0139 1000 ILE A O   
7415  C CB  A ILE A 1002 ? 0.2118 0.1657 0.1823 0.0179  0.0020  -0.0099 1000 ILE A CB  
7416  C CB  B ILE A 1002 ? 0.2046 0.1590 0.1749 0.0183  0.0020  -0.0102 1000 ILE A CB  
7417  C CG1 A ILE A 1002 ? 0.2511 0.2033 0.2245 0.0180  0.0001  -0.0121 1000 ILE A CG1 
7418  C CG1 B ILE A 1002 ? 0.2503 0.2028 0.2235 0.0183  0.0002  -0.0123 1000 ILE A CG1 
7419  C CG2 A ILE A 1002 ? 0.2222 0.1740 0.1932 0.0157  0.0024  -0.0074 1000 ILE A CG2 
7420  C CG2 B ILE A 1002 ? 0.2228 0.1751 0.1937 0.0160  0.0024  -0.0078 1000 ILE A CG2 
7421  C CD1 A ILE A 1002 ? 0.2470 0.1974 0.2229 0.0166  -0.0020 -0.0130 1000 ILE A CD1 
7422  C CD1 B ILE A 1002 ? 0.2466 0.1972 0.2224 0.0169  -0.0019 -0.0132 1000 ILE A CD1 
7423  N N   A ILE A 1003 ? 0.2453 0.2072 0.2125 0.0231  0.0046  -0.0115 1001 ILE A N   
7424  N N   B ILE A 1003 ? 0.2377 0.1997 0.2049 0.0232  0.0048  -0.0113 1001 ILE A N   
7425  C CA  A ILE A 1003 ? 0.2543 0.2203 0.2208 0.0255  0.0043  -0.0143 1001 ILE A CA  
7426  C CA  B ILE A 1003 ? 0.2528 0.2189 0.2194 0.0256  0.0046  -0.0140 1001 ILE A CA  
7427  C C   A ILE A 1003 ? 0.2907 0.2619 0.2542 0.0268  0.0060  -0.0127 1001 ILE A C   
7428  C C   B ILE A 1003 ? 0.2579 0.2287 0.2221 0.0268  0.0067  -0.0119 1001 ILE A C   
7429  O O   A ILE A 1003 ? 0.3032 0.2793 0.2658 0.0289  0.0062  -0.0145 1001 ILE A O   
7430  O O   B ILE A 1003 ? 0.2731 0.2431 0.2367 0.0258  0.0080  -0.0084 1001 ILE A O   
7431  C CB  A ILE A 1003 ? 0.2579 0.2236 0.2264 0.0263  0.0040  -0.0160 1001 ILE A CB  
7432  C CB  B ILE A 1003 ? 0.2644 0.2292 0.2336 0.0261  0.0036  -0.0164 1001 ILE A CB  
7433  C CG1 A ILE A 1003 ? 0.2564 0.2216 0.2246 0.0257  0.0058  -0.0129 1001 ILE A CG1 
7434  C CG1 B ILE A 1003 ? 0.2525 0.2158 0.2222 0.0254  0.0049  -0.0139 1001 ILE A CG1 
7435  C CG2 A ILE A 1003 ? 0.2699 0.2311 0.2419 0.0251  0.0018  -0.0178 1001 ILE A CG2 
7436  C CG2 B ILE A 1003 ? 0.2545 0.2150 0.2269 0.0248  0.0012  -0.0181 1001 ILE A CG2 
7437  C CD1 A ILE A 1003 ? 0.3212 0.2868 0.2912 0.0267  0.0056  -0.0145 1001 ILE A CD1 
7438  C CD1 B ILE A 1003 ? 0.2949 0.2587 0.2669 0.0267  0.0043  -0.0163 1001 ILE A CD1 
7439  N N   A GLY A 1004 ? 0.2736 0.2443 0.2361 0.0258  0.0070  -0.0094 1002 GLY A N   
7440  N N   B GLY A 1004 ? 0.2821 0.2581 0.2451 0.0290  0.0067  -0.0141 1002 GLY A N   
7441  C CA  A GLY A 1004 ? 0.2415 0.2168 0.2020 0.0268  0.0085  -0.0070 1002 GLY A CA  
7442  C CA  B GLY A 1004 ? 0.3097 0.2914 0.2706 0.0302  0.0086  -0.0120 1002 GLY A CA  
7443  C C   A GLY A 1004 ? 0.2626 0.2424 0.2212 0.0283  0.0079  -0.0086 1002 GLY A C   
7444  C C   B GLY A 1004 ? 0.2938 0.2777 0.2527 0.0300  0.0093  -0.0090 1002 GLY A C   
7445  O O   A GLY A 1004 ? 0.2664 0.2446 0.2251 0.0277  0.0067  -0.0096 1002 GLY A O   
7446  O O   B GLY A 1004 ? 0.2822 0.2677 0.2406 0.0297  0.0109  -0.0052 1002 GLY A O   
7447  N N   A ALA A 1005 ? 0.2467 0.2326 0.2036 0.0301  0.0086  -0.0088 1003 ALA A N   
7448  N N   B ALA A 1005 ? 0.2772 0.2612 0.2354 0.0301  0.0081  -0.0106 1003 ALA A N   
7449  C CA  A ALA A 1005 ? 0.2659 0.2573 0.2208 0.0316  0.0081  -0.0101 1003 ALA A CA  
7450  C CA  B ALA A 1005 ? 0.2710 0.2574 0.2274 0.0300  0.0087  -0.0080 1003 ALA A CA  
7451  C C   A ALA A 1005 ? 0.2652 0.2631 0.2181 0.0327  0.0097  -0.0068 1003 ALA A C   
7452  C C   B ALA A 1005 ? 0.2843 0.2781 0.2387 0.0317  0.0100  -0.0061 1003 ALA A C   
7453  O O   A ALA A 1005 ? 0.2522 0.2571 0.2032 0.0346  0.0097  -0.0083 1003 ALA A O   
7454  O O   B ALA A 1005 ? 0.2979 0.2967 0.2514 0.0335  0.0099  -0.0088 1003 ALA A O   
7455  C CB  A ALA A 1005 ? 0.2677 0.2611 0.2228 0.0331  0.0066  -0.0154 1003 ALA A CB  
7456  C CB  B ALA A 1005 ? 0.2970 0.2837 0.2530 0.0303  0.0070  -0.0106 1003 ALA A CB  
7457  N N   A VAL A 1006 ? 0.2689 0.2652 0.2227 0.0316  0.0110  -0.0023 1004 VAL A N   
7458  N N   B VAL A 1006 ? 0.2623 0.2571 0.2164 0.0311  0.0111  -0.0016 1004 VAL A N   
7459  C CA  A VAL A 1006 ? 0.2544 0.2565 0.2073 0.0322  0.0125  0.0018  1004 VAL A CA  
7460  C CA  B VAL A 1006 ? 0.2550 0.2568 0.2078 0.0322  0.0124  0.0015  1004 VAL A CA  
7461  C C   A VAL A 1006 ? 0.2419 0.2490 0.1928 0.0331  0.0121  0.0028  1004 VAL A C   
7462  C C   B VAL A 1006 ? 0.2439 0.2508 0.1948 0.0332  0.0119  0.0021  1004 VAL A C   
7463  O O   A VAL A 1006 ? 0.2410 0.2451 0.1926 0.0321  0.0116  0.0043  1004 VAL A O   
7464  O O   B VAL A 1006 ? 0.2444 0.2481 0.1956 0.0323  0.0111  0.0026  1004 VAL A O   
7465  C CB  A VAL A 1006 ? 0.2613 0.2596 0.2164 0.0306  0.0135  0.0063  1004 VAL A CB  
7466  C CB  B VAL A 1006 ? 0.2560 0.2556 0.2107 0.0309  0.0137  0.0065  1004 VAL A CB  
7467  C CG1 A VAL A 1006 ? 0.2671 0.2716 0.2219 0.0311  0.0148  0.0110  1004 VAL A CG1 
7468  C CG1 B VAL A 1006 ? 0.2818 0.2888 0.2358 0.0317  0.0149  0.0106  1004 VAL A CG1 
7469  C CG2 A VAL A 1006 ? 0.2818 0.2756 0.2385 0.0298  0.0139  0.0052  1004 VAL A CG2 
7470  C CG2 B VAL A 1006 ? 0.2801 0.2754 0.2366 0.0301  0.0141  0.0057  1004 VAL A CG2 
7471  N N   . VAL A 1007 ? 0.2503 0.2656 0.1990 0.0350  0.0124  0.0019  1005 VAL A N   
7472  C CA  . VAL A 1007 ? 0.2465 0.2677 0.1930 0.0360  0.0119  0.0025  1005 VAL A CA  
7473  C C   . VAL A 1007 ? 0.2276 0.2483 0.1752 0.0349  0.0124  0.0083  1005 VAL A C   
7474  O O   . VAL A 1007 ? 0.2452 0.2662 0.1942 0.0342  0.0136  0.0128  1005 VAL A O   
7475  C CB  . VAL A 1007 ? 0.2370 0.2684 0.1811 0.0381  0.0125  0.0015  1005 VAL A CB  
7476  C CG1 . VAL A 1007 ? 0.2615 0.3003 0.2033 0.0392  0.0121  0.0029  1005 VAL A CG1 
7477  C CG2 . VAL A 1007 ? 0.2640 0.2958 0.2078 0.0395  0.0116  -0.0050 1005 VAL A CG2 
7478  N N   . GLY A 1008 ? 0.2318 0.2516 0.1790 0.0347  0.0112  0.0082  1006 GLY A N   
7479  C CA  . GLY A 1008 ? 0.2480 0.2673 0.1966 0.0338  0.0114  0.0134  1006 GLY A CA  
7480  C C   . GLY A 1008 ? 0.2426 0.2535 0.1947 0.0319  0.0116  0.0153  1006 GLY A C   
7481  O O   . GLY A 1008 ? 0.2638 0.2738 0.2180 0.0312  0.0115  0.0195  1006 GLY A O   
7482  N N   . VAL A 1009 ? 0.2333 0.2386 0.1864 0.0311  0.0116  0.0124  1007 VAL A N   
7483  C CA  . VAL A 1009 ? 0.2497 0.2476 0.2058 0.0294  0.0118  0.0136  1007 VAL A CA  
7484  C C   . VAL A 1009 ? 0.2579 0.2500 0.2142 0.0285  0.0107  0.0095  1007 VAL A C   
7485  O O   . VAL A 1009 ? 0.2690 0.2570 0.2270 0.0275  0.0102  0.0100  1007 VAL A O   
7486  C CB  . VAL A 1009 ? 0.2442 0.2411 0.2017 0.0289  0.0130  0.0151  1007 VAL A CB  
7487  C CG1 . VAL A 1009 ? 0.2528 0.2425 0.2134 0.0272  0.0130  0.0160  1007 VAL A CG1 
7488  C CG2 . VAL A 1009 ? 0.2507 0.2536 0.2084 0.0295  0.0140  0.0198  1007 VAL A CG2 
7489  N N   . GLN A 1010 ? 0.2375 0.2296 0.1924 0.0291  0.0103  0.0054  1008 GLN A N   
7490  C CA  . GLN A 1010 ? 0.2233 0.2117 0.1782 0.0285  0.0089  0.0015  1008 GLN A CA  
7491  C C   . GLN A 1010 ? 0.2344 0.2280 0.1872 0.0302  0.0080  -0.0017 1008 GLN A C   
7492  O O   . GLN A 1010 ? 0.2764 0.2706 0.2289 0.0309  0.0076  -0.0051 1008 GLN A O   
7493  C CB  . GLN A 1010 ? 0.2641 0.2476 0.2204 0.0275  0.0088  -0.0007 1008 GLN A CB  
7494  C CG  . GLN A 1010 ? 0.2749 0.2540 0.2333 0.0260  0.0097  0.0019  1008 GLN A CG  
7495  C CD  . GLN A 1010 ? 0.2740 0.2543 0.2328 0.0263  0.0109  0.0035  1008 GLN A CD  
7496  O OE1 . GLN A 1010 ? 0.2735 0.2562 0.2314 0.0274  0.0109  0.0015  1008 GLN A OE1 
7497  N NE2 . GLN A 1010 ? 0.2636 0.2425 0.2241 0.0255  0.0118  0.0069  1008 GLN A NE2 
7498  N N   . PRO A 1011 ? 0.2477 0.2450 0.1993 0.0309  0.0076  -0.0007 1009 PRO A N   
7499  C CA  . PRO A 1011 ? 0.2546 0.2563 0.2043 0.0323  0.0063  -0.0044 1009 PRO A CA  
7500  C C   . PRO A 1011 ? 0.2369 0.2338 0.1879 0.0316  0.0049  -0.0089 1009 PRO A C   
7501  O O   . PRO A 1011 ? 0.2345 0.2255 0.1874 0.0299  0.0046  -0.0085 1009 PRO A O   
7502  C CB  . PRO A 1011 ? 0.2370 0.2407 0.1861 0.0324  0.0058  -0.0024 1009 PRO A CB  
7503  C CG  . PRO A 1011 ? 0.2539 0.2574 0.2041 0.0318  0.0071  0.0029  1009 PRO A CG  
7504  C CD  . PRO A 1011 ? 0.2410 0.2384 0.1933 0.0304  0.0079  0.0034  1009 PRO A CD  
7505  N N   . PHE A 1012 ? 0.2299 0.2294 0.1804 0.0330  0.0041  -0.0130 1010 PHE A N   
7506  C CA  . PHE A 1012 ? 0.2281 0.2228 0.1808 0.0323  0.0028  -0.0168 1010 PHE A CA  
7507  C C   . PHE A 1012 ? 0.2372 0.2331 0.1903 0.0329  0.0007  -0.0210 1010 PHE A C   
7508  O O   . PHE A 1012 ? 0.2476 0.2498 0.1988 0.0349  0.0002  -0.0231 1010 PHE A O   
7509  C CB  . PHE A 1012 ? 0.2317 0.2275 0.1848 0.0333  0.0032  -0.0186 1010 PHE A CB  
7510  C CG  . PHE A 1012 ? 0.2347 0.2249 0.1908 0.0324  0.0018  -0.0217 1010 PHE A CG  
7511  C CD1 . PHE A 1012 ? 0.2447 0.2286 0.2027 0.0304  0.0022  -0.0195 1010 PHE A CD1 
7512  C CD2 . PHE A 1012 ? 0.2536 0.2450 0.2111 0.0336  -0.0002 -0.0268 1010 PHE A CD2 
7513  C CE1 . PHE A 1012 ? 0.2532 0.2323 0.2143 0.0294  0.0007  -0.0218 1010 PHE A CE1 
7514  C CE2 . PHE A 1012 ? 0.2831 0.2692 0.2442 0.0326  -0.0018 -0.0292 1010 PHE A CE2 
7515  C CZ  . PHE A 1012 ? 0.2430 0.2230 0.2058 0.0305  -0.0013 -0.0264 1010 PHE A CZ  
7516  N N   . GLY A 1013 ? 0.2278 0.2181 0.1833 0.0313  -0.0007 -0.0222 1011 GLY A N   
7517  C CA  . GLY A 1013 ? 0.2486 0.2393 0.2055 0.0317  -0.0029 -0.0264 1011 GLY A CA  
7518  C C   . GLY A 1013 ? 0.2349 0.2203 0.1940 0.0294  -0.0038 -0.0255 1011 GLY A C   
7519  O O   . GLY A 1013 ? 0.2592 0.2429 0.2176 0.0282  -0.0027 -0.0218 1011 GLY A O   
7520  N N   . GLY A 1014 ? 0.2516 0.2347 0.2137 0.0289  -0.0060 -0.0289 1012 GLY A N   
7521  C CA  . GLY A 1014 ? 0.2807 0.2591 0.2452 0.0266  -0.0070 -0.0280 1012 GLY A CA  
7522  C C   . GLY A 1014 ? 0.2762 0.2561 0.2417 0.0266  -0.0089 -0.0304 1012 GLY A C   
7523  O O   . GLY A 1014 ? 0.2647 0.2497 0.2284 0.0285  -0.0093 -0.0324 1012 GLY A O   
7524  N N   . ARG A 1015 ? 0.2445 0.2204 0.2132 0.0245  -0.0101 -0.0301 1013 ARG A N   
7525  C CA  . ARG A 1015 ? 0.2432 0.2199 0.2133 0.0239  -0.0119 -0.0315 1013 ARG A CA  
7526  C C   . ARG A 1015 ? 0.2480 0.2211 0.2232 0.0226  -0.0144 -0.0340 1013 ARG A C   
7527  O O   . ARG A 1015 ? 0.2479 0.2179 0.2254 0.0221  -0.0148 -0.0342 1013 ARG A O   
7528  C CB  . ARG A 1015 ? 0.2570 0.2328 0.2264 0.0223  -0.0107 -0.0278 1013 ARG A CB  
7529  C CG  . ARG A 1015 ? 0.2553 0.2265 0.2267 0.0198  -0.0100 -0.0251 1013 ARG A CG  
7530  C CD  . ARG A 1015 ? 0.3145 0.2853 0.2861 0.0181  -0.0094 -0.0225 1013 ARG A CD  
7531  N NE  . ARG A 1015 ? 0.3978 0.3709 0.3700 0.0183  -0.0109 -0.0240 1013 ARG A NE  
7532  C CZ  . ARG A 1015 ? 0.4290 0.4011 0.4048 0.0171  -0.0131 -0.0259 1013 ARG A CZ  
7533  N NH1 . ARG A 1015 ? 0.3858 0.3546 0.3651 0.0156  -0.0143 -0.0262 1013 ARG A NH1 
7534  N NH2 . ARG A 1015 ? 0.3516 0.3262 0.3278 0.0175  -0.0144 -0.0274 1013 ARG A NH2 
7535  N N   . GLY A 1016 ? 0.2745 0.2481 0.2519 0.0219  -0.0164 -0.0356 1014 GLY A N   
7536  C CA  . GLY A 1016 ? 0.2726 0.2429 0.2557 0.0204  -0.0190 -0.0374 1014 GLY A CA  
7537  C C   . GLY A 1016 ? 0.2471 0.2177 0.2324 0.0223  -0.0208 -0.0420 1014 GLY A C   
7538  O O   . GLY A 1016 ? 0.2720 0.2470 0.2550 0.0249  -0.0210 -0.0453 1014 GLY A O   
7539  N N   . LEU A 1017 ? 0.2535 0.2197 0.2435 0.0210  -0.0222 -0.0421 1015 LEU A N   
7540  C CA  . LEU A 1017 ? 0.2686 0.2346 0.2617 0.0227  -0.0241 -0.0465 1015 LEU A CA  
7541  C C   . LEU A 1017 ? 0.2475 0.2160 0.2363 0.0250  -0.0219 -0.0469 1015 LEU A C   
7542  O O   . LEU A 1017 ? 0.2552 0.2248 0.2459 0.0269  -0.0231 -0.0510 1015 LEU A O   
7543  C CB  . LEU A 1017 ? 0.2747 0.2350 0.2741 0.0206  -0.0260 -0.0457 1015 LEU A CB  
7544  C CG  . LEU A 1017 ? 0.2817 0.2396 0.2867 0.0181  -0.0287 -0.0453 1015 LEU A CG  
7545  C CD1 . LEU A 1017 ? 0.2858 0.2384 0.2969 0.0158  -0.0304 -0.0432 1015 LEU A CD1 
7546  C CD2 . LEU A 1017 ? 0.2918 0.2519 0.2999 0.0197  -0.0317 -0.0510 1015 LEU A CD2 
7547  N N   . SER A 1018 ? 0.2158 0.1856 0.1994 0.0249  -0.0187 -0.0429 1016 SER A N   
7548  C CA  . SER A 1018 ? 0.2438 0.2159 0.2236 0.0267  -0.0165 -0.0424 1016 SER A CA  
7549  C C   . SER A 1018 ? 0.2295 0.2084 0.2046 0.0292  -0.0154 -0.0438 1016 SER A C   
7550  O O   . SER A 1018 ? 0.2546 0.2365 0.2269 0.0310  -0.0138 -0.0439 1016 SER A O   
7551  C CB  . SER A 1018 ? 0.2472 0.2169 0.2248 0.0250  -0.0139 -0.0370 1016 SER A CB  
7552  O OG  . SER A 1018 ? 0.2399 0.2042 0.2215 0.0228  -0.0148 -0.0355 1016 SER A OG  
7553  N N   . GLY A 1019 ? 0.2291 0.2108 0.2031 0.0295  -0.0160 -0.0445 1017 GLY A N   
7554  C CA  . GLY A 1019 ? 0.2456 0.2343 0.2150 0.0319  -0.0150 -0.0454 1017 GLY A CA  
7555  C C   . GLY A 1019 ? 0.2603 0.2519 0.2284 0.0319  -0.0156 -0.0454 1017 GLY A C   
7556  O O   . GLY A 1019 ? 0.2642 0.2523 0.2339 0.0297  -0.0161 -0.0434 1017 GLY A O   
7557  N N   . THR A 1020 ? 0.2597 0.2582 0.2249 0.0343  -0.0158 -0.0479 1018 THR A N   
7558  C CA  . THR A 1020 ? 0.2553 0.2578 0.2182 0.0346  -0.0159 -0.0471 1018 THR A CA  
7559  C C   . THR A 1020 ? 0.2268 0.2320 0.1852 0.0348  -0.0132 -0.0419 1018 THR A C   
7560  O O   . THR A 1020 ? 0.2616 0.2684 0.2187 0.0344  -0.0130 -0.0397 1018 THR A O   
7561  C CB  . THR A 1020 ? 0.2464 0.2562 0.2084 0.0373  -0.0176 -0.0525 1018 THR A CB  
7562  O OG1 . THR A 1020 ? 0.2608 0.2761 0.2197 0.0395  -0.0162 -0.0531 1018 THR A OG1 
7563  C CG2 . THR A 1020 ? 0.2738 0.2810 0.2412 0.0372  -0.0209 -0.0582 1018 THR A CG2 
7564  N N   . GLY A 1021 ? 0.2570 0.2633 0.2134 0.0355  -0.0112 -0.0399 1019 GLY A N   
7565  C CA  . GLY A 1021 ? 0.2763 0.2867 0.2287 0.0362  -0.0089 -0.0355 1019 GLY A CA  
7566  C C   . GLY A 1021 ? 0.2703 0.2897 0.2197 0.0386  -0.0094 -0.0374 1019 GLY A C   
7567  O O   . GLY A 1021 ? 0.2549 0.2774 0.2052 0.0399  -0.0114 -0.0426 1019 GLY A O   
7568  N N   . PRO A 1022 ? 0.2612 0.2854 0.2072 0.0393  -0.0076 -0.0330 1020 PRO A N   
7569  C CA  . PRO A 1022 ? 0.2596 0.2808 0.2051 0.0380  -0.0053 -0.0271 1020 PRO A CA  
7570  C C   . PRO A 1022 ? 0.2661 0.2854 0.2120 0.0380  -0.0039 -0.0268 1020 PRO A C   
7571  O O   . PRO A 1022 ? 0.2831 0.3048 0.2291 0.0394  -0.0046 -0.0309 1020 PRO A O   
7572  C CB  . PRO A 1022 ? 0.2649 0.2937 0.2071 0.0393  -0.0044 -0.0235 1020 PRO A CB  
7573  C CG  . PRO A 1022 ? 0.2687 0.3059 0.2088 0.0417  -0.0054 -0.0279 1020 PRO A CG  
7574  C CD  . PRO A 1022 ? 0.2581 0.2921 0.2009 0.0416  -0.0078 -0.0339 1020 PRO A CD  
7575  N N   . LYS A 1023 ? 0.2493 0.2644 0.1956 0.0366  -0.0022 -0.0221 1021 LYS A N   
7576  C CA  . LYS A 1023 ? 0.2441 0.2569 0.1910 0.0364  -0.0009 -0.0214 1021 LYS A CA  
7577  C C   . LYS A 1023 ? 0.2614 0.2820 0.2056 0.0384  0.0003  -0.0208 1021 LYS A C   
7578  O O   . LYS A 1023 ? 0.2620 0.2880 0.2041 0.0390  0.0012  -0.0171 1021 LYS A O   
7579  C CB  . LYS A 1023 ? 0.2292 0.2366 0.1772 0.0345  0.0006  -0.0164 1021 LYS A CB  
7580  C CG  . LYS A 1023 ? 0.2305 0.2302 0.1812 0.0323  -0.0001 -0.0167 1021 LYS A CG  
7581  C CD  . LYS A 1023 ? 0.2403 0.2365 0.1917 0.0309  0.0015  -0.0119 1021 LYS A CD  
7582  C CE  . LYS A 1023 ? 0.2469 0.2361 0.2009 0.0288  0.0011  -0.0120 1021 LYS A CE  
7583  N NZ  . LYS A 1023 ? 0.2501 0.2357 0.2055 0.0281  0.0012  -0.0135 1021 LYS A NZ  
7584  N N   . ALA A 1024 ? 0.2573 0.2787 0.2021 0.0393  0.0003  -0.0241 1022 ALA A N   
7585  C CA  . ALA A 1024 ? 0.2593 0.2872 0.2020 0.0408  0.0019  -0.0228 1022 ALA A CA  
7586  C C   . ALA A 1024 ? 0.2444 0.2697 0.1872 0.0394  0.0039  -0.0165 1022 ALA A C   
7587  O O   . ALA A 1024 ? 0.2590 0.2764 0.2041 0.0374  0.0042  -0.0148 1022 ALA A O   
7588  C CB  . ALA A 1024 ? 0.2693 0.2970 0.2135 0.0418  0.0014  -0.0276 1022 ALA A CB  
7589  N N   . GLY A 1025 ? 0.2489 0.2815 0.1896 0.0404  0.0054  -0.0132 1023 GLY A N   
7590  C CA  . GLY A 1025 ? 0.2490 0.2797 0.1905 0.0391  0.0072  -0.0072 1023 GLY A CA  
7591  C C   . GLY A 1025 ? 0.2638 0.2905 0.2063 0.0376  0.0071  -0.0030 1023 GLY A C   
7592  O O   . GLY A 1025 ? 0.2391 0.2616 0.1833 0.0362  0.0082  0.0012  1023 GLY A O   
7593  N N   . GLY A 1026 ? 0.2269 0.2549 0.1685 0.0379  0.0058  -0.0043 1024 GLY A N   
7594  C CA  . GLY A 1026 ? 0.2577 0.2829 0.2004 0.0368  0.0055  -0.0007 1024 GLY A CA  
7595  C C   . GLY A 1026 ? 0.2388 0.2718 0.1795 0.0380  0.0050  0.0009  1024 GLY A C   
7596  O O   . GLY A 1026 ? 0.2444 0.2853 0.1825 0.0398  0.0047  -0.0012 1024 GLY A O   
7597  N N   . PRO A 1027 ? 0.2210 0.2523 0.1629 0.0372  0.0047  0.0046  1025 PRO A N   
7598  C CA  . PRO A 1027 ? 0.2559 0.2948 0.1963 0.0382  0.0044  0.0080  1025 PRO A CA  
7599  C C   . PRO A 1027 ? 0.2049 0.2475 0.1435 0.0393  0.0027  0.0043  1025 PRO A C   
7600  O O   . PRO A 1027 ? 0.2297 0.2797 0.1665 0.0403  0.0023  0.0066  1025 PRO A O   
7601  C CB  . PRO A 1027 ? 0.2643 0.2987 0.2078 0.0368  0.0046  0.0134  1025 PRO A CB  
7602  C CG  . PRO A 1027 ? 0.2609 0.2856 0.2069 0.0353  0.0043  0.0106  1025 PRO A CG  
7603  C CD  . PRO A 1027 ? 0.2307 0.2534 0.1759 0.0353  0.0048  0.0066  1025 PRO A CD  
7604  N N   . LEU A 1028 ? 0.2363 0.2739 0.1755 0.0389  0.0015  -0.0011 1026 LEU A N   
7605  C CA  . LEU A 1028 ? 0.2350 0.2760 0.1730 0.0399  -0.0002 -0.0051 1026 LEU A CA  
7606  C C   . LEU A 1028 ? 0.2252 0.2723 0.1609 0.0417  -0.0008 -0.0103 1026 LEU A C   
7607  O O   . LEU A 1028 ? 0.2473 0.2984 0.1818 0.0428  -0.0024 -0.0140 1026 LEU A O   
7608  C CB  . LEU A 1028 ? 0.2393 0.2722 0.1798 0.0384  -0.0015 -0.0081 1026 LEU A CB  
7609  C CG  . LEU A 1028 ? 0.2926 0.3202 0.2354 0.0369  -0.0013 -0.0041 1026 LEU A CG  
7610  C CD1 . LEU A 1028 ? 0.2918 0.3125 0.2369 0.0355  -0.0023 -0.0074 1026 LEU A CD1 
7611  C CD2 . LEU A 1028 ? 0.3841 0.4175 0.3260 0.0377  -0.0018 -0.0010 1026 LEU A CD2 
7612  N N   . TYR A 1029 ? 0.2363 0.2844 0.1715 0.0421  0.0004  -0.0108 1027 TYR A N   
7613  C CA  . TYR A 1029 ? 0.2460 0.2986 0.1800 0.0438  -0.0003 -0.0168 1027 TYR A CA  
7614  C C   . TYR A 1029 ? 0.2320 0.2965 0.1626 0.0461  -0.0007 -0.0177 1027 TYR A C   
7615  O O   . TYR A 1029 ? 0.2469 0.3148 0.1768 0.0474  -0.0025 -0.0234 1027 TYR A O   
7616  C CB  . TYR A 1029 ? 0.2408 0.2923 0.1752 0.0438  0.0013  -0.0163 1027 TYR A CB  
7617  C CG  . TYR A 1029 ? 0.2300 0.2821 0.1650 0.0451  0.0005  -0.0229 1027 TYR A CG  
7618  C CD1 . TYR A 1029 ? 0.2244 0.2687 0.1622 0.0442  -0.0011 -0.0274 1027 TYR A CD1 
7619  C CD2 . TYR A 1029 ? 0.2433 0.3036 0.1763 0.0470  0.0014  -0.0242 1027 TYR A CD2 
7620  C CE1 . TYR A 1029 ? 0.2354 0.2797 0.1747 0.0453  -0.0020 -0.0333 1027 TYR A CE1 
7621  C CE2 . TYR A 1029 ? 0.2640 0.3247 0.1981 0.0482  0.0006  -0.0304 1027 TYR A CE2 
7622  C CZ  . TYR A 1029 ? 0.2542 0.3066 0.1917 0.0474  -0.0012 -0.0349 1027 TYR A CZ  
7623  O OH  . TYR A 1029 ? 0.2680 0.3204 0.2073 0.0487  -0.0022 -0.0410 1027 TYR A OH  
7624  N N   . LEU A 1030 ? 0.2311 0.3024 0.1598 0.0465  0.0008  -0.0121 1028 LEU A N   
7625  C CA  . LEU A 1030 ? 0.2369 0.3209 0.1620 0.0486  0.0005  -0.0125 1028 LEU A CA  
7626  C C   . LEU A 1030 ? 0.2504 0.3370 0.1747 0.0491  -0.0014 -0.0140 1028 LEU A C   
7627  O O   . LEU A 1030 ? 0.2577 0.3534 0.1796 0.0511  -0.0024 -0.0181 1028 LEU A O   
7628  C CB  . LEU A 1030 ? 0.2410 0.3318 0.1648 0.0486  0.0024  -0.0050 1028 LEU A CB  
7629  C CG  . LEU A 1030 ? 0.2483 0.3390 0.1726 0.0484  0.0044  -0.0031 1028 LEU A CG  
7630  C CD1 . LEU A 1030 ? 0.2982 0.3966 0.2214 0.0482  0.0059  0.0049  1028 LEU A CD1 
7631  C CD2 . LEU A 1030 ? 0.2985 0.3943 0.2213 0.0503  0.0043  -0.0100 1028 LEU A CD2 
7632  N N   . GLY A 1031 ? 0.2352 0.3144 0.1616 0.0474  -0.0019 -0.0111 1029 GLY A N   
7633  C CA  . GLY A 1031 ? 0.2692 0.3508 0.1951 0.0477  -0.0037 -0.0120 1029 GLY A CA  
7634  C C   . GLY A 1031 ? 0.2533 0.3341 0.1796 0.0485  -0.0058 -0.0200 1029 GLY A C   
7635  O O   . GLY A 1031 ? 0.2809 0.3665 0.2061 0.0494  -0.0074 -0.0218 1029 GLY A O   
7636  N N   . ARG A 1032 ? 0.2392 0.3140 0.1674 0.0482  -0.0059 -0.0247 1030 ARG A N   
7637  C CA  . ARG A 1032 ? 0.2257 0.2999 0.1552 0.0490  -0.0082 -0.0325 1030 ARG A CA  
7638  C C   . ARG A 1032 ? 0.2648 0.3501 0.1915 0.0518  -0.0088 -0.0374 1030 ARG A C   
7639  O O   . ARG A 1032 ? 0.2759 0.3631 0.2035 0.0529  -0.0111 -0.0440 1030 ARG A O   
7640  C CB  . ARG A 1032 ? 0.2565 0.3204 0.1895 0.0477  -0.0083 -0.0353 1030 ARG A CB  
7641  C CG  . ARG A 1032 ? 0.2372 0.2979 0.1731 0.0478  -0.0109 -0.0424 1030 ARG A CG  
7642  C CD  . ARG A 1032 ? 0.2636 0.3198 0.2013 0.0463  -0.0123 -0.0417 1030 ARG A CD  
7643  N NE  . ARG A 1032 ? 0.2624 0.3138 0.2038 0.0459  -0.0147 -0.0477 1030 ARG A NE  
7644  C CZ  . ARG A 1032 ? 0.3012 0.3552 0.2435 0.0465  -0.0171 -0.0516 1030 ARG A CZ  
7645  N NH1 . ARG A 1032 ? 0.3312 0.3929 0.2704 0.0476  -0.0174 -0.0505 1030 ARG A NH1 
7646  N NH2 . ARG A 1032 ? 0.3287 0.3774 0.2753 0.0457  -0.0194 -0.0566 1030 ARG A NH2 
7647  N N   . LEU A 1033 ? 0.2360 0.3293 0.1599 0.0529  -0.0070 -0.0343 1031 LEU A N   
7648  C CA  . LEU A 1033 ? 0.2481 0.3528 0.1695 0.0556  -0.0072 -0.0390 1031 LEU A CA  
7649  C C   . LEU A 1033 ? 0.2364 0.3538 0.1538 0.0571  -0.0074 -0.0368 1031 LEU A C   
7650  O O   . LEU A 1033 ? 0.2586 0.3876 0.1731 0.0594  -0.0070 -0.0391 1031 LEU A O   
7651  C CB  . LEU A 1033 ? 0.2491 0.3551 0.1701 0.0559  -0.0051 -0.0376 1031 LEU A CB  
7652  C CG  . LEU A 1033 ? 0.2564 0.3495 0.1814 0.0542  -0.0048 -0.0385 1031 LEU A CG  
7653  C CD1 . LEU A 1033 ? 0.2591 0.3537 0.1837 0.0544  -0.0026 -0.0366 1031 LEU A CD1 
7654  C CD2 . LEU A 1033 ? 0.2932 0.3818 0.2212 0.0547  -0.0073 -0.0468 1031 LEU A CD2 
7655  N N   . VAL A 1034 ? 0.2562 0.3721 0.1734 0.0560  -0.0078 -0.0323 1032 VAL A N   
7656  C CA  . VAL A 1034 ? 0.2698 0.3970 0.1836 0.0572  -0.0084 -0.0299 1032 VAL A CA  
7657  C C   . VAL A 1034 ? 0.2766 0.4004 0.1918 0.0568  -0.0107 -0.0324 1032 VAL A C   
7658  O O   . VAL A 1034 ? 0.2871 0.3993 0.2058 0.0550  -0.0115 -0.0336 1032 VAL A O   
7659  C CB  . VAL A 1034 ? 0.2652 0.3952 0.1778 0.0562  -0.0064 -0.0199 1032 VAL A CB  
7660  C CG1 . VAL A 1034 ? 0.2943 0.4306 0.2052 0.0569  -0.0042 -0.0175 1032 VAL A CG1 
7661  C CG2 . VAL A 1034 ? 0.2579 0.3744 0.1741 0.0535  -0.0059 -0.0152 1032 VAL A CG2 
7662  N N   . THR A 1035 ? 0.2942 0.4287 0.2065 0.0584  -0.0120 -0.0331 1033 THR A N   
7663  C CA  . THR A 1035 ? 0.3001 0.4324 0.2137 0.0582  -0.0144 -0.0362 1033 THR A CA  
7664  C C   . THR A 1035 ? 0.3813 0.5063 0.2967 0.0560  -0.0142 -0.0294 1033 THR A C   
7665  O O   . THR A 1035 ? 0.4221 0.5398 0.3403 0.0549  -0.0158 -0.0317 1033 THR A O   
7666  C CB  . THR A 1035 ? 0.3803 0.5267 0.2905 0.0606  -0.0160 -0.0396 1033 THR A CB  
7667  O OG1 . THR A 1035 ? 0.4776 0.6340 0.3841 0.0611  -0.0146 -0.0321 1033 THR A OG1 
7668  C CG2 . THR A 1035 ? 0.3416 0.4943 0.2509 0.0629  -0.0166 -0.0478 1033 THR A CG2 
7669  N N   . THR A 1036 ? 0.3044 0.4315 0.2188 0.0553  -0.0124 -0.0211 1034 THR A N   
7670  C CA  . THR A 1036 ? 0.3169 0.4371 0.2335 0.0534  -0.0121 -0.0144 1034 THR A CA  
7671  C C   . THR A 1036 ? 0.3332 0.4463 0.2517 0.0518  -0.0098 -0.0092 1034 THR A C   
7672  O O   . THR A 1036 ? 0.3200 0.4394 0.2366 0.0524  -0.0082 -0.0051 1034 THR A O   
7673  C CB  . THR A 1036 ? 0.4030 0.5332 0.3175 0.0541  -0.0125 -0.0086 1034 THR A CB  
7674  O OG1 . THR A 1036 ? 0.4339 0.5714 0.3464 0.0557  -0.0147 -0.0138 1034 THR A OG1 
7675  C CG2 . THR A 1036 ? 0.4337 0.5565 0.3513 0.0523  -0.0124 -0.0020 1034 THR A CG2 
7676  N N   . ALA A 1037 ? 0.3385 0.4391 0.2606 0.0499  -0.0096 -0.0095 1035 ALA A N   
7677  C CA  . ALA A 1037 ? 0.3307 0.4243 0.2547 0.0485  -0.0076 -0.0058 1035 ALA A CA  
7678  C C   . ALA A 1037 ? 0.3040 0.3986 0.2289 0.0477  -0.0066 0.0030  1035 ALA A C   
7679  O O   . ALA A 1037 ? 0.3320 0.4261 0.2582 0.0473  -0.0076 0.0059  1035 ALA A O   
7680  C CB  . ALA A 1037 ? 0.3446 0.4253 0.2723 0.0467  -0.0078 -0.0086 1035 ALA A CB  
7681  N N   . PRO A 1038 ? 0.2780 0.3743 0.2027 0.0475  -0.0047 0.0074  1036 PRO A N   
7682  C CA  . PRO A 1038 ? 0.2526 0.3482 0.1794 0.0465  -0.0039 0.0158  1036 PRO A CA  
7683  C C   . PRO A 1038 ? 0.2692 0.3519 0.2005 0.0445  -0.0037 0.0169  1036 PRO A C   
7684  O O   . PRO A 1038 ? 0.2788 0.3536 0.2111 0.0438  -0.0038 0.0118  1036 PRO A O   
7685  C CB  . PRO A 1038 ? 0.2950 0.3957 0.2205 0.0468  -0.0020 0.0189  1036 PRO A CB  
7686  C CG  . PRO A 1038 ? 0.3124 0.4089 0.2373 0.0470  -0.0015 0.0120  1036 PRO A CG  
7687  C CD  . PRO A 1038 ? 0.3049 0.4027 0.2282 0.0481  -0.0033 0.0046  1036 PRO A CD  
7688  N N   . VAL A 1039 ? 0.2777 0.3587 0.2119 0.0436  -0.0033 0.0239  1037 VAL A N   
7689  C CA  . VAL A 1039 ? 0.2591 0.3290 0.1979 0.0418  -0.0030 0.0254  1037 VAL A CA  
7690  C C   . VAL A 1039 ? 0.2752 0.3421 0.2149 0.0411  -0.0011 0.0271  1037 VAL A C   
7691  O O   . VAL A 1039 ? 0.2714 0.3436 0.2113 0.0412  -0.0003 0.0327  1037 VAL A O   
7692  C CB  . VAL A 1039 ? 0.2565 0.3261 0.1988 0.0414  -0.0038 0.0318  1037 VAL A CB  
7693  C CG1 . VAL A 1039 ? 0.2832 0.3419 0.2305 0.0398  -0.0035 0.0328  1037 VAL A CG1 
7694  C CG2 . VAL A 1039 ? 0.3148 0.3880 0.2562 0.0422  -0.0057 0.0302  1037 VAL A CG2 
7695  N N   . PRO A 1040 ? 0.2577 0.3167 0.1981 0.0403  -0.0005 0.0227  1038 PRO A N   
7696  C CA  . PRO A 1040 ? 0.2744 0.3309 0.2155 0.0396  0.0012  0.0240  1038 PRO A CA  
7697  C C   . PRO A 1040 ? 0.2644 0.3169 0.2099 0.0384  0.0017  0.0305  1038 PRO A C   
7698  O O   . PRO A 1040 ? 0.2557 0.3046 0.2043 0.0378  0.0007  0.0325  1038 PRO A O   
7699  C CB  . PRO A 1040 ? 0.2707 0.3189 0.2122 0.0389  0.0013  0.0179  1038 PRO A CB  
7700  C CG  . PRO A 1040 ? 0.3065 0.3559 0.2463 0.0396  -0.0003 0.0127  1038 PRO A CG  
7701  C CD  . PRO A 1040 ? 0.2917 0.3447 0.2321 0.0399  -0.0014 0.0162  1038 PRO A CD  
7702  N N   . PRO A 1041 ? 0.2398 0.2930 0.1861 0.0380  0.0031  0.0337  1039 PRO A N   
7703  C CA  . PRO A 1041 ? 0.2441 0.2923 0.1954 0.0367  0.0035  0.0392  1039 PRO A CA  
7704  C C   . PRO A 1041 ? 0.2447 0.2822 0.1992 0.0355  0.0031  0.0361  1039 PRO A C   
7705  O O   . PRO A 1041 ? 0.2659 0.2991 0.2189 0.0353  0.0034  0.0305  1039 PRO A O   
7706  C CB  . PRO A 1041 ? 0.2688 0.3185 0.2198 0.0364  0.0051  0.0409  1039 PRO A CB  
7707  C CG  . PRO A 1041 ? 0.3062 0.3651 0.2520 0.0379  0.0056  0.0384  1039 PRO A CG  
7708  C CD  . PRO A 1041 ? 0.2760 0.3340 0.2192 0.0387  0.0044  0.0319  1039 PRO A CD  
7709  N N   . GLN A 1042 ? 0.2260 0.2598 0.1852 0.0348  0.0024  0.0399  1040 GLN A N   
7710  C CA  . GLN A 1042 ? 0.2355 0.2601 0.1985 0.0337  0.0021  0.0378  1040 GLN A CA  
7711  C C   . GLN A 1042 ? 0.2477 0.2696 0.2091 0.0338  0.0012  0.0322  1040 GLN A C   
7712  O O   . GLN A 1042 ? 0.2714 0.2863 0.2352 0.0329  0.0011  0.0296  1040 GLN A O   
7713  C CB  . GLN A 1042 ? 0.2985 0.3174 0.2628 0.0327  0.0034  0.0365  1040 GLN A CB  
7714  C CG  . GLN A 1042 ? 0.3820 0.4030 0.3485 0.0323  0.0042  0.0420  1040 GLN A CG  
7715  C CD  . GLN A 1042 ? 0.4452 0.4602 0.4134 0.0313  0.0053  0.0406  1040 GLN A CD  
7716  O OE1 . GLN A 1042 ? 0.5662 0.5756 0.5393 0.0303  0.0051  0.0420  1040 GLN A OE1 
7717  N NE2 . GLN A 1042 ? 0.4938 0.5101 0.4581 0.0314  0.0064  0.0375  1040 GLN A NE2 
7718  N N   . HIS A 1043 ? 0.2278 0.2553 0.1854 0.0349  0.0005  0.0302  1041 HIS A N   
7719  C CA  . HIS A 1043 ? 0.2195 0.2449 0.1754 0.0349  -0.0003 0.0245  1041 HIS A CA  
7720  C C   . HIS A 1043 ? 0.2508 0.2760 0.2092 0.0350  -0.0018 0.0258  1041 HIS A C   
7721  O O   . HIS A 1043 ? 0.2439 0.2755 0.2009 0.0361  -0.0027 0.0273  1041 HIS A O   
7722  C CB  . HIS A 1043 ? 0.2320 0.2639 0.1830 0.0361  -0.0005 0.0212  1041 HIS A CB  
7723  C CG  . HIS A 1043 ? 0.2385 0.2684 0.1882 0.0361  -0.0016 0.0154  1041 HIS A CG  
7724  N ND1 . HIS A 1043 ? 0.2399 0.2648 0.1893 0.0353  -0.0013 0.0107  1041 HIS A ND1 
7725  C CD2 . HIS A 1043 ? 0.2446 0.2773 0.1937 0.0366  -0.0031 0.0139  1041 HIS A CD2 
7726  C CE1 . HIS A 1043 ? 0.2642 0.2886 0.2130 0.0353  -0.0026 0.0066  1041 HIS A CE1 
7727  N NE2 . HIS A 1043 ? 0.2563 0.2854 0.2049 0.0362  -0.0036 0.0082  1041 HIS A NE2 
7728  N N   . SER A 1044 ? 0.2323 0.2508 0.1945 0.0341  -0.0019 0.0250  1042 SER A N   
7729  C CA  . SER A 1044 ? 0.2127 0.2302 0.1778 0.0342  -0.0033 0.0253  1042 SER A CA  
7730  C C   . SER A 1044 ? 0.2278 0.2378 0.1960 0.0330  -0.0030 0.0227  1042 SER A C   
7731  O O   . SER A 1044 ? 0.2567 0.2626 0.2254 0.0321  -0.0018 0.0217  1042 SER A O   
7732  C CB  . SER A 1044 ? 0.2483 0.2686 0.2169 0.0347  -0.0040 0.0314  1042 SER A CB  
7733  O OG  . SER A 1044 ? 0.2505 0.2665 0.2233 0.0340  -0.0033 0.0343  1042 SER A OG  
7734  N N   . SER A 1045 ? 0.2128 0.2216 0.1834 0.0330  -0.0041 0.0215  1043 SER A N   
7735  C CA  . SER A 1045 ? 0.2363 0.2392 0.2103 0.0319  -0.0039 0.0192  1043 SER A CA  
7736  C C   . SER A 1045 ? 0.2176 0.2205 0.1958 0.0324  -0.0052 0.0204  1043 SER A C   
7737  O O   . SER A 1045 ? 0.2298 0.2365 0.2070 0.0332  -0.0063 0.0203  1043 SER A O   
7738  C CB  . SER A 1045 ? 0.2404 0.2413 0.2118 0.0311  -0.0036 0.0139  1043 SER A CB  
7739  O OG  . SER A 1045 ? 0.2393 0.2358 0.2140 0.0301  -0.0034 0.0120  1043 SER A OG  
7740  N N   . VAL A 1046 ? 0.2310 0.2299 0.2143 0.0321  -0.0051 0.0211  1044 VAL A N   
7741  C CA  . VAL A 1046 ? 0.2308 0.2295 0.2190 0.0326  -0.0064 0.0216  1044 VAL A CA  
7742  C C   . VAL A 1046 ? 0.2217 0.2188 0.2098 0.0321  -0.0065 0.0168  1044 VAL A C   
7743  O O   . VAL A 1046 ? 0.2575 0.2549 0.2493 0.0326  -0.0076 0.0165  1044 VAL A O   
7744  C CB  . VAL A 1046 ? 0.2605 0.2559 0.2552 0.0328  -0.0067 0.0241  1044 VAL A CB  
7745  C CG1 . VAL A 1046 ? 0.2675 0.2648 0.2631 0.0332  -0.0069 0.0297  1044 VAL A CG1 
7746  C CG2 . VAL A 1046 ? 0.2465 0.2371 0.2422 0.0317  -0.0055 0.0209  1044 VAL A CG2 
7747  N N   . HIS A 1047 ? 0.2136 0.2096 0.1979 0.0310  -0.0055 0.0132  1045 HIS A N   
7748  C CA  . HIS A 1047 ? 0.2571 0.2519 0.2418 0.0302  -0.0056 0.0091  1045 HIS A CA  
7749  C C   . HIS A 1047 ? 0.2562 0.2545 0.2379 0.0304  -0.0065 0.0075  1045 HIS A C   
7750  O O   . HIS A 1047 ? 0.2682 0.2690 0.2459 0.0308  -0.0066 0.0081  1045 HIS A O   
7751  C CB  . HIS A 1047 ? 0.2791 0.2707 0.2621 0.0287  -0.0042 0.0066  1045 HIS A CB  
7752  C CG  . HIS A 1047 ? 0.3367 0.3251 0.3224 0.0286  -0.0034 0.0080  1045 HIS A CG  
7753  N ND1 . HIS A 1047 ? 0.3772 0.3639 0.3680 0.0287  -0.0036 0.0076  1045 HIS A ND1 
7754  C CD2 . HIS A 1047 ? 0.3473 0.3342 0.3318 0.0284  -0.0025 0.0097  1045 HIS A CD2 
7755  C CE1 . HIS A 1047 ? 0.3653 0.3494 0.3580 0.0286  -0.0029 0.0089  1045 HIS A CE1 
7756  N NE2 . HIS A 1047 ? 0.3801 0.3643 0.3690 0.0283  -0.0022 0.0103  1045 HIS A NE2 
7757  N N   . THR A 1048 ? 0.2409 0.2396 0.2247 0.0302  -0.0072 0.0055  1046 THR A N   
7758  C CA  . THR A 1048 ? 0.2451 0.2470 0.2268 0.0303  -0.0082 0.0037  1046 THR A CA  
7759  C C   . THR A 1048 ? 0.2469 0.2474 0.2284 0.0287  -0.0078 -0.0001 1046 THR A C   
7760  O O   . THR A 1048 ? 0.2581 0.2569 0.2427 0.0281  -0.0073 -0.0012 1046 THR A O   
7761  C CB  . THR A 1048 ? 0.2654 0.2701 0.2503 0.0315  -0.0096 0.0051  1046 THR A CB  
7762  O OG1 . THR A 1048 ? 0.2838 0.2897 0.2696 0.0328  -0.0101 0.0094  1046 THR A OG1 
7763  C CG2 . THR A 1048 ? 0.2715 0.2799 0.2539 0.0317  -0.0108 0.0035  1046 THR A CG2 
7764  N N   . ASP A 1049 ? 0.2419 0.2434 0.2200 0.0281  -0.0081 -0.0020 1047 ASP A N   
7765  C CA  . ASP A 1049 ? 0.2241 0.2244 0.2023 0.0264  -0.0080 -0.0051 1047 ASP A CA  
7766  C C   . ASP A 1049 ? 0.2422 0.2444 0.2235 0.0262  -0.0087 -0.0062 1047 ASP A C   
7767  O O   . ASP A 1049 ? 0.2295 0.2347 0.2112 0.0273  -0.0100 -0.0058 1047 ASP A O   
7768  C CB  . ASP A 1049 ? 0.2141 0.2153 0.1890 0.0259  -0.0086 -0.0070 1047 ASP A CB  
7769  C CG  . ASP A 1049 ? 0.2462 0.2461 0.2219 0.0239  -0.0087 -0.0096 1047 ASP A CG  
7770  O OD1 . ASP A 1049 ? 0.2557 0.2576 0.2331 0.0234  -0.0096 -0.0109 1047 ASP A OD1 
7771  O OD2 . ASP A 1049 ? 0.2618 0.2589 0.2367 0.0228  -0.0078 -0.0101 1047 ASP A OD2 
7772  N N   . PRO A 1050 ? 0.2220 0.2230 0.2057 0.0250  -0.0080 -0.0076 1048 PRO A N   
7773  C CA  . PRO A 1050 ? 0.2192 0.2225 0.2063 0.0251  -0.0086 -0.0087 1048 PRO A CA  
7774  C C   . PRO A 1050 ? 0.2393 0.2451 0.2257 0.0242  -0.0097 -0.0105 1048 PRO A C   
7775  O O   . PRO A 1050 ? 0.2432 0.2518 0.2319 0.0247  -0.0106 -0.0109 1048 PRO A O   
7776  C CB  . PRO A 1050 ? 0.2737 0.2756 0.2631 0.0240  -0.0073 -0.0098 1048 PRO A CB  
7777  C CG  . PRO A 1050 ? 0.2699 0.2691 0.2565 0.0226  -0.0063 -0.0100 1048 PRO A CG  
7778  C CD  . PRO A 1050 ? 0.2390 0.2370 0.2226 0.0237  -0.0066 -0.0082 1048 PRO A CD  
7779  N N   . VAL A 1051 ? 0.2184 0.2232 0.2024 0.0228  -0.0097 -0.0116 1049 VAL A N   
7780  C CA  . VAL A 1051 ? 0.2198 0.2267 0.2036 0.0220  -0.0111 -0.0134 1049 VAL A CA  
7781  C C   . VAL A 1051 ? 0.2342 0.2436 0.2165 0.0237  -0.0126 -0.0130 1049 VAL A C   
7782  O O   . VAL A 1051 ? 0.2378 0.2501 0.2213 0.0237  -0.0139 -0.0140 1049 VAL A O   
7783  C CB  . VAL A 1051 ? 0.2243 0.2292 0.2068 0.0201  -0.0111 -0.0147 1049 VAL A CB  
7784  C CG1 . VAL A 1051 ? 0.2601 0.2670 0.2435 0.0191  -0.0127 -0.0165 1049 VAL A CG1 
7785  C CG2 . VAL A 1051 ? 0.2539 0.2572 0.2380 0.0183  -0.0096 -0.0146 1049 VAL A CG2 
7786  N N   . LEU A 1052 ? 0.2217 0.2305 0.2014 0.0250  -0.0124 -0.0116 1050 LEU A N   
7787  C CA  . LEU A 1052 ? 0.2120 0.2242 0.1902 0.0268  -0.0136 -0.0106 1050 LEU A CA  
7788  C C   . LEU A 1052 ? 0.2406 0.2551 0.2217 0.0279  -0.0142 -0.0093 1050 LEU A C   
7789  O O   . LEU A 1052 ? 0.2139 0.2319 0.1952 0.0286  -0.0157 -0.0098 1050 LEU A O   
7790  C CB  . LEU A 1052 ? 0.2132 0.2249 0.1886 0.0280  -0.0130 -0.0085 1050 LEU A CB  
7791  C CG  . LEU A 1052 ? 0.2156 0.2315 0.1890 0.0300  -0.0140 -0.0068 1050 LEU A CG  
7792  C CD1 . LEU A 1052 ? 0.2141 0.2316 0.1902 0.0313  -0.0143 -0.0036 1050 LEU A CD1 
7793  C CD2 . LEU A 1052 ? 0.2233 0.2428 0.1952 0.0301  -0.0158 -0.0095 1050 LEU A CD2 
7794  N N   . LEU A 1053 ? 0.2173 0.2301 0.2010 0.0282  -0.0132 -0.0077 1051 LEU A N   
7795  C CA  . LEU A 1053 ? 0.2154 0.2301 0.2027 0.0293  -0.0139 -0.0066 1051 LEU A CA  
7796  C C   . LEU A 1053 ? 0.2114 0.2283 0.2008 0.0285  -0.0147 -0.0090 1051 LEU A C   
7797  O O   . LEU A 1053 ? 0.2231 0.2433 0.2141 0.0295  -0.0160 -0.0086 1051 LEU A O   
7798  C CB  . LEU A 1053 ? 0.2351 0.2472 0.2257 0.0297  -0.0127 -0.0053 1051 LEU A CB  
7799  C CG  . LEU A 1053 ? 0.2611 0.2716 0.2507 0.0307  -0.0123 -0.0021 1051 LEU A CG  
7800  C CD1 . LEU A 1053 ? 0.2741 0.2815 0.2674 0.0308  -0.0113 -0.0016 1051 LEU A CD1 
7801  C CD2 . LEU A 1053 ? 0.2774 0.2911 0.2672 0.0325  -0.0137 0.0008  1051 LEU A CD2 
7802  N N   . ASP A 1054 ? 0.2200 0.2356 0.2098 0.0266  -0.0139 -0.0112 1052 ASP A N   
7803  C CA  . ASP A 1054 ? 0.2221 0.2403 0.2143 0.0255  -0.0146 -0.0132 1052 ASP A CA  
7804  C C   . ASP A 1054 ? 0.2112 0.2319 0.2017 0.0255  -0.0163 -0.0142 1052 ASP A C   
7805  O O   . ASP A 1054 ? 0.2392 0.2631 0.2318 0.0257  -0.0175 -0.0149 1052 ASP A O   
7806  C CB  . ASP A 1054 ? 0.2325 0.2493 0.2252 0.0232  -0.0134 -0.0148 1052 ASP A CB  
7807  C CG  . ASP A 1054 ? 0.2902 0.3060 0.2853 0.0231  -0.0119 -0.0146 1052 ASP A CG  
7808  O OD1 . ASP A 1054 ? 0.2555 0.2716 0.2527 0.0249  -0.0119 -0.0136 1052 ASP A OD1 
7809  O OD2 . ASP A 1054 ? 0.3312 0.3461 0.3264 0.0213  -0.0108 -0.0155 1052 ASP A OD2 
7810  N N   . PHE A 1055 ? 0.2063 0.2259 0.1933 0.0254  -0.0166 -0.0145 1053 PHE A N   
7811  C CA  . PHE A 1055 ? 0.2113 0.2335 0.1967 0.0256  -0.0185 -0.0159 1053 PHE A CA  
7812  C C   . PHE A 1055 ? 0.2351 0.2610 0.2203 0.0278  -0.0197 -0.0144 1053 PHE A C   
7813  O O   . PHE A 1055 ? 0.2305 0.2598 0.2165 0.0280  -0.0213 -0.0156 1053 PHE A O   
7814  C CB  . PHE A 1055 ? 0.2213 0.2417 0.2033 0.0253  -0.0185 -0.0169 1053 PHE A CB  
7815  C CG  . PHE A 1055 ? 0.2210 0.2443 0.2017 0.0257  -0.0205 -0.0190 1053 PHE A CG  
7816  C CD1 . PHE A 1055 ? 0.2565 0.2811 0.2395 0.0244  -0.0219 -0.0213 1053 PHE A CD1 
7817  C CD2 . PHE A 1055 ? 0.2430 0.2679 0.2201 0.0273  -0.0210 -0.0189 1053 PHE A CD2 
7818  C CE1 . PHE A 1055 ? 0.2676 0.2949 0.2498 0.0247  -0.0240 -0.0237 1053 PHE A CE1 
7819  C CE2 . PHE A 1055 ? 0.2558 0.2839 0.2317 0.0278  -0.0230 -0.0214 1053 PHE A CE2 
7820  C CZ  . PHE A 1055 ? 0.2650 0.2941 0.2436 0.0265  -0.0245 -0.0240 1053 PHE A CZ  
7821  N N   . ALA A 1056 ? 0.2315 0.2569 0.2158 0.0293  -0.0190 -0.0116 1054 ALA A N   
7822  C CA  . ALA A 1056 ? 0.2296 0.2588 0.2141 0.0313  -0.0202 -0.0094 1054 ALA A CA  
7823  C C   . ALA A 1056 ? 0.2605 0.2916 0.2491 0.0316  -0.0210 -0.0094 1054 ALA A C   
7824  O O   . ALA A 1056 ? 0.2537 0.2887 0.2426 0.0326  -0.0227 -0.0093 1054 ALA A O   
7825  C CB  . ALA A 1056 ? 0.2562 0.2842 0.2399 0.0327  -0.0193 -0.0058 1054 ALA A CB  
7826  N N   . LYS A 1057 ? 0.2492 0.2780 0.2412 0.0308  -0.0198 -0.0098 1055 LYS A N   
7827  C CA  . LYS A 1057 ? 0.2657 0.2967 0.2621 0.0311  -0.0205 -0.0104 1055 LYS A CA  
7828  C C   . LYS A 1057 ? 0.2448 0.2786 0.2415 0.0299  -0.0216 -0.0131 1055 LYS A C   
7829  O O   . LYS A 1057 ? 0.2607 0.2979 0.2596 0.0307  -0.0230 -0.0132 1055 LYS A O   
7830  C CB  . LYS A 1057 ? 0.2865 0.3152 0.2863 0.0306  -0.0190 -0.0109 1055 LYS A CB  
7831  C CG  . LYS A 1057 ? 0.2973 0.3241 0.2990 0.0321  -0.0185 -0.0083 1055 LYS A CG  
7832  C CD  . LYS A 1057 ? 0.2741 0.2997 0.2802 0.0319  -0.0174 -0.0095 1055 LYS A CD  
7833  C CE  . LYS A 1057 ? 0.3117 0.3350 0.3160 0.0298  -0.0156 -0.0115 1055 LYS A CE  
7834  N NZ  . LYS A 1057 ? 0.3498 0.3718 0.3578 0.0300  -0.0144 -0.0122 1055 LYS A NZ  
7835  N N   . TRP A 1058 ? 0.2372 0.2693 0.2321 0.0280  -0.0212 -0.0151 1056 TRP A N   
7836  C CA  . TRP A 1058 ? 0.2540 0.2883 0.2496 0.0266  -0.0225 -0.0176 1056 TRP A CA  
7837  C C   . TRP A 1058 ? 0.2727 0.3103 0.2663 0.0278  -0.0245 -0.0179 1056 TRP A C   
7838  O O   . TRP A 1058 ? 0.2814 0.3225 0.2770 0.0278  -0.0261 -0.0190 1056 TRP A O   
7839  C CB  . TRP A 1058 ? 0.2631 0.2945 0.2575 0.0243  -0.0218 -0.0192 1056 TRP A CB  
7840  C CG  . TRP A 1058 ? 0.2782 0.3114 0.2739 0.0227  -0.0233 -0.0215 1056 TRP A CG  
7841  C CD1 . TRP A 1058 ? 0.3343 0.3693 0.3337 0.0209  -0.0234 -0.0225 1056 TRP A CD1 
7842  C CD2 . TRP A 1058 ? 0.2710 0.3050 0.2648 0.0227  -0.0251 -0.0233 1056 TRP A CD2 
7843  N NE1 . TRP A 1058 ? 0.3373 0.3735 0.3374 0.0196  -0.0253 -0.0244 1056 TRP A NE1 
7844  C CE2 . TRP A 1058 ? 0.3536 0.3891 0.3505 0.0208  -0.0264 -0.0252 1056 TRP A CE2 
7845  C CE3 . TRP A 1058 ? 0.2801 0.3141 0.2702 0.0241  -0.0258 -0.0235 1056 TRP A CE3 
7846  C CZ2 . TRP A 1058 ? 0.3426 0.3790 0.3392 0.0203  -0.0285 -0.0276 1056 TRP A CZ2 
7847  C CZ3 . TRP A 1058 ? 0.3230 0.3583 0.3124 0.0238  -0.0278 -0.0262 1056 TRP A CZ3 
7848  C CH2 . TRP A 1058 ? 0.3168 0.3530 0.3097 0.0219  -0.0293 -0.0283 1056 TRP A CH2 
7849  N N   . LEU A 1059 ? 0.2383 0.2755 0.2281 0.0290  -0.0247 -0.0169 1057 LEU A N   
7850  C CA  . LEU A 1059 ? 0.2637 0.3050 0.2512 0.0304  -0.0266 -0.0172 1057 LEU A CA  
7851  C C   . LEU A 1059 ? 0.2659 0.3111 0.2556 0.0321  -0.0277 -0.0153 1057 LEU A C   
7852  O O   . LEU A 1059 ? 0.2853 0.3345 0.2754 0.0324  -0.0296 -0.0165 1057 LEU A O   
7853  C CB  . LEU A 1059 ? 0.2362 0.2772 0.2195 0.0316  -0.0262 -0.0159 1057 LEU A CB  
7854  C CG  . LEU A 1059 ? 0.2528 0.2914 0.2337 0.0304  -0.0259 -0.0185 1057 LEU A CG  
7855  C CD1 . LEU A 1059 ? 0.2559 0.2942 0.2329 0.0316  -0.0250 -0.0169 1057 LEU A CD1 
7856  C CD2 . LEU A 1059 ? 0.2691 0.3106 0.2496 0.0300  -0.0281 -0.0221 1057 LEU A CD2 
7857  N N   . ASP A 1060 ? 0.2555 0.2994 0.2468 0.0331  -0.0267 -0.0123 1058 ASP A N   
7858  C CA  . ASP A 1060 ? 0.3044 0.3515 0.2987 0.0347  -0.0278 -0.0103 1058 ASP A CA  
7859  C C   . ASP A 1060 ? 0.2950 0.3438 0.2932 0.0339  -0.0285 -0.0125 1058 ASP A C   
7860  O O   . ASP A 1060 ? 0.3456 0.3986 0.3451 0.0348  -0.0303 -0.0124 1058 ASP A O   
7861  C CB  . ASP A 1060 ? 0.3397 0.3845 0.3363 0.0357  -0.0267 -0.0070 1058 ASP A CB  
7862  C CG  . ASP A 1060 ? 0.3039 0.3499 0.2978 0.0374  -0.0271 -0.0033 1058 ASP A CG  
7863  O OD1 . ASP A 1060 ? 0.4140 0.4646 0.4057 0.0383  -0.0287 -0.0027 1058 ASP A OD1 
7864  O OD2 . ASP A 1060 ? 0.4194 0.4623 0.4138 0.0376  -0.0258 -0.0010 1058 ASP A OD2 
7865  N N   . GLY A 1061 ? 0.3123 0.3585 0.3125 0.0320  -0.0272 -0.0144 1059 GLY A N   
7866  C CA  . GLY A 1061 ? 0.3228 0.3711 0.3268 0.0310  -0.0277 -0.0164 1059 GLY A CA  
7867  C C   . GLY A 1061 ? 0.3596 0.4110 0.3627 0.0302  -0.0296 -0.0187 1059 GLY A C   
7868  O O   . GLY A 1061 ? 0.3333 0.3881 0.3394 0.0301  -0.0308 -0.0196 1059 GLY A O   
7869  N N   . LYS A 1062 ? 0.3199 0.3702 0.3192 0.0296  -0.0299 -0.0198 1060 LYS A N   
7870  C CA  . LYS A 1062 ? 0.3253 0.3783 0.3239 0.0290  -0.0320 -0.0223 1060 LYS A CA  
7871  C C   . LYS A 1062 ? 0.3407 0.3982 0.3374 0.0312  -0.0339 -0.0215 1060 LYS A C   
7872  O O   . LYS A 1062 ? 0.4408 0.5015 0.4371 0.0311  -0.0359 -0.0239 1060 LYS A O   
7873  C CB  . LYS A 1062 ? 0.3525 0.4026 0.3484 0.0277  -0.0318 -0.0243 1060 LYS A CB  
7874  C CG  . LYS A 1062 ? 0.3878 0.4343 0.3859 0.0251  -0.0305 -0.0252 1060 LYS A CG  
7875  C CD  . LYS A 1062 ? 0.4515 0.5003 0.4538 0.0233  -0.0316 -0.0269 1060 LYS A CD  
7876  C CE  . LYS A 1062 ? 0.5364 0.5826 0.5412 0.0207  -0.0301 -0.0271 1060 LYS A CE  
7877  N NZ  . LYS A 1062 ? 0.5523 0.6013 0.5614 0.0187  -0.0313 -0.0284 1060 LYS A NZ  
7878  N N   . GLY A 1063 ? 0.3133 0.3716 0.3092 0.0332  -0.0335 -0.0182 1061 GLY A N   
7879  C CA  . GLY A 1063 ? 0.3444 0.4075 0.3383 0.0353  -0.0353 -0.0167 1061 GLY A CA  
7880  C C   . GLY A 1063 ? 0.3800 0.4441 0.3687 0.0361  -0.0355 -0.0166 1061 GLY A C   
7881  O O   . GLY A 1063 ? 0.3740 0.4432 0.3606 0.0377  -0.0371 -0.0156 1061 GLY A O   
7882  N N   . ALA A 1064 ? 0.3195 0.3795 0.3062 0.0350  -0.0340 -0.0176 1062 ALA A N   
7883  C CA  . ALA A 1064 ? 0.3011 0.3620 0.2829 0.0358  -0.0340 -0.0179 1062 ALA A CA  
7884  C C   . ALA A 1064 ? 0.3214 0.3820 0.3017 0.0372  -0.0326 -0.0133 1062 ALA A C   
7885  O O   . ALA A 1064 ? 0.2710 0.3276 0.2498 0.0368  -0.0308 -0.0125 1062 ALA A O   
7886  C CB  . ALA A 1064 ? 0.3189 0.3756 0.2999 0.0340  -0.0331 -0.0211 1062 ALA A CB  
7887  N N   . ARG A 1065 ? 0.2792 0.3441 0.2601 0.0389  -0.0337 -0.0102 1063 ARG A N   
7888  C CA  . ARG A 1065 ? 0.2762 0.3407 0.2574 0.0401  -0.0328 -0.0052 1063 ARG A CA  
7889  C C   . ARG A 1065 ? 0.2993 0.3648 0.2758 0.0407  -0.0320 -0.0038 1063 ARG A C   
7890  O O   . ARG A 1065 ? 0.2893 0.3513 0.2658 0.0407  -0.0303 -0.0010 1063 ARG A O   
7891  C CB  . ARG A 1065 ? 0.3002 0.3696 0.2834 0.0417  -0.0345 -0.0019 1063 ARG A CB  
7892  N N   . ALA A 1066 ? 0.2911 0.3619 0.2635 0.0414  -0.0332 -0.0057 1064 ALA A N   
7893  C CA  . ALA A 1066 ? 0.2753 0.3482 0.2433 0.0421  -0.0324 -0.0046 1064 ALA A CA  
7894  C C   . ALA A 1066 ? 0.2824 0.3492 0.2495 0.0407  -0.0305 -0.0070 1064 ALA A C   
7895  O O   . ALA A 1066 ? 0.2910 0.3563 0.2564 0.0410  -0.0290 -0.0045 1064 ALA A O   
7896  C CB  . ALA A 1066 ? 0.2898 0.3705 0.2538 0.0433  -0.0342 -0.0070 1064 ALA A CB  
7897  N N   . GLU A 1067 ? 0.2752 0.3384 0.2437 0.0392  -0.0307 -0.0116 1065 GLU A N   
7898  C CA  . GLU A 1067 ? 0.2559 0.3133 0.2239 0.0378  -0.0291 -0.0137 1065 GLU A CA  
7899  C C   . GLU A 1067 ? 0.2691 0.3206 0.2397 0.0369  -0.0270 -0.0107 1065 GLU A C   
7900  O O   . GLU A 1067 ? 0.2680 0.3159 0.2373 0.0365  -0.0254 -0.0102 1065 GLU A O   
7901  C CB  . GLU A 1067 ? 0.2958 0.3511 0.2654 0.0362  -0.0300 -0.0188 1065 GLU A CB  
7902  C CG  . GLU A 1067 ? 0.2723 0.3324 0.2395 0.0369  -0.0320 -0.0229 1065 GLU A CG  
7903  C CD  . GLU A 1067 ? 0.3522 0.4187 0.3198 0.0380  -0.0343 -0.0233 1065 GLU A CD  
7904  O OE1 . GLU A 1067 ? 0.2916 0.3583 0.2619 0.0380  -0.0344 -0.0206 1065 GLU A OE1 
7905  O OE2 . GLU A 1067 ? 0.3863 0.4577 0.3517 0.0389  -0.0360 -0.0265 1065 GLU A OE2 
7906  N N   . ALA A 1068 ? 0.2688 0.3195 0.2432 0.0369  -0.0272 -0.0090 1066 ALA A N   
7907  C CA  . ALA A 1068 ? 0.2714 0.3171 0.2487 0.0364  -0.0255 -0.0064 1066 ALA A CA  
7908  C C   . ALA A 1068 ? 0.2650 0.3112 0.2409 0.0376  -0.0246 -0.0020 1066 ALA A C   
7909  O O   . ALA A 1068 ? 0.2610 0.3028 0.2374 0.0370  -0.0229 -0.0008 1066 ALA A O   
7910  C CB  . ALA A 1068 ? 0.2788 0.3248 0.2608 0.0365  -0.0261 -0.0056 1066 ALA A CB  
7911  N N   . GLU A 1069 ? 0.2531 0.3050 0.2276 0.0392  -0.0259 0.0007  1067 GLU A N   
7912  C CA  . GLU A 1069 ? 0.2592 0.3125 0.2325 0.0403  -0.0252 0.0054  1067 GLU A CA  
7913  C C   . GLU A 1069 ? 0.2883 0.3409 0.2572 0.0399  -0.0239 0.0042  1067 GLU A C   
7914  O O   . GLU A 1069 ? 0.2789 0.3288 0.2479 0.0398  -0.0224 0.0069  1067 GLU A O   
7915  C CB  . GLU A 1069 ? 0.3112 0.3719 0.2835 0.0420  -0.0270 0.0087  1067 GLU A CB  
7916  C CG  . GLU A 1069 ? 0.3966 0.4602 0.3672 0.0429  -0.0265 0.0139  1067 GLU A CG  
7917  C CD  . GLU A 1069 ? 0.4760 0.5356 0.4515 0.0430  -0.0258 0.0187  1067 GLU A CD  
7918  O OE1 . GLU A 1069 ? 0.5487 0.6034 0.5288 0.0424  -0.0258 0.0175  1067 GLU A OE1 
7919  O OE2 . GLU A 1069 ? 0.6258 0.6874 0.6008 0.0436  -0.0255 0.0235  1067 GLU A OE2 
7920  N N   . ALA A 1070 ? 0.2811 0.3362 0.2467 0.0398  -0.0246 0.0000  1068 ALA A N   
7921  C CA  . ALA A 1070 ? 0.2612 0.3159 0.2232 0.0396  -0.0235 -0.0018 1068 ALA A CA  
7922  C C   . ALA A 1070 ? 0.2463 0.2932 0.2099 0.0380  -0.0217 -0.0031 1068 ALA A C   
7923  O O   . ALA A 1070 ? 0.2673 0.3123 0.2292 0.0378  -0.0203 -0.0022 1068 ALA A O   
7924  C CB  . ALA A 1070 ? 0.2986 0.3572 0.2578 0.0399  -0.0250 -0.0069 1068 ALA A CB  
7925  N N   . ALA A 1071 ? 0.2491 0.2919 0.2161 0.0367  -0.0218 -0.0051 1069 ALA A N   
7926  C CA  . ALA A 1071 ? 0.2133 0.2494 0.1820 0.0350  -0.0202 -0.0061 1069 ALA A CA  
7927  C C   . ALA A 1071 ? 0.2525 0.2858 0.2228 0.0353  -0.0187 -0.0019 1069 ALA A C   
7928  O O   . ALA A 1071 ? 0.2223 0.2520 0.1918 0.0347  -0.0172 -0.0016 1069 ALA A O   
7929  C CB  . ALA A 1071 ? 0.2429 0.2766 0.2149 0.0336  -0.0207 -0.0088 1069 ALA A CB  
7930  N N   . ARG A 1072 ? 0.2342 0.2691 0.2073 0.0362  -0.0193 0.0013  1070 ARG A N   
7931  C CA  . ARG A 1072 ? 0.2453 0.2776 0.2209 0.0365  -0.0183 0.0053  1070 ARG A CA  
7932  C C   . ARG A 1072 ? 0.2443 0.2783 0.2168 0.0372  -0.0176 0.0082  1070 ARG A C   
7933  O O   . ARG A 1072 ? 0.2645 0.2948 0.2378 0.0368  -0.0161 0.0098  1070 ARG A O   
7934  C CB  . ARG A 1072 ? 0.2373 0.2715 0.2171 0.0376  -0.0195 0.0083  1070 ARG A CB  
7935  C CG  . ARG A 1072 ? 0.2828 0.3143 0.2668 0.0369  -0.0197 0.0059  1070 ARG A CG  
7936  C CD  . ARG A 1072 ? 0.3007 0.3338 0.2895 0.0382  -0.0209 0.0090  1070 ARG A CD  
7937  N NE  . ARG A 1072 ? 0.3489 0.3879 0.3364 0.0393  -0.0228 0.0102  1070 ARG A NE  
7938  C CZ  . ARG A 1072 ? 0.3337 0.3752 0.3218 0.0393  -0.0240 0.0076  1070 ARG A CZ  
7939  N NH1 . ARG A 1072 ? 0.3692 0.4081 0.3592 0.0381  -0.0236 0.0038  1070 ARG A NH1 
7940  N NH2 . ARG A 1072 ? 0.3676 0.4148 0.3545 0.0404  -0.0258 0.0090  1070 ARG A NH2 
7941  N N   . ASN A 1073 ? 0.2373 0.2775 0.2062 0.0383  -0.0185 0.0087  1071 ASN A N   
7942  C CA  . ASN A 1073 ? 0.2515 0.2945 0.2172 0.0390  -0.0178 0.0114  1071 ASN A CA  
7943  C C   . ASN A 1073 ? 0.2637 0.3032 0.2269 0.0380  -0.0163 0.0083  1071 ASN A C   
7944  O O   . ASN A 1073 ? 0.2785 0.3166 0.2411 0.0380  -0.0149 0.0108  1071 ASN A O   
7945  C CB  . ASN A 1073 ? 0.2818 0.3332 0.2439 0.0404  -0.0192 0.0119  1071 ASN A CB  
7946  C CG  . ASN A 1073 ? 0.3264 0.3820 0.2908 0.0415  -0.0206 0.0166  1071 ASN A CG  
7947  O OD1 . ASN A 1073 ? 0.3806 0.4329 0.3495 0.0413  -0.0204 0.0202  1071 ASN A OD1 
7948  N ND2 . ASN A 1073 ? 0.3647 0.4278 0.3266 0.0426  -0.0221 0.0164  1071 ASN A ND2 
7949  N N   . ALA A 1074 ? 0.2306 0.2685 0.1928 0.0372  -0.0166 0.0031  1072 ALA A N   
7950  C CA  . ALA A 1074 ? 0.2292 0.2632 0.1898 0.0362  -0.0154 0.0002  1072 ALA A CA  
7951  C C   . ALA A 1074 ? 0.2530 0.2804 0.2165 0.0350  -0.0138 0.0016  1072 ALA A C   
7952  O O   . ALA A 1074 ? 0.2354 0.2605 0.1977 0.0346  -0.0124 0.0020  1072 ALA A O   
7953  C CB  . ALA A 1074 ? 0.2966 0.3297 0.2568 0.0353  -0.0164 -0.0052 1072 ALA A CB  
7954  N N   . GLY A 1075 ? 0.2353 0.2600 0.2026 0.0344  -0.0140 0.0021  1073 GLY A N   
7955  C CA  . GLY A 1075 ? 0.2277 0.2468 0.1980 0.0334  -0.0126 0.0030  1073 GLY A CA  
7956  C C   . GLY A 1075 ? 0.2451 0.2637 0.2159 0.0341  -0.0117 0.0073  1073 GLY A C   
7957  O O   . GLY A 1075 ? 0.2663 0.2809 0.2376 0.0333  -0.0103 0.0075  1073 GLY A O   
7958  N N   . SER A 1076 ? 0.2443 0.2673 0.2154 0.0354  -0.0125 0.0111  1074 SER A N   
7959  C CA  . SER A 1076 ? 0.2526 0.2759 0.2247 0.0360  -0.0119 0.0159  1074 SER A CA  
7960  C C   . SER A 1076 ? 0.2598 0.2853 0.2275 0.0361  -0.0109 0.0162  1074 SER A C   
7961  O O   . SER A 1076 ? 0.2925 0.3157 0.2607 0.0358  -0.0097 0.0183  1074 SER A O   
7962  C CB  . SER A 1076 ? 0.2911 0.3190 0.2651 0.0373  -0.0133 0.0204  1074 SER A CB  
7963  O OG  . SER A 1076 ? 0.4184 0.4441 0.3974 0.0373  -0.0142 0.0205  1074 SER A OG  
7964  N N   . SER A 1077 ? 0.2502 0.2804 0.2136 0.0367  -0.0116 0.0138  1075 SER A N   
7965  C CA  A SER A 1077 ? 0.2659 0.2995 0.2252 0.0372  -0.0108 0.0138  1075 SER A CA  
7966  C CA  B SER A 1077 ? 0.2659 0.2996 0.2252 0.0372  -0.0108 0.0137  1075 SER A CA  
7967  C C   . SER A 1077 ? 0.2500 0.2786 0.2083 0.0361  -0.0095 0.0104  1075 SER A C   
7968  O O   . SER A 1077 ? 0.2711 0.3007 0.2274 0.0362  -0.0084 0.0113  1075 SER A O   
7969  C CB  A SER A 1077 ? 0.2587 0.2994 0.2142 0.0383  -0.0121 0.0116  1075 SER A CB  
7970  C CB  B SER A 1077 ? 0.2581 0.2986 0.2136 0.0383  -0.0121 0.0113  1075 SER A CB  
7971  O OG  A SER A 1077 ? 0.3197 0.3665 0.2755 0.0395  -0.0132 0.0157  1075 SER A OG  
7972  O OG  B SER A 1077 ? 0.3137 0.3582 0.2652 0.0389  -0.0114 0.0103  1075 SER A OG  
7973  N N   . SER A 1078 ? 0.2201 0.2437 0.1800 0.0349  -0.0095 0.0068  1076 SER A N   
7974  C CA  . SER A 1078 ? 0.2189 0.2376 0.1783 0.0337  -0.0085 0.0038  1076 SER A CA  
7975  C C   . SER A 1078 ? 0.2350 0.2502 0.1958 0.0332  -0.0069 0.0069  1076 SER A C   
7976  O O   . SER A 1078 ? 0.2458 0.2593 0.2099 0.0332  -0.0067 0.0101  1076 SER A O   
7977  C CB  . SER A 1078 ? 0.2362 0.2506 0.1979 0.0323  -0.0089 0.0007  1076 SER A CB  
7978  O OG  . SER A 1078 ? 0.2310 0.2407 0.1927 0.0310  -0.0078 -0.0014 1076 SER A OG  
7979  N N   . ALA A 1079 ? 0.2108 0.2250 0.1695 0.0329  -0.0059 0.0058  1077 ALA A N   
7980  C CA  . ALA A 1079 ? 0.2142 0.2247 0.1743 0.0323  -0.0044 0.0081  1077 ALA A CA  
7981  C C   . ALA A 1079 ? 0.2411 0.2453 0.2026 0.0307  -0.0037 0.0053  1077 ALA A C   
7982  O O   . ALA A 1079 ? 0.2173 0.2184 0.1796 0.0301  -0.0025 0.0063  1077 ALA A O   
7983  C CB  . ALA A 1079 ? 0.2257 0.2395 0.1828 0.0331  -0.0035 0.0093  1077 ALA A CB  
7984  N N   . LEU A 1080 ? 0.2183 0.2211 0.1804 0.0300  -0.0045 0.0020  1078 LEU A N   
7985  C CA  . LEU A 1080 ? 0.2077 0.2054 0.1717 0.0283  -0.0040 -0.0001 1078 LEU A CA  
7986  C C   . LEU A 1080 ? 0.2085 0.2032 0.1756 0.0279  -0.0031 0.0024  1078 LEU A C   
7987  O O   . LEU A 1080 ? 0.2170 0.2127 0.1864 0.0285  -0.0035 0.0045  1078 LEU A O   
7988  C CB  . LEU A 1080 ? 0.2019 0.1997 0.1670 0.0276  -0.0052 -0.0027 1078 LEU A CB  
7989  C CG  . LEU A 1080 ? 0.2125 0.2062 0.1798 0.0258  -0.0047 -0.0043 1078 LEU A CG  
7990  C CD1 . LEU A 1080 ? 0.2553 0.2466 0.2211 0.0248  -0.0043 -0.0063 1078 LEU A CD1 
7991  C CD2 . LEU A 1080 ? 0.2288 0.2235 0.1977 0.0252  -0.0058 -0.0060 1078 LEU A CD2 
7992  N N   . GLY A 1081 ? 0.2131 0.2041 0.1806 0.0269  -0.0019 0.0021  1079 GLY A N   
7993  C CA  . GLY A 1081 ? 0.2269 0.2151 0.1976 0.0266  -0.0012 0.0039  1079 GLY A CA  
7994  C C   . GLY A 1081 ? 0.2271 0.2154 0.1980 0.0272  -0.0004 0.0072  1079 GLY A C   
7995  O O   . GLY A 1081 ? 0.2492 0.2349 0.2232 0.0269  0.0001  0.0086  1079 GLY A O   
7996  N N   . LEU A 1082 ? 0.2192 0.2109 0.1872 0.0282  -0.0005 0.0086  1080 LEU A N   
7997  C CA  A LEU A 1082 ? 0.2191 0.2113 0.1871 0.0286  0.0004  0.0117  1080 LEU A CA  
7998  C CA  B LEU A 1082 ? 0.2190 0.2112 0.1870 0.0286  0.0004  0.0117  1080 LEU A CA  
7999  C C   . LEU A 1082 ? 0.2405 0.2283 0.2090 0.0275  0.0016  0.0106  1080 LEU A C   
8000  O O   . LEU A 1082 ? 0.2431 0.2291 0.2100 0.0266  0.0017  0.0074  1080 LEU A O   
8001  C CB  A LEU A 1082 ? 0.2259 0.2230 0.1899 0.0296  0.0004  0.0120  1080 LEU A CB  
8002  C CB  B LEU A 1082 ? 0.2258 0.2230 0.1898 0.0297  0.0004  0.0120  1080 LEU A CB  
8003  C CG  A LEU A 1082 ? 0.2403 0.2393 0.2038 0.0301  0.0014  0.0154  1080 LEU A CG  
8004  C CG  B LEU A 1082 ? 0.2402 0.2394 0.2034 0.0301  0.0014  0.0152  1080 LEU A CG  
8005  C CD1 A LEU A 1082 ? 0.2268 0.2265 0.1939 0.0304  0.0012  0.0203  1080 LEU A CD1 
8006  C CD1 B LEU A 1082 ? 0.2354 0.2416 0.1957 0.0316  0.0010  0.0168  1080 LEU A CD1 
8007  C CD2 A LEU A 1082 ? 0.2340 0.2390 0.1934 0.0313  0.0013  0.0150  1080 LEU A CD2 
8008  C CD2 B LEU A 1082 ? 0.2121 0.2086 0.1738 0.0294  0.0024  0.0129  1080 LEU A CD2 
8009  N N   . ASP A 1083 ? 0.2432 0.2293 0.2144 0.0274  0.0022  0.0134  1081 ASP A N   
8010  C CA  . ASP A 1083 ? 0.2527 0.2347 0.2249 0.0263  0.0032  0.0125  1081 ASP A CA  
8011  C C   . ASP A 1083 ? 0.2647 0.2470 0.2387 0.0266  0.0038  0.0163  1081 ASP A C   
8012  O O   . ASP A 1083 ? 0.3091 0.2906 0.2872 0.0268  0.0034  0.0189  1081 ASP A O   
8013  C CB  . ASP A 1083 ? 0.2937 0.2725 0.2693 0.0254  0.0029  0.0107  1081 ASP A CB  
8014  C CG  . ASP A 1083 ? 0.3901 0.3652 0.3664 0.0242  0.0038  0.0093  1081 ASP A CG  
8015  O OD1 . ASP A 1083 ? 0.4399 0.4146 0.4140 0.0240  0.0046  0.0094  1081 ASP A OD1 
8016  O OD2 . ASP A 1083 ? 0.4179 0.3909 0.3972 0.0236  0.0037  0.0081  1081 ASP A OD2 
8017  N N   . LEU A 1084 ? 0.2524 0.2358 0.2237 0.0266  0.0046  0.0167  1082 LEU A N   
8018  C CA  . LEU A 1084 ? 0.2623 0.2472 0.2349 0.0270  0.0052  0.0207  1082 LEU A CA  
8019  C C   . LEU A 1084 ? 0.2619 0.2438 0.2343 0.0261  0.0063  0.0198  1082 LEU A C   
8020  O O   . LEU A 1084 ? 0.2785 0.2587 0.2485 0.0256  0.0066  0.0164  1082 LEU A O   
8021  C CB  . LEU A 1084 ? 0.2742 0.2651 0.2433 0.0281  0.0053  0.0224  1082 LEU A CB  
8022  C CG  . LEU A 1084 ? 0.3099 0.3052 0.2784 0.0291  0.0042  0.0237  1082 LEU A CG  
8023  C CD1 . LEU A 1084 ? 0.3231 0.3248 0.2873 0.0302  0.0045  0.0242  1082 LEU A CD1 
8024  C CD2 . LEU A 1084 ? 0.3452 0.3407 0.3183 0.0293  0.0036  0.0284  1082 LEU A CD2 
8025  N N   . GLU A 1085 ? 0.2551 0.2364 0.2305 0.0259  0.0067  0.0232  1083 GLU A N   
8026  C CA  . GLU A 1085 ? 0.2373 0.2171 0.2126 0.0253  0.0078  0.0232  1083 GLU A CA  
8027  C C   . GLU A 1085 ? 0.2564 0.2411 0.2298 0.0261  0.0084  0.0263  1083 GLU A C   
8028  O O   . GLU A 1085 ? 0.3135 0.3014 0.2889 0.0266  0.0081  0.0306  1083 GLU A O   
8029  C CB  . GLU A 1085 ? 0.2711 0.2467 0.2514 0.0245  0.0078  0.0244  1083 GLU A CB  
8030  C CG  . GLU A 1085 ? 0.2810 0.2554 0.2609 0.0239  0.0089  0.0245  1083 GLU A CG  
8031  C CD  . GLU A 1085 ? 0.3769 0.3470 0.3613 0.0229  0.0088  0.0245  1083 GLU A CD  
8032  O OE1 . GLU A 1085 ? 0.3770 0.3446 0.3646 0.0227  0.0080  0.0233  1083 GLU A OE1 
8033  O OE2 . GLU A 1085 ? 0.3807 0.3501 0.3656 0.0224  0.0096  0.0254  1083 GLU A OE2 
8034  N N   . LEU A 1086 ? 0.2568 0.2427 0.2267 0.0262  0.0093  0.0243  1084 LEU A N   
8035  C CA  . LEU A 1086 ? 0.2490 0.2407 0.2167 0.0271  0.0100  0.0266  1084 LEU A CA  
8036  C C   . LEU A 1086 ? 0.2817 0.2723 0.2517 0.0265  0.0110  0.0291  1084 LEU A C   
8037  O O   . LEU A 1086 ? 0.2734 0.2592 0.2446 0.0255  0.0113  0.0271  1084 LEU A O   
8038  C CB  . LEU A 1086 ? 0.2553 0.2490 0.2184 0.0278  0.0102  0.0224  1084 LEU A CB  
8039  C CG  . LEU A 1086 ? 0.3006 0.2953 0.2616 0.0284  0.0091  0.0195  1084 LEU A CG  
8040  C CD1 . LEU A 1086 ? 0.2891 0.2860 0.2465 0.0291  0.0090  0.0152  1084 LEU A CD1 
8041  C CD2 . LEU A 1086 ? 0.3212 0.3209 0.2824 0.0292  0.0085  0.0228  1084 LEU A CD2 
8042  N N   . PRO A 1087 ? 0.2839 0.2795 0.2547 0.0269  0.0114  0.0338  1085 PRO A N   
8043  C CA  . PRO A 1087 ? 0.2837 0.2789 0.2571 0.0262  0.0123  0.0366  1085 PRO A CA  
8044  C C   . PRO A 1087 ? 0.2653 0.2603 0.2357 0.0263  0.0133  0.0333  1085 PRO A C   
8045  O O   . PRO A 1087 ? 0.3142 0.3129 0.2804 0.0273  0.0136  0.0306  1085 PRO A O   
8046  C CB  . PRO A 1087 ? 0.3636 0.3660 0.3375 0.0268  0.0126  0.0422  1085 PRO A CB  
8047  C CG  . PRO A 1087 ? 0.3577 0.3627 0.3310 0.0275  0.0115  0.0430  1085 PRO A CG  
8048  C CD  . PRO A 1087 ? 0.2789 0.2811 0.2487 0.0279  0.0110  0.0370  1085 PRO A CD  
8049  N N   . GLY A 1088 ? 0.2918 0.2825 0.2648 0.0253  0.0138  0.0332  1086 GLY A N   
8050  C CA  . GLY A 1088 ? 0.3089 0.2989 0.2799 0.0252  0.0146  0.0304  1086 GLY A CA  
8051  C C   . GLY A 1088 ? 0.2429 0.2295 0.2175 0.0241  0.0152  0.0320  1086 GLY A C   
8052  O O   . GLY A 1088 ? 0.2663 0.2526 0.2451 0.0235  0.0150  0.0361  1086 GLY A O   
8053  N N   . PRO A 1089 ? 0.2873 0.2714 0.2608 0.0238  0.0156  0.0289  1087 PRO A N   
8054  C CA  . PRO A 1089 ? 0.2757 0.2569 0.2524 0.0227  0.0161  0.0301  1087 PRO A CA  
8055  C C   . PRO A 1089 ? 0.2888 0.2641 0.2693 0.0215  0.0152  0.0297  1087 PRO A C   
8056  O O   . PRO A 1089 ? 0.2865 0.2592 0.2664 0.0214  0.0144  0.0273  1087 PRO A O   
8057  C CB  . PRO A 1089 ? 0.3073 0.2874 0.2813 0.0229  0.0165  0.0262  1087 PRO A CB  
8058  C CG  . PRO A 1089 ? 0.3153 0.2943 0.2861 0.0233  0.0157  0.0222  1087 PRO A CG  
8059  C CD  . PRO A 1089 ? 0.2873 0.2709 0.2570 0.0243  0.0155  0.0240  1087 PRO A CD  
8060  N N   . VAL A 1090 ? 0.2768 0.2503 0.2614 0.0206  0.0154  0.0319  1088 VAL A N   
8061  C CA  . VAL A 1090 ? 0.2248 0.1928 0.2131 0.0196  0.0145  0.0307  1088 VAL A CA  
8062  C C   . VAL A 1090 ? 0.2485 0.2132 0.2343 0.0191  0.0145  0.0259  1088 VAL A C   
8063  O O   . VAL A 1090 ? 0.2639 0.2296 0.2462 0.0194  0.0151  0.0241  1088 VAL A O   
8064  C CB  . VAL A 1090 ? 0.2661 0.2329 0.2597 0.0187  0.0145  0.0336  1088 VAL A CB  
8065  C CG1 . VAL A 1090 ? 0.2804 0.2508 0.2773 0.0189  0.0144  0.0389  1088 VAL A CG1 
8066  C CG2 . VAL A 1090 ? 0.2662 0.2335 0.2585 0.0184  0.0155  0.0330  1088 VAL A CG2 
8067  N N   . GLY A 1091 ? 0.2481 0.2090 0.2360 0.0184  0.0136  0.0239  1089 GLY A N   
8068  C CA  . GLY A 1091 ? 0.2622 0.2204 0.2482 0.0177  0.0135  0.0200  1089 GLY A CA  
8069  C C   . GLY A 1091 ? 0.2462 0.2051 0.2280 0.0182  0.0133  0.0175  1089 GLY A C   
8070  O O   . GLY A 1091 ? 0.2457 0.2031 0.2255 0.0176  0.0132  0.0148  1089 GLY A O   
8071  N N   . GLU A 1092 ? 0.2505 0.2118 0.2310 0.0191  0.0131  0.0185  1090 GLU A N   
8072  C CA  . GLU A 1092 ? 0.2570 0.2191 0.2340 0.0195  0.0128  0.0160  1090 GLU A CA  
8073  C C   . GLU A 1092 ? 0.2405 0.2039 0.2182 0.0201  0.0122  0.0171  1090 GLU A C   
8074  O O   . GLU A 1092 ? 0.2660 0.2312 0.2459 0.0205  0.0122  0.0204  1090 GLU A O   
8075  C CB  . GLU A 1092 ? 0.3022 0.2673 0.2758 0.0204  0.0133  0.0158  1090 GLU A CB  
8076  C CG  . GLU A 1092 ? 0.3574 0.3223 0.3279 0.0205  0.0128  0.0124  1090 GLU A CG  
8077  C CD  . GLU A 1092 ? 0.3788 0.3466 0.3469 0.0216  0.0132  0.0118  1090 GLU A CD  
8078  O OE1 . GLU A 1092 ? 0.3202 0.2924 0.2869 0.0228  0.0134  0.0128  1090 GLU A OE1 
8079  O OE2 . GLU A 1092 ? 0.4036 0.3700 0.3715 0.0212  0.0133  0.0103  1090 GLU A OE2 
8080  N N   . ARG A 1093 ? 0.2249 0.1875 0.2011 0.0199  0.0115  0.0146  1091 ARG A N   
8081  C CA  A ARG A 1093 ? 0.2498 0.2141 0.2262 0.0206  0.0109  0.0152  1091 ARG A CA  
8082  C CA  B ARG A 1093 ? 0.2500 0.2142 0.2264 0.0206  0.0109  0.0151  1091 ARG A CA  
8083  C C   . ARG A 1093 ? 0.2223 0.1887 0.1946 0.0212  0.0106  0.0133  1091 ARG A C   
8084  O O   . ARG A 1093 ? 0.2527 0.2176 0.2234 0.0206  0.0104  0.0104  1091 ARG A O   
8085  C CB  A ARG A 1093 ? 0.2962 0.2582 0.2753 0.0200  0.0101  0.0137  1091 ARG A CB  
8086  C CB  B ARG A 1093 ? 0.2970 0.2587 0.2759 0.0199  0.0102  0.0135  1091 ARG A CB  
8087  C CG  A ARG A 1093 ? 0.3245 0.2848 0.3084 0.0198  0.0100  0.0155  1091 ARG A CG  
8088  C CG  B ARG A 1093 ? 0.3149 0.2781 0.2952 0.0206  0.0094  0.0144  1091 ARG A CG  
8089  C CD  A ARG A 1093 ? 0.4149 0.3739 0.4018 0.0196  0.0091  0.0138  1091 ARG A CD  
8090  C CD  B ARG A 1093 ? 0.3554 0.3165 0.3385 0.0201  0.0088  0.0123  1091 ARG A CD  
8091  N NE  A ARG A 1093 ? 0.3944 0.3554 0.3818 0.0205  0.0084  0.0149  1091 ARG A NE  
8092  N NE  B ARG A 1093 ? 0.4121 0.3709 0.3988 0.0194  0.0089  0.0121  1091 ARG A NE  
8093  C CZ  A ARG A 1093 ? 0.4233 0.3848 0.4091 0.0206  0.0079  0.0128  1091 ARG A CZ  
8094  C CZ  B ARG A 1093 ? 0.4156 0.3727 0.4021 0.0184  0.0090  0.0094  1091 ARG A CZ  
8095  N NH1 A ARG A 1093 ? 0.4182 0.3789 0.4022 0.0198  0.0081  0.0095  1091 ARG A NH1 
8096  N NH1 B ARG A 1093 ? 0.4425 0.4000 0.4259 0.0178  0.0090  0.0069  1091 ARG A NH1 
8097  N NH2 A ARG A 1093 ? 0.4242 0.3877 0.4106 0.0216  0.0073  0.0141  1091 ARG A NH2 
8098  N NH2 B ARG A 1093 ? 0.4593 0.4148 0.4493 0.0180  0.0090  0.0092  1091 ARG A NH2 
8099  N N   . ASN A 1094 ? 0.2428 0.2131 0.2139 0.0224  0.0106  0.0151  1092 ASN A N   
8100  C CA  . ASN A 1094 ? 0.2213 0.1943 0.1888 0.0232  0.0103  0.0131  1092 ASN A CA  
8101  C C   . ASN A 1094 ? 0.2298 0.2046 0.1972 0.0238  0.0095  0.0135  1092 ASN A C   
8102  O O   . ASN A 1094 ? 0.2504 0.2278 0.2191 0.0245  0.0094  0.0167  1092 ASN A O   
8103  C CB  . ASN A 1094 ? 0.2194 0.1964 0.1849 0.0243  0.0110  0.0144  1092 ASN A CB  
8104  C CG  . ASN A 1094 ? 0.2210 0.1962 0.1863 0.0238  0.0117  0.0130  1092 ASN A CG  
8105  O OD1 . ASN A 1094 ? 0.2405 0.2140 0.2044 0.0235  0.0112  0.0098  1092 ASN A OD1 
8106  N ND2 . ASN A 1094 ? 0.2725 0.2480 0.2395 0.0236  0.0125  0.0157  1092 ASN A ND2 
8107  N N   . LEU A 1095 ? 0.2375 0.2111 0.2039 0.0234  0.0087  0.0104  1093 LEU A N   
8108  C CA  . LEU A 1095 ? 0.2217 0.1961 0.1886 0.0237  0.0078  0.0103  1093 LEU A CA  
8109  C C   . LEU A 1095 ? 0.2495 0.2270 0.2133 0.0245  0.0072  0.0083  1093 LEU A C   
8110  O O   . LEU A 1095 ? 0.2391 0.2164 0.2010 0.0244  0.0071  0.0058  1093 LEU A O   
8111  C CB  . LEU A 1095 ? 0.2618 0.2326 0.2305 0.0225  0.0074  0.0083  1093 LEU A CB  
8112  C CG  . LEU A 1095 ? 0.3049 0.2729 0.2769 0.0217  0.0080  0.0095  1093 LEU A CG  
8113  C CD1 . LEU A 1095 ? 0.3802 0.3459 0.3538 0.0206  0.0076  0.0072  1093 LEU A CD1 
8114  C CD2 . LEU A 1095 ? 0.3423 0.3113 0.3172 0.0224  0.0080  0.0130  1093 LEU A CD2 
8115  N N   . TYR A 1096 ? 0.2393 0.2197 0.2029 0.0253  0.0065  0.0093  1094 TYR A N   
8116  C CA  . TYR A 1096 ? 0.2346 0.2186 0.1955 0.0263  0.0057  0.0074  1094 TYR A CA  
8117  C C   . TYR A 1096 ? 0.2126 0.1967 0.1746 0.0262  0.0047  0.0071  1094 TYR A C   
8118  O O   . TYR A 1096 ? 0.2367 0.2215 0.2006 0.0265  0.0046  0.0100  1094 TYR A O   
8119  C CB  . TYR A 1096 ? 0.2312 0.2208 0.1904 0.0277  0.0061  0.0098  1094 TYR A CB  
8120  C CG  . TYR A 1096 ? 0.2279 0.2224 0.1843 0.0290  0.0051  0.0080  1094 TYR A CG  
8121  C CD1 . TYR A 1096 ? 0.2438 0.2398 0.1977 0.0296  0.0048  0.0044  1094 TYR A CD1 
8122  C CD2 . TYR A 1096 ? 0.2321 0.2299 0.1886 0.0297  0.0044  0.0098  1094 TYR A CD2 
8123  C CE1 . TYR A 1096 ? 0.2246 0.2256 0.1763 0.0308  0.0038  0.0023  1094 TYR A CE1 
8124  C CE2 . TYR A 1096 ? 0.2605 0.2633 0.2144 0.0309  0.0035  0.0081  1094 TYR A CE2 
8125  C CZ  . TYR A 1096 ? 0.2456 0.2500 0.1971 0.0315  0.0032  0.0041  1094 TYR A CZ  
8126  O OH  . TYR A 1096 ? 0.2459 0.2557 0.1951 0.0328  0.0021  0.0019  1094 TYR A OH  
8127  N N   . THR A 1097 ? 0.2178 0.2012 0.1789 0.0258  0.0038  0.0038  1095 THR A N   
8128  C CA  . THR A 1097 ? 0.2232 0.2064 0.1856 0.0255  0.0029  0.0032  1095 THR A CA  
8129  C C   . THR A 1097 ? 0.2523 0.2381 0.2127 0.0260  0.0017  0.0005  1095 THR A C   
8130  O O   . THR A 1097 ? 0.2366 0.2227 0.1953 0.0261  0.0015  -0.0019 1095 THR A O   
8131  C CB  . THR A 1097 ? 0.2880 0.2668 0.2526 0.0239  0.0030  0.0018  1095 THR A CB  
8132  O OG1 . THR A 1097 ? 0.3356 0.3127 0.2991 0.0229  0.0029  -0.0008 1095 THR A OG1 
8133  C CG2 . THR A 1097 ? 0.2751 0.2515 0.2420 0.0234  0.0040  0.0039  1095 THR A CG2 
8134  N N   . LEU A 1098 ? 0.2364 0.2242 0.1974 0.0264  0.0009  0.0008  1096 LEU A N   
8135  C CA  . LEU A 1098 ? 0.2460 0.2363 0.2055 0.0268  -0.0005 -0.0019 1096 LEU A CA  
8136  C C   . LEU A 1098 ? 0.2047 0.1925 0.1662 0.0255  -0.0012 -0.0037 1096 LEU A C   
8137  O O   . LEU A 1098 ? 0.2229 0.2102 0.1866 0.0253  -0.0011 -0.0023 1096 LEU A O   
8138  C CB  . LEU A 1098 ? 0.2124 0.2081 0.1708 0.0285  -0.0011 -0.0003 1096 LEU A CB  
8139  C CG  . LEU A 1098 ? 0.2168 0.2164 0.1729 0.0298  -0.0004 0.0016  1096 LEU A CG  
8140  C CD1 . LEU A 1098 ? 0.2429 0.2484 0.1978 0.0312  -0.0012 0.0034  1096 LEU A CD1 
8141  C CD2 . LEU A 1098 ? 0.2315 0.2318 0.1854 0.0301  -0.0005 -0.0018 1096 LEU A CD2 
8142  N N   . HIS A 1099 ? 0.2118 0.1986 0.1732 0.0247  -0.0020 -0.0068 1097 HIS A N   
8143  C CA  . HIS A 1099 ? 0.2138 0.1987 0.1771 0.0232  -0.0027 -0.0084 1097 HIS A CA  
8144  C C   . HIS A 1099 ? 0.2280 0.2155 0.1909 0.0235  -0.0044 -0.0109 1097 HIS A C   
8145  O O   . HIS A 1099 ? 0.2288 0.2192 0.1897 0.0249  -0.0051 -0.0119 1097 HIS A O   
8146  C CB  . HIS A 1099 ? 0.2479 0.2291 0.2121 0.0215  -0.0024 -0.0094 1097 HIS A CB  
8147  C CG  . HIS A 1099 ? 0.2735 0.2522 0.2383 0.0210  -0.0009 -0.0074 1097 HIS A CG  
8148  N ND1 . HIS A 1099 ? 0.3520 0.3289 0.3188 0.0197  -0.0003 -0.0068 1097 HIS A ND1 
8149  C CD2 . HIS A 1099 ? 0.3097 0.2878 0.2734 0.0217  0.0002  -0.0060 1097 HIS A CD2 
8150  C CE1 . HIS A 1099 ? 0.3324 0.3076 0.2995 0.0196  0.0009  -0.0053 1097 HIS A CE1 
8151  N NE2 . HIS A 1099 ? 0.3324 0.3081 0.2977 0.0208  0.0012  -0.0047 1097 HIS A NE2 
8152  N N   . ALA A 1100 ? 0.2252 0.2118 0.1901 0.0221  -0.0052 -0.0121 1098 ALA A N   
8153  C CA  . ALA A 1100 ? 0.2343 0.2226 0.1995 0.0221  -0.0071 -0.0148 1098 ALA A CA  
8154  C C   . ALA A 1100 ? 0.2469 0.2336 0.2121 0.0217  -0.0078 -0.0171 1098 ALA A C   
8155  O O   . ALA A 1100 ? 0.2620 0.2455 0.2276 0.0208  -0.0070 -0.0166 1098 ALA A O   
8156  C CB  . ALA A 1100 ? 0.2442 0.2319 0.2121 0.0204  -0.0076 -0.0152 1098 ALA A CB  
8157  N N   . ARG A 1101 ? 0.2424 0.2315 0.2072 0.0226  -0.0095 -0.0199 1099 ARG A N   
8158  C CA  A ARG A 1101 ? 0.2629 0.2505 0.2287 0.0223  -0.0107 -0.0228 1099 ARG A CA  
8159  C CA  B ARG A 1101 ? 0.2630 0.2506 0.2289 0.0223  -0.0107 -0.0228 1099 ARG A CA  
8160  C C   . ARG A 1101 ? 0.2567 0.2410 0.2262 0.0199  -0.0118 -0.0236 1099 ARG A C   
8161  O O   . ARG A 1101 ? 0.2772 0.2585 0.2484 0.0189  -0.0122 -0.0242 1099 ARG A O   
8162  C CB  A ARG A 1101 ? 0.2716 0.2632 0.2364 0.0242  -0.0124 -0.0260 1099 ARG A CB  
8163  C CB  B ARG A 1101 ? 0.2716 0.2633 0.2364 0.0242  -0.0124 -0.0260 1099 ARG A CB  
8164  C CG  A ARG A 1101 ? 0.2844 0.2802 0.2454 0.0265  -0.0114 -0.0252 1099 ARG A CG  
8165  C CG  B ARG A 1101 ? 0.2866 0.2820 0.2478 0.0265  -0.0114 -0.0255 1099 ARG A CG  
8166  C CD  A ARG A 1101 ? 0.2713 0.2719 0.2313 0.0284  -0.0131 -0.0290 1099 ARG A CD  
8167  C CD  B ARG A 1101 ? 0.3065 0.3034 0.2675 0.0277  -0.0126 -0.0295 1099 ARG A CD  
8168  N NE  A ARG A 1101 ? 0.2507 0.2502 0.2118 0.0287  -0.0141 -0.0325 1099 ARG A NE  
8169  N NE  B ARG A 1101 ? 0.2882 0.2888 0.2460 0.0297  -0.0113 -0.0288 1099 ARG A NE  
8170  C CZ  A ARG A 1101 ? 0.2853 0.2861 0.2445 0.0300  -0.0130 -0.0328 1099 ARG A CZ  
8171  C CZ  B ARG A 1101 ? 0.2972 0.3003 0.2543 0.0312  -0.0121 -0.0322 1099 ARG A CZ  
8172  N NH1 A ARG A 1101 ? 0.3003 0.3035 0.2564 0.0310  -0.0110 -0.0293 1099 ARG A NH1 
8173  N NH1 B ARG A 1101 ? 0.2923 0.2943 0.2522 0.0311  -0.0142 -0.0367 1099 ARG A NH1 
8174  N NH2 A ARG A 1101 ? 0.3096 0.3093 0.2705 0.0304  -0.0142 -0.0364 1099 ARG A NH2 
8175  N NH2 B ARG A 1101 ? 0.2593 0.2665 0.2134 0.0329  -0.0107 -0.0310 1099 ARG A NH2 
8176  N N   . GLY A 1102 ? 0.2638 0.2490 0.2349 0.0189  -0.0125 -0.0232 1100 GLY A N   
8177  C CA  . GLY A 1102 ? 0.2758 0.2588 0.2507 0.0165  -0.0137 -0.0236 1100 GLY A CA  
8178  C C   . GLY A 1102 ? 0.2325 0.2180 0.2092 0.0163  -0.0155 -0.0254 1100 GLY A C   
8179  O O   . GLY A 1102 ? 0.2677 0.2559 0.2432 0.0170  -0.0151 -0.0245 1100 GLY A O   
8180  N N   . ARG A 1103 ? 0.2460 0.2306 0.2260 0.0154  -0.0178 -0.0278 1101 ARG A N   
8181  C CA  . ARG A 1103 ? 0.2393 0.2261 0.2215 0.0151  -0.0199 -0.0296 1101 ARG A CA  
8182  C C   . ARG A 1103 ? 0.2415 0.2308 0.2226 0.0174  -0.0215 -0.0334 1101 ARG A C   
8183  O O   . ARG A 1103 ? 0.2612 0.2490 0.2434 0.0179  -0.0226 -0.0358 1101 ARG A O   
8184  C CB  . ARG A 1103 ? 0.2725 0.2572 0.2600 0.0123  -0.0216 -0.0297 1101 ARG A CB  
8185  C CG  . ARG A 1103 ? 0.3013 0.2886 0.2913 0.0118  -0.0235 -0.0311 1101 ARG A CG  
8186  C CD  . ARG A 1103 ? 0.3368 0.3227 0.3322 0.0086  -0.0248 -0.0299 1101 ARG A CD  
8187  N NE  . ARG A 1103 ? 0.3965 0.3820 0.3916 0.0068  -0.0227 -0.0261 1101 ARG A NE  
8188  C CZ  . ARG A 1103 ? 0.4520 0.4401 0.4472 0.0060  -0.0217 -0.0243 1101 ARG A CZ  
8189  N NH1 . ARG A 1103 ? 0.3485 0.3398 0.3439 0.0068  -0.0226 -0.0256 1101 ARG A NH1 
8190  N NH2 . ARG A 1103 ? 0.4558 0.4439 0.4509 0.0044  -0.0198 -0.0213 1101 ARG A NH2 
8191  N N   . ILE A 1104 ? 0.2203 0.2137 0.1993 0.0190  -0.0217 -0.0340 1102 ILE A N   
8192  C CA  . ILE A 1104 ? 0.2158 0.2130 0.1932 0.0213  -0.0232 -0.0375 1102 ILE A CA  
8193  C C   . ILE A 1104 ? 0.2341 0.2325 0.2154 0.0206  -0.0261 -0.0406 1102 ILE A C   
8194  O O   . ILE A 1104 ? 0.2462 0.2452 0.2291 0.0193  -0.0263 -0.0392 1102 ILE A O   
8195  C CB  . ILE A 1104 ? 0.2309 0.2327 0.2038 0.0234  -0.0218 -0.0359 1102 ILE A CB  
8196  C CG1 . ILE A 1104 ? 0.2458 0.2463 0.2157 0.0238  -0.0190 -0.0322 1102 ILE A CG1 
8197  C CG2 . ILE A 1104 ? 0.2412 0.2479 0.2120 0.0259  -0.0233 -0.0395 1102 ILE A CG2 
8198  C CD1 . ILE A 1104 ? 0.2571 0.2564 0.2256 0.0247  -0.0185 -0.0333 1102 ILE A CD1 
8199  N N   . LEU A 1105 ? 0.2329 0.2315 0.2160 0.0214  -0.0283 -0.0449 1103 LEU A N   
8200  C CA  . LEU A 1105 ? 0.2394 0.2397 0.2263 0.0212  -0.0314 -0.0485 1103 LEU A CA  
8201  C C   . LEU A 1105 ? 0.2371 0.2436 0.2206 0.0234  -0.0317 -0.0499 1103 LEU A C   
8202  O O   . LEU A 1105 ? 0.2432 0.2534 0.2227 0.0260  -0.0312 -0.0514 1103 LEU A O   
8203  C CB  . LEU A 1105 ? 0.2611 0.2598 0.2515 0.0216  -0.0339 -0.0531 1103 LEU A CB  
8204  C CG  . LEU A 1105 ? 0.2556 0.2562 0.2505 0.0217  -0.0375 -0.0578 1103 LEU A CG  
8205  C CD1 . LEU A 1105 ? 0.2898 0.2874 0.2902 0.0185  -0.0388 -0.0559 1103 LEU A CD1 
8206  C CD2 . LEU A 1105 ? 0.2705 0.2700 0.2685 0.0229  -0.0398 -0.0629 1103 LEU A CD2 
8207  N N   . LEU A 1106 ? 0.2093 0.2174 0.1943 0.0226  -0.0326 -0.0493 1104 LEU A N   
8208  C CA  . LEU A 1106 ? 0.2236 0.2378 0.2060 0.0245  -0.0333 -0.0506 1104 LEU A CA  
8209  C C   . LEU A 1106 ? 0.2884 0.3044 0.2749 0.0246  -0.0369 -0.0557 1104 LEU A C   
8210  O O   . LEU A 1106 ? 0.2613 0.2745 0.2530 0.0222  -0.0384 -0.0559 1104 LEU A O   
8211  C CB  . LEU A 1106 ? 0.2388 0.2541 0.2203 0.0238  -0.0320 -0.0467 1104 LEU A CB  
8212  C CG  . LEU A 1106 ? 0.3378 0.3515 0.3162 0.0236  -0.0287 -0.0417 1104 LEU A CG  
8213  C CD1 . LEU A 1106 ? 0.2727 0.2895 0.2500 0.0240  -0.0280 -0.0390 1104 LEU A CD1 
8214  C CD2 . LEU A 1106 ? 0.3055 0.3201 0.2795 0.0256  -0.0271 -0.0412 1104 LEU A CD2 
8215  N N   . VAL A 1107 ? 0.2380 0.2591 0.2222 0.0272  -0.0382 -0.0596 1105 VAL A N   
8216  C CA  . VAL A 1107 ? 0.2493 0.2730 0.2372 0.0276  -0.0417 -0.0651 1105 VAL A CA  
8217  C C   . VAL A 1107 ? 0.2447 0.2756 0.2288 0.0296  -0.0420 -0.0655 1105 VAL A C   
8218  O O   . VAL A 1107 ? 0.2427 0.2794 0.2231 0.0323  -0.0423 -0.0682 1105 VAL A O   
8219  C CB  . VAL A 1107 ? 0.2469 0.2705 0.2363 0.0290  -0.0435 -0.0705 1105 VAL A CB  
8220  C CG1 . VAL A 1107 ? 0.2744 0.2996 0.2692 0.0291  -0.0476 -0.0764 1105 VAL A CG1 
8221  C CG2 . VAL A 1107 ? 0.2692 0.2856 0.2616 0.0272  -0.0426 -0.0688 1105 VAL A CG2 
8222  N N   . PRO A 1108 ? 0.2225 0.2540 0.2074 0.0284  -0.0419 -0.0628 1106 PRO A N   
8223  C CA  . PRO A 1108 ? 0.2293 0.2676 0.2108 0.0302  -0.0422 -0.0627 1106 PRO A CA  
8224  C C   . PRO A 1108 ? 0.2708 0.3129 0.2555 0.0308  -0.0459 -0.0683 1106 PRO A C   
8225  O O   . PRO A 1108 ? 0.2877 0.3264 0.2782 0.0293  -0.0483 -0.0717 1106 PRO A O   
8226  C CB  . PRO A 1108 ? 0.2593 0.2957 0.2414 0.0285  -0.0407 -0.0575 1106 PRO A CB  
8227  C CG  . PRO A 1108 ? 0.2548 0.2849 0.2428 0.0254  -0.0413 -0.0574 1106 PRO A CG  
8228  C CD  . PRO A 1108 ? 0.2620 0.2883 0.2507 0.0254  -0.0412 -0.0592 1106 PRO A CD  
8229  N N   . ALA A 1109 ? 0.2426 0.2919 0.2238 0.0329  -0.0465 -0.0691 1107 ALA A N   
8230  C CA  . ALA A 1109 ? 0.2512 0.3053 0.2348 0.0336  -0.0499 -0.0740 1107 ALA A CA  
8231  C C   . ALA A 1109 ? 0.2981 0.3554 0.2813 0.0333  -0.0500 -0.0712 1107 ALA A C   
8232  O O   . ALA A 1109 ? 0.3121 0.3707 0.2995 0.0326  -0.0527 -0.0741 1107 ALA A O   
8233  C CB  . ALA A 1109 ? 0.2761 0.3379 0.2560 0.0369  -0.0511 -0.0787 1107 ALA A CB  
8234  N N   . THR A 1110 ? 0.2610 0.3197 0.2399 0.0339  -0.0473 -0.0657 1108 THR A N   
8235  C CA  . THR A 1110 ? 0.2689 0.3310 0.2473 0.0339  -0.0474 -0.0629 1108 THR A CA  
8236  C C   . THR A 1110 ? 0.2467 0.3039 0.2253 0.0323  -0.0445 -0.0567 1108 THR A C   
8237  O O   . THR A 1110 ? 0.2518 0.3046 0.2291 0.0318  -0.0421 -0.0542 1108 THR A O   
8238  C CB  . THR A 1110 ? 0.2809 0.3516 0.2538 0.0368  -0.0474 -0.0623 1108 THR A CB  
8239  O OG1 . THR A 1110 ? 0.2685 0.3391 0.2367 0.0379  -0.0445 -0.0582 1108 THR A OG1 
8240  C CG2 . THR A 1110 ? 0.2821 0.3589 0.2543 0.0388  -0.0502 -0.0688 1108 THR A CG2 
8241  N N   . GLU A 1111 ? 0.2808 0.3391 0.2611 0.0316  -0.0448 -0.0546 1109 GLU A N   
8242  C CA  . GLU A 1111 ? 0.2650 0.3196 0.2459 0.0303  -0.0422 -0.0493 1109 GLU A CA  
8243  C C   . GLU A 1111 ? 0.2886 0.3442 0.2646 0.0320  -0.0397 -0.0451 1109 GLU A C   
8244  O O   . GLU A 1111 ? 0.2656 0.3163 0.2414 0.0310  -0.0373 -0.0421 1109 GLU A O   
8245  C CB  . GLU A 1111 ? 0.2851 0.3420 0.2687 0.0297  -0.0432 -0.0481 1109 GLU A CB  
8246  C CG  . GLU A 1111 ? 0.2944 0.3490 0.2783 0.0290  -0.0407 -0.0430 1109 GLU A CG  
8247  C CD  . GLU A 1111 ? 0.3264 0.3831 0.3137 0.0283  -0.0417 -0.0423 1109 GLU A CD  
8248  O OE1 . GLU A 1111 ? 0.3757 0.4304 0.3676 0.0261  -0.0427 -0.0440 1109 GLU A OE1 
8249  O OE2 . GLU A 1111 ? 0.3707 0.4314 0.3565 0.0299  -0.0416 -0.0399 1109 GLU A OE2 
8250  N N   . SER A 1112 ? 0.2754 0.3376 0.2476 0.0344  -0.0403 -0.0448 1110 SER A N   
8251  C CA  . SER A 1112 ? 0.2532 0.3168 0.2212 0.0359  -0.0381 -0.0404 1110 SER A CA  
8252  C C   . SER A 1112 ? 0.2737 0.3343 0.2395 0.0360  -0.0366 -0.0410 1110 SER A C   
8253  O O   . SER A 1112 ? 0.2671 0.3246 0.2317 0.0358  -0.0342 -0.0371 1110 SER A O   
8254  C CB  . SER A 1112 ? 0.2994 0.3716 0.2638 0.0384  -0.0392 -0.0398 1110 SER A CB  
8255  O OG  . SER A 1112 ? 0.3016 0.3751 0.2629 0.0395  -0.0371 -0.0348 1110 SER A OG  
8256  N N   . GLY A 1113 ? 0.2545 0.3160 0.2204 0.0363  -0.0382 -0.0462 1111 GLY A N   
8257  C CA  . GLY A 1113 ? 0.2224 0.2808 0.1869 0.0363  -0.0369 -0.0471 1111 GLY A CA  
8258  C C   . GLY A 1113 ? 0.2218 0.2717 0.1892 0.0339  -0.0352 -0.0452 1111 GLY A C   
8259  O O   . GLY A 1113 ? 0.2403 0.2873 0.2059 0.0339  -0.0329 -0.0426 1111 GLY A O   
8260  N N   . LEU A 1114 ? 0.2403 0.2866 0.2124 0.0318  -0.0362 -0.0462 1112 LEU A N   
8261  C CA  . LEU A 1114 ? 0.2475 0.2867 0.2224 0.0294  -0.0346 -0.0440 1112 LEU A CA  
8262  C C   . LEU A 1114 ? 0.2532 0.2912 0.2265 0.0294  -0.0319 -0.0386 1112 LEU A C   
8263  O O   . LEU A 1114 ? 0.2367 0.2701 0.2095 0.0286  -0.0299 -0.0366 1112 LEU A O   
8264  C CB  . LEU A 1114 ? 0.2547 0.2919 0.2350 0.0271  -0.0363 -0.0455 1112 LEU A CB  
8265  C CG  . LEU A 1114 ? 0.2631 0.2944 0.2463 0.0245  -0.0346 -0.0427 1112 LEU A CG  
8266  C CD1 . LEU A 1114 ? 0.2681 0.2946 0.2510 0.0238  -0.0335 -0.0430 1112 LEU A CD1 
8267  C CD2 . LEU A 1114 ? 0.2876 0.3181 0.2762 0.0222  -0.0363 -0.0439 1112 LEU A CD2 
8268  N N   . TYR A 1115 ? 0.2489 0.2906 0.2214 0.0304  -0.0320 -0.0364 1113 TYR A N   
8269  C CA  . TYR A 1115 ? 0.2401 0.2806 0.2120 0.0305  -0.0298 -0.0315 1113 TYR A CA  
8270  C C   . TYR A 1115 ? 0.2362 0.2768 0.2042 0.0319  -0.0280 -0.0292 1113 TYR A C   
8271  O O   . TYR A 1115 ? 0.2493 0.2860 0.2174 0.0313  -0.0259 -0.0262 1113 TYR A O   
8272  C CB  . TYR A 1115 ? 0.2206 0.2655 0.1930 0.0315  -0.0306 -0.0297 1113 TYR A CB  
8273  C CG  . TYR A 1115 ? 0.2253 0.2699 0.2019 0.0300  -0.0319 -0.0312 1113 TYR A CG  
8274  C CD1 . TYR A 1115 ? 0.2265 0.2666 0.2065 0.0276  -0.0318 -0.0328 1113 TYR A CD1 
8275  C CD2 . TYR A 1115 ? 0.2605 0.3099 0.2380 0.0310  -0.0333 -0.0308 1113 TYR A CD2 
8276  C CE1 . TYR A 1115 ? 0.2786 0.3192 0.2628 0.0261  -0.0330 -0.0338 1113 TYR A CE1 
8277  C CE2 . TYR A 1115 ? 0.2722 0.3217 0.2536 0.0296  -0.0345 -0.0320 1113 TYR A CE2 
8278  C CZ  . TYR A 1115 ? 0.2970 0.3422 0.2818 0.0271  -0.0343 -0.0335 1113 TYR A CZ  
8279  O OH  . TYR A 1115 ? 0.2942 0.3402 0.2832 0.0256  -0.0355 -0.0345 1113 TYR A OH  
8280  N N   . HIS A 1116 ? 0.2444 0.2901 0.2091 0.0338  -0.0289 -0.0307 1114 HIS A N   
8281  C CA  . HIS A 1116 ? 0.2694 0.3160 0.2304 0.0351  -0.0273 -0.0286 1114 HIS A CA  
8282  C C   . HIS A 1116 ? 0.2346 0.2757 0.1959 0.0340  -0.0261 -0.0299 1114 HIS A C   
8283  O O   . HIS A 1116 ? 0.2325 0.2711 0.1926 0.0340  -0.0240 -0.0268 1114 HIS A O   
8284  C CB  . HIS A 1116 ? 0.2716 0.3259 0.2290 0.0374  -0.0286 -0.0303 1114 HIS A CB  
8285  C CG  . HIS A 1116 ? 0.2734 0.3339 0.2294 0.0388  -0.0291 -0.0269 1114 HIS A CG  
8286  N ND1 . HIS A 1116 ? 0.3111 0.3752 0.2685 0.0391  -0.0311 -0.0281 1114 HIS A ND1 
8287  C CD2 . HIS A 1116 ? 0.3069 0.3706 0.2606 0.0401  -0.0279 -0.0219 1114 HIS A CD2 
8288  C CE1 . HIS A 1116 ? 0.3145 0.3838 0.2704 0.0405  -0.0311 -0.0241 1114 HIS A CE1 
8289  N NE2 . HIS A 1116 ? 0.3556 0.4247 0.3094 0.0411  -0.0293 -0.0202 1114 HIS A NE2 
8290  N N   . GLN A 1117 ? 0.2205 0.2596 0.1838 0.0330  -0.0275 -0.0344 1115 GLN A N   
8291  C CA  . GLN A 1117 ? 0.2143 0.2481 0.1784 0.0318  -0.0266 -0.0355 1115 GLN A CA  
8292  C C   . GLN A 1117 ? 0.2120 0.2397 0.1783 0.0299  -0.0247 -0.0322 1115 GLN A C   
8293  O O   . GLN A 1117 ? 0.2233 0.2476 0.1886 0.0295  -0.0229 -0.0305 1115 GLN A O   
8294  C CB  . GLN A 1117 ? 0.2369 0.2694 0.2040 0.0310  -0.0289 -0.0408 1115 GLN A CB  
8295  C CG  . GLN A 1117 ? 0.2552 0.2933 0.2204 0.0331  -0.0308 -0.0451 1115 GLN A CG  
8296  C CD  . GLN A 1117 ? 0.2737 0.3099 0.2430 0.0321  -0.0334 -0.0504 1115 GLN A CD  
8297  O OE1 . GLN A 1117 ? 0.2533 0.2846 0.2269 0.0298  -0.0339 -0.0503 1115 GLN A OE1 
8298  N NE2 . GLN A 1117 ? 0.2468 0.2871 0.2151 0.0339  -0.0351 -0.0551 1115 GLN A NE2 
8299  N N   . LEU A 1118 ? 0.2114 0.2381 0.1807 0.0285  -0.0252 -0.0316 1116 LEU A N   
8300  C CA  A LEU A 1118 ? 0.2201 0.2422 0.1916 0.0267  -0.0235 -0.0288 1116 LEU A CA  
8301  C CA  B LEU A 1118 ? 0.2202 0.2423 0.1917 0.0267  -0.0235 -0.0288 1116 LEU A CA  
8302  C C   . LEU A 1118 ? 0.2246 0.2466 0.1941 0.0277  -0.0214 -0.0247 1116 LEU A C   
8303  O O   . LEU A 1118 ? 0.2258 0.2438 0.1957 0.0268  -0.0196 -0.0228 1116 LEU A O   
8304  C CB  A LEU A 1118 ? 0.2155 0.2379 0.1907 0.0253  -0.0245 -0.0292 1116 LEU A CB  
8305  C CB  B LEU A 1118 ? 0.2159 0.2386 0.1909 0.0254  -0.0245 -0.0290 1116 LEU A CB  
8306  C CG  A LEU A 1118 ? 0.2257 0.2442 0.2039 0.0231  -0.0232 -0.0274 1116 LEU A CG  
8307  C CG  B LEU A 1118 ? 0.2311 0.2520 0.2097 0.0234  -0.0262 -0.0320 1116 LEU A CG  
8308  C CD1 A LEU A 1118 ? 0.2367 0.2506 0.2155 0.0215  -0.0226 -0.0281 1116 LEU A CD1 
8309  C CD1 B LEU A 1118 ? 0.2293 0.2525 0.2109 0.0226  -0.0273 -0.0320 1116 LEU A CD1 
8310  C CD2 A LEU A 1118 ? 0.2329 0.2528 0.2147 0.0217  -0.0246 -0.0286 1116 LEU A CD2 
8311  C CD2 B LEU A 1118 ? 0.2350 0.2507 0.2154 0.0213  -0.0248 -0.0310 1116 LEU A CD2 
8312  N N   . ALA A 1119 ? 0.2455 0.2721 0.2132 0.0296  -0.0217 -0.0230 1117 ALA A N   
8313  C CA  . ALA A 1119 ? 0.2576 0.2843 0.2242 0.0306  -0.0200 -0.0188 1117 ALA A CA  
8314  C C   . ALA A 1119 ? 0.2558 0.2808 0.2199 0.0310  -0.0186 -0.0179 1117 ALA A C   
8315  O O   . ALA A 1119 ? 0.2459 0.2674 0.2106 0.0305  -0.0168 -0.0153 1117 ALA A O   
8316  C CB  . ALA A 1119 ? 0.2705 0.3030 0.2359 0.0325  -0.0210 -0.0169 1117 ALA A CB  
8317  N N   . ALA A 1120 ? 0.2276 0.2553 0.1891 0.0319  -0.0194 -0.0204 1118 ALA A N   
8318  C CA  . ALA A 1120 ? 0.2177 0.2444 0.1768 0.0324  -0.0180 -0.0198 1118 ALA A CA  
8319  C C   . ALA A 1120 ? 0.2273 0.2474 0.1882 0.0305  -0.0169 -0.0204 1118 ALA A C   
8320  O O   . ALA A 1120 ? 0.2302 0.2477 0.1905 0.0304  -0.0151 -0.0179 1118 ALA A O   
8321  C CB  . ALA A 1120 ? 0.2208 0.2521 0.1773 0.0338  -0.0193 -0.0233 1118 ALA A CB  
8322  N N   . ALA A 1121 ? 0.2245 0.2421 0.1879 0.0290  -0.0180 -0.0235 1119 ALA A N   
8323  C CA  . ALA A 1121 ? 0.2151 0.2270 0.1804 0.0271  -0.0172 -0.0239 1119 ALA A CA  
8324  C C   . ALA A 1121 ? 0.2051 0.2139 0.1721 0.0259  -0.0155 -0.0207 1119 ALA A C   
8325  O O   . ALA A 1121 ? 0.2182 0.2233 0.1851 0.0251  -0.0140 -0.0194 1119 ALA A O   
8326  C CB  . ALA A 1121 ? 0.2444 0.2550 0.2126 0.0256  -0.0191 -0.0275 1119 ALA A CB  
8327  N N   . LEU A 1122 ? 0.2094 0.2196 0.1781 0.0257  -0.0159 -0.0198 1120 LEU A N   
8328  C CA  . LEU A 1122 ? 0.2035 0.2113 0.1743 0.0247  -0.0144 -0.0174 1120 LEU A CA  
8329  C C   . LEU A 1122 ? 0.2240 0.2316 0.1934 0.0260  -0.0129 -0.0141 1120 LEU A C   
8330  O O   . LEU A 1122 ? 0.2189 0.2233 0.1894 0.0252  -0.0114 -0.0127 1120 LEU A O   
8331  C CB  . LEU A 1122 ? 0.2438 0.2538 0.2170 0.0245  -0.0153 -0.0174 1120 LEU A CB  
8332  C CG  . LEU A 1122 ? 0.2142 0.2243 0.1897 0.0228  -0.0168 -0.0201 1120 LEU A CG  
8333  C CD1 . LEU A 1122 ? 0.2603 0.2734 0.2382 0.0228  -0.0176 -0.0199 1120 LEU A CD1 
8334  C CD2 . LEU A 1122 ? 0.2463 0.2525 0.2237 0.0205  -0.0160 -0.0204 1120 LEU A CD2 
8335  N N   . ALA A 1123 ? 0.2213 0.2326 0.1886 0.0279  -0.0133 -0.0128 1121 ALA A N   
8336  C CA  . ALA A 1123 ? 0.1952 0.2066 0.1618 0.0290  -0.0121 -0.0092 1121 ALA A CA  
8337  C C   . ALA A 1123 ? 0.2187 0.2270 0.1839 0.0287  -0.0106 -0.0087 1121 ALA A C   
8338  O O   . ALA A 1123 ? 0.2343 0.2411 0.2001 0.0289  -0.0094 -0.0059 1121 ALA A O   
8339  C CB  . ALA A 1123 ? 0.2133 0.2302 0.1776 0.0310  -0.0129 -0.0077 1121 ALA A CB  
8340  N N   . THR A 1124 ? 0.1977 0.2050 0.1615 0.0281  -0.0109 -0.0116 1122 THR A N   
8341  C CA  . THR A 1124 ? 0.2040 0.2085 0.1667 0.0277  -0.0097 -0.0115 1122 THR A CA  
8342  C C   . THR A 1124 ? 0.2078 0.2074 0.1726 0.0256  -0.0091 -0.0127 1122 THR A C   
8343  O O   . THR A 1124 ? 0.2204 0.2174 0.1845 0.0250  -0.0085 -0.0133 1122 THR A O   
8344  C CB  . THR A 1124 ? 0.2280 0.2352 0.1879 0.0288  -0.0104 -0.0137 1122 THR A CB  
8345  O OG1 . THR A 1124 ? 0.2302 0.2388 0.1908 0.0285  -0.0123 -0.0173 1122 THR A OG1 
8346  C CG2 . THR A 1124 ? 0.2347 0.2473 0.1920 0.0308  -0.0103 -0.0115 1122 THR A CG2 
8347  N N   . GLY A 1125 ? 0.2029 0.2017 0.1704 0.0244  -0.0094 -0.0128 1123 GLY A N   
8348  C CA  . GLY A 1125 ? 0.2228 0.2180 0.1924 0.0224  -0.0087 -0.0131 1123 GLY A CA  
8349  C C   . GLY A 1125 ? 0.2124 0.2064 0.1830 0.0208  -0.0098 -0.0157 1123 GLY A C   
8350  O O   . GLY A 1125 ? 0.2311 0.2225 0.2034 0.0190  -0.0092 -0.0156 1123 GLY A O   
8351  N N   . ASN A 1126 ? 0.2213 0.2173 0.1913 0.0214  -0.0114 -0.0179 1124 ASN A N   
8352  C CA  . ASN A 1126 ? 0.2226 0.2171 0.1942 0.0200  -0.0128 -0.0205 1124 ASN A CA  
8353  C C   . ASN A 1126 ? 0.2164 0.2116 0.1910 0.0184  -0.0140 -0.0212 1124 ASN A C   
8354  O O   . ASN A 1126 ? 0.2373 0.2352 0.2123 0.0189  -0.0141 -0.0206 1124 ASN A O   
8355  C CB  . ASN A 1126 ? 0.2252 0.2218 0.1952 0.0215  -0.0143 -0.0231 1124 ASN A CB  
8356  C CG  . ASN A 1126 ? 0.2398 0.2364 0.2069 0.0230  -0.0132 -0.0226 1124 ASN A CG  
8357  O OD1 . ASN A 1126 ? 0.2416 0.2351 0.2089 0.0223  -0.0125 -0.0225 1124 ASN A OD1 
8358  N ND2 . ASN A 1126 ? 0.2224 0.2230 0.1868 0.0251  -0.0131 -0.0219 1124 ASN A ND2 
8359  N N   . SER A 1127 ? 0.2446 0.2378 0.2218 0.0164  -0.0149 -0.0224 1125 SER A N   
8360  C CA  . SER A 1127 ? 0.2357 0.2300 0.2161 0.0150  -0.0167 -0.0236 1125 SER A CA  
8361  C C   . SER A 1127 ? 0.2395 0.2350 0.2203 0.0159  -0.0190 -0.0269 1125 SER A C   
8362  O O   . SER A 1127 ? 0.2378 0.2332 0.2163 0.0175  -0.0191 -0.0283 1125 SER A O   
8363  C CB  . SER A 1127 ? 0.2491 0.2410 0.2328 0.0122  -0.0167 -0.0227 1125 SER A CB  
8364  O OG  . SER A 1127 ? 0.3274 0.3162 0.3115 0.0117  -0.0172 -0.0235 1125 SER A OG  
8365  N N   . VAL A 1128 ? 0.2564 0.2535 0.2402 0.0149  -0.0209 -0.0284 1126 VAL A N   
8366  C CA  . VAL A 1128 ? 0.2482 0.2468 0.2328 0.0159  -0.0234 -0.0319 1126 VAL A CA  
8367  C C   . VAL A 1128 ? 0.2736 0.2708 0.2635 0.0135  -0.0257 -0.0333 1126 VAL A C   
8368  O O   . VAL A 1128 ? 0.2792 0.2762 0.2719 0.0113  -0.0254 -0.0313 1126 VAL A O   
8369  C CB  . VAL A 1128 ? 0.2446 0.2479 0.2273 0.0179  -0.0241 -0.0328 1126 VAL A CB  
8370  C CG1 . VAL A 1128 ? 0.2903 0.2952 0.2683 0.0201  -0.0221 -0.0309 1126 VAL A CG1 
8371  C CG2 . VAL A 1128 ? 0.2832 0.2881 0.2684 0.0165  -0.0243 -0.0316 1126 VAL A CG2 
8372  N N   . ALA A 1129 ? 0.2365 0.2332 0.2281 0.0140  -0.0280 -0.0368 1127 ALA A N   
8373  C CA  . ALA A 1129 ? 0.2482 0.2444 0.2455 0.0122  -0.0309 -0.0388 1127 ALA A CA  
8374  C C   . ALA A 1129 ? 0.2323 0.2323 0.2292 0.0143  -0.0330 -0.0428 1127 ALA A C   
8375  O O   . ALA A 1129 ? 0.2680 0.2690 0.2625 0.0166  -0.0335 -0.0457 1127 ALA A O   
8376  C CB  . ALA A 1129 ? 0.3041 0.2961 0.3051 0.0110  -0.0322 -0.0399 1127 ALA A CB  
8377  N N   . ILE A 1130 ? 0.2540 0.2565 0.2530 0.0135  -0.0342 -0.0430 1128 ILE A N   
8378  C CA  . ILE A 1130 ? 0.2422 0.2490 0.2407 0.0154  -0.0362 -0.0465 1128 ILE A CA  
8379  C C   . ILE A 1130 ? 0.2952 0.3010 0.2997 0.0143  -0.0398 -0.0503 1128 ILE A C   
8380  O O   . ILE A 1130 ? 0.2939 0.2975 0.3038 0.0115  -0.0408 -0.0490 1128 ILE A O   
8381  C CB  . ILE A 1130 ? 0.2272 0.2378 0.2245 0.0155  -0.0356 -0.0447 1128 ILE A CB  
8382  C CG1 . ILE A 1130 ? 0.2786 0.2894 0.2714 0.0163  -0.0322 -0.0407 1128 ILE A CG1 
8383  C CG2 . ILE A 1130 ? 0.2443 0.2599 0.2401 0.0179  -0.0375 -0.0482 1128 ILE A CG2 
8384  C CD1 . ILE A 1130 ? 0.2516 0.2653 0.2447 0.0160  -0.0316 -0.0386 1128 ILE A CD1 
8385  N N   . ASP A 1131 ? 0.2589 0.2668 0.2630 0.0165  -0.0418 -0.0551 1129 ASP A N   
8386  C CA  . ASP A 1131 ? 0.2611 0.2684 0.2713 0.0159  -0.0456 -0.0596 1129 ASP A CA  
8387  C C   . ASP A 1131 ? 0.2665 0.2756 0.2807 0.0141  -0.0474 -0.0593 1129 ASP A C   
8388  O O   . ASP A 1131 ? 0.2716 0.2855 0.2832 0.0156  -0.0474 -0.0600 1129 ASP A O   
8389  C CB  . ASP A 1131 ? 0.2646 0.2758 0.2726 0.0191  -0.0473 -0.0651 1129 ASP A CB  
8390  C CG  . ASP A 1131 ? 0.3381 0.3489 0.3529 0.0188  -0.0515 -0.0705 1129 ASP A CG  
8391  O OD1 . ASP A 1131 ? 0.2994 0.3054 0.3208 0.0161  -0.0530 -0.0698 1129 ASP A OD1 
8392  O OD2 . ASP A 1131 ? 0.3022 0.3178 0.3159 0.0212  -0.0534 -0.0754 1129 ASP A OD2 
8393  N N   . ALA A 1132 ? 0.2911 0.2968 0.3121 0.0110  -0.0488 -0.0580 1130 ALA A N   
8394  C CA  . ALA A 1132 ? 0.3256 0.3331 0.3512 0.0091  -0.0505 -0.0576 1130 ALA A CA  
8395  C C   . ALA A 1132 ? 0.3648 0.3752 0.3935 0.0104  -0.0543 -0.0633 1130 ALA A C   
8396  O O   . ALA A 1132 ? 0.3386 0.3523 0.3690 0.0099  -0.0554 -0.0635 1130 ALA A O   
8397  C CB  . ALA A 1132 ? 0.3295 0.3331 0.3619 0.0052  -0.0513 -0.0544 1130 ALA A CB  
8398  N N   . ALA A 1133 ? 0.3146 0.3243 0.3442 0.0122  -0.0562 -0.0682 1131 ALA A N   
8399  C CA  . ALA A 1133 ? 0.3552 0.3681 0.3876 0.0137  -0.0599 -0.0743 1131 ALA A CA  
8400  C C   . ALA A 1133 ? 0.3433 0.3629 0.3690 0.0167  -0.0591 -0.0759 1131 ALA A C   
8401  O O   . ALA A 1133 ? 0.3481 0.3716 0.3756 0.0180  -0.0620 -0.0808 1131 ALA A O   
8402  C CB  . ALA A 1133 ? 0.3468 0.3575 0.3823 0.0150  -0.0623 -0.0796 1131 ALA A CB  
8403  N N   . SER A 1134 ? 0.3428 0.3640 0.3612 0.0178  -0.0553 -0.0718 1132 SER A N   
8404  C CA  . SER A 1134 ? 0.3170 0.3446 0.3295 0.0204  -0.0545 -0.0723 1132 SER A CA  
8405  C C   . SER A 1134 ? 0.3097 0.3401 0.3247 0.0192  -0.0556 -0.0713 1132 SER A C   
8406  O O   . SER A 1134 ? 0.3301 0.3663 0.3419 0.0212  -0.0562 -0.0729 1132 SER A O   
8407  C CB  . SER A 1134 ? 0.3080 0.3360 0.3134 0.0214  -0.0504 -0.0674 1132 SER A CB  
8408  O OG  . SER A 1134 ? 0.2981 0.3230 0.3044 0.0189  -0.0483 -0.0620 1132 SER A OG  
8409  N N   . GLY A 1135 ? 0.3506 0.3774 0.3710 0.0159  -0.0558 -0.0685 1133 GLY A N   
8410  C CA  . GLY A 1135 ? 0.3375 0.3669 0.3604 0.0145  -0.0566 -0.0672 1133 GLY A CA  
8411  C C   . GLY A 1135 ? 0.3524 0.3849 0.3697 0.0155  -0.0536 -0.0630 1133 GLY A C   
8412  O O   . GLY A 1135 ? 0.3746 0.4107 0.3931 0.0152  -0.0543 -0.0626 1133 GLY A O   
8413  N N   . LEU A 1136 ? 0.2841 0.3153 0.2960 0.0165  -0.0503 -0.0598 1134 LEU A N   
8414  C CA  . LEU A 1136 ? 0.3023 0.3364 0.3092 0.0178  -0.0476 -0.0561 1134 LEU A CA  
8415  C C   . LEU A 1136 ? 0.3089 0.3404 0.3171 0.0155  -0.0452 -0.0512 1134 LEU A C   
8416  O O   . LEU A 1136 ? 0.3113 0.3440 0.3157 0.0165  -0.0427 -0.0480 1134 LEU A O   
8417  C CB  . LEU A 1136 ? 0.2816 0.3168 0.2818 0.0206  -0.0457 -0.0557 1134 LEU A CB  
8418  C CG  . LEU A 1136 ? 0.3004 0.3405 0.2978 0.0234  -0.0477 -0.0602 1134 LEU A CG  
8419  C CD1 . LEU A 1136 ? 0.2718 0.3128 0.2631 0.0257  -0.0455 -0.0592 1134 LEU A CD1 
8420  C CD2 . LEU A 1136 ? 0.3315 0.3776 0.3283 0.0245  -0.0490 -0.0607 1134 LEU A CD2 
8421  N N   . GLN A 1137 ? 0.3168 0.3451 0.3307 0.0124  -0.0459 -0.0506 1135 GLN A N   
8422  C CA  . GLN A 1137 ? 0.3669 0.3938 0.3823 0.0101  -0.0436 -0.0461 1135 GLN A CA  
8423  C C   . GLN A 1137 ? 0.3388 0.3698 0.3530 0.0107  -0.0425 -0.0441 1135 GLN A C   
8424  O O   . GLN A 1137 ? 0.3387 0.3695 0.3508 0.0107  -0.0397 -0.0407 1135 GLN A O   
8425  C CB  . GLN A 1137 ? 0.3412 0.3658 0.3637 0.0066  -0.0453 -0.0458 1135 GLN A CB  
8426  C CG  . GLN A 1137 ? 0.3187 0.3382 0.3431 0.0054  -0.0458 -0.0462 1135 GLN A CG  
8427  C CD  . GLN A 1137 ? 0.3030 0.3219 0.3295 0.0066  -0.0491 -0.0513 1135 GLN A CD  
8428  O OE1 . GLN A 1137 ? 0.3501 0.3726 0.3753 0.0086  -0.0508 -0.0547 1135 GLN A OE1 
8429  N NE2 . GLN A 1137 ? 0.3759 0.3904 0.4058 0.0053  -0.0503 -0.0520 1135 GLN A NE2 
8430  N N   . ALA A 1138 ? 0.3467 0.3817 0.3626 0.0113  -0.0448 -0.0463 1136 ALA A N   
8431  C CA  . ALA A 1138 ? 0.3208 0.3599 0.3363 0.0119  -0.0440 -0.0445 1136 ALA A CA  
8432  C C   . ALA A 1138 ? 0.3833 0.4241 0.3927 0.0148  -0.0420 -0.0430 1136 ALA A C   
8433  O O   . ALA A 1138 ? 0.4249 0.4684 0.4341 0.0154  -0.0409 -0.0409 1136 ALA A O   
8434  C CB  . ALA A 1138 ? 0.3368 0.3799 0.3556 0.0119  -0.0472 -0.0474 1136 ALA A CB  
8435  N N   . SER A 1139 ? 0.3373 0.3767 0.3423 0.0167  -0.0414 -0.0438 1137 SER A N   
8436  C CA  . SER A 1139 ? 0.3268 0.3678 0.3265 0.0193  -0.0395 -0.0417 1137 SER A CA  
8437  C C   . SER A 1139 ? 0.3166 0.3544 0.3152 0.0188  -0.0364 -0.0379 1137 SER A C   
8438  O O   . SER A 1139 ? 0.3574 0.3963 0.3527 0.0206  -0.0348 -0.0357 1137 SER A O   
8439  C CB  . SER A 1139 ? 0.3306 0.3722 0.3261 0.0215  -0.0401 -0.0438 1137 SER A CB  
8440  O OG  . SER A 1139 ? 0.3663 0.4122 0.3621 0.0227  -0.0430 -0.0475 1137 SER A OG  
8441  N N   . LEU A 1140 ? 0.3160 0.3501 0.3174 0.0162  -0.0355 -0.0371 1138 LEU A N   
8442  C CA  . LEU A 1140 ? 0.3206 0.3519 0.3209 0.0156  -0.0326 -0.0340 1138 LEU A CA  
8443  C C   . LEU A 1140 ? 0.3603 0.3922 0.3647 0.0133  -0.0318 -0.0323 1138 LEU A C   
8444  O O   . LEU A 1140 ? 0.4154 0.4447 0.4207 0.0115  -0.0303 -0.0307 1138 LEU A O   
8445  C CB  . LEU A 1140 ? 0.3256 0.3524 0.3246 0.0150  -0.0319 -0.0342 1138 LEU A CB  
8446  C CG  . LEU A 1140 ? 0.4004 0.4264 0.3945 0.0174  -0.0314 -0.0347 1138 LEU A CG  
8447  C CD1 . LEU A 1140 ? 0.3948 0.4161 0.3884 0.0164  -0.0301 -0.0342 1138 LEU A CD1 
8448  C CD2 . LEU A 1140 ? 0.3246 0.3526 0.3154 0.0196  -0.0297 -0.0322 1138 LEU A CD2 
8449  N N   . LYS A 1141 ? 0.3510 0.3869 0.3578 0.0133  -0.0329 -0.0326 1139 LYS A N   
8450  C CA  . LYS A 1141 ? 0.4060 0.4436 0.4167 0.0112  -0.0321 -0.0311 1139 LYS A CA  
8451  C C   . LYS A 1141 ? 0.3684 0.4066 0.3777 0.0123  -0.0294 -0.0288 1139 LYS A C   
8452  O O   . LYS A 1141 ? 0.3591 0.3979 0.3656 0.0149  -0.0289 -0.0283 1139 LYS A O   
8453  C CB  . LYS A 1141 ? 0.4559 0.4980 0.4700 0.0110  -0.0342 -0.0324 1139 LYS A CB  
8454  N N   . ASN A 1142 ? 0.3736 0.4117 0.3852 0.0102  -0.0278 -0.0273 1140 ASN A N   
8455  C CA  . ASN A 1142 ? 0.3950 0.4345 0.4065 0.0110  -0.0255 -0.0257 1140 ASN A CA  
8456  C C   . ASN A 1142 ? 0.3718 0.4079 0.3793 0.0129  -0.0237 -0.0247 1140 ASN A C   
8457  O O   . ASN A 1142 ? 0.3256 0.3627 0.3325 0.0148  -0.0226 -0.0239 1140 ASN A O   
8458  C CB  . ASN A 1142 ? 0.4462 0.4902 0.4595 0.0125  -0.0260 -0.0260 1140 ASN A CB  
8459  C CG  . ASN A 1142 ? 0.5511 0.5988 0.5684 0.0107  -0.0279 -0.0270 1140 ASN A CG  
8460  O OD1 . ASN A 1142 ? 0.5839 0.6334 0.6014 0.0119  -0.0300 -0.0283 1140 ASN A OD1 
8461  N ND2 . ASN A 1142 ? 0.4973 0.5465 0.5180 0.0079  -0.0274 -0.0263 1140 ASN A ND2 
8462  N N   . LEU A 1143 ? 0.3893 0.4214 0.3945 0.0123  -0.0236 -0.0247 1141 LEU A N   
8463  C CA  . LEU A 1143 ? 0.3375 0.3664 0.3392 0.0139  -0.0219 -0.0236 1141 LEU A CA  
8464  C C   . LEU A 1143 ? 0.3613 0.3905 0.3641 0.0133  -0.0196 -0.0222 1141 LEU A C   
8465  O O   . LEU A 1143 ? 0.3547 0.3855 0.3602 0.0111  -0.0191 -0.0220 1141 LEU A O   
8466  C CB  . LEU A 1143 ? 0.3177 0.3425 0.3173 0.0131  -0.0220 -0.0240 1141 LEU A CB  
8467  C CG  . LEU A 1143 ? 0.3723 0.3962 0.3695 0.0145  -0.0238 -0.0256 1141 LEU A CG  
8468  C CD1 . LEU A 1143 ? 0.3404 0.3604 0.3366 0.0134  -0.0238 -0.0261 1141 LEU A CD1 
8469  C CD2 . LEU A 1143 ? 0.3185 0.3432 0.3123 0.0174  -0.0233 -0.0248 1141 LEU A CD2 
8470  N N   . PRO A 1144 ? 0.3291 0.3571 0.3301 0.0154  -0.0182 -0.0213 1142 PRO A N   
8471  C CA  . PRO A 1144 ? 0.3248 0.3525 0.3266 0.0150  -0.0161 -0.0204 1142 PRO A CA  
8472  C C   . PRO A 1144 ? 0.3350 0.3599 0.3359 0.0127  -0.0153 -0.0201 1142 PRO A C   
8473  O O   . PRO A 1144 ? 0.2997 0.3215 0.2985 0.0124  -0.0161 -0.0202 1142 PRO A O   
8474  C CB  . PRO A 1144 ? 0.3812 0.4066 0.3808 0.0175  -0.0154 -0.0195 1142 PRO A CB  
8475  C CG  . PRO A 1144 ? 0.3987 0.4252 0.3973 0.0194  -0.0171 -0.0195 1142 PRO A CG  
8476  C CD  . PRO A 1144 ? 0.3565 0.3836 0.3547 0.0180  -0.0187 -0.0208 1142 PRO A CD  
8477  N N   . GLN A 1145 ? 0.3291 0.3558 0.3319 0.0111  -0.0139 -0.0197 1143 GLN A N   
8478  C CA  . GLN A 1145 ? 0.3305 0.3553 0.3328 0.0089  -0.0132 -0.0189 1143 GLN A CA  
8479  C C   . GLN A 1145 ? 0.3027 0.3225 0.3015 0.0099  -0.0125 -0.0184 1143 GLN A C   
8480  O O   . GLN A 1145 ? 0.3107 0.3277 0.3086 0.0084  -0.0128 -0.0180 1143 GLN A O   
8481  C CB  . GLN A 1145 ? 0.4015 0.4298 0.4059 0.0074  -0.0115 -0.0185 1143 GLN A CB  
8482  N N   . THR A 1146 ? 0.3245 0.3431 0.3218 0.0123  -0.0116 -0.0182 1144 THR A N   
8483  C CA  . THR A 1146 ? 0.3522 0.3664 0.3464 0.0132  -0.0109 -0.0175 1144 THR A CA  
8484  C C   . THR A 1146 ? 0.2867 0.2986 0.2787 0.0135  -0.0124 -0.0179 1144 THR A C   
8485  O O   . THR A 1146 ? 0.3075 0.3161 0.2975 0.0130  -0.0122 -0.0176 1144 THR A O   
8486  C CB  . THR A 1146 ? 0.3520 0.3657 0.3457 0.0157  -0.0101 -0.0170 1144 THR A CB  
8487  O OG1 . THR A 1146 ? 0.3436 0.3595 0.3381 0.0174  -0.0114 -0.0172 1144 THR A OG1 
8488  C CG2 . THR A 1146 ? 0.3080 0.3233 0.3039 0.0155  -0.0086 -0.0172 1144 THR A CG2 
8489  N N   . VAL A 1147 ? 0.2876 0.3015 0.2799 0.0145  -0.0140 -0.0187 1145 VAL A N   
8490  C CA  . VAL A 1147 ? 0.2791 0.2917 0.2694 0.0150  -0.0156 -0.0196 1145 VAL A CA  
8491  C C   . VAL A 1147 ? 0.2735 0.2856 0.2657 0.0126  -0.0168 -0.0207 1145 VAL A C   
8492  O O   . VAL A 1147 ? 0.2741 0.2835 0.2651 0.0122  -0.0175 -0.0214 1145 VAL A O   
8493  C CB  . VAL A 1147 ? 0.2503 0.2658 0.2402 0.0170  -0.0170 -0.0202 1145 VAL A CB  
8494  C CG1 . VAL A 1147 ? 0.2469 0.2618 0.2345 0.0178  -0.0185 -0.0215 1145 VAL A CG1 
8495  C CG2 . VAL A 1147 ? 0.2777 0.2938 0.2669 0.0192  -0.0160 -0.0186 1145 VAL A CG2 
8496  N N   . GLY A 1148 ? 0.2753 0.2901 0.2708 0.0107  -0.0172 -0.0207 1146 GLY A N   
8497  C CA  . GLY A 1148 ? 0.2734 0.2878 0.2716 0.0081  -0.0185 -0.0211 1146 GLY A CA  
8498  C C   . GLY A 1148 ? 0.2977 0.3087 0.2955 0.0066  -0.0177 -0.0201 1146 GLY A C   
8499  O O   . GLY A 1148 ? 0.2963 0.3051 0.2952 0.0054  -0.0192 -0.0207 1146 GLY A O   
8500  N N   . LEU A 1149 ? 0.2726 0.2829 0.2689 0.0068  -0.0154 -0.0187 1147 LEU A N   
8501  C CA  . LEU A 1149 ? 0.3006 0.3078 0.2962 0.0055  -0.0146 -0.0176 1147 LEU A CA  
8502  C C   . LEU A 1149 ? 0.2836 0.2868 0.2768 0.0067  -0.0154 -0.0186 1147 LEU A C   
8503  O O   . LEU A 1149 ? 0.3430 0.3434 0.3368 0.0053  -0.0157 -0.0182 1147 LEU A O   
8504  C CB  . LEU A 1149 ? 0.3132 0.3206 0.3074 0.0059  -0.0122 -0.0164 1147 LEU A CB  
8505  C CG  . LEU A 1149 ? 0.4192 0.4309 0.4161 0.0042  -0.0112 -0.0155 1147 LEU A CG  
8506  C CD1 . LEU A 1149 ? 0.4526 0.4646 0.4480 0.0052  -0.0090 -0.0151 1147 LEU A CD1 
8507  C CD2 . LEU A 1149 ? 0.3871 0.3992 0.3863 0.0010  -0.0117 -0.0142 1147 LEU A CD2 
8508  N N   . ARG A 1150 ? 0.2656 0.2688 0.2563 0.0093  -0.0157 -0.0197 1148 ARG A N   
8509  C CA  . ARG A 1150 ? 0.2634 0.2639 0.2516 0.0107  -0.0163 -0.0208 1148 ARG A CA  
8510  C C   . ARG A 1150 ? 0.2749 0.2759 0.2644 0.0107  -0.0189 -0.0232 1148 ARG A C   
8511  O O   . ARG A 1150 ? 0.2761 0.2754 0.2639 0.0118  -0.0196 -0.0246 1148 ARG A O   
8512  C CB  . ARG A 1150 ? 0.2750 0.2762 0.2598 0.0135  -0.0153 -0.0204 1148 ARG A CB  
8513  C CG  . ARG A 1150 ? 0.3139 0.3138 0.2975 0.0138  -0.0130 -0.0184 1148 ARG A CG  
8514  C CD  . ARG A 1150 ? 0.3036 0.3016 0.2840 0.0156  -0.0124 -0.0180 1148 ARG A CD  
8515  N NE  . ARG A 1150 ? 0.2958 0.2929 0.2754 0.0163  -0.0105 -0.0162 1148 ARG A NE  
8516  C CZ  . ARG A 1150 ? 0.2976 0.2948 0.2752 0.0184  -0.0099 -0.0151 1148 ARG A CZ  
8517  N NH1 . ARG A 1150 ? 0.2538 0.2525 0.2294 0.0200  -0.0109 -0.0156 1148 ARG A NH1 
8518  N NH2 . ARG A 1150 ? 0.2479 0.2443 0.2258 0.0189  -0.0084 -0.0134 1148 ARG A NH2 
8519  N N   . VAL A 1151 ? 0.2608 0.2641 0.2534 0.0095  -0.0203 -0.0238 1149 VAL A N   
8520  C CA  . VAL A 1151 ? 0.2483 0.2526 0.2425 0.0098  -0.0230 -0.0265 1149 VAL A CA  
8521  C C   . VAL A 1151 ? 0.3230 0.3261 0.3220 0.0069  -0.0246 -0.0267 1149 VAL A C   
8522  O O   . VAL A 1151 ? 0.3485 0.3530 0.3504 0.0047  -0.0243 -0.0249 1149 VAL A O   
8523  C CB  . VAL A 1151 ? 0.2735 0.2820 0.2678 0.0110  -0.0237 -0.0272 1149 VAL A CB  
8524  C CG1 . VAL A 1151 ? 0.3166 0.3265 0.3133 0.0109  -0.0267 -0.0301 1149 VAL A CG1 
8525  C CG2 . VAL A 1151 ? 0.2854 0.2952 0.2754 0.0139  -0.0225 -0.0267 1149 VAL A CG2 
8526  N N   . SER A 1152 ? 0.2783 0.2791 0.2786 0.0069  -0.0266 -0.0289 1150 SER A N   
8527  C CA  . SER A 1152 ? 0.3161 0.3158 0.3220 0.0044  -0.0290 -0.0295 1150 SER A CA  
8528  C C   . SER A 1152 ? 0.3113 0.3117 0.3186 0.0057  -0.0319 -0.0336 1150 SER A C   
8529  O O   . SER A 1152 ? 0.3011 0.3024 0.3045 0.0085  -0.0318 -0.0358 1150 SER A O   
8530  C CB  . SER A 1152 ? 0.3403 0.3359 0.3479 0.0028  -0.0289 -0.0283 1150 SER A CB  
8531  O OG  . SER A 1152 ? 0.3971 0.3902 0.4022 0.0048  -0.0291 -0.0304 1150 SER A OG  
8532  N N   . TRP A 1153 ? 0.2826 0.2831 0.2955 0.0037  -0.0345 -0.0345 1151 TRP A N   
8533  C CA  . TRP A 1153 ? 0.3187 0.3197 0.3341 0.0047  -0.0377 -0.0388 1151 TRP A CA  
8534  C C   . TRP A 1153 ? 0.3371 0.3340 0.3576 0.0032  -0.0400 -0.0401 1151 TRP A C   
8535  O O   . TRP A 1153 ? 0.3977 0.3926 0.4224 0.0002  -0.0401 -0.0371 1151 TRP A O   
8536  C CB  . TRP A 1153 ? 0.2936 0.2981 0.3126 0.0036  -0.0394 -0.0393 1151 TRP A CB  
8537  C CG  . TRP A 1153 ? 0.2985 0.3071 0.3131 0.0056  -0.0379 -0.0390 1151 TRP A CG  
8538  C CD1 . TRP A 1153 ? 0.3322 0.3427 0.3448 0.0051  -0.0353 -0.0356 1151 TRP A CD1 
8539  C CD2 . TRP A 1153 ? 0.2948 0.3066 0.3066 0.0084  -0.0390 -0.0422 1151 TRP A CD2 
8540  N NE1 . TRP A 1153 ? 0.3485 0.3626 0.3578 0.0075  -0.0348 -0.0364 1151 TRP A NE1 
8541  C CE2 . TRP A 1153 ? 0.3084 0.3235 0.3169 0.0094  -0.0370 -0.0401 1151 TRP A CE2 
8542  C CE3 . TRP A 1153 ? 0.2854 0.2979 0.2973 0.0102  -0.0415 -0.0467 1151 TRP A CE3 
8543  C CZ2 . TRP A 1153 ? 0.2929 0.3120 0.2983 0.0121  -0.0376 -0.0419 1151 TRP A CZ2 
8544  C CZ3 . TRP A 1153 ? 0.3271 0.3441 0.3355 0.0128  -0.0419 -0.0487 1151 TRP A CZ3 
8545  C CH2 . TRP A 1153 ? 0.3234 0.3436 0.3285 0.0137  -0.0400 -0.0461 1151 TRP A CH2 
8546  N N   . SER A 1154 ? 0.3051 0.3012 0.3254 0.0052  -0.0419 -0.0444 1152 SER A N   
8547  C CA  . SER A 1154 ? 0.3114 0.3034 0.3364 0.0044  -0.0440 -0.0461 1152 SER A CA  
8548  C C   . SER A 1154 ? 0.3348 0.3273 0.3651 0.0048  -0.0481 -0.0510 1152 SER A C   
8549  O O   . SER A 1154 ? 0.3304 0.3259 0.3578 0.0077  -0.0489 -0.0553 1152 SER A O   
8550  C CB  . SER A 1154 ? 0.3193 0.3095 0.3396 0.0067  -0.0425 -0.0472 1152 SER A CB  
8551  O OG  . SER A 1154 ? 0.3415 0.3278 0.3668 0.0061  -0.0447 -0.0491 1152 SER A OG  
8552  N N   . LYS A 1155 ? 0.3300 0.3201 0.3685 0.0019  -0.0508 -0.0505 1153 LYS A N   
8553  C CA  . LYS A 1155 ? 0.3849 0.3746 0.4299 0.0021  -0.0551 -0.0555 1153 LYS A CA  
8554  C C   . LYS A 1155 ? 0.4113 0.3968 0.4595 0.0028  -0.0570 -0.0584 1153 LYS A C   
8555  O O   . LYS A 1155 ? 0.5778 0.5636 0.6292 0.0046  -0.0601 -0.0643 1153 LYS A O   
8556  C CB  . LYS A 1155 ? 0.4256 0.4150 0.4787 -0.0015 -0.0575 -0.0535 1153 LYS A CB  
8557  N N   . ASP A 1156 ? 0.3551 0.3370 0.4028 0.0017  -0.0552 -0.0548 1154 ASP A N   
8558  C CA  . ASP A 1156 ? 0.3489 0.3267 0.3998 0.0023  -0.0568 -0.0570 1154 ASP A CA  
8559  C C   . ASP A 1156 ? 0.3510 0.3286 0.3937 0.0043  -0.0530 -0.0556 1154 ASP A C   
8560  O O   . ASP A 1156 ? 0.3622 0.3377 0.4035 0.0025  -0.0506 -0.0504 1154 ASP A O   
8561  C CB  . ASP A 1156 ? 0.4168 0.3901 0.4764 -0.0015 -0.0588 -0.0534 1154 ASP A CB  
8562  C CG  . ASP A 1156 ? 0.5304 0.4991 0.5942 -0.0009 -0.0607 -0.0555 1154 ASP A CG  
8563  O OD1 . ASP A 1156 ? 0.5633 0.5324 0.6230 0.0025  -0.0602 -0.0600 1154 ASP A OD1 
8564  O OD2 . ASP A 1156 ? 0.5587 0.5237 0.6303 -0.0039 -0.0628 -0.0526 1154 ASP A OD2 
8565  N N   . TRP A 1157 ? 0.3231 0.3033 0.3606 0.0079  -0.0524 -0.0600 1155 TRP A N   
8566  C CA  . TRP A 1157 ? 0.3061 0.2869 0.3356 0.0099  -0.0487 -0.0585 1155 TRP A CA  
8567  C C   . TRP A 1157 ? 0.3175 0.2935 0.3489 0.0089  -0.0483 -0.0565 1155 TRP A C   
8568  O O   . TRP A 1157 ? 0.3245 0.2997 0.3510 0.0087  -0.0450 -0.0526 1155 TRP A O   
8569  C CB  . TRP A 1157 ? 0.3225 0.3074 0.3472 0.0138  -0.0488 -0.0637 1155 TRP A CB  
8570  C CG  . TRP A 1157 ? 0.3047 0.2949 0.3270 0.0152  -0.0493 -0.0659 1155 TRP A CG  
8571  C CD1 . TRP A 1157 ? 0.2986 0.2904 0.3214 0.0135  -0.0491 -0.0632 1155 TRP A CD1 
8572  C CD2 . TRP A 1157 ? 0.2930 0.2883 0.3119 0.0186  -0.0501 -0.0712 1155 TRP A CD2 
8573  N NE1 . TRP A 1157 ? 0.2984 0.2956 0.3185 0.0156  -0.0499 -0.0665 1155 TRP A NE1 
8574  C CE2 . TRP A 1157 ? 0.3064 0.3060 0.3239 0.0188  -0.0505 -0.0713 1155 TRP A CE2 
8575  C CE3 . TRP A 1157 ? 0.2863 0.2835 0.3032 0.0216  -0.0506 -0.0758 1155 TRP A CE3 
8576  C CZ2 . TRP A 1157 ? 0.3007 0.3065 0.3148 0.0218  -0.0514 -0.0758 1155 TRP A CZ2 
8577  C CZ3 . TRP A 1157 ? 0.3050 0.3087 0.3185 0.0246  -0.0513 -0.0804 1155 TRP A CZ3 
8578  C CH2 . TRP A 1157 ? 0.3349 0.3428 0.3469 0.0247  -0.0518 -0.0802 1155 TRP A CH2 
8579  N N   . ALA A 1158 ? 0.3283 0.3010 0.3672 0.0084  -0.0517 -0.0595 1156 ALA A N   
8580  C CA  . ALA A 1158 ? 0.3680 0.3361 0.4092 0.0077  -0.0516 -0.0578 1156 ALA A CA  
8581  C C   . ALA A 1158 ? 0.3965 0.3619 0.4395 0.0040  -0.0502 -0.0508 1156 ALA A C   
8582  O O   . ALA A 1158 ? 0.4947 0.4575 0.5364 0.0035  -0.0486 -0.0480 1156 ALA A O   
8583  C CB  . ALA A 1158 ? 0.4281 0.3933 0.4781 0.0080  -0.0561 -0.0627 1156 ALA A CB  
8584  N N   . ALA A 1159 ? 0.3800 0.3466 0.4258 0.0014  -0.0508 -0.0480 1157 ALA A N   
8585  C CA  . ALA A 1159 ? 0.4000 0.3654 0.4473 -0.0022 -0.0494 -0.0414 1157 ALA A CA  
8586  C C   . ALA A 1159 ? 0.4372 0.4052 0.4760 -0.0018 -0.0448 -0.0377 1157 ALA A C   
8587  O O   . ALA A 1159 ? 0.4302 0.3973 0.4685 -0.0039 -0.0430 -0.0328 1157 ALA A O   
8588  C CB  . ALA A 1159 ? 0.4110 0.3774 0.4648 -0.0052 -0.0517 -0.0397 1157 ALA A CB  
8589  N N   . ASP A 1160 ? 0.4026 0.3741 0.4349 0.0009  -0.0431 -0.0400 1158 ASP A N   
8590  C CA  . ASP A 1160 ? 0.4037 0.3780 0.4291 0.0012  -0.0393 -0.0367 1158 ASP A CA  
8591  C C   . ASP A 1160 ? 0.3611 0.3352 0.3796 0.0037  -0.0364 -0.0370 1158 ASP A C   
8592  O O   . ASP A 1160 ? 0.3873 0.3635 0.4002 0.0043  -0.0334 -0.0347 1158 ASP A O   
8593  C CB  . ASP A 1160 ? 0.3610 0.3395 0.3845 0.0020  -0.0393 -0.0381 1158 ASP A CB  
8594  C CG  . ASP A 1160 ? 0.4039 0.3832 0.4341 -0.0008 -0.0417 -0.0371 1158 ASP A CG  
8595  O OD1 . ASP A 1160 ? 0.5172 0.4943 0.5523 -0.0039 -0.0424 -0.0337 1158 ASP A OD1 
8596  O OD2 . ASP A 1160 ? 0.4003 0.3825 0.4309 -0.0001 -0.0429 -0.0395 1158 ASP A OD2 
8597  N N   . GLY A 1161 ? 0.3464 0.3180 0.3655 0.0052  -0.0374 -0.0397 1159 GLY A N   
8598  C CA  . GLY A 1161 ? 0.3764 0.3479 0.3896 0.0074  -0.0348 -0.0397 1159 GLY A CA  
8599  C C   . GLY A 1161 ? 0.3771 0.3456 0.3902 0.0056  -0.0330 -0.0353 1159 GLY A C   
8600  O O   . GLY A 1161 ? 0.4104 0.3778 0.4270 0.0026  -0.0333 -0.0317 1159 GLY A O   
8601  N N   . PRO A 1162 ? 0.3540 0.3216 0.3631 0.0073  -0.0312 -0.0355 1160 PRO A N   
8602  C CA  . PRO A 1162 ? 0.3495 0.3190 0.3543 0.0108  -0.0306 -0.0391 1160 PRO A CA  
8603  C C   . PRO A 1162 ? 0.3428 0.3165 0.3416 0.0124  -0.0284 -0.0386 1160 PRO A C   
8604  O O   . PRO A 1162 ? 0.3441 0.3184 0.3405 0.0113  -0.0262 -0.0348 1160 PRO A O   
8605  C CB  . PRO A 1162 ? 0.3571 0.3241 0.3600 0.0112  -0.0289 -0.0377 1160 PRO A CB  
8606  C CG  . PRO A 1162 ? 0.3687 0.3342 0.3713 0.0085  -0.0270 -0.0324 1160 PRO A CG  
8607  C CD  . PRO A 1162 ? 0.3789 0.3440 0.3873 0.0058  -0.0293 -0.0314 1160 PRO A CD  
8608  N N   . PHE A 1163 ? 0.2902 0.2672 0.2868 0.0150  -0.0291 -0.0424 1161 PHE A N   
8609  C CA  . PHE A 1163 ? 0.2630 0.2442 0.2538 0.0168  -0.0270 -0.0416 1161 PHE A CA  
8610  C C   . PHE A 1163 ? 0.2805 0.2625 0.2664 0.0189  -0.0247 -0.0411 1161 PHE A C   
8611  O O   . PHE A 1163 ? 0.3251 0.3049 0.3119 0.0193  -0.0249 -0.0422 1161 PHE A O   
8612  C CB  . PHE A 1163 ? 0.2641 0.2494 0.2552 0.0184  -0.0292 -0.0456 1161 PHE A CB  
8613  C CG  . PHE A 1163 ? 0.2650 0.2495 0.2615 0.0162  -0.0316 -0.0461 1161 PHE A CG  
8614  C CD1 . PHE A 1163 ? 0.3037 0.2883 0.3004 0.0142  -0.0305 -0.0424 1161 PHE A CD1 
8615  C CD2 . PHE A 1163 ? 0.2762 0.2599 0.2781 0.0162  -0.0350 -0.0504 1161 PHE A CD2 
8616  C CE1 . PHE A 1163 ? 0.3288 0.3131 0.3306 0.0121  -0.0326 -0.0425 1161 PHE A CE1 
8617  C CE2 . PHE A 1163 ? 0.3189 0.3018 0.3263 0.0140  -0.0374 -0.0505 1161 PHE A CE2 
8618  C CZ  . PHE A 1163 ? 0.2934 0.2767 0.3007 0.0119  -0.0361 -0.0464 1161 PHE A CZ  
8619  N N   . ALA A 1164 ? 0.2413 0.2265 0.2223 0.0201  -0.0225 -0.0390 1162 ALA A N   
8620  C CA  . ALA A 1164 ? 0.2675 0.2540 0.2439 0.0220  -0.0203 -0.0380 1162 ALA A CA  
8621  C C   . ALA A 1164 ? 0.2562 0.2486 0.2290 0.0248  -0.0204 -0.0401 1162 ALA A C   
8622  O O   . ALA A 1164 ? 0.2778 0.2724 0.2466 0.0264  -0.0185 -0.0386 1162 ALA A O   
8623  C CB  . ALA A 1164 ? 0.3110 0.2960 0.2852 0.0210  -0.0175 -0.0331 1162 ALA A CB  
8624  N N   . GLY A 1165 ? 0.2419 0.2372 0.2161 0.0254  -0.0226 -0.0432 1163 GLY A N   
8625  C CA  . GLY A 1165 ? 0.2253 0.2270 0.1962 0.0280  -0.0230 -0.0455 1163 GLY A CA  
8626  C C   . GLY A 1165 ? 0.2250 0.2287 0.1983 0.0277  -0.0255 -0.0480 1163 GLY A C   
8627  O O   . GLY A 1165 ? 0.2335 0.2336 0.2108 0.0254  -0.0266 -0.0475 1163 GLY A O   
8628  N N   . ALA A 1166 ? 0.2294 0.2393 0.2002 0.0300  -0.0264 -0.0506 1164 ALA A N   
8629  C CA  . ALA A 1166 ? 0.2241 0.2366 0.1970 0.0299  -0.0288 -0.0531 1164 ALA A CA  
8630  C C   . ALA A 1166 ? 0.2374 0.2573 0.2057 0.0322  -0.0284 -0.0529 1164 ALA A C   
8631  O O   . ALA A 1166 ? 0.2655 0.2896 0.2297 0.0342  -0.0271 -0.0527 1164 ALA A O   
8632  C CB  . ALA A 1166 ? 0.2489 0.2611 0.2263 0.0303  -0.0320 -0.0592 1164 ALA A CB  
8633  N N   . LEU A 1167 ? 0.2242 0.2459 0.1934 0.0317  -0.0295 -0.0526 1165 LEU A N   
8634  C CA  . LEU A 1167 ? 0.2144 0.2434 0.1802 0.0336  -0.0298 -0.0527 1165 LEU A CA  
8635  C C   . LEU A 1167 ? 0.2485 0.2800 0.2174 0.0338  -0.0331 -0.0578 1165 LEU A C   
8636  O O   . LEU A 1167 ? 0.2475 0.2750 0.2209 0.0317  -0.0344 -0.0581 1165 LEU A O   
8637  C CB  . LEU A 1167 ? 0.2463 0.2752 0.2105 0.0329  -0.0280 -0.0473 1165 LEU A CB  
8638  C CG  . LEU A 1167 ? 0.2266 0.2529 0.1885 0.0326  -0.0250 -0.0422 1165 LEU A CG  
8639  C CD1 . LEU A 1167 ? 0.2823 0.3083 0.2440 0.0318  -0.0238 -0.0375 1165 LEU A CD1 
8640  C CD2 . LEU A 1167 ? 0.2594 0.2907 0.2168 0.0349  -0.0239 -0.0419 1165 LEU A CD2 
8641  N N   . VAL A 1168 ? 0.2325 0.2710 0.1991 0.0364  -0.0344 -0.0617 1166 VAL A N   
8642  C CA  . VAL A 1168 ? 0.2340 0.2754 0.2037 0.0369  -0.0378 -0.0676 1166 VAL A CA  
8643  C C   . VAL A 1168 ? 0.2584 0.3084 0.2243 0.0389  -0.0383 -0.0677 1166 VAL A C   
8644  O O   . VAL A 1168 ? 0.2421 0.2978 0.2028 0.0408  -0.0367 -0.0658 1166 VAL A O   
8645  C CB  . VAL A 1168 ? 0.2304 0.2727 0.2021 0.0383  -0.0396 -0.0738 1166 VAL A CB  
8646  C CG1 . VAL A 1168 ? 0.2720 0.3174 0.2476 0.0390  -0.0435 -0.0804 1166 VAL A CG1 
8647  C CG2 . VAL A 1168 ? 0.2453 0.2791 0.2209 0.0364  -0.0391 -0.0731 1166 VAL A CG2 
8648  N N   . GLU A 1169 ? 0.2268 0.2780 0.1956 0.0383  -0.0407 -0.0697 1167 GLU A N   
8649  C CA  . GLU A 1169 ? 0.2429 0.3026 0.2088 0.0401  -0.0418 -0.0706 1167 GLU A CA  
8650  C C   . GLU A 1169 ? 0.2722 0.3353 0.2414 0.0411  -0.0455 -0.0781 1167 GLU A C   
8651  O O   . GLU A 1169 ? 0.2750 0.3328 0.2502 0.0393  -0.0475 -0.0808 1167 GLU A O   
8652  C CB  . GLU A 1169 ? 0.2469 0.3054 0.2135 0.0386  -0.0413 -0.0661 1167 GLU A CB  
8653  C CG  . GLU A 1169 ? 0.2583 0.3254 0.2223 0.0404  -0.0426 -0.0666 1167 GLU A CG  
8654  C CD  . GLU A 1169 ? 0.2553 0.3209 0.2214 0.0388  -0.0428 -0.0633 1167 GLU A CD  
8655  O OE1 . GLU A 1169 ? 0.2480 0.3062 0.2179 0.0363  -0.0422 -0.0613 1167 GLU A OE1 
8656  O OE2 . GLU A 1169 ? 0.2644 0.3365 0.2283 0.0401  -0.0437 -0.0627 1167 GLU A OE2 
8657  N N   . GLY A 1170 ? 0.2426 0.3149 0.2081 0.0439  -0.0464 -0.0815 1168 GLY A N   
8658  C CA  . GLY A 1170 ? 0.2975 0.3740 0.2661 0.0451  -0.0501 -0.0891 1168 GLY A CA  
8659  C C   . GLY A 1170 ? 0.2751 0.3623 0.2390 0.0485  -0.0506 -0.0930 1168 GLY A C   
8660  O O   . GLY A 1170 ? 0.2933 0.3842 0.2517 0.0499  -0.0480 -0.0898 1168 GLY A O   
8661  N N   . ASP A 1171 ? 0.2849 0.3771 0.2512 0.0499  -0.0541 -0.1003 1169 ASP A N   
8662  C CA  . ASP A 1171 ? 0.2727 0.3755 0.2354 0.0532  -0.0549 -0.1056 1169 ASP A CA  
8663  C C   . ASP A 1171 ? 0.2888 0.3889 0.2533 0.0540  -0.0548 -0.1096 1169 ASP A C   
8664  O O   . ASP A 1171 ? 0.2917 0.3816 0.2605 0.0519  -0.0542 -0.1083 1169 ASP A O   
8665  C CB  . ASP A 1171 ? 0.3060 0.4161 0.2705 0.0547  -0.0587 -0.1122 1169 ASP A CB  
8666  C CG  . ASP A 1171 ? 0.4100 0.5137 0.3832 0.0534  -0.0624 -0.1187 1169 ASP A CG  
8667  O OD1 . ASP A 1171 ? 0.3256 0.4210 0.3034 0.0521  -0.0624 -0.1197 1169 ASP A OD1 
8668  O OD2 . ASP A 1171 ? 0.4525 0.5599 0.4284 0.0537  -0.0655 -0.1229 1169 ASP A OD2 
8669  N N   . ALA A 1172 ? 0.3100 0.4197 0.2712 0.0572  -0.0552 -0.1146 1170 ALA A N   
8670  C CA  . ALA A 1172 ? 0.3042 0.4129 0.2662 0.0583  -0.0546 -0.1179 1170 ALA A CA  
8671  C C   . ALA A 1172 ? 0.2920 0.3914 0.2627 0.0570  -0.0574 -0.1235 1170 ALA A C   
8672  O O   . ALA A 1172 ? 0.3036 0.3954 0.2766 0.0559  -0.0562 -0.1220 1170 ALA A O   
8673  C CB  . ALA A 1172 ? 0.3002 0.4223 0.2579 0.0622  -0.0552 -0.1236 1170 ALA A CB  
8674  N N   . GLU A 1173 ? 0.3220 0.4221 0.2980 0.0571  -0.0614 -0.1296 1171 GLU A N   
8675  C CA  . GLU A 1173 ? 0.3420 0.4338 0.3273 0.0559  -0.0644 -0.1349 1171 GLU A CA  
8676  C C   . GLU A 1173 ? 0.3309 0.4101 0.3205 0.0519  -0.0636 -0.1286 1171 GLU A C   
8677  O O   . GLU A 1173 ? 0.3334 0.4043 0.3291 0.0504  -0.0644 -0.1297 1171 GLU A O   
8678  C CB  . GLU A 1173 ? 0.3755 0.4718 0.3660 0.0572  -0.0692 -0.1439 1171 GLU A CB  
8679  C CG  . GLU A 1173 ? 0.3961 0.5043 0.3837 0.0614  -0.0704 -0.1519 1171 GLU A CG  
8680  C CD  . GLU A 1173 ? 0.4384 0.5454 0.4265 0.0629  -0.0693 -0.1544 1171 GLU A CD  
8681  O OE1 . GLU A 1173 ? 0.4313 0.5276 0.4261 0.0610  -0.0701 -0.1544 1171 GLU A OE1 
8682  O OE2 . GLU A 1173 ? 0.4313 0.5484 0.4131 0.0659  -0.0677 -0.1561 1171 GLU A OE2 
8683  N N   . ARG A 1174 ? 0.2798 0.3581 0.2667 0.0500  -0.0620 -0.1220 1172 ARG A N   
8684  C CA  . ARG A 1174 ? 0.2726 0.3402 0.2626 0.0463  -0.0606 -0.1154 1172 ARG A CA  
8685  C C   . ARG A 1174 ? 0.3163 0.3792 0.3034 0.0458  -0.0570 -0.1104 1172 ARG A C   
8686  O O   . ARG A 1174 ? 0.2931 0.3468 0.2850 0.0434  -0.0569 -0.1087 1172 ARG A O   
8687  C CB  . ARG A 1174 ? 0.2944 0.3631 0.2814 0.0449  -0.0594 -0.1096 1172 ARG A CB  
8688  C CG  . ARG A 1174 ? 0.3261 0.3854 0.3153 0.0414  -0.0574 -0.1024 1172 ARG A CG  
8689  C CD  . ARG A 1174 ? 0.3574 0.4087 0.3557 0.0388  -0.0602 -0.1047 1172 ARG A CD  
8690  N NE  . ARG A 1174 ? 0.3055 0.3491 0.3057 0.0354  -0.0583 -0.0978 1172 ARG A NE  
8691  C CZ  . ARG A 1174 ? 0.3230 0.3587 0.3302 0.0327  -0.0596 -0.0974 1172 ARG A CZ  
8692  N NH1 . ARG A 1174 ? 0.3507 0.3843 0.3645 0.0328  -0.0629 -0.1034 1172 ARG A NH1 
8693  N NH2 . ARG A 1174 ? 0.3185 0.3486 0.3265 0.0297  -0.0575 -0.0909 1172 ARG A NH2 
8694  N N   . ILE A 1175 ? 0.2765 0.3457 0.2559 0.0478  -0.0541 -0.1078 1173 ILE A N   
8695  C CA  . ILE A 1175 ? 0.2809 0.3464 0.2574 0.0475  -0.0507 -0.1033 1173 ILE A CA  
8696  C C   . ILE A 1175 ? 0.2694 0.3312 0.2506 0.0480  -0.0522 -0.1087 1173 ILE A C   
8697  O O   . ILE A 1175 ? 0.2944 0.3480 0.2781 0.0461  -0.0509 -0.1056 1173 ILE A O   
8698  C CB  . ILE A 1175 ? 0.3214 0.3957 0.2894 0.0498  -0.0478 -0.1002 1173 ILE A CB  
8699  C CG1 . ILE A 1175 ? 0.2820 0.3580 0.2462 0.0488  -0.0462 -0.0936 1173 ILE A CG1 
8700  C CG2 . ILE A 1175 ? 0.2904 0.3619 0.2560 0.0499  -0.0448 -0.0971 1173 ILE A CG2 
8701  C CD1 . ILE A 1175 ? 0.3132 0.3992 0.2698 0.0511  -0.0441 -0.0906 1173 ILE A CD1 
8702  N N   . ARG A 1176 ? 0.3036 0.3718 0.2866 0.0507  -0.0550 -0.1169 1174 ARG A N   
8703  C CA  . ARG A 1176 ? 0.2932 0.3584 0.2813 0.0516  -0.0567 -0.1227 1174 ARG A CA  
8704  C C   . ARG A 1176 ? 0.2890 0.3431 0.2862 0.0485  -0.0590 -0.1229 1174 ARG A C   
8705  O O   . ARG A 1176 ? 0.2936 0.3408 0.2940 0.0475  -0.0585 -0.1218 1174 ARG A O   
8706  C CB  . ARG A 1176 ? 0.2747 0.3495 0.2636 0.0551  -0.0597 -0.1323 1174 ARG A CB  
8707  C CG  . ARG A 1176 ? 0.3422 0.4163 0.3346 0.0569  -0.0606 -0.1381 1174 ARG A CG  
8708  C CD  . ARG A 1176 ? 0.3629 0.4446 0.3589 0.0601  -0.0646 -0.1489 1174 ARG A CD  
8709  N NE  . ARG A 1176 ? 0.3284 0.4232 0.3173 0.0628  -0.0641 -0.1507 1174 ARG A NE  
8710  C CZ  . ARG A 1176 ? 0.3896 0.4944 0.3718 0.0658  -0.0620 -0.1519 1174 ARG A CZ  
8711  N NH1 . ARG A 1176 ? 0.3700 0.4733 0.3516 0.0665  -0.0600 -0.1514 1174 ARG A NH1 
8712  N NH2 . ARG A 1176 ? 0.3826 0.4999 0.3590 0.0681  -0.0620 -0.1536 1174 ARG A NH2 
8713  N N   . ALA A 1177 ? 0.3081 0.3606 0.3096 0.0470  -0.0616 -0.1238 1175 ALA A N   
8714  C CA  . ALA A 1177 ? 0.3447 0.3875 0.3554 0.0439  -0.0641 -0.1235 1175 ALA A CA  
8715  C C   . ALA A 1177 ? 0.3070 0.3416 0.3166 0.0407  -0.0609 -0.1147 1175 ALA A C   
8716  O O   . ALA A 1177 ? 0.3129 0.3397 0.3281 0.0388  -0.0615 -0.1138 1175 ALA A O   
8717  C CB  . ALA A 1177 ? 0.3271 0.3707 0.3418 0.0427  -0.0671 -0.1254 1175 ALA A CB  
8718  N N   . VAL A 1178 ? 0.2837 0.3202 0.2865 0.0400  -0.0575 -0.1082 1176 VAL A N   
8719  C CA  . VAL A 1178 ? 0.2562 0.2858 0.2577 0.0372  -0.0544 -0.1002 1176 VAL A CA  
8720  C C   . VAL A 1178 ? 0.2852 0.3122 0.2850 0.0378  -0.0522 -0.0989 1176 VAL A C   
8721  O O   . VAL A 1178 ? 0.2863 0.3056 0.2893 0.0354  -0.0515 -0.0954 1176 VAL A O   
8722  C CB  . VAL A 1178 ? 0.2588 0.2916 0.2536 0.0368  -0.0515 -0.0941 1176 VAL A CB  
8723  C CG1 . VAL A 1178 ? 0.2509 0.2775 0.2441 0.0345  -0.0480 -0.0866 1176 VAL A CG1 
8724  C CG2 . VAL A 1178 ? 0.2695 0.3031 0.2673 0.0355  -0.0536 -0.0944 1176 VAL A CG2 
8725  N N   . ASN A 1179 ? 0.2825 0.3164 0.2771 0.0410  -0.0511 -0.1017 1177 ASN A N   
8726  C CA  . ASN A 1179 ? 0.2648 0.2971 0.2575 0.0419  -0.0490 -0.1007 1177 ASN A CA  
8727  C C   . ASN A 1179 ? 0.2882 0.3142 0.2889 0.0412  -0.0517 -0.1048 1177 ASN A C   
8728  O O   . ASN A 1179 ? 0.2970 0.3171 0.2988 0.0400  -0.0502 -0.1016 1177 ASN A O   
8729  C CB  . ASN A 1179 ? 0.3484 0.3906 0.3349 0.0456  -0.0480 -0.1040 1177 ASN A CB  
8730  C CG  . ASN A 1179 ? 0.4252 0.4682 0.4057 0.0461  -0.0440 -0.0989 1177 ASN A CG  
8731  O OD1 . ASN A 1179 ? 0.4644 0.5007 0.4445 0.0437  -0.0417 -0.0926 1177 ASN A OD1 
8732  N ND2 . ASN A 1179 ? 0.5032 0.5549 0.4790 0.0492  -0.0431 -0.1016 1177 ASN A ND2 
8733  N N   . LYS A 1180 ? 0.2796 0.3068 0.2865 0.0421  -0.0558 -0.1120 1178 LYS A N   
8734  C CA  . LYS A 1180 ? 0.3012 0.3219 0.3172 0.0413  -0.0589 -0.1158 1178 LYS A CA  
8735  C C   . LYS A 1180 ? 0.2810 0.2922 0.3023 0.0371  -0.0592 -0.1100 1178 LYS A C   
8736  O O   . LYS A 1180 ? 0.2909 0.2955 0.3163 0.0358  -0.0593 -0.1084 1178 LYS A O   
8737  C CB  . LYS A 1180 ? 0.3463 0.3706 0.3683 0.0431  -0.0636 -0.1248 1178 LYS A CB  
8738  C CG  . LYS A 1180 ? 0.3180 0.3524 0.3356 0.0475  -0.0637 -0.1315 1178 LYS A CG  
8739  C CD  . LYS A 1180 ? 0.3563 0.3959 0.3786 0.0494  -0.0681 -0.1403 1178 LYS A CD  
8740  C CE  . LYS A 1180 ? 0.4802 0.5124 0.5148 0.0480  -0.0728 -0.1449 1178 LYS A CE  
8741  N NZ  . LYS A 1180 ? 0.5066 0.5442 0.5465 0.0503  -0.0775 -0.1547 1178 LYS A NZ  
8742  N N   . ALA A 1181 ? 0.2928 0.3035 0.3141 0.0350  -0.0593 -0.1066 1179 ALA A N   
8743  C CA  . ALA A 1181 ? 0.2824 0.2853 0.3082 0.0310  -0.0592 -0.1008 1179 ALA A CA  
8744  C C   . ALA A 1181 ? 0.2924 0.2918 0.3134 0.0296  -0.0550 -0.0935 1179 ALA A C   
8745  O O   . ALA A 1181 ? 0.2900 0.2826 0.3154 0.0270  -0.0552 -0.0901 1179 ALA A O   
8746  C CB  . ALA A 1181 ? 0.2846 0.2889 0.3105 0.0293  -0.0598 -0.0986 1179 ALA A CB  
8747  N N   . ILE A 1182 ? 0.2636 0.2678 0.2757 0.0314  -0.0515 -0.0911 1180 ILE A N   
8748  C CA  . ILE A 1182 ? 0.2716 0.2727 0.2792 0.0302  -0.0476 -0.0846 1180 ILE A CA  
8749  C C   . ILE A 1182 ? 0.2858 0.2838 0.2953 0.0309  -0.0475 -0.0861 1180 ILE A C   
8750  O O   . ILE A 1182 ? 0.2751 0.2671 0.2861 0.0288  -0.0462 -0.0816 1180 ILE A O   
8751  C CB  . ILE A 1182 ? 0.2801 0.2872 0.2785 0.0319  -0.0441 -0.0816 1180 ILE A CB  
8752  C CG1 . ILE A 1182 ? 0.2768 0.2853 0.2739 0.0305  -0.0438 -0.0785 1180 ILE A CG1 
8753  C CG2 . ILE A 1182 ? 0.2937 0.2982 0.2878 0.0315  -0.0404 -0.0763 1180 ILE A CG2 
8754  C CD1 . ILE A 1182 ? 0.3237 0.3383 0.3127 0.0322  -0.0410 -0.0757 1180 ILE A CD1 
8755  N N   . ALA A 1183 ? 0.2838 0.2861 0.2934 0.0341  -0.0489 -0.0925 1181 ALA A N   
8756  C CA  . ALA A 1183 ? 0.2852 0.2849 0.2970 0.0350  -0.0490 -0.0944 1181 ALA A CA  
8757  C C   . ALA A 1183 ? 0.3045 0.2961 0.3257 0.0325  -0.0519 -0.0945 1181 ALA A C   
8758  O O   . ALA A 1183 ? 0.2960 0.2831 0.3191 0.0319  -0.0513 -0.0928 1181 ALA A O   
8759  C CB  . ALA A 1183 ? 0.2964 0.3031 0.3073 0.0390  -0.0504 -0.1021 1181 ALA A CB  
8760  N N   . ALA A 1184 ? 0.2878 0.2776 0.3154 0.0309  -0.0552 -0.0961 1182 ALA A N   
8761  C CA  . ALA A 1184 ? 0.3036 0.2861 0.3411 0.0283  -0.0584 -0.0959 1182 ALA A CA  
8762  C C   . ALA A 1184 ? 0.3089 0.2857 0.3467 0.0244  -0.0564 -0.0876 1182 ALA A C   
8763  O O   . ALA A 1184 ? 0.3018 0.2726 0.3473 0.0220  -0.0586 -0.0861 1182 ALA A O   
8764  C CB  . ALA A 1184 ? 0.2991 0.2820 0.3440 0.0279  -0.0628 -0.1006 1182 ALA A CB  
8765  N N   . LEU A 1185 ? 0.2773 0.2561 0.3072 0.0238  -0.0526 -0.0822 1183 LEU A N   
8766  C CA  . LEU A 1185 ? 0.2922 0.2665 0.3222 0.0203  -0.0506 -0.0747 1183 LEU A CA  
8767  C C   . LEU A 1185 ? 0.3047 0.2747 0.3354 0.0199  -0.0495 -0.0724 1183 LEU A C   
8768  O O   . LEU A 1185 ? 0.3044 0.2764 0.3313 0.0225  -0.0481 -0.0747 1183 LEU A O   
8769  C CB  . LEU A 1185 ? 0.2479 0.2256 0.2695 0.0202  -0.0467 -0.0702 1183 LEU A CB  
8770  C CG  . LEU A 1185 ? 0.2747 0.2569 0.2949 0.0206  -0.0476 -0.0717 1183 LEU A CG  
8771  C CD1 . LEU A 1185 ? 0.2924 0.2778 0.3045 0.0208  -0.0437 -0.0672 1183 LEU A CD1 
8772  C CD2 . LEU A 1185 ? 0.2871 0.2664 0.3150 0.0177  -0.0506 -0.0711 1183 LEU A CD2 
8773  N N   . PRO A 1186 ? 0.2993 0.2639 0.3350 0.0165  -0.0500 -0.0678 1184 PRO A N   
8774  C CA  . PRO A 1186 ? 0.2898 0.2505 0.3260 0.0160  -0.0489 -0.0653 1184 PRO A CA  
8775  C C   . PRO A 1186 ? 0.2545 0.2170 0.2817 0.0166  -0.0442 -0.0611 1184 PRO A C   
8776  O O   . PRO A 1186 ? 0.3021 0.2675 0.3237 0.0163  -0.0418 -0.0584 1184 PRO A O   
8777  C CB  . PRO A 1186 ? 0.3478 0.3036 0.3910 0.0119  -0.0505 -0.0604 1184 PRO A CB  
8778  C CG  . PRO A 1186 ? 0.3791 0.3371 0.4213 0.0102  -0.0502 -0.0581 1184 PRO A CG  
8779  C CD  . PRO A 1186 ? 0.3307 0.2932 0.3712 0.0130  -0.0514 -0.0643 1184 PRO A CD  
8780  N N   . GLY A 1187 ? 0.2875 0.2483 0.3137 0.0175  -0.0431 -0.0609 1185 GLY A N   
8781  C CA  . GLY A 1187 ? 0.3327 0.2939 0.3517 0.0175  -0.0390 -0.0564 1185 GLY A CA  
8782  C C   . GLY A 1187 ? 0.2731 0.2395 0.2847 0.0209  -0.0366 -0.0587 1185 GLY A C   
8783  O O   . GLY A 1187 ? 0.2995 0.2681 0.3115 0.0236  -0.0377 -0.0639 1185 GLY A O   
8784  N N   . PRO A 1188 ? 0.2813 0.2501 0.2863 0.0207  -0.0333 -0.0548 1186 PRO A N   
8785  C CA  . PRO A 1188 ? 0.2567 0.2299 0.2547 0.0235  -0.0306 -0.0554 1186 PRO A CA  
8786  C C   . PRO A 1188 ? 0.2593 0.2385 0.2556 0.0262  -0.0318 -0.0604 1186 PRO A C   
8787  O O   . PRO A 1188 ? 0.2717 0.2520 0.2702 0.0257  -0.0337 -0.0620 1186 PRO A O   
8788  C CB  . PRO A 1188 ? 0.3062 0.2797 0.2992 0.0221  -0.0274 -0.0496 1186 PRO A CB  
8789  C CG  . PRO A 1188 ? 0.3158 0.2878 0.3120 0.0196  -0.0287 -0.0480 1186 PRO A CG  
8790  C CD  . PRO A 1188 ? 0.2792 0.2470 0.2831 0.0181  -0.0320 -0.0498 1186 PRO A CD  
8791  N N   . LEU A 1189 ? 0.2551 0.2385 0.2472 0.0290  -0.0305 -0.0626 1187 LEU A N   
8792  C CA  . LEU A 1189 ? 0.2484 0.2391 0.2372 0.0317  -0.0309 -0.0663 1187 LEU A CA  
8793  C C   . LEU A 1189 ? 0.2722 0.2653 0.2558 0.0311  -0.0286 -0.0618 1187 LEU A C   
8794  O O   . LEU A 1189 ? 0.3091 0.3004 0.2896 0.0299  -0.0258 -0.0565 1187 LEU A O   
8795  C CB  . LEU A 1189 ? 0.2646 0.2600 0.2498 0.0347  -0.0296 -0.0688 1187 LEU A CB  
8796  C CG  . LEU A 1189 ? 0.2773 0.2730 0.2673 0.0365  -0.0322 -0.0753 1187 LEU A CG  
8797  C CD1 . LEU A 1189 ? 0.2981 0.2863 0.2931 0.0347  -0.0328 -0.0738 1187 LEU A CD1 
8798  C CD2 . LEU A 1189 ? 0.3230 0.3263 0.3084 0.0399  -0.0308 -0.0781 1187 LEU A CD2 
8799  N N   . LEU A 1190 ? 0.2698 0.2671 0.2530 0.0318  -0.0300 -0.0641 1188 LEU A N   
8800  C CA  . LEU A 1190 ? 0.2622 0.2620 0.2413 0.0313  -0.0283 -0.0602 1188 LEU A CA  
8801  C C   . LEU A 1190 ? 0.2489 0.2567 0.2222 0.0342  -0.0271 -0.0611 1188 LEU A C   
8802  O O   . LEU A 1190 ? 0.2881 0.3008 0.2615 0.0364  -0.0289 -0.0665 1188 LEU A O   
8803  C CB  . LEU A 1190 ? 0.2931 0.2923 0.2755 0.0299  -0.0306 -0.0612 1188 LEU A CB  
8804  C CG  . LEU A 1190 ? 0.2854 0.2775 0.2738 0.0267  -0.0319 -0.0596 1188 LEU A CG  
8805  C CD1 . LEU A 1190 ? 0.3557 0.3484 0.3466 0.0253  -0.0336 -0.0596 1188 LEU A CD1 
8806  C CD2 . LEU A 1190 ? 0.3165 0.3044 0.3034 0.0248  -0.0291 -0.0536 1188 LEU A CD2 
8807  N N   . LEU A 1191 ? 0.2505 0.2596 0.2189 0.0341  -0.0242 -0.0560 1189 LEU A N   
8808  C CA  . LEU A 1191 ? 0.2551 0.2722 0.2183 0.0365  -0.0231 -0.0556 1189 LEU A CA  
8809  C C   . LEU A 1191 ? 0.2543 0.2744 0.2174 0.0364  -0.0245 -0.0562 1189 LEU A C   
8810  O O   . LEU A 1191 ? 0.2686 0.2863 0.2318 0.0347  -0.0237 -0.0521 1189 LEU A O   
8811  C CB  . LEU A 1191 ? 0.2453 0.2622 0.2045 0.0362  -0.0198 -0.0495 1189 LEU A CB  
8812  C CG  . LEU A 1191 ? 0.2545 0.2795 0.2085 0.0386  -0.0183 -0.0483 1189 LEU A CG  
8813  C CD1 . LEU A 1191 ? 0.2540 0.2771 0.2058 0.0380  -0.0153 -0.0425 1189 LEU A CD1 
8814  C CD2 . LEU A 1191 ? 0.2536 0.2844 0.2055 0.0394  -0.0190 -0.0478 1189 LEU A CD2 
8815  N N   . VAL A 1192 ? 0.2599 0.2856 0.2233 0.0384  -0.0268 -0.0615 1190 VAL A N   
8816  C CA  . VAL A 1192 ? 0.2654 0.2945 0.2294 0.0385  -0.0287 -0.0632 1190 VAL A CA  
8817  C C   . VAL A 1192 ? 0.2556 0.2935 0.2139 0.0407  -0.0275 -0.0617 1190 VAL A C   
8818  O O   . VAL A 1192 ? 0.2716 0.3155 0.2268 0.0430  -0.0270 -0.0634 1190 VAL A O   
8819  C CB  . VAL A 1192 ? 0.2704 0.3005 0.2388 0.0393  -0.0322 -0.0705 1190 VAL A CB  
8820  C CG1 . VAL A 1192 ? 0.2722 0.3060 0.2414 0.0394  -0.0343 -0.0723 1190 VAL A CG1 
8821  C CG2 . VAL A 1192 ? 0.3019 0.3234 0.2767 0.0371  -0.0336 -0.0716 1190 VAL A CG2 
8822  N N   . GLN A 1193 ? 0.2422 0.2813 0.1994 0.0400  -0.0273 -0.0584 1191 GLN A N   
8823  C CA  . GLN A 1193 ? 0.2313 0.2791 0.1839 0.0420  -0.0270 -0.0572 1191 GLN A CA  
8824  C C   . GLN A 1193 ? 0.2298 0.2806 0.1842 0.0421  -0.0297 -0.0606 1191 GLN A C   
8825  O O   . GLN A 1193 ? 0.2532 0.2986 0.2111 0.0401  -0.0306 -0.0598 1191 GLN A O   
8826  C CB  . GLN A 1193 ? 0.2550 0.3020 0.2050 0.0411  -0.0244 -0.0499 1191 GLN A CB  
8827  C CG  . GLN A 1193 ? 0.2701 0.3139 0.2187 0.0407  -0.0217 -0.0461 1191 GLN A CG  
8828  C CD  . GLN A 1193 ? 0.2543 0.2992 0.2004 0.0405  -0.0196 -0.0393 1191 GLN A CD  
8829  O OE1 . GLN A 1193 ? 0.2730 0.3255 0.2157 0.0422  -0.0192 -0.0375 1191 GLN A OE1 
8830  N NE2 . GLN A 1193 ? 0.2678 0.3054 0.2159 0.0384  -0.0183 -0.0356 1191 GLN A NE2 
8831  N N   . ALA A 1194 ? 0.2323 0.2920 0.1842 0.0446  -0.0310 -0.0642 1192 ALA A N   
8832  C CA  . ALA A 1194 ? 0.2219 0.2853 0.1754 0.0450  -0.0339 -0.0681 1192 ALA A CA  
8833  C C   . ALA A 1194 ? 0.2463 0.3191 0.1949 0.0468  -0.0334 -0.0656 1192 ALA A C   
8834  O O   . ALA A 1194 ? 0.2600 0.3388 0.2041 0.0484  -0.0316 -0.0632 1192 ALA A O   
8835  C CB  . ALA A 1194 ? 0.2577 0.3238 0.2138 0.0465  -0.0367 -0.0764 1192 ALA A CB  
8836  N N   . ALA A 1195 ? 0.2400 0.3144 0.1898 0.0464  -0.0352 -0.0661 1193 ALA A N   
8837  C CA  . ALA A 1195 ? 0.2541 0.3378 0.1999 0.0480  -0.0353 -0.0641 1193 ALA A CA  
8838  C C   . ALA A 1195 ? 0.2392 0.3252 0.1875 0.0481  -0.0385 -0.0684 1193 ALA A C   
8839  O O   . ALA A 1195 ? 0.2590 0.3380 0.2124 0.0461  -0.0399 -0.0702 1193 ALA A O   
8840  C CB  . ALA A 1195 ? 0.2616 0.3431 0.2057 0.0469  -0.0330 -0.0559 1193 ALA A CB  
8841  N N   . SER A 1196 ? 0.2339 0.3304 0.1790 0.0503  -0.0396 -0.0700 1194 SER A N   
8842  C CA  . SER A 1196 ? 0.2553 0.3548 0.2024 0.0504  -0.0425 -0.0733 1194 SER A CA  
8843  C C   . SER A 1196 ? 0.2552 0.3524 0.2023 0.0489  -0.0417 -0.0669 1194 SER A C   
8844  O O   . SER A 1196 ? 0.2557 0.3512 0.2007 0.0484  -0.0391 -0.0601 1194 SER A O   
8845  C CB  . SER A 1196 ? 0.3025 0.4149 0.2457 0.0534  -0.0440 -0.0770 1194 SER A CB  
8846  O OG  . SER A 1196 ? 0.2763 0.3955 0.2141 0.0544  -0.0420 -0.0706 1194 SER A OG  
8847  N N   . SER A 1197 ? 0.2671 0.3644 0.2173 0.0483  -0.0441 -0.0692 1195 SER A N   
8848  C CA  . SER A 1197 ? 0.2396 0.3360 0.1901 0.0472  -0.0436 -0.0637 1195 SER A CA  
8849  C C   . SER A 1197 ? 0.2634 0.3687 0.2085 0.0491  -0.0426 -0.0590 1195 SER A C   
8850  O O   . SER A 1197 ? 0.2800 0.3833 0.2245 0.0484  -0.0407 -0.0522 1195 SER A O   
8851  C CB  . SER A 1197 ? 0.2911 0.3880 0.2456 0.0465  -0.0467 -0.0676 1195 SER A CB  
8852  O OG  . SER A 1197 ? 0.3000 0.3886 0.2601 0.0445  -0.0478 -0.0713 1195 SER A OG  
8853  N N   . GLY A 1198 ? 0.2777 0.3934 0.2194 0.0515  -0.0438 -0.0624 1196 GLY A N   
8854  C CA  . GLY A 1198 ? 0.2957 0.4209 0.2322 0.0533  -0.0429 -0.0576 1196 GLY A CA  
8855  C C   . GLY A 1198 ? 0.2968 0.4204 0.2306 0.0532  -0.0397 -0.0514 1196 GLY A C   
8856  O O   . GLY A 1198 ? 0.3014 0.4275 0.2333 0.0533  -0.0384 -0.0444 1196 GLY A O   
8857  N N   . GLU A 1199 ? 0.2751 0.3945 0.2092 0.0530  -0.0385 -0.0539 1197 GLU A N   
8858  C CA  . GLU A 1199 ? 0.2873 0.4046 0.2193 0.0528  -0.0355 -0.0484 1197 GLU A CA  
8859  C C   . GLU A 1199 ? 0.2845 0.3921 0.2192 0.0505  -0.0338 -0.0421 1197 GLU A C   
8860  O O   . GLU A 1199 ? 0.2894 0.3978 0.2225 0.0505  -0.0318 -0.0354 1197 GLU A O   
8861  C CB  . GLU A 1199 ? 0.2754 0.3895 0.2079 0.0529  -0.0349 -0.0531 1197 GLU A CB  
8862  C CG  . GLU A 1199 ? 0.3499 0.4631 0.2801 0.0530  -0.0319 -0.0486 1197 GLU A CG  
8863  C CD  . GLU A 1199 ? 0.5351 0.6466 0.4658 0.0535  -0.0318 -0.0543 1197 GLU A CD  
8864  O OE1 . GLU A 1199 ? 0.4430 0.5548 0.3760 0.0540  -0.0343 -0.0617 1197 GLU A OE1 
8865  O OE2 . GLU A 1199 ? 0.5703 0.6802 0.4995 0.0534  -0.0295 -0.0514 1197 GLU A OE2 
8866  N N   . ILE A 1200 ? 0.2766 0.3756 0.2159 0.0486  -0.0346 -0.0443 1198 ILE A N   
8867  C CA  . ILE A 1200 ? 0.2838 0.3747 0.2258 0.0466  -0.0332 -0.0390 1198 ILE A CA  
8868  C C   . ILE A 1200 ? 0.3212 0.4168 0.2623 0.0471  -0.0334 -0.0338 1198 ILE A C   
8869  O O   . ILE A 1200 ? 0.2896 0.3821 0.2312 0.0465  -0.0316 -0.0276 1198 ILE A O   
8870  C CB  . ILE A 1200 ? 0.2669 0.3495 0.2139 0.0445  -0.0343 -0.0426 1198 ILE A CB  
8871  C CG1 . ILE A 1200 ? 0.2608 0.3377 0.2092 0.0437  -0.0338 -0.0463 1198 ILE A CG1 
8872  C CG2 . ILE A 1200 ? 0.2843 0.3604 0.2342 0.0426  -0.0331 -0.0376 1198 ILE A CG2 
8873  C CD1 . ILE A 1200 ? 0.2894 0.3592 0.2430 0.0417  -0.0353 -0.0501 1198 ILE A CD1 
8874  N N   . ALA A 1201 ? 0.2718 0.3753 0.2120 0.0484  -0.0357 -0.0361 1199 ALA A N   
8875  C CA  . ALA A 1201 ? 0.3171 0.4254 0.2568 0.0490  -0.0362 -0.0312 1199 ALA A CA  
8876  C C   . ALA A 1201 ? 0.3035 0.4187 0.2392 0.0504  -0.0348 -0.0254 1199 ALA A C   
8877  O O   . ALA A 1201 ? 0.3259 0.4413 0.2623 0.0503  -0.0342 -0.0189 1199 ALA A O   
8878  C CB  . ALA A 1201 ? 0.3125 0.4276 0.2522 0.0500  -0.0392 -0.0354 1199 ALA A CB  
8879  N N   . ARG A 1202 ? 0.2735 0.3948 0.2054 0.0518  -0.0344 -0.0276 1200 ARG A N   
8880  C CA  . ARG A 1202 ? 0.2805 0.4104 0.2086 0.0532  -0.0333 -0.0222 1200 ARG A CA  
8881  C C   . ARG A 1202 ? 0.3227 0.4472 0.2509 0.0524  -0.0305 -0.0172 1200 ARG A C   
8882  O O   . ARG A 1202 ? 0.3586 0.4868 0.2858 0.0527  -0.0295 -0.0101 1200 ARG A O   
8883  C CB  . ARG A 1202 ? 0.2862 0.4272 0.2098 0.0554  -0.0343 -0.0269 1200 ARG A CB  
8884  C CG  . ARG A 1202 ? 0.2752 0.4241 0.1981 0.0566  -0.0372 -0.0312 1200 ARG A CG  
8885  C CD  . ARG A 1202 ? 0.3364 0.4975 0.2548 0.0590  -0.0381 -0.0359 1200 ARG A CD  
8886  N NE  . ARG A 1202 ? 0.3424 0.4997 0.2614 0.0591  -0.0377 -0.0426 1200 ARG A NE  
8887  C CZ  . ARG A 1202 ? 0.3675 0.5235 0.2885 0.0594  -0.0398 -0.0511 1200 ARG A CZ  
8888  N NH1 . ARG A 1202 ? 0.3222 0.4818 0.2443 0.0598  -0.0426 -0.0547 1200 ARG A NH1 
8889  N NH2 . ARG A 1202 ? 0.3599 0.5108 0.2823 0.0592  -0.0394 -0.0562 1200 ARG A NH2 
8890  N N   . ASN A 1203 ? 0.2845 0.4005 0.2143 0.0512  -0.0294 -0.0204 1201 ASN A N   
8891  C CA  . ASN A 1203 ? 0.2693 0.3814 0.1987 0.0506  -0.0268 -0.0167 1201 ASN A CA  
8892  C C   . ASN A 1203 ? 0.3401 0.4398 0.2738 0.0484  -0.0256 -0.0150 1201 ASN A C   
8893  O O   . ASN A 1203 ? 0.3178 0.4105 0.2535 0.0474  -0.0258 -0.0200 1201 ASN A O   
8894  C CB  . ASN A 1203 ? 0.3236 0.4378 0.2506 0.0515  -0.0263 -0.0220 1201 ASN A CB  
8895  C CG  . ASN A 1203 ? 0.3769 0.4878 0.3034 0.0510  -0.0237 -0.0182 1201 ASN A CG  
8896  O OD1 . ASN A 1203 ? 0.3502 0.4579 0.2779 0.0501  -0.0223 -0.0115 1201 ASN A OD1 
8897  N ND2 . ASN A 1203 ? 0.3728 0.4845 0.2978 0.0516  -0.0231 -0.0228 1201 ASN A ND2 
8898  N N   . PRO A 1204 ? 0.3425 0.4393 0.2779 0.0477  -0.0245 -0.0082 1202 PRO A N   
8899  C CA  . PRO A 1204 ? 0.3772 0.4629 0.3167 0.0458  -0.0233 -0.0070 1202 PRO A CA  
8900  C C   . PRO A 1204 ? 0.3538 0.4335 0.2932 0.0449  -0.0216 -0.0091 1202 PRO A C   
8901  O O   . PRO A 1204 ? 0.3453 0.4161 0.2878 0.0433  -0.0210 -0.0102 1202 PRO A O   
8902  C CB  . PRO A 1204 ? 0.4680 0.5538 0.4091 0.0457  -0.0225 0.0008  1202 PRO A CB  
8903  C CG  . PRO A 1204 ? 0.4366 0.5326 0.3756 0.0473  -0.0241 0.0031  1202 PRO A CG  
8904  C CD  . PRO A 1204 ? 0.3956 0.4995 0.3299 0.0487  -0.0245 -0.0015 1202 PRO A CD  
8905  N N   . ASP A 1205 ? 0.3613 0.4460 0.2973 0.0460  -0.0208 -0.0098 1203 ASP A N   
8906  C CA  . ASP A 1205 ? 0.3348 0.4145 0.2707 0.0454  -0.0193 -0.0121 1203 ASP A CA  
8907  C C   . ASP A 1205 ? 0.3388 0.4199 0.2736 0.0460  -0.0206 -0.0197 1203 ASP A C   
8908  O O   . ASP A 1205 ? 0.3814 0.4619 0.3151 0.0463  -0.0196 -0.0219 1203 ASP A O   
8909  C CB  . ASP A 1205 ? 0.3831 0.4670 0.3166 0.0461  -0.0175 -0.0075 1203 ASP A CB  
8910  C CG  . ASP A 1205 ? 0.4985 0.5805 0.4339 0.0455  -0.0165 0.0001  1203 ASP A CG  
8911  O OD1 . ASP A 1205 ? 0.4259 0.5005 0.3650 0.0441  -0.0166 0.0013  1203 ASP A OD1 
8912  O OD2 . ASP A 1205 ? 0.5120 0.6003 0.4456 0.0463  -0.0157 0.0050  1203 ASP A OD2 
8913  N N   . ALA A 1206 ? 0.2895 0.3726 0.2251 0.0463  -0.0228 -0.0239 1204 ALA A N   
8914  C CA  . ALA A 1206 ? 0.3209 0.4047 0.2567 0.0468  -0.0245 -0.0315 1204 ALA A CA  
8915  C C   . ALA A 1206 ? 0.3015 0.3762 0.2398 0.0453  -0.0236 -0.0339 1204 ALA A C   
8916  O O   . ALA A 1206 ? 0.3361 0.4119 0.2738 0.0461  -0.0239 -0.0384 1204 ALA A O   
8917  C CB  . ALA A 1206 ? 0.3271 0.4113 0.2651 0.0465  -0.0270 -0.0348 1204 ALA A CB  
8918  N N   . TYR A 1207 ? 0.2945 0.3605 0.2358 0.0432  -0.0227 -0.0310 1205 TYR A N   
8919  C CA  . TYR A 1207 ? 0.2838 0.3413 0.2273 0.0417  -0.0215 -0.0318 1205 TYR A CA  
8920  C C   . TYR A 1207 ? 0.3034 0.3588 0.2459 0.0413  -0.0189 -0.0259 1205 TYR A C   
8921  O O   . TYR A 1207 ? 0.3831 0.4371 0.3265 0.0407  -0.0182 -0.0210 1205 TYR A O   
8922  C CB  . TYR A 1207 ? 0.2718 0.3217 0.2196 0.0395  -0.0223 -0.0329 1205 TYR A CB  
8923  C CG  . TYR A 1207 ? 0.2414 0.2929 0.1911 0.0396  -0.0250 -0.0385 1205 TYR A CG  
8924  C CD1 . TYR A 1207 ? 0.2714 0.3239 0.2216 0.0403  -0.0264 -0.0442 1205 TYR A CD1 
8925  C CD2 . TYR A 1207 ? 0.2599 0.3121 0.2114 0.0390  -0.0264 -0.0382 1205 TYR A CD2 
8926  C CE1 . TYR A 1207 ? 0.2499 0.3036 0.2025 0.0403  -0.0292 -0.0495 1205 TYR A CE1 
8927  C CE2 . TYR A 1207 ? 0.2674 0.3210 0.2210 0.0390  -0.0290 -0.0433 1205 TYR A CE2 
8928  C CZ  . TYR A 1207 ? 0.2603 0.3146 0.2146 0.0396  -0.0304 -0.0490 1205 TYR A CZ  
8929  O OH  . TYR A 1207 ? 0.2683 0.3239 0.2255 0.0396  -0.0333 -0.0542 1205 TYR A OH  
8930  N N   . CYS A 1208 ? 0.2994 0.3545 0.2406 0.0417  -0.0176 -0.0264 1206 CYS A N   
8931  C CA  . CYS A 1208 ? 0.2817 0.3357 0.2219 0.0415  -0.0153 -0.0209 1206 CYS A CA  
8932  C C   . CYS A 1208 ? 0.2645 0.3086 0.2079 0.0393  -0.0141 -0.0196 1206 CYS A C   
8933  O O   . CYS A 1208 ? 0.2688 0.3080 0.2139 0.0384  -0.0144 -0.0233 1206 CYS A O   
8934  C CB  . CYS A 1208 ? 0.3006 0.3596 0.2379 0.0430  -0.0144 -0.0222 1206 CYS A CB  
8935  S SG  . CYS A 1208 ? 0.3625 0.4205 0.2989 0.0427  -0.0116 -0.0156 1206 CYS A SG  
8936  N N   . LEU A 1209 ? 0.2518 0.2933 0.1963 0.0386  -0.0129 -0.0143 1207 LEU A N   
8937  C CA  . LEU A 1209 ? 0.2388 0.2719 0.1863 0.0366  -0.0119 -0.0131 1207 LEU A CA  
8938  C C   . LEU A 1209 ? 0.2639 0.2938 0.2110 0.0362  -0.0102 -0.0127 1207 LEU A C   
8939  O O   . LEU A 1209 ? 0.2657 0.2888 0.2151 0.0346  -0.0096 -0.0130 1207 LEU A O   
8940  C CB  . LEU A 1209 ? 0.2342 0.2657 0.1836 0.0361  -0.0113 -0.0081 1207 LEU A CB  
8941  C CG  . LEU A 1209 ? 0.2538 0.2883 0.2041 0.0365  -0.0129 -0.0082 1207 LEU A CG  
8942  C CD1 . LEU A 1209 ? 0.2931 0.3256 0.2461 0.0361  -0.0123 -0.0035 1207 LEU A CD1 
8943  C CD2 . LEU A 1209 ? 0.2756 0.3071 0.2277 0.0354  -0.0143 -0.0129 1207 LEU A CD2 
8944  N N   . ASN A 1210 ? 0.2626 0.2977 0.2068 0.0377  -0.0095 -0.0120 1208 ASN A N   
8945  C CA  . ASN A 1210 ? 0.2646 0.2972 0.2085 0.0374  -0.0080 -0.0118 1208 ASN A CA  
8946  C C   . ASN A 1210 ? 0.2610 0.2884 0.2064 0.0365  -0.0086 -0.0168 1208 ASN A C   
8947  O O   . ASN A 1210 ? 0.2856 0.3076 0.2323 0.0354  -0.0075 -0.0164 1208 ASN A O   
8948  C CB  . ASN A 1210 ? 0.2976 0.3381 0.2381 0.0393  -0.0075 -0.0116 1208 ASN A CB  
8949  C CG  . ASN A 1210 ? 0.3055 0.3514 0.2448 0.0401  -0.0066 -0.0056 1208 ASN A CG  
8950  O OD1 . ASN A 1210 ? 0.4063 0.4506 0.3473 0.0394  -0.0068 -0.0020 1208 ASN A OD1 
8951  N ND2 . ASN A 1210 ? 0.4148 0.4675 0.3514 0.0414  -0.0058 -0.0044 1208 ASN A ND2 
8952  N N   . TRP A 1211 ? 0.2564 0.2856 0.2020 0.0370  -0.0106 -0.0216 1209 TRP A N   
8953  C CA  . TRP A 1211 ? 0.2563 0.2816 0.2039 0.0363  -0.0116 -0.0265 1209 TRP A CA  
8954  C C   . TRP A 1211 ? 0.2607 0.2793 0.2118 0.0342  -0.0125 -0.0272 1209 TRP A C   
8955  O O   . TRP A 1211 ? 0.2978 0.3130 0.2513 0.0334  -0.0137 -0.0308 1209 TRP A O   
8956  C CB  . TRP A 1211 ? 0.2708 0.3019 0.2172 0.0381  -0.0135 -0.0318 1209 TRP A CB  
8957  C CG  . TRP A 1211 ? 0.2751 0.3151 0.2177 0.0404  -0.0128 -0.0308 1209 TRP A CG  
8958  C CD1 . TRP A 1211 ? 0.2843 0.3324 0.2247 0.0421  -0.0140 -0.0321 1209 TRP A CD1 
8959  C CD2 . TRP A 1211 ? 0.2595 0.3018 0.1999 0.0411  -0.0108 -0.0279 1209 TRP A CD2 
8960  N NE1 . TRP A 1211 ? 0.3000 0.3557 0.2368 0.0438  -0.0128 -0.0300 1209 TRP A NE1 
8961  C CE2 . TRP A 1211 ? 0.2544 0.3066 0.1914 0.0432  -0.0108 -0.0273 1209 TRP A CE2 
8962  C CE3 . TRP A 1211 ? 0.2547 0.2920 0.1959 0.0401  -0.0090 -0.0255 1209 TRP A CE3 
8963  C CZ2 . TRP A 1211 ? 0.2933 0.3507 0.2276 0.0443  -0.0090 -0.0243 1209 TRP A CZ2 
8964  C CZ3 . TRP A 1211 ? 0.2700 0.3120 0.2087 0.0412  -0.0073 -0.0228 1209 TRP A CZ3 
8965  C CH2 . TRP A 1211 ? 0.2692 0.3213 0.2046 0.0432  -0.0073 -0.0221 1209 TRP A CH2 
8966  N N   . LEU A 1212 ? 0.2435 0.2606 0.1953 0.0332  -0.0120 -0.0236 1210 LEU A N   
8967  C CA  . LEU A 1212 ? 0.2393 0.2512 0.1944 0.0312  -0.0125 -0.0238 1210 LEU A CA  
8968  C C   . LEU A 1212 ? 0.2190 0.2255 0.1754 0.0296  -0.0106 -0.0203 1210 LEU A C   
8969  O O   . LEU A 1212 ? 0.2304 0.2331 0.1894 0.0279  -0.0108 -0.0201 1210 LEU A O   
8970  C CB  . LEU A 1212 ? 0.2097 0.2246 0.1653 0.0314  -0.0136 -0.0232 1210 LEU A CB  
8971  C CG  . LEU A 1212 ? 0.2302 0.2492 0.1856 0.0323  -0.0159 -0.0275 1210 LEU A CG  
8972  C CD1 . LEU A 1212 ? 0.2567 0.2804 0.2115 0.0332  -0.0167 -0.0262 1210 LEU A CD1 
8973  C CD2 . LEU A 1212 ? 0.2659 0.2804 0.2249 0.0306  -0.0174 -0.0310 1210 LEU A CD2 
8974  N N   . VAL A 1213 ? 0.2304 0.2370 0.1852 0.0302  -0.0089 -0.0177 1211 VAL A N   
8975  C CA  . VAL A 1213 ? 0.2489 0.2504 0.2050 0.0289  -0.0073 -0.0152 1211 VAL A CA  
8976  C C   . VAL A 1213 ? 0.2354 0.2347 0.1911 0.0287  -0.0069 -0.0169 1211 VAL A C   
8977  O O   . VAL A 1213 ? 0.2577 0.2602 0.2120 0.0300  -0.0075 -0.0194 1211 VAL A O   
8978  C CB  . VAL A 1213 ? 0.2339 0.2364 0.1893 0.0295  -0.0058 -0.0106 1211 VAL A CB  
8979  C CG1 . VAL A 1213 ? 0.2555 0.2591 0.2123 0.0294  -0.0063 -0.0089 1211 VAL A CG1 
8980  C CG2 . VAL A 1213 ? 0.2620 0.2699 0.2146 0.0313  -0.0053 -0.0095 1211 VAL A CG2 
8981  N N   . GLU A 1214 ? 0.2309 0.2252 0.1882 0.0272  -0.0058 -0.0156 1212 GLU A N   
8982  C CA  . GLU A 1214 ? 0.2699 0.2614 0.2274 0.0268  -0.0053 -0.0166 1212 GLU A CA  
8983  C C   . GLU A 1214 ? 0.2489 0.2394 0.2057 0.0268  -0.0033 -0.0131 1212 GLU A C   
8984  O O   . GLU A 1214 ? 0.2377 0.2261 0.1957 0.0259  -0.0025 -0.0105 1212 GLU A O   
8985  C CB  . GLU A 1214 ? 0.3209 0.3075 0.2813 0.0246  -0.0060 -0.0178 1212 GLU A CB  
8986  C CG  . GLU A 1214 ? 0.4510 0.4344 0.4124 0.0240  -0.0060 -0.0191 1212 GLU A CG  
8987  C CD  . GLU A 1214 ? 0.4825 0.4622 0.4471 0.0218  -0.0071 -0.0201 1212 GLU A CD  
8988  O OE1 . GLU A 1214 ? 0.5061 0.4863 0.4723 0.0216  -0.0091 -0.0228 1212 GLU A OE1 
8989  O OE2 . GLU A 1214 ? 0.5546 0.5311 0.5203 0.0202  -0.0061 -0.0181 1212 GLU A OE2 
8990  N N   . GLU A 1215 ? 0.2340 0.2262 0.1892 0.0280  -0.0026 -0.0132 1213 GLU A N   
8991  C CA  . GLU A 1215 ? 0.2271 0.2184 0.1820 0.0279  -0.0008 -0.0099 1213 GLU A CA  
8992  C C   . GLU A 1215 ? 0.2281 0.2139 0.1847 0.0263  -0.0003 -0.0103 1213 GLU A C   
8993  O O   . GLU A 1215 ? 0.2333 0.2174 0.1906 0.0259  -0.0012 -0.0132 1213 GLU A O   
8994  C CB  . GLU A 1215 ? 0.2404 0.2364 0.1929 0.0297  -0.0003 -0.0098 1213 GLU A CB  
8995  C CG  . GLU A 1215 ? 0.2366 0.2393 0.1870 0.0314  -0.0007 -0.0090 1213 GLU A CG  
8996  C CD  . GLU A 1215 ? 0.2462 0.2545 0.1942 0.0332  -0.0004 -0.0103 1213 GLU A CD  
8997  O OE1 . GLU A 1215 ? 0.2515 0.2610 0.1991 0.0339  -0.0016 -0.0148 1213 GLU A OE1 
8998  O OE2 . GLU A 1215 ? 0.2660 0.2774 0.2128 0.0339  0.0009  -0.0068 1213 GLU A OE2 
8999  N N   . VAL A 1216 ? 0.2184 0.2015 0.1760 0.0254  0.0009  -0.0073 1214 VAL A N   
9000  C CA  . VAL A 1216 ? 0.2289 0.2075 0.1879 0.0240  0.0016  -0.0073 1214 VAL A CA  
9001  C C   . VAL A 1216 ? 0.2384 0.2170 0.1972 0.0244  0.0032  -0.0043 1214 VAL A C   
9002  O O   . VAL A 1216 ? 0.2485 0.2282 0.2077 0.0247  0.0038  -0.0016 1214 VAL A O   
9003  C CB  . VAL A 1216 ? 0.2385 0.2139 0.1997 0.0221  0.0013  -0.0072 1214 VAL A CB  
9004  C CG1 . VAL A 1216 ? 0.2552 0.2269 0.2176 0.0207  0.0020  -0.0068 1214 VAL A CG1 
9005  C CG2 . VAL A 1216 ? 0.2573 0.2329 0.2192 0.0216  -0.0003 -0.0098 1214 VAL A CG2 
9006  N N   . SER A 1217 ? 0.2262 0.2037 0.1848 0.0243  0.0037  -0.0049 1215 SER A N   
9007  C CA  . SER A 1217 ? 0.2302 0.2073 0.1890 0.0244  0.0051  -0.0023 1215 SER A CA  
9008  C C   . SER A 1217 ? 0.2231 0.1954 0.1837 0.0227  0.0055  -0.0022 1215 SER A C   
9009  O O   . SER A 1217 ? 0.2327 0.2028 0.1938 0.0218  0.0047  -0.0044 1215 SER A O   
9010  C CB  . SER A 1217 ? 0.2289 0.2088 0.1861 0.0257  0.0054  -0.0031 1215 SER A CB  
9011  O OG  . SER A 1217 ? 0.2621 0.2404 0.2200 0.0254  0.0067  -0.0013 1215 SER A OG  
9012  N N   . ALA A 1218 ? 0.2163 0.1873 0.1782 0.0222  0.0065  0.0004  1216 ALA A N   
9013  C CA  . ALA A 1218 ? 0.2154 0.1826 0.1790 0.0207  0.0069  0.0004  1216 ALA A CA  
9014  C C   . ALA A 1218 ? 0.2304 0.1973 0.1946 0.0209  0.0081  0.0027  1216 ALA A C   
9015  O O   . ALA A 1218 ? 0.2464 0.2147 0.2114 0.0216  0.0085  0.0051  1216 ALA A O   
9016  C CB  . ALA A 1218 ? 0.2370 0.2027 0.2023 0.0196  0.0067  0.0006  1216 ALA A CB  
9017  N N   . SER A 1219 ? 0.2186 0.1836 0.1829 0.0204  0.0084  0.0021  1217 SER A N   
9018  C CA  . SER A 1219 ? 0.2315 0.1963 0.1967 0.0205  0.0094  0.0041  1217 SER A CA  
9019  C C   . SER A 1219 ? 0.1994 0.1606 0.1664 0.0189  0.0096  0.0039  1217 SER A C   
9020  O O   . SER A 1219 ? 0.2395 0.1989 0.2063 0.0180  0.0091  0.0023  1217 SER A O   
9021  C CB  . SER A 1219 ? 0.2686 0.2348 0.2324 0.0214  0.0097  0.0034  1217 SER A CB  
9022  O OG  . SER A 1219 ? 0.2536 0.2200 0.2184 0.0214  0.0108  0.0056  1217 SER A OG  
9023  N N   . ILE A 1220 ? 0.2264 0.1869 0.1954 0.0186  0.0101  0.0057  1218 ILE A N   
9024  C CA  . ILE A 1220 ? 0.2110 0.1690 0.1820 0.0173  0.0102  0.0054  1218 ILE A CA  
9025  C C   . ILE A 1220 ? 0.2365 0.1938 0.2089 0.0173  0.0110  0.0070  1218 ILE A C   
9026  O O   . ILE A 1220 ? 0.2369 0.1952 0.2108 0.0180  0.0114  0.0092  1218 ILE A O   
9027  C CB  . ILE A 1220 ? 0.2493 0.2072 0.2223 0.0171  0.0099  0.0054  1218 ILE A CB  
9028  C CG1 . ILE A 1220 ? 0.2977 0.2567 0.2695 0.0171  0.0092  0.0040  1218 ILE A CG1 
9029  C CG2 . ILE A 1220 ? 0.2665 0.2227 0.2416 0.0158  0.0100  0.0046  1218 ILE A CG2 
9030  C CD1 . ILE A 1220 ? 0.4297 0.3897 0.4032 0.0177  0.0089  0.0045  1218 ILE A CD1 
9031  N N   . ASN A 1221 ? 0.2262 0.1819 0.1985 0.0164  0.0111  0.0061  1219 ASN A N   
9032  C CA  . ASN A 1221 ? 0.2371 0.1919 0.2110 0.0162  0.0117  0.0075  1219 ASN A CA  
9033  C C   . ASN A 1221 ? 0.2379 0.1915 0.2148 0.0154  0.0116  0.0076  1219 ASN A C   
9034  O O   . ASN A 1221 ? 0.2948 0.2474 0.2720 0.0143  0.0113  0.0059  1219 ASN A O   
9035  C CB  . ASN A 1221 ? 0.2702 0.2239 0.2433 0.0155  0.0117  0.0064  1219 ASN A CB  
9036  C CG  . ASN A 1221 ? 0.2475 0.2003 0.2224 0.0152  0.0123  0.0075  1219 ASN A CG  
9037  O OD1 . ASN A 1221 ? 0.2453 0.1985 0.2222 0.0155  0.0127  0.0093  1219 ASN A OD1 
9038  N ND2 . ASN A 1221 ? 0.2894 0.2410 0.2639 0.0144  0.0121  0.0066  1219 ASN A ND2 
9039  N N   . THR A 1222 ? 0.2259 0.1799 0.2053 0.0160  0.0119  0.0095  1220 THR A N   
9040  C CA  . THR A 1222 ? 0.2663 0.2192 0.2494 0.0156  0.0115  0.0092  1220 THR A CA  
9041  C C   . THR A 1222 ? 0.2994 0.2509 0.2847 0.0150  0.0118  0.0097  1220 THR A C   
9042  O O   . THR A 1222 ? 0.3660 0.3167 0.3549 0.0146  0.0114  0.0091  1220 THR A O   
9043  C CB  . THR A 1222 ? 0.3028 0.2565 0.2884 0.0165  0.0112  0.0110  1220 THR A CB  
9044  O OG1 . THR A 1222 ? 0.2872 0.2419 0.2734 0.0171  0.0117  0.0142  1220 THR A OG1 
9045  C CG2 . THR A 1222 ? 0.2799 0.2350 0.2632 0.0170  0.0108  0.0104  1220 THR A CG2 
9046  N N   . ALA A 1223 ? 0.2560 0.2076 0.2397 0.0149  0.0123  0.0104  1221 ALA A N   
9047  C CA  . ALA A 1223 ? 0.3099 0.2604 0.2955 0.0142  0.0125  0.0106  1221 ALA A CA  
9048  C C   . ALA A 1223 ? 0.3612 0.3109 0.3451 0.0131  0.0123  0.0084  1221 ALA A C   
9049  O O   . ALA A 1223 ? 0.4605 0.4095 0.4456 0.0125  0.0125  0.0084  1221 ALA A O   
9050  C CB  . ALA A 1223 ? 0.3175 0.2690 0.3029 0.0148  0.0133  0.0130  1221 ALA A CB  
9051  N N   . ALA A 1224 ? 0.3664 0.3165 0.3479 0.0128  0.0120  0.0067  1222 ALA A N   
9052  C CA  . ALA A 1224 ? 0.4019 0.3516 0.3817 0.0117  0.0117  0.0053  1222 ALA A CA  
9053  C C   . ALA A 1224 ? 0.4179 0.3676 0.3995 0.0107  0.0114  0.0042  1222 ALA A C   
9054  O O   . ALA A 1224 ? 0.5186 0.4681 0.4995 0.0097  0.0112  0.0038  1222 ALA A O   
9055  C CB  . ALA A 1224 ? 0.3959 0.3462 0.3733 0.0115  0.0112  0.0042  1222 ALA A CB  
9056  N N   . ALA A 1225 ? 0.4204 0.3704 0.4045 0.0108  0.0112  0.0034  1223 ALA A N   
9057  C CA  . ALA A 1225 ? 0.4484 0.3991 0.4345 0.0099  0.0108  0.0017  1223 ALA A CA  
9058  C C   . ALA A 1225 ? 0.5284 0.4781 0.5166 0.0098  0.0110  0.0024  1223 ALA A C   
9059  O O   . ALA A 1225 ? 0.5347 0.4852 0.5244 0.0090  0.0106  0.0009  1223 ALA A O   
9060  C CB  . ALA A 1225 ? 0.4486 0.4001 0.4375 0.0104  0.0104  0.0001  1223 ALA A CB  
9061  N N   . GLY A 1226 ? 0.4583 0.4068 0.4468 0.0104  0.0115  0.0047  1224 GLY A N   
9062  C CA  . GLY A 1226 ? 0.4930 0.4408 0.4836 0.0102  0.0116  0.0056  1224 GLY A CA  
9063  C C   . GLY A 1226 ? 0.5223 0.4694 0.5165 0.0110  0.0118  0.0076  1224 GLY A C   
9064  O O   . GLY A 1226 ? 0.4667 0.4134 0.4629 0.0108  0.0120  0.0089  1224 GLY A O   
9065  N N   . GLY A 1227 ? 0.4156 0.3628 0.4111 0.0117  0.0116  0.0082  1225 GLY A N   
9066  C CA  . GLY A 1227 ? 0.5156 0.4624 0.5150 0.0123  0.0116  0.0107  1225 GLY A CA  
9067  C C   . GLY A 1227 ? 0.4916 0.4391 0.4909 0.0132  0.0115  0.0118  1225 GLY A C   
9068  O O   . GLY A 1227 ? 0.4581 0.4062 0.4544 0.0134  0.0114  0.0102  1225 GLY A O   
9069  N N   . ASN A 1228 ? 0.3979 0.3454 0.4007 0.0137  0.0114  0.0148  1226 ASN A N   
9070  C CA  . ASN A 1228 ? 0.4839 0.4325 0.4872 0.0146  0.0112  0.0167  1226 ASN A CA  
9071  C C   . ASN A 1228 ? 0.4937 0.4410 0.5032 0.0147  0.0100  0.0166  1226 ASN A C   
9072  O O   . ASN A 1228 ? 0.4630 0.4095 0.4777 0.0144  0.0095  0.0186  1226 ASN A O   
9073  C CB  . ASN A 1228 ? 0.4747 0.4253 0.4773 0.0150  0.0120  0.0208  1226 ASN A CB  
9074  C CG  . ASN A 1228 ? 0.5030 0.4555 0.5050 0.0159  0.0119  0.0230  1226 ASN A CG  
9075  O OD1 . ASN A 1228 ? 0.4874 0.4391 0.4924 0.0162  0.0109  0.0229  1226 ASN A OD1 
9076  N ND2 . ASN A 1228 ? 0.4778 0.4332 0.4760 0.0166  0.0128  0.0249  1226 ASN A ND2 
9077  N N   . ALA A 1229 ? 0.4488 0.3960 0.4583 0.0150  0.0093  0.0142  1227 ALA A N   
9078  C CA  . ALA A 1229 ? 0.4292 0.3752 0.4449 0.0153  0.0079  0.0133  1227 ALA A CA  
9079  C C   . ALA A 1229 ? 0.4948 0.4408 0.5149 0.0159  0.0074  0.0178  1227 ALA A C   
9080  O O   . ALA A 1229 ? 0.4796 0.4243 0.5066 0.0158  0.0062  0.0187  1227 ALA A O   
9081  C CB  . ALA A 1229 ? 0.4297 0.3764 0.4440 0.0157  0.0075  0.0100  1227 ALA A CB  
9082  N N   . SER A 1230 ? 0.4972 0.4452 0.5139 0.0164  0.0080  0.0205  1228 SER A N   
9083  C CA  . SER A 1230 ? 0.4927 0.4416 0.5133 0.0169  0.0074  0.0252  1228 SER A CA  
9084  C C   . SER A 1230 ? 0.5888 0.5377 0.6129 0.0163  0.0076  0.0289  1228 SER A C   
9085  O O   . SER A 1230 ? 0.5551 0.5035 0.5859 0.0162  0.0064  0.0322  1228 SER A O   
9086  C CB  . SER A 1230 ? 0.5446 0.4965 0.5601 0.0176  0.0081  0.0273  1228 SER A CB  
9087  N N   . LEU A 1231 ? 0.4642 0.4138 0.4844 0.0158  0.0089  0.0286  1229 LEU A N   
9088  C CA  . LEU A 1231 ? 0.5551 0.5052 0.5785 0.0151  0.0091  0.0319  1229 LEU A CA  
9089  C C   . LEU A 1231 ? 0.5888 0.5358 0.6186 0.0144  0.0080  0.0303  1229 LEU A C   
9090  O O   . LEU A 1231 ? 0.5752 0.5222 0.6094 0.0138  0.0078  0.0334  1229 LEU A O   
9091  C CB  . LEU A 1231 ? 0.5109 0.4631 0.5282 0.0150  0.0108  0.0321  1229 LEU A CB  
9092  C CG  . LEU A 1231 ? 0.5623 0.5187 0.5749 0.0158  0.0120  0.0349  1229 LEU A CG  
9093  C CD1 . LEU A 1231 ? 0.4820 0.4403 0.4903 0.0157  0.0134  0.0348  1229 LEU A CD1 
9094  C CD2 . LEU A 1231 ? 0.5705 0.5293 0.5875 0.0159  0.0115  0.0405  1229 LEU A CD2 
9095  N N   . MET A 1232 ? 0.5895 0.5343 0.6201 0.0144  0.0071  0.0254  1230 MET A N   
9096  C CA  . MET A 1232 ? 0.5891 0.5314 0.6264 0.0139  0.0057  0.0233  1230 MET A CA  
9097  C C   . MET A 1232 ? 0.6348 0.5760 0.6809 0.0141  0.0040  0.0264  1230 MET A C   
9098  O O   . MET A 1232 ? 0.5669 0.5063 0.6200 0.0136  0.0027  0.0261  1230 MET A O   
9099  C CB  . MET A 1232 ? 0.5409 0.4823 0.5772 0.0141  0.0052  0.0173  1230 MET A CB  
9100  N N   . ALA A 1233 ? 0.6935 0.6358 0.7400 0.0147  0.0037  0.0295  1231 ALA A N   
9101  C CA  . ALA A 1233 ? 0.7123 0.6538 0.7673 0.0148  0.0020  0.0333  1231 ALA A CA  
9102  C C   . ALA A 1233 ? 0.7466 0.6905 0.8027 0.0143  0.0025  0.0403  1231 ALA A C   
9103  O O   . ALA A 1233 ? 0.7783 0.7222 0.8413 0.0143  0.0011  0.0447  1231 ALA A O   
9104  C CB  . ALA A 1233 ? 0.6983 0.6399 0.7540 0.0159  0.0010  0.0326  1231 ALA A CB  
9105  N N   . ILE A 1234 ? 0.7066 0.6530 0.7564 0.0139  0.0045  0.0416  1232 ILE A N   
9106  C CA  . ILE A 1234 ? 0.6795 0.6295 0.7296 0.0135  0.0053  0.0480  1232 ILE A CA  
9107  C C   . ILE A 1234 ? 0.6333 0.5825 0.6869 0.0124  0.0055  0.0489  1232 ILE A C   
9108  O O   . ILE A 1234 ? 0.5696 0.5191 0.6181 0.0122  0.0069  0.0463  1232 ILE A O   
9109  C CB  . ILE A 1234 ? 0.5981 0.5524 0.6389 0.0141  0.0074  0.0489  1232 ILE A CB  
9110  C CG1 . ILE A 1234 ? 0.6610 0.6160 0.6990 0.0152  0.0071  0.0481  1232 ILE A CG1 
9111  C CG2 . ILE A 1234 ? 0.4855 0.4444 0.5267 0.0137  0.0083  0.0553  1232 ILE A CG2 
9112  C CD1 . ILE A 1234 ? 0.5608 0.5211 0.5931 0.0158  0.0084  0.0516  1232 ILE A CD1 
9113  N N   . GLY A 1235 ? 0.5957 0.5438 0.6585 0.0117  0.0038  0.0527  1233 GLY A N   
9114  C CA  . GLY A 1235 ? 0.4854 0.4331 0.5527 0.0105  0.0037  0.0543  1233 GLY A CA  
9115  C C   . GLY A 1235 ? 0.4728 0.4233 0.5462 0.0097  0.0032  0.0622  1233 GLY A C   
9116  O O   . GLY A 1235 ? 0.5767 0.5271 0.6552 0.0099  0.0017  0.0655  1233 GLY A O   
9117  O OXT . GLY A 1235 ? 0.3176 0.2708 0.3912 0.0088  0.0042  0.0657  1233 GLY A OXT 
9118  N N   . ALA B 16   ? 0.5766 0.5106 0.5779 0.0462  -0.0047 -0.0169 14   ALA B N   
9119  C CA  . ALA B 16   ? 0.5707 0.5084 0.5719 0.0422  -0.0050 -0.0168 14   ALA B CA  
9120  C C   . ALA B 16   ? 0.5477 0.4794 0.5425 0.0390  -0.0056 -0.0172 14   ALA B C   
9121  O O   . ALA B 16   ? 0.5644 0.4907 0.5552 0.0394  -0.0047 -0.0184 14   ALA B O   
9122  C CB  . ALA B 16   ? 0.5112 0.4546 0.5155 0.0420  -0.0029 -0.0178 14   ALA B CB  
9123  N N   . PRO B 17   ? 0.5280 0.4609 0.5219 0.0358  -0.0071 -0.0162 15   PRO B N   
9124  C CA  . PRO B 17   ? 0.4959 0.4240 0.4843 0.0324  -0.0076 -0.0165 15   PRO B CA  
9125  C C   . PRO B 17   ? 0.4548 0.3839 0.4419 0.0308  -0.0059 -0.0180 15   PRO B C   
9126  O O   . PRO B 17   ? 0.4509 0.3860 0.4417 0.0309  -0.0047 -0.0185 15   PRO B O   
9127  C CB  . PRO B 17   ? 0.5319 0.4631 0.5210 0.0297  -0.0092 -0.0150 15   PRO B CB  
9128  C CG  . PRO B 17   ? 0.5764 0.5151 0.5714 0.0310  -0.0091 -0.0147 15   PRO B CG  
9129  C CD  . PRO B 17   ? 0.5225 0.4612 0.5204 0.0351  -0.0084 -0.0149 15   PRO B CD  
9130  N N   . ALA B 18   ? 0.4103 0.3333 0.3921 0.0293  -0.0058 -0.0188 16   ALA B N   
9131  C CA  . ALA B 18   ? 0.4021 0.3255 0.3821 0.0276  -0.0044 -0.0203 16   ALA B CA  
9132  C C   . ALA B 18   ? 0.3573 0.2863 0.3389 0.0244  -0.0047 -0.0198 16   ALA B C   
9133  O O   . ALA B 18   ? 0.3848 0.3143 0.3661 0.0223  -0.0061 -0.0186 16   ALA B O   
9134  C CB  . ALA B 18   ? 0.3802 0.2956 0.3538 0.0261  -0.0048 -0.0210 16   ALA B CB  
9135  N N   . PRO B 19   ? 0.3276 0.2609 0.3109 0.0239  -0.0033 -0.0208 17   PRO B N   
9136  C CA  . PRO B 19   ? 0.3100 0.2487 0.2950 0.0212  -0.0035 -0.0204 17   PRO B CA  
9137  C C   . PRO B 19   ? 0.3118 0.2477 0.2928 0.0176  -0.0046 -0.0201 17   PRO B C   
9138  O O   . PRO B 19   ? 0.3304 0.2615 0.3071 0.0165  -0.0045 -0.0209 17   PRO B O   
9139  C CB  . PRO B 19   ? 0.3306 0.2724 0.3167 0.0216  -0.0017 -0.0217 17   PRO B CB  
9140  C CG  . PRO B 19   ? 0.3539 0.2946 0.3413 0.0252  -0.0005 -0.0223 17   PRO B CG  
9141  C CD  . PRO B 19   ? 0.3580 0.2917 0.3420 0.0263  -0.0013 -0.0222 17   PRO B CD  
9142  N N   . PHE B 20   ? 0.3083 0.2476 0.2907 0.0158  -0.0056 -0.0189 18   PHE B N   
9143  C CA  . PHE B 20   ? 0.2811 0.2194 0.2607 0.0122  -0.0065 -0.0184 18   PHE B CA  
9144  C C   . PHE B 20   ? 0.3265 0.2579 0.3016 0.0112  -0.0077 -0.0179 18   PHE B C   
9145  O O   . PHE B 20   ? 0.3545 0.2846 0.3269 0.0081  -0.0083 -0.0175 18   PHE B O   
9146  C CB  . PHE B 20   ? 0.2949 0.2350 0.2735 0.0101  -0.0057 -0.0194 18   PHE B CB  
9147  C CG  . PHE B 20   ? 0.2707 0.2173 0.2532 0.0107  -0.0047 -0.0198 18   PHE B CG  
9148  C CD1 . PHE B 20   ? 0.2655 0.2173 0.2508 0.0097  -0.0050 -0.0189 18   PHE B CD1 
9149  C CD2 . PHE B 20   ? 0.2899 0.2372 0.2733 0.0124  -0.0033 -0.0210 18   PHE B CD2 
9150  C CE1 . PHE B 20   ? 0.2945 0.2519 0.2833 0.0102  -0.0042 -0.0193 18   PHE B CE1 
9151  C CE2 . PHE B 20   ? 0.2837 0.2367 0.2705 0.0129  -0.0024 -0.0212 18   PHE B CE2 
9152  C CZ  . PHE B 20   ? 0.2722 0.2301 0.2618 0.0118  -0.0029 -0.0203 18   PHE B CZ  
9153  N N   . ALA B 21   ? 0.3817 0.3088 0.3562 0.0138  -0.0080 -0.0177 19   ALA B N   
9154  C CA  . ALA B 21   ? 0.4112 0.3311 0.3812 0.0130  -0.0091 -0.0172 19   ALA B CA  
9155  C C   . ALA B 21   ? 0.4607 0.3809 0.4300 0.0108  -0.0106 -0.0154 19   ALA B C   
9156  O O   . ALA B 21   ? 0.5177 0.4325 0.4827 0.0088  -0.0115 -0.0148 19   ALA B O   
9157  C CB  . ALA B 21   ? 0.4580 0.3735 0.4278 0.0168  -0.0091 -0.0173 19   ALA B CB  
9158  N N   . ASP B 22   ? 0.3624 0.2885 0.3353 0.0110  -0.0107 -0.0146 20   ASP B N   
9159  C CA  . ASP B 22   ? 0.3830 0.3098 0.3552 0.0091  -0.0119 -0.0130 20   ASP B CA  
9160  C C   . ASP B 22   ? 0.3186 0.2522 0.2932 0.0071  -0.0114 -0.0129 20   ASP B C   
9161  O O   . ASP B 22   ? 0.3409 0.2778 0.3170 0.0069  -0.0120 -0.0119 20   ASP B O   
9162  C CB  . ASP B 22   ? 0.4754 0.4018 0.4491 0.0116  -0.0130 -0.0118 20   ASP B CB  
9163  C CG  . ASP B 22   ? 0.6415 0.5607 0.6124 0.0134  -0.0137 -0.0115 20   ASP B CG  
9164  O OD1 . ASP B 22   ? 0.7545 0.6679 0.7209 0.0116  -0.0140 -0.0115 20   ASP B OD1 
9165  O OD2 . ASP B 22   ? 0.7512 0.6703 0.7243 0.0167  -0.0141 -0.0113 20   ASP B OD2 
9166  N N   . PHE B 23   ? 0.2861 0.2218 0.2608 0.0057  -0.0104 -0.0141 21   PHE B N   
9167  C CA  . PHE B 23   ? 0.2866 0.2291 0.2642 0.0045  -0.0098 -0.0142 21   PHE B CA  
9168  C C   . PHE B 23   ? 0.2669 0.2110 0.2434 0.0018  -0.0105 -0.0129 21   PHE B C   
9169  O O   . PHE B 23   ? 0.2711 0.2194 0.2499 0.0021  -0.0106 -0.0123 21   PHE B O   
9170  C CB  . PHE B 23   ? 0.2635 0.2076 0.2411 0.0034  -0.0087 -0.0155 21   PHE B CB  
9171  C CG  . PHE B 23   ? 0.2444 0.1950 0.2246 0.0022  -0.0082 -0.0156 21   PHE B CG  
9172  C CD1 . PHE B 23   ? 0.2579 0.2132 0.2420 0.0041  -0.0077 -0.0157 21   PHE B CD1 
9173  C CD2 . PHE B 23   ? 0.2752 0.2273 0.2541 -0.0009 -0.0082 -0.0154 21   PHE B CD2 
9174  C CE1 . PHE B 23   ? 0.2583 0.2192 0.2447 0.0032  -0.0073 -0.0158 21   PHE B CE1 
9175  C CE2 . PHE B 23   ? 0.2769 0.2350 0.2583 -0.0016 -0.0077 -0.0155 21   PHE B CE2 
9176  C CZ  . PHE B 23   ? 0.2660 0.2282 0.2510 0.0004  -0.0072 -0.0157 21   PHE B CZ  
9177  N N   . ALA B 24   ? 0.2555 0.1964 0.2285 -0.0010 -0.0108 -0.0125 22   ALA B N   
9178  C CA  . ALA B 24   ? 0.2589 0.2016 0.2309 -0.0037 -0.0112 -0.0112 22   ALA B CA  
9179  C C   . ALA B 24   ? 0.2660 0.2031 0.2336 -0.0062 -0.0120 -0.0104 22   ALA B C   
9180  O O   . ALA B 24   ? 0.2896 0.2279 0.2560 -0.0093 -0.0118 -0.0101 22   ALA B O   
9181  C CB  . ALA B 24   ? 0.2998 0.2487 0.2739 -0.0053 -0.0103 -0.0117 22   ALA B CB  
9182  N N   . PRO B 25   ? 0.2868 0.2177 0.2519 -0.0051 -0.0129 -0.0097 23   PRO B N   
9183  C CA  . PRO B 25   ? 0.3285 0.2535 0.2891 -0.0076 -0.0137 -0.0088 23   PRO B CA  
9184  C C   . PRO B 25   ? 0.3198 0.2470 0.2794 -0.0106 -0.0139 -0.0072 23   PRO B C   
9185  O O   . PRO B 25   ? 0.3207 0.2511 0.2817 -0.0098 -0.0141 -0.0064 23   PRO B O   
9186  C CB  . PRO B 25   ? 0.3700 0.2888 0.3289 -0.0050 -0.0147 -0.0083 23   PRO B CB  
9187  C CG  . PRO B 25   ? 0.3528 0.2758 0.3153 -0.0020 -0.0147 -0.0082 23   PRO B CG  
9188  C CD  . PRO B 25   ? 0.3110 0.2406 0.2774 -0.0015 -0.0134 -0.0096 23   PRO B CD  
9189  N N   . PRO B 26   ? 0.3102 0.2359 0.2673 -0.0142 -0.0140 -0.0068 24   PRO B N   
9190  C CA  . PRO B 26   ? 0.3121 0.2401 0.2682 -0.0172 -0.0140 -0.0051 24   PRO B CA  
9191  C C   . PRO B 26   ? 0.3149 0.2381 0.2680 -0.0170 -0.0151 -0.0034 24   PRO B C   
9192  O O   . PRO B 26   ? 0.3274 0.2441 0.2784 -0.0153 -0.0160 -0.0033 24   PRO B O   
9193  C CB  . PRO B 26   ? 0.3425 0.2692 0.2966 -0.0210 -0.0140 -0.0051 24   PRO B CB  
9194  C CG  . PRO B 26   ? 0.3471 0.2671 0.2989 -0.0201 -0.0146 -0.0062 24   PRO B CG  
9195  C CD  . PRO B 26   ? 0.3440 0.2654 0.2987 -0.0158 -0.0141 -0.0077 24   PRO B CD  
9196  N N   . VAL B 27   ? 0.3206 0.2470 0.2734 -0.0186 -0.0149 -0.0019 25   VAL B N   
9197  C CA  . VAL B 27   ? 0.3397 0.2618 0.2893 -0.0188 -0.0159 0.0000  25   VAL B CA  
9198  C C   . VAL B 27   ? 0.3303 0.2446 0.2754 -0.0211 -0.0168 0.0009  25   VAL B C   
9199  O O   . VAL B 27   ? 0.3688 0.2767 0.3110 -0.0198 -0.0180 0.0019  25   VAL B O   
9200  C CB  . VAL B 27   ? 0.3080 0.2352 0.2577 -0.0206 -0.0154 0.0013  25   VAL B CB  
9201  C CG1 . VAL B 27   ? 0.3505 0.2727 0.2960 -0.0216 -0.0164 0.0035  25   VAL B CG1 
9202  C CG2 . VAL B 27   ? 0.3288 0.2622 0.2823 -0.0179 -0.0149 0.0004  25   VAL B CG2 
9203  N N   . ARG B 28   ? 0.3208 0.2353 0.2650 -0.0244 -0.0164 0.0007  26   ARG B N   
9204  C CA  . ARG B 28   ? 0.3375 0.2446 0.2774 -0.0270 -0.0173 0.0015  26   ARG B CA  
9205  C C   . ARG B 28   ? 0.3965 0.3041 0.3369 -0.0290 -0.0169 0.0000  26   ARG B C   
9206  O O   . ARG B 28   ? 0.3475 0.2621 0.2916 -0.0291 -0.0158 -0.0011 26   ARG B O   
9207  C CB  . ARG B 28   ? 0.3596 0.2662 0.2966 -0.0307 -0.0174 0.0039  26   ARG B CB  
9208  C CG  . ARG B 28   ? 0.3769 0.2911 0.3161 -0.0340 -0.0161 0.0041  26   ARG B CG  
9209  C CD  . ARG B 28   ? 0.3838 0.2982 0.3204 -0.0373 -0.0159 0.0065  26   ARG B CD  
9210  N NE  . ARG B 28   ? 0.3987 0.3156 0.3356 -0.0351 -0.0157 0.0074  26   ARG B NE  
9211  C CZ  . ARG B 28   ? 0.4894 0.4008 0.4231 -0.0340 -0.0168 0.0088  26   ARG B CZ  
9212  N NH1 . ARG B 28   ? 0.4742 0.3771 0.4039 -0.0348 -0.0181 0.0097  26   ARG B NH1 
9213  N NH2 . ARG B 28   ? 0.4344 0.3488 0.3687 -0.0319 -0.0167 0.0094  26   ARG B NH2 
9214  N N   . PRO B 29   ? 0.3701 0.2702 0.3068 -0.0304 -0.0178 -0.0001 27   PRO B N   
9215  C CA  . PRO B 29   ? 0.3706 0.2709 0.3072 -0.0330 -0.0176 -0.0012 27   PRO B CA  
9216  C C   . PRO B 29   ? 0.3363 0.2431 0.2743 -0.0372 -0.0170 -0.0002 27   PRO B C   
9217  O O   . PRO B 29   ? 0.3593 0.2661 0.2958 -0.0395 -0.0170 0.0018  27   PRO B O   
9218  C CB  . PRO B 29   ? 0.4305 0.3206 0.3619 -0.0344 -0.0190 -0.0010 27   PRO B CB  
9219  C CG  . PRO B 29   ? 0.4380 0.3227 0.3678 -0.0306 -0.0196 -0.0005 27   PRO B CG  
9220  C CD  . PRO B 29   ? 0.4101 0.3006 0.3423 -0.0297 -0.0191 0.0009  27   PRO B CD  
9221  N N   . GLN B 30   ? 0.3287 0.2411 0.2697 -0.0379 -0.0163 -0.0015 28   GLN B N   
9222  C CA  . GLN B 30   ? 0.3444 0.2643 0.2878 -0.0413 -0.0155 -0.0007 28   GLN B CA  
9223  C C   . GLN B 30   ? 0.3312 0.2476 0.2716 -0.0462 -0.0163 0.0002  28   GLN B C   
9224  O O   . GLN B 30   ? 0.3604 0.2734 0.2995 -0.0471 -0.0170 -0.0011 28   GLN B O   
9225  C CB  . GLN B 30   ? 0.3353 0.2627 0.2831 -0.0399 -0.0146 -0.0025 28   GLN B CB  
9226  C CG  . GLN B 30   ? 0.3325 0.2631 0.2833 -0.0353 -0.0138 -0.0034 28   GLN B CG  
9227  C CD  . GLN B 30   ? 0.3371 0.2724 0.2893 -0.0348 -0.0131 -0.0021 28   GLN B CD  
9228  O OE1 . GLN B 30   ? 0.3233 0.2658 0.2782 -0.0361 -0.0121 -0.0017 28   GLN B OE1 
9229  N NE2 . GLN B 30   ? 0.2917 0.2229 0.2421 -0.0327 -0.0136 -0.0013 28   GLN B NE2 
9230  N N   . SER B 31   ? 0.3310 0.2485 0.2703 -0.0494 -0.0161 0.0024  29   SER B N   
9231  C CA  . SER B 31   ? 0.3256 0.2404 0.2623 -0.0544 -0.0168 0.0035  29   SER B CA  
9232  C C   . SER B 31   ? 0.3302 0.2525 0.2705 -0.0570 -0.0163 0.0028  29   SER B C   
9233  O O   . SER B 31   ? 0.3180 0.2477 0.2625 -0.0548 -0.0153 0.0017  29   SER B O   
9234  C CB  . SER B 31   ? 0.3296 0.2449 0.2648 -0.0571 -0.0164 0.0062  29   SER B CB  
9235  O OG  . SER B 31   ? 0.3427 0.2679 0.2819 -0.0573 -0.0148 0.0068  29   SER B OG  
9236  N N   . THR B 32   ? 0.3316 0.2515 0.2699 -0.0616 -0.0172 0.0035  30   THR B N   
9237  C CA  . THR B 32   ? 0.3521 0.2793 0.2938 -0.0646 -0.0170 0.0032  30   THR B CA  
9238  C C   . THR B 32   ? 0.3007 0.2384 0.2469 -0.0646 -0.0152 0.0043  30   THR B C   
9239  O O   . THR B 32   ? 0.3182 0.2635 0.2687 -0.0635 -0.0145 0.0032  30   THR B O   
9240  C CB  . THR B 32   ? 0.3721 0.2953 0.3109 -0.0701 -0.0182 0.0044  30   THR B CB  
9241  O OG1 . THR B 32   ? 0.4302 0.3436 0.3647 -0.0699 -0.0199 0.0030  30   THR B OG1 
9242  C CG2 . THR B 32   ? 0.4224 0.3541 0.3651 -0.0736 -0.0180 0.0045  30   THR B CG2 
9243  N N   . LEU B 33   ? 0.3218 0.2598 0.2669 -0.0656 -0.0145 0.0064  31   LEU B N   
9244  C CA  . LEU B 33   ? 0.3291 0.2767 0.2780 -0.0655 -0.0126 0.0073  31   LEU B CA  
9245  C C   . LEU B 33   ? 0.3003 0.2522 0.2522 -0.0603 -0.0117 0.0058  31   LEU B C   
9246  O O   . LEU B 33   ? 0.2779 0.2384 0.2341 -0.0596 -0.0104 0.0054  31   LEU B O   
9247  C CB  . LEU B 33   ? 0.3005 0.2468 0.2469 -0.0677 -0.0121 0.0099  31   LEU B CB  
9248  C CG  . LEU B 33   ? 0.3216 0.2658 0.2660 -0.0734 -0.0128 0.0116  31   LEU B CG  
9249  C CD1 . LEU B 33   ? 0.3518 0.2924 0.2925 -0.0754 -0.0124 0.0142  31   LEU B CD1 
9250  C CD2 . LEU B 33   ? 0.3847 0.3389 0.3338 -0.0763 -0.0118 0.0119  31   LEU B CD2 
9251  N N   . ARG B 34   ? 0.2826 0.2284 0.2324 -0.0566 -0.0122 0.0050  32   ARG B N   
9252  C CA  . ARG B 34   ? 0.2785 0.2282 0.2312 -0.0519 -0.0114 0.0035  32   ARG B CA  
9253  C C   . ARG B 34   ? 0.2868 0.2402 0.2428 -0.0507 -0.0114 0.0015  32   ARG B C   
9254  O O   . ARG B 34   ? 0.2765 0.2368 0.2364 -0.0484 -0.0104 0.0006  32   ARG B O   
9255  C CB  . ARG B 34   ? 0.2859 0.2285 0.2359 -0.0484 -0.0121 0.0032  32   ARG B CB  
9256  C CG  . ARG B 34   ? 0.3014 0.2414 0.2486 -0.0487 -0.0120 0.0052  32   ARG B CG  
9257  C CD  . ARG B 34   ? 0.3147 0.2622 0.2646 -0.0471 -0.0105 0.0056  32   ARG B CD  
9258  N NE  . ARG B 34   ? 0.3020 0.2513 0.2543 -0.0425 -0.0104 0.0038  32   ARG B NE  
9259  C CZ  . ARG B 34   ? 0.3103 0.2561 0.2613 -0.0394 -0.0109 0.0038  32   ARG B CZ  
9260  N NH1 . ARG B 34   ? 0.3149 0.2550 0.2619 -0.0401 -0.0116 0.0055  32   ARG B NH1 
9261  N NH2 . ARG B 34   ? 0.3124 0.2604 0.2662 -0.0356 -0.0107 0.0022  32   ARG B NH2 
9262  N N   . ARG B 35   ? 0.2890 0.2375 0.2432 -0.0521 -0.0127 0.0006  33   ARG B N   
9263  C CA  . ARG B 35   ? 0.3104 0.2621 0.2673 -0.0510 -0.0128 -0.0014 33   ARG B CA  
9264  C C   . ARG B 35   ? 0.2730 0.2337 0.2338 -0.0533 -0.0121 -0.0010 33   ARG B C   
9265  O O   . ARG B 35   ? 0.2788 0.2450 0.2431 -0.0514 -0.0116 -0.0023 33   ARG B O   
9266  C CB  . ARG B 35   ? 0.3183 0.2624 0.2718 -0.0524 -0.0144 -0.0023 33   ARG B CB  
9267  C CG  . ARG B 35   ? 0.3616 0.2976 0.3120 -0.0490 -0.0150 -0.0033 33   ARG B CG  
9268  C CD  . ARG B 35   ? 0.4309 0.3589 0.3775 -0.0504 -0.0165 -0.0043 33   ARG B CD  
9269  N NE  . ARG B 35   ? 0.5109 0.4311 0.4546 -0.0469 -0.0168 -0.0051 33   ARG B NE  
9270  C CZ  . ARG B 35   ? 0.6064 0.5266 0.5513 -0.0427 -0.0164 -0.0068 33   ARG B CZ  
9271  N NH1 . ARG B 35   ? 0.6179 0.5447 0.5665 -0.0415 -0.0157 -0.0081 33   ARG B NH1 
9272  N NH2 . ARG B 35   ? 0.5516 0.4652 0.4942 -0.0396 -0.0167 -0.0072 33   ARG B NH2 
9273  N N   . ALA B 36   ? 0.2717 0.2343 0.2321 -0.0575 -0.0120 0.0009  34   ALA B N   
9274  C CA  . ALA B 36   ? 0.2766 0.2485 0.2412 -0.0597 -0.0112 0.0014  34   ALA B CA  
9275  C C   . ALA B 36   ? 0.2715 0.2511 0.2398 -0.0568 -0.0094 0.0015  34   ALA B C   
9276  O O   . ALA B 36   ? 0.2967 0.2840 0.2691 -0.0564 -0.0087 0.0010  34   ALA B O   
9277  C CB  . ALA B 36   ? 0.2780 0.2501 0.2414 -0.0649 -0.0115 0.0035  34   ALA B CB  
9278  N N   . ILE B 37   ? 0.2636 0.2410 0.2303 -0.0547 -0.0087 0.0021  35   ILE B N   
9279  C CA  . ILE B 37   ? 0.2520 0.2354 0.2215 -0.0515 -0.0071 0.0018  35   ILE B CA  
9280  C C   . ILE B 37   ? 0.2576 0.2425 0.2296 -0.0476 -0.0072 -0.0003 35   ILE B C   
9281  O O   . ILE B 37   ? 0.2355 0.2277 0.2114 -0.0465 -0.0063 -0.0009 35   ILE B O   
9282  C CB  . ILE B 37   ? 0.2673 0.2468 0.2339 -0.0501 -0.0068 0.0028  35   ILE B CB  
9283  C CG1 . ILE B 37   ? 0.2571 0.2363 0.2215 -0.0540 -0.0064 0.0051  35   ILE B CG1 
9284  C CG2 . ILE B 37   ? 0.2447 0.2289 0.2136 -0.0462 -0.0055 0.0021  35   ILE B CG2 
9285  C CD1 . ILE B 37   ? 0.2775 0.2507 0.2378 -0.0531 -0.0065 0.0063  35   ILE B CD1 
9286  N N   . THR B 38   ? 0.2342 0.2122 0.2039 -0.0456 -0.0083 -0.0015 36   THR B N   
9287  C CA  . THR B 38   ? 0.2465 0.2256 0.2183 -0.0419 -0.0083 -0.0034 36   THR B CA  
9288  C C   . THR B 38   ? 0.2362 0.2199 0.2107 -0.0428 -0.0084 -0.0043 36   THR B C   
9289  O O   . THR B 38   ? 0.2471 0.2358 0.2248 -0.0404 -0.0078 -0.0054 36   THR B O   
9290  C CB  . THR B 38   ? 0.2379 0.2086 0.2066 -0.0399 -0.0093 -0.0043 36   THR B CB  
9291  O OG1 . THR B 38   ? 0.2571 0.2236 0.2232 -0.0394 -0.0094 -0.0032 36   THR B OG1 
9292  C CG2 . THR B 38   ? 0.3015 0.2734 0.2724 -0.0359 -0.0091 -0.0061 36   THR B CG2 
9293  N N   . ALA B 39   ? 0.2510 0.2331 0.2242 -0.0465 -0.0094 -0.0039 37   ALA B N   
9294  C CA  . ALA B 39   ? 0.2649 0.2511 0.2405 -0.0477 -0.0099 -0.0047 37   ALA B CA  
9295  C C   . ALA B 39   ? 0.2681 0.2640 0.2483 -0.0477 -0.0087 -0.0042 37   ALA B C   
9296  O O   . ALA B 39   ? 0.2726 0.2730 0.2556 -0.0470 -0.0089 -0.0051 37   ALA B O   
9297  C CB  . ALA B 39   ? 0.2887 0.2714 0.2618 -0.0522 -0.0113 -0.0041 37   ALA B CB  
9298  N N   . ALA B 40   ? 0.2334 0.2328 0.2144 -0.0483 -0.0075 -0.0028 38   ALA B N   
9299  C CA  . ALA B 40   ? 0.2487 0.2574 0.2339 -0.0484 -0.0062 -0.0022 38   ALA B CA  
9300  C C   . ALA B 40   ? 0.2158 0.2279 0.2032 -0.0440 -0.0049 -0.0031 38   ALA B C   
9301  O O   . ALA B 40   ? 0.2372 0.2568 0.2282 -0.0434 -0.0038 -0.0029 38   ALA B O   
9302  C CB  . ALA B 40   ? 0.2552 0.2663 0.2401 -0.0515 -0.0053 -0.0001 38   ALA B CB  
9303  N N   . TYR B 41   ? 0.2249 0.2315 0.2103 -0.0410 -0.0051 -0.0041 39   TYR B N   
9304  C CA  . TYR B 41   ? 0.2162 0.2249 0.2029 -0.0373 -0.0040 -0.0047 39   TYR B CA  
9305  C C   . TYR B 41   ? 0.2197 0.2358 0.2107 -0.0356 -0.0032 -0.0054 39   TYR B C   
9306  O O   . TYR B 41   ? 0.2298 0.2509 0.2226 -0.0344 -0.0019 -0.0051 39   TYR B O   
9307  C CB  . TYR B 41   ? 0.2216 0.2238 0.2063 -0.0345 -0.0048 -0.0059 39   TYR B CB  
9308  C CG  . TYR B 41   ? 0.2393 0.2408 0.2238 -0.0313 -0.0041 -0.0061 39   TYR B CG  
9309  C CD1 . TYR B 41   ? 0.2478 0.2551 0.2346 -0.0297 -0.0028 -0.0061 39   TYR B CD1 
9310  C CD2 . TYR B 41   ? 0.2491 0.2441 0.2311 -0.0296 -0.0049 -0.0065 39   TYR B CD2 
9311  C CE1 . TYR B 41   ? 0.2212 0.2275 0.2076 -0.0269 -0.0024 -0.0064 39   TYR B CE1 
9312  C CE2 . TYR B 41   ? 0.2392 0.2336 0.2211 -0.0268 -0.0045 -0.0067 39   TYR B CE2 
9313  C CZ  . TYR B 41   ? 0.2284 0.2283 0.2124 -0.0256 -0.0033 -0.0067 39   TYR B CZ  
9314  O OH  . TYR B 41   ? 0.2401 0.2391 0.2237 -0.0230 -0.0031 -0.0070 39   TYR B OH  
9315  N N   . ARG B 42   ? 0.2364 0.2531 0.2287 -0.0354 -0.0041 -0.0064 40   ARG B N   
9316  C CA  . ARG B 42   ? 0.2311 0.2543 0.2272 -0.0336 -0.0036 -0.0071 40   ARG B CA  
9317  C C   . ARG B 42   ? 0.2365 0.2636 0.2345 -0.0362 -0.0043 -0.0068 40   ARG B C   
9318  O O   . ARG B 42   ? 0.2576 0.2876 0.2578 -0.0349 -0.0047 -0.0077 40   ARG B O   
9319  C CB  . ARG B 42   ? 0.2619 0.2828 0.2582 -0.0300 -0.0038 -0.0087 40   ARG B CB  
9320  C CG  . ARG B 42   ? 0.2559 0.2744 0.2511 -0.0274 -0.0030 -0.0088 40   ARG B CG  
9321  C CD  . ARG B 42   ? 0.2595 0.2752 0.2548 -0.0241 -0.0033 -0.0102 40   ARG B CD  
9322  N NE  . ARG B 42   ? 0.2535 0.2655 0.2469 -0.0226 -0.0030 -0.0102 40   ARG B NE  
9323  C CZ  . ARG B 42   ? 0.2364 0.2507 0.2307 -0.0208 -0.0021 -0.0101 40   ARG B CZ  
9324  N NH1 . ARG B 42   ? 0.2390 0.2593 0.2360 -0.0199 -0.0012 -0.0102 40   ARG B NH1 
9325  N NH2 . ARG B 42   ? 0.2358 0.2463 0.2281 -0.0198 -0.0022 -0.0099 40   ARG B NH2 
9326  N N   . ARG B 43   ? 0.2269 0.2543 0.2241 -0.0400 -0.0046 -0.0055 41   ARG B N   
9327  C CA  . ARG B 43   ? 0.2293 0.2603 0.2282 -0.0431 -0.0055 -0.0051 41   ARG B CA  
9328  C C   . ARG B 43   ? 0.2365 0.2766 0.2403 -0.0418 -0.0047 -0.0050 41   ARG B C   
9329  O O   . ARG B 43   ? 0.2524 0.2968 0.2579 -0.0403 -0.0030 -0.0045 41   ARG B O   
9330  C CB  . ARG B 43   ? 0.2306 0.2611 0.2281 -0.0474 -0.0057 -0.0034 41   ARG B CB  
9331  C CG  . ARG B 43   ? 0.2261 0.2606 0.2256 -0.0512 -0.0068 -0.0028 41   ARG B CG  
9332  C CD  . ARG B 43   ? 0.2488 0.2800 0.2457 -0.0557 -0.0074 -0.0013 41   ARG B CD  
9333  N NE  . ARG B 43   ? 0.2717 0.2929 0.2636 -0.0560 -0.0087 -0.0020 41   ARG B NE  
9334  C CZ  . ARG B 43   ? 0.3230 0.3384 0.3113 -0.0582 -0.0088 -0.0010 41   ARG B CZ  
9335  N NH1 . ARG B 43   ? 0.2625 0.2811 0.2513 -0.0604 -0.0077 0.0008  41   ARG B NH1 
9336  N NH2 . ARG B 43   ? 0.2820 0.2883 0.2659 -0.0581 -0.0101 -0.0018 41   ARG B NH2 
9337  N N   . PRO B 44   ? 0.2409 0.2838 0.2466 -0.0423 -0.0058 -0.0055 42   PRO B N   
9338  C CA  . PRO B 44   ? 0.2472 0.2989 0.2577 -0.0410 -0.0051 -0.0053 42   PRO B CA  
9339  C C   . PRO B 44   ? 0.2245 0.2827 0.2374 -0.0430 -0.0038 -0.0037 42   PRO B C   
9340  O O   . PRO B 44   ? 0.2247 0.2822 0.2365 -0.0469 -0.0041 -0.0025 42   PRO B O   
9341  C CB  . PRO B 44   ? 0.2543 0.3071 0.2657 -0.0425 -0.0070 -0.0057 42   PRO B CB  
9342  C CG  . PRO B 44   ? 0.2870 0.3308 0.2939 -0.0421 -0.0082 -0.0069 42   PRO B CG  
9343  C CD  . PRO B 44   ? 0.2521 0.2902 0.2556 -0.0434 -0.0077 -0.0064 42   PRO B CD  
9344  N N   . GLU B 45   ? 0.2324 0.2970 0.2487 -0.0404 -0.0022 -0.0036 43   GLU B N   
9345  C CA  . GLU B 45   ? 0.2289 0.3001 0.2476 -0.0416 -0.0005 -0.0022 43   GLU B CA  
9346  C C   . GLU B 45   ? 0.2462 0.3230 0.2678 -0.0456 -0.0014 -0.0009 43   GLU B C   
9347  O O   . GLU B 45   ? 0.2725 0.3520 0.2946 -0.0486 -0.0006 0.0006  43   GLU B O   
9348  C CB  . GLU B 45   ? 0.2867 0.3634 0.3084 -0.0376 0.0012  -0.0027 43   GLU B CB  
9349  C CG  . GLU B 45   ? 0.3213 0.4015 0.3434 -0.0374 0.0034  -0.0017 43   GLU B CG  
9350  C CD  . GLU B 45   ? 0.2170 0.2979 0.2394 -0.0329 0.0050  -0.0027 43   GLU B CD  
9351  O OE1 . GLU B 45   ? 0.2181 0.2960 0.2401 -0.0299 0.0043  -0.0042 43   GLU B OE1 
9352  O OE2 . GLU B 45   ? 0.2391 0.3237 0.2620 -0.0326 0.0070  -0.0021 43   GLU B OE2 
9353  N N   . THR B 46   ? 0.2308 0.3092 0.2541 -0.0458 -0.0031 -0.0015 44   THR B N   
9354  C CA  . THR B 46   ? 0.2455 0.3291 0.2716 -0.0497 -0.0043 -0.0003 44   THR B CA  
9355  C C   . THR B 46   ? 0.2431 0.3210 0.2657 -0.0543 -0.0056 0.0004  44   THR B C   
9356  O O   . THR B 46   ? 0.2651 0.3473 0.2896 -0.0583 -0.0063 0.0017  44   THR B O   
9357  C CB  . THR B 46   ? 0.2581 0.3439 0.2862 -0.0487 -0.0061 -0.0012 44   THR B CB  
9358  O OG1 . THR B 46   ? 0.2591 0.3362 0.2829 -0.0473 -0.0074 -0.0027 44   THR B OG1 
9359  C CG2 . THR B 46   ? 0.2647 0.3577 0.2972 -0.0447 -0.0048 -0.0014 44   THR B CG2 
9360  N N   . GLU B 47   ? 0.2469 0.3153 0.2644 -0.0540 -0.0062 -0.0005 45   GLU B N   
9361  C CA  . GLU B 47   ? 0.2643 0.3267 0.2781 -0.0582 -0.0073 0.0002  45   GLU B CA  
9362  C C   . GLU B 47   ? 0.2536 0.3155 0.2661 -0.0596 -0.0056 0.0016  45   GLU B C   
9363  O O   . GLU B 47   ? 0.3022 0.3631 0.3136 -0.0640 -0.0061 0.0030  45   GLU B O   
9364  C CB  . GLU B 47   ? 0.2503 0.3025 0.2591 -0.0572 -0.0088 -0.0013 45   GLU B CB  
9365  C CG  . GLU B 47   ? 0.3434 0.3950 0.3524 -0.0564 -0.0106 -0.0027 45   GLU B CG  
9366  C CD  . GLU B 47   ? 0.4090 0.4508 0.4131 -0.0550 -0.0116 -0.0042 45   GLU B CD  
9367  O OE1 . GLU B 47   ? 0.4173 0.4523 0.4176 -0.0561 -0.0115 -0.0040 45   GLU B OE1 
9368  O OE2 . GLU B 47   ? 0.4509 0.4920 0.4551 -0.0526 -0.0123 -0.0056 45   GLU B OE2 
9369  N N   . CYS B 48   ? 0.2306 0.2931 0.2431 -0.0561 -0.0036 0.0014  46   CYS B N   
9370  C CA  . CYS B 48   ? 0.2407 0.3022 0.2514 -0.0571 -0.0020 0.0027  46   CYS B CA  
9371  C C   . CYS B 48   ? 0.2276 0.2980 0.2420 -0.0597 -0.0006 0.0045  46   CYS B C   
9372  O O   . CYS B 48   ? 0.2486 0.3179 0.2613 -0.0630 0.0000  0.0061  46   CYS B O   
9373  C CB  . CYS B 48   ? 0.2252 0.2856 0.2350 -0.0525 -0.0003 0.0018  46   CYS B CB  
9374  S SG  . CYS B 48   ? 0.2486 0.2989 0.2541 -0.0494 -0.0014 0.0000  46   CYS B SG  
9375  N N   . LEU B 49   ? 0.2414 0.3205 0.2609 -0.0583 0.0000  0.0044  47   LEU B N   
9376  C CA  . LEU B 49   ? 0.2376 0.3259 0.2610 -0.0597 0.0019  0.0061  47   LEU B CA  
9377  C C   . LEU B 49   ? 0.2372 0.3288 0.2622 -0.0653 0.0011  0.0079  47   LEU B C   
9378  O O   . LEU B 49   ? 0.2441 0.3390 0.2695 -0.0676 0.0027  0.0096  47   LEU B O   
9379  C CB  . LEU B 49   ? 0.2303 0.3271 0.2588 -0.0559 0.0031  0.0055  47   LEU B CB  
9380  C CG  . LEU B 49   ? 0.2293 0.3269 0.2572 -0.0518 0.0056  0.0050  47   LEU B CG  
9381  C CD1 . LEU B 49   ? 0.2578 0.3584 0.2853 -0.0539 0.0079  0.0068  47   LEU B CD1 
9382  C CD2 . LEU B 49   ? 0.2380 0.3260 0.2610 -0.0491 0.0050  0.0034  47   LEU B CD2 
9383  N N   . PRO B 50   ? 0.2478 0.3388 0.2735 -0.0677 -0.0014 0.0077  48   PRO B N   
9384  C CA  . PRO B 50   ? 0.2609 0.3561 0.2887 -0.0732 -0.0022 0.0095  48   PRO B CA  
9385  C C   . PRO B 50   ? 0.2969 0.3867 0.3207 -0.0772 -0.0019 0.0110  48   PRO B C   
9386  O O   . PRO B 50   ? 0.2790 0.3748 0.3052 -0.0804 -0.0007 0.0130  48   PRO B O   
9387  C CB  . PRO B 50   ? 0.2674 0.3600 0.2951 -0.0747 -0.0054 0.0085  48   PRO B CB  
9388  C CG  . PRO B 50   ? 0.2465 0.3401 0.2755 -0.0695 -0.0054 0.0067  48   PRO B CG  
9389  C CD  . PRO B 50   ? 0.2232 0.3118 0.2490 -0.0655 -0.0034 0.0058  48   PRO B CD  
9390  N N   . PRO B 51   ? 0.2764 0.3552 0.2942 -0.0771 -0.0029 0.0102  49   PRO B N   
9391  C CA  . PRO B 51   ? 0.2702 0.3441 0.2841 -0.0807 -0.0024 0.0119  49   PRO B CA  
9392  C C   . PRO B 51   ? 0.2398 0.3174 0.2541 -0.0795 0.0006  0.0131  49   PRO B C   
9393  O O   . PRO B 51   ? 0.2747 0.3531 0.2881 -0.0834 0.0015  0.0152  49   PRO B O   
9394  C CB  . PRO B 51   ? 0.3070 0.3684 0.3146 -0.0798 -0.0041 0.0105  49   PRO B CB  
9395  C CG  . PRO B 51   ? 0.3297 0.3903 0.3379 -0.0745 -0.0042 0.0082  49   PRO B CG  
9396  C CD  . PRO B 51   ? 0.2636 0.3339 0.2778 -0.0741 -0.0045 0.0080  49   PRO B CD  
9397  N N   . LEU B 52   ? 0.2658 0.3456 0.2811 -0.0743 0.0022  0.0119  50   LEU B N   
9398  C CA  . LEU B 52   ? 0.2562 0.3398 0.2716 -0.0730 0.0052  0.0129  50   LEU B CA  
9399  C C   . LEU B 52   ? 0.2858 0.3810 0.3068 -0.0749 0.0069  0.0146  50   LEU B C   
9400  O O   . LEU B 52   ? 0.2551 0.3529 0.2757 -0.0771 0.0088  0.0164  50   LEU B O   
9401  C CB  . LEU B 52   ? 0.2513 0.3342 0.2663 -0.0670 0.0063  0.0111  50   LEU B CB  
9402  C CG  . LEU B 52   ? 0.2337 0.3058 0.2435 -0.0646 0.0049  0.0095  50   LEU B CG  
9403  C CD1 . LEU B 52   ? 0.2286 0.3014 0.2391 -0.0589 0.0058  0.0076  50   LEU B CD1 
9404  C CD2 . LEU B 52   ? 0.2589 0.3243 0.2635 -0.0664 0.0054  0.0107  50   LEU B CD2 
9405  N N   . VAL B 53   ? 0.2642 0.3667 0.2905 -0.0740 0.0063  0.0140  51   VAL B N   
9406  C CA  . VAL B 53   ? 0.2401 0.3542 0.2724 -0.0760 0.0077  0.0156  51   VAL B CA  
9407  C C   . VAL B 53   ? 0.2930 0.4074 0.3249 -0.0824 0.0072  0.0179  51   VAL B C   
9408  O O   . VAL B 53   ? 0.2741 0.3949 0.3080 -0.0845 0.0095  0.0198  51   VAL B O   
9409  C CB  . VAL B 53   ? 0.2493 0.3700 0.2871 -0.0744 0.0064  0.0146  51   VAL B CB  
9410  C CG1 . VAL B 53   ? 0.2586 0.3912 0.3028 -0.0774 0.0073  0.0165  51   VAL B CG1 
9411  C CG2 . VAL B 53   ? 0.2789 0.4010 0.3177 -0.0681 0.0075  0.0127  51   VAL B CG2 
9412  N N   . GLU B 54   ? 0.2726 0.3798 0.3017 -0.0857 0.0043  0.0177  52   GLU B N   
9413  C CA  . GLU B 54   ? 0.3171 0.4234 0.3452 -0.0921 0.0035  0.0198  52   GLU B CA  
9414  C C   . GLU B 54   ? 0.2979 0.4003 0.3218 -0.0935 0.0055  0.0214  52   GLU B C   
9415  O O   . GLU B 54   ? 0.3219 0.4296 0.3475 -0.0974 0.0069  0.0237  52   GLU B O   
9416  C CB  . GLU B 54   ? 0.3512 0.4487 0.3759 -0.0948 0.0000  0.0190  52   GLU B CB  
9417  N N   . ALA B 55   ? 0.3023 0.3954 0.3206 -0.0904 0.0056  0.0202  53   ALA B N   
9418  C CA  . ALA B 55   ? 0.3139 0.4023 0.3275 -0.0917 0.0071  0.0217  53   ALA B CA  
9419  C C   . ALA B 55   ? 0.2944 0.3914 0.3105 -0.0900 0.0107  0.0228  53   ALA B C   
9420  O O   . ALA B 55   ? 0.3167 0.4134 0.3306 -0.0927 0.0123  0.0248  53   ALA B O   
9421  C CB  . ALA B 55   ? 0.3124 0.3893 0.3198 -0.0884 0.0062  0.0201  53   ALA B CB  
9422  N N   . ALA B 56   ? 0.2838 0.3881 0.3043 -0.0856 0.0120  0.0215  54   ALA B N   
9423  C CA  . ALA B 56   ? 0.2756 0.3879 0.2983 -0.0833 0.0155  0.0222  54   ALA B CA  
9424  C C   . ALA B 56   ? 0.2879 0.4122 0.3169 -0.0864 0.0170  0.0240  54   ALA B C   
9425  O O   . ALA B 56   ? 0.3325 0.4644 0.3638 -0.0847 0.0201  0.0248  54   ALA B O   
9426  C CB  . ALA B 56   ? 0.2995 0.4135 0.3237 -0.0769 0.0162  0.0198  54   ALA B CB  
9427  N N   . THR B 57   ? 0.3014 0.4277 0.3333 -0.0906 0.0148  0.0248  55   THR B N   
9428  C CA  . THR B 57   ? 0.3343 0.4727 0.3729 -0.0935 0.0160  0.0266  55   THR B CA  
9429  C C   . THR B 57   ? 0.3651 0.5062 0.4027 -0.0976 0.0184  0.0294  55   THR B C   
9430  O O   . THR B 57   ? 0.3551 0.4880 0.3874 -0.1011 0.0176  0.0305  55   THR B O   
9431  C CB  . THR B 57   ? 0.3928 0.5317 0.4342 -0.0974 0.0126  0.0267  55   THR B CB  
9432  O OG1 . THR B 57   ? 0.3512 0.4901 0.3945 -0.0932 0.0109  0.0243  55   THR B OG1 
9433  C CG2 . THR B 57   ? 0.3483 0.4992 0.3963 -0.1014 0.0135  0.0290  55   THR B CG2 
9434  N N   . GLN B 58   ? 0.3999 0.5527 0.4428 -0.0969 0.0215  0.0306  56   GLN B N   
9435  C CA  . GLN B 58   ? 0.3527 0.5101 0.3957 -0.1009 0.0241  0.0334  56   GLN B CA  
9436  C C   . GLN B 58   ? 0.3614 0.5325 0.4128 -0.1035 0.0250  0.0350  56   GLN B C   
9437  O O   . GLN B 58   ? 0.3781 0.5562 0.4351 -0.1007 0.0245  0.0338  56   GLN B O   
9438  C CB  . GLN B 58   ? 0.3668 0.5247 0.4068 -0.0970 0.0278  0.0333  56   GLN B CB  
9439  C CG  . GLN B 58   ? 0.3724 0.5183 0.4052 -0.0931 0.0269  0.0313  56   GLN B CG  
9440  C CD  . GLN B 58   ? 0.4712 0.6146 0.4989 -0.0923 0.0299  0.0322  56   GLN B CD  
9441  O OE1 . GLN B 58   ? 0.4723 0.6130 0.4968 -0.0968 0.0304  0.0345  56   GLN B OE1 
9442  N NE2 . GLN B 58   ? 0.3936 0.5378 0.4203 -0.0865 0.0318  0.0305  56   GLN B NE2 
9443  N N   . SER B 59   ? 0.4269 0.6018 0.4790 -0.1090 0.0264  0.0380  57   SER B N   
9444  C CA  . SER B 59   ? 0.4257 0.6138 0.4858 -0.1123 0.0273  0.0399  57   SER B CA  
9445  C C   . SER B 59   ? 0.4400 0.6398 0.5055 -0.1073 0.0309  0.0395  57   SER B C   
9446  O O   . SER B 59   ? 0.3775 0.5751 0.4398 -0.1022 0.0332  0.0382  57   SER B O   
9447  C CB  . SER B 59   ? 0.4201 0.6095 0.4791 -0.1189 0.0287  0.0432  57   SER B CB  
9448  O OG  . SER B 59   ? 0.4568 0.6466 0.5125 -0.1171 0.0326  0.0441  57   SER B OG  
9449  N N   . LYS B 60   ? 0.3777 0.5902 0.4517 -0.1087 0.0313  0.0406  58   LYS B N   
9450  C CA  . LYS B 60   ? 0.4055 0.6300 0.4853 -0.1041 0.0348  0.0404  58   LYS B CA  
9451  C C   . LYS B 60   ? 0.3715 0.5986 0.4489 -0.1041 0.0394  0.0420  58   LYS B C   
9452  O O   . LYS B 60   ? 0.4038 0.6342 0.4812 -0.0986 0.0424  0.0409  58   LYS B O   
9453  C CB  . LYS B 60   ? 0.3437 0.5818 0.4332 -0.1064 0.0344  0.0418  58   LYS B CB  
9454  N N   . GLU B 61   ? 0.3930 0.6182 0.4679 -0.1104 0.0398  0.0447  59   GLU B N   
9455  C CA  . GLU B 61   ? 0.3568 0.5844 0.4290 -0.1109 0.0441  0.0465  59   GLU B CA  
9456  C C   . GLU B 61   ? 0.3632 0.5802 0.4270 -0.1061 0.0451  0.0446  59   GLU B C   
9457  O O   . GLU B 61   ? 0.4246 0.6457 0.4879 -0.1021 0.0489  0.0442  59   GLU B O   
9458  C CB  . GLU B 61   ? 0.4739 0.6997 0.5442 -0.1189 0.0438  0.0497  59   GLU B CB  
9459  N N   . ILE B 62   ? 0.4012 0.6048 0.4586 -0.1065 0.0418  0.0433  60   ILE B N   
9460  C CA  . ILE B 62   ? 0.3733 0.5667 0.4229 -0.1021 0.0423  0.0415  60   ILE B CA  
9461  C C   . ILE B 62   ? 0.3373 0.5334 0.3890 -0.0946 0.0431  0.0385  60   ILE B C   
9462  O O   . ILE B 62   ? 0.4165 0.6112 0.4646 -0.0903 0.0457  0.0376  60   ILE B O   
9463  C CB  . ILE B 62   ? 0.4329 0.6117 0.4758 -0.1041 0.0384  0.0408  60   ILE B CB  
9464  C CG1 . ILE B 62   ? 0.4780 0.6527 0.5171 -0.1110 0.0382  0.0438  60   ILE B CG1 
9465  C CG2 . ILE B 62   ? 0.4539 0.6228 0.4901 -0.0987 0.0383  0.0384  60   ILE B CG2 
9466  C CD1 . ILE B 62   ? 0.4784 0.6390 0.5112 -0.1132 0.0344  0.0433  60   ILE B CD1 
9467  N N   . ARG B 63   ? 0.3564 0.5561 0.4136 -0.0930 0.0408  0.0371  61   ARG B N   
9468  C CA  . ARG B 63   ? 0.3552 0.5570 0.4143 -0.0860 0.0413  0.0343  61   ARG B CA  
9469  C C   . ARG B 63   ? 0.3844 0.5977 0.4477 -0.0828 0.0457  0.0347  61   ARG B C   
9470  O O   . ARG B 63   ? 0.4067 0.6191 0.4681 -0.0770 0.0474  0.0328  61   ARG B O   
9471  C CB  . ARG B 63   ? 0.3679 0.5716 0.4322 -0.0854 0.0378  0.0330  61   ARG B CB  
9472  C CG  . ARG B 63   ? 0.3787 0.5699 0.4380 -0.0868 0.0336  0.0318  61   ARG B CG  
9473  C CD  . ARG B 63   ? 0.4804 0.6727 0.5439 -0.0855 0.0304  0.0302  61   ARG B CD  
9474  N NE  . ARG B 63   ? 0.4003 0.6006 0.4700 -0.0904 0.0290  0.0320  61   ARG B NE  
9475  C CZ  . ARG B 63   ? 0.4967 0.7086 0.5743 -0.0891 0.0295  0.0322  61   ARG B CZ  
9476  N NH1 . ARG B 63   ? 0.4946 0.7118 0.5749 -0.0830 0.0314  0.0307  61   ARG B NH1 
9477  N NH2 . ARG B 63   ? 0.4897 0.7079 0.5725 -0.0941 0.0277  0.0339  61   ARG B NH2 
9478  N N   . ASP B 64   ? 0.3324 0.5569 0.4017 -0.0865 0.0475  0.0372  62   ASP B N   
9479  C CA  . ASP B 64   ? 0.3510 0.5868 0.4241 -0.0836 0.0521  0.0378  62   ASP B CA  
9480  C C   . ASP B 64   ? 0.3146 0.5459 0.3806 -0.0828 0.0554  0.0383  62   ASP B C   
9481  O O   . ASP B 64   ? 0.3913 0.6253 0.4565 -0.0775 0.0585  0.0370  62   ASP B O   
9482  C CB  . ASP B 64   ? 0.3104 0.5594 0.3916 -0.0881 0.0534  0.0406  62   ASP B CB  
9483  C CG  . ASP B 64   ? 0.4320 0.6874 0.5210 -0.0882 0.0505  0.0402  62   ASP B CG  
9484  O OD1 . ASP B 64   ? 0.4310 0.6834 0.5203 -0.0832 0.0486  0.0375  62   ASP B OD1 
9485  O OD2 . ASP B 64   ? 0.4373 0.7010 0.5322 -0.0932 0.0501  0.0425  62   ASP B OD2 
9486  N N   . ALA B 65   ? 0.3054 0.5296 0.3660 -0.0881 0.0548  0.0401  63   ALA B N   
9487  C CA  . ALA B 65   ? 0.3543 0.5739 0.4076 -0.0877 0.0577  0.0408  63   ALA B CA  
9488  C C   . ALA B 65   ? 0.4081 0.6175 0.4547 -0.0820 0.0570  0.0378  63   ALA B C   
9489  O O   . ALA B 65   ? 0.4267 0.6362 0.4696 -0.0786 0.0602  0.0373  63   ALA B O   
9490  C CB  . ALA B 65   ? 0.3486 0.5617 0.3972 -0.0946 0.0566  0.0435  63   ALA B CB  
9491  N N   . ALA B 66   ? 0.3539 0.5546 0.3989 -0.0808 0.0530  0.0359  64   ALA B N   
9492  C CA  . ALA B 66   ? 0.3508 0.5422 0.3900 -0.0755 0.0521  0.0331  64   ALA B CA  
9493  C C   . ALA B 66   ? 0.3166 0.5144 0.3596 -0.0690 0.0540  0.0308  64   ALA B C   
9494  O O   . ALA B 66   ? 0.3691 0.5629 0.4075 -0.0644 0.0554  0.0290  64   ALA B O   
9495  C CB  . ALA B 66   ? 0.3357 0.5166 0.3725 -0.0762 0.0474  0.0317  64   ALA B CB  
9496  N N   . ALA B 67   ? 0.3610 0.5687 0.4122 -0.0684 0.0539  0.0308  65   ALA B N   
9497  C CA  . ALA B 67   ? 0.3264 0.5405 0.3813 -0.0621 0.0558  0.0287  65   ALA B CA  
9498  C C   . ALA B 67   ? 0.3814 0.6019 0.4354 -0.0601 0.0607  0.0294  65   ALA B C   
9499  O O   . ALA B 67   ? 0.3625 0.5823 0.4145 -0.0544 0.0625  0.0273  65   ALA B O   
9500  C CB  . ALA B 67   ? 0.3687 0.5927 0.4329 -0.0622 0.0546  0.0289  65   ALA B CB  
9501  N N   . SER B 68   ? 0.3944 0.6211 0.4498 -0.0648 0.0630  0.0323  66   SER B N   
9502  C CA  . SER B 68   ? 0.3579 0.5903 0.4118 -0.0634 0.0679  0.0332  66   SER B CA  
9503  C C   . SER B 68   ? 0.4313 0.6529 0.4752 -0.0618 0.0687  0.0322  66   SER B C   
9504  O O   . SER B 68   ? 0.4334 0.6562 0.4747 -0.0572 0.0717  0.0309  66   SER B O   
9505  C CB  . SER B 68   ? 0.4508 0.6918 0.5082 -0.0694 0.0701  0.0368  66   SER B CB  
9506  N N   . THR B 69   ? 0.3609 0.5717 0.3990 -0.0655 0.0658  0.0329  67   THR B N   
9507  C CA  . THR B 69   ? 0.3727 0.5730 0.4013 -0.0641 0.0661  0.0321  67   THR B CA  
9508  C C   . THR B 69   ? 0.3896 0.5841 0.4157 -0.0576 0.0650  0.0286  67   THR B C   
9509  O O   . THR B 69   ? 0.3798 0.5713 0.4004 -0.0542 0.0671  0.0274  67   THR B O   
9510  C CB  . THR B 69   ? 0.3900 0.5800 0.4135 -0.0693 0.0629  0.0336  67   THR B CB  
9511  O OG1 . THR B 69   ? 0.4117 0.6062 0.4360 -0.0752 0.0646  0.0370  67   THR B OG1 
9512  C CG2 . THR B 69   ? 0.3691 0.5473 0.3831 -0.0672 0.0624  0.0324  67   THR B CG2 
9513  N N   . ALA B 70   ? 0.3360 0.5287 0.3658 -0.0561 0.0616  0.0269  68   ALA B N   
9514  C CA  . ALA B 70   ? 0.3802 0.5681 0.4083 -0.0500 0.0605  0.0236  68   ALA B CA  
9515  C C   . ALA B 70   ? 0.3627 0.5587 0.3932 -0.0449 0.0643  0.0224  68   ALA B C   
9516  O O   . ALA B 70   ? 0.3713 0.5626 0.3970 -0.0404 0.0652  0.0203  68   ALA B O   
9517  C CB  . ALA B 70   ? 0.3455 0.5312 0.3777 -0.0496 0.0565  0.0223  68   ALA B CB  
9518  N N   . ARG B 71   ? 0.4341 0.6423 0.4722 -0.0455 0.0664  0.0236  69   ARG B N   
9519  C CA  A ARG B 71   ? 0.4236 0.6403 0.4644 -0.0406 0.0703  0.0226  69   ARG B CA  
9520  C CA  B ARG B 71   ? 0.4230 0.6395 0.4637 -0.0405 0.0702  0.0226  69   ARG B CA  
9521  C C   . ARG B 71   ? 0.3138 0.5291 0.3480 -0.0397 0.0740  0.0229  69   ARG B C   
9522  O O   . ARG B 71   ? 0.3942 0.6081 0.4254 -0.0344 0.0758  0.0207  69   ARG B O   
9523  C CB  A ARG B 71   ? 0.4403 0.6708 0.4905 -0.0422 0.0720  0.0245  69   ARG B CB  
9524  C CB  B ARG B 71   ? 0.4397 0.6700 0.4900 -0.0418 0.0719  0.0242  69   ARG B CB  
9525  C CG  A ARG B 71   ? 0.4239 0.6646 0.4768 -0.0382 0.0769  0.0242  69   ARG B CG  
9526  C CG  B ARG B 71   ? 0.4284 0.6682 0.4819 -0.0366 0.0761  0.0233  69   ARG B CG  
9527  C CD  A ARG B 71   ? 0.4482 0.6947 0.5076 -0.0329 0.0766  0.0223  69   ARG B CD  
9528  C CD  B ARG B 71   ? 0.4183 0.6717 0.4822 -0.0371 0.0770  0.0247  69   ARG B CD  
9529  N NE  A ARG B 71   ? 0.4162 0.6701 0.4842 -0.0356 0.0745  0.0236  69   ARG B NE  
9530  N NE  B ARG B 71   ? 0.4343 0.6881 0.5031 -0.0338 0.0740  0.0228  69   ARG B NE  
9531  C CZ  A ARG B 71   ? 0.4511 0.7094 0.5253 -0.0321 0.0730  0.0223  69   ARG B CZ  
9532  C CZ  B ARG B 71   ? 0.4679 0.7230 0.5379 -0.0273 0.0750  0.0204  69   ARG B CZ  
9533  N NH1 A ARG B 71   ? 0.4786 0.7346 0.5514 -0.0256 0.0736  0.0196  69   ARG B NH1 
9534  N NH1 B ARG B 71   ? 0.4188 0.6748 0.4853 -0.0231 0.0788  0.0192  69   ARG B NH1 
9535  N NH2 A ARG B 71   ? 0.4460 0.7105 0.5274 -0.0353 0.0708  0.0238  69   ARG B NH2 
9536  N NH2 B ARG B 71   ? 0.4692 0.7243 0.5435 -0.0250 0.0719  0.0190  69   ARG B NH2 
9537  N N   . LYS B 72   ? 0.3599 0.5751 0.3913 -0.0449 0.0752  0.0256  70   LYS B N   
9538  C CA  . LYS B 72   ? 0.3688 0.5824 0.3934 -0.0446 0.0787  0.0262  70   LYS B CA  
9539  C C   . LYS B 72   ? 0.4046 0.6058 0.4204 -0.0414 0.0771  0.0238  70   LYS B C   
9540  O O   . LYS B 72   ? 0.3910 0.5915 0.4022 -0.0376 0.0799  0.0225  70   LYS B O   
9541  C CB  . LYS B 72   ? 0.3925 0.6067 0.4154 -0.0514 0.0794  0.0297  70   LYS B CB  
9542  C CG  . LYS B 72   ? 0.4179 0.6306 0.4334 -0.0518 0.0830  0.0308  70   LYS B CG  
9543  C CD  . LYS B 72   ? 0.3951 0.6099 0.4102 -0.0588 0.0839  0.0346  70   LYS B CD  
9544  C CE  . LYS B 72   ? 0.4731 0.6848 0.4799 -0.0597 0.0870  0.0359  70   LYS B CE  
9545  N NZ  . LYS B 72   ? 0.4315 0.6524 0.4392 -0.0560 0.0923  0.0355  70   LYS B NZ  
9546  N N   . LEU B 73   ? 0.3937 0.5850 0.4070 -0.0428 0.0727  0.0232  71   LEU B N   
9547  C CA  . LEU B 73   ? 0.3848 0.5647 0.3903 -0.0399 0.0709  0.0210  71   LEU B CA  
9548  C C   . LEU B 73   ? 0.3386 0.5187 0.3452 -0.0333 0.0712  0.0177  71   LEU B C   
9549  O O   . LEU B 73   ? 0.3849 0.5600 0.3853 -0.0299 0.0722  0.0160  71   LEU B O   
9550  C CB  . LEU B 73   ? 0.3305 0.5005 0.3340 -0.0428 0.0662  0.0211  71   LEU B CB  
9551  C CG  . LEU B 73   ? 0.3137 0.4812 0.3152 -0.0493 0.0653  0.0242  71   LEU B CG  
9552  C CD1 . LEU B 73   ? 0.3411 0.5004 0.3425 -0.0515 0.0605  0.0240  71   LEU B CD1 
9553  C CD2 . LEU B 73   ? 0.3740 0.5361 0.3669 -0.0502 0.0671  0.0252  71   LEU B CD2 
9554  N N   . ILE B 74   ? 0.3605 0.5461 0.3747 -0.0316 0.0701  0.0168  72   ILE B N   
9555  C CA  . ILE B 74   ? 0.3600 0.5448 0.3752 -0.0256 0.0697  0.0137  72   ILE B CA  
9556  C C   . ILE B 74   ? 0.4463 0.6382 0.4617 -0.0214 0.0743  0.0129  72   ILE B C   
9557  O O   . ILE B 74   ? 0.3911 0.5787 0.4024 -0.0166 0.0749  0.0104  72   ILE B O   
9558  C CB  . ILE B 74   ? 0.3876 0.5759 0.4106 -0.0252 0.0670  0.0132  72   ILE B CB  
9559  C CG1 . ILE B 74   ? 0.4004 0.5795 0.4217 -0.0280 0.0624  0.0132  72   ILE B CG1 
9560  C CG2 . ILE B 74   ? 0.3977 0.5874 0.4228 -0.0188 0.0674  0.0104  72   ILE B CG2 
9561  C CD1 . ILE B 74   ? 0.3934 0.5765 0.4220 -0.0295 0.0598  0.0136  72   ILE B CD1 
9562  N N   . GLU B 75   ? 0.4362 0.6390 0.4564 -0.0232 0.0775  0.0150  73   GLU B N   
9563  C CA  . GLU B 75   ? 0.4570 0.6668 0.4770 -0.0195 0.0823  0.0144  73   GLU B CA  
9564  C C   . GLU B 75   ? 0.4636 0.6662 0.4737 -0.0188 0.0841  0.0139  73   GLU B C   
9565  O O   . GLU B 75   ? 0.4731 0.6745 0.4797 -0.0137 0.0861  0.0116  73   GLU B O   
9566  C CB  . GLU B 75   ? 0.4400 0.6627 0.4668 -0.0223 0.0855  0.0172  73   GLU B CB  
9567  C CG  . GLU B 75   ? 0.4996 0.7308 0.5365 -0.0217 0.0842  0.0173  73   GLU B CG  
9568  C CD  . GLU B 75   ? 0.5834 0.8273 0.6275 -0.0254 0.0867  0.0203  73   GLU B CD  
9569  O OE1 . GLU B 75   ? 0.6189 0.8637 0.6605 -0.0300 0.0883  0.0228  73   GLU B OE1 
9570  O OE2 . GLU B 75   ? 0.5180 0.7711 0.5706 -0.0237 0.0868  0.0203  73   GLU B OE2 
9571  N N   . ALA B 76   ? 0.3891 0.5864 0.3943 -0.0238 0.0832  0.0159  74   ALA B N   
9572  C CA  . ALA B 76   ? 0.4665 0.6559 0.4618 -0.0234 0.0841  0.0155  74   ALA B CA  
9573  C C   . ALA B 76   ? 0.4735 0.6525 0.4636 -0.0191 0.0814  0.0123  74   ALA B C   
9574  O O   . ALA B 76   ? 0.4879 0.6637 0.4719 -0.0156 0.0833  0.0105  74   ALA B O   
9575  C CB  . ALA B 76   ? 0.4535 0.6381 0.4448 -0.0296 0.0828  0.0183  74   ALA B CB  
9576  N N   . LEU B 77   ? 0.4538 0.6275 0.4462 -0.0195 0.0770  0.0114  75   LEU B N   
9577  C CA  . LEU B 77   ? 0.4898 0.6540 0.4779 -0.0156 0.0744  0.0084  75   LEU B CA  
9578  C C   . LEU B 77   ? 0.4508 0.6186 0.4406 -0.0095 0.0764  0.0057  75   LEU B C   
9579  O O   . LEU B 77   ? 0.4751 0.6371 0.4587 -0.0060 0.0768  0.0035  75   LEU B O   
9580  C CB  . LEU B 77   ? 0.4069 0.5661 0.3982 -0.0172 0.0696  0.0082  75   LEU B CB  
9581  C CG  . LEU B 77   ? 0.4341 0.5858 0.4216 -0.0222 0.0667  0.0100  75   LEU B CG  
9582  C CD1 . LEU B 77   ? 0.3584 0.5067 0.3501 -0.0234 0.0624  0.0096  75   LEU B CD1 
9583  C CD2 . LEU B 77   ? 0.4308 0.5727 0.4091 -0.0212 0.0660  0.0090  75   LEU B CD2 
9584  N N   . ARG B 78   ? 0.4181 0.5952 0.4162 -0.0082 0.0775  0.0058  76   ARG B N   
9585  C CA  . ARG B 78   ? 0.4373 0.6177 0.4375 -0.0022 0.0791  0.0033  76   ARG B CA  
9586  C C   . ARG B 78   ? 0.4149 0.5998 0.4118 0.0004  0.0840  0.0029  76   ARG B C   
9587  O O   . ARG B 78   ? 0.4618 0.6466 0.4576 0.0058  0.0855  0.0004  76   ARG B O   
9588  C CB  . ARG B 78   ? 0.5006 0.6896 0.5107 -0.0014 0.0787  0.0036  76   ARG B CB  
9589  C CG  . ARG B 78   ? 0.4439 0.6279 0.4568 -0.0031 0.0738  0.0035  76   ARG B CG  
9590  C CD  . ARG B 78   ? 0.4688 0.6603 0.4906 -0.0013 0.0731  0.0032  76   ARG B CD  
9591  N NE  . ARG B 78   ? 0.4315 0.6158 0.4535 0.0005  0.0692  0.0013  76   ARG B NE  
9592  C CZ  . ARG B 78   ? 0.5188 0.7069 0.5476 0.0017  0.0674  0.0011  76   ARG B CZ  
9593  N NH1 . ARG B 78   ? 0.5137 0.7128 0.5501 0.0010  0.0689  0.0026  76   ARG B NH1 
9594  N NH2 . ARG B 78   ? 0.4988 0.6797 0.5269 0.0035  0.0640  -0.0007 76   ARG B NH2 
9595  N N   . GLY B 79   ? 0.4352 0.6237 0.4301 -0.0032 0.0867  0.0054  77   GLY B N   
9596  C CA  . GLY B 79   ? 0.4664 0.6595 0.4580 -0.0009 0.0916  0.0052  77   GLY B CA  
9597  C C   . GLY B 79   ? 0.5143 0.6980 0.4953 0.0010  0.0920  0.0034  77   GLY B C   
9598  O O   . GLY B 79   ? 0.4748 0.6612 0.4524 0.0041  0.0959  0.0025  77   GLY B O   
9599  N N   . LYS B 80   ? 0.5739 0.7466 0.5496 -0.0007 0.0880  0.0030  78   LYS B N   
9600  C CA  . LYS B 80   ? 0.5490 0.7126 0.5142 0.0003  0.0880  0.0017  78   LYS B CA  
9601  C C   . LYS B 80   ? 0.4903 0.6440 0.4522 0.0036  0.0843  -0.0014 78   LYS B C   
9602  O O   . LYS B 80   ? 0.5528 0.7061 0.5202 0.0049  0.0817  -0.0024 78   LYS B O   
9603  C CB  . LYS B 80   ? 0.5781 0.7376 0.5385 -0.0053 0.0871  0.0045  78   LYS B CB  
9604  C CG  . LYS B 80   ? 0.5000 0.6546 0.4631 -0.0093 0.0824  0.0057  78   LYS B CG  
9605  C CD  . LYS B 80   ? 0.5519 0.7051 0.5121 -0.0152 0.0822  0.0090  78   LYS B CD  
9606  C CE  . LYS B 80   ? 0.4391 0.5861 0.4010 -0.0187 0.0773  0.0099  78   LYS B CE  
9607  N NZ  . LYS B 80   ? 0.4560 0.6014 0.4154 -0.0245 0.0769  0.0133  78   LYS B NZ  
9608  N N   . GLY B 85   ? 0.5283 0.6074 0.4505 0.0208  0.0612  -0.0209 83   GLY B N   
9609  C CA  . GLY B 85   ? 0.5279 0.5996 0.4419 0.0232  0.0606  -0.0234 83   GLY B CA  
9610  C C   . GLY B 85   ? 0.4864 0.5541 0.4018 0.0268  0.0586  -0.0263 83   GLY B C   
9611  O O   . GLY B 85   ? 0.4844 0.5497 0.3953 0.0304  0.0600  -0.0288 83   GLY B O   
9612  N N   . VAL B 86   ? 0.5275 0.5941 0.4487 0.0258  0.0554  -0.0259 84   VAL B N   
9613  C CA  . VAL B 86   ? 0.5331 0.5956 0.4559 0.0289  0.0533  -0.0284 84   VAL B CA  
9614  C C   . VAL B 86   ? 0.4782 0.5465 0.4051 0.0328  0.0564  -0.0297 84   VAL B C   
9615  O O   . VAL B 86   ? 0.4757 0.5405 0.4002 0.0365  0.0564  -0.0324 84   VAL B O   
9616  C CB  . VAL B 86   ? 0.5157 0.5758 0.4436 0.0267  0.0493  -0.0275 84   VAL B CB  
9617  C CG1 . VAL B 86   ? 0.5374 0.5959 0.4691 0.0299  0.0479  -0.0296 84   VAL B CG1 
9618  C CG2 . VAL B 86   ? 0.5541 0.6065 0.4768 0.0242  0.0460  -0.0273 84   VAL B CG2 
9619  N N   . GLU B 87   ? 0.5213 0.5986 0.4541 0.0321  0.0590  -0.0278 85   GLU B N   
9620  C CA  . GLU B 87   ? 0.5185 0.6022 0.4555 0.0359  0.0620  -0.0289 85   GLU B CA  
9621  C C   . GLU B 87   ? 0.4613 0.5439 0.3915 0.0394  0.0653  -0.0309 85   GLU B C   
9622  O O   . GLU B 87   ? 0.4925 0.5746 0.4228 0.0437  0.0663  -0.0332 85   GLU B O   
9623  C CB  . GLU B 87   ? 0.6207 0.7147 0.5648 0.0341  0.0644  -0.0262 85   GLU B CB  
9624  N N   . GLY B 88   ? 0.4816 0.5637 0.4056 0.0376  0.0670  -0.0301 86   GLY B N   
9625  C CA  . GLY B 88   ? 0.4830 0.5640 0.4000 0.0408  0.0702  -0.0320 86   GLY B CA  
9626  C C   . GLY B 88   ? 0.4063 0.4774 0.3166 0.0433  0.0679  -0.0351 86   GLY B C   
9627  O O   . GLY B 88   ? 0.4406 0.5106 0.3474 0.0475  0.0700  -0.0376 86   GLY B O   
9628  N N   . LEU B 89   ? 0.4576 0.5214 0.3661 0.0409  0.0634  -0.0351 87   LEU B N   
9629  C CA  . LEU B 89   ? 0.4663 0.5206 0.3691 0.0429  0.0608  -0.0380 87   LEU B CA  
9630  C C   . LEU B 89   ? 0.3545 0.4085 0.2620 0.0466  0.0602  -0.0399 87   LEU B C   
9631  O O   . LEU B 89   ? 0.3907 0.4403 0.2937 0.0502  0.0607  -0.0428 87   LEU B O   
9632  C CB  . LEU B 89   ? 0.4608 0.5085 0.3618 0.0392  0.0562  -0.0371 87   LEU B CB  
9633  C CG  . LEU B 89   ? 0.5097 0.5480 0.4067 0.0404  0.0525  -0.0396 87   LEU B CG  
9634  C CD1 . LEU B 89   ? 0.5185 0.5514 0.4056 0.0423  0.0535  -0.0418 87   LEU B CD1 
9635  C CD2 . LEU B 89   ? 0.5404 0.5744 0.4382 0.0365  0.0480  -0.0381 87   LEU B CD2 
9636  N N   . VAL B 90   ? 0.3752 0.4336 0.2915 0.0456  0.0590  -0.0384 88   VAL B N   
9637  C CA  . VAL B 90   ? 0.4007 0.4594 0.3220 0.0489  0.0584  -0.0399 88   VAL B CA  
9638  C C   . VAL B 90   ? 0.4509 0.5144 0.3724 0.0534  0.0627  -0.0413 88   VAL B C   
9639  O O   . VAL B 90   ? 0.4189 0.4788 0.3392 0.0574  0.0626  -0.0439 88   VAL B O   
9640  C CB  . VAL B 90   ? 0.4088 0.4721 0.3393 0.0467  0.0566  -0.0378 88   VAL B CB  
9641  C CG1 . VAL B 90   ? 0.4277 0.4930 0.3639 0.0503  0.0567  -0.0389 88   VAL B CG1 
9642  C CG2 . VAL B 90   ? 0.3736 0.4308 0.3037 0.0431  0.0522  -0.0370 88   VAL B CG2 
9643  N N   . GLN B 91   ? 0.4606 0.5323 0.3835 0.0529  0.0665  -0.0397 89   GLN B N   
9644  C CA  . GLN B 91   ? 0.4737 0.5508 0.3971 0.0573  0.0709  -0.0409 89   GLN B CA  
9645  C C   . GLN B 91   ? 0.4512 0.5220 0.3649 0.0603  0.0724  -0.0437 89   GLN B C   
9646  O O   . GLN B 91   ? 0.4749 0.5445 0.3876 0.0651  0.0739  -0.0461 89   GLN B O   
9647  C CB  . GLN B 91   ? 0.5440 0.6319 0.4717 0.0557  0.0745  -0.0382 89   GLN B CB  
9648  N N   . GLU B 92   ? 0.4234 0.4896 0.3295 0.0577  0.0718  -0.0435 90   GLU B N   
9649  C CA  . GLU B 92   ? 0.4274 0.4878 0.3236 0.0603  0.0734  -0.0461 90   GLU B CA  
9650  C C   . GLU B 92   ? 0.4265 0.4775 0.3191 0.0632  0.0706  -0.0493 90   GLU B C   
9651  O O   . GLU B 92   ? 0.4713 0.5196 0.3590 0.0674  0.0727  -0.0521 90   GLU B O   
9652  C CB  . GLU B 92   ? 0.5025 0.5594 0.3913 0.0566  0.0728  -0.0451 90   GLU B CB  
9653  C CG  . GLU B 92   ? 0.5302 0.5805 0.4081 0.0590  0.0741  -0.0478 90   GLU B CG  
9654  C CD  . GLU B 92   ? 0.5340 0.5810 0.4043 0.0554  0.0735  -0.0466 90   GLU B CD  
9655  O OE1 . GLU B 92   ? 0.5816 0.6312 0.4550 0.0510  0.0721  -0.0437 90   GLU B OE1 
9656  O OE2 . GLU B 92   ? 0.5288 0.5703 0.3896 0.0570  0.0745  -0.0488 90   GLU B OE2 
9657  N N   . TYR B 93   ? 0.4289 0.4747 0.3237 0.0609  0.0660  -0.0491 91   TYR B N   
9658  C CA  . TYR B 93   ? 0.4398 0.4764 0.3312 0.0631  0.0630  -0.0519 91   TYR B CA  
9659  C C   . TYR B 93   ? 0.4264 0.4645 0.3256 0.0654  0.0620  -0.0523 91   TYR B C   
9660  O O   . TYR B 93   ? 0.4089 0.4396 0.3065 0.0665  0.0591  -0.0542 91   TYR B O   
9661  C CB  . TYR B 93   ? 0.3824 0.4110 0.2696 0.0593  0.0585  -0.0518 91   TYR B CB  
9662  C CG  . TYR B 93   ? 0.3897 0.4149 0.2675 0.0581  0.0593  -0.0522 91   TYR B CG  
9663  C CD1 . TYR B 93   ? 0.4008 0.4187 0.2697 0.0608  0.0596  -0.0553 91   TYR B CD1 
9664  C CD2 . TYR B 93   ? 0.4053 0.4345 0.2829 0.0544  0.0600  -0.0494 91   TYR B CD2 
9665  C CE1 . TYR B 93   ? 0.4372 0.4520 0.2971 0.0598  0.0604  -0.0557 91   TYR B CE1 
9666  C CE2 . TYR B 93   ? 0.4747 0.5008 0.3433 0.0533  0.0609  -0.0497 91   TYR B CE2 
9667  C CZ  . TYR B 93   ? 0.4475 0.4664 0.3072 0.0561  0.0610  -0.0529 91   TYR B CZ  
9668  O OH  . TYR B 93   ? 0.4716 0.4872 0.3220 0.0551  0.0618  -0.0532 91   TYR B OH  
9669  N N   . SER B 94   ? 0.3551 0.4028 0.2624 0.0660  0.0644  -0.0505 92   SER B N   
9670  C CA  . SER B 94   ? 0.3712 0.4212 0.2860 0.0684  0.0637  -0.0507 92   SER B CA  
9671  C C   . SER B 94   ? 0.3957 0.4398 0.3128 0.0660  0.0588  -0.0504 92   SER B C   
9672  O O   . SER B 94   ? 0.3943 0.4335 0.3119 0.0684  0.0570  -0.0521 92   SER B O   
9673  C CB  . SER B 94   ? 0.3697 0.4176 0.2818 0.0742  0.0659  -0.0536 92   SER B CB  
9674  O OG  . SER B 94   ? 0.4452 0.4990 0.3553 0.0765  0.0707  -0.0538 92   SER B OG  
9675  N N   . LEU B 95   ? 0.3250 0.3694 0.2432 0.0612  0.0566  -0.0482 93   LEU B N   
9676  C CA  . LEU B 95   ? 0.3095 0.3486 0.2297 0.0587  0.0520  -0.0478 93   LEU B CA  
9677  C C   . LEU B 95   ? 0.3433 0.3877 0.2730 0.0587  0.0513  -0.0463 93   LEU B C   
9678  O O   . LEU B 95   ? 0.3431 0.3963 0.2785 0.0581  0.0534  -0.0443 93   LEU B O   
9679  C CB  . LEU B 95   ? 0.3197 0.3575 0.2380 0.0538  0.0500  -0.0460 93   LEU B CB  
9680  C CG  . LEU B 95   ? 0.3416 0.3740 0.2503 0.0532  0.0503  -0.0471 93   LEU B CG  
9681  C CD1 . LEU B 95   ? 0.3745 0.4047 0.2818 0.0485  0.0476  -0.0452 93   LEU B CD1 
9682  C CD2 . LEU B 95   ? 0.3482 0.3718 0.2509 0.0560  0.0489  -0.0504 93   LEU B CD2 
9683  N N   . SER B 96   ? 0.3116 0.3507 0.2429 0.0592  0.0482  -0.0472 94   SER B N   
9684  C CA  . SER B 96   ? 0.3029 0.3458 0.2425 0.0580  0.0466  -0.0455 94   SER B CA  
9685  C C   . SER B 96   ? 0.3097 0.3533 0.2510 0.0529  0.0443  -0.0431 94   SER B C   
9686  O O   . SER B 96   ? 0.2959 0.3358 0.2318 0.0506  0.0435  -0.0431 94   SER B O   
9687  C CB  . SER B 96   ? 0.3246 0.3609 0.2647 0.0596  0.0437  -0.0470 94   SER B CB  
9688  O OG  . SER B 96   ? 0.2797 0.3081 0.2153 0.0571  0.0404  -0.0476 94   SER B OG  
9689  N N   . SER B 97   ? 0.2819 0.3300 0.2306 0.0513  0.0433  -0.0412 95   SER B N   
9690  C CA  . SER B 97   ? 0.2670 0.3153 0.2175 0.0467  0.0410  -0.0391 95   SER B CA  
9691  C C   . SER B 97   ? 0.2587 0.2981 0.2049 0.0451  0.0375  -0.0400 95   SER B C   
9692  O O   . SER B 97   ? 0.2846 0.3218 0.2276 0.0421  0.0364  -0.0391 95   SER B O   
9693  C CB  . SER B 97   ? 0.3463 0.3999 0.3051 0.0456  0.0402  -0.0372 95   SER B CB  
9694  O OG  . SER B 97   ? 0.4335 0.4960 0.3963 0.0463  0.0433  -0.0360 95   SER B OG  
9695  N N   . GLN B 98   ? 0.2699 0.3041 0.2162 0.0470  0.0356  -0.0416 96   GLN B N   
9696  C CA  . GLN B 98   ? 0.2793 0.3054 0.2221 0.0454  0.0321  -0.0424 96   GLN B CA  
9697  C C   . GLN B 98   ? 0.2534 0.2744 0.1880 0.0454  0.0323  -0.0439 96   GLN B C   
9698  O O   . GLN B 98   ? 0.2755 0.2920 0.2071 0.0428  0.0298  -0.0436 96   GLN B O   
9699  C CB  . GLN B 98   ? 0.2721 0.2938 0.2165 0.0476  0.0303  -0.0439 96   GLN B CB  
9700  C CG  . GLN B 98   ? 0.2701 0.2950 0.2220 0.0467  0.0291  -0.0423 96   GLN B CG  
9701  C CD  . GLN B 98   ? 0.2860 0.3099 0.2396 0.0426  0.0264  -0.0406 96   GLN B CD  
9702  O OE1 . GLN B 98   ? 0.3300 0.3584 0.2853 0.0402  0.0271  -0.0388 96   GLN B OE1 
9703  N NE2 . GLN B 98   ? 0.2887 0.3066 0.2419 0.0419  0.0235  -0.0412 96   GLN B NE2 
9704  N N   . GLU B 99   ? 0.2552 0.2769 0.1860 0.0485  0.0352  -0.0454 97   GLU B N   
9705  C CA  . GLU B 99   ? 0.2637 0.2809 0.1862 0.0485  0.0356  -0.0468 97   GLU B CA  
9706  C C   . GLU B 99   ? 0.3318 0.3521 0.2528 0.0452  0.0362  -0.0448 97   GLU B C   
9707  O O   . GLU B 99   ? 0.2964 0.3117 0.2118 0.0433  0.0345  -0.0450 97   GLU B O   
9708  C CB  . GLU B 99   ? 0.3067 0.3242 0.2255 0.0528  0.0389  -0.0489 97   GLU B CB  
9709  C CG  . GLU B 99   ? 0.2905 0.3019 0.2079 0.0559  0.0377  -0.0514 97   GLU B CG  
9710  C CD  . GLU B 99   ? 0.3069 0.3199 0.2223 0.0606  0.0412  -0.0533 97   GLU B CD  
9711  O OE1 . GLU B 99   ? 0.3188 0.3382 0.2343 0.0612  0.0447  -0.0525 97   GLU B OE1 
9712  O OE2 . GLU B 99   ? 0.3232 0.3310 0.2369 0.0635  0.0406  -0.0554 97   GLU B OE2 
9713  N N   . GLY B 100  ? 0.2821 0.3106 0.2080 0.0445  0.0386  -0.0427 98   GLY B N   
9714  C CA  . GLY B 100  ? 0.2956 0.3270 0.2205 0.0411  0.0391  -0.0405 98   GLY B CA  
9715  C C   . GLY B 100  ? 0.2990 0.3268 0.2249 0.0374  0.0353  -0.0392 98   GLY B C   
9716  O O   . GLY B 100  ? 0.2995 0.3245 0.2206 0.0350  0.0344  -0.0385 98   GLY B O   
9717  N N   . VAL B 101  ? 0.2645 0.2921 0.1962 0.0369  0.0331  -0.0387 99   VAL B N   
9718  C CA  . VAL B 101  ? 0.2556 0.2799 0.1886 0.0337  0.0296  -0.0375 99   VAL B CA  
9719  C C   . VAL B 101  ? 0.2735 0.2896 0.2003 0.0336  0.0270  -0.0392 99   VAL B C   
9720  O O   . VAL B 101  ? 0.2769 0.2903 0.2009 0.0309  0.0251  -0.0383 99   VAL B O   
9721  C CB  . VAL B 101  ? 0.2576 0.2834 0.1979 0.0336  0.0281  -0.0369 99   VAL B CB  
9722  C CG1 . VAL B 101  ? 0.2838 0.3056 0.2250 0.0307  0.0244  -0.0361 99   VAL B CG1 
9723  C CG2 . VAL B 101  ? 0.2750 0.3090 0.2212 0.0331  0.0302  -0.0351 99   VAL B CG2 
9724  N N   . ALA B 102  ? 0.2652 0.2773 0.1900 0.0364  0.0267  -0.0416 100  ALA B N   
9725  C CA  . ALA B 102  ? 0.2948 0.2990 0.2139 0.0363  0.0240  -0.0433 100  ALA B CA  
9726  C C   . ALA B 102  ? 0.2841 0.2863 0.1956 0.0355  0.0246  -0.0435 100  ALA B C   
9727  O O   . ALA B 102  ? 0.2930 0.2903 0.2008 0.0335  0.0219  -0.0435 100  ALA B O   
9728  C CB  . ALA B 102  ? 0.2816 0.2819 0.1993 0.0396  0.0240  -0.0459 100  ALA B CB  
9729  N N   . LEU B 103  ? 0.2633 0.2694 0.1725 0.0370  0.0283  -0.0437 101  LEU B N   
9730  C CA  . LEU B 103  ? 0.2754 0.2798 0.1770 0.0364  0.0293  -0.0439 101  LEU B CA  
9731  C C   . LEU B 103  ? 0.3273 0.3329 0.2291 0.0326  0.0279  -0.0413 101  LEU B C   
9732  O O   . LEU B 103  ? 0.3275 0.3284 0.2233 0.0311  0.0262  -0.0414 101  LEU B O   
9733  C CB  . LEU B 103  ? 0.2994 0.3088 0.1996 0.0388  0.0338  -0.0443 101  LEU B CB  
9734  C CG  . LEU B 103  ? 0.3233 0.3320 0.2157 0.0382  0.0355  -0.0442 101  LEU B CG  
9735  C CD1 . LEU B 103  ? 0.3722 0.3726 0.2565 0.0393  0.0336  -0.0468 101  LEU B CD1 
9736  C CD2 . LEU B 103  ? 0.3211 0.3362 0.2137 0.0405  0.0404  -0.0443 101  LEU B CD2 
9737  N N   . MET B 104  ? 0.2836 0.2950 0.1920 0.0309  0.0287  -0.0390 102  MET B N   
9738  C CA  . MET B 104  ? 0.3158 0.3281 0.2245 0.0273  0.0275  -0.0364 102  MET B CA  
9739  C C   . MET B 104  ? 0.3099 0.3166 0.2187 0.0255  0.0231  -0.0363 102  MET B C   
9740  O O   . MET B 104  ? 0.3271 0.3313 0.2323 0.0232  0.0214  -0.0352 102  MET B O   
9741  C CB  . MET B 104  ? 0.3119 0.3315 0.2276 0.0260  0.0291  -0.0341 102  MET B CB  
9742  C CG  . MET B 104  ? 0.3190 0.3449 0.2348 0.0275  0.0335  -0.0339 102  MET B CG  
9743  S SD  . MET B 104  ? 0.4481 0.4731 0.3548 0.0271  0.0358  -0.0338 102  MET B SD  
9744  C CE  . MET B 104  ? 0.5105 0.5363 0.4180 0.0225  0.0343  -0.0305 102  MET B CE  
9745  N N   . CYS B 105  ? 0.2875 0.2922 0.2002 0.0265  0.0212  -0.0374 103  CYS B N   
9746  C CA  . CYS B 105  ? 0.3188 0.3183 0.2316 0.0250  0.0171  -0.0375 103  CYS B CA  
9747  C C   . CYS B 105  ? 0.2974 0.2907 0.2023 0.0251  0.0155  -0.0390 103  CYS B C   
9748  O O   . CYS B 105  ? 0.3307 0.3207 0.2335 0.0229  0.0127  -0.0382 103  CYS B O   
9749  C CB  . CYS B 105  ? 0.2931 0.2916 0.2110 0.0263  0.0158  -0.0386 103  CYS B CB  
9750  S SG  . CYS B 105  ? 0.2922 0.2970 0.2194 0.0255  0.0166  -0.0366 103  CYS B SG  
9751  N N   . LEU B 106  ? 0.2937 0.2849 0.1941 0.0278  0.0170  -0.0414 104  LEU B N   
9752  C CA  . LEU B 106  ? 0.3085 0.2937 0.2006 0.0280  0.0157  -0.0430 104  LEU B CA  
9753  C C   . LEU B 106  ? 0.3470 0.3329 0.2341 0.0261  0.0163  -0.0415 104  LEU B C   
9754  O O   . LEU B 106  ? 0.3584 0.3399 0.2410 0.0245  0.0135  -0.0414 104  LEU B O   
9755  C CB  . LEU B 106  ? 0.3066 0.2900 0.1945 0.0313  0.0178  -0.0458 104  LEU B CB  
9756  C CG  . LEU B 106  ? 0.3160 0.2932 0.1944 0.0317  0.0168  -0.0477 104  LEU B CG  
9757  C CD1 . LEU B 106  ? 0.3871 0.3578 0.2643 0.0304  0.0123  -0.0485 104  LEU B CD1 
9758  C CD2 . LEU B 106  ? 0.3589 0.3349 0.2328 0.0353  0.0197  -0.0503 104  LEU B CD2 
9759  N N   . ALA B 107  ? 0.3185 0.3102 0.2065 0.0263  0.0199  -0.0402 105  ALA B N   
9760  C CA  . ALA B 107  ? 0.3167 0.3092 0.1998 0.0244  0.0209  -0.0386 105  ALA B CA  
9761  C C   . ALA B 107  ? 0.3564 0.3481 0.2416 0.0211  0.0178  -0.0362 105  ALA B C   
9762  O O   . ALA B 107  ? 0.3658 0.3540 0.2453 0.0196  0.0161  -0.0356 105  ALA B O   
9763  C CB  . ALA B 107  ? 0.3682 0.3678 0.2532 0.0250  0.0253  -0.0374 105  ALA B CB  
9764  N N   . GLU B 108  ? 0.3368 0.3314 0.2300 0.0202  0.0169  -0.0348 106  GLU B N   
9765  C CA  . GLU B 108  ? 0.3358 0.3294 0.2315 0.0174  0.0140  -0.0327 106  GLU B CA  
9766  C C   . GLU B 108  ? 0.3839 0.3710 0.2760 0.0168  0.0099  -0.0337 106  GLU B C   
9767  O O   . GLU B 108  ? 0.3770 0.3619 0.2663 0.0148  0.0079  -0.0323 106  GLU B O   
9768  C CB  . GLU B 108  ? 0.3461 0.3431 0.2507 0.0170  0.0136  -0.0318 106  GLU B CB  
9769  C CG  . GLU B 108  ? 0.4054 0.4011 0.3133 0.0145  0.0105  -0.0299 106  GLU B CG  
9770  C CD  . GLU B 108  ? 0.4659 0.4635 0.3818 0.0146  0.0096  -0.0297 106  GLU B CD  
9771  O OE1 . GLU B 108  ? 0.3974 0.3987 0.3170 0.0161  0.0119  -0.0303 106  GLU B OE1 
9772  O OE2 . GLU B 108  ? 0.4811 0.4765 0.3994 0.0133  0.0066  -0.0290 106  GLU B OE2 
9773  N N   . ALA B 109  ? 0.3624 0.3464 0.2547 0.0186  0.0087  -0.0360 107  ALA B N   
9774  C CA  . ALA B 109  ? 0.3736 0.3517 0.2630 0.0179  0.0047  -0.0370 107  ALA B CA  
9775  C C   . ALA B 109  ? 0.3684 0.3427 0.2486 0.0177  0.0043  -0.0376 107  ALA B C   
9776  O O   . ALA B 109  ? 0.3905 0.3615 0.2680 0.0160  0.0011  -0.0369 107  ALA B O   
9777  C CB  . ALA B 109  ? 0.3876 0.3632 0.2790 0.0197  0.0037  -0.0393 107  ALA B CB  
9778  N N   . LEU B 110  ? 0.3397 0.3145 0.2149 0.0196  0.0075  -0.0390 108  LEU B N   
9779  C CA  . LEU B 110  ? 0.3713 0.3425 0.2371 0.0195  0.0074  -0.0397 108  LEU B CA  
9780  C C   . LEU B 110  ? 0.4024 0.3750 0.2661 0.0171  0.0073  -0.0369 108  LEU B C   
9781  O O   . LEU B 110  ? 0.4305 0.3991 0.2872 0.0161  0.0055  -0.0369 108  LEU B O   
9782  C CB  . LEU B 110  ? 0.3658 0.3379 0.2272 0.0222  0.0113  -0.0416 108  LEU B CB  
9783  C CG  . LEU B 110  ? 0.3758 0.3445 0.2367 0.0247  0.0109  -0.0447 108  LEU B CG  
9784  C CD1 . LEU B 110  ? 0.3667 0.3376 0.2252 0.0277  0.0154  -0.0463 108  LEU B CD1 
9785  C CD2 . LEU B 110  ? 0.4277 0.3890 0.2819 0.0243  0.0073  -0.0465 108  LEU B CD2 
9786  N N   . LEU B 111  ? 0.3850 0.3630 0.2541 0.0161  0.0093  -0.0346 109  LEU B N   
9787  C CA  . LEU B 111  ? 0.4373 0.4164 0.3046 0.0137  0.0091  -0.0319 109  LEU B CA  
9788  C C   . LEU B 111  ? 0.4799 0.4560 0.3491 0.0116  0.0048  -0.0304 109  LEU B C   
9789  O O   . LEU B 111  ? 0.5097 0.4852 0.3761 0.0097  0.0039  -0.0282 109  LEU B O   
9790  C CB  . LEU B 111  ? 0.4382 0.4237 0.3104 0.0131  0.0126  -0.0299 109  LEU B CB  
9791  C CG  . LEU B 111  ? 0.4076 0.3966 0.2770 0.0148  0.0172  -0.0307 109  LEU B CG  
9792  C CD1 . LEU B 111  ? 0.4190 0.4149 0.2949 0.0140  0.0201  -0.0288 109  LEU B CD1 
9793  C CD2 . LEU B 111  ? 0.4427 0.4294 0.3028 0.0143  0.0181  -0.0304 109  LEU B CD2 
9794  N N   . ARG B 112  ? 0.4362 0.4108 0.3103 0.0119  0.0021  -0.0314 110  ARG B N   
9795  C CA  . ARG B 112  ? 0.4647 0.4363 0.3401 0.0102  -0.0022 -0.0303 110  ARG B CA  
9796  C C   . ARG B 112  ? 0.5090 0.4751 0.3766 0.0100  -0.0050 -0.0312 110  ARG B C   
9797  O O   . ARG B 112  ? 0.5138 0.4776 0.3814 0.0085  -0.0086 -0.0300 110  ARG B O   
9798  C CB  . ARG B 112  ? 0.4578 0.4298 0.3410 0.0106  -0.0040 -0.0309 110  ARG B CB  
9799  C CG  . ARG B 112  ? 0.4932 0.4705 0.3841 0.0105  -0.0018 -0.0296 110  ARG B CG  
9800  C CD  . ARG B 112  ? 0.5836 0.5610 0.4819 0.0103  -0.0041 -0.0296 110  ARG B CD  
9801  N NE  . ARG B 112  ? 0.5642 0.5403 0.4640 0.0121  -0.0043 -0.0320 110  ARG B NE  
9802  C CZ  . ARG B 112  ? 0.5866 0.5656 0.4906 0.0135  -0.0020 -0.0329 110  ARG B CZ  
9803  N NH1 . ARG B 112  ? 0.6208 0.6047 0.5282 0.0135  0.0009  -0.0316 110  ARG B NH1 
9804  N NH2 . ARG B 112  ? 0.6684 0.6454 0.5732 0.0151  -0.0026 -0.0351 110  ARG B NH2 
9805  N N   . ILE B 113  ? 0.4604 0.4245 0.3216 0.0115  -0.0036 -0.0334 111  ILE B N   
9806  C CA  . ILE B 113  ? 0.4654 0.4242 0.3179 0.0112  -0.0059 -0.0343 111  ILE B CA  
9807  C C   . ILE B 113  ? 0.5454 0.5051 0.3925 0.0100  -0.0043 -0.0322 111  ILE B C   
9808  O O   . ILE B 113  ? 0.5576 0.5199 0.4020 0.0109  -0.0002 -0.0323 111  ILE B O   
9809  C CB  . ILE B 113  ? 0.4874 0.4433 0.3347 0.0133  -0.0049 -0.0376 111  ILE B CB  
9810  C CG1 . ILE B 113  ? 0.4792 0.4339 0.3319 0.0143  -0.0065 -0.0395 111  ILE B CG1 
9811  C CG2 . ILE B 113  ? 0.4994 0.4498 0.3369 0.0129  -0.0071 -0.0385 111  ILE B CG2 
9812  C CD1 . ILE B 113  ? 0.4788 0.4310 0.3275 0.0168  -0.0049 -0.0427 111  ILE B CD1 
9813  N N   . PRO B 114  ? 0.5846 0.5424 0.4299 0.0080  -0.0073 -0.0301 112  PRO B N   
9814  C CA  . PRO B 114  ? 0.5752 0.5339 0.4158 0.0067  -0.0057 -0.0278 112  PRO B CA  
9815  C C   . PRO B 114  ? 0.5300 0.4857 0.3601 0.0072  -0.0047 -0.0289 112  PRO B C   
9816  O O   . PRO B 114  ? 0.6131 0.5708 0.4394 0.0068  -0.0014 -0.0276 112  PRO B O   
9817  C CB  . PRO B 114  ? 0.5333 0.4903 0.3757 0.0047  -0.0097 -0.0253 112  PRO B CB  
9818  C CG  . PRO B 114  ? 0.5878 0.5415 0.4318 0.0051  -0.0138 -0.0271 112  PRO B CG  
9819  C CD  . PRO B 114  ? 0.5423 0.4975 0.3907 0.0069  -0.0121 -0.0296 112  PRO B CD  
9820  N N   . ASP B 115  ? 0.5491 0.5000 0.3742 0.0080  -0.0072 -0.0312 113  ASP B N   
9821  C CA  . ASP B 115  ? 0.6244 0.5716 0.4387 0.0085  -0.0066 -0.0324 113  ASP B CA  
9822  C C   . ASP B 115  ? 0.6458 0.5948 0.4581 0.0108  -0.0020 -0.0347 113  ASP B C   
9823  O O   . ASP B 115  ? 0.5964 0.5447 0.4113 0.0125  -0.0020 -0.0373 113  ASP B O   
9824  C CB  . ASP B 115  ? 0.5940 0.5353 0.4038 0.0083  -0.0114 -0.0341 113  ASP B CB  
9825  C CG  . ASP B 115  ? 0.6799 0.6169 0.4780 0.0088  -0.0110 -0.0357 113  ASP B CG  
9826  O OD1 . ASP B 115  ? 0.7376 0.6746 0.5298 0.0079  -0.0098 -0.0338 113  ASP B OD1 
9827  O OD2 . ASP B 115  ? 0.6815 0.6149 0.4761 0.0102  -0.0119 -0.0387 113  ASP B OD2 
9828  N N   . THR B 116  ? 0.5781 0.5294 0.3856 0.0109  0.0019  -0.0338 114  THR B N   
9829  C CA  . THR B 116  ? 0.6139 0.5675 0.4197 0.0133  0.0067  -0.0358 114  THR B CA  
9830  C C   . THR B 116  ? 0.6152 0.5636 0.4145 0.0153  0.0058  -0.0395 114  THR B C   
9831  O O   . THR B 116  ? 0.5951 0.5445 0.3962 0.0177  0.0082  -0.0418 114  THR B O   
9832  C CB  . THR B 116  ? 0.6348 0.5914 0.4356 0.0127  0.0107  -0.0340 114  THR B CB  
9833  N N   . ALA B 117  ? 0.5887 0.5313 0.3801 0.0144  0.0023  -0.0400 115  ALA B N   
9834  C CA  . ALA B 117  ? 0.6080 0.5450 0.3922 0.0161  0.0014  -0.0435 115  ALA B CA  
9835  C C   . ALA B 117  ? 0.5512 0.4862 0.3412 0.0169  -0.0014 -0.0456 115  ALA B C   
9836  O O   . ALA B 117  ? 0.6520 0.5850 0.4402 0.0192  0.0000  -0.0487 115  ALA B O   
9837  C CB  . ALA B 117  ? 0.5873 0.5185 0.3614 0.0147  -0.0019 -0.0434 115  ALA B CB  
9838  N N   . THR B 118  ? 0.5814 0.5168 0.3784 0.0151  -0.0052 -0.0440 116  THR B N   
9839  C CA  . THR B 118  ? 0.5699 0.5038 0.3729 0.0156  -0.0078 -0.0457 116  THR B CA  
9840  C C   . THR B 118  ? 0.5664 0.5047 0.3767 0.0176  -0.0040 -0.0465 116  THR B C   
9841  O O   . THR B 118  ? 0.5812 0.5173 0.3927 0.0192  -0.0043 -0.0491 116  THR B O   
9842  C CB  . THR B 118  ? 0.5378 0.4721 0.3472 0.0132  -0.0122 -0.0435 116  THR B CB  
9843  O OG1 . THR B 118  ? 0.6174 0.5476 0.4200 0.0115  -0.0158 -0.0427 116  THR B OG1 
9844  C CG2 . THR B 118  ? 0.5888 0.5216 0.4044 0.0136  -0.0148 -0.0451 116  THR B CG2 
9845  N N   . ARG B 119  ? 0.5525 0.4969 0.3675 0.0174  -0.0007 -0.0442 117  ARG B N   
9846  C CA  . ARG B 119  ? 0.4802 0.4295 0.3023 0.0192  0.0029  -0.0447 117  ARG B CA  
9847  C C   . ARG B 119  ? 0.5561 0.5046 0.3729 0.0222  0.0066  -0.0474 117  ARG B C   
9848  O O   . ARG B 119  ? 0.5235 0.4716 0.3434 0.0243  0.0074  -0.0496 117  ARG B O   
9849  C CB  . ARG B 119  ? 0.5002 0.4560 0.3276 0.0181  0.0056  -0.0415 117  ARG B CB  
9850  C CG  . ARG B 119  ? 0.4621 0.4236 0.2976 0.0196  0.0089  -0.0416 117  ARG B CG  
9851  C CD  . ARG B 119  ? 0.4994 0.4670 0.3378 0.0185  0.0121  -0.0387 117  ARG B CD  
9852  N NE  . ARG B 119  ? 0.4978 0.4654 0.3381 0.0155  0.0094  -0.0358 117  ARG B NE  
9853  C CZ  . ARG B 119  ? 0.6012 0.5709 0.4391 0.0138  0.0107  -0.0333 117  ARG B CZ  
9854  N NH1 . ARG B 119  ? 0.4887 0.4610 0.3222 0.0145  0.0149  -0.0332 117  ARG B NH1 
9855  N NH2 . ARG B 119  ? 0.6440 0.6130 0.4837 0.0113  0.0079  -0.0308 117  ARG B NH2 
9856  N N   . ASP B 120  ? 0.5320 0.4799 0.3404 0.0225  0.0089  -0.0474 118  ASP B N   
9857  C CA  . ASP B 120  ? 0.5333 0.4804 0.3359 0.0254  0.0126  -0.0501 118  ASP B CA  
9858  C C   . ASP B 120  ? 0.6071 0.5469 0.4047 0.0269  0.0101  -0.0536 118  ASP B C   
9859  O O   . ASP B 120  ? 0.5513 0.4905 0.3482 0.0298  0.0124  -0.0562 118  ASP B O   
9860  C CB  . ASP B 120  ? 0.5399 0.4876 0.3341 0.0252  0.0155  -0.0493 118  ASP B CB  
9861  C CG  . ASP B 120  ? 0.6429 0.5982 0.4421 0.0242  0.0189  -0.0461 118  ASP B CG  
9862  O OD1 . ASP B 120  ? 0.6257 0.5856 0.4348 0.0237  0.0191  -0.0447 118  ASP B OD1 
9863  O OD2 . ASP B 120  ? 0.6918 0.6484 0.4849 0.0237  0.0214  -0.0449 118  ASP B OD2 
9864  N N   . ALA B 121  ? 0.5699 0.5042 0.3641 0.0249  0.0051  -0.0537 119  ALA B N   
9865  C CA  . ALA B 121  ? 0.6366 0.5640 0.4264 0.0258  0.0023  -0.0570 119  ALA B CA  
9866  C C   . ALA B 121  ? 0.5700 0.4978 0.3684 0.0268  0.0013  -0.0580 119  ALA B C   
9867  O O   . ALA B 121  ? 0.5884 0.5124 0.3844 0.0290  0.0018  -0.0611 119  ALA B O   
9868  C CB  . ALA B 121  ? 0.6114 0.5333 0.3960 0.0232  -0.0030 -0.0567 119  ALA B CB  
9869  N N   . LEU B 122  ? 0.5412 0.4734 0.3493 0.0251  0.0001  -0.0556 120  LEU B N   
9870  C CA  . LEU B 122  ? 0.5311 0.4639 0.3474 0.0259  -0.0007 -0.0563 120  LEU B CA  
9871  C C   . LEU B 122  ? 0.5459 0.4821 0.3648 0.0290  0.0040  -0.0575 120  LEU B C   
9872  O O   . LEU B 122  ? 0.5300 0.4638 0.3507 0.0308  0.0038  -0.0597 120  LEU B O   
9873  C CB  . LEU B 122  ? 0.5594 0.4966 0.3853 0.0235  -0.0026 -0.0533 120  LEU B CB  
9874  C CG  . LEU B 122  ? 0.5524 0.4899 0.3867 0.0238  -0.0041 -0.0537 120  LEU B CG  
9875  C CD1 . LEU B 122  ? 0.6133 0.5441 0.4447 0.0230  -0.0086 -0.0557 120  LEU B CD1 
9876  C CD2 . LEU B 122  ? 0.5263 0.4691 0.3699 0.0219  -0.0049 -0.0507 120  LEU B CD2 
9877  N N   . ILE B 123  ? 0.4841 0.4260 0.3033 0.0297  0.0083  -0.0561 121  ILE B N   
9878  C CA  . ILE B 123  ? 0.5167 0.4626 0.3385 0.0328  0.0130  -0.0570 121  ILE B CA  
9879  C C   . ILE B 123  ? 0.5847 0.5253 0.3985 0.0358  0.0143  -0.0606 121  ILE B C   
9880  O O   . ILE B 123  ? 0.5289 0.4684 0.3451 0.0384  0.0152  -0.0626 121  ILE B O   
9881  C CB  . ILE B 123  ? 0.4644 0.4173 0.2873 0.0326  0.0171  -0.0546 121  ILE B CB  
9882  C CG1 . ILE B 123  ? 0.4226 0.3809 0.2544 0.0300  0.0160  -0.0512 121  ILE B CG1 
9883  C CG2 . ILE B 123  ? 0.4791 0.4362 0.3033 0.0361  0.0221  -0.0558 121  ILE B CG2 
9884  C CD1 . ILE B 123  ? 0.4298 0.3941 0.2619 0.0289  0.0193  -0.0486 121  ILE B CD1 
9885  N N   . ARG B 124  ? 0.5303 0.4670 0.3340 0.0357  0.0143  -0.0616 122  ARG B N   
9886  C CA  . ARG B 124  ? 0.6338 0.5655 0.4288 0.0387  0.0161  -0.0650 122  ARG B CA  
9887  C C   . ARG B 124  ? 0.6608 0.5844 0.4534 0.0390  0.0121  -0.0678 122  ARG B C   
9888  O O   . ARG B 124  ? 0.7505 0.6706 0.5397 0.0420  0.0137  -0.0708 122  ARG B O   
9889  C CB  . ARG B 124  ? 0.6507 0.5805 0.4353 0.0382  0.0172  -0.0651 122  ARG B CB  
9890  N N   . ASP B 125  ? 0.6159 0.5365 0.4101 0.0358  0.0070  -0.0669 123  ASP B N   
9891  C CA  . ASP B 125  ? 0.7128 0.6255 0.5038 0.0356  0.0029  -0.0694 123  ASP B CA  
9892  C C   . ASP B 125  ? 0.6631 0.5762 0.4635 0.0353  0.0009  -0.0693 123  ASP B C   
9893  O O   . ASP B 125  ? 0.7085 0.6154 0.5067 0.0360  -0.0013 -0.0718 123  ASP B O   
9894  C CB  . ASP B 125  ? 0.7360 0.6444 0.5218 0.0323  -0.0018 -0.0688 123  ASP B CB  
9895  C CG  . ASP B 125  ? 0.8143 0.7217 0.5902 0.0322  -0.0003 -0.0688 123  ASP B CG  
9896  O OD1 . ASP B 125  ? 0.8019 0.7094 0.5725 0.0351  0.0040  -0.0704 123  ASP B OD1 
9897  O OD2 . ASP B 125  ? 0.8387 0.7452 0.6121 0.0294  -0.0034 -0.0671 123  ASP B OD2 
9898  N N   . LYS B 126  ? 0.5972 0.5172 0.4075 0.0343  0.0016  -0.0665 124  LYS B N   
9899  C CA  . LYS B 126  ? 0.6423 0.5626 0.4613 0.0339  -0.0005 -0.0662 124  LYS B CA  
9900  C C   . LYS B 126  ? 0.6373 0.5642 0.4647 0.0358  0.0032  -0.0652 124  LYS B C   
9901  O O   . LYS B 126  ? 0.6825 0.6082 0.5139 0.0372  0.0031  -0.0663 124  LYS B O   
9902  C CB  . LYS B 126  ? 0.6660 0.5869 0.4895 0.0301  -0.0049 -0.0638 124  LYS B CB  
9903  N N   . ILE B 127  ? 0.5744 0.5084 0.4046 0.0357  0.0064  -0.0629 125  ILE B N   
9904  C CA  . ILE B 127  ? 0.5152 0.4560 0.3541 0.0370  0.0094  -0.0615 125  ILE B CA  
9905  C C   . ILE B 127  ? 0.5813 0.5228 0.4181 0.0411  0.0137  -0.0636 125  ILE B C   
9906  O O   . ILE B 127  ? 0.5452 0.4883 0.3877 0.0430  0.0148  -0.0641 125  ILE B O   
9907  C CB  . ILE B 127  ? 0.4940 0.4421 0.3376 0.0351  0.0108  -0.0581 125  ILE B CB  
9908  C CG1 . ILE B 127  ? 0.5037 0.4506 0.3486 0.0314  0.0066  -0.0562 125  ILE B CG1 
9909  C CG2 . ILE B 127  ? 0.4802 0.4349 0.3334 0.0361  0.0132  -0.0568 125  ILE B CG2 
9910  C CD1 . ILE B 127  ? 0.6182 0.5632 0.4694 0.0302  0.0030  -0.0561 125  ILE B CD1 
9911  N N   . ALA B 128  ? 0.4969 0.4374 0.3255 0.0425  0.0162  -0.0648 126  ALA B N   
9912  C CA  . ALA B 128  ? 0.5275 0.4690 0.3537 0.0465  0.0206  -0.0668 126  ALA B CA  
9913  C C   . ALA B 128  ? 0.6540 0.5886 0.4778 0.0491  0.0194  -0.0701 126  ALA B C   
9914  O O   . ALA B 128  ? 0.6279 0.5638 0.4526 0.0527  0.0227  -0.0715 126  ALA B O   
9915  C CB  . ALA B 128  ? 0.5329 0.4744 0.3503 0.0474  0.0234  -0.0674 126  ALA B CB  
9916  N N   . ASP B 129  ? 0.6388 0.5660 0.4595 0.0472  0.0149  -0.0712 127  ASP B N   
9917  C CA  . ASP B 129  ? 0.7328 0.6531 0.5519 0.0489  0.0131  -0.0740 127  ASP B CA  
9918  C C   . ASP B 129  ? 0.7756 0.6978 0.6046 0.0484  0.0115  -0.0729 127  ASP B C   
9919  O O   . ASP B 129  ? 0.8830 0.7990 0.7116 0.0486  0.0089  -0.0746 127  ASP B O   
9920  C CB  . ASP B 129  ? 0.7740 0.6855 0.5850 0.0469  0.0088  -0.0758 127  ASP B CB  
9921  N N   . GLY B 130  ? 0.7741 0.7044 0.6118 0.0475  0.0129  -0.0699 128  GLY B N   
9922  C CA  . GLY B 130  ? 0.7597 0.6925 0.6068 0.0472  0.0119  -0.0687 128  GLY B CA  
9923  C C   . GLY B 130  ? 0.8397 0.7701 0.6904 0.0435  0.0071  -0.0675 128  GLY B C   
9924  O O   . GLY B 130  ? 0.7911 0.7246 0.6500 0.0428  0.0064  -0.0660 128  GLY B O   
9925  N N   . ASN B 131  ? 0.9013 0.8265 0.7461 0.0412  0.0038  -0.0681 129  ASN B N   
9926  C CA  . ASN B 131  ? 0.9264 0.8496 0.7747 0.0377  -0.0008 -0.0670 129  ASN B CA  
9927  C C   . ASN B 131  ? 0.8570 0.7869 0.7115 0.0351  -0.0011 -0.0636 129  ASN B C   
9928  O O   . ASN B 131  ? 0.9159 0.8446 0.7694 0.0322  -0.0043 -0.0625 129  ASN B O   
9929  C CB  . ASN B 131  ? 0.9214 0.8370 0.7613 0.0361  -0.0043 -0.0687 129  ASN B CB  
9930  N N   . TRP B 132  ? 0.7270 0.6639 0.5881 0.0361  0.0020  -0.0618 130  TRP B N   
9931  C CA  . TRP B 132  ? 0.6616 0.6048 0.5280 0.0338  0.0021  -0.0587 130  TRP B CA  
9932  C C   . TRP B 132  ? 0.6252 0.5692 0.4990 0.0314  -0.0012 -0.0570 130  TRP B C   
9933  O O   . TRP B 132  ? 0.7261 0.6729 0.6026 0.0289  -0.0025 -0.0547 130  TRP B O   
9934  C CB  . TRP B 132  ? 0.6112 0.5618 0.4816 0.0356  0.0065  -0.0575 130  TRP B CB  
9935  C CG  . TRP B 132  ? 0.4951 0.4481 0.3724 0.0375  0.0079  -0.0576 130  TRP B CG  
9936  C CD1 . TRP B 132  ? 0.5047 0.4569 0.3809 0.0410  0.0104  -0.0596 130  TRP B CD1 
9937  C CD2 . TRP B 132  ? 0.4513 0.4079 0.3374 0.0361  0.0068  -0.0556 130  TRP B CD2 
9938  N NE1 . TRP B 132  ? 0.4619 0.4170 0.3458 0.0418  0.0108  -0.0588 130  TRP B NE1 
9939  C CE2 . TRP B 132  ? 0.3989 0.3567 0.2888 0.0388  0.0086  -0.0564 130  TRP B CE2 
9940  C CE3 . TRP B 132  ? 0.4320 0.3908 0.3230 0.0330  0.0045  -0.0532 130  TRP B CE3 
9941  C CZ2 . TRP B 132  ? 0.3675 0.3286 0.2656 0.0383  0.0081  -0.0549 130  TRP B CZ2 
9942  C CZ3 . TRP B 132  ? 0.3784 0.3405 0.2775 0.0326  0.0041  -0.0519 130  TRP B CZ3 
9943  C CH2 . TRP B 132  ? 0.4028 0.3660 0.3053 0.0352  0.0059  -0.0527 130  TRP B CH2 
9944  N N   . LYS B 133  ? 0.6530 0.5944 0.5301 0.0321  -0.0023 -0.0581 131  LYS B N   
9945  C CA  . LYS B 133  ? 0.6933 0.6356 0.5775 0.0299  -0.0051 -0.0565 131  LYS B CA  
9946  C C   . LYS B 133  ? 0.8256 0.7645 0.7076 0.0269  -0.0093 -0.0561 131  LYS B C   
9947  O O   . LYS B 133  ? 0.8629 0.8050 0.7494 0.0246  -0.0107 -0.0538 131  LYS B O   
9948  C CB  . LYS B 133  ? 0.6917 0.6311 0.5788 0.0313  -0.0056 -0.0579 131  LYS B CB  
9949  N N   . SER B 134  ? 0.8736 0.8059 0.7485 0.0269  -0.0112 -0.0583 132  SER B N   
9950  C CA  . SER B 134  ? 0.8658 0.7947 0.7384 0.0240  -0.0155 -0.0581 132  SER B CA  
9951  C C   . SER B 134  ? 0.9210 0.8527 0.7912 0.0226  -0.0156 -0.0563 132  SER B C   
9952  O O   . SER B 134  ? 0.9281 0.8618 0.8022 0.0202  -0.0180 -0.0542 132  SER B O   
9953  C CB  . SER B 134  ? 0.7849 0.7060 0.6498 0.0244  -0.0175 -0.0610 132  SER B CB  
9954  N N   . HIS B 135  ? 0.9472 0.8791 0.8111 0.0241  -0.0128 -0.0570 133  HIS B N   
9955  C CA  . HIS B 135  ? 0.9481 0.8813 0.8080 0.0227  -0.0131 -0.0556 133  HIS B CA  
9956  C C   . HIS B 135  ? 0.9582 0.8980 0.8250 0.0213  -0.0123 -0.0524 133  HIS B C   
9957  O O   . HIS B 135  ? 1.0051 0.9456 0.8709 0.0193  -0.0142 -0.0507 133  HIS B O   
9958  C CB  . HIS B 135  ? 0.8387 0.7711 0.6906 0.0247  -0.0099 -0.0570 133  HIS B CB  
9959  N N   . LEU B 136  ? 0.8888 0.8333 0.7624 0.0224  -0.0097 -0.0515 134  LEU B N   
9960  C CA  . LEU B 136  ? 0.8234 0.7739 0.7035 0.0211  -0.0089 -0.0486 134  LEU B CA  
9961  C C   . LEU B 136  ? 0.8247 0.7774 0.7137 0.0207  -0.0099 -0.0477 134  LEU B C   
9962  O O   . LEU B 136  ? 0.6937 0.6504 0.5883 0.0193  -0.0101 -0.0454 134  LEU B O   
9963  C CB  . LEU B 136  ? 0.7558 0.7113 0.6357 0.0226  -0.0044 -0.0479 134  LEU B CB  
9964  C CG  . LEU B 136  ? 0.6428 0.5974 0.5145 0.0228  -0.0029 -0.0481 134  LEU B CG  
9965  C CD1 . LEU B 136  ? 0.5711 0.5312 0.4437 0.0242  0.0017  -0.0473 134  LEU B CD1 
9966  C CD2 . LEU B 136  ? 0.7119 0.6660 0.5820 0.0200  -0.0056 -0.0461 134  LEU B CD2 
9967  N N   . ARG B 140  ? 0.5103 0.4758 0.4343 0.0140  -0.0163 -0.0390 138  ARG B N   
9968  C CA  . ARG B 140  ? 0.5663 0.5366 0.4937 0.0147  -0.0131 -0.0377 138  ARG B CA  
9969  C C   . ARG B 140  ? 0.5576 0.5284 0.4822 0.0168  -0.0099 -0.0392 138  ARG B C   
9970  O O   . ARG B 140  ? 0.4712 0.4396 0.3894 0.0176  -0.0094 -0.0405 138  ARG B O   
9971  C CB  . ARG B 140  ? 0.5357 0.5082 0.4621 0.0134  -0.0129 -0.0357 138  ARG B CB  
9972  N N   . SER B 141  ? 0.4416 0.4155 0.3711 0.0179  -0.0078 -0.0390 139  SER B N   
9973  C CA  . SER B 141  ? 0.3871 0.3623 0.3150 0.0202  -0.0048 -0.0403 139  SER B CA  
9974  C C   . SER B 141  ? 0.4071 0.3844 0.3308 0.0205  -0.0024 -0.0398 139  SER B C   
9975  O O   . SER B 141  ? 0.4002 0.3801 0.3248 0.0189  -0.0023 -0.0379 139  SER B O   
9976  C CB  . SER B 141  ? 0.4105 0.3897 0.3451 0.0210  -0.0031 -0.0395 139  SER B CB  
9977  O OG  . SER B 141  ? 0.4384 0.4193 0.3720 0.0234  -0.0001 -0.0406 139  SER B OG  
9978  N N   . LEU B 142  ? 0.3614 0.3373 0.2801 0.0224  -0.0006 -0.0416 140  LEU B N   
9979  C CA  . LEU B 142  ? 0.3454 0.3242 0.2608 0.0230  0.0023  -0.0412 140  LEU B CA  
9980  C C   . LEU B 142  ? 0.3022 0.2874 0.2232 0.0230  0.0049  -0.0395 140  LEU B C   
9981  O O   . LEU B 142  ? 0.3111 0.2996 0.2309 0.0224  0.0068  -0.0382 140  LEU B O   
9982  C CB  . LEU B 142  ? 0.3295 0.3062 0.2397 0.0257  0.0043  -0.0436 140  LEU B CB  
9983  C CG  . LEU B 142  ? 0.3936 0.3703 0.2970 0.0258  0.0060  -0.0438 140  LEU B CG  
9984  C CD1 . LEU B 142  ? 0.4263 0.3977 0.3242 0.0241  0.0028  -0.0441 140  LEU B CD1 
9985  C CD2 . LEU B 142  ? 0.4315 0.4072 0.3310 0.0289  0.0086  -0.0460 140  LEU B CD2 
9986  N N   . PHE B 143  ? 0.2833 0.2703 0.2104 0.0236  0.0050  -0.0393 141  PHE B N   
9987  C CA  . PHE B 143  ? 0.2835 0.2764 0.2158 0.0241  0.0075  -0.0381 141  PHE B CA  
9988  C C   . PHE B 143  ? 0.2982 0.2938 0.2360 0.0218  0.0064  -0.0359 141  PHE B C   
9989  O O   . PHE B 143  ? 0.3039 0.3039 0.2467 0.0220  0.0079  -0.0349 141  PHE B O   
9990  C CB  . PHE B 143  ? 0.2733 0.2666 0.2081 0.0267  0.0087  -0.0396 141  PHE B CB  
9991  C CG  . PHE B 143  ? 0.2713 0.2612 0.2004 0.0291  0.0097  -0.0419 141  PHE B CG  
9992  C CD1 . PHE B 143  ? 0.2886 0.2803 0.2133 0.0302  0.0123  -0.0423 141  PHE B CD1 
9993  C CD2 . PHE B 143  ? 0.2673 0.2520 0.1950 0.0302  0.0079  -0.0438 141  PHE B CD2 
9994  C CE1 . PHE B 143  ? 0.3049 0.2933 0.2240 0.0325  0.0133  -0.0446 141  PHE B CE1 
9995  C CE2 . PHE B 143  ? 0.2927 0.2736 0.2147 0.0325  0.0087  -0.0461 141  PHE B CE2 
9996  C CZ  . PHE B 143  ? 0.2832 0.2659 0.2007 0.0337  0.0115  -0.0466 141  PHE B CZ  
9997  N N   . VAL B 144  ? 0.3082 0.3013 0.2450 0.0197  0.0038  -0.0350 142  VAL B N   
9998  C CA  . VAL B 144  ? 0.3117 0.3068 0.2534 0.0177  0.0027  -0.0329 142  VAL B CA  
9999  C C   . VAL B 144  ? 0.3477 0.3480 0.2915 0.0170  0.0051  -0.0313 142  VAL B C   
10000 O O   . VAL B 144  ? 0.3273 0.3304 0.2765 0.0164  0.0053  -0.0301 142  VAL B O   
10001 C CB  . VAL B 144  ? 0.3646 0.3563 0.3040 0.0158  -0.0002 -0.0322 142  VAL B CB  
10002 C CG1 . VAL B 144  ? 0.3779 0.3716 0.3217 0.0139  -0.0011 -0.0300 142  VAL B CG1 
10003 C CG2 . VAL B 144  ? 0.3820 0.3691 0.3206 0.0161  -0.0029 -0.0336 142  VAL B CG2 
10004 N N   . ASN B 145  ? 0.3075 0.3092 0.2472 0.0171  0.0071  -0.0311 143  ASN B N   
10005 C CA  . ASN B 145  ? 0.3174 0.3241 0.2589 0.0161  0.0094  -0.0294 143  ASN B CA  
10006 C C   . ASN B 145  ? 0.3221 0.3331 0.2647 0.0181  0.0126  -0.0300 143  ASN B C   
10007 O O   . ASN B 145  ? 0.3309 0.3461 0.2735 0.0175  0.0150  -0.0289 143  ASN B O   
10008 C CB  . ASN B 145  ? 0.3576 0.3635 0.2942 0.0144  0.0095  -0.0281 143  ASN B CB  
10009 C CG  . ASN B 145  ? 0.4591 0.4624 0.3961 0.0123  0.0067  -0.0267 143  ASN B CG  
10010 O OD1 . ASN B 145  ? 0.4732 0.4778 0.4154 0.0113  0.0058  -0.0257 143  ASN B OD1 
10011 N ND2 . ASN B 145  ? 0.4516 0.4512 0.3833 0.0115  0.0052  -0.0267 143  ASN B ND2 
10012 N N   . ALA B 146  ? 0.3022 0.3124 0.2461 0.0204  0.0128  -0.0318 144  ALA B N   
10013 C CA  . ALA B 146  ? 0.3059 0.3200 0.2507 0.0227  0.0158  -0.0326 144  ALA B CA  
10014 C C   . ALA B 146  ? 0.3031 0.3233 0.2539 0.0221  0.0173  -0.0310 144  ALA B C   
10015 O O   . ALA B 146  ? 0.3287 0.3536 0.2803 0.0234  0.0201  -0.0310 144  ALA B O   
10016 C CB  . ALA B 146  ? 0.2911 0.3022 0.2357 0.0254  0.0153  -0.0348 144  ALA B CB  
10017 N N   . ALA B 147  ? 0.2875 0.3080 0.2427 0.0203  0.0156  -0.0297 145  ALA B N   
10018 C CA  . ALA B 147  ? 0.2985 0.3248 0.2589 0.0195  0.0169  -0.0282 145  ALA B CA  
10019 C C   . ALA B 147  ? 0.3301 0.3599 0.2890 0.0177  0.0187  -0.0266 145  ALA B C   
10020 O O   . ALA B 147  ? 0.3409 0.3763 0.3025 0.0178  0.0210  -0.0258 145  ALA B O   
10021 C CB  . ALA B 147  ? 0.3275 0.3528 0.2922 0.0178  0.0146  -0.0272 145  ALA B CB  
10022 N N   . THR B 148  ? 0.3222 0.3488 0.2767 0.0160  0.0177  -0.0260 146  THR B N   
10023 C CA  . THR B 148  ? 0.3150 0.3444 0.2673 0.0143  0.0195  -0.0245 146  THR B CA  
10024 C C   . THR B 148  ? 0.3332 0.3653 0.2825 0.0161  0.0225  -0.0253 146  THR B C   
10025 O O   . THR B 148  ? 0.3442 0.3818 0.2952 0.0156  0.0250  -0.0242 146  THR B O   
10026 C CB  . THR B 148  ? 0.4102 0.4349 0.3582 0.0122  0.0175  -0.0236 146  THR B CB  
10027 O OG1 . THR B 148  ? 0.4472 0.4700 0.3986 0.0106  0.0149  -0.0227 146  THR B OG1 
10028 C CG2 . THR B 148  ? 0.4483 0.4755 0.3937 0.0102  0.0192  -0.0218 146  THR B CG2 
10029 N N   . TRP B 149  ? 0.3232 0.3516 0.2683 0.0184  0.0224  -0.0274 147  TRP B N   
10030 C CA  . TRP B 149  ? 0.3149 0.3457 0.2570 0.0205  0.0254  -0.0284 147  TRP B CA  
10031 C C   . TRP B 149  ? 0.3039 0.3400 0.2511 0.0227  0.0275  -0.0289 147  TRP B C   
10032 O O   . TRP B 149  ? 0.3227 0.3636 0.2695 0.0238  0.0307  -0.0288 147  TRP B O   
10033 C CB  . TRP B 149  ? 0.3272 0.3522 0.2630 0.0224  0.0247  -0.0306 147  TRP B CB  
10034 C CG  . TRP B 149  ? 0.3100 0.3305 0.2403 0.0203  0.0229  -0.0300 147  TRP B CG  
10035 C CD1 . TRP B 149  ? 0.3467 0.3613 0.2750 0.0196  0.0195  -0.0306 147  TRP B CD1 
10036 C CD2 . TRP B 149  ? 0.3633 0.3852 0.2895 0.0186  0.0244  -0.0286 147  TRP B CD2 
10037 N NE1 . TRP B 149  ? 0.3519 0.3639 0.2751 0.0177  0.0187  -0.0296 147  TRP B NE1 
10038 C CE2 . TRP B 149  ? 0.3475 0.3637 0.2691 0.0170  0.0216  -0.0284 147  TRP B CE2 
10039 C CE3 . TRP B 149  ? 0.4045 0.4319 0.3304 0.0183  0.0278  -0.0274 147  TRP B CE3 
10040 C CZ2 . TRP B 149  ? 0.3934 0.4089 0.3099 0.0152  0.0221  -0.0270 147  TRP B CZ2 
10041 C CZ3 . TRP B 149  ? 0.4158 0.4426 0.3367 0.0163  0.0284  -0.0261 147  TRP B CZ3 
10042 C CH2 . TRP B 149  ? 0.4351 0.4558 0.3511 0.0148  0.0255  -0.0258 147  TRP B CH2 
10043 N N   . GLY B 150  ? 0.3032 0.3388 0.2551 0.0234  0.0259  -0.0293 148  GLY B N   
10044 C CA  . GLY B 150  ? 0.3151 0.3561 0.2724 0.0253  0.0276  -0.0294 148  GLY B CA  
10045 C C   . GLY B 150  ? 0.3066 0.3546 0.2678 0.0234  0.0294  -0.0272 148  GLY B C   
10046 O O   . GLY B 150  ? 0.3108 0.3646 0.2741 0.0249  0.0321  -0.0272 148  GLY B O   
10047 N N   . LEU B 151  ? 0.3197 0.3673 0.2817 0.0200  0.0279  -0.0254 149  LEU B N   
10048 C CA  A LEU B 151  ? 0.3702 0.4238 0.3353 0.0177  0.0295  -0.0233 149  LEU B CA  
10049 C CA  B LEU B 151  ? 0.3701 0.4238 0.3353 0.0177  0.0295  -0.0233 149  LEU B CA  
10050 C C   . LEU B 151  ? 0.3707 0.4274 0.3322 0.0176  0.0324  -0.0228 149  LEU B C   
10051 O O   . LEU B 151  ? 0.3924 0.4560 0.3569 0.0176  0.0350  -0.0218 149  LEU B O   
10052 C CB  A LEU B 151  ? 0.3957 0.4470 0.3615 0.0142  0.0272  -0.0215 149  LEU B CB  
10053 C CB  B LEU B 151  ? 0.3956 0.4469 0.3615 0.0142  0.0271  -0.0216 149  LEU B CB  
10054 C CG  A LEU B 151  ? 0.3953 0.4493 0.3673 0.0128  0.0261  -0.0204 149  LEU B CG  
10055 C CG  B LEU B 151  ? 0.4099 0.4664 0.3803 0.0115  0.0277  -0.0194 149  LEU B CG  
10056 C CD1 A LEU B 151  ? 0.4419 0.4930 0.4134 0.0094  0.0240  -0.0188 149  LEU B CD1 
10057 C CD1 B LEU B 151  ? 0.4162 0.4780 0.3926 0.0130  0.0285  -0.0196 149  LEU B CD1 
10058 C CD2 A LEU B 151  ? 0.4166 0.4786 0.3928 0.0127  0.0286  -0.0194 149  LEU B CD2 
10059 C CD2 B LEU B 151  ? 0.4392 0.4916 0.4100 0.0088  0.0249  -0.0183 149  LEU B CD2 
10060 N N   . VAL B 152  ? 0.3592 0.4111 0.3142 0.0177  0.0322  -0.0235 150  VAL B N   
10061 C CA  . VAL B 152  ? 0.3976 0.4519 0.3483 0.0176  0.0351  -0.0231 150  VAL B CA  
10062 C C   . VAL B 152  ? 0.3741 0.4327 0.3255 0.0212  0.0381  -0.0246 150  VAL B C   
10063 O O   . VAL B 152  ? 0.4027 0.4675 0.3548 0.0211  0.0412  -0.0236 150  VAL B O   
10064 C CB  . VAL B 152  ? 0.3184 0.3661 0.2615 0.0172  0.0339  -0.0237 150  VAL B CB  
10065 C CG1 . VAL B 152  ? 0.4269 0.4768 0.3650 0.0176  0.0370  -0.0236 150  VAL B CG1 
10066 C CG2 . VAL B 152  ? 0.3958 0.4401 0.3384 0.0137  0.0312  -0.0219 150  VAL B CG2 
10067 N N   . VAL B 153  ? 0.3465 0.4019 0.2976 0.0243  0.0373  -0.0268 151  VAL B N   
10068 C CA  . VAL B 153  ? 0.3357 0.3937 0.2863 0.0281  0.0401  -0.0285 151  VAL B CA  
10069 C C   . VAL B 153  ? 0.3529 0.4181 0.3109 0.0294  0.0415  -0.0280 151  VAL B C   
10070 O O   . VAL B 153  ? 0.3554 0.4265 0.3145 0.0313  0.0447  -0.0280 151  VAL B O   
10071 C CB  . VAL B 153  ? 0.3384 0.3893 0.2849 0.0309  0.0385  -0.0312 151  VAL B CB  
10072 C CG1 . VAL B 153  ? 0.3495 0.4027 0.2960 0.0352  0.0411  -0.0331 151  VAL B CG1 
10073 C CG2 . VAL B 153  ? 0.3481 0.3927 0.2868 0.0298  0.0375  -0.0318 151  VAL B CG2 
10074 N N   . THR B 154  ? 0.3422 0.4071 0.3053 0.0286  0.0391  -0.0275 152  THR B N   
10075 C CA  . THR B 154  ? 0.3711 0.4417 0.3409 0.0302  0.0398  -0.0273 152  THR B CA  
10076 C C   . THR B 154  ? 0.4078 0.4840 0.3833 0.0269  0.0395  -0.0248 152  THR B C   
10077 O O   . THR B 154  ? 0.4298 0.5122 0.4110 0.0279  0.0405  -0.0242 152  THR B O   
10078 C CB  . THR B 154  ? 0.3403 0.4063 0.3117 0.0322  0.0373  -0.0288 152  THR B CB  
10079 O OG1 . THR B 154  ? 0.3478 0.4110 0.3213 0.0292  0.0343  -0.0277 152  THR B OG1 
10080 C CG2 . THR B 154  ? 0.4029 0.4617 0.3682 0.0345  0.0368  -0.0312 152  THR B CG2 
10081 N N   . GLY B 155  ? 0.3396 0.4136 0.3137 0.0231  0.0380  -0.0233 153  GLY B N   
10082 C CA  . GLY B 155  ? 0.3861 0.4640 0.3650 0.0199  0.0373  -0.0211 153  GLY B CA  
10083 C C   . GLY B 155  ? 0.4117 0.4876 0.3948 0.0196  0.0344  -0.0212 153  GLY B C   
10084 O O   . GLY B 155  ? 0.4515 0.5304 0.4386 0.0170  0.0336  -0.0195 153  GLY B O   
10085 N N   . LYS B 156  ? 0.3932 0.4637 0.3750 0.0220  0.0328  -0.0230 154  LYS B N   
10086 C CA  . LYS B 156  ? 0.4147 0.4831 0.4001 0.0219  0.0302  -0.0231 154  LYS B CA  
10087 C C   . LYS B 156  ? 0.3905 0.4510 0.3724 0.0209  0.0274  -0.0238 154  LYS B C   
10088 O O   . LYS B 156  ? 0.3901 0.4460 0.3668 0.0218  0.0274  -0.0249 154  LYS B O   
10089 C CB  . LYS B 156  ? 0.4987 0.5683 0.4867 0.0257  0.0306  -0.0246 154  LYS B CB  
10090 N N   . LEU B 157  ? 0.3707 0.4296 0.3554 0.0190  0.0251  -0.0230 155  LEU B N   
10091 C CA  . LEU B 157  ? 0.4001 0.4521 0.3823 0.0179  0.0225  -0.0233 155  LEU B CA  
10092 C C   . LEU B 157  ? 0.4898 0.5390 0.4742 0.0197  0.0207  -0.0245 155  LEU B C   
10093 O O   . LEU B 157  ? 0.5144 0.5669 0.5032 0.0204  0.0208  -0.0242 155  LEU B O   
10094 C CB  . LEU B 157  ? 0.4516 0.5035 0.4349 0.0143  0.0212  -0.0215 155  LEU B CB  
10095 C CG  . LEU B 157  ? 0.5717 0.6170 0.5531 0.0131  0.0184  -0.0216 155  LEU B CG  
10096 C CD1 . LEU B 157  ? 0.4481 0.4894 0.4237 0.0130  0.0183  -0.0221 155  LEU B CD1 
10097 C CD2 . LEU B 157  ? 0.4996 0.5451 0.4831 0.0101  0.0172  -0.0199 155  LEU B CD2 
10098 N N   . THR B 158  ? 0.4931 0.5360 0.4742 0.0203  0.0191  -0.0257 156  THR B N   
10099 C CA  . THR B 158  ? 0.5096 0.5490 0.4925 0.0212  0.0170  -0.0264 156  THR B CA  
10100 C C   . THR B 158  ? 0.5169 0.5512 0.4980 0.0191  0.0146  -0.0261 156  THR B C   
10101 O O   . THR B 158  ? 0.4705 0.5029 0.4479 0.0178  0.0145  -0.0258 156  THR B O   
10102 C CB  . THR B 158  ? 0.5335 0.5701 0.5144 0.0243  0.0173  -0.0284 156  THR B CB  
10103 O OG1 . THR B 158  ? 0.4822 0.5142 0.4576 0.0244  0.0168  -0.0294 156  THR B OG1 
10104 C CG2 . THR B 158  ? 0.5135 0.5551 0.4957 0.0268  0.0198  -0.0288 156  THR B CG2 
10105 N N   . SER B 159  ? 0.4278 0.4599 0.4115 0.0188  0.0128  -0.0261 157  SER B N   
10106 C CA  . SER B 159  ? 0.4504 0.4780 0.4330 0.0171  0.0105  -0.0258 157  SER B CA  
10107 C C   . SER B 159  ? 0.4047 0.4272 0.3838 0.0183  0.0093  -0.0273 157  SER B C   
10108 O O   . SER B 159  ? 0.4212 0.4402 0.3977 0.0170  0.0078  -0.0271 157  SER B O   
10109 C CB  . SER B 159  ? 0.4342 0.4617 0.4210 0.0164  0.0091  -0.0252 157  SER B CB  
10110 O OG  . SER B 159  ? 0.6035 0.6328 0.5930 0.0184  0.0097  -0.0259 157  SER B OG  
10111 N N   . THR B 160  ? 0.3610 0.3828 0.3397 0.0207  0.0099  -0.0288 158  THR B N   
10112 C CA  . THR B 160  ? 0.3208 0.3374 0.2960 0.0218  0.0087  -0.0303 158  THR B CA  
10113 C C   . THR B 160  ? 0.2924 0.3094 0.2647 0.0243  0.0106  -0.0317 158  THR B C   
10114 O O   . THR B 160  ? 0.3502 0.3718 0.3241 0.0255  0.0127  -0.0315 158  THR B O   
10115 C CB  . THR B 160  ? 0.3501 0.3637 0.3276 0.0223  0.0069  -0.0308 158  THR B CB  
10116 O OG1 . THR B 160  ? 0.3726 0.3891 0.3535 0.0240  0.0080  -0.0309 158  THR B OG1 
10117 C CG2 . THR B 160  ? 0.3486 0.3615 0.3286 0.0200  0.0051  -0.0295 158  THR B CG2 
10118 N N   . VAL B 161  ? 0.2541 0.2662 0.2223 0.0252  0.0096  -0.0333 159  VAL B N   
10119 C CA  . VAL B 161  ? 0.2963 0.3075 0.2599 0.0271  0.0111  -0.0347 159  VAL B CA  
10120 C C   . VAL B 161  ? 0.2670 0.2745 0.2298 0.0295  0.0106  -0.0366 159  VAL B C   
10121 O O   . VAL B 161  ? 0.2554 0.2586 0.2184 0.0289  0.0083  -0.0370 159  VAL B O   
10122 C CB  . VAL B 161  ? 0.3567 0.3646 0.3151 0.0256  0.0101  -0.0349 159  VAL B CB  
10123 C CG1 . VAL B 161  ? 0.4563 0.4605 0.4091 0.0275  0.0105  -0.0369 159  VAL B CG1 
10124 C CG2 . VAL B 161  ? 0.4896 0.5015 0.4477 0.0239  0.0115  -0.0332 159  VAL B CG2 
10125 N N   . ASN B 162  ? 0.2509 0.2599 0.2128 0.0322  0.0128  -0.0376 160  ASN B N   
10126 C CA  . ASN B 162  ? 0.2627 0.2674 0.2230 0.0346  0.0123  -0.0395 160  ASN B CA  
10127 C C   . ASN B 162  ? 0.2487 0.2484 0.2023 0.0350  0.0119  -0.0412 160  ASN B C   
10128 O O   . ASN B 162  ? 0.2646 0.2647 0.2145 0.0369  0.0139  -0.0423 160  ASN B O   
10129 C CB  . ASN B 162  ? 0.2604 0.2683 0.2226 0.0377  0.0146  -0.0400 160  ASN B CB  
10130 C CG  . ASN B 162  ? 0.2612 0.2640 0.2218 0.0402  0.0139  -0.0418 160  ASN B CG  
10131 O OD1 . ASN B 162  ? 0.2711 0.2678 0.2277 0.0399  0.0122  -0.0431 160  ASN B OD1 
10132 N ND2 . ASN B 162  ? 0.2963 0.3015 0.2600 0.0427  0.0151  -0.0419 160  ASN B ND2 
10133 N N   . ASP B 163  ? 0.2523 0.2471 0.2042 0.0331  0.0091  -0.0414 161  ASP B N   
10134 C CA  . ASP B 163  ? 0.2530 0.2430 0.1985 0.0329  0.0082  -0.0428 161  ASP B CA  
10135 C C   . ASP B 163  ? 0.2616 0.2468 0.2032 0.0356  0.0084  -0.0452 161  ASP B C   
10136 O O   . ASP B 163  ? 0.2580 0.2402 0.1936 0.0362  0.0087  -0.0466 161  ASP B O   
10137 C CB  . ASP B 163  ? 0.2650 0.2515 0.2102 0.0300  0.0050  -0.0422 161  ASP B CB  
10138 C CG  . ASP B 163  ? 0.3038 0.2883 0.2531 0.0295  0.0029  -0.0420 161  ASP B CG  
10139 O OD1 . ASP B 163  ? 0.2644 0.2524 0.2189 0.0298  0.0037  -0.0409 161  ASP B OD1 
10140 O OD2 . ASP B 163  ? 0.3214 0.3010 0.2688 0.0285  0.0004  -0.0427 161  ASP B OD2 
10141 N N   . ARG B 164  ? 0.2527 0.2370 0.1973 0.0372  0.0083  -0.0457 162  ARG B N   
10142 C CA  . ARG B 164  ? 0.2394 0.2192 0.1801 0.0401  0.0088  -0.0480 162  ARG B CA  
10143 C C   . ARG B 164  ? 0.2262 0.2095 0.1652 0.0430  0.0122  -0.0487 162  ARG B C   
10144 O O   . ARG B 164  ? 0.2385 0.2181 0.1718 0.0450  0.0131  -0.0507 162  ARG B O   
10145 C CB  . ARG B 164  ? 0.2516 0.2292 0.1958 0.0410  0.0077  -0.0481 162  ARG B CB  
10146 C CG  . ARG B 164  ? 0.2574 0.2309 0.2028 0.0383  0.0044  -0.0477 162  ARG B CG  
10147 C CD  . ARG B 164  ? 0.3637 0.3319 0.3035 0.0368  0.0024  -0.0489 162  ARG B CD  
10148 N NE  . ARG B 164  ? 0.4645 0.4277 0.3981 0.0391  0.0029  -0.0513 162  ARG B NE  
10149 C CZ  . ARG B 164  ? 0.5102 0.4697 0.4377 0.0385  0.0021  -0.0526 162  ARG B CZ  
10150 N NH1 . ARG B 164  ? 0.5510 0.5112 0.4776 0.0358  0.0007  -0.0516 162  ARG B NH1 
10151 N NH2 . ARG B 164  ? 0.4617 0.4164 0.3835 0.0409  0.0027  -0.0550 162  ARG B NH2 
10152 N N   . SER B 165  ? 0.2596 0.2499 0.2035 0.0434  0.0142  -0.0470 163  SER B N   
10153 C CA  . SER B 165  ? 0.2335 0.2282 0.1765 0.0459  0.0176  -0.0474 163  SER B CA  
10154 C C   . SER B 165  ? 0.2265 0.2215 0.1643 0.0450  0.0187  -0.0477 163  SER B C   
10155 O O   . SER B 165  ? 0.2390 0.2337 0.1725 0.0475  0.0209  -0.0492 163  SER B O   
10156 C CB  . SER B 165  ? 0.2310 0.2336 0.1809 0.0457  0.0191  -0.0453 163  SER B CB  
10157 O OG  . SER B 165  ? 0.2691 0.2771 0.2186 0.0476  0.0224  -0.0453 163  SER B OG  
10158 N N   . LEU B 166  ? 0.2384 0.2338 0.1762 0.0416  0.0172  -0.0462 164  LEU B N   
10159 C CA  . LEU B 166  ? 0.2610 0.2566 0.1938 0.0405  0.0180  -0.0462 164  LEU B CA  
10160 C C   . LEU B 166  ? 0.2453 0.2335 0.1706 0.0413  0.0168  -0.0485 164  LEU B C   
10161 O O   . LEU B 166  ? 0.2636 0.2515 0.1835 0.0424  0.0186  -0.0495 164  LEU B O   
10162 C CB  . LEU B 166  ? 0.2311 0.2284 0.1658 0.0368  0.0164  -0.0440 164  LEU B CB  
10163 C CG  . LEU B 166  ? 0.2423 0.2473 0.1829 0.0360  0.0183  -0.0418 164  LEU B CG  
10164 C CD1 . LEU B 166  ? 0.3129 0.3189 0.2560 0.0325  0.0164  -0.0398 164  LEU B CD1 
10165 C CD2 . LEU B 166  ? 0.2676 0.2773 0.2062 0.0373  0.0218  -0.0418 164  LEU B CD2 
10166 N N   . ALA B 167  ? 0.2455 0.2278 0.1703 0.0405  0.0137  -0.0494 165  ALA B N   
10167 C CA  . ALA B 167  ? 0.2616 0.2366 0.1794 0.0410  0.0122  -0.0516 165  ALA B CA  
10168 C C   . ALA B 167  ? 0.2667 0.2399 0.1809 0.0449  0.0146  -0.0539 165  ALA B C   
10169 O O   . ALA B 167  ? 0.2899 0.2600 0.1972 0.0460  0.0154  -0.0556 165  ALA B O   
10170 C CB  . ALA B 167  ? 0.2943 0.2639 0.2133 0.0394  0.0085  -0.0519 165  ALA B CB  
10171 N N   . ALA B 168  ? 0.2779 0.2531 0.1966 0.0472  0.0158  -0.0540 166  ALA B N   
10172 C CA  . ALA B 168  ? 0.2501 0.2243 0.1661 0.0513  0.0183  -0.0560 166  ALA B CA  
10173 C C   . ALA B 168  ? 0.2522 0.2316 0.1660 0.0528  0.0219  -0.0559 166  ALA B C   
10174 O O   . ALA B 168  ? 0.2803 0.2567 0.1879 0.0552  0.0235  -0.0580 166  ALA B O   
10175 C CB  . ALA B 168  ? 0.2768 0.2536 0.1992 0.0533  0.0189  -0.0554 166  ALA B CB  
10176 N N   . ALA B 169  ? 0.2518 0.2387 0.1703 0.0511  0.0232  -0.0535 167  ALA B N   
10177 C CA  . ALA B 169  ? 0.2503 0.2428 0.1673 0.0522  0.0268  -0.0531 167  ALA B CA  
10178 C C   . ALA B 169  ? 0.2778 0.2669 0.1870 0.0510  0.0267  -0.0539 167  ALA B C   
10179 O O   . ALA B 169  ? 0.2691 0.2592 0.1738 0.0531  0.0296  -0.0550 167  ALA B O   
10180 C CB  . ALA B 169  ? 0.2525 0.2533 0.1763 0.0502  0.0278  -0.0502 167  ALA B CB  
10181 N N   . LEU B 170  ? 0.2692 0.2544 0.1767 0.0476  0.0235  -0.0533 168  LEU B N   
10182 C CA  . LEU B 170  ? 0.2597 0.2416 0.1597 0.0464  0.0231  -0.0540 168  LEU B CA  
10183 C C   . LEU B 170  ? 0.2707 0.2452 0.1631 0.0488  0.0228  -0.0571 168  LEU B C   
10184 O O   . LEU B 170  ? 0.2847 0.2583 0.1705 0.0500  0.0248  -0.0583 168  LEU B O   
10185 C CB  . LEU B 170  ? 0.2783 0.2581 0.1789 0.0423  0.0194  -0.0525 168  LEU B CB  
10186 C CG  . LEU B 170  ? 0.2888 0.2657 0.1820 0.0407  0.0188  -0.0526 168  LEU B CG  
10187 C CD1 . LEU B 170  ? 0.3322 0.3149 0.2240 0.0408  0.0223  -0.0514 168  LEU B CD1 
10188 C CD2 . LEU B 170  ? 0.3306 0.3057 0.2254 0.0370  0.0150  -0.0510 168  LEU B CD2 
10189 N N   . THR B 171  ? 0.3027 0.2717 0.1957 0.0496  0.0205  -0.0585 169  THR B N   
10190 C CA  . THR B 171  ? 0.3175 0.2792 0.2035 0.0521  0.0203  -0.0616 169  THR B CA  
10191 C C   . THR B 171  ? 0.3084 0.2727 0.1925 0.0563  0.0246  -0.0630 169  THR B C   
10192 O O   . THR B 171  ? 0.3191 0.2798 0.1955 0.0581  0.0259  -0.0651 169  THR B O   
10193 C CB  . THR B 171  ? 0.3245 0.2808 0.2128 0.0523  0.0175  -0.0626 169  THR B CB  
10194 O OG1 . THR B 171  ? 0.3618 0.3158 0.2515 0.0484  0.0136  -0.0614 169  THR B OG1 
10195 C CG2 . THR B 171  ? 0.3509 0.2992 0.2319 0.0549  0.0172  -0.0658 169  THR B CG2 
10196 N N   . ARG B 172  ? 0.2956 0.2665 0.1867 0.0580  0.0268  -0.0618 170  ARG B N   
10197 C CA  . ARG B 172  ? 0.2837 0.2577 0.1741 0.0622  0.0309  -0.0629 170  ARG B CA  
10198 C C   . ARG B 172  ? 0.2999 0.2781 0.1862 0.0623  0.0340  -0.0626 170  ARG B C   
10199 O O   . ARG B 172  ? 0.3060 0.2821 0.1862 0.0653  0.0364  -0.0647 170  ARG B O   
10200 C CB  . ARG B 172  ? 0.2761 0.2571 0.1755 0.0636  0.0323  -0.0613 170  ARG B CB  
10201 C CG  . ARG B 172  ? 0.2792 0.2625 0.1783 0.0685  0.0360  -0.0627 170  ARG B CG  
10202 C CD  . ARG B 172  ? 0.2791 0.2702 0.1873 0.0697  0.0374  -0.0608 170  ARG B CD  
10203 N NE  . ARG B 172  ? 0.2737 0.2631 0.1873 0.0680  0.0341  -0.0598 170  ARG B NE  
10204 C CZ  . ARG B 172  ? 0.2659 0.2598 0.1854 0.0644  0.0327  -0.0572 170  ARG B CZ  
10205 N NH1 . ARG B 172  ? 0.2784 0.2784 0.1992 0.0621  0.0340  -0.0553 170  ARG B NH1 
10206 N NH2 . ARG B 172  ? 0.2563 0.2480 0.1801 0.0632  0.0298  -0.0564 170  ARG B NH2 
10207 N N   . LEU B 173  ? 0.2957 0.2795 0.1851 0.0589  0.0340  -0.0599 171  LEU B N   
10208 C CA  . LEU B 173  ? 0.2947 0.2829 0.1806 0.0588  0.0372  -0.0593 171  LEU B CA  
10209 C C   . LEU B 173  ? 0.3116 0.2930 0.1874 0.0583  0.0363  -0.0610 171  LEU B C   
10210 O O   . LEU B 173  ? 0.3097 0.2920 0.1801 0.0602  0.0395  -0.0621 171  LEU B O   
10211 C CB  . LEU B 173  ? 0.3180 0.3136 0.2096 0.0553  0.0374  -0.0559 171  LEU B CB  
10212 C CG  . LEU B 173  ? 0.3370 0.3302 0.2282 0.0508  0.0338  -0.0543 171  LEU B CG  
10213 C CD1 . LEU B 173  ? 0.3551 0.3477 0.2391 0.0493  0.0348  -0.0540 171  LEU B CD1 
10214 C CD2 . LEU B 173  ? 0.3215 0.3211 0.2213 0.0483  0.0333  -0.0513 171  LEU B CD2 
10215 N N   . ILE B 174  ? 0.3113 0.2860 0.1845 0.0556  0.0321  -0.0614 172  ILE B N   
10216 C CA  . ILE B 174  ? 0.3054 0.2735 0.1689 0.0550  0.0310  -0.0631 172  ILE B CA  
10217 C C   . ILE B 174  ? 0.3365 0.2984 0.1935 0.0589  0.0320  -0.0666 172  ILE B C   
10218 O O   . ILE B 174  ? 0.3645 0.3241 0.2135 0.0602  0.0339  -0.0682 172  ILE B O   
10219 C CB  . ILE B 174  ? 0.3300 0.2928 0.1928 0.0512  0.0260  -0.0625 172  ILE B CB  
10220 C CG1 . ILE B 174  ? 0.3250 0.2935 0.1930 0.0475  0.0252  -0.0591 172  ILE B CG1 
10221 C CG2 . ILE B 174  ? 0.3619 0.3172 0.2143 0.0508  0.0245  -0.0646 172  ILE B CG2 
10222 C CD1 . ILE B 174  ? 0.3492 0.3136 0.2182 0.0439  0.0204  -0.0583 172  ILE B CD1 
10223 N N   . SER B 175  ? 0.3497 0.3085 0.2098 0.0608  0.0309  -0.0679 173  SER B N   
10224 C CA  . SER B 175  ? 0.3437 0.2961 0.1977 0.0647  0.0318  -0.0713 173  SER B CA  
10225 C C   . SER B 175  ? 0.3423 0.2998 0.1954 0.0688  0.0370  -0.0720 173  SER B C   
10226 O O   . SER B 175  ? 0.3938 0.3464 0.2394 0.0719  0.0386  -0.0748 173  SER B O   
10227 C CB  . SER B 175  ? 0.3819 0.3299 0.2398 0.0657  0.0294  -0.0722 173  SER B CB  
10228 O OG  . SER B 175  ? 0.4481 0.3910 0.3060 0.0620  0.0247  -0.0718 173  SER B OG  
10229 N N   . ARG B 176  ? 0.3353 0.3025 0.1959 0.0689  0.0397  -0.0695 174  ARG B N   
10230 C CA  . ARG B 176  ? 0.3396 0.3128 0.2004 0.0727  0.0447  -0.0699 174  ARG B CA  
10231 C C   . ARG B 176  ? 0.3478 0.3240 0.2030 0.0718  0.0474  -0.0694 174  ARG B C   
10232 O O   . ARG B 176  ? 0.3679 0.3442 0.2178 0.0752  0.0509  -0.0712 174  ARG B O   
10233 C CB  . ARG B 176  ? 0.3361 0.3188 0.2078 0.0731  0.0463  -0.0674 174  ARG B CB  
10234 C CG  . ARG B 176  ? 0.3552 0.3445 0.2286 0.0775  0.0513  -0.0678 174  ARG B CG  
10235 C CD  . ARG B 176  ? 0.3275 0.3254 0.2119 0.0778  0.0521  -0.0654 174  ARG B CD  
10236 N NE  . ARG B 176  ? 0.3228 0.3285 0.2122 0.0738  0.0524  -0.0622 174  ARG B NE  
10237 C CZ  . ARG B 176  ? 0.3425 0.3497 0.2379 0.0702  0.0494  -0.0599 174  ARG B CZ  
10238 N NH1 . ARG B 176  ? 0.3268 0.3294 0.2251 0.0699  0.0460  -0.0603 174  ARG B NH1 
10239 N NH2 . ARG B 176  ? 0.3850 0.3986 0.2837 0.0667  0.0499  -0.0571 174  ARG B NH2 
10240 N N   . CYS B 177  ? 0.3431 0.3219 0.1995 0.0673  0.0458  -0.0669 175  CYS B N   
10241 C CA  . CYS B 177  ? 0.3847 0.3677 0.2371 0.0661  0.0485  -0.0657 175  CYS B CA  
10242 C C   . CYS B 177  ? 0.4146 0.3912 0.2587 0.0631  0.0459  -0.0660 175  CYS B C   
10243 O O   . CYS B 177  ? 0.4392 0.4176 0.2778 0.0627  0.0483  -0.0657 175  CYS B O   
10244 C CB  . CYS B 177  ? 0.3585 0.3514 0.2194 0.0636  0.0499  -0.0621 175  CYS B CB  
10245 S SG  . CYS B 177  ? 0.4381 0.4398 0.3097 0.0668  0.0527  -0.0612 175  CYS B SG  
10246 N N   . GLY B 178  ? 0.3884 0.3581 0.2316 0.0608  0.0411  -0.0665 176  GLY B N   
10247 C CA  . GLY B 178  ? 0.4149 0.3776 0.2491 0.0586  0.0385  -0.0674 176  GLY B CA  
10248 C C   . GLY B 178  ? 0.3793 0.3459 0.2134 0.0547  0.0381  -0.0645 176  GLY B C   
10249 O O   . GLY B 178  ? 0.3883 0.3618 0.2301 0.0528  0.0386  -0.0616 176  GLY B O   
10250 N N   . GLU B 179  ? 0.4145 0.3760 0.2393 0.0535  0.0372  -0.0653 177  GLU B N   
10251 C CA  . GLU B 179  ? 0.4437 0.4075 0.2672 0.0497  0.0363  -0.0626 177  GLU B CA  
10252 C C   . GLU B 179  ? 0.3659 0.3392 0.1933 0.0494  0.0406  -0.0600 177  GLU B C   
10253 O O   . GLU B 179  ? 0.3918 0.3689 0.2236 0.0460  0.0394  -0.0569 177  GLU B O   
10254 C CB  . GLU B 179  ? 0.4586 0.4154 0.2707 0.0489  0.0348  -0.0641 177  GLU B CB  
10255 C CG  . GLU B 179  ? 0.4798 0.4379 0.2904 0.0448  0.0332  -0.0612 177  GLU B CG  
10256 C CD  . GLU B 179  ? 0.6869 0.6384 0.4858 0.0441  0.0317  -0.0625 177  GLU B CD  
10257 O OE1 . GLU B 179  ? 0.7483 0.6928 0.5405 0.0461  0.0309  -0.0658 177  GLU B OE1 
10258 O OE2 . GLU B 179  ? 0.7345 0.6874 0.5308 0.0414  0.0314  -0.0602 177  GLU B OE2 
10259 N N   . PRO B 180  ? 0.3892 0.3667 0.2156 0.0527  0.0455  -0.0609 178  PRO B N   
10260 C CA  . PRO B 180  ? 0.4074 0.3942 0.2377 0.0520  0.0494  -0.0581 178  PRO B CA  
10261 C C   . PRO B 180  ? 0.4190 0.4125 0.2607 0.0500  0.0487  -0.0552 178  PRO B C   
10262 O O   . PRO B 180  ? 0.4026 0.4016 0.2470 0.0471  0.0496  -0.0522 178  PRO B O   
10263 C CB  . PRO B 180  ? 0.4343 0.4242 0.2625 0.0565  0.0545  -0.0600 178  PRO B CB  
10264 C CG  . PRO B 180  ? 0.4576 0.4382 0.2760 0.0588  0.0535  -0.0637 178  PRO B CG  
10265 C CD  . PRO B 180  ? 0.4577 0.4312 0.2775 0.0571  0.0478  -0.0644 178  PRO B CD  
10266 N N   . VAL B 181  ? 0.3615 0.3548 0.2099 0.0513  0.0472  -0.0560 179  VAL B N   
10267 C CA  . VAL B 181  ? 0.3428 0.3424 0.2016 0.0493  0.0465  -0.0532 179  VAL B CA  
10268 C C   . VAL B 181  ? 0.3514 0.3481 0.2113 0.0449  0.0421  -0.0513 179  VAL B C   
10269 O O   . VAL B 181  ? 0.3675 0.3695 0.2333 0.0422  0.0420  -0.0484 179  VAL B O   
10270 C CB  . VAL B 181  ? 0.3521 0.3528 0.2178 0.0520  0.0464  -0.0544 179  VAL B CB  
10271 C CG1 . VAL B 181  ? 0.3439 0.3363 0.2087 0.0518  0.0419  -0.0561 179  VAL B CG1 
10272 C CG2 . VAL B 181  ? 0.3822 0.3911 0.2582 0.0504  0.0469  -0.0515 179  VAL B CG2 
10273 N N   . ILE B 182  ? 0.3462 0.3346 0.2007 0.0442  0.0383  -0.0529 180  ILE B N   
10274 C CA  . ILE B 182  ? 0.3359 0.3215 0.1910 0.0403  0.0341  -0.0511 180  ILE B CA  
10275 C C   . ILE B 182  ? 0.3813 0.3695 0.2329 0.0376  0.0352  -0.0488 180  ILE B C   
10276 O O   . ILE B 182  ? 0.3814 0.3725 0.2376 0.0345  0.0338  -0.0460 180  ILE B O   
10277 C CB  . ILE B 182  ? 0.3500 0.3263 0.1994 0.0401  0.0300  -0.0534 180  ILE B CB  
10278 C CG1 . ILE B 182  ? 0.3442 0.3180 0.1976 0.0425  0.0289  -0.0554 180  ILE B CG1 
10279 C CG2 . ILE B 182  ? 0.3932 0.3672 0.2436 0.0362  0.0257  -0.0514 180  ILE B CG2 
10280 C CD1 . ILE B 182  ? 0.3904 0.3550 0.2373 0.0429  0.0256  -0.0582 180  ILE B CD1 
10281 N N   . ARG B 183  ? 0.4022 0.3890 0.2454 0.0388  0.0376  -0.0498 181  ARG B N   
10282 C CA  . ARG B 183  ? 0.4255 0.4146 0.2646 0.0364  0.0390  -0.0476 181  ARG B CA  
10283 C C   . ARG B 183  ? 0.4215 0.4196 0.2679 0.0352  0.0420  -0.0447 181  ARG B C   
10284 O O   . ARG B 183  ? 0.4200 0.4200 0.2680 0.0318  0.0409  -0.0418 181  ARG B O   
10285 C CB  . ARG B 183  ? 0.4361 0.4227 0.2650 0.0384  0.0417  -0.0495 181  ARG B CB  
10286 C CG  . ARG B 183  ? 0.5517 0.5416 0.3762 0.0365  0.0442  -0.0472 181  ARG B CG  
10287 C CD  . ARG B 183  ? 0.5760 0.5638 0.4001 0.0322  0.0404  -0.0446 181  ARG B CD  
10288 N NE  . ARG B 183  ? 0.6343 0.6135 0.4531 0.0315  0.0357  -0.0461 181  ARG B NE  
10289 C CZ  . ARG B 183  ? 0.5599 0.5365 0.3806 0.0285  0.0313  -0.0444 181  ARG B CZ  
10290 N NH1 . ARG B 183  ? 0.5630 0.5442 0.3905 0.0260  0.0310  -0.0413 181  ARG B NH1 
10291 N NH2 . ARG B 183  ? 0.6039 0.5731 0.4196 0.0281  0.0271  -0.0460 181  ARG B NH2 
10292 N N   . ARG B 184  ? 0.3969 0.4007 0.2480 0.0380  0.0456  -0.0453 182  ARG B N   
10293 C CA  . ARG B 184  ? 0.3804 0.3932 0.2390 0.0368  0.0483  -0.0426 182  ARG B CA  
10294 C C   . ARG B 184  ? 0.3940 0.4081 0.2609 0.0340  0.0451  -0.0405 182  ARG B C   
10295 O O   . ARG B 184  ? 0.4155 0.4339 0.2857 0.0311  0.0455  -0.0375 182  ARG B O   
10296 C CB  . ARG B 184  ? 0.4224 0.4410 0.2850 0.0406  0.0524  -0.0438 182  ARG B CB  
10297 C CG  . ARG B 184  ? 0.5043 0.5248 0.3603 0.0429  0.0570  -0.0448 182  ARG B CG  
10298 C CD  . ARG B 184  ? 0.5587 0.5875 0.4168 0.0408  0.0606  -0.0418 182  ARG B CD  
10299 N NE  . ARG B 184  ? 0.5312 0.5688 0.3977 0.0425  0.0639  -0.0411 182  ARG B NE  
10300 C CZ  . ARG B 184  ? 0.4748 0.5192 0.3497 0.0400  0.0640  -0.0382 182  ARG B CZ  
10301 N NH1 . ARG B 184  ? 0.5021 0.5452 0.3781 0.0357  0.0611  -0.0358 182  ARG B NH1 
10302 N NH2 . ARG B 184  ? 0.5232 0.5756 0.4055 0.0418  0.0669  -0.0378 182  ARG B NH2 
10303 N N   . GLY B 185  ? 0.3818 0.3918 0.2518 0.0349  0.0419  -0.0419 183  GLY B N   
10304 C CA  . GLY B 185  ? 0.3388 0.3497 0.2162 0.0324  0.0388  -0.0401 183  GLY B CA  
10305 C C   . GLY B 185  ? 0.3912 0.3989 0.2660 0.0286  0.0358  -0.0382 183  GLY B C   
10306 O O   . GLY B 185  ? 0.3685 0.3796 0.2486 0.0260  0.0351  -0.0356 183  GLY B O   
10307 N N   . VAL B 186  ? 0.3529 0.3539 0.2197 0.0284  0.0338  -0.0394 184  VAL B N   
10308 C CA  . VAL B 186  ? 0.4272 0.4248 0.2910 0.0251  0.0307  -0.0376 184  VAL B CA  
10309 C C   . VAL B 186  ? 0.4218 0.4241 0.2846 0.0229  0.0332  -0.0348 184  VAL B C   
10310 O O   . VAL B 186  ? 0.4176 0.4212 0.2840 0.0200  0.0317  -0.0321 184  VAL B O   
10311 C CB  . VAL B 186  ? 0.4018 0.3916 0.2565 0.0255  0.0283  -0.0396 184  VAL B CB  
10312 C CG1 . VAL B 186  ? 0.4073 0.3944 0.2576 0.0224  0.0260  -0.0374 184  VAL B CG1 
10313 C CG2 . VAL B 186  ? 0.4082 0.3930 0.2649 0.0266  0.0248  -0.0417 184  VAL B CG2 
10314 N N   . ASP B 187  ? 0.3945 0.3993 0.2526 0.0243  0.0372  -0.0352 185  ASP B N   
10315 C CA  . ASP B 187  ? 0.4496 0.4590 0.3065 0.0222  0.0399  -0.0325 185  ASP B CA  
10316 C C   . ASP B 187  ? 0.4627 0.4793 0.3290 0.0207  0.0412  -0.0302 185  ASP B C   
10317 O O   . ASP B 187  ? 0.4196 0.4384 0.2870 0.0176  0.0412  -0.0273 185  ASP B O   
10318 C CB  . ASP B 187  ? 0.4582 0.4697 0.3089 0.0243  0.0443  -0.0336 185  ASP B CB  
10319 C CG  . ASP B 187  ? 0.4651 0.4691 0.3052 0.0252  0.0431  -0.0356 185  ASP B CG  
10320 O OD1 . ASP B 187  ? 0.5600 0.5580 0.3972 0.0234  0.0388  -0.0354 185  ASP B OD1 
10321 O OD2 . ASP B 187  ? 0.5272 0.5315 0.3618 0.0278  0.0463  -0.0375 185  ASP B OD2 
10322 N N   . MET B 188  ? 0.4278 0.4480 0.3009 0.0230  0.0423  -0.0314 186  MET B N   
10323 C CA  . MET B 188  ? 0.4164 0.4434 0.2985 0.0218  0.0433  -0.0294 186  MET B CA  
10324 C C   . MET B 188  ? 0.3965 0.4212 0.2829 0.0188  0.0393  -0.0277 186  MET B C   
10325 O O   . MET B 188  ? 0.4259 0.4543 0.3160 0.0160  0.0396  -0.0250 186  MET B O   
10326 C CB  . MET B 188  ? 0.4246 0.4552 0.3125 0.0251  0.0450  -0.0312 186  MET B CB  
10327 C CG  . MET B 188  ? 0.4891 0.5270 0.3864 0.0241  0.0460  -0.0293 186  MET B CG  
10328 S SD  . MET B 188  ? 0.7103 0.7565 0.6083 0.0221  0.0504  -0.0266 186  MET B SD  
10329 C CE  . MET B 188  ? 0.5790 0.6266 0.4709 0.0262  0.0548  -0.0289 186  MET B CE  
10330 N N   . ALA B 189  ? 0.4189 0.4377 0.3051 0.0194  0.0356  -0.0292 187  ALA B N   
10331 C CA  . ALA B 189  ? 0.4051 0.4218 0.2954 0.0169  0.0318  -0.0277 187  ALA B CA  
10332 C C   . ALA B 189  ? 0.4187 0.4327 0.3045 0.0138  0.0303  -0.0255 187  ALA B C   
10333 O O   . ALA B 189  ? 0.4055 0.4206 0.2952 0.0112  0.0289  -0.0232 187  ALA B O   
10334 C CB  . ALA B 189  ? 0.4153 0.4264 0.3062 0.0183  0.0283  -0.0299 187  ALA B CB  
10335 N N   . MET B 190  ? 0.3923 0.4027 0.2695 0.0141  0.0306  -0.0262 188  MET B N   
10336 C CA  . MET B 190  ? 0.4190 0.4267 0.2911 0.0113  0.0293  -0.0240 188  MET B CA  
10337 C C   . MET B 190  ? 0.4342 0.4476 0.3088 0.0090  0.0321  -0.0210 188  MET B C   
10338 O O   . MET B 190  ? 0.4508 0.4634 0.3267 0.0061  0.0303  -0.0186 188  MET B O   
10339 C CB  . MET B 190  ? 0.4162 0.4197 0.2783 0.0123  0.0298  -0.0253 188  MET B CB  
10340 C CG  . MET B 190  ? 0.4997 0.4986 0.3559 0.0097  0.0272  -0.0235 188  MET B CG  
10341 S SD  . MET B 190  ? 0.6096 0.6040 0.4536 0.0108  0.0281  -0.0249 188  MET B SD  
10342 C CE  . MET B 190  ? 0.5187 0.5101 0.3621 0.0146  0.0275  -0.0292 188  MET B CE  
10343 N N   . ARG B 191  ? 0.4144 0.4336 0.2898 0.0102  0.0364  -0.0212 189  ARG B N   
10344 C CA  . ARG B 191  ? 0.4869 0.5121 0.3649 0.0078  0.0392  -0.0184 189  ARG B CA  
10345 C C   . ARG B 191  ? 0.4809 0.5094 0.3681 0.0062  0.0380  -0.0170 189  ARG B C   
10346 O O   . ARG B 191  ? 0.4360 0.4655 0.3247 0.0031  0.0375  -0.0143 189  ARG B O   
10347 C CB  . ARG B 191  ? 0.4174 0.4488 0.2949 0.0097  0.0442  -0.0191 189  ARG B CB  
10348 N N   . MET B 192  ? 0.4053 0.4352 0.2984 0.0084  0.0375  -0.0188 190  MET B N   
10349 C CA  . MET B 192  ? 0.3912 0.4242 0.2928 0.0070  0.0364  -0.0175 190  MET B CA  
10350 C C   . MET B 192  ? 0.4336 0.4615 0.3354 0.0046  0.0323  -0.0162 190  MET B C   
10351 O O   . MET B 192  ? 0.4033 0.4328 0.3084 0.0018  0.0319  -0.0139 190  MET B O   
10352 C CB  . MET B 192  ? 0.4185 0.4532 0.3256 0.0100  0.0364  -0.0198 190  MET B CB  
10353 C CG  . MET B 192  ? 0.4753 0.5156 0.3831 0.0126  0.0404  -0.0210 190  MET B CG  
10354 S SD  . MET B 192  ? 0.5771 0.6198 0.4924 0.0157  0.0401  -0.0231 190  MET B SD  
10355 C CE  . MET B 192  ? 0.4715 0.5198 0.3955 0.0127  0.0398  -0.0204 190  MET B CE  
10356 N N   . MET B 193  ? 0.3942 0.4157 0.2926 0.0056  0.0292  -0.0178 191  MET B N   
10357 C CA  A MET B 193  ? 0.4310 0.4478 0.3302 0.0038  0.0252  -0.0167 191  MET B CA  
10358 C CA  B MET B 193  ? 0.4307 0.4475 0.3300 0.0038  0.0252  -0.0167 191  MET B CA  
10359 C C   . MET B 193  ? 0.4412 0.4551 0.3349 0.0011  0.0244  -0.0144 191  MET B C   
10360 O O   . MET B 193  ? 0.4037 0.4151 0.2990 -0.0008 0.0217  -0.0128 191  MET B O   
10361 C CB  A MET B 193  ? 0.4459 0.4572 0.3437 0.0057  0.0221  -0.0190 191  MET B CB  
10362 C CB  B MET B 193  ? 0.4457 0.4572 0.3441 0.0057  0.0221  -0.0190 191  MET B CB  
10363 C CG  A MET B 193  ? 0.4194 0.4325 0.3220 0.0084  0.0226  -0.0214 191  MET B CG  
10364 C CG  B MET B 193  ? 0.4315 0.4451 0.3368 0.0075  0.0218  -0.0206 191  MET B CG  
10365 S SD  A MET B 193  ? 0.4111 0.4175 0.3117 0.0103  0.0189  -0.0240 191  MET B SD  
10366 S SD  B MET B 193  ? 0.4804 0.4876 0.3857 0.0088  0.0176  -0.0226 191  MET B SD  
10367 C CE  A MET B 193  ? 0.5032 0.5082 0.4102 0.0084  0.0153  -0.0226 191  MET B CE  
10368 C CE  B MET B 193  ? 0.4555 0.4592 0.3525 0.0112  0.0183  -0.0252 191  MET B CE  
10369 N N   . GLY B 194  ? 0.4268 0.4412 0.3140 0.0011  0.0268  -0.0141 192  GLY B N   
10370 C CA  . GLY B 194  ? 0.4410 0.4522 0.3222 -0.0013 0.0260  -0.0119 192  GLY B CA  
10371 C C   . GLY B 194  ? 0.4297 0.4456 0.3115 -0.0038 0.0290  -0.0092 192  GLY B C   
10372 O O   . GLY B 194  ? 0.4137 0.4270 0.2922 -0.0064 0.0279  -0.0068 192  GLY B O   
10373 N N   . GLU B 195  ? 0.4112 0.4338 0.2971 -0.0032 0.0326  -0.0095 193  GLU B N   
10374 C CA  . GLU B 195  ? 0.4479 0.4755 0.3338 -0.0055 0.0359  -0.0070 193  GLU B CA  
10375 C C   . GLU B 195  ? 0.4348 0.4688 0.3294 -0.0064 0.0374  -0.0061 193  GLU B C   
10376 O O   . GLU B 195  ? 0.4043 0.4416 0.3002 -0.0093 0.0389  -0.0035 193  GLU B O   
10377 C CB  . GLU B 195  ? 0.4881 0.5183 0.3685 -0.0041 0.0397  -0.0077 193  GLU B CB  
10378 C CG  . GLU B 195  ? 0.6372 0.6614 0.5080 -0.0036 0.0387  -0.0082 193  GLU B CG  
10379 C CD  . GLU B 195  ? 0.6563 0.6831 0.5217 -0.0018 0.0427  -0.0094 193  GLU B CD  
10380 O OE1 . GLU B 195  ? 0.7116 0.7453 0.5810 -0.0010 0.0464  -0.0095 193  GLU B OE1 
10381 O OE2 . GLU B 195  ? 0.8330 0.8548 0.6900 -0.0011 0.0420  -0.0102 193  GLU B OE2 
10382 N N   . GLN B 196  ? 0.4460 0.4820 0.3464 -0.0041 0.0370  -0.0082 194  GLN B N   
10383 C CA  . GLN B 196  ? 0.4131 0.4555 0.3217 -0.0046 0.0383  -0.0076 194  GLN B CA  
10384 C C   . GLN B 196  ? 0.4458 0.4858 0.3598 -0.0058 0.0349  -0.0071 194  GLN B C   
10385 O O   . GLN B 196  ? 0.4763 0.5187 0.3941 -0.0086 0.0349  -0.0050 194  GLN B O   
10386 C CB  . GLN B 196  ? 0.4554 0.5026 0.3672 -0.0012 0.0408  -0.0099 194  GLN B CB  
10387 N N   . PHE B 197  ? 0.4060 0.4413 0.3204 -0.0038 0.0320  -0.0091 195  PHE B N   
10388 C CA  . PHE B 197  ? 0.4576 0.4906 0.3768 -0.0048 0.0288  -0.0088 195  PHE B CA  
10389 C C   . PHE B 197  ? 0.4074 0.4357 0.3237 -0.0077 0.0264  -0.0066 195  PHE B C   
10390 O O   . PHE B 197  ? 0.4380 0.4655 0.3585 -0.0093 0.0246  -0.0055 195  PHE B O   
10391 C CB  . PHE B 197  ? 0.4448 0.4739 0.3647 -0.0020 0.0263  -0.0113 195  PHE B CB  
10392 C CG  . PHE B 197  ? 0.4445 0.4775 0.3677 0.0010  0.0281  -0.0135 195  PHE B CG  
10393 C CD1 . PHE B 197  ? 0.5025 0.5425 0.4311 0.0009  0.0308  -0.0130 195  PHE B CD1 
10394 C CD2 . PHE B 197  ? 0.4723 0.5019 0.3933 0.0039  0.0271  -0.0161 195  PHE B CD2 
10395 C CE1 . PHE B 197  ? 0.5313 0.5748 0.4630 0.0039  0.0324  -0.0150 195  PHE B CE1 
10396 C CE2 . PHE B 197  ? 0.4774 0.5101 0.4012 0.0068  0.0287  -0.0181 195  PHE B CE2 
10397 C CZ  . PHE B 197  ? 0.5080 0.5477 0.4372 0.0069  0.0314  -0.0175 195  PHE B CZ  
10398 N N   . VAL B 198  ? 0.3971 0.4218 0.3062 -0.0082 0.0263  -0.0059 196  VAL B N   
10399 C CA  . VAL B 198  ? 0.3759 0.3962 0.2816 -0.0109 0.0244  -0.0036 196  VAL B CA  
10400 C C   . VAL B 198  ? 0.3898 0.4116 0.2899 -0.0127 0.0270  -0.0018 196  VAL B C   
10401 O O   . VAL B 198  ? 0.3887 0.4131 0.2858 -0.0112 0.0298  -0.0028 196  VAL B O   
10402 C CB  . VAL B 198  ? 0.3483 0.3614 0.2502 -0.0100 0.0206  -0.0044 196  VAL B CB  
10403 C CG1 . VAL B 198  ? 0.3712 0.3830 0.2788 -0.0086 0.0180  -0.0059 196  VAL B CG1 
10404 C CG2 . VAL B 198  ? 0.4157 0.4270 0.3110 -0.0080 0.0212  -0.0060 196  VAL B CG2 
10405 N N   . THR B 199  ? 0.3414 0.3613 0.2400 -0.0158 0.0263  0.0010  197  THR B N   
10406 C CA  . THR B 199  ? 0.3623 0.3824 0.2547 -0.0177 0.0284  0.0030  197  THR B CA  
10407 C C   . THR B 199  ? 0.4088 0.4231 0.2932 -0.0167 0.0268  0.0025  197  THR B C   
10408 O O   . THR B 199  ? 0.4346 0.4497 0.3130 -0.0167 0.0292  0.0028  197  THR B O   
10409 C CB  . THR B 199  ? 0.3602 0.3796 0.2536 -0.0215 0.0279  0.0061  197  THR B CB  
10410 O OG1 . THR B 199  ? 0.3860 0.4109 0.2870 -0.0225 0.0292  0.0064  197  THR B OG1 
10411 C CG2 . THR B 199  ? 0.3840 0.4038 0.2712 -0.0239 0.0302  0.0085  197  THR B CG2 
10412 N N   . GLY B 200  ? 0.3421 0.3508 0.2261 -0.0157 0.0229  0.0016  198  GLY B N   
10413 C CA  . GLY B 200  ? 0.3756 0.3789 0.2524 -0.0145 0.0210  0.0009  198  GLY B CA  
10414 C C   . GLY B 200  ? 0.3650 0.3640 0.2443 -0.0129 0.0169  -0.0006 198  GLY B C   
10415 O O   . GLY B 200  ? 0.3635 0.3629 0.2492 -0.0133 0.0155  -0.0005 198  GLY B O   
10416 N N   . GLU B 201  ? 0.4269 0.4217 0.3008 -0.0113 0.0151  -0.0020 199  GLU B N   
10417 C CA  . GLU B 201  ? 0.4202 0.4110 0.2962 -0.0099 0.0111  -0.0034 199  GLU B CA  
10418 C C   . GLU B 201  ? 0.3910 0.3772 0.2663 -0.0117 0.0078  -0.0011 199  GLU B C   
10419 O O   . GLU B 201  ? 0.4731 0.4574 0.3529 -0.0111 0.0049  -0.0015 199  GLU B O   
10420 C CB  . GLU B 201  ? 0.4957 0.4837 0.3665 -0.0077 0.0100  -0.0057 199  GLU B CB  
10421 C CG  . GLU B 201  ? 0.6238 0.6090 0.4979 -0.0060 0.0065  -0.0076 199  GLU B CG  
10422 C CD  . GLU B 201  ? 0.6935 0.6751 0.5618 -0.0044 0.0049  -0.0097 199  GLU B CD  
10423 O OE1 . GLU B 201  ? 0.6525 0.6332 0.5135 -0.0045 0.0064  -0.0095 199  GLU B OE1 
10424 O OE2 . GLU B 201  ? 0.7810 0.7606 0.6518 -0.0030 0.0022  -0.0114 199  GLU B OE2 
10425 N N   . THR B 202  ? 0.3689 0.3532 0.2385 -0.0137 0.0081  0.0014  200  THR B N   
10426 C CA  . THR B 202  ? 0.3748 0.3546 0.2432 -0.0154 0.0052  0.0038  200  THR B CA  
10427 C C   . THR B 202  ? 0.4040 0.3855 0.2723 -0.0183 0.0075  0.0066  200  THR B C   
10428 O O   . THR B 202  ? 0.3823 0.3680 0.2497 -0.0191 0.0112  0.0069  200  THR B O   
10429 C CB  . THR B 202  ? 0.4191 0.3936 0.2792 -0.0153 0.0029  0.0044  200  THR B CB  
10430 O OG1 . THR B 202  ? 0.4520 0.4276 0.3056 -0.0165 0.0059  0.0055  200  THR B OG1 
10431 C CG2 . THR B 202  ? 0.4710 0.4441 0.3302 -0.0127 0.0010  0.0015  200  THR B CG2 
10432 N N   . ILE B 203  ? 0.3844 0.3623 0.2536 -0.0199 0.0052  0.0088  201  ILE B N   
10433 C CA  . ILE B 203  ? 0.3686 0.3473 0.2374 -0.0229 0.0070  0.0117  201  ILE B CA  
10434 C C   . ILE B 203  ? 0.4088 0.3869 0.2695 -0.0244 0.0089  0.0134  201  ILE B C   
10435 O O   . ILE B 203  ? 0.3805 0.3620 0.2408 -0.0265 0.0121  0.0149  201  ILE B O   
10436 C CB  . ILE B 203  ? 0.3704 0.3447 0.2412 -0.0242 0.0040  0.0136  201  ILE B CB  
10437 C CG1 . ILE B 203  ? 0.3741 0.3497 0.2461 -0.0274 0.0060  0.0162  201  ILE B CG1 
10438 C CG2 . ILE B 203  ? 0.3982 0.3659 0.2626 -0.0241 0.0007  0.0150  201  ILE B CG2 
10439 C CD1 . ILE B 203  ? 0.3319 0.3142 0.2109 -0.0277 0.0089  0.0150  201  ILE B CD1 
10440 N N   . ARG B 204  ? 0.4158 0.3899 0.2698 -0.0233 0.0070  0.0131  202  ARG B N   
10441 C CA  . ARG B 204  ? 0.4088 0.3820 0.2543 -0.0244 0.0088  0.0145  202  ARG B CA  
10442 C C   . ARG B 204  ? 0.3820 0.3613 0.2274 -0.0240 0.0134  0.0132  202  ARG B C   
10443 O O   . ARG B 204  ? 0.4408 0.4225 0.2832 -0.0261 0.0166  0.0151  202  ARG B O   
10444 C CB  . ARG B 204  ? 0.4606 0.4287 0.2996 -0.0228 0.0057  0.0138  202  ARG B CB  
10445 C CG  . ARG B 204  ? 0.6304 0.5950 0.4599 -0.0244 0.0059  0.0162  202  ARG B CG  
10446 C CD  . ARG B 204  ? 0.5686 0.5275 0.3926 -0.0229 0.0019  0.0157  202  ARG B CD  
10447 N NE  . ARG B 204  ? 0.4841 0.4443 0.3073 -0.0203 0.0019  0.0123  202  ARG B NE  
10448 C CZ  . ARG B 204  ? 0.5696 0.5314 0.3870 -0.0198 0.0046  0.0112  202  ARG B CZ  
10449 N NH1 . ARG B 204  ? 0.6043 0.5672 0.4164 -0.0217 0.0078  0.0132  202  ARG B NH1 
10450 N NH2 . ARG B 204  ? 0.5591 0.5212 0.3758 -0.0173 0.0042  0.0079  202  ARG B NH2 
10451 N N   . GLU B 205  ? 0.3990 0.3811 0.2476 -0.0213 0.0138  0.0099  203  GLU B N   
10452 C CA  . GLU B 205  ? 0.4199 0.4078 0.2687 -0.0204 0.0181  0.0084  203  GLU B CA  
10453 C C   . GLU B 205  ? 0.3898 0.3836 0.2451 -0.0221 0.0212  0.0095  203  GLU B C   
10454 O O   . GLU B 205  ? 0.3888 0.3871 0.2425 -0.0231 0.0251  0.0103  203  GLU B O   
10455 C CB  . GLU B 205  ? 0.4516 0.4403 0.3027 -0.0170 0.0175  0.0047  203  GLU B CB  
10456 C CG  . GLU B 205  ? 0.4799 0.4738 0.3302 -0.0154 0.0216  0.0029  203  GLU B CG  
10457 C CD  . GLU B 205  ? 0.5886 0.5822 0.4405 -0.0120 0.0207  -0.0007 203  GLU B CD  
10458 O OE1 . GLU B 205  ? 0.5452 0.5392 0.4040 -0.0111 0.0189  -0.0019 203  GLU B OE1 
10459 O OE2 . GLU B 205  ? 0.7556 0.7483 0.6015 -0.0104 0.0218  -0.0024 203  GLU B OE2 
10460 N N   . ALA B 206  ? 0.3568 0.3509 0.2195 -0.0224 0.0194  0.0096  204  ALA B N   
10461 C CA  . ALA B 206  ? 0.3292 0.3289 0.1983 -0.0241 0.0219  0.0105  204  ALA B CA  
10462 C C   . ALA B 206  ? 0.3906 0.3904 0.2566 -0.0278 0.0236  0.0139  204  ALA B C   
10463 O O   . ALA B 206  ? 0.3562 0.3618 0.2239 -0.0292 0.0273  0.0147  204  ALA B O   
10464 C CB  . ALA B 206  ? 0.3406 0.3395 0.2172 -0.0239 0.0193  0.0100  204  ALA B CB  
10465 N N   . LEU B 207  ? 0.3436 0.3371 0.2050 -0.0294 0.0209  0.0161  205  LEU B N   
10466 C CA  . LEU B 207  ? 0.3742 0.3669 0.2317 -0.0329 0.0222  0.0195  205  LEU B CA  
10467 C C   . LEU B 207  ? 0.4050 0.4006 0.2564 -0.0333 0.0259  0.0200  205  LEU B C   
10468 O O   . LEU B 207  ? 0.4088 0.4085 0.2603 -0.0360 0.0291  0.0221  205  LEU B O   
10469 C CB  . LEU B 207  ? 0.4225 0.4072 0.2755 -0.0340 0.0184  0.0216  205  LEU B CB  
10470 C CG  . LEU B 207  ? 0.4419 0.4236 0.3008 -0.0343 0.0152  0.0218  205  LEU B CG  
10471 C CD1 . LEU B 207  ? 0.4655 0.4392 0.3198 -0.0341 0.0110  0.0231  205  LEU B CD1 
10472 C CD2 . LEU B 207  ? 0.3701 0.3544 0.2331 -0.0376 0.0169  0.0239  205  LEU B CD2 
10473 N N   . LYS B 208  ? 0.3479 0.3417 0.1937 -0.0308 0.0256  0.0183  206  LYS B N   
10474 C CA  . LYS B 208  ? 0.3883 0.3846 0.2277 -0.0309 0.0292  0.0185  206  LYS B CA  
10475 C C   . LYS B 208  ? 0.4078 0.4127 0.2522 -0.0305 0.0337  0.0174  206  LYS B C   
10476 O O   . LYS B 208  ? 0.4009 0.4099 0.2429 -0.0323 0.0375  0.0191  206  LYS B O   
10477 C CB  . LYS B 208  ? 0.4498 0.4422 0.2826 -0.0280 0.0276  0.0164  206  LYS B CB  
10478 N N   . ARG B 209  ? 0.3852 0.3933 0.2368 -0.0281 0.0334  0.0147  207  ARG B N   
10479 C CA  . ARG B 209  ? 0.3806 0.3969 0.2374 -0.0272 0.0374  0.0134  207  ARG B CA  
10480 C C   . ARG B 209  ? 0.4378 0.4589 0.3009 -0.0303 0.0391  0.0157  207  ARG B C   
10481 O O   . ARG B 209  ? 0.4211 0.4497 0.2881 -0.0302 0.0427  0.0154  207  ARG B O   
10482 C CB  . ARG B 209  ? 0.3955 0.4129 0.2575 -0.0235 0.0363  0.0099  207  ARG B CB  
10483 C CG  . ARG B 209  ? 0.4311 0.4445 0.2870 -0.0204 0.0352  0.0074  207  ARG B CG  
10484 C CD  . ARG B 209  ? 0.4532 0.4674 0.3145 -0.0171 0.0338  0.0041  207  ARG B CD  
10485 N NE  . ARG B 209  ? 0.5982 0.6092 0.4540 -0.0141 0.0332  0.0014  207  ARG B NE  
10486 C CZ  . ARG B 209  ? 0.6154 0.6258 0.4744 -0.0112 0.0317  -0.0016 207  ARG B CZ  
10487 N NH1 . ARG B 209  ? 0.4730 0.4858 0.3404 -0.0107 0.0308  -0.0023 207  ARG B NH1 
10488 N NH2 . ARG B 209  ? 0.6478 0.6550 0.5010 -0.0088 0.0312  -0.0039 207  ARG B NH2 
10489 N N   . SER B 210  ? 0.3573 0.3744 0.2212 -0.0331 0.0364  0.0180  208  SER B N   
10490 C CA  . SER B 210  ? 0.3472 0.3681 0.2169 -0.0363 0.0376  0.0201  208  SER B CA  
10491 C C   . SER B 210  ? 0.3783 0.4017 0.2442 -0.0398 0.0408  0.0232  208  SER B C   
10492 O O   . SER B 210  ? 0.3748 0.4035 0.2457 -0.0424 0.0427  0.0248  208  SER B O   
10493 C CB  . SER B 210  ? 0.3162 0.3313 0.1884 -0.0377 0.0334  0.0211  208  SER B CB  
10494 O OG  . SER B 210  ? 0.3660 0.3797 0.2427 -0.0346 0.0308  0.0183  208  SER B OG  
10495 N N   . LYS B 211  ? 0.3646 0.3845 0.2217 -0.0400 0.0413  0.0243  209  LYS B N   
10496 C CA  . LYS B 211  ? 0.3575 0.3791 0.2103 -0.0436 0.0441  0.0276  209  LYS B CA  
10497 C C   . LYS B 211  ? 0.3700 0.4014 0.2267 -0.0441 0.0492  0.0275  209  LYS B C   
10498 O O   . LYS B 211  ? 0.4230 0.4580 0.2813 -0.0478 0.0513  0.0303  209  LYS B O   
10499 C CB  . LYS B 211  ? 0.4335 0.4497 0.2758 -0.0433 0.0439  0.0283  209  LYS B CB  
10500 C CG  . LYS B 211  ? 0.4642 0.4712 0.3027 -0.0422 0.0388  0.0281  209  LYS B CG  
10501 C CD  . LYS B 211  ? 0.5116 0.5140 0.3523 -0.0452 0.0359  0.0306  209  LYS B CD  
10502 C CE  . LYS B 211  ? 0.5926 0.5862 0.4301 -0.0438 0.0308  0.0302  209  LYS B CE  
10503 N NZ  . LYS B 211  ? 0.6375 0.6262 0.4772 -0.0462 0.0278  0.0325  209  LYS B NZ  
10504 N N   . GLU B 212  ? 0.3795 0.4154 0.2379 -0.0403 0.0510  0.0244  210  GLU B N   
10505 C CA  . GLU B 212  ? 0.4328 0.4782 0.2944 -0.0401 0.0560  0.0243  210  GLU B CA  
10506 C C   . GLU B 212  ? 0.4101 0.4617 0.2808 -0.0427 0.0569  0.0256  210  GLU B C   
10507 O O   . GLU B 212  ? 0.3939 0.4512 0.2657 -0.0457 0.0602  0.0280  210  GLU B O   
10508 C CB  . GLU B 212  ? 0.5035 0.5518 0.3662 -0.0352 0.0572  0.0204  210  GLU B CB  
10509 C CG  . GLU B 212  ? 0.6320 0.6903 0.4984 -0.0343 0.0623  0.0199  210  GLU B CG  
10510 C CD  . GLU B 212  ? 0.7410 0.8021 0.6105 -0.0294 0.0630  0.0160  210  GLU B CD  
10511 O OE1 . GLU B 212  ? 0.8529 0.9076 0.7197 -0.0266 0.0598  0.0136  210  GLU B OE1 
10512 O OE2 . GLU B 212  ? 0.8852 0.9548 0.7598 -0.0282 0.0666  0.0153  210  GLU B OE2 
10513 N N   . LEU B 213  ? 0.3597 0.4105 0.2372 -0.0416 0.0540  0.0240  211  LEU B N   
10514 C CA  . LEU B 213  ? 0.3773 0.4338 0.2635 -0.0440 0.0545  0.0250  211  LEU B CA  
10515 C C   . LEU B 213  ? 0.3637 0.4162 0.2493 -0.0489 0.0527  0.0284  211  LEU B C   
10516 O O   . LEU B 213  ? 0.3449 0.4027 0.2354 -0.0521 0.0542  0.0303  211  LEU B O   
10517 C CB  . LEU B 213  ? 0.3348 0.3924 0.2283 -0.0411 0.0524  0.0221  211  LEU B CB  
10518 C CG  . LEU B 213  ? 0.3661 0.4295 0.2621 -0.0367 0.0549  0.0190  211  LEU B CG  
10519 C CD1 . LEU B 213  ? 0.4081 0.4726 0.3115 -0.0341 0.0527  0.0165  211  LEU B CD1 
10520 C CD2 . LEU B 213  ? 0.4226 0.4958 0.3209 -0.0377 0.0598  0.0202  211  LEU B CD2 
10521 N N   . GLU B 214  ? 0.3487 0.3919 0.2282 -0.0495 0.0493  0.0293  212  GLU B N   
10522 C CA  . GLU B 214  ? 0.3261 0.3650 0.2040 -0.0540 0.0478  0.0327  212  GLU B CA  
10523 C C   . GLU B 214  ? 0.3594 0.4023 0.2341 -0.0577 0.0516  0.0358  212  GLU B C   
10524 O O   . GLU B 214  ? 0.3934 0.4379 0.2710 -0.0619 0.0520  0.0384  212  GLU B O   
10525 C CB  . GLU B 214  ? 0.3539 0.3821 0.2254 -0.0536 0.0437  0.0331  212  GLU B CB  
10526 C CG  . GLU B 214  ? 0.3619 0.3858 0.2377 -0.0513 0.0396  0.0308  212  GLU B CG  
10527 C CD  . GLU B 214  ? 0.3735 0.3873 0.2437 -0.0512 0.0355  0.0316  212  GLU B CD  
10528 O OE1 . GLU B 214  ? 0.4176 0.4276 0.2799 -0.0519 0.0356  0.0332  212  GLU B OE1 
10529 O OE2 . GLU B 214  ? 0.3671 0.3770 0.2409 -0.0503 0.0321  0.0306  212  GLU B OE2 
10530 N N   . GLU B 215  ? 0.3722 0.4169 0.2410 -0.0563 0.0545  0.0356  213  GLU B N   
10531 C CA  . GLU B 215  ? 0.3846 0.4338 0.2503 -0.0596 0.0585  0.0386  213  GLU B CA  
10532 C C   . GLU B 215  ? 0.4074 0.4674 0.2814 -0.0612 0.0620  0.0390  213  GLU B C   
10533 O O   . GLU B 215  ? 0.4455 0.5092 0.3190 -0.0652 0.0647  0.0421  213  GLU B O   
10534 C CB  . GLU B 215  ? 0.4245 0.4734 0.2821 -0.0572 0.0610  0.0379  213  GLU B CB  
10535 C CG  . GLU B 215  ? 0.4788 0.5173 0.3273 -0.0567 0.0577  0.0383  213  GLU B CG  
10536 C CD  . GLU B 215  ? 0.6155 0.6535 0.4556 -0.0542 0.0599  0.0374  213  GLU B CD  
10537 O OE1 . GLU B 215  ? 0.7999 0.8447 0.6389 -0.0550 0.0646  0.0383  213  GLU B OE1 
10538 O OE2 . GLU B 215  ? 0.6815 0.7126 0.5163 -0.0516 0.0569  0.0358  213  GLU B OE2 
10539 N N   . LYS B 216  ? 0.3655 0.4305 0.2469 -0.0581 0.0620  0.0361  214  LYS B N   
10540 C CA  . LYS B 216  ? 0.3619 0.4372 0.2519 -0.0593 0.0649  0.0364  214  LYS B CA  
10541 C C   . LYS B 216  ? 0.4130 0.4878 0.3094 -0.0629 0.0623  0.0378  214  LYS B C   
10542 O O   . LYS B 216  ? 0.4080 0.4911 0.3113 -0.0649 0.0644  0.0386  214  LYS B O   
10543 C CB  . LYS B 216  ? 0.3880 0.4692 0.2831 -0.0543 0.0661  0.0327  214  LYS B CB  
10544 C CG  . LYS B 216  ? 0.4521 0.5352 0.3417 -0.0507 0.0693  0.0311  214  LYS B CG  
10545 C CD  . LYS B 216  ? 0.5636 0.6514 0.4583 -0.0456 0.0700  0.0273  214  LYS B CD  
10546 C CE  . LYS B 216  ? 0.7049 0.7910 0.5927 -0.0414 0.0717  0.0250  214  LYS B CE  
10547 N NZ  . LYS B 216  ? 0.6919 0.7807 0.5841 -0.0363 0.0717  0.0212  214  LYS B NZ  
10548 N N   . GLY B 217  ? 0.3423 0.4076 0.2365 -0.0637 0.0579  0.0380  215  GLY B N   
10549 C CA  . GLY B 217  ? 0.3375 0.4012 0.2369 -0.0669 0.0553  0.0392  215  GLY B CA  
10550 C C   . GLY B 217  ? 0.3843 0.4450 0.2885 -0.0639 0.0516  0.0363  215  GLY B C   
10551 O O   . GLY B 217  ? 0.3569 0.4164 0.2657 -0.0663 0.0494  0.0369  215  GLY B O   
10552 N N   . PHE B 218  ? 0.3238 0.3833 0.2271 -0.0590 0.0510  0.0332  216  PHE B N   
10553 C CA  . PHE B 218  ? 0.2901 0.3454 0.1968 -0.0563 0.0473  0.0306  216  PHE B CA  
10554 C C   . PHE B 218  ? 0.3410 0.3854 0.2422 -0.0569 0.0433  0.0314  216  PHE B C   
10555 O O   . PHE B 218  ? 0.3286 0.3683 0.2224 -0.0582 0.0434  0.0333  216  PHE B O   
10556 C CB  . PHE B 218  ? 0.3127 0.3700 0.2200 -0.0509 0.0478  0.0271  216  PHE B CB  
10557 C CG  . PHE B 218  ? 0.3257 0.3933 0.2395 -0.0494 0.0510  0.0258  216  PHE B CG  
10558 C CD1 . PHE B 218  ? 0.3341 0.4084 0.2464 -0.0494 0.0554  0.0265  216  PHE B CD1 
10559 C CD2 . PHE B 218  ? 0.3381 0.4086 0.2594 -0.0476 0.0498  0.0238  216  PHE B CD2 
10560 C CE1 . PHE B 218  ? 0.3334 0.4173 0.2519 -0.0477 0.0584  0.0253  216  PHE B CE1 
10561 C CE2 . PHE B 218  ? 0.3524 0.4322 0.2797 -0.0460 0.0526  0.0226  216  PHE B CE2 
10562 C CZ  . PHE B 218  ? 0.3210 0.4077 0.2471 -0.0460 0.0569  0.0234  216  PHE B CZ  
10563 N N   . SER B 219  ? 0.3210 0.3613 0.2258 -0.0557 0.0399  0.0299  217  SER B N   
10564 C CA  . SER B 219  ? 0.3251 0.3555 0.2257 -0.0551 0.0359  0.0299  217  SER B CA  
10565 C C   . SER B 219  ? 0.2927 0.3218 0.1960 -0.0504 0.0338  0.0264  217  SER B C   
10566 O O   . SER B 219  ? 0.2931 0.3286 0.2012 -0.0480 0.0354  0.0242  217  SER B O   
10567 C CB  . SER B 219  ? 0.3112 0.3369 0.2131 -0.0588 0.0335  0.0320  217  SER B CB  
10568 O OG  . SER B 219  ? 0.3433 0.3727 0.2530 -0.0588 0.0329  0.0307  217  SER B OG  
10569 N N   . TYR B 220  ? 0.2975 0.3184 0.1980 -0.0492 0.0302  0.0260  218  TYR B N   
10570 C CA  . TYR B 220  ? 0.2879 0.3069 0.1900 -0.0449 0.0281  0.0229  218  TYR B CA  
10571 C C   . TYR B 220  ? 0.2685 0.2813 0.1727 -0.0448 0.0242  0.0226  218  TYR B C   
10572 O O   . TYR B 220  ? 0.2919 0.2990 0.1933 -0.0473 0.0225  0.0248  218  TYR B O   
10573 C CB  . TYR B 220  ? 0.2838 0.2993 0.1791 -0.0424 0.0278  0.0221  218  TYR B CB  
10574 C CG  . TYR B 220  ? 0.2812 0.3033 0.1759 -0.0406 0.0314  0.0208  218  TYR B CG  
10575 C CD1 . TYR B 220  ? 0.3019 0.3276 0.1930 -0.0428 0.0348  0.0227  218  TYR B CD1 
10576 C CD2 . TYR B 220  ? 0.2777 0.3024 0.1754 -0.0367 0.0315  0.0176  218  TYR B CD2 
10577 C CE1 . TYR B 220  ? 0.2931 0.3250 0.1837 -0.0408 0.0383  0.0214  218  TYR B CE1 
10578 C CE2 . TYR B 220  ? 0.2965 0.3270 0.1936 -0.0348 0.0348  0.0162  218  TYR B CE2 
10579 C CZ  . TYR B 220  ? 0.2899 0.3239 0.1834 -0.0368 0.0382  0.0181  218  TYR B CZ  
10580 O OH  . TYR B 220  ? 0.3456 0.3854 0.2384 -0.0347 0.0417  0.0168  218  TYR B OH  
10581 N N   . SER B 221  ? 0.2572 0.2709 0.1662 -0.0418 0.0229  0.0199  219  SER B N   
10582 C CA  . SER B 221  ? 0.2539 0.2617 0.1644 -0.0406 0.0193  0.0190  219  SER B CA  
10583 C C   . SER B 221  ? 0.2754 0.2824 0.1859 -0.0363 0.0182  0.0162  219  SER B C   
10584 O O   . SER B 221  ? 0.2990 0.3115 0.2135 -0.0343 0.0197  0.0141  219  SER B O   
10585 C CB  . SER B 221  ? 0.2667 0.2768 0.1841 -0.0416 0.0188  0.0186  219  SER B CB  
10586 O OG  . SER B 221  ? 0.2747 0.2789 0.1933 -0.0403 0.0154  0.0177  219  SER B OG  
10587 N N   . TYR B 222  ? 0.2584 0.2589 0.1646 -0.0351 0.0155  0.0162  220  TYR B N   
10588 C CA  . TYR B 222  ? 0.2717 0.2712 0.1771 -0.0313 0.0143  0.0138  220  TYR B CA  
10589 C C   . TYR B 222  ? 0.2918 0.2895 0.2022 -0.0293 0.0117  0.0119  220  TYR B C   
10590 O O   . TYR B 222  ? 0.2905 0.2841 0.2021 -0.0303 0.0095  0.0128  220  TYR B O   
10591 C CB  . TYR B 222  ? 0.2635 0.2574 0.1614 -0.0310 0.0128  0.0147  220  TYR B CB  
10592 C CG  . TYR B 222  ? 0.2721 0.2682 0.1647 -0.0327 0.0157  0.0163  220  TYR B CG  
10593 C CD1 . TYR B 222  ? 0.2836 0.2846 0.1753 -0.0310 0.0183  0.0147  220  TYR B CD1 
10594 C CD2 . TYR B 222  ? 0.2723 0.2658 0.1611 -0.0360 0.0159  0.0194  220  TYR B CD2 
10595 C CE1 . TYR B 222  ? 0.2744 0.2778 0.1613 -0.0324 0.0213  0.0161  220  TYR B CE1 
10596 C CE2 . TYR B 222  ? 0.2883 0.2841 0.1722 -0.0377 0.0188  0.0209  220  TYR B CE2 
10597 C CZ  . TYR B 222  ? 0.2896 0.2905 0.1727 -0.0359 0.0215  0.0193  220  TYR B CZ  
10598 O OH  . TYR B 222  ? 0.3158 0.3193 0.1941 -0.0375 0.0246  0.0208  220  TYR B OH  
10599 N N   . ASP B 223  ? 0.2956 0.2964 0.2089 -0.0264 0.0121  0.0093  221  ASP B N   
10600 C CA  . ASP B 223  ? 0.3117 0.3116 0.2299 -0.0242 0.0100  0.0073  221  ASP B CA  
10601 C C   . ASP B 223  ? 0.3131 0.3099 0.2283 -0.0214 0.0082  0.0057  221  ASP B C   
10602 O O   . ASP B 223  ? 0.3419 0.3414 0.2559 -0.0197 0.0097  0.0041  221  ASP B O   
10603 C CB  . ASP B 223  ? 0.3560 0.3622 0.2800 -0.0233 0.0121  0.0056  221  ASP B CB  
10604 C CG  . ASP B 223  ? 0.4077 0.4134 0.3363 -0.0206 0.0102  0.0033  221  ASP B CG  
10605 O OD1 . ASP B 223  ? 0.4060 0.4068 0.3347 -0.0202 0.0074  0.0034  221  ASP B OD1 
10606 O OD2 . ASP B 223  ? 0.4779 0.4881 0.4098 -0.0189 0.0117  0.0015  221  ASP B OD2 
10607 N N   . MET B 224  ? 0.3249 0.3160 0.2389 -0.0209 0.0050  0.0061  222  MET B N   
10608 C CA  . MET B 224  ? 0.3810 0.3691 0.2923 -0.0185 0.0030  0.0048  222  MET B CA  
10609 C C   . MET B 224  ? 0.4100 0.3998 0.3263 -0.0159 0.0022  0.0021  222  MET B C   
10610 O O   . MET B 224  ? 0.5099 0.4971 0.4249 -0.0140 0.0000  0.0010  222  MET B O   
10611 C CB  . MET B 224  ? 0.3968 0.3785 0.3049 -0.0189 -0.0002 0.0064  222  MET B CB  
10612 C CG  . MET B 224  ? 0.3436 0.3229 0.2461 -0.0215 0.0003  0.0091  222  MET B CG  
10613 S SD  . MET B 224  ? 0.4048 0.3866 0.3009 -0.0219 0.0031  0.0093  222  MET B SD  
10614 C CE  . MET B 224  ? 0.4215 0.4003 0.3143 -0.0190 0.0006  0.0074  222  MET B CE  
10615 N N   . LEU B 225  ? 0.4838 0.4779 0.4056 -0.0158 0.0038  0.0012  223  LEU B N   
10616 C CA  . LEU B 225  ? 0.4205 0.4171 0.3470 -0.0135 0.0037  -0.0013 223  LEU B CA  
10617 C C   . LEU B 225  ? 0.5655 0.5589 0.4954 -0.0123 0.0008  -0.0019 223  LEU B C   
10618 O O   . LEU B 225  ? 0.5485 0.5433 0.4819 -0.0103 0.0004  -0.0039 223  LEU B O   
10619 C CB  . LEU B 225  ? 0.4715 0.4693 0.3952 -0.0114 0.0045  -0.0031 223  LEU B CB  
10620 C CG  . LEU B 225  ? 0.5277 0.5298 0.4492 -0.0119 0.0080  -0.0030 223  LEU B CG  
10621 C CD1 . LEU B 225  ? 0.5477 0.5500 0.4661 -0.0096 0.0085  -0.0051 223  LEU B CD1 
10622 C CD2 . LEU B 225  ? 0.5140 0.5217 0.4412 -0.0124 0.0103  -0.0032 223  LEU B CD2 
10623 N N   . GLY B 226  ? 0.5281 0.5175 0.4574 -0.0135 -0.0011 -0.0003 224  GLY B N   
10624 C CA  . GLY B 226  ? 0.5163 0.5032 0.4492 -0.0123 -0.0036 -0.0009 224  GLY B CA  
10625 C C   . GLY B 226  ? 0.4244 0.4140 0.3632 -0.0126 -0.0028 -0.0014 224  GLY B C   
10626 O O   . GLY B 226  ? 0.4160 0.4072 0.3555 -0.0145 -0.0012 -0.0003 224  GLY B O   
10627 N N   . GLU B 227  ? 0.3854 0.3752 0.3283 -0.0107 -0.0039 -0.0031 225  GLU B N   
10628 C CA  . GLU B 227  ? 0.4228 0.4151 0.3710 -0.0107 -0.0032 -0.0037 225  GLU B CA  
10629 C C   . GLU B 227  ? 0.3435 0.3345 0.2953 -0.0087 -0.0050 -0.0051 225  GLU B C   
10630 O O   . GLU B 227  ? 0.3702 0.3605 0.3212 -0.0070 -0.0061 -0.0062 225  GLU B O   
10631 C CB  . GLU B 227  ? 0.4690 0.4667 0.4191 -0.0106 -0.0005 -0.0047 225  GLU B CB  
10632 C CG  . GLU B 227  ? 0.5052 0.5058 0.4603 -0.0110 0.0004  -0.0052 225  GLU B CG  
10633 C CD  . GLU B 227  ? 0.5280 0.5342 0.4846 -0.0109 0.0029  -0.0059 225  GLU B CD  
10634 O OE1 . GLU B 227  ? 0.5053 0.5130 0.4585 -0.0113 0.0044  -0.0055 225  GLU B OE1 
10635 O OE2 . GLU B 227  ? 0.5626 0.5716 0.5236 -0.0104 0.0035  -0.0068 225  GLU B OE2 
10636 N N   . ALA B 228  ? 0.3069 0.2975 0.2624 -0.0090 -0.0054 -0.0050 226  ALA B N   
10637 C CA  . ALA B 228  ? 0.3256 0.3159 0.2852 -0.0072 -0.0066 -0.0063 226  ALA B CA  
10638 C C   . ALA B 228  ? 0.3030 0.2904 0.2615 -0.0056 -0.0089 -0.0066 226  ALA B C   
10639 O O   . ALA B 228  ? 0.3304 0.3190 0.2900 -0.0041 -0.0093 -0.0080 226  ALA B O   
10640 C CB  . ALA B 228  ? 0.3622 0.3568 0.3251 -0.0062 -0.0051 -0.0080 226  ALA B CB  
10641 N N   . ALA B 229  ? 0.2749 0.2584 0.2312 -0.0061 -0.0105 -0.0051 227  ALA B N   
10642 C CA  . ALA B 229  ? 0.2772 0.2581 0.2332 -0.0046 -0.0130 -0.0052 227  ALA B CA  
10643 C C   . ALA B 229  ? 0.2383 0.2202 0.1995 -0.0030 -0.0136 -0.0066 227  ALA B C   
10644 O O   . ALA B 229  ? 0.2822 0.2647 0.2466 -0.0031 -0.0130 -0.0067 227  ALA B O   
10645 C CB  . ALA B 229  ? 0.2658 0.2424 0.2197 -0.0052 -0.0146 -0.0034 227  ALA B CB  
10646 N N   . THR B 230  ? 0.2607 0.2429 0.2225 -0.0015 -0.0149 -0.0077 228  THR B N   
10647 C CA  . THR B 230  ? 0.2435 0.2267 0.2101 0.0000  -0.0157 -0.0088 228  THR B CA  
10648 C C   . THR B 230  ? 0.2359 0.2165 0.2035 0.0009  -0.0182 -0.0081 228  THR B C   
10649 O O   . THR B 230  ? 0.2511 0.2320 0.2228 0.0019  -0.0186 -0.0085 228  THR B O   
10650 C CB  . THR B 230  ? 0.2702 0.2555 0.2372 0.0009  -0.0156 -0.0104 228  THR B CB  
10651 O OG1 . THR B 230  ? 0.3268 0.3146 0.2927 0.0002  -0.0133 -0.0110 228  THR B OG1 
10652 C CG2 . THR B 230  ? 0.2495 0.2360 0.2215 0.0021  -0.0161 -0.0116 228  THR B CG2 
10653 N N   . THR B 231  ? 0.2404 0.2186 0.2042 0.0007  -0.0198 -0.0070 229  THR B N   
10654 C CA  . THR B 231  ? 0.2348 0.2106 0.1993 0.0017  -0.0223 -0.0062 229  THR B CA  
10655 C C   . THR B 231  ? 0.2274 0.1997 0.1880 0.0009  -0.0230 -0.0043 229  THR B C   
10656 O O   . THR B 231  ? 0.2404 0.2121 0.1971 -0.0006 -0.0217 -0.0035 229  THR B O   
10657 C CB  . THR B 231  ? 0.2430 0.2191 0.2066 0.0025  -0.0242 -0.0068 229  THR B CB  
10658 O OG1 . THR B 231  ? 0.2700 0.2447 0.2278 0.0016  -0.0244 -0.0062 229  THR B OG1 
10659 C CG2 . THR B 231  ? 0.2750 0.2540 0.2414 0.0030  -0.0234 -0.0087 229  THR B CG2 
10660 N N   . ALA B 232  ? 0.2526 0.2226 0.2143 0.0020  -0.0252 -0.0033 230  ALA B N   
10661 C CA  . ALA B 232  ? 0.2659 0.2320 0.2237 0.0015  -0.0263 -0.0013 230  ALA B CA  
10662 C C   . ALA B 232  ? 0.2455 0.2107 0.1978 0.0006  -0.0270 -0.0007 230  ALA B C   
10663 O O   . ALA B 232  ? 0.2841 0.2470 0.2319 -0.0008 -0.0265 0.0008  230  ALA B O   
10664 C CB  . ALA B 232  ? 0.2576 0.2218 0.2178 0.0032  -0.0288 -0.0006 230  ALA B CB  
10665 N N   . ALA B 233  ? 0.2517 0.2185 0.2040 0.0013  -0.0282 -0.0017 231  ALA B N   
10666 C CA  . ALA B 233  ? 0.2759 0.2416 0.2224 0.0005  -0.0289 -0.0013 231  ALA B CA  
10667 C C   . ALA B 233  ? 0.2918 0.2587 0.2350 -0.0011 -0.0260 -0.0015 231  ALA B C   
10668 O O   . ALA B 233  ? 0.2826 0.2476 0.2203 -0.0022 -0.0259 -0.0003 231  ALA B O   
10669 C CB  . ALA B 233  ? 0.3005 0.2677 0.2477 0.0015  -0.0306 -0.0026 231  ALA B CB  
10670 N N   . ASP B 234  ? 0.2599 0.2299 0.2063 -0.0012 -0.0237 -0.0030 232  ASP B N   
10671 C CA  . ASP B 234  ? 0.2654 0.2371 0.2094 -0.0027 -0.0209 -0.0032 232  ASP B CA  
10672 C C   . ASP B 234  ? 0.2667 0.2363 0.2082 -0.0043 -0.0201 -0.0012 232  ASP B C   
10673 O O   . ASP B 234  ? 0.2679 0.2370 0.2046 -0.0057 -0.0191 -0.0003 232  ASP B O   
10674 C CB  . ASP B 234  ? 0.2858 0.2611 0.2345 -0.0024 -0.0188 -0.0048 232  ASP B CB  
10675 C CG  . ASP B 234  ? 0.3328 0.3103 0.2834 -0.0011 -0.0190 -0.0068 232  ASP B CG  
10676 O OD1 . ASP B 234  ? 0.3541 0.3309 0.3014 -0.0008 -0.0201 -0.0072 232  ASP B OD1 
10677 O OD2 . ASP B 234  ? 0.3312 0.3111 0.2865 -0.0005 -0.0181 -0.0079 232  ASP B OD2 
10678 N N   . ALA B 235  ? 0.2592 0.2274 0.2038 -0.0041 -0.0205 -0.0006 233  ALA B N   
10679 C CA  . ALA B 235  ? 0.2563 0.2222 0.1989 -0.0058 -0.0197 0.0012  233  ALA B CA  
10680 C C   . ALA B 235  ? 0.2554 0.2173 0.1927 -0.0064 -0.0214 0.0032  233  ALA B C   
10681 O O   . ALA B 235  ? 0.2774 0.2379 0.2107 -0.0083 -0.0203 0.0046  233  ALA B O   
10682 C CB  . ALA B 235  ? 0.2571 0.2219 0.2040 -0.0053 -0.0199 0.0012  233  ALA B CB  
10683 N N   . GLU B 236  ? 0.2476 0.2075 0.1847 -0.0048 -0.0241 0.0034  234  GLU B N   
10684 C CA  . GLU B 236  ? 0.2735 0.2296 0.2054 -0.0051 -0.0259 0.0053  234  GLU B CA  
10685 C C   . GLU B 236  ? 0.3015 0.2584 0.2279 -0.0064 -0.0250 0.0055  234  GLU B C   
10686 O O   . GLU B 236  ? 0.2895 0.2437 0.2107 -0.0078 -0.0249 0.0073  234  GLU B O   
10687 C CB  . GLU B 236  ? 0.2946 0.2491 0.2279 -0.0030 -0.0292 0.0054  234  GLU B CB  
10688 C CG  . GLU B 236  ? 0.3399 0.2898 0.2685 -0.0032 -0.0314 0.0077  234  GLU B CG  
10689 C CD  . GLU B 236  ? 0.4877 0.4366 0.4181 -0.0010 -0.0347 0.0079  234  GLU B CD  
10690 O OE1 . GLU B 236  ? 0.5035 0.4556 0.4386 0.0003  -0.0352 0.0061  234  GLU B OE1 
10691 O OE2 . GLU B 236  ? 0.5243 0.4694 0.4518 -0.0007 -0.0369 0.0098  234  GLU B OE2 
10692 N N   . ARG B 237  ? 0.2621 0.2224 0.1894 -0.0058 -0.0242 0.0036  235  ARG B N   
10693 C CA  . ARG B 237  ? 0.2934 0.2545 0.2153 -0.0067 -0.0231 0.0035  235  ARG B CA  
10694 C C   . ARG B 237  ? 0.2986 0.2609 0.2187 -0.0088 -0.0200 0.0042  235  ARG B C   
10695 O O   . ARG B 237  ? 0.3054 0.2664 0.2199 -0.0102 -0.0193 0.0056  235  ARG B O   
10696 C CB  . ARG B 237  ? 0.3155 0.2796 0.2388 -0.0055 -0.0229 0.0011  235  ARG B CB  
10697 C CG  . ARG B 237  ? 0.3314 0.2961 0.2489 -0.0063 -0.0216 0.0008  235  ARG B CG  
10698 C CD  . ARG B 237  ? 0.3919 0.3596 0.3106 -0.0052 -0.0208 -0.0017 235  ARG B CD  
10699 N NE  . ARG B 237  ? 0.4405 0.4081 0.3529 -0.0057 -0.0196 -0.0019 235  ARG B NE  
10700 C CZ  . ARG B 237  ? 0.4267 0.3954 0.3376 -0.0048 -0.0195 -0.0038 235  ARG B CZ  
10701 N NH1 . ARG B 237  ? 0.5013 0.4711 0.4165 -0.0034 -0.0206 -0.0057 235  ARG B NH1 
10702 N NH2 . ARG B 237  ? 0.4462 0.4146 0.3508 -0.0053 -0.0183 -0.0039 235  ARG B NH2 
10703 N N   . TYR B 238  ? 0.2707 0.2359 0.1955 -0.0090 -0.0180 0.0033  236  TYR B N   
10704 C CA  . TYR B 238  ? 0.2695 0.2365 0.1932 -0.0111 -0.0151 0.0040  236  TYR B CA  
10705 C C   . TYR B 238  ? 0.2682 0.2313 0.1886 -0.0129 -0.0155 0.0066  236  TYR B C   
10706 O O   . TYR B 238  ? 0.2652 0.2286 0.1817 -0.0149 -0.0137 0.0078  236  TYR B O   
10707 C CB  . TYR B 238  ? 0.2586 0.2291 0.1884 -0.0110 -0.0134 0.0027  236  TYR B CB  
10708 C CG  . TYR B 238  ? 0.3209 0.2957 0.2536 -0.0096 -0.0122 0.0003  236  TYR B CG  
10709 C CD1 . TYR B 238  ? 0.3918 0.3683 0.3210 -0.0094 -0.0112 -0.0005 236  TYR B CD1 
10710 C CD2 . TYR B 238  ? 0.3388 0.3155 0.2773 -0.0085 -0.0122 -0.0012 236  TYR B CD2 
10711 C CE1 . TYR B 238  ? 0.4725 0.4524 0.4042 -0.0080 -0.0102 -0.0027 236  TYR B CE1 
10712 C CE2 . TYR B 238  ? 0.3560 0.3361 0.2969 -0.0072 -0.0113 -0.0033 236  TYR B CE2 
10713 C CZ  . TYR B 238  ? 0.4535 0.4352 0.3911 -0.0069 -0.0103 -0.0040 236  TYR B CZ  
10714 O OH  . TYR B 238  ? 0.5180 0.5026 0.4579 -0.0056 -0.0094 -0.0061 236  TYR B OH  
10715 N N   . TYR B 239  ? 0.2758 0.2353 0.1978 -0.0123 -0.0177 0.0074  237  TYR B N   
10716 C CA  . TYR B 239  ? 0.2672 0.2221 0.1857 -0.0138 -0.0185 0.0099  237  TYR B CA  
10717 C C   . TYR B 239  ? 0.2961 0.2485 0.2078 -0.0145 -0.0193 0.0115  237  TYR B C   
10718 O O   . TYR B 239  ? 0.2975 0.2486 0.2050 -0.0167 -0.0180 0.0133  237  TYR B O   
10719 C CB  . TYR B 239  ? 0.2837 0.2349 0.2048 -0.0123 -0.0210 0.0103  237  TYR B CB  
10720 C CG  . TYR B 239  ? 0.3366 0.2821 0.2535 -0.0135 -0.0223 0.0129  237  TYR B CG  
10721 C CD1 . TYR B 239  ? 0.3207 0.2646 0.2372 -0.0156 -0.0209 0.0141  237  TYR B CD1 
10722 C CD2 . TYR B 239  ? 0.4664 0.4082 0.3795 -0.0125 -0.0249 0.0143  237  TYR B CD2 
10723 C CE1 . TYR B 239  ? 0.3212 0.2595 0.2337 -0.0168 -0.0221 0.0165  237  TYR B CE1 
10724 C CE2 . TYR B 239  ? 0.4732 0.4095 0.3823 -0.0136 -0.0261 0.0168  237  TYR B CE2 
10725 C CZ  . TYR B 239  ? 0.4720 0.4064 0.3807 -0.0157 -0.0246 0.0179  237  TYR B CZ  
10726 O OH  . TYR B 239  ? 0.5511 0.4796 0.4555 -0.0168 -0.0258 0.0204  237  TYR B OH  
10727 N N   . ARG B 240  ? 0.2866 0.2383 0.1970 -0.0127 -0.0214 0.0109  238  ARG B N   
10728 C CA  . ARG B 240  ? 0.3035 0.2527 0.2071 -0.0132 -0.0225 0.0123  238  ARG B CA  
10729 C C   . ARG B 240  ? 0.3068 0.2589 0.2066 -0.0147 -0.0196 0.0121  238  ARG B C   
10730 O O   . ARG B 240  ? 0.3158 0.2658 0.2095 -0.0163 -0.0193 0.0140  238  ARG B O   
10731 C CB  . ARG B 240  ? 0.3109 0.2592 0.2143 -0.0109 -0.0255 0.0115  238  ARG B CB  
10732 C CG  . ARG B 240  ? 0.3536 0.2989 0.2601 -0.0093 -0.0285 0.0121  238  ARG B CG  
10733 C CD  . ARG B 240  ? 0.3876 0.3276 0.2900 -0.0103 -0.0298 0.0150  238  ARG B CD  
10734 N NE  . ARG B 240  ? 0.4386 0.3758 0.3443 -0.0085 -0.0324 0.0155  238  ARG B NE  
10735 C CZ  . ARG B 240  ? 0.5444 0.4768 0.4482 -0.0088 -0.0337 0.0178  238  ARG B CZ  
10736 N NH1 . ARG B 240  ? 0.4898 0.4193 0.3883 -0.0111 -0.0326 0.0198  238  ARG B NH1 
10737 N NH2 . ARG B 240  ? 0.5592 0.4895 0.4665 -0.0067 -0.0361 0.0180  238  ARG B NH2 
10738 N N   . ASP B 241  ? 0.3033 0.2604 0.2066 -0.0142 -0.0175 0.0099  239  ASP B N   
10739 C CA  . ASP B 241  ? 0.3264 0.2867 0.2266 -0.0154 -0.0145 0.0095  239  ASP B CA  
10740 C C   . ASP B 241  ? 0.3052 0.2660 0.2044 -0.0181 -0.0120 0.0113  239  ASP B C   
10741 O O   . ASP B 241  ? 0.3017 0.2630 0.1959 -0.0197 -0.0103 0.0125  239  ASP B O   
10742 C CB  . ASP B 241  ? 0.3564 0.3217 0.2609 -0.0140 -0.0129 0.0067  239  ASP B CB  
10743 C CG  . ASP B 241  ? 0.4183 0.3831 0.3222 -0.0118 -0.0150 0.0049  239  ASP B CG  
10744 O OD1 . ASP B 241  ? 0.4418 0.4030 0.3413 -0.0114 -0.0175 0.0058  239  ASP B OD1 
10745 O OD2 . ASP B 241  ? 0.4953 0.4633 0.4031 -0.0104 -0.0143 0.0026  239  ASP B OD2 
10746 N N   . TYR B 242  ? 0.2994 0.2603 0.2033 -0.0188 -0.0118 0.0116  240  TYR B N   
10747 C CA  . TYR B 242  ? 0.2729 0.2337 0.1758 -0.0216 -0.0098 0.0135  240  TYR B CA  
10748 C C   . TYR B 242  ? 0.2881 0.2434 0.1850 -0.0231 -0.0112 0.0163  240  TYR B C   
10749 O O   . TYR B 242  ? 0.2909 0.2463 0.1839 -0.0256 -0.0094 0.0181  240  TYR B O   
10750 C CB  . TYR B 242  ? 0.2815 0.2424 0.1902 -0.0220 -0.0099 0.0132  240  TYR B CB  
10751 C CG  . TYR B 242  ? 0.2643 0.2309 0.1789 -0.0213 -0.0080 0.0110  240  TYR B CG  
10752 C CD1 . TYR B 242  ? 0.3142 0.2861 0.2288 -0.0219 -0.0051 0.0101  240  TYR B CD1 
10753 C CD2 . TYR B 242  ? 0.2848 0.2513 0.2049 -0.0201 -0.0090 0.0097  240  TYR B CD2 
10754 C CE1 . TYR B 242  ? 0.3248 0.3017 0.2449 -0.0212 -0.0035 0.0082  240  TYR B CE1 
10755 C CE2 . TYR B 242  ? 0.2942 0.2655 0.2194 -0.0196 -0.0074 0.0079  240  TYR B CE2 
10756 C CZ  . TYR B 242  ? 0.2934 0.2698 0.2186 -0.0201 -0.0047 0.0071  240  TYR B CZ  
10757 O OH  . TYR B 242  ? 0.2969 0.2780 0.2275 -0.0194 -0.0033 0.0053  240  TYR B OH  
10758 N N   . GLU B 243  ? 0.3065 0.2570 0.2027 -0.0217 -0.0145 0.0169  241  GLU B N   
10759 C CA  . GLU B 243  ? 0.3102 0.2550 0.2007 -0.0228 -0.0161 0.0196  241  GLU B CA  
10760 C C   . GLU B 243  ? 0.2887 0.2336 0.1724 -0.0236 -0.0154 0.0205  241  GLU B C   
10761 O O   . GLU B 243  ? 0.2902 0.2329 0.1688 -0.0260 -0.0145 0.0229  241  GLU B O   
10762 C CB  . GLU B 243  ? 0.3076 0.2481 0.1991 -0.0204 -0.0199 0.0197  241  GLU B CB  
10763 C CG  . GLU B 243  ? 0.3598 0.2941 0.2456 -0.0211 -0.0221 0.0225  241  GLU B CG  
10764 C CD  . GLU B 243  ? 0.4663 0.3972 0.3532 -0.0183 -0.0258 0.0224  241  GLU B CD  
10765 O OE1 . GLU B 243  ? 0.4752 0.4089 0.3653 -0.0161 -0.0268 0.0203  241  GLU B OE1 
10766 O OE2 . GLU B 243  ? 0.5080 0.4335 0.3929 -0.0184 -0.0278 0.0245  241  GLU B OE2 
10767 N N   . SER B 244  ? 0.2916 0.2388 0.1747 -0.0216 -0.0158 0.0187  242  SER B N   
10768 C CA  A SER B 244  ? 0.3095 0.2569 0.1859 -0.0221 -0.0150 0.0192  242  SER B CA  
10769 C CA  B SER B 244  ? 0.3100 0.2572 0.1863 -0.0222 -0.0150 0.0192  242  SER B CA  
10770 C C   . SER B 244  ? 0.2944 0.2457 0.1692 -0.0244 -0.0110 0.0196  242  SER B C   
10771 O O   . SER B 244  ? 0.3064 0.2563 0.1749 -0.0262 -0.0099 0.0215  242  SER B O   
10772 C CB  A SER B 244  ? 0.3161 0.2655 0.1931 -0.0196 -0.0161 0.0166  242  SER B CB  
10773 C CB  B SER B 244  ? 0.3176 0.2667 0.1941 -0.0196 -0.0162 0.0167  242  SER B CB  
10774 O OG  A SER B 244  ? 0.3363 0.2856 0.2064 -0.0199 -0.0154 0.0168  242  SER B OG  
10775 O OG  B SER B 244  ? 0.3280 0.2736 0.2053 -0.0177 -0.0200 0.0167  242  SER B OG  
10776 N N   . ALA B 245  ? 0.2905 0.2469 0.1711 -0.0244 -0.0087 0.0178  243  ALA B N   
10777 C CA  . ALA B 245  ? 0.3021 0.2630 0.1822 -0.0264 -0.0048 0.0181  243  ALA B CA  
10778 C C   . ALA B 245  ? 0.3038 0.2625 0.1820 -0.0297 -0.0039 0.0211  243  ALA B C   
10779 O O   . ALA B 245  ? 0.3140 0.2743 0.1883 -0.0318 -0.0015 0.0226  243  ALA B O   
10780 C CB  . ALA B 245  ? 0.2983 0.2649 0.1856 -0.0255 -0.0029 0.0157  243  ALA B CB  
10781 N N   . ILE B 246  ? 0.2876 0.2427 0.1687 -0.0301 -0.0059 0.0220  244  ILE B N   
10782 C CA  . ILE B 246  ? 0.3039 0.2562 0.1829 -0.0333 -0.0053 0.0248  244  ILE B CA  
10783 C C   . ILE B 246  ? 0.3280 0.2759 0.1988 -0.0346 -0.0060 0.0274  244  ILE B C   
10784 O O   . ILE B 246  ? 0.3358 0.2840 0.2032 -0.0376 -0.0038 0.0295  244  ILE B O   
10785 C CB  . ILE B 246  ? 0.3001 0.2486 0.1831 -0.0333 -0.0075 0.0252  244  ILE B CB  
10786 C CG1 . ILE B 246  ? 0.3274 0.2807 0.2178 -0.0331 -0.0060 0.0231  244  ILE B CG1 
10787 C CG2 . ILE B 246  ? 0.3166 0.2603 0.1958 -0.0365 -0.0076 0.0283  244  ILE B CG2 
10788 C CD1 . ILE B 246  ? 0.3249 0.2746 0.2194 -0.0322 -0.0083 0.0228  244  ILE B CD1 
10789 N N   . HIS B 247  ? 0.3070 0.2509 0.1747 -0.0325 -0.0089 0.0274  245  HIS B N   
10790 C CA  . HIS B 247  ? 0.3190 0.2587 0.1784 -0.0335 -0.0097 0.0298  245  HIS B CA  
10791 C C   . HIS B 247  ? 0.3110 0.2549 0.1662 -0.0347 -0.0064 0.0298  245  HIS B C   
10792 O O   . HIS B 247  ? 0.3379 0.2801 0.1875 -0.0373 -0.0051 0.0324  245  HIS B O   
10793 C CB  . HIS B 247  ? 0.3205 0.2559 0.1775 -0.0308 -0.0135 0.0295  245  HIS B CB  
10794 C CG  . HIS B 247  ? 0.3367 0.2667 0.1958 -0.0299 -0.0168 0.0305  245  HIS B CG  
10795 N ND1 . HIS B 247  ? 0.3504 0.2748 0.2059 -0.0319 -0.0177 0.0336  245  HIS B ND1 
10796 C CD2 . HIS B 247  ? 0.3685 0.2978 0.2329 -0.0273 -0.0193 0.0289  245  HIS B CD2 
10797 C CE1 . HIS B 247  ? 0.3777 0.2980 0.2361 -0.0303 -0.0207 0.0337  245  HIS B CE1 
10798 N NE2 . HIS B 247  ? 0.3977 0.3212 0.2616 -0.0275 -0.0216 0.0309  245  HIS B NE2 
10799 N N   . ALA B 248  ? 0.3071 0.2564 0.1649 -0.0329 -0.0049 0.0270  246  ALA B N   
10800 C CA  . ALA B 248  ? 0.3044 0.2577 0.1581 -0.0335 -0.0017 0.0268  246  ALA B CA  
10801 C C   . ALA B 248  ? 0.3032 0.2609 0.1586 -0.0365 0.0022  0.0279  246  ALA B C   
10802 O O   . ALA B 248  ? 0.3409 0.2991 0.1909 -0.0387 0.0044  0.0299  246  ALA B O   
10803 C CB  . ALA B 248  ? 0.3433 0.3009 0.1996 -0.0306 -0.0011 0.0233  246  ALA B CB  
10804 N N   . ILE B 249  ? 0.3174 0.2783 0.1803 -0.0367 0.0029  0.0269  247  ILE B N   
10805 C CA  . ILE B 249  ? 0.2943 0.2597 0.1598 -0.0397 0.0063  0.0279  247  ILE B CA  
10806 C C   . ILE B 249  ? 0.3266 0.2875 0.1883 -0.0432 0.0060  0.0315  247  ILE B C   
10807 O O   . ILE B 249  ? 0.3392 0.3026 0.1984 -0.0461 0.0089  0.0334  247  ILE B O   
10808 C CB  . ILE B 249  ? 0.2922 0.2614 0.1664 -0.0390 0.0065  0.0260  247  ILE B CB  
10809 C CG1 . ILE B 249  ? 0.3016 0.2756 0.1793 -0.0357 0.0072  0.0226  247  ILE B CG1 
10810 C CG2 . ILE B 249  ? 0.3206 0.2940 0.1976 -0.0424 0.0095  0.0274  247  ILE B CG2 
10811 C CD1 . ILE B 249  ? 0.2966 0.2723 0.1822 -0.0343 0.0062  0.0205  247  ILE B CD1 
10812 N N   . GLY B 250  ? 0.3291 0.2833 0.1903 -0.0430 0.0025  0.0325  248  GLY B N   
10813 C CA  . GLY B 250  ? 0.3403 0.2891 0.1977 -0.0462 0.0019  0.0359  248  GLY B CA  
10814 C C   . GLY B 250  ? 0.3979 0.3444 0.2467 -0.0476 0.0026  0.0384  248  GLY B C   
10815 O O   . GLY B 250  ? 0.3944 0.3404 0.2401 -0.0511 0.0044  0.0411  248  GLY B O   
10816 N N   . LYS B 251  ? 0.3589 0.3037 0.2034 -0.0450 0.0011  0.0375  249  LYS B N   
10817 C CA  . LYS B 251  ? 0.3988 0.3414 0.2346 -0.0462 0.0018  0.0396  249  LYS B CA  
10818 C C   . LYS B 251  ? 0.3558 0.3052 0.1905 -0.0480 0.0064  0.0397  249  LYS B C   
10819 O O   . LYS B 251  ? 0.4007 0.3493 0.2300 -0.0510 0.0083  0.0425  249  LYS B O   
10820 C CB  . LYS B 251  ? 0.4151 0.3547 0.2468 -0.0430 -0.0010 0.0385  249  LYS B CB  
10821 N N   . ALA B 252  ? 0.3537 0.3100 0.1937 -0.0462 0.0085  0.0366  250  ALA B N   
10822 C CA  . ALA B 252  ? 0.3637 0.3271 0.2034 -0.0475 0.0131  0.0365  250  ALA B CA  
10823 C C   . ALA B 252  ? 0.3619 0.3280 0.2046 -0.0514 0.0155  0.0386  250  ALA B C   
10824 O O   . ALA B 252  ? 0.3864 0.3560 0.2260 -0.0538 0.0189  0.0403  250  ALA B O   
10825 C CB  . ALA B 252  ? 0.3741 0.3438 0.2194 -0.0444 0.0144  0.0327  250  ALA B CB  
10826 N N   . SER B 253  ? 0.3813 0.3461 0.2299 -0.0521 0.0139  0.0386  251  SER B N   
10827 C CA  . SER B 253  ? 0.3528 0.3196 0.2041 -0.0561 0.0157  0.0407  251  SER B CA  
10828 C C   . SER B 253  ? 0.3682 0.3305 0.2122 -0.0597 0.0161  0.0446  251  SER B C   
10829 O O   . SER B 253  ? 0.3956 0.3617 0.2391 -0.0631 0.0193  0.0465  251  SER B O   
10830 C CB  . SER B 253  ? 0.3466 0.3105 0.2039 -0.0562 0.0131  0.0402  251  SER B CB  
10831 O OG  . SER B 253  ? 0.3639 0.3288 0.2231 -0.0604 0.0146  0.0424  251  SER B OG  
10832 N N   . ALA B 254  ? 0.3724 0.3264 0.2104 -0.0589 0.0129  0.0459  252  ALA B N   
10833 C CA  . ALA B 254  ? 0.4219 0.3710 0.2518 -0.0618 0.0129  0.0497  252  ALA B CA  
10834 C C   . ALA B 254  ? 0.4271 0.3752 0.2581 -0.0665 0.0140  0.0526  252  ALA B C   
10835 O O   . ALA B 254  ? 0.4626 0.4114 0.2890 -0.0699 0.0164  0.0554  252  ALA B O   
10836 C CB  . ALA B 254  ? 0.4307 0.3831 0.2544 -0.0618 0.0159  0.0500  252  ALA B CB  
10837 N N   . GLY B 255  ? 0.4666 0.4131 0.3036 -0.0668 0.0122  0.0519  253  GLY B N   
10838 C CA  . GLY B 255  ? 0.4380 0.3829 0.2762 -0.0712 0.0128  0.0544  253  GLY B CA  
10839 C C   . GLY B 255  ? 0.4030 0.3567 0.2464 -0.0740 0.0167  0.0543  253  GLY B C   
10840 O O   . GLY B 255  ? 0.4420 0.3948 0.2854 -0.0783 0.0175  0.0569  253  GLY B O   
10841 N N   . ARG B 256  ? 0.3860 0.3480 0.2338 -0.0717 0.0190  0.0515  254  ARG B N   
10842 C CA  . ARG B 256  ? 0.4153 0.3862 0.2687 -0.0741 0.0226  0.0513  254  ARG B CA  
10843 C C   . ARG B 256  ? 0.3713 0.3425 0.2320 -0.0754 0.0213  0.0507  254  ARG B C   
10844 O O   . ARG B 256  ? 0.3900 0.3675 0.2550 -0.0784 0.0238  0.0513  254  ARG B O   
10845 C CB  . ARG B 256  ? 0.3574 0.3369 0.2137 -0.0709 0.0253  0.0485  254  ARG B CB  
10846 C CG  . ARG B 256  ? 0.3777 0.3597 0.2274 -0.0713 0.0282  0.0497  254  ARG B CG  
10847 C CD  . ARG B 256  ? 0.3977 0.3874 0.2499 -0.0678 0.0307  0.0467  254  ARG B CD  
10848 N NE  . ARG B 256  ? 0.3692 0.3552 0.2204 -0.0631 0.0279  0.0439  254  ARG B NE  
10849 C CZ  . ARG B 256  ? 0.3794 0.3703 0.2335 -0.0594 0.0288  0.0406  254  ARG B CZ  
10850 N NH1 . ARG B 256  ? 0.4027 0.4026 0.2618 -0.0594 0.0324  0.0394  254  ARG B NH1 
10851 N NH2 . ARG B 256  ? 0.4010 0.3878 0.2532 -0.0556 0.0261  0.0384  254  ARG B NH2 
10852 N N   . GLY B 257  ? 0.3847 0.3495 0.2467 -0.0733 0.0175  0.0494  255  GLY B N   
10853 C CA  . GLY B 257  ? 0.3514 0.3156 0.2195 -0.0744 0.0162  0.0487  255  GLY B CA  
10854 C C   . GLY B 257  ? 0.3698 0.3411 0.2456 -0.0715 0.0168  0.0451  255  GLY B C   
10855 O O   . GLY B 257  ? 0.3583 0.3352 0.2350 -0.0687 0.0185  0.0432  255  GLY B O   
10856 N N   . ILE B 258  ? 0.3523 0.3232 0.2336 -0.0723 0.0155  0.0443  256  ILE B N   
10857 C CA  . ILE B 258  ? 0.3484 0.3243 0.2367 -0.0692 0.0154  0.0409  256  ILE B CA  
10858 C C   . ILE B 258  ? 0.3238 0.3105 0.2173 -0.0701 0.0190  0.0401  256  ILE B C   
10859 O O   . ILE B 258  ? 0.3342 0.3259 0.2327 -0.0670 0.0193  0.0372  256  ILE B O   
10860 C CB  . ILE B 258  ? 0.3541 0.3254 0.2461 -0.0694 0.0126  0.0401  256  ILE B CB  
10861 C CG1 . ILE B 258  ? 0.3455 0.3172 0.2387 -0.0746 0.0134  0.0423  256  ILE B CG1 
10862 C CG2 . ILE B 258  ? 0.3675 0.3287 0.2550 -0.0677 0.0091  0.0406  256  ILE B CG2 
10863 C CD1 . ILE B 258  ? 0.3608 0.3280 0.2573 -0.0751 0.0108  0.0415  256  ILE B CD1 
10864 N N   . TYR B 259  ? 0.3406 0.3310 0.2330 -0.0742 0.0216  0.0426  257  TYR B N   
10865 C CA  . TYR B 259  ? 0.3464 0.3474 0.2442 -0.0752 0.0250  0.0420  257  TYR B CA  
10866 C C   . TYR B 259  ? 0.3502 0.3568 0.2454 -0.0734 0.0281  0.0417  257  TYR B C   
10867 O O   . TYR B 259  ? 0.3252 0.3385 0.2245 -0.0703 0.0296  0.0392  257  TYR B O   
10868 C CB  . TYR B 259  ? 0.3360 0.3390 0.2351 -0.0808 0.0263  0.0448  257  TYR B CB  
10869 C CG  . TYR B 259  ? 0.3528 0.3495 0.2538 -0.0827 0.0231  0.0450  257  TYR B CG  
10870 C CD1 . TYR B 259  ? 0.3751 0.3739 0.2825 -0.0809 0.0218  0.0424  257  TYR B CD1 
10871 C CD2 . TYR B 259  ? 0.4028 0.3911 0.2987 -0.0861 0.0214  0.0478  257  TYR B CD2 
10872 C CE1 . TYR B 259  ? 0.3548 0.3475 0.2634 -0.0824 0.0189  0.0424  257  TYR B CE1 
10873 C CE2 . TYR B 259  ? 0.3608 0.3428 0.2580 -0.0876 0.0185  0.0478  257  TYR B CE2 
10874 C CZ  . TYR B 259  ? 0.3800 0.3643 0.2835 -0.0856 0.0173  0.0450  257  TYR B CZ  
10875 O OH  . TYR B 259  ? 0.4086 0.3866 0.3132 -0.0870 0.0145  0.0449  257  TYR B OH  
10876 N N   . GLU B 260  ? 0.3549 0.3586 0.2431 -0.0752 0.0291  0.0443  258  GLU B N   
10877 C CA  . GLU B 260  ? 0.3482 0.3565 0.2331 -0.0734 0.0320  0.0440  258  GLU B CA  
10878 C C   . GLU B 260  ? 0.3923 0.3968 0.2744 -0.0683 0.0302  0.0414  258  GLU B C   
10879 O O   . GLU B 260  ? 0.3959 0.4057 0.2787 -0.0652 0.0321  0.0393  258  GLU B O   
10880 C CB  . GLU B 260  ? 0.3710 0.3770 0.2487 -0.0769 0.0336  0.0476  258  GLU B CB  
10881 C CG  . GLU B 260  ? 0.4986 0.5085 0.3718 -0.0750 0.0366  0.0473  258  GLU B CG  
10882 C CD  . GLU B 260  ? 0.5340 0.5405 0.3991 -0.0784 0.0379  0.0509  258  GLU B CD  
10883 O OE1 . GLU B 260  ? 0.5977 0.6002 0.4617 -0.0827 0.0370  0.0538  258  GLU B OE1 
10884 O OE2 . GLU B 260  ? 0.5601 0.5676 0.4198 -0.0767 0.0398  0.0508  258  GLU B OE2 
10885 N N   . GLY B 261  ? 0.3348 0.3303 0.2141 -0.0673 0.0264  0.0414  259  GLY B N   
10886 C CA  . GLY B 261  ? 0.3545 0.3457 0.2302 -0.0631 0.0243  0.0396  259  GLY B CA  
10887 C C   . GLY B 261  ? 0.3543 0.3472 0.2362 -0.0592 0.0228  0.0360  259  GLY B C   
10888 O O   . GLY B 261  ? 0.3312 0.3269 0.2196 -0.0598 0.0226  0.0351  259  GLY B O   
10889 N N   . PRO B 262  ? 0.3191 0.3101 0.1986 -0.0553 0.0215  0.0340  260  PRO B N   
10890 C CA  . PRO B 262  ? 0.2997 0.2926 0.1846 -0.0515 0.0203  0.0306  260  PRO B CA  
10891 C C   . PRO B 262  ? 0.3246 0.3114 0.2121 -0.0509 0.0165  0.0302  260  PRO B C   
10892 O O   . PRO B 262  ? 0.3496 0.3293 0.2334 -0.0524 0.0143  0.0322  260  PRO B O   
10893 C CB  . PRO B 262  ? 0.3112 0.3028 0.1914 -0.0481 0.0199  0.0291  260  PRO B CB  
10894 C CG  . PRO B 262  ? 0.3412 0.3264 0.2132 -0.0499 0.0190  0.0319  260  PRO B CG  
10895 C CD  . PRO B 262  ? 0.3254 0.3130 0.1969 -0.0543 0.0215  0.0348  260  PRO B CD  
10896 N N   . GLY B 263  ? 0.2891 0.2787 0.1829 -0.0486 0.0159  0.0275  261  GLY B N   
10897 C CA  . GLY B 263  ? 0.2961 0.2807 0.1927 -0.0472 0.0125  0.0266  261  GLY B CA  
10898 C C   . GLY B 263  ? 0.2817 0.2672 0.1809 -0.0429 0.0113  0.0234  261  GLY B C   
10899 O O   . GLY B 263  ? 0.2879 0.2770 0.1860 -0.0409 0.0128  0.0220  261  GLY B O   
10900 N N   . ILE B 264  ? 0.2911 0.2732 0.1937 -0.0415 0.0087  0.0223  262  ILE B N   
10901 C CA  . ILE B 264  ? 0.2713 0.2541 0.1770 -0.0376 0.0073  0.0194  262  ILE B CA  
10902 C C   . ILE B 264  ? 0.2866 0.2717 0.1993 -0.0373 0.0070  0.0179  262  ILE B C   
10903 O O   . ILE B 264  ? 0.3031 0.2867 0.2173 -0.0398 0.0067  0.0192  262  ILE B O   
10904 C CB  . ILE B 264  ? 0.2993 0.2750 0.2016 -0.0356 0.0039  0.0195  262  ILE B CB  
10905 C CG1 . ILE B 264  ? 0.2820 0.2590 0.1865 -0.0318 0.0028  0.0166  262  ILE B CG1 
10906 C CG2 . ILE B 264  ? 0.3127 0.2828 0.2162 -0.0366 0.0015  0.0205  262  ILE B CG2 
10907 C CD1 . ILE B 264  ? 0.3212 0.2922 0.2222 -0.0299 -0.0004 0.0167  262  ILE B CD1 
10908 N N   . SER B 265  ? 0.2412 0.2300 0.1580 -0.0344 0.0072  0.0153  263  SER B N   
10909 C CA  . SER B 265  ? 0.2428 0.2336 0.1660 -0.0336 0.0067  0.0137  263  SER B CA  
10910 C C   . SER B 265  ? 0.2802 0.2677 0.2046 -0.0303 0.0041  0.0118  263  SER B C   
10911 O O   . SER B 265  ? 0.3124 0.2997 0.2346 -0.0280 0.0038  0.0108  263  SER B O   
10912 C CB  . SER B 265  ? 0.2822 0.2808 0.2096 -0.0331 0.0094  0.0122  263  SER B CB  
10913 O OG  . SER B 265  ? 0.2919 0.2943 0.2198 -0.0364 0.0116  0.0139  263  SER B OG  
10914 N N   . ILE B 266  ? 0.2536 0.2383 0.1812 -0.0300 0.0023  0.0114  264  ILE B N   
10915 C CA  . ILE B 266  ? 0.2409 0.2228 0.1702 -0.0270 -0.0001 0.0098  264  ILE B CA  
10916 C C   . ILE B 266  ? 0.2484 0.2332 0.1839 -0.0260 0.0001  0.0080  264  ILE B C   
10917 O O   . ILE B 266  ? 0.2582 0.2455 0.1962 -0.0280 0.0013  0.0083  264  ILE B O   
10918 C CB  . ILE B 266  ? 0.2790 0.2536 0.2056 -0.0271 -0.0028 0.0112  264  ILE B CB  
10919 C CG1 . ILE B 266  ? 0.3294 0.3016 0.2575 -0.0293 -0.0032 0.0122  264  ILE B CG1 
10920 C CG2 . ILE B 266  ? 0.2921 0.2635 0.2121 -0.0280 -0.0031 0.0131  264  ILE B CG2 
10921 C CD1 . ILE B 266  ? 0.3422 0.3071 0.2688 -0.0287 -0.0060 0.0131  264  ILE B CD1 
10922 N N   . LYS B 267  ? 0.2439 0.2283 0.1817 -0.0231 -0.0013 0.0061  265  LYS B N   
10923 C CA  . LYS B 267  ? 0.2419 0.2280 0.1852 -0.0219 -0.0016 0.0044  265  LYS B CA  
10924 C C   . LYS B 267  ? 0.2358 0.2166 0.1796 -0.0206 -0.0042 0.0043  265  LYS B C   
10925 O O   . LYS B 267  ? 0.2490 0.2271 0.1910 -0.0188 -0.0058 0.0041  265  LYS B O   
10926 C CB  . LYS B 267  ? 0.2653 0.2559 0.2112 -0.0195 -0.0007 0.0022  265  LYS B CB  
10927 C CG  . LYS B 267  ? 0.3469 0.3436 0.2938 -0.0205 0.0021  0.0020  265  LYS B CG  
10928 C CD  . LYS B 267  ? 0.4202 0.4207 0.3692 -0.0179 0.0029  -0.0001 265  LYS B CD  
10929 C CE  . LYS B 267  ? 0.4665 0.4732 0.4168 -0.0185 0.0058  -0.0003 265  LYS B CE  
10930 N NZ  . LYS B 267  ? 0.4593 0.4669 0.4055 -0.0206 0.0074  0.0014  265  LYS B NZ  
10931 N N   . LEU B 268  ? 0.2335 0.2127 0.1797 -0.0215 -0.0047 0.0045  266  LEU B N   
10932 C CA  . LEU B 268  ? 0.2458 0.2200 0.1927 -0.0201 -0.0069 0.0043  266  LEU B CA  
10933 C C   . LEU B 268  ? 0.2583 0.2339 0.2083 -0.0169 -0.0078 0.0023  266  LEU B C   
10934 O O   . LEU B 268  ? 0.2478 0.2198 0.1974 -0.0152 -0.0098 0.0024  266  LEU B O   
10935 C CB  . LEU B 268  ? 0.2497 0.2223 0.1986 -0.0215 -0.0070 0.0045  266  LEU B CB  
10936 C CG  . LEU B 268  ? 0.2576 0.2282 0.2034 -0.0249 -0.0065 0.0066  266  LEU B CG  
10937 C CD1 . LEU B 268  ? 0.2969 0.2652 0.2445 -0.0262 -0.0068 0.0066  266  LEU B CD1 
10938 C CD2 . LEU B 268  ? 0.3025 0.2677 0.2431 -0.0254 -0.0078 0.0085  266  LEU B CD2 
10939 N N   . SER B 269  ? 0.2415 0.2222 0.1946 -0.0161 -0.0064 0.0007  267  SER B N   
10940 C CA  . SER B 269  ? 0.2332 0.2151 0.1892 -0.0133 -0.0072 -0.0011 267  SER B CA  
10941 C C   . SER B 269  ? 0.2470 0.2276 0.2001 -0.0119 -0.0084 -0.0011 267  SER B C   
10942 O O   . SER B 269  ? 0.2494 0.2294 0.2043 -0.0098 -0.0097 -0.0022 267  SER B O   
10943 C CB  . SER B 269  ? 0.2619 0.2492 0.2213 -0.0127 -0.0055 -0.0027 267  SER B CB  
10944 O OG  . SER B 269  ? 0.2614 0.2518 0.2187 -0.0131 -0.0040 -0.0027 267  SER B OG  
10945 N N   . ALA B 270  ? 0.2170 0.1971 0.1656 -0.0132 -0.0078 0.0001  268  ALA B N   
10946 C CA  . ALA B 270  ? 0.2459 0.2242 0.1911 -0.0121 -0.0092 0.0003  268  ALA B CA  
10947 C C   . ALA B 270  ? 0.2742 0.2472 0.2180 -0.0115 -0.0118 0.0014  268  ALA B C   
10948 O O   . ALA B 270  ? 0.2488 0.2204 0.1911 -0.0100 -0.0135 0.0012  268  ALA B O   
10949 C CB  . ALA B 270  ? 0.2668 0.2457 0.2071 -0.0137 -0.0078 0.0014  268  ALA B CB  
10950 N N   . LEU B 271  ? 0.2491 0.2192 0.1932 -0.0125 -0.0122 0.0026  269  LEU B N   
10951 C CA  . LEU B 271  ? 0.2783 0.2430 0.2202 -0.0122 -0.0145 0.0040  269  LEU B CA  
10952 C C   . LEU B 271  ? 0.2441 0.2073 0.1901 -0.0101 -0.0161 0.0031  269  LEU B C   
10953 O O   . LEU B 271  ? 0.2746 0.2335 0.2193 -0.0093 -0.0181 0.0042  269  LEU B O   
10954 C CB  . LEU B 271  ? 0.2467 0.2082 0.1855 -0.0147 -0.0140 0.0061  269  LEU B CB  
10955 C CG  . LEU B 271  ? 0.2771 0.2395 0.2112 -0.0167 -0.0127 0.0073  269  LEU B CG  
10956 C CD1 . LEU B 271  ? 0.3335 0.2932 0.2652 -0.0196 -0.0120 0.0093  269  LEU B CD1 
10957 C CD2 . LEU B 271  ? 0.3086 0.2688 0.2385 -0.0158 -0.0143 0.0081  269  LEU B CD2 
10958 N N   . HIS B 272  ? 0.2508 0.2174 0.2015 -0.0091 -0.0152 0.0013  270  HIS B N   
10959 C CA  . HIS B 272  ? 0.2510 0.2164 0.2055 -0.0070 -0.0166 0.0005  270  HIS B CA  
10960 C C   . HIS B 272  ? 0.2206 0.1905 0.1794 -0.0058 -0.0157 -0.0016 270  HIS B C   
10961 O O   . HIS B 272  ? 0.2578 0.2310 0.2177 -0.0069 -0.0137 -0.0023 270  HIS B O   
10962 C CB  . HIS B 272  ? 0.2616 0.2242 0.2170 -0.0078 -0.0164 0.0011  270  HIS B CB  
10963 C CG  . HIS B 272  ? 0.2768 0.2369 0.2347 -0.0056 -0.0181 0.0008  270  HIS B CG  
10964 N ND1 . HIS B 272  ? 0.2772 0.2397 0.2398 -0.0039 -0.0178 -0.0009 270  HIS B ND1 
10965 C CD2 . HIS B 272  ? 0.3356 0.2910 0.2920 -0.0046 -0.0200 0.0020  270  HIS B CD2 
10966 C CE1 . HIS B 272  ? 0.2949 0.2547 0.2590 -0.0021 -0.0193 -0.0007 270  HIS B CE1 
10967 N NE2 . HIS B 272  ? 0.3273 0.2828 0.2878 -0.0023 -0.0207 0.0010  270  HIS B NE2 
10968 N N   . PRO B 273  ? 0.2347 0.2050 0.1963 -0.0036 -0.0171 -0.0025 271  PRO B N   
10969 C CA  . PRO B 273  ? 0.2501 0.2244 0.2157 -0.0026 -0.0162 -0.0044 271  PRO B CA  
10970 C C   . PRO B 273  ? 0.2222 0.1976 0.1916 -0.0025 -0.0151 -0.0051 271  PRO B C   
10971 O O   . PRO B 273  ? 0.2501 0.2288 0.2224 -0.0019 -0.0141 -0.0066 271  PRO B O   
10972 C CB  . PRO B 273  ? 0.2599 0.2338 0.2270 -0.0006 -0.0183 -0.0048 271  PRO B CB  
10973 C CG  . PRO B 273  ? 0.2926 0.2623 0.2582 -0.0002 -0.0201 -0.0032 271  PRO B CG  
10974 C CD  . PRO B 273  ? 0.2452 0.2125 0.2061 -0.0022 -0.0195 -0.0017 271  PRO B CD  
10975 N N   . ARG B 274  ? 0.2236 0.1960 0.1927 -0.0030 -0.0153 -0.0043 272  ARG B N   
10976 C CA  . ARG B 274  ? 0.2196 0.1923 0.1917 -0.0029 -0.0144 -0.0051 272  ARG B CA  
10977 C C   . ARG B 274  ? 0.2387 0.2099 0.2085 -0.0052 -0.0134 -0.0042 272  ARG B C   
10978 O O   . ARG B 274  ? 0.2547 0.2227 0.2245 -0.0055 -0.0137 -0.0038 272  ARG B O   
10979 C CB  . ARG B 274  ? 0.2448 0.2152 0.2193 -0.0010 -0.0157 -0.0052 272  ARG B CB  
10980 C CG  . ARG B 274  ? 0.2532 0.2256 0.2307 0.0012  -0.0166 -0.0061 272  ARG B CG  
10981 C CD  . ARG B 274  ? 0.2555 0.2323 0.2358 0.0013  -0.0153 -0.0076 272  ARG B CD  
10982 N NE  . ARG B 274  ? 0.2563 0.2340 0.2389 0.0011  -0.0139 -0.0084 272  ARG B NE  
10983 C CZ  . ARG B 274  ? 0.2461 0.2234 0.2317 0.0025  -0.0141 -0.0090 272  ARG B CZ  
10984 N NH1 . ARG B 274  ? 0.2416 0.2178 0.2288 0.0043  -0.0155 -0.0088 272  ARG B NH1 
10985 N NH2 . ARG B 274  ? 0.2537 0.2318 0.2408 0.0021  -0.0128 -0.0097 272  ARG B NH2 
10986 N N   . TYR B 275  ? 0.2181 0.1915 0.1859 -0.0071 -0.0122 -0.0038 273  TYR B N   
10987 C CA  . TYR B 275  ? 0.2573 0.2300 0.2233 -0.0096 -0.0111 -0.0029 273  TYR B CA  
10988 C C   . TYR B 275  ? 0.2394 0.2149 0.2086 -0.0100 -0.0099 -0.0041 273  TYR B C   
10989 O O   . TYR B 275  ? 0.2388 0.2189 0.2094 -0.0105 -0.0085 -0.0048 273  TYR B O   
10990 C CB  . TYR B 275  ? 0.2374 0.2118 0.2002 -0.0113 -0.0102 -0.0019 273  TYR B CB  
10991 C CG  . TYR B 275  ? 0.2256 0.2001 0.1869 -0.0142 -0.0090 -0.0009 273  TYR B CG  
10992 C CD1 . TYR B 275  ? 0.2521 0.2219 0.2118 -0.0155 -0.0098 0.0001  273  TYR B CD1 
10993 C CD2 . TYR B 275  ? 0.2223 0.2015 0.1839 -0.0156 -0.0072 -0.0010 273  TYR B CD2 
10994 C CE1 . TYR B 275  ? 0.2587 0.2284 0.2171 -0.0184 -0.0088 0.0011  273  TYR B CE1 
10995 C CE2 . TYR B 275  ? 0.2406 0.2203 0.2012 -0.0185 -0.0061 0.0000  273  TYR B CE2 
10996 C CZ  . TYR B 275  ? 0.2411 0.2160 0.2002 -0.0200 -0.0070 0.0010  273  TYR B CZ  
10997 O OH  . TYR B 275  ? 0.2709 0.2462 0.2291 -0.0230 -0.0061 0.0021  273  TYR B OH  
10998 N N   . SER B 276  ? 0.2273 0.2001 0.1976 -0.0097 -0.0104 -0.0043 274  SER B N   
10999 C CA  . SER B 276  ? 0.2360 0.2111 0.2093 -0.0100 -0.0094 -0.0055 274  SER B CA  
11000 C C   . SER B 276  ? 0.2380 0.2086 0.2106 -0.0104 -0.0100 -0.0053 274  SER B C   
11001 O O   . SER B 276  ? 0.2326 0.1986 0.2037 -0.0095 -0.0112 -0.0046 274  SER B O   
11002 C CB  . SER B 276  ? 0.2738 0.2518 0.2507 -0.0076 -0.0093 -0.0070 274  SER B CB  
11003 O OG  . SER B 276  ? 0.3288 0.3038 0.3067 -0.0056 -0.0105 -0.0073 274  SER B OG  
11004 N N   . ARG B 277  ? 0.2323 0.2041 0.2060 -0.0117 -0.0091 -0.0058 275  ARG B N   
11005 C CA  . ARG B 277  ? 0.2158 0.1832 0.1887 -0.0121 -0.0096 -0.0059 275  ARG B CA  
11006 C C   . ARG B 277  ? 0.2233 0.1886 0.1979 -0.0092 -0.0104 -0.0068 275  ARG B C   
11007 O O   . ARG B 277  ? 0.2332 0.1934 0.2063 -0.0088 -0.0112 -0.0066 275  ARG B O   
11008 C CB  . ARG B 277  ? 0.2358 0.2056 0.2098 -0.0140 -0.0087 -0.0065 275  ARG B CB  
11009 C CG  . ARG B 277  ? 0.2507 0.2162 0.2239 -0.0143 -0.0092 -0.0070 275  ARG B CG  
11010 C CD  . ARG B 277  ? 0.2507 0.2100 0.2200 -0.0158 -0.0101 -0.0057 275  ARG B CD  
11011 N NE  . ARG B 277  ? 0.2559 0.2105 0.2240 -0.0161 -0.0106 -0.0063 275  ARG B NE  
11012 C CZ  . ARG B 277  ? 0.2677 0.2182 0.2357 -0.0136 -0.0112 -0.0069 275  ARG B CZ  
11013 N NH1 . ARG B 277  ? 0.2831 0.2343 0.2528 -0.0107 -0.0115 -0.0071 275  ARG B NH1 
11014 N NH2 . ARG B 277  ? 0.2644 0.2102 0.2307 -0.0140 -0.0116 -0.0074 275  ARG B NH2 
11015 N N   . ALA B 278  ? 0.2305 0.1995 0.2083 -0.0072 -0.0100 -0.0079 276  ALA B N   
11016 C CA  . ALA B 278  ? 0.2422 0.2098 0.2220 -0.0045 -0.0106 -0.0087 276  ALA B CA  
11017 C C   . ALA B 278  ? 0.2328 0.1966 0.2112 -0.0032 -0.0119 -0.0077 276  ALA B C   
11018 O O   . ALA B 278  ? 0.2542 0.2154 0.2335 -0.0012 -0.0125 -0.0081 276  ALA B O   
11019 C CB  . ALA B 278  ? 0.2629 0.2353 0.2463 -0.0029 -0.0100 -0.0098 276  ALA B CB  
11020 N N   . GLN B 279  ? 0.2380 0.2015 0.2141 -0.0041 -0.0125 -0.0065 277  GLN B N   
11021 C CA  . GLN B 279  ? 0.2290 0.1890 0.2034 -0.0029 -0.0140 -0.0055 277  GLN B CA  
11022 C C   . GLN B 279  ? 0.2595 0.2150 0.2296 -0.0050 -0.0145 -0.0039 277  GLN B C   
11023 O O   . GLN B 279  ? 0.2461 0.1997 0.2138 -0.0050 -0.0155 -0.0026 277  GLN B O   
11024 C CB  . GLN B 279  ? 0.2685 0.2315 0.2435 -0.0020 -0.0145 -0.0053 277  GLN B CB  
11025 C CG  . GLN B 279  ? 0.2532 0.2203 0.2325 -0.0001 -0.0142 -0.0067 277  GLN B CG  
11026 C CD  . GLN B 279  ? 0.2985 0.2637 0.2801 0.0023  -0.0149 -0.0071 277  GLN B CD  
11027 O OE1 . GLN B 279  ? 0.3288 0.2900 0.3091 0.0031  -0.0161 -0.0063 277  GLN B OE1 
11028 N NE2 . GLN B 279  ? 0.2668 0.2350 0.2521 0.0034  -0.0141 -0.0084 277  GLN B NE2 
11029 N N   . ALA B 280  ? 0.2602 0.2137 0.2291 -0.0067 -0.0139 -0.0040 278  ALA B N   
11030 C CA  . ALA B 280  ? 0.2552 0.2046 0.2199 -0.0092 -0.0142 -0.0025 278  ALA B CA  
11031 C C   . ALA B 280  ? 0.2672 0.2107 0.2293 -0.0080 -0.0158 -0.0013 278  ALA B C   
11032 O O   . ALA B 280  ? 0.2668 0.2078 0.2254 -0.0096 -0.0164 0.0004  278  ALA B O   
11033 C CB  . ALA B 280  ? 0.2748 0.2224 0.2389 -0.0112 -0.0136 -0.0029 278  ALA B CB  
11034 N N   . ALA B 281  ? 0.2523 0.1937 0.2162 -0.0051 -0.0166 -0.0019 279  ALA B N   
11035 C CA  . ALA B 281  ? 0.2643 0.2003 0.2260 -0.0037 -0.0182 -0.0007 279  ALA B CA  
11036 C C   . ALA B 281  ? 0.2692 0.2066 0.2301 -0.0031 -0.0192 0.0004  279  ALA B C   
11037 O O   . ALA B 281  ? 0.2855 0.2187 0.2427 -0.0038 -0.0203 0.0021  279  ALA B O   
11038 C CB  . ALA B 281  ? 0.3081 0.2424 0.2724 -0.0004 -0.0186 -0.0018 279  ALA B CB  
11039 N N   . ARG B 282  ? 0.2422 0.1851 0.2062 -0.0020 -0.0189 -0.0004 280  ARG B N   
11040 C CA  . ARG B 282  ? 0.2613 0.2057 0.2243 -0.0017 -0.0199 0.0005  280  ARG B CA  
11041 C C   . ARG B 282  ? 0.2668 0.2116 0.2260 -0.0047 -0.0193 0.0016  280  ARG B C   
11042 O O   . ARG B 282  ? 0.2810 0.2241 0.2372 -0.0049 -0.0204 0.0031  280  ARG B O   
11043 C CB  . ARG B 282  ? 0.2828 0.2328 0.2498 -0.0001 -0.0197 -0.0008 280  ARG B CB  
11044 C CG  . ARG B 282  ? 0.2728 0.2229 0.2436 0.0030  -0.0205 -0.0016 280  ARG B CG  
11045 C CD  . ARG B 282  ? 0.2904 0.2457 0.2645 0.0042  -0.0206 -0.0025 280  ARG B CD  
11046 N NE  . ARG B 282  ? 0.2940 0.2492 0.2659 0.0042  -0.0221 -0.0014 280  ARG B NE  
11047 C CZ  . ARG B 282  ? 0.2797 0.2388 0.2528 0.0043  -0.0223 -0.0020 280  ARG B CZ  
11048 N NH1 . ARG B 282  ? 0.2803 0.2437 0.2567 0.0045  -0.0211 -0.0035 280  ARG B NH1 
11049 N NH2 . ARG B 282  ? 0.3125 0.2708 0.2829 0.0043  -0.0239 -0.0009 280  ARG B NH2 
11050 N N   . VAL B 283  ? 0.2542 0.2014 0.2137 -0.0069 -0.0176 0.0011  281  VAL B N   
11051 C CA  . VAL B 283  ? 0.2866 0.2345 0.2428 -0.0099 -0.0168 0.0022  281  VAL B CA  
11052 C C   . VAL B 283  ? 0.2700 0.2117 0.2216 -0.0114 -0.0177 0.0042  281  VAL B C   
11053 O O   . VAL B 283  ? 0.2727 0.2133 0.2209 -0.0124 -0.0182 0.0057  281  VAL B O   
11054 C CB  . VAL B 283  ? 0.2522 0.2041 0.2100 -0.0118 -0.0148 0.0013  281  VAL B CB  
11055 C CG1 . VAL B 283  ? 0.2909 0.2432 0.2455 -0.0151 -0.0139 0.0027  281  VAL B CG1 
11056 C CG2 . VAL B 283  ? 0.2603 0.2183 0.2219 -0.0104 -0.0140 -0.0004 281  VAL B CG2 
11057 N N   . MET B 284  ? 0.2599 0.1971 0.2112 -0.0114 -0.0180 0.0041  282  MET B N   
11058 C CA  . MET B 284  ? 0.2935 0.2242 0.2403 -0.0129 -0.0189 0.0059  282  MET B CA  
11059 C C   . MET B 284  ? 0.3105 0.2373 0.2555 -0.0107 -0.0209 0.0072  282  MET B C   
11060 O O   . MET B 284  ? 0.3316 0.2543 0.2722 -0.0121 -0.0217 0.0091  282  MET B O   
11061 C CB  . MET B 284  ? 0.2755 0.2019 0.2222 -0.0134 -0.0189 0.0054  282  MET B CB  
11062 C CG  . MET B 284  ? 0.3053 0.2353 0.2536 -0.0159 -0.0172 0.0044  282  MET B CG  
11063 S SD  . MET B 284  ? 0.3344 0.2668 0.2799 -0.0203 -0.0160 0.0059  282  MET B SD  
11064 C CE  . MET B 284  ? 0.3643 0.2879 0.3043 -0.0224 -0.0172 0.0080  282  MET B CE  
11065 N N   . GLY B 285  ? 0.2760 0.2041 0.2243 -0.0073 -0.0218 0.0061  283  GLY B N   
11066 C CA  . GLY B 285  ? 0.2997 0.2245 0.2468 -0.0050 -0.0238 0.0073  283  GLY B CA  
11067 C C   . GLY B 285  ? 0.3261 0.2534 0.2718 -0.0050 -0.0246 0.0082  283  GLY B C   
11068 O O   . GLY B 285  ? 0.3481 0.2717 0.2907 -0.0044 -0.0263 0.0098  283  GLY B O   
11069 N N   . GLU B 286  ? 0.2707 0.2042 0.2183 -0.0056 -0.0233 0.0071  284  GLU B N   
11070 C CA  . GLU B 286  ? 0.2593 0.1956 0.2061 -0.0052 -0.0240 0.0074  284  GLU B CA  
11071 C C   . GLU B 286  ? 0.2982 0.2371 0.2421 -0.0080 -0.0225 0.0079  284  GLU B C   
11072 O O   . GLU B 286  ? 0.3365 0.2747 0.2768 -0.0086 -0.0233 0.0092  284  GLU B O   
11073 C CB  . GLU B 286  ? 0.2916 0.2328 0.2433 -0.0028 -0.0241 0.0056  284  GLU B CB  
11074 C CG  . GLU B 286  ? 0.2984 0.2379 0.2536 0.0001  -0.0254 0.0050  284  GLU B CG  
11075 C CD  . GLU B 286  ? 0.3403 0.2850 0.3009 0.0020  -0.0250 0.0031  284  GLU B CD  
11076 O OE1 . GLU B 286  ? 0.3246 0.2734 0.2856 0.0016  -0.0247 0.0025  284  GLU B OE1 
11077 O OE2 . GLU B 286  ? 0.3945 0.3389 0.3585 0.0038  -0.0250 0.0023  284  GLU B OE2 
11078 N N   . LEU B 287  ? 0.2820 0.2242 0.2275 -0.0098 -0.0204 0.0069  285  LEU B N   
11079 C CA  . LEU B 287  ? 0.2978 0.2432 0.2412 -0.0123 -0.0187 0.0073  285  LEU B CA  
11080 C C   . LEU B 287  ? 0.3180 0.2592 0.2566 -0.0151 -0.0186 0.0094  285  LEU B C   
11081 O O   . LEU B 287  ? 0.2746 0.2158 0.2093 -0.0166 -0.0184 0.0108  285  LEU B O   
11082 C CB  . LEU B 287  ? 0.2756 0.2261 0.2227 -0.0131 -0.0166 0.0055  285  LEU B CB  
11083 C CG  . LEU B 287  ? 0.3214 0.2774 0.2682 -0.0144 -0.0148 0.0052  285  LEU B CG  
11084 C CD1 . LEU B 287  ? 0.3020 0.2628 0.2532 -0.0143 -0.0132 0.0033  285  LEU B CD1 
11085 C CD2 . LEU B 287  ? 0.3555 0.3106 0.2981 -0.0176 -0.0138 0.0069  285  LEU B CD2 
11086 N N   . LEU B 288  ? 0.2923 0.2296 0.2309 -0.0160 -0.0187 0.0097  286  LEU B N   
11087 C CA  . LEU B 288  ? 0.3070 0.2400 0.2412 -0.0190 -0.0185 0.0118  286  LEU B CA  
11088 C C   . LEU B 288  ? 0.3104 0.2389 0.2396 -0.0190 -0.0201 0.0140  286  LEU B C   
11089 O O   . LEU B 288  ? 0.2986 0.2270 0.2240 -0.0217 -0.0193 0.0156  286  LEU B O   
11090 C CB  . LEU B 288  ? 0.3351 0.2638 0.2698 -0.0196 -0.0187 0.0116  286  LEU B CB  
11091 C CG  . LEU B 288  ? 0.3535 0.2764 0.2834 -0.0226 -0.0190 0.0138  286  LEU B CG  
11092 C CD1 . LEU B 288  ? 0.3636 0.2903 0.2921 -0.0264 -0.0171 0.0146  286  LEU B CD1 
11093 C CD2 . LEU B 288  ? 0.4506 0.3690 0.3812 -0.0229 -0.0194 0.0132  286  LEU B CD2 
11094 N N   . PRO B 289  ? 0.2978 0.2228 0.2268 -0.0162 -0.0223 0.0142  287  PRO B N   
11095 C CA  . PRO B 289  ? 0.3200 0.2410 0.2441 -0.0162 -0.0239 0.0164  287  PRO B CA  
11096 C C   . PRO B 289  ? 0.2975 0.2225 0.2193 -0.0171 -0.0232 0.0168  287  PRO B C   
11097 O O   . PRO B 289  ? 0.3133 0.2355 0.2299 -0.0188 -0.0235 0.0189  287  PRO B O   
11098 C CB  . PRO B 289  ? 0.3738 0.2923 0.2996 -0.0125 -0.0263 0.0161  287  PRO B CB  
11099 C CG  . PRO B 289  ? 0.3451 0.2633 0.2753 -0.0113 -0.0258 0.0144  287  PRO B CG  
11100 C CD  . PRO B 289  ? 0.3173 0.2415 0.2504 -0.0130 -0.0234 0.0128  287  PRO B CD  
11101 N N   . ARG B 290  ? 0.2859 0.2172 0.2112 -0.0161 -0.0221 0.0149  288  ARG B N   
11102 C CA  . ARG B 290  ? 0.3032 0.2383 0.2262 -0.0169 -0.0213 0.0150  288  ARG B CA  
11103 C C   . ARG B 290  ? 0.2762 0.2130 0.1967 -0.0204 -0.0189 0.0160  288  ARG B C   
11104 O O   . ARG B 290  ? 0.2837 0.2201 0.1996 -0.0219 -0.0186 0.0175  288  ARG B O   
11105 C CB  . ARG B 290  ? 0.3217 0.2627 0.2491 -0.0149 -0.0207 0.0126  288  ARG B CB  
11106 C CG  . ARG B 290  ? 0.3511 0.2912 0.2805 -0.0117 -0.0231 0.0119  288  ARG B CG  
11107 C CD  . ARG B 290  ? 0.4476 0.3932 0.3817 -0.0100 -0.0226 0.0095  288  ARG B CD  
11108 N NE  . ARG B 290  ? 0.4887 0.4343 0.4232 -0.0076 -0.0248 0.0092  288  ARG B NE  
11109 C CZ  . ARG B 290  ? 0.5334 0.4827 0.4720 -0.0058 -0.0250 0.0073  288  ARG B CZ  
11110 N NH1 . ARG B 290  ? 0.4642 0.4174 0.4070 -0.0058 -0.0232 0.0055  288  ARG B NH1 
11111 N NH2 . ARG B 290  ? 0.5061 0.4552 0.4447 -0.0040 -0.0273 0.0073  288  ARG B NH2 
11112 N N   . VAL B 291  ? 0.2925 0.2313 0.2160 -0.0219 -0.0172 0.0151  289  VAL B N   
11113 C CA  . VAL B 291  ? 0.2824 0.2231 0.2040 -0.0254 -0.0150 0.0162  289  VAL B CA  
11114 C C   . VAL B 291  ? 0.3009 0.2354 0.2173 -0.0277 -0.0158 0.0189  289  VAL B C   
11115 O O   . VAL B 291  ? 0.3028 0.2380 0.2153 -0.0302 -0.0145 0.0205  289  VAL B O   
11116 C CB  . VAL B 291  ? 0.2874 0.2314 0.2135 -0.0265 -0.0134 0.0148  289  VAL B CB  
11117 C CG1 . VAL B 291  ? 0.3088 0.2558 0.2333 -0.0301 -0.0111 0.0159  289  VAL B CG1 
11118 C CG2 . VAL B 291  ? 0.3383 0.2878 0.2694 -0.0241 -0.0128 0.0122  289  VAL B CG2 
11119 N N   . LYS B 292  ? 0.2977 0.2260 0.2136 -0.0269 -0.0177 0.0195  290  LYS B N   
11120 C CA  . LYS B 292  ? 0.3137 0.2354 0.2243 -0.0290 -0.0186 0.0222  290  LYS B CA  
11121 C C   . LYS B 292  ? 0.3426 0.2627 0.2481 -0.0288 -0.0195 0.0239  290  LYS B C   
11122 O O   . LYS B 292  ? 0.3347 0.2528 0.2354 -0.0317 -0.0188 0.0262  290  LYS B O   
11123 C CB  . LYS B 292  ? 0.3447 0.2596 0.2556 -0.0275 -0.0207 0.0223  290  LYS B CB  
11124 C CG  . LYS B 292  ? 0.3934 0.3007 0.2989 -0.0298 -0.0216 0.0251  290  LYS B CG  
11125 C CD  . LYS B 292  ? 0.4520 0.3545 0.3533 -0.0280 -0.0239 0.0268  290  LYS B CD  
11126 C CE  . LYS B 292  ? 0.4566 0.3514 0.3521 -0.0305 -0.0248 0.0297  290  LYS B CE  
11127 N NZ  . LYS B 292  ? 0.4252 0.3140 0.3214 -0.0304 -0.0257 0.0296  290  LYS B NZ  
11128 N N   . ALA B 293  ? 0.2965 0.2177 0.2029 -0.0256 -0.0209 0.0230  291  ALA B N   
11129 C CA  . ALA B 293  ? 0.3061 0.2259 0.2075 -0.0253 -0.0220 0.0246  291  ALA B CA  
11130 C C   . ALA B 293  ? 0.3495 0.2740 0.2484 -0.0276 -0.0195 0.0249  291  ALA B C   
11131 O O   . ALA B 293  ? 0.3216 0.2436 0.2147 -0.0294 -0.0195 0.0272  291  ALA B O   
11132 C CB  . ALA B 293  ? 0.3198 0.2407 0.2233 -0.0215 -0.0240 0.0232  291  ALA B CB  
11133 N N   . LEU B 294  ? 0.2859 0.2172 0.1890 -0.0275 -0.0174 0.0228  292  LEU B N   
11134 C CA  . LEU B 294  ? 0.2928 0.2291 0.1940 -0.0295 -0.0148 0.0229  292  LEU B CA  
11135 C C   . LEU B 294  ? 0.3086 0.2439 0.2075 -0.0335 -0.0130 0.0249  292  LEU B C   
11136 O O   . LEU B 294  ? 0.3210 0.2571 0.2155 -0.0356 -0.0117 0.0266  292  LEU B O   
11137 C CB  . LEU B 294  ? 0.2922 0.2356 0.1988 -0.0283 -0.0131 0.0201  292  LEU B CB  
11138 C CG  . LEU B 294  ? 0.2922 0.2371 0.2012 -0.0246 -0.0147 0.0181  292  LEU B CG  
11139 C CD1 . LEU B 294  ? 0.3144 0.2657 0.2289 -0.0237 -0.0129 0.0155  292  LEU B CD1 
11140 C CD2 . LEU B 294  ? 0.3046 0.2488 0.2085 -0.0239 -0.0154 0.0188  292  LEU B CD2 
11141 N N   . ALA B 295  ? 0.3073 0.2411 0.2091 -0.0346 -0.0130 0.0248  293  ALA B N   
11142 C CA  . ALA B 295  ? 0.3139 0.2467 0.2138 -0.0387 -0.0115 0.0267  293  ALA B CA  
11143 C C   . ALA B 295  ? 0.3309 0.2568 0.2243 -0.0403 -0.0128 0.0298  293  ALA B C   
11144 O O   . ALA B 295  ? 0.3222 0.2484 0.2119 -0.0437 -0.0112 0.0318  293  ALA B O   
11145 C CB  . ALA B 295  ? 0.3063 0.2381 0.2105 -0.0394 -0.0116 0.0258  293  ALA B CB  
11146 N N   . LEU B 296  ? 0.3379 0.2576 0.2296 -0.0380 -0.0157 0.0302  294  LEU B N   
11147 C CA  . LEU B 296  ? 0.3536 0.2663 0.2387 -0.0392 -0.0172 0.0332  294  LEU B CA  
11148 C C   . LEU B 296  ? 0.3523 0.2670 0.2326 -0.0398 -0.0163 0.0344  294  LEU B C   
11149 O O   . LEU B 296  ? 0.3547 0.2665 0.2295 -0.0427 -0.0158 0.0371  294  LEU B O   
11150 C CB  . LEU B 296  ? 0.3693 0.2757 0.2542 -0.0359 -0.0205 0.0332  294  LEU B CB  
11151 C CG  . LEU B 296  ? 0.4507 0.3489 0.3291 -0.0366 -0.0225 0.0363  294  LEU B CG  
11152 C CD1 . LEU B 296  ? 0.4798 0.3739 0.3554 -0.0408 -0.0216 0.0384  294  LEU B CD1 
11153 C CD2 . LEU B 296  ? 0.5101 0.4030 0.3897 -0.0329 -0.0257 0.0359  294  LEU B CD2 
11154 N N   . LEU B 297  ? 0.3239 0.2435 0.2058 -0.0372 -0.0162 0.0325  295  LEU B N   
11155 C CA  . LEU B 297  ? 0.3474 0.2692 0.2245 -0.0377 -0.0151 0.0334  295  LEU B CA  
11156 C C   . LEU B 297  ? 0.3358 0.2625 0.2122 -0.0413 -0.0116 0.0341  295  LEU B C   
11157 O O   . LEU B 297  ? 0.3320 0.2575 0.2027 -0.0436 -0.0106 0.0364  295  LEU B O   
11158 C CB  . LEU B 297  ? 0.3323 0.2586 0.2117 -0.0344 -0.0155 0.0309  295  LEU B CB  
11159 C CG  . LEU B 297  ? 0.4596 0.3818 0.3382 -0.0310 -0.0191 0.0306  295  LEU B CG  
11160 C CD1 . LEU B 297  ? 0.4051 0.3325 0.2872 -0.0281 -0.0192 0.0278  295  LEU B CD1 
11161 C CD2 . LEU B 297  ? 0.4463 0.3635 0.3173 -0.0317 -0.0205 0.0333  295  LEU B CD2 
11162 N N   . ALA B 298  ? 0.3178 0.2502 0.2001 -0.0417 -0.0096 0.0322  296  ALA B N   
11163 C CA  . ALA B 298  ? 0.3013 0.2390 0.1837 -0.0450 -0.0062 0.0328  296  ALA B CA  
11164 C C   . ALA B 298  ? 0.3472 0.2804 0.2260 -0.0491 -0.0059 0.0359  296  ALA B C   
11165 O O   . ALA B 298  ? 0.3642 0.2992 0.2394 -0.0519 -0.0038 0.0378  296  ALA B O   
11166 C CB  . ALA B 298  ? 0.3082 0.2522 0.1980 -0.0447 -0.0046 0.0303  296  ALA B CB  
11167 N N   . LYS B 299  ? 0.3438 0.2710 0.2235 -0.0494 -0.0080 0.0364  297  LYS B N   
11168 C CA  . LYS B 299  ? 0.3625 0.2842 0.2383 -0.0532 -0.0082 0.0394  297  LYS B CA  
11169 C C   . LYS B 299  ? 0.3965 0.3136 0.2646 -0.0540 -0.0088 0.0422  297  LYS B C   
11170 O O   . LYS B 299  ? 0.4026 0.3190 0.2668 -0.0578 -0.0073 0.0448  297  LYS B O   
11171 C CB  . LYS B 299  ? 0.3764 0.2914 0.2539 -0.0526 -0.0107 0.0393  297  LYS B CB  
11172 C CG  . LYS B 299  ? 0.4493 0.3570 0.3219 -0.0562 -0.0113 0.0424  297  LYS B CG  
11173 C CD  . LYS B 299  ? 0.5843 0.4834 0.4566 -0.0544 -0.0145 0.0425  297  LYS B CD  
11174 C CE  . LYS B 299  ? 0.5219 0.4134 0.3893 -0.0581 -0.0151 0.0455  297  LYS B CE  
11175 N NZ  . LYS B 299  ? 0.6082 0.4968 0.4686 -0.0596 -0.0151 0.0486  297  LYS B NZ  
11176 N N   . ASN B 300  ? 0.3803 0.2941 0.2460 -0.0506 -0.0112 0.0419  298  ASN B N   
11177 C CA  . ASN B 300  ? 0.4304 0.3391 0.2885 -0.0512 -0.0123 0.0447  298  ASN B CA  
11178 C C   . ASN B 300  ? 0.3992 0.3132 0.2538 -0.0531 -0.0093 0.0455  298  ASN B C   
11179 O O   . ASN B 300  ? 0.4187 0.3292 0.2668 -0.0556 -0.0090 0.0485  298  ASN B O   
11180 C CB  . ASN B 300  ? 0.4006 0.3055 0.2575 -0.0470 -0.0156 0.0440  298  ASN B CB  
11181 C CG  . ASN B 300  ? 0.4574 0.3552 0.3158 -0.0455 -0.0186 0.0442  298  ASN B CG  
11182 O OD1 . ASN B 300  ? 0.5800 0.4735 0.4378 -0.0481 -0.0186 0.0457  298  ASN B OD1 
11183 N ND2 . ASN B 300  ? 0.5750 0.4714 0.4353 -0.0414 -0.0212 0.0427  298  ASN B ND2 
11184 N N   . TYR B 301  ? 0.3663 0.2886 0.2250 -0.0520 -0.0071 0.0430  299  TYR B N   
11185 C CA  . TYR B 301  ? 0.3751 0.3031 0.2310 -0.0536 -0.0038 0.0436  299  TYR B CA  
11186 C C   . TYR B 301  ? 0.3536 0.2866 0.2123 -0.0575 -0.0006 0.0442  299  TYR B C   
11187 O O   . TYR B 301  ? 0.3752 0.3134 0.2320 -0.0592 0.0025  0.0449  299  TYR B O   
11188 C CB  . TYR B 301  ? 0.3552 0.2894 0.2137 -0.0503 -0.0031 0.0405  299  TYR B CB  
11189 C CG  . TYR B 301  ? 0.3522 0.2828 0.2070 -0.0469 -0.0058 0.0400  299  TYR B CG  
11190 C CD1 . TYR B 301  ? 0.3664 0.2943 0.2134 -0.0476 -0.0059 0.0420  299  TYR B CD1 
11191 C CD2 . TYR B 301  ? 0.3566 0.2868 0.2157 -0.0432 -0.0082 0.0375  299  TYR B CD2 
11192 C CE1 . TYR B 301  ? 0.3824 0.3072 0.2260 -0.0446 -0.0086 0.0416  299  TYR B CE1 
11193 C CE2 . TYR B 301  ? 0.3673 0.2947 0.2234 -0.0403 -0.0108 0.0370  299  TYR B CE2 
11194 C CZ  . TYR B 301  ? 0.3673 0.2919 0.2156 -0.0411 -0.0111 0.0391  299  TYR B CZ  
11195 O OH  . TYR B 301  ? 0.3784 0.3003 0.2236 -0.0383 -0.0139 0.0387  299  TYR B OH  
11196 N N   . ASP B 302  ? 0.3478 0.2794 0.2109 -0.0589 -0.0011 0.0441  300  ASP B N   
11197 C CA  . ASP B 302  ? 0.3967 0.3335 0.2636 -0.0624 0.0016  0.0444  300  ASP B CA  
11198 C C   . ASP B 302  ? 0.3515 0.2984 0.2228 -0.0614 0.0047  0.0421  300  ASP B C   
11199 O O   . ASP B 302  ? 0.3786 0.3309 0.2493 -0.0641 0.0078  0.0432  300  ASP B O   
11200 C CB  . ASP B 302  ? 0.3895 0.3237 0.2513 -0.0673 0.0029  0.0481  300  ASP B CB  
11201 C CG  . ASP B 302  ? 0.3968 0.3337 0.2630 -0.0711 0.0043  0.0486  300  ASP B CG  
11202 O OD1 . ASP B 302  ? 0.4370 0.3736 0.3086 -0.0700 0.0030  0.0466  300  ASP B OD1 
11203 O OD2 . ASP B 302  ? 0.4839 0.4235 0.3484 -0.0751 0.0068  0.0509  300  ASP B OD2 
11204 N N   . ILE B 303  ? 0.3184 0.2677 0.1942 -0.0575 0.0037  0.0390  301  ILE B N   
11205 C CA  . ILE B 303  ? 0.3253 0.2837 0.2063 -0.0562 0.0062  0.0365  301  ILE B CA  
11206 C C   . ILE B 303  ? 0.3393 0.2995 0.2275 -0.0556 0.0056  0.0344  301  ILE B C   
11207 O O   . ILE B 303  ? 0.3330 0.2873 0.2221 -0.0552 0.0029  0.0344  301  ILE B O   
11208 C CB  . ILE B 303  ? 0.2915 0.2518 0.1713 -0.0521 0.0060  0.0343  301  ILE B CB  
11209 C CG1 . ILE B 303  ? 0.3374 0.2937 0.2196 -0.0485 0.0027  0.0323  301  ILE B CG1 
11210 C CG2 . ILE B 303  ? 0.3261 0.2837 0.1981 -0.0526 0.0063  0.0363  301  ILE B CG2 
11211 C CD1 . ILE B 303  ? 0.3495 0.3087 0.2322 -0.0446 0.0024  0.0298  301  ILE B CD1 
11212 N N   . GLY B 304  ? 0.2932 0.2616 0.1866 -0.0553 0.0080  0.0327  302  GLY B N   
11213 C CA  . GLY B 304  ? 0.2751 0.2459 0.1753 -0.0544 0.0075  0.0305  302  GLY B CA  
11214 C C   . GLY B 304  ? 0.2967 0.2669 0.1993 -0.0497 0.0056  0.0277  302  GLY B C   
11215 O O   . GLY B 304  ? 0.3224 0.2944 0.2232 -0.0472 0.0060  0.0266  302  GLY B O   
11216 N N   . LEU B 305  ? 0.2704 0.2381 0.1769 -0.0487 0.0036  0.0264  303  LEU B N   
11217 C CA  . LEU B 305  ? 0.2951 0.2630 0.2049 -0.0446 0.0021  0.0237  303  LEU B CA  
11218 C C   . LEU B 305  ? 0.2837 0.2557 0.2001 -0.0447 0.0027  0.0220  303  LEU B C   
11219 O O   . LEU B 305  ? 0.2853 0.2541 0.2030 -0.0465 0.0017  0.0226  303  LEU B O   
11220 C CB  . LEU B 305  ? 0.2944 0.2543 0.2020 -0.0429 -0.0012 0.0239  303  LEU B CB  
11221 C CG  . LEU B 305  ? 0.2948 0.2550 0.2059 -0.0387 -0.0028 0.0212  303  LEU B CG  
11222 C CD1 . LEU B 305  ? 0.3724 0.3269 0.2796 -0.0365 -0.0054 0.0217  303  LEU B CD1 
11223 C CD2 . LEU B 305  ? 0.3522 0.3114 0.2683 -0.0383 -0.0038 0.0200  303  LEU B CD2 
11224 N N   . ASN B 306  ? 0.2633 0.2419 0.1835 -0.0428 0.0042  0.0198  304  ASN B N   
11225 C CA  . ASN B 306  ? 0.2574 0.2410 0.1838 -0.0429 0.0051  0.0183  304  ASN B CA  
11226 C C   . ASN B 306  ? 0.2598 0.2431 0.1899 -0.0392 0.0035  0.0157  304  ASN B C   
11227 O O   . ASN B 306  ? 0.2655 0.2492 0.1948 -0.0362 0.0032  0.0144  304  ASN B O   
11228 C CB  . ASN B 306  ? 0.2853 0.2774 0.2138 -0.0434 0.0082  0.0179  304  ASN B CB  
11229 C CG  . ASN B 306  ? 0.2936 0.2911 0.2286 -0.0430 0.0089  0.0162  304  ASN B CG  
11230 O OD1 . ASN B 306  ? 0.3079 0.3064 0.2451 -0.0458 0.0091  0.0170  304  ASN B OD1 
11231 N ND2 . ASN B 306  ? 0.2727 0.2733 0.2106 -0.0395 0.0090  0.0138  304  ASN B ND2 
11232 N N   . ILE B 307  ? 0.2628 0.2453 0.1967 -0.0394 0.0025  0.0149  305  ILE B N   
11233 C CA  . ILE B 307  ? 0.2591 0.2418 0.1970 -0.0362 0.0013  0.0124  305  ILE B CA  
11234 C C   . ILE B 307  ? 0.2592 0.2496 0.2020 -0.0357 0.0033  0.0109  305  ILE B C   
11235 O O   . ILE B 307  ? 0.2427 0.2358 0.1882 -0.0380 0.0041  0.0112  305  ILE B O   
11236 C CB  . ILE B 307  ? 0.2623 0.2395 0.2012 -0.0364 -0.0008 0.0124  305  ILE B CB  
11237 C CG1 . ILE B 307  ? 0.2880 0.2574 0.2221 -0.0363 -0.0028 0.0139  305  ILE B CG1 
11238 C CG2 . ILE B 307  ? 0.2720 0.2505 0.2154 -0.0333 -0.0016 0.0099  305  ILE B CG2 
11239 C CD1 . ILE B 307  ? 0.3298 0.2935 0.2645 -0.0366 -0.0047 0.0139  305  ILE B CD1 
11240 N N   . ASP B 308  ? 0.2556 0.2495 0.1995 -0.0329 0.0039  0.0092  306  ASP B N   
11241 C CA  . ASP B 308  ? 0.2480 0.2488 0.1965 -0.0319 0.0057  0.0076  306  ASP B CA  
11242 C C   . ASP B 308  ? 0.2381 0.2387 0.1912 -0.0310 0.0045  0.0062  306  ASP B C   
11243 O O   . ASP B 308  ? 0.2664 0.2618 0.2192 -0.0299 0.0024  0.0058  306  ASP B O   
11244 C CB  . ASP B 308  ? 0.2456 0.2487 0.1937 -0.0288 0.0063  0.0060  306  ASP B CB  
11245 C CG  . ASP B 308  ? 0.2928 0.2977 0.2368 -0.0295 0.0080  0.0071  306  ASP B CG  
11246 O OD1 . ASP B 308  ? 0.2675 0.2730 0.2095 -0.0325 0.0092  0.0091  306  ASP B OD1 
11247 O OD2 . ASP B 308  ? 0.2993 0.3048 0.2416 -0.0270 0.0082  0.0060  306  ASP B OD2 
11248 N N   . ALA B 309  ? 0.2120 0.2184 0.1692 -0.0315 0.0058  0.0055  307  ALA B N   
11249 C CA  . ALA B 309  ? 0.2047 0.2113 0.1661 -0.0308 0.0049  0.0041  307  ALA B CA  
11250 C C   . ALA B 309  ? 0.2205 0.2301 0.1848 -0.0272 0.0051  0.0019  307  ALA B C   
11251 O O   . ALA B 309  ? 0.2361 0.2503 0.2008 -0.0261 0.0067  0.0014  307  ALA B O   
11252 C CB  . ALA B 309  ? 0.2284 0.2396 0.1927 -0.0335 0.0060  0.0047  307  ALA B CB  
11253 N N   . GLU B 310  ? 0.2122 0.2189 0.1783 -0.0254 0.0034  0.0007  308  GLU B N   
11254 C CA  . GLU B 310  ? 0.2264 0.2348 0.1948 -0.0221 0.0033  -0.0013 308  GLU B CA  
11255 C C   . GLU B 310  ? 0.1974 0.2083 0.1703 -0.0217 0.0032  -0.0025 308  GLU B C   
11256 O O   . GLU B 310  ? 0.2029 0.2177 0.1777 -0.0235 0.0043  -0.0021 308  GLU B O   
11257 C CB  . GLU B 310  ? 0.2190 0.2220 0.1852 -0.0201 0.0015  -0.0017 308  GLU B CB  
11258 C CG  . GLU B 310  ? 0.2594 0.2602 0.2209 -0.0206 0.0015  -0.0005 308  GLU B CG  
11259 C CD  . GLU B 310  ? 0.2727 0.2687 0.2322 -0.0186 -0.0004 -0.0009 308  GLU B CD  
11260 O OE1 . GLU B 310  ? 0.2901 0.2876 0.2507 -0.0162 -0.0005 -0.0023 308  GLU B OE1 
11261 O OE2 . GLU B 310  ? 0.2631 0.2542 0.2201 -0.0194 -0.0019 0.0004  308  GLU B OE2 
11262 N N   . GLU B 311  ? 0.2036 0.2125 0.1781 -0.0193 0.0020  -0.0039 309  GLU B N   
11263 C CA  . GLU B 311  ? 0.1918 0.2031 0.1703 -0.0187 0.0020  -0.0051 309  GLU B CA  
11264 C C   . GLU B 311  ? 0.2037 0.2131 0.1826 -0.0210 0.0013  -0.0043 309  GLU B C   
11265 O O   . GLU B 311  ? 0.2172 0.2219 0.1933 -0.0226 0.0004  -0.0032 309  GLU B O   
11266 C CB  . GLU B 311  ? 0.2140 0.2233 0.1939 -0.0158 0.0009  -0.0066 309  GLU B CB  
11267 C CG  . GLU B 311  ? 0.2483 0.2595 0.2282 -0.0133 0.0014  -0.0076 309  GLU B CG  
11268 C CD  . GLU B 311  ? 0.2858 0.2933 0.2621 -0.0127 0.0006  -0.0071 309  GLU B CD  
11269 O OE1 . GLU B 311  ? 0.2485 0.2524 0.2219 -0.0143 -0.0001 -0.0058 309  GLU B OE1 
11270 O OE2 . GLU B 311  ? 0.3593 0.3674 0.3353 -0.0107 0.0006  -0.0081 309  GLU B OE2 
11271 N N   . ALA B 312  ? 0.2007 0.2136 0.1829 -0.0213 0.0016  -0.0050 310  ALA B N   
11272 C CA  . ALA B 312  ? 0.2098 0.2212 0.1923 -0.0238 0.0010  -0.0044 310  ALA B CA  
11273 C C   . ALA B 312  ? 0.2026 0.2072 0.1835 -0.0233 -0.0007 -0.0047 310  ALA B C   
11274 O O   . ALA B 312  ? 0.2067 0.2078 0.1858 -0.0256 -0.0015 -0.0038 310  ALA B O   
11275 C CB  . ALA B 312  ? 0.2256 0.2419 0.2120 -0.0238 0.0014  -0.0053 310  ALA B CB  
11276 N N   . ASP B 313  ? 0.2061 0.2088 0.1876 -0.0204 -0.0014 -0.0059 311  ASP B N   
11277 C CA  . ASP B 313  ? 0.2076 0.2044 0.1879 -0.0196 -0.0028 -0.0062 311  ASP B CA  
11278 C C   . ASP B 313  ? 0.2353 0.2271 0.2121 -0.0199 -0.0037 -0.0051 311  ASP B C   
11279 O O   . ASP B 313  ? 0.2420 0.2287 0.2177 -0.0190 -0.0049 -0.0052 311  ASP B O   
11280 C CB  . ASP B 313  ? 0.2433 0.2402 0.2260 -0.0165 -0.0032 -0.0078 311  ASP B CB  
11281 C CG  . ASP B 313  ? 0.2599 0.2579 0.2427 -0.0142 -0.0031 -0.0082 311  ASP B CG  
11282 O OD1 . ASP B 313  ? 0.2590 0.2574 0.2398 -0.0148 -0.0027 -0.0073 311  ASP B OD1 
11283 O OD2 . ASP B 313  ? 0.2870 0.2853 0.2718 -0.0119 -0.0033 -0.0094 311  ASP B OD2 
11284 N N   . ARG B 314  ? 0.2105 0.2035 0.1852 -0.0211 -0.0030 -0.0039 312  ARG B N   
11285 C CA  . ARG B 314  ? 0.2200 0.2082 0.1909 -0.0218 -0.0038 -0.0025 312  ARG B CA  
11286 C C   . ARG B 314  ? 0.2142 0.2010 0.1827 -0.0253 -0.0036 -0.0008 312  ARG B C   
11287 O O   . ARG B 314  ? 0.2357 0.2178 0.2006 -0.0262 -0.0043 0.0005  312  ARG B O   
11288 C CB  . ARG B 314  ? 0.2297 0.2193 0.1992 -0.0204 -0.0034 -0.0023 312  ARG B CB  
11289 C CG  . ARG B 314  ? 0.2200 0.2088 0.1909 -0.0172 -0.0043 -0.0037 312  ARG B CG  
11290 C CD  . ARG B 314  ? 0.2602 0.2516 0.2305 -0.0158 -0.0037 -0.0040 312  ARG B CD  
11291 N NE  . ARG B 314  ? 0.2340 0.2232 0.2046 -0.0132 -0.0050 -0.0048 312  ARG B NE  
11292 C CZ  . ARG B 314  ? 0.2324 0.2233 0.2029 -0.0115 -0.0050 -0.0055 312  ARG B CZ  
11293 N NH1 . ARG B 314  ? 0.2486 0.2436 0.2187 -0.0118 -0.0035 -0.0057 312  ARG B NH1 
11294 N NH2 . ARG B 314  ? 0.2589 0.2474 0.2296 -0.0095 -0.0065 -0.0060 312  ARG B NH2 
11295 N N   . LEU B 315  ? 0.2122 0.2031 0.1826 -0.0274 -0.0026 -0.0008 313  LEU B N   
11296 C CA  . LEU B 315  ? 0.2274 0.2178 0.1958 -0.0312 -0.0023 0.0009  313  LEU B CA  
11297 C C   . LEU B 315  ? 0.2381 0.2210 0.2036 -0.0325 -0.0038 0.0016  313  LEU B C   
11298 O O   . LEU B 315  ? 0.2419 0.2209 0.2038 -0.0340 -0.0042 0.0033  313  LEU B O   
11299 C CB  . LEU B 315  ? 0.2201 0.2163 0.1918 -0.0330 -0.0013 0.0007  313  LEU B CB  
11300 C CG  . LEU B 315  ? 0.2460 0.2447 0.2168 -0.0368 -0.0003 0.0025  313  LEU B CG  
11301 C CD1 . LEU B 315  ? 0.2449 0.2502 0.2198 -0.0380 0.0005  0.0020  313  LEU B CD1 
11302 C CD2 . LEU B 315  ? 0.2957 0.2881 0.2630 -0.0398 -0.0015 0.0039  313  LEU B CD2 
11303 N N   . GLU B 316  ? 0.2344 0.2150 0.2012 -0.0319 -0.0048 0.0005  314  GLU B N   
11304 C CA  . GLU B 316  ? 0.2492 0.2227 0.2132 -0.0333 -0.0061 0.0011  314  GLU B CA  
11305 C C   . GLU B 316  ? 0.2477 0.2151 0.2088 -0.0312 -0.0073 0.0014  314  GLU B C   
11306 O O   . GLU B 316  ? 0.2652 0.2269 0.2228 -0.0328 -0.0082 0.0028  314  GLU B O   
11307 C CB  . GLU B 316  ? 0.2441 0.2167 0.2098 -0.0330 -0.0067 -0.0004 314  GLU B CB  
11308 C CG  . GLU B 316  ? 0.2533 0.2314 0.2213 -0.0357 -0.0059 -0.0004 314  GLU B CG  
11309 C CD  . GLU B 316  ? 0.2898 0.2671 0.2593 -0.0359 -0.0066 -0.0017 314  GLU B CD  
11310 O OE1 . GLU B 316  ? 0.2744 0.2450 0.2415 -0.0358 -0.0078 -0.0021 314  GLU B OE1 
11311 O OE2 . GLU B 316  ? 0.2738 0.2570 0.2465 -0.0361 -0.0060 -0.0025 314  GLU B OE2 
11312 N N   . LEU B 317  ? 0.2545 0.2232 0.2172 -0.0277 -0.0074 0.0004  315  LEU B N   
11313 C CA  . LEU B 317  ? 0.2803 0.2441 0.2407 -0.0257 -0.0085 0.0009  315  LEU B CA  
11314 C C   . LEU B 317  ? 0.2885 0.2510 0.2452 -0.0275 -0.0084 0.0029  315  LEU B C   
11315 O O   . LEU B 317  ? 0.2820 0.2383 0.2353 -0.0278 -0.0096 0.0041  315  LEU B O   
11316 C CB  . LEU B 317  ? 0.2895 0.2563 0.2525 -0.0222 -0.0084 -0.0005 315  LEU B CB  
11317 C CG  . LEU B 317  ? 0.2948 0.2572 0.2559 -0.0200 -0.0098 0.0000  315  LEU B CG  
11318 C CD1 . LEU B 317  ? 0.3297 0.2854 0.2893 -0.0195 -0.0112 0.0002  315  LEU B CD1 
11319 C CD2 . LEU B 317  ? 0.3017 0.2672 0.2658 -0.0168 -0.0098 -0.0014 315  LEU B CD2 
11320 N N   . SER B 318  ? 0.2380 0.2060 0.1952 -0.0288 -0.0070 0.0034  316  SER B N   
11321 C CA  . SER B 318  ? 0.2409 0.2078 0.1943 -0.0306 -0.0067 0.0053  316  SER B CA  
11322 C C   . SER B 318  ? 0.2546 0.2169 0.2049 -0.0341 -0.0071 0.0071  316  SER B C   
11323 O O   . SER B 318  ? 0.2751 0.2334 0.2214 -0.0351 -0.0077 0.0089  316  SER B O   
11324 C CB  . SER B 318  ? 0.2562 0.2303 0.2108 -0.0313 -0.0048 0.0054  316  SER B CB  
11325 O OG  . SER B 318  ? 0.2592 0.2372 0.2156 -0.0341 -0.0036 0.0057  316  SER B OG  
11326 N N   . LEU B 319  ? 0.2494 0.2121 0.2013 -0.0360 -0.0070 0.0067  317  LEU B N   
11327 C CA  . LEU B 319  ? 0.2494 0.2074 0.1983 -0.0396 -0.0076 0.0082  317  LEU B CA  
11328 C C   . LEU B 319  ? 0.2802 0.2293 0.2256 -0.0385 -0.0095 0.0087  317  LEU B C   
11329 O O   . LEU B 319  ? 0.2905 0.2345 0.2321 -0.0410 -0.0101 0.0105  317  LEU B O   
11330 C CB  . LEU B 319  ? 0.2470 0.2069 0.1983 -0.0417 -0.0073 0.0074  317  LEU B CB  
11331 C CG  . LEU B 319  ? 0.2743 0.2431 0.2293 -0.0430 -0.0056 0.0072  317  LEU B CG  
11332 C CD1 . LEU B 319  ? 0.2773 0.2473 0.2347 -0.0446 -0.0059 0.0061  317  LEU B CD1 
11333 C CD2 . LEU B 319  ? 0.3057 0.2770 0.2588 -0.0463 -0.0044 0.0093  317  LEU B CD2 
11334 N N   . ASP B 320  ? 0.2799 0.2270 0.2267 -0.0349 -0.0104 0.0071  318  ASP B N   
11335 C CA  . ASP B 320  ? 0.3073 0.2463 0.2512 -0.0335 -0.0121 0.0076  318  ASP B CA  
11336 C C   . ASP B 320  ? 0.2981 0.2345 0.2385 -0.0330 -0.0127 0.0094  318  ASP B C   
11337 O O   . ASP B 320  ? 0.3362 0.2656 0.2729 -0.0334 -0.0140 0.0107  318  ASP B O   
11338 C CB  . ASP B 320  ? 0.3165 0.2547 0.2631 -0.0296 -0.0128 0.0056  318  ASP B CB  
11339 C CG  . ASP B 320  ? 0.2844 0.2222 0.2328 -0.0302 -0.0127 0.0041  318  ASP B CG  
11340 O OD1 . ASP B 320  ? 0.3401 0.2725 0.2857 -0.0324 -0.0134 0.0047  318  ASP B OD1 
11341 O OD2 . ASP B 320  ? 0.3240 0.2667 0.2762 -0.0285 -0.0120 0.0023  318  ASP B OD2 
11342 N N   . LEU B 321  ? 0.2601 0.2019 0.2015 -0.0321 -0.0118 0.0094  319  LEU B N   
11343 C CA  . LEU B 321  ? 0.3010 0.2407 0.2386 -0.0320 -0.0123 0.0112  319  LEU B CA  
11344 C C   . LEU B 321  ? 0.2936 0.2324 0.2277 -0.0362 -0.0115 0.0134  319  LEU B C   
11345 O O   . LEU B 321  ? 0.3247 0.2577 0.2544 -0.0371 -0.0125 0.0154  319  LEU B O   
11346 C CB  . LEU B 321  ? 0.2966 0.2421 0.2360 -0.0299 -0.0115 0.0105  319  LEU B CB  
11347 C CG  . LEU B 321  ? 0.2960 0.2411 0.2378 -0.0258 -0.0127 0.0089  319  LEU B CG  
11348 C CD1 . LEU B 321  ? 0.3331 0.2827 0.2799 -0.0245 -0.0119 0.0066  319  LEU B CD1 
11349 C CD2 . LEU B 321  ? 0.3543 0.3017 0.2952 -0.0240 -0.0129 0.0091  319  LEU B CD2 
11350 N N   . LEU B 322  ? 0.2844 0.2288 0.2205 -0.0388 -0.0098 0.0133  320  LEU B N   
11351 C CA  . LEU B 322  ? 0.2833 0.2276 0.2166 -0.0430 -0.0089 0.0155  320  LEU B CA  
11352 C C   . LEU B 322  ? 0.2879 0.2242 0.2179 -0.0452 -0.0103 0.0168  320  LEU B C   
11353 O O   . LEU B 322  ? 0.3086 0.2410 0.2342 -0.0476 -0.0106 0.0191  320  LEU B O   
11354 C CB  . LEU B 322  ? 0.2746 0.2265 0.2115 -0.0452 -0.0070 0.0149  320  LEU B CB  
11355 C CG  . LEU B 322  ? 0.2913 0.2442 0.2259 -0.0499 -0.0058 0.0172  320  LEU B CG  
11356 C CD1 . LEU B 322  ? 0.2975 0.2518 0.2290 -0.0499 -0.0049 0.0188  320  LEU B CD1 
11357 C CD2 . LEU B 322  ? 0.3066 0.2671 0.2455 -0.0520 -0.0042 0.0166  320  LEU B CD2 
11358 N N   . GLU B 323  ? 0.2974 0.2307 0.2290 -0.0444 -0.0113 0.0153  321  GLU B N   
11359 C CA  . GLU B 323  ? 0.3262 0.2513 0.2546 -0.0463 -0.0127 0.0162  321  GLU B CA  
11360 C C   . GLU B 323  ? 0.3560 0.2735 0.2799 -0.0447 -0.0143 0.0176  321  GLU B C   
11361 O O   . GLU B 323  ? 0.3543 0.2662 0.2738 -0.0475 -0.0149 0.0198  321  GLU B O   
11362 C CB  . GLU B 323  ? 0.3729 0.2963 0.3039 -0.0448 -0.0135 0.0140  321  GLU B CB  
11363 C CG  . GLU B 323  ? 0.4206 0.3343 0.3479 -0.0457 -0.0152 0.0145  321  GLU B CG  
11364 C CD  . GLU B 323  ? 0.4563 0.3691 0.3829 -0.0502 -0.0150 0.0149  321  GLU B CD  
11365 O OE1 . GLU B 323  ? 0.4161 0.3362 0.3459 -0.0522 -0.0136 0.0144  321  GLU B OE1 
11366 O OE2 . GLU B 323  ? 0.4228 0.3273 0.3456 -0.0518 -0.0163 0.0156  321  GLU B OE2 
11367 N N   . VAL B 324  ? 0.3143 0.2316 0.2393 -0.0404 -0.0151 0.0166  322  VAL B N   
11368 C CA  . VAL B 324  ? 0.3392 0.2496 0.2604 -0.0386 -0.0169 0.0179  322  VAL B CA  
11369 C C   . VAL B 324  ? 0.3046 0.2149 0.2218 -0.0406 -0.0165 0.0204  322  VAL B C   
11370 O O   . VAL B 324  ? 0.3459 0.2491 0.2583 -0.0418 -0.0177 0.0225  322  VAL B O   
11371 C CB  . VAL B 324  ? 0.3333 0.2447 0.2572 -0.0336 -0.0177 0.0163  322  VAL B CB  
11372 C CG1 . VAL B 324  ? 0.3831 0.2883 0.3033 -0.0316 -0.0196 0.0178  322  VAL B CG1 
11373 C CG2 . VAL B 324  ? 0.3792 0.2898 0.3064 -0.0316 -0.0180 0.0140  322  VAL B CG2 
11374 N N   . LEU B 325  ? 0.2995 0.2175 0.2183 -0.0411 -0.0148 0.0203  323  LEU B N   
11375 C CA  . LEU B 325  ? 0.3326 0.2509 0.2474 -0.0428 -0.0143 0.0226  323  LEU B CA  
11376 C C   . LEU B 325  ? 0.3400 0.2553 0.2514 -0.0476 -0.0138 0.0249  323  LEU B C   
11377 O O   . LEU B 325  ? 0.3357 0.2462 0.2419 -0.0490 -0.0144 0.0273  323  LEU B O   
11378 C CB  . LEU B 325  ? 0.3209 0.2481 0.2382 -0.0423 -0.0124 0.0218  323  LEU B CB  
11379 C CG  . LEU B 325  ? 0.3174 0.2470 0.2374 -0.0377 -0.0131 0.0198  323  LEU B CG  
11380 C CD1 . LEU B 325  ? 0.3694 0.3079 0.2926 -0.0373 -0.0110 0.0185  323  LEU B CD1 
11381 C CD2 . LEU B 325  ? 0.3500 0.2749 0.2660 -0.0358 -0.0148 0.0211  323  LEU B CD2 
11382 N N   . CYS B 326  ? 0.3243 0.2422 0.2381 -0.0504 -0.0127 0.0243  324  CYS B N   
11383 C CA  . CYS B 326  ? 0.3126 0.2283 0.2236 -0.0553 -0.0122 0.0264  324  CYS B CA  
11384 C C   . CYS B 326  ? 0.3479 0.2530 0.2546 -0.0562 -0.0143 0.0277  324  CYS B C   
11385 O O   . CYS B 326  ? 0.3433 0.2446 0.2460 -0.0601 -0.0143 0.0301  324  CYS B O   
11386 C CB  . CYS B 326  ? 0.3305 0.2522 0.2457 -0.0580 -0.0108 0.0254  324  CYS B CB  
11387 S SG  . CYS B 326  ? 0.3581 0.2920 0.2773 -0.0580 -0.0079 0.0247  324  CYS B SG  
11388 N N   . LEU B 327  ? 0.3371 0.2373 0.2445 -0.0527 -0.0161 0.0262  325  LEU B N   
11389 C CA  . LEU B 327  ? 0.3816 0.2713 0.2849 -0.0528 -0.0181 0.0271  325  LEU B CA  
11390 C C   . LEU B 327  ? 0.4120 0.2962 0.3116 -0.0499 -0.0197 0.0284  325  LEU B C   
11391 O O   . LEU B 327  ? 0.4265 0.3017 0.3226 -0.0495 -0.0216 0.0293  325  LEU B O   
11392 C CB  . LEU B 327  ? 0.3578 0.2450 0.2639 -0.0507 -0.0190 0.0246  325  LEU B CB  
11393 C CG  . LEU B 327  ? 0.4300 0.3213 0.3392 -0.0537 -0.0179 0.0233  325  LEU B CG  
11394 C CD1 . LEU B 327  ? 0.4914 0.3802 0.4030 -0.0512 -0.0188 0.0207  325  LEU B CD1 
11395 C CD2 . LEU B 327  ? 0.4517 0.3389 0.3572 -0.0590 -0.0180 0.0255  325  LEU B CD2 
11396 N N   . ASP B 328  ? 0.3410 0.2302 0.2412 -0.0479 -0.0192 0.0286  326  ASP B N   
11397 C CA  . ASP B 328  ? 0.3683 0.2531 0.2654 -0.0449 -0.0209 0.0297  326  ASP B CA  
11398 C C   . ASP B 328  ? 0.3981 0.2785 0.2890 -0.0482 -0.0211 0.0330  326  ASP B C   
11399 O O   . ASP B 328  ? 0.4140 0.2996 0.3040 -0.0506 -0.0194 0.0342  326  ASP B O   
11400 C CB  . ASP B 328  ? 0.3668 0.2590 0.2670 -0.0418 -0.0203 0.0284  326  ASP B CB  
11401 C CG  . ASP B 328  ? 0.4657 0.3540 0.3634 -0.0383 -0.0223 0.0292  326  ASP B CG  
11402 O OD1 . ASP B 328  ? 0.4467 0.3276 0.3393 -0.0390 -0.0238 0.0315  326  ASP B OD1 
11403 O OD2 . ASP B 328  ? 0.4760 0.3689 0.3768 -0.0350 -0.0225 0.0276  326  ASP B OD2 
11404 N N   . GLY B 329  ? 0.4162 0.2869 0.3027 -0.0481 -0.0231 0.0347  327  GLY B N   
11405 C CA  . GLY B 329  ? 0.4056 0.2712 0.2859 -0.0513 -0.0234 0.0380  327  GLY B CA  
11406 C C   . GLY B 329  ? 0.4185 0.2864 0.2960 -0.0503 -0.0234 0.0395  327  GLY B C   
11407 O O   . GLY B 329  ? 0.4380 0.3042 0.3108 -0.0535 -0.0228 0.0422  327  GLY B O   
11408 N N   . ASP B 330  ? 0.4105 0.2823 0.2909 -0.0459 -0.0239 0.0379  328  ASP B N   
11409 C CA  . ASP B 330  ? 0.3854 0.2602 0.2633 -0.0451 -0.0238 0.0390  328  ASP B CA  
11410 C C   . ASP B 330  ? 0.4668 0.3495 0.3451 -0.0483 -0.0209 0.0393  328  ASP B C   
11411 O O   . ASP B 330  ? 0.4719 0.3558 0.3464 -0.0490 -0.0205 0.0410  328  ASP B O   
11412 C CB  . ASP B 330  ? 0.4293 0.3073 0.3107 -0.0400 -0.0250 0.0369  328  ASP B CB  
11413 C CG  . ASP B 330  ? 0.5151 0.3856 0.3955 -0.0364 -0.0279 0.0372  328  ASP B CG  
11414 O OD1 . ASP B 330  ? 0.5300 0.3922 0.4054 -0.0376 -0.0293 0.0395  328  ASP B OD1 
11415 O OD2 . ASP B 330  ? 0.4994 0.3722 0.3841 -0.0324 -0.0288 0.0350  328  ASP B OD2 
11416 N N   . LEU B 331  ? 0.3799 0.2680 0.2625 -0.0502 -0.0190 0.0377  329  LEU B N   
11417 C CA  . LEU B 331  ? 0.3699 0.2659 0.2535 -0.0532 -0.0161 0.0379  329  LEU B CA  
11418 C C   . LEU B 331  ? 0.3432 0.2372 0.2243 -0.0585 -0.0150 0.0401  329  LEU B C   
11419 O O   . LEU B 331  ? 0.3989 0.2998 0.2822 -0.0613 -0.0125 0.0400  329  LEU B O   
11420 C CB  . LEU B 331  ? 0.3652 0.2697 0.2558 -0.0517 -0.0146 0.0348  329  LEU B CB  
11421 C CG  . LEU B 331  ? 0.3700 0.2766 0.2633 -0.0466 -0.0157 0.0325  329  LEU B CG  
11422 C CD1 . LEU B 331  ? 0.3741 0.2882 0.2742 -0.0452 -0.0144 0.0295  329  LEU B CD1 
11423 C CD2 . LEU B 331  ? 0.3510 0.2598 0.2411 -0.0456 -0.0155 0.0335  329  LEU B CD2 
11424 N N   . SER B 332  ? 0.4119 0.2966 0.2885 -0.0599 -0.0168 0.0422  330  SER B N   
11425 C CA  . SER B 332  ? 0.4084 0.2898 0.2825 -0.0651 -0.0161 0.0443  330  SER B CA  
11426 C C   . SER B 332  ? 0.4110 0.2984 0.2834 -0.0690 -0.0134 0.0462  330  SER B C   
11427 O O   . SER B 332  ? 0.4399 0.3280 0.3087 -0.0684 -0.0131 0.0477  330  SER B O   
11428 C CB  . SER B 332  ? 0.4631 0.3330 0.3311 -0.0655 -0.0186 0.0467  330  SER B CB  
11429 O OG  . SER B 332  ? 0.5286 0.3945 0.3939 -0.0706 -0.0181 0.0488  330  SER B OG  
11430 N N   . GLY B 333  ? 0.4078 0.2995 0.2829 -0.0729 -0.0116 0.0462  331  GLY B N   
11431 C CA  . GLY B 333  ? 0.4156 0.3130 0.2896 -0.0771 -0.0089 0.0483  331  GLY B CA  
11432 C C   . GLY B 333  ? 0.3981 0.3059 0.2751 -0.0755 -0.0064 0.0470  331  GLY B C   
11433 O O   . GLY B 333  ? 0.4236 0.3367 0.2996 -0.0787 -0.0040 0.0486  331  GLY B O   
11434 N N   . TRP B 334  ? 0.4021 0.3131 0.2825 -0.0707 -0.0070 0.0441  332  TRP B N   
11435 C CA  . TRP B 334  ? 0.3641 0.2844 0.2472 -0.0689 -0.0048 0.0427  332  TRP B CA  
11436 C C   . TRP B 334  ? 0.3519 0.2806 0.2417 -0.0701 -0.0028 0.0408  332  TRP B C   
11437 O O   . TRP B 334  ? 0.3699 0.2983 0.2640 -0.0686 -0.0039 0.0386  332  TRP B O   
11438 C CB  . TRP B 334  ? 0.4005 0.3201 0.2845 -0.0634 -0.0065 0.0405  332  TRP B CB  
11439 C CG  . TRP B 334  ? 0.3802 0.3084 0.2670 -0.0610 -0.0046 0.0386  332  TRP B CG  
11440 C CD1 . TRP B 334  ? 0.3943 0.3274 0.2787 -0.0619 -0.0024 0.0396  332  TRP B CD1 
11441 C CD2 . TRP B 334  ? 0.3463 0.2788 0.2386 -0.0571 -0.0049 0.0353  332  TRP B CD2 
11442 N NE1 . TRP B 334  ? 0.3293 0.2693 0.2173 -0.0587 -0.0013 0.0370  332  TRP B NE1 
11443 C CE2 . TRP B 334  ? 0.3230 0.2627 0.2159 -0.0558 -0.0029 0.0344  332  TRP B CE2 
11444 C CE3 . TRP B 334  ? 0.3306 0.2614 0.2271 -0.0546 -0.0066 0.0331  332  TRP B CE3 
11445 C CZ2 . TRP B 334  ? 0.3237 0.2685 0.2213 -0.0522 -0.0027 0.0314  332  TRP B CZ2 
11446 C CZ3 . TRP B 334  ? 0.3922 0.3285 0.2935 -0.0511 -0.0063 0.0302  332  TRP B CZ3 
11447 C CH2 . TRP B 334  ? 0.3440 0.2871 0.2457 -0.0500 -0.0044 0.0294  332  TRP B CH2 
11448 N N   . ASN B 335  ? 0.3438 0.2799 0.2344 -0.0727 0.0001  0.0416  333  ASN B N   
11449 C CA  . ASN B 335  ? 0.3310 0.2757 0.2279 -0.0739 0.0021  0.0401  333  ASN B CA  
11450 C C   . ASN B 335  ? 0.3134 0.2665 0.2141 -0.0703 0.0037  0.0377  333  ASN B C   
11451 O O   . ASN B 335  ? 0.3558 0.3172 0.2613 -0.0711 0.0058  0.0367  333  ASN B O   
11452 C CB  . ASN B 335  ? 0.3406 0.2887 0.2368 -0.0793 0.0043  0.0427  333  ASN B CB  
11453 C CG  . ASN B 335  ? 0.4247 0.3650 0.3183 -0.0833 0.0026  0.0447  333  ASN B CG  
11454 O OD1 . ASN B 335  ? 0.3693 0.3038 0.2639 -0.0821 0.0002  0.0434  333  ASN B OD1 
11455 N ND2 . ASN B 335  ? 0.4244 0.3643 0.3147 -0.0880 0.0039  0.0478  333  ASN B ND2 
11456 N N   . GLY B 336  ? 0.3356 0.2865 0.2341 -0.0663 0.0026  0.0367  334  GLY B N   
11457 C CA  . GLY B 336  ? 0.3475 0.3054 0.2487 -0.0628 0.0040  0.0345  334  GLY B CA  
11458 C C   . GLY B 336  ? 0.3061 0.2654 0.2126 -0.0591 0.0027  0.0313  334  GLY B C   
11459 O O   . GLY B 336  ? 0.2991 0.2635 0.2077 -0.0560 0.0036  0.0293  334  GLY B O   
11460 N N   . MET B 337  ? 0.3232 0.2781 0.2318 -0.0591 0.0008  0.0306  335  MET B N   
11461 C CA  . MET B 337  ? 0.3148 0.2717 0.2286 -0.0557 -0.0001 0.0276  335  MET B CA  
11462 C C   . MET B 337  ? 0.3067 0.2727 0.2260 -0.0564 0.0022  0.0262  335  MET B C   
11463 O O   . MET B 337  ? 0.2897 0.2577 0.2105 -0.0601 0.0031  0.0272  335  MET B O   
11464 C CB  . MET B 337  ? 0.3433 0.2934 0.2578 -0.0557 -0.0025 0.0272  335  MET B CB  
11465 C CG  . MET B 337  ? 0.3452 0.2969 0.2647 -0.0523 -0.0034 0.0242  335  MET B CG  
11466 S SD  . MET B 337  ? 0.4839 0.4326 0.4024 -0.0471 -0.0053 0.0229  335  MET B SD  
11467 C CE  . MET B 337  ? 0.4032 0.3616 0.3261 -0.0446 -0.0032 0.0205  335  MET B CE  
11468 N N   . GLY B 338  ? 0.2651 0.2365 0.1875 -0.0531 0.0030  0.0240  336  GLY B N   
11469 C CA  . GLY B 338  ? 0.3080 0.2882 0.2355 -0.0531 0.0052  0.0226  336  GLY B CA  
11470 C C   . GLY B 338  ? 0.2688 0.2502 0.2014 -0.0501 0.0041  0.0198  336  GLY B C   
11471 O O   . GLY B 338  ? 0.2648 0.2422 0.1969 -0.0469 0.0023  0.0186  336  GLY B O   
11472 N N   . PHE B 339  ? 0.2680 0.2551 0.2055 -0.0512 0.0052  0.0190  337  PHE B N   
11473 C CA  . PHE B 339  ? 0.2396 0.2279 0.1817 -0.0487 0.0042  0.0165  337  PHE B CA  
11474 C C   . PHE B 339  ? 0.2422 0.2394 0.1892 -0.0490 0.0063  0.0155  337  PHE B C   
11475 O O   . PHE B 339  ? 0.2618 0.2628 0.2100 -0.0524 0.0076  0.0169  337  PHE B O   
11476 C CB  . PHE B 339  ? 0.2745 0.2569 0.2167 -0.0503 0.0022  0.0167  337  PHE B CB  
11477 C CG  . PHE B 339  ? 0.2757 0.2574 0.2214 -0.0474 0.0009  0.0143  337  PHE B CG  
11478 C CD1 . PHE B 339  ? 0.2907 0.2674 0.2353 -0.0441 -0.0008 0.0132  337  PHE B CD1 
11479 C CD2 . PHE B 339  ? 0.2485 0.2350 0.1989 -0.0481 0.0014  0.0131  337  PHE B CD2 
11480 C CE1 . PHE B 339  ? 0.2904 0.2667 0.2384 -0.0415 -0.0019 0.0111  337  PHE B CE1 
11481 C CE2 . PHE B 339  ? 0.2871 0.2728 0.2405 -0.0456 0.0002  0.0110  337  PHE B CE2 
11482 C CZ  . PHE B 339  ? 0.2957 0.2765 0.2479 -0.0423 -0.0013 0.0100  337  PHE B CZ  
11483 N N   . VAL B 340  ? 0.2297 0.2306 0.1798 -0.0454 0.0066  0.0133  338  VAL B N   
11484 C CA  . VAL B 340  ? 0.2104 0.2197 0.1654 -0.0449 0.0085  0.0122  338  VAL B CA  
11485 C C   . VAL B 340  ? 0.2442 0.2540 0.2033 -0.0453 0.0074  0.0111  338  VAL B C   
11486 O O   . VAL B 340  ? 0.2441 0.2489 0.2033 -0.0436 0.0054  0.0099  338  VAL B O   
11487 C CB  . VAL B 340  ? 0.2479 0.2601 0.2037 -0.0408 0.0092  0.0103  338  VAL B CB  
11488 C CG1 . VAL B 340  ? 0.2504 0.2710 0.2112 -0.0400 0.0110  0.0091  338  VAL B CG1 
11489 C CG2 . VAL B 340  ? 0.2483 0.2596 0.1993 -0.0405 0.0102  0.0113  338  VAL B CG2 
11490 N N   . VAL B 341  ? 0.2367 0.2530 0.1995 -0.0473 0.0087  0.0114  339  VAL B N   
11491 C CA  . VAL B 341  ? 0.2300 0.2484 0.1973 -0.0474 0.0079  0.0101  339  VAL B CA  
11492 C C   . VAL B 341  ? 0.2073 0.2347 0.1792 -0.0458 0.0098  0.0091  339  VAL B C   
11493 O O   . VAL B 341  ? 0.2265 0.2595 0.1988 -0.0469 0.0119  0.0101  339  VAL B O   
11494 C CB  . VAL B 341  ? 0.2426 0.2595 0.2099 -0.0518 0.0071  0.0116  339  VAL B CB  
11495 C CG1 . VAL B 341  ? 0.3001 0.3075 0.2625 -0.0530 0.0053  0.0126  339  VAL B CG1 
11496 C CG2 . VAL B 341  ? 0.3315 0.3544 0.2994 -0.0553 0.0092  0.0136  339  VAL B CG2 
11497 N N   . GLN B 342  ? 0.1991 0.2276 0.1743 -0.0432 0.0090  0.0071  340  GLN B N   
11498 C CA  . GLN B 342  ? 0.2194 0.2554 0.1988 -0.0408 0.0105  0.0058  340  GLN B CA  
11499 C C   . GLN B 342  ? 0.2104 0.2516 0.1943 -0.0429 0.0105  0.0059  340  GLN B C   
11500 O O   . GLN B 342  ? 0.2198 0.2584 0.2050 -0.0429 0.0087  0.0050  340  GLN B O   
11501 C CB  . GLN B 342  ? 0.1985 0.2325 0.1786 -0.0366 0.0096  0.0036  340  GLN B CB  
11502 C CG  . GLN B 342  ? 0.1928 0.2223 0.1688 -0.0345 0.0095  0.0034  340  GLN B CG  
11503 C CD  . GLN B 342  ? 0.2059 0.2302 0.1817 -0.0316 0.0076  0.0017  340  GLN B CD  
11504 O OE1 . GLN B 342  ? 0.2179 0.2383 0.1940 -0.0322 0.0059  0.0015  340  GLN B OE1 
11505 N NE2 . GLN B 342  ? 0.1974 0.2217 0.1725 -0.0284 0.0079  0.0006  340  GLN B NE2 
11506 N N   . ALA B 343  ? 0.1978 0.2464 0.1840 -0.0444 0.0125  0.0069  341  ALA B N   
11507 C CA  . ALA B 343  ? 0.2057 0.2601 0.1964 -0.0466 0.0125  0.0072  341  ALA B CA  
11508 C C   . ALA B 343  ? 0.1995 0.2576 0.1945 -0.0435 0.0121  0.0053  341  ALA B C   
11509 O O   . ALA B 343  ? 0.2195 0.2808 0.2179 -0.0450 0.0114  0.0053  341  ALA B O   
11510 C CB  . ALA B 343  ? 0.2092 0.2711 0.2015 -0.0488 0.0149  0.0090  341  ALA B CB  
11511 N N   . TYR B 344  ? 0.1983 0.2557 0.1930 -0.0393 0.0125  0.0037  342  TYR B N   
11512 C CA  . TYR B 344  ? 0.1932 0.2529 0.1915 -0.0365 0.0119  0.0019  342  TYR B CA  
11513 C C   . TYR B 344  ? 0.1885 0.2419 0.1861 -0.0365 0.0094  0.0010  342  TYR B C   
11514 O O   . TYR B 344  ? 0.2150 0.2699 0.2154 -0.0347 0.0086  -0.0003 342  TYR B O   
11515 C CB  . TYR B 344  ? 0.2074 0.2688 0.2061 -0.0320 0.0130  0.0004  342  TYR B CB  
11516 C CG  . TYR B 344  ? 0.2025 0.2570 0.1976 -0.0294 0.0122  -0.0007 342  TYR B CG  
11517 C CD1 . TYR B 344  ? 0.1842 0.2311 0.1756 -0.0307 0.0105  -0.0003 342  TYR B CD1 
11518 C CD2 . TYR B 344  ? 0.1916 0.2474 0.1869 -0.0257 0.0130  -0.0022 342  TYR B CD2 
11519 C CE1 . TYR B 344  ? 0.1936 0.2350 0.1821 -0.0282 0.0097  -0.0013 342  TYR B CE1 
11520 C CE2 . TYR B 344  ? 0.2075 0.2575 0.1998 -0.0235 0.0122  -0.0031 342  TYR B CE2 
11521 C CZ  . TYR B 344  ? 0.2135 0.2566 0.2026 -0.0247 0.0105  -0.0027 342  TYR B CZ  
11522 O OH  . TYR B 344  ? 0.1968 0.2348 0.1832 -0.0224 0.0096  -0.0036 342  TYR B OH  
11523 N N   . GLY B 345  ? 0.1992 0.2457 0.1930 -0.0385 0.0081  0.0017  343  GLY B N   
11524 C CA  . GLY B 345  ? 0.2174 0.2575 0.2101 -0.0383 0.0059  0.0009  343  GLY B CA  
11525 C C   . GLY B 345  ? 0.2156 0.2559 0.2093 -0.0421 0.0048  0.0016  343  GLY B C   
11526 O O   . GLY B 345  ? 0.2120 0.2536 0.2051 -0.0456 0.0053  0.0033  343  GLY B O   
11527 N N   . LYS B 346  ? 0.2044 0.2427 0.1993 -0.0413 0.0033  0.0004  344  LYS B N   
11528 C CA  . LYS B 346  ? 0.2075 0.2458 0.2033 -0.0446 0.0019  0.0008  344  LYS B CA  
11529 C C   . LYS B 346  ? 0.2058 0.2366 0.1973 -0.0477 0.0008  0.0018  344  LYS B C   
11530 O O   . LYS B 346  ? 0.2243 0.2552 0.2159 -0.0514 -0.0001 0.0027  344  LYS B O   
11531 C CB  . LYS B 346  ? 0.2042 0.2415 0.2015 -0.0427 0.0006  -0.0009 344  LYS B CB  
11532 C CG  . LYS B 346  ? 0.1998 0.2443 0.2013 -0.0400 0.0016  -0.0017 344  LYS B CG  
11533 C CD  . LYS B 346  ? 0.2102 0.2533 0.2129 -0.0380 0.0003  -0.0033 344  LYS B CD  
11534 C CE  . LYS B 346  ? 0.2141 0.2645 0.2210 -0.0356 0.0011  -0.0039 344  LYS B CE  
11535 N NZ  . LYS B 346  ? 0.2140 0.2627 0.2216 -0.0334 0.0000  -0.0054 344  LYS B NZ  
11536 N N   . ARG B 347  ? 0.2135 0.2380 0.2013 -0.0463 0.0006  0.0018  345  ARG B N   
11537 C CA  . ARG B 347  ? 0.2361 0.2530 0.2196 -0.0489 -0.0006 0.0028  345  ARG B CA  
11538 C C   . ARG B 347  ? 0.2206 0.2384 0.2023 -0.0519 0.0004  0.0049  345  ARG B C   
11539 O O   . ARG B 347  ? 0.2447 0.2566 0.2229 -0.0546 -0.0005 0.0060  345  ARG B O   
11540 C CB  . ARG B 347  ? 0.2029 0.2123 0.1834 -0.0459 -0.0015 0.0018  345  ARG B CB  
11541 C CG  . ARG B 347  ? 0.2091 0.2166 0.1908 -0.0436 -0.0026 -0.0002 345  ARG B CG  
11542 C CD  . ARG B 347  ? 0.2298 0.2322 0.2097 -0.0400 -0.0030 -0.0012 345  ARG B CD  
11543 N NE  . ARG B 347  ? 0.2130 0.2197 0.1946 -0.0370 -0.0017 -0.0016 345  ARG B NE  
11544 C CZ  . ARG B 347  ? 0.2258 0.2293 0.2061 -0.0340 -0.0019 -0.0022 345  ARG B CZ  
11545 N NH1 . ARG B 347  ? 0.2209 0.2172 0.1984 -0.0334 -0.0032 -0.0024 345  ARG B NH1 
11546 N NH2 . ARG B 347  ? 0.2176 0.2251 0.1994 -0.0316 -0.0008 -0.0027 345  ARG B NH2 
11547 N N   . CYS B 348  ? 0.2324 0.2575 0.2164 -0.0516 0.0024  0.0056  346  CYS B N   
11548 C CA  . CYS B 348  ? 0.2460 0.2719 0.2278 -0.0538 0.0038  0.0076  346  CYS B CA  
11549 C C   . CYS B 348  ? 0.2473 0.2708 0.2274 -0.0589 0.0030  0.0094  346  CYS B C   
11550 O O   . CYS B 348  ? 0.2584 0.2760 0.2341 -0.0603 0.0027  0.0107  346  CYS B O   
11551 C CB  . CYS B 348  ? 0.2207 0.2559 0.2059 -0.0528 0.0061  0.0078  346  CYS B CB  
11552 S SG  . CYS B 348  ? 0.2928 0.3286 0.2746 -0.0544 0.0081  0.0100  346  CYS B SG  
11553 N N   . PRO B 349  ? 0.2439 0.2716 0.2270 -0.0618 0.0026  0.0098  347  PRO B N   
11554 C CA  . PRO B 349  ? 0.2671 0.2921 0.2482 -0.0670 0.0019  0.0117  347  PRO B CA  
11555 C C   . PRO B 349  ? 0.2576 0.2718 0.2341 -0.0677 -0.0003 0.0114  347  PRO B C   
11556 O O   . PRO B 349  ? 0.2526 0.2620 0.2254 -0.0710 -0.0007 0.0132  347  PRO B O   
11557 C CB  . PRO B 349  ? 0.2590 0.2908 0.2448 -0.0694 0.0016  0.0117  347  PRO B CB  
11558 C CG  . PRO B 349  ? 0.2715 0.3067 0.2607 -0.0654 0.0014  0.0095  347  PRO B CG  
11559 C CD  . PRO B 349  ? 0.2643 0.2988 0.2525 -0.0607 0.0026  0.0085  347  PRO B CD  
11560 N N   . PHE B 350  ? 0.2468 0.2569 0.2231 -0.0646 -0.0017 0.0093  348  PHE B N   
11561 C CA  . PHE B 350  ? 0.2429 0.2427 0.2148 -0.0647 -0.0037 0.0089  348  PHE B CA  
11562 C C   . PHE B 350  ? 0.2351 0.2290 0.2029 -0.0628 -0.0034 0.0095  348  PHE B C   
11563 O O   . PHE B 350  ? 0.2672 0.2531 0.2306 -0.0645 -0.0046 0.0104  348  PHE B O   
11564 C CB  . PHE B 350  ? 0.2434 0.2415 0.2166 -0.0620 -0.0049 0.0065  348  PHE B CB  
11565 C CG  . PHE B 350  ? 0.2581 0.2627 0.2354 -0.0636 -0.0052 0.0060  348  PHE B CG  
11566 C CD1 . PHE B 350  ? 0.2838 0.2865 0.2603 -0.0679 -0.0066 0.0066  348  PHE B CD1 
11567 C CD2 . PHE B 350  ? 0.2606 0.2732 0.2424 -0.0610 -0.0040 0.0051  348  PHE B CD2 
11568 C CE1 . PHE B 350  ? 0.3416 0.3507 0.3221 -0.0696 -0.0069 0.0063  348  PHE B CE1 
11569 C CE2 . PHE B 350  ? 0.2820 0.3010 0.2678 -0.0624 -0.0043 0.0048  348  PHE B CE2 
11570 C CZ  . PHE B 350  ? 0.2872 0.3046 0.2724 -0.0667 -0.0058 0.0054  348  PHE B CZ  
11571 N N   . VAL B 351  ? 0.2330 0.2307 0.2020 -0.0594 -0.0020 0.0091  349  VAL B N   
11572 C CA  . VAL B 351  ? 0.2302 0.2231 0.1953 -0.0579 -0.0018 0.0098  349  VAL B CA  
11573 C C   . VAL B 351  ? 0.2516 0.2441 0.2140 -0.0618 -0.0010 0.0124  349  VAL B C   
11574 O O   . VAL B 351  ? 0.2495 0.2346 0.2073 -0.0626 -0.0019 0.0136  349  VAL B O   
11575 C CB  . VAL B 351  ? 0.2420 0.2395 0.2089 -0.0537 -0.0004 0.0088  349  VAL B CB  
11576 C CG1 . VAL B 351  ? 0.2542 0.2472 0.2170 -0.0523 -0.0003 0.0097  349  VAL B CG1 
11577 C CG2 . VAL B 351  ? 0.2476 0.2445 0.2167 -0.0500 -0.0013 0.0064  349  VAL B CG2 
11578 N N   . LEU B 352  ? 0.2386 0.2389 0.2037 -0.0643 0.0005  0.0135  350  LEU B N   
11579 C CA  . LEU B 352  ? 0.2623 0.2627 0.2252 -0.0684 0.0014  0.0161  350  LEU B CA  
11580 C C   . LEU B 352  ? 0.2738 0.2667 0.2335 -0.0723 -0.0005 0.0172  350  LEU B C   
11581 O O   . LEU B 352  ? 0.2863 0.2736 0.2414 -0.0744 -0.0007 0.0190  350  LEU B O   
11582 C CB  . LEU B 352  ? 0.2712 0.2821 0.2384 -0.0705 0.0034  0.0169  350  LEU B CB  
11583 C CG  . LEU B 352  ? 0.2579 0.2757 0.2272 -0.0670 0.0057  0.0163  350  LEU B CG  
11584 C CD1 . LEU B 352  ? 0.2748 0.3030 0.2489 -0.0688 0.0076  0.0170  350  LEU B CD1 
11585 C CD2 . LEU B 352  ? 0.2997 0.3144 0.2645 -0.0665 0.0066  0.0177  350  LEU B CD2 
11586 N N   . ASP B 353  ? 0.2702 0.2623 0.2317 -0.0734 -0.0020 0.0160  351  ASP B N   
11587 C CA  . ASP B 353  ? 0.2894 0.2736 0.2475 -0.0770 -0.0039 0.0167  351  ASP B CA  
11588 C C   . ASP B 353  ? 0.2663 0.2400 0.2192 -0.0748 -0.0053 0.0166  351  ASP B C   
11589 O O   . ASP B 353  ? 0.3021 0.2687 0.2505 -0.0777 -0.0061 0.0182  351  ASP B O   
11590 C CB  . ASP B 353  ? 0.2976 0.2818 0.2581 -0.0775 -0.0054 0.0150  351  ASP B CB  
11591 C CG  . ASP B 353  ? 0.3442 0.3380 0.3096 -0.0804 -0.0047 0.0154  351  ASP B CG  
11592 O OD1 . ASP B 353  ? 0.3428 0.3413 0.3090 -0.0838 -0.0033 0.0176  351  ASP B OD1 
11593 O OD2 . ASP B 353  ? 0.3623 0.3589 0.3309 -0.0794 -0.0055 0.0137  351  ASP B OD2 
11594 N N   . PHE B 354  ? 0.2702 0.2426 0.2236 -0.0698 -0.0055 0.0146  352  PHE B N   
11595 C CA  . PHE B 354  ? 0.2826 0.2458 0.2316 -0.0674 -0.0067 0.0144  352  PHE B CA  
11596 C C   . PHE B 354  ? 0.2857 0.2471 0.2312 -0.0679 -0.0060 0.0166  352  PHE B C   
11597 O O   . PHE B 354  ? 0.2946 0.2475 0.2354 -0.0688 -0.0072 0.0178  352  PHE B O   
11598 C CB  . PHE B 354  ? 0.2761 0.2399 0.2271 -0.0620 -0.0069 0.0120  352  PHE B CB  
11599 C CG  . PHE B 354  ? 0.2889 0.2452 0.2362 -0.0590 -0.0078 0.0120  352  PHE B CG  
11600 C CD1 . PHE B 354  ? 0.3188 0.2661 0.2631 -0.0584 -0.0097 0.0114  352  PHE B CD1 
11601 C CD2 . PHE B 354  ? 0.2959 0.2539 0.2425 -0.0567 -0.0069 0.0126  352  PHE B CD2 
11602 C CE1 . PHE B 354  ? 0.3049 0.2456 0.2462 -0.0555 -0.0106 0.0115  352  PHE B CE1 
11603 C CE2 . PHE B 354  ? 0.3074 0.2587 0.2507 -0.0540 -0.0080 0.0127  352  PHE B CE2 
11604 C CZ  . PHE B 354  ? 0.3170 0.2599 0.2579 -0.0533 -0.0098 0.0122  352  PHE B CZ  
11605 N N   . ILE B 355  ? 0.2711 0.2401 0.2186 -0.0673 -0.0039 0.0172  353  ILE B N   
11606 C CA  . ILE B 355  ? 0.2776 0.2451 0.2215 -0.0675 -0.0031 0.0191  353  ILE B CA  
11607 C C   . ILE B 355  ? 0.2775 0.2427 0.2184 -0.0728 -0.0030 0.0218  353  ILE B C   
11608 O O   . ILE B 355  ? 0.3039 0.2623 0.2398 -0.0737 -0.0036 0.0236  353  ILE B O   
11609 C CB  . ILE B 355  ? 0.2527 0.2291 0.1994 -0.0655 -0.0009 0.0188  353  ILE B CB  
11610 C CG1 . ILE B 355  ? 0.3052 0.2822 0.2538 -0.0602 -0.0012 0.0164  353  ILE B CG1 
11611 C CG2 . ILE B 355  ? 0.2899 0.2655 0.2326 -0.0666 0.0003  0.0211  353  ILE B CG2 
11612 C CD1 . ILE B 355  ? 0.2894 0.2752 0.2412 -0.0581 0.0009  0.0157  353  ILE B CD1 
11613 N N   . ILE B 356  ? 0.2848 0.2556 0.2288 -0.0765 -0.0023 0.0223  354  ILE B N   
11614 C CA  . ILE B 356  ? 0.3045 0.2735 0.2460 -0.0820 -0.0022 0.0250  354  ILE B CA  
11615 C C   . ILE B 356  ? 0.2982 0.2557 0.2350 -0.0836 -0.0047 0.0254  354  ILE B C   
11616 O O   . ILE B 356  ? 0.3139 0.2657 0.2460 -0.0863 -0.0050 0.0278  354  ILE B O   
11617 C CB  . ILE B 356  ? 0.3042 0.2816 0.2505 -0.0856 -0.0012 0.0252  354  ILE B CB  
11618 C CG1 . ILE B 356  ? 0.3129 0.3014 0.2631 -0.0843 0.0015  0.0254  354  ILE B CG1 
11619 C CG2 . ILE B 356  ? 0.3092 0.2837 0.2531 -0.0916 -0.0017 0.0278  354  ILE B CG2 
11620 C CD1 . ILE B 356  ? 0.3041 0.3023 0.2603 -0.0864 0.0025  0.0250  354  ILE B CD1 
11621 N N   . ASP B 357  ? 0.2965 0.2502 0.2342 -0.0818 -0.0064 0.0232  355  ASP B N   
11622 C CA  . ASP B 357  ? 0.3371 0.2795 0.2701 -0.0827 -0.0087 0.0233  355  ASP B CA  
11623 C C   . ASP B 357  ? 0.2894 0.2244 0.2179 -0.0796 -0.0094 0.0239  355  ASP B C   
11624 O O   . ASP B 357  ? 0.3176 0.2441 0.2410 -0.0816 -0.0105 0.0256  355  ASP B O   
11625 C CB  . ASP B 357  ? 0.3209 0.2613 0.2558 -0.0810 -0.0102 0.0207  355  ASP B CB  
11626 C CG  . ASP B 357  ? 0.3159 0.2442 0.2458 -0.0808 -0.0125 0.0204  355  ASP B CG  
11627 O OD1 . ASP B 357  ? 0.3863 0.3096 0.3134 -0.0853 -0.0135 0.0216  355  ASP B OD1 
11628 O OD2 . ASP B 357  ? 0.3419 0.2657 0.2707 -0.0763 -0.0132 0.0190  355  ASP B OD2 
11629 N N   . LEU B 358  ? 0.3090 0.2469 0.2391 -0.0747 -0.0088 0.0225  356  LEU B N   
11630 C CA  . LEU B 358  ? 0.2932 0.2248 0.2194 -0.0716 -0.0095 0.0230  356  LEU B CA  
11631 C C   . LEU B 358  ? 0.2936 0.2240 0.2158 -0.0743 -0.0087 0.0260  356  LEU B C   
11632 O O   . LEU B 358  ? 0.3280 0.2497 0.2452 -0.0745 -0.0100 0.0275  356  LEU B O   
11633 C CB  . LEU B 358  ? 0.2816 0.2181 0.2108 -0.0664 -0.0088 0.0211  356  LEU B CB  
11634 C CG  . LEU B 358  ? 0.2919 0.2237 0.2178 -0.0629 -0.0094 0.0216  356  LEU B CG  
11635 C CD1 . LEU B 358  ? 0.3126 0.2338 0.2349 -0.0617 -0.0117 0.0215  356  LEU B CD1 
11636 C CD2 . LEU B 358  ? 0.3047 0.2424 0.2343 -0.0583 -0.0087 0.0195  356  LEU B CD2 
11637 N N   . ALA B 359  ? 0.2947 0.2337 0.2192 -0.0765 -0.0065 0.0271  357  ALA B N   
11638 C CA  . ALA B 359  ? 0.2942 0.2327 0.2149 -0.0793 -0.0055 0.0301  357  ALA B CA  
11639 C C   . ALA B 359  ? 0.3412 0.2721 0.2578 -0.0841 -0.0067 0.0322  357  ALA B C   
11640 O O   . ALA B 359  ? 0.3509 0.2750 0.2622 -0.0850 -0.0074 0.0343  357  ALA B O   
11641 C CB  . ALA B 359  ? 0.3389 0.2887 0.2633 -0.0811 -0.0028 0.0306  357  ALA B CB  
11642 N N   . ARG B 360  ? 0.3268 0.2584 0.2457 -0.0872 -0.0073 0.0316  358  ARG B N   
11643 C CA  A ARG B 360  ? 0.3637 0.2883 0.2789 -0.0922 -0.0085 0.0336  358  ARG B CA  
11644 C CA  B ARG B 360  ? 0.3636 0.2881 0.2788 -0.0922 -0.0085 0.0336  358  ARG B CA  
11645 C C   . ARG B 360  ? 0.3220 0.2340 0.2320 -0.0905 -0.0110 0.0335  358  ARG B C   
11646 O O   . ARG B 360  ? 0.3674 0.2719 0.2720 -0.0931 -0.0117 0.0359  358  ARG B O   
11647 C CB  A ARG B 360  ? 0.3684 0.2964 0.2874 -0.0954 -0.0088 0.0325  358  ARG B CB  
11648 C CB  B ARG B 360  ? 0.3688 0.2969 0.2878 -0.0955 -0.0088 0.0326  358  ARG B CB  
11649 C CG  A ARG B 360  ? 0.3736 0.3122 0.2965 -0.0991 -0.0066 0.0338  358  ARG B CG  
11650 C CG  B ARG B 360  ? 0.4288 0.3630 0.3491 -0.1013 -0.0073 0.0350  358  ARG B CG  
11651 C CD  A ARG B 360  ? 0.3963 0.3389 0.3234 -0.1020 -0.0072 0.0327  358  ARG B CD  
11652 C CD  B ARG B 360  ? 0.3854 0.3214 0.3087 -0.1049 -0.0082 0.0342  358  ARG B CD  
11653 N NE  A ARG B 360  ? 0.4013 0.3531 0.3317 -0.1065 -0.0053 0.0346  358  ARG B NE  
11654 N NE  B ARG B 360  ? 0.4152 0.3624 0.3453 -0.1035 -0.0069 0.0324  358  ARG B NE  
11655 C CZ  A ARG B 360  ? 0.4315 0.3926 0.3677 -0.1076 -0.0046 0.0336  358  ARG B CZ  
11656 C CZ  B ARG B 360  ? 0.4296 0.3873 0.3640 -0.1063 -0.0049 0.0335  358  ARG B CZ  
11657 N NH1 A ARG B 360  ? 0.4662 0.4287 0.4057 -0.1046 -0.0056 0.0308  358  ARG B NH1 
11658 N NH1 B ARG B 360  ? 0.4715 0.4303 0.4041 -0.1109 -0.0038 0.0366  358  ARG B NH1 
11659 N NH2 A ARG B 360  ? 0.4849 0.4543 0.4240 -0.1117 -0.0028 0.0356  358  ARG B NH2 
11660 N NH2 B ARG B 360  ? 0.4516 0.4187 0.3920 -0.1046 -0.0040 0.0317  358  ARG B NH2 
11661 N N   . ARG B 361  ? 0.3499 0.2592 0.2612 -0.0860 -0.0122 0.0308  359  ARG B N   
11662 C CA  . ARG B 361  ? 0.3663 0.2638 0.2729 -0.0843 -0.0145 0.0306  359  ARG B CA  
11663 C C   . ARG B 361  ? 0.3452 0.2384 0.2481 -0.0809 -0.0149 0.0316  359  ARG B C   
11664 O O   . ARG B 361  ? 0.3710 0.2539 0.2691 -0.0804 -0.0167 0.0325  359  ARG B O   
11665 C CB  . ARG B 361  ? 0.4051 0.3006 0.3140 -0.0811 -0.0158 0.0274  359  ARG B CB  
11666 C CG  . ARG B 361  ? 0.3942 0.2962 0.3075 -0.0758 -0.0150 0.0251  359  ARG B CG  
11667 C CD  . ARG B 361  ? 0.3511 0.2519 0.2669 -0.0736 -0.0159 0.0221  359  ARG B CD  
11668 N NE  . ARG B 361  ? 0.3320 0.2415 0.2531 -0.0699 -0.0148 0.0199  359  ARG B NE  
11669 C CZ  . ARG B 361  ? 0.3047 0.2138 0.2267 -0.0648 -0.0149 0.0186  359  ARG B CZ  
11670 N NH1 . ARG B 361  ? 0.3567 0.2577 0.2748 -0.0624 -0.0162 0.0191  359  ARG B NH1 
11671 N NH2 . ARG B 361  ? 0.3272 0.2442 0.2540 -0.0619 -0.0139 0.0167  359  ARG B NH2 
11672 N N   . SER B 362  ? 0.3442 0.2450 0.2493 -0.0786 -0.0132 0.0317  360  SER B N   
11673 C CA  . SER B 362  ? 0.3559 0.2532 0.2578 -0.0753 -0.0137 0.0326  360  SER B CA  
11674 C C   . SER B 362  ? 0.3430 0.2398 0.2407 -0.0784 -0.0128 0.0359  360  SER B C   
11675 O O   . SER B 362  ? 0.3908 0.2834 0.2847 -0.0763 -0.0134 0.0370  360  SER B O   
11676 C CB  . SER B 362  ? 0.3545 0.2593 0.2606 -0.0705 -0.0127 0.0304  360  SER B CB  
11677 O OG  . SER B 362  ? 0.3445 0.2593 0.2535 -0.0721 -0.0103 0.0309  360  SER B OG  
11678 N N   . GLY B 363  ? 0.3281 0.2293 0.2263 -0.0835 -0.0113 0.0374  361  GLY B N   
11679 C CA  . GLY B 363  ? 0.3349 0.2361 0.2291 -0.0864 -0.0101 0.0406  361  GLY B CA  
11680 C C   . GLY B 363  ? 0.3450 0.2537 0.2404 -0.0837 -0.0083 0.0406  361  GLY B C   
11681 O O   . GLY B 363  ? 0.3919 0.2978 0.2826 -0.0838 -0.0081 0.0428  361  GLY B O   
11682 N N   . ARG B 364  ? 0.3564 0.2741 0.2574 -0.0813 -0.0070 0.0382  362  ARG B N   
11683 C CA  . ARG B 364  ? 0.3578 0.2830 0.2602 -0.0787 -0.0051 0.0377  362  ARG B CA  
11684 C C   . ARG B 364  ? 0.3451 0.2812 0.2526 -0.0809 -0.0025 0.0373  362  ARG B C   
11685 O O   . ARG B 364  ? 0.3623 0.3018 0.2745 -0.0812 -0.0026 0.0355  362  ARG B O   
11686 C CB  . ARG B 364  ? 0.3394 0.2654 0.2445 -0.0728 -0.0061 0.0348  362  ARG B CB  
11687 C CG  . ARG B 364  ? 0.3483 0.2646 0.2498 -0.0697 -0.0087 0.0347  362  ARG B CG  
11688 C CD  . ARG B 364  ? 0.3693 0.2830 0.2657 -0.0688 -0.0088 0.0367  362  ARG B CD  
11689 N NE  . ARG B 364  ? 0.3354 0.2396 0.2283 -0.0661 -0.0115 0.0370  362  ARG B NE  
11690 C CZ  . ARG B 364  ? 0.3567 0.2603 0.2513 -0.0612 -0.0128 0.0350  362  ARG B CZ  
11691 N NH1 . ARG B 364  ? 0.3515 0.2629 0.2508 -0.0584 -0.0117 0.0326  362  ARG B NH1 
11692 N NH2 . ARG B 364  ? 0.3888 0.2836 0.2802 -0.0590 -0.0152 0.0354  362  ARG B NH2 
11693 N N   . ARG B 365  ? 0.3510 0.2927 0.2574 -0.0824 -0.0002 0.0390  363  ARG B N   
11694 C CA  . ARG B 365  ? 0.3285 0.2816 0.2404 -0.0828 0.0024  0.0380  363  ARG B CA  
11695 C C   . ARG B 365  ? 0.3314 0.2885 0.2461 -0.0773 0.0026  0.0352  363  ARG B C   
11696 O O   . ARG B 365  ? 0.3692 0.3236 0.2805 -0.0744 0.0022  0.0353  363  ARG B O   
11697 C CB  . ARG B 365  ? 0.3502 0.3084 0.2603 -0.0861 0.0050  0.0406  363  ARG B CB  
11698 C CG  . ARG B 365  ? 0.3531 0.3227 0.2693 -0.0878 0.0076  0.0400  363  ARG B CG  
11699 C CD  . ARG B 365  ? 0.4156 0.3898 0.3299 -0.0918 0.0103  0.0430  363  ARG B CD  
11700 N NE  . ARG B 365  ? 0.4042 0.3893 0.3245 -0.0938 0.0127  0.0427  363  ARG B NE  
11701 C CZ  . ARG B 365  ? 0.3779 0.3715 0.2993 -0.0939 0.0158  0.0434  363  ARG B CZ  
11702 N NH1 . ARG B 365  ? 0.3620 0.3546 0.2786 -0.0923 0.0170  0.0443  363  ARG B NH1 
11703 N NH2 . ARG B 365  ? 0.3354 0.3390 0.2627 -0.0956 0.0178  0.0432  363  ARG B NH2 
11704 N N   . ILE B 366  ? 0.3101 0.2730 0.2307 -0.0758 0.0029  0.0328  364  ILE B N   
11705 C CA  . ILE B 366  ? 0.3130 0.2797 0.2366 -0.0707 0.0031  0.0301  364  ILE B CA  
11706 C C   . ILE B 366  ? 0.3300 0.3075 0.2572 -0.0708 0.0060  0.0298  364  ILE B C   
11707 O O   . ILE B 366  ? 0.3137 0.2970 0.2443 -0.0739 0.0074  0.0302  364  ILE B O   
11708 C CB  . ILE B 366  ? 0.2989 0.2642 0.2264 -0.0687 0.0013  0.0275  364  ILE B CB  
11709 C CG1 . ILE B 366  ? 0.3396 0.2940 0.2633 -0.0684 -0.0015 0.0278  364  ILE B CG1 
11710 C CG2 . ILE B 366  ? 0.2923 0.2623 0.2234 -0.0637 0.0017  0.0248  364  ILE B CG2 
11711 C CD1 . ILE B 366  ? 0.3297 0.2819 0.2566 -0.0667 -0.0031 0.0255  364  ILE B CD1 
11712 N N   . MET B 367  ? 0.2954 0.2755 0.2216 -0.0675 0.0070  0.0290  365  MET B N   
11713 C CA  . MET B 367  ? 0.2972 0.2872 0.2267 -0.0668 0.0099  0.0284  365  MET B CA  
11714 C C   . MET B 367  ? 0.3096 0.3042 0.2451 -0.0637 0.0096  0.0254  365  MET B C   
11715 O O   . MET B 367  ? 0.3131 0.3042 0.2487 -0.0600 0.0080  0.0235  365  MET B O   
11716 C CB  . MET B 367  ? 0.2870 0.2771 0.2125 -0.0644 0.0109  0.0286  365  MET B CB  
11717 C CG  . MET B 367  ? 0.2921 0.2759 0.2108 -0.0668 0.0105  0.0315  365  MET B CG  
11718 S SD  . MET B 367  ? 0.3300 0.3140 0.2435 -0.0641 0.0116  0.0318  365  MET B SD  
11719 C CE  . MET B 367  ? 0.4233 0.4155 0.3363 -0.0674 0.0157  0.0338  365  MET B CE  
11720 N N   . VAL B 368  ? 0.2573 0.2594 0.1977 -0.0654 0.0111  0.0251  366  VAL B N   
11721 C CA  . VAL B 368  ? 0.2613 0.2674 0.2073 -0.0628 0.0108  0.0225  366  VAL B CA  
11722 C C   . VAL B 368  ? 0.2765 0.2921 0.2259 -0.0610 0.0134  0.0216  366  VAL B C   
11723 O O   . VAL B 368  ? 0.2723 0.2947 0.2238 -0.0637 0.0156  0.0228  366  VAL B O   
11724 C CB  . VAL B 368  ? 0.2726 0.2792 0.2220 -0.0659 0.0098  0.0226  366  VAL B CB  
11725 C CG1 . VAL B 368  ? 0.2784 0.2894 0.2332 -0.0631 0.0095  0.0199  366  VAL B CG1 
11726 C CG2 . VAL B 368  ? 0.3074 0.3038 0.2530 -0.0674 0.0071  0.0233  366  VAL B CG2 
11727 N N   . ARG B 369  ? 0.2437 0.2600 0.1937 -0.0565 0.0134  0.0194  367  ARG B N   
11728 C CA  . ARG B 369  ? 0.2438 0.2684 0.1968 -0.0544 0.0158  0.0183  367  ARG B CA  
11729 C C   . ARG B 369  ? 0.2445 0.2738 0.2038 -0.0533 0.0155  0.0164  367  ARG B C   
11730 O O   . ARG B 369  ? 0.2521 0.2780 0.2125 -0.0508 0.0136  0.0146  367  ARG B O   
11731 C CB  . ARG B 369  ? 0.2370 0.2600 0.1874 -0.0502 0.0159  0.0168  367  ARG B CB  
11732 C CG  . ARG B 369  ? 0.2718 0.3031 0.2250 -0.0478 0.0184  0.0156  367  ARG B CG  
11733 C CD  . ARG B 369  ? 0.2677 0.2969 0.2194 -0.0434 0.0179  0.0135  367  ARG B CD  
11734 N NE  . ARG B 369  ? 0.2593 0.2834 0.2047 -0.0433 0.0176  0.0145  367  ARG B NE  
11735 C CZ  . ARG B 369  ? 0.2585 0.2778 0.2013 -0.0403 0.0160  0.0133  367  ARG B CZ  
11736 N NH1 . ARG B 369  ? 0.2558 0.2746 0.2016 -0.0372 0.0146  0.0110  367  ARG B NH1 
11737 N NH2 . ARG B 369  ? 0.2763 0.2912 0.2131 -0.0405 0.0157  0.0145  367  ARG B NH2 
11738 N N   . LEU B 370  ? 0.2255 0.2626 0.1886 -0.0553 0.0173  0.0171  368  LEU B N   
11739 C CA  . LEU B 370  ? 0.2161 0.2586 0.1853 -0.0542 0.0171  0.0154  368  LEU B CA  
11740 C C   . LEU B 370  ? 0.2281 0.2766 0.1995 -0.0502 0.0190  0.0137  368  LEU B C   
11741 O O   . LEU B 370  ? 0.2403 0.2940 0.2113 -0.0503 0.0216  0.0145  368  LEU B O   
11742 C CB  . LEU B 370  ? 0.2490 0.2970 0.2216 -0.0584 0.0179  0.0170  368  LEU B CB  
11743 C CG  . LEU B 370  ? 0.2250 0.2786 0.2038 -0.0577 0.0175  0.0156  368  LEU B CG  
11744 C CD1 . LEU B 370  ? 0.2705 0.3175 0.2493 -0.0570 0.0145  0.0142  368  LEU B CD1 
11745 C CD2 . LEU B 370  ? 0.2455 0.3058 0.2277 -0.0621 0.0186  0.0174  368  LEU B CD2 
11746 N N   . VAL B 371  ? 0.2033 0.2505 0.1766 -0.0466 0.0177  0.0114  369  VAL B N   
11747 C CA  . VAL B 371  ? 0.2191 0.2712 0.1946 -0.0426 0.0192  0.0096  369  VAL B CA  
11748 C C   . VAL B 371  ? 0.2288 0.2850 0.2100 -0.0416 0.0185  0.0082  369  VAL B C   
11749 O O   . VAL B 371  ? 0.2243 0.2783 0.2070 -0.0435 0.0167  0.0084  369  VAL B O   
11750 C CB  . VAL B 371  ? 0.2054 0.2518 0.1774 -0.0390 0.0181  0.0081  369  VAL B CB  
11751 C CG1 . VAL B 371  ? 0.2261 0.2676 0.1921 -0.0402 0.0182  0.0096  369  VAL B CG1 
11752 C CG2 . VAL B 371  ? 0.2217 0.2625 0.1946 -0.0377 0.0154  0.0067  369  VAL B CG2 
11753 N N   . LYS B 372  ? 0.2017 0.2635 0.1858 -0.0385 0.0200  0.0068  370  LYS B N   
11754 C CA  . LYS B 372  ? 0.2080 0.2726 0.1971 -0.0369 0.0190  0.0053  370  LYS B CA  
11755 C C   . LYS B 372  ? 0.1996 0.2576 0.1873 -0.0340 0.0168  0.0034  370  LYS B C   
11756 O O   . LYS B 372  ? 0.2266 0.2808 0.2150 -0.0349 0.0147  0.0032  370  LYS B O   
11757 C CB  . LYS B 372  ? 0.2262 0.2997 0.2194 -0.0349 0.0213  0.0047  370  LYS B CB  
11758 C CG  . LYS B 372  ? 0.2142 0.2943 0.2096 -0.0384 0.0230  0.0067  370  LYS B CG  
11759 C CD  . LYS B 372  ? 0.2241 0.3137 0.2240 -0.0366 0.0254  0.0064  370  LYS B CD  
11760 C CE  . LYS B 372  ? 0.2394 0.3354 0.2409 -0.0404 0.0273  0.0087  370  LYS B CE  
11761 N NZ  . LYS B 372  ? 0.2472 0.3530 0.2529 -0.0385 0.0301  0.0085  370  LYS B NZ  
11762 N N   . GLY B 373  ? 0.2148 0.2709 0.2004 -0.0307 0.0172  0.0022  371  GLY B N   
11763 C CA  . GLY B 373  ? 0.2072 0.2568 0.1912 -0.0284 0.0151  0.0007  371  GLY B CA  
11764 C C   . GLY B 373  ? 0.1975 0.2480 0.1816 -0.0243 0.0158  -0.0011 371  GLY B C   
11765 O O   . GLY B 373  ? 0.2162 0.2728 0.2034 -0.0228 0.0173  -0.0018 371  GLY B O   
11766 N N   . ALA B 374  ? 0.1967 0.2413 0.1776 -0.0225 0.0145  -0.0019 372  ALA B N   
11767 C CA  . ALA B 374  ? 0.2131 0.2578 0.1930 -0.0190 0.0151  -0.0035 372  ALA B CA  
11768 C C   . ALA B 374  ? 0.2197 0.2625 0.2018 -0.0163 0.0136  -0.0054 372  ALA B C   
11769 O O   . ALA B 374  ? 0.2424 0.2852 0.2239 -0.0134 0.0140  -0.0068 372  ALA B O   
11770 C CB  . ALA B 374  ? 0.2361 0.2759 0.2104 -0.0189 0.0148  -0.0031 372  ALA B CB  
11771 N N   . TYR B 375  ? 0.2018 0.2428 0.1862 -0.0170 0.0120  -0.0055 373  TYR B N   
11772 C CA  . TYR B 375  ? 0.2065 0.2450 0.1925 -0.0146 0.0105  -0.0071 373  TYR B CA  
11773 C C   . TYR B 375  ? 0.2130 0.2556 0.2036 -0.0140 0.0106  -0.0078 373  TYR B C   
11774 O O   . TYR B 375  ? 0.1979 0.2381 0.1900 -0.0131 0.0091  -0.0086 373  TYR B O   
11775 C CB  . TYR B 375  ? 0.2416 0.2735 0.2258 -0.0153 0.0083  -0.0068 373  TYR B CB  
11776 C CG  . TYR B 375  ? 0.2244 0.2519 0.2040 -0.0159 0.0079  -0.0060 373  TYR B CG  
11777 C CD1 . TYR B 375  ? 0.2262 0.2534 0.2033 -0.0187 0.0085  -0.0042 373  TYR B CD1 
11778 C CD2 . TYR B 375  ? 0.2660 0.2894 0.2437 -0.0137 0.0067  -0.0070 373  TYR B CD2 
11779 C CE1 . TYR B 375  ? 0.2379 0.2608 0.2105 -0.0191 0.0079  -0.0034 373  TYR B CE1 
11780 C CE2 . TYR B 375  ? 0.2755 0.2949 0.2490 -0.0142 0.0060  -0.0062 373  TYR B CE2 
11781 C CZ  . TYR B 375  ? 0.2657 0.2848 0.2366 -0.0168 0.0067  -0.0044 373  TYR B CZ  
11782 O OH  . TYR B 375  ? 0.3212 0.3360 0.2876 -0.0172 0.0059  -0.0035 373  TYR B OH  
11783 N N   . TRP B 376  ? 0.2010 0.2500 0.1940 -0.0145 0.0123  -0.0073 374  TRP B N   
11784 C CA  . TRP B 376  ? 0.1925 0.2455 0.1898 -0.0147 0.0121  -0.0075 374  TRP B CA  
11785 C C   . TRP B 376  ? 0.1845 0.2368 0.1839 -0.0116 0.0113  -0.0092 374  TRP B C   
11786 O O   . TRP B 376  ? 0.1894 0.2401 0.1904 -0.0118 0.0099  -0.0096 374  TRP B O   
11787 C CB  . TRP B 376  ? 0.1862 0.2467 0.1860 -0.0154 0.0142  -0.0068 374  TRP B CB  
11788 C CG  . TRP B 376  ? 0.2031 0.2678 0.2074 -0.0157 0.0137  -0.0068 374  TRP B CG  
11789 C CD1 . TRP B 376  ? 0.1895 0.2545 0.1953 -0.0186 0.0127  -0.0059 374  TRP B CD1 
11790 C CD2 . TRP B 376  ? 0.2040 0.2728 0.2117 -0.0129 0.0142  -0.0079 374  TRP B CD2 
11791 N NE1 . TRP B 376  ? 0.1940 0.2634 0.2039 -0.0179 0.0124  -0.0063 374  TRP B NE1 
11792 C CE2 . TRP B 376  ? 0.2002 0.2721 0.2115 -0.0143 0.0133  -0.0075 374  TRP B CE2 
11793 C CE3 . TRP B 376  ? 0.2559 0.3259 0.2638 -0.0093 0.0152  -0.0092 374  TRP B CE3 
11794 C CZ2 . TRP B 376  ? 0.2185 0.2945 0.2334 -0.0123 0.0133  -0.0082 374  TRP B CZ2 
11795 C CZ3 . TRP B 376  ? 0.2645 0.3385 0.2762 -0.0072 0.0153  -0.0100 374  TRP B CZ3 
11796 C CH2 . TRP B 376  ? 0.2435 0.3205 0.2587 -0.0087 0.0144  -0.0094 374  TRP B CH2 
11797 N N   . ASP B 377  ? 0.2017 0.2549 0.2006 -0.0087 0.0123  -0.0103 375  ASP B N   
11798 C CA  . ASP B 377  ? 0.2348 0.2873 0.2355 -0.0058 0.0116  -0.0119 375  ASP B CA  
11799 C C   . ASP B 377  ? 0.1940 0.2403 0.1936 -0.0057 0.0096  -0.0124 375  ASP B C   
11800 O O   . ASP B 377  ? 0.2138 0.2595 0.2155 -0.0048 0.0086  -0.0130 375  ASP B O   
11801 C CB  . ASP B 377  ? 0.2798 0.3325 0.2790 -0.0029 0.0127  -0.0130 375  ASP B CB  
11802 C CG  . ASP B 377  ? 0.4276 0.4866 0.4282 -0.0023 0.0150  -0.0128 375  ASP B CG  
11803 O OD1 . ASP B 377  ? 0.5461 0.6101 0.5504 -0.0024 0.0154  -0.0125 375  ASP B OD1 
11804 O OD2 . ASP B 377  ? 0.6048 0.6639 0.6026 -0.0016 0.0163  -0.0130 375  ASP B OD2 
11805 N N   . ALA B 378  ? 0.1868 0.2285 0.1829 -0.0066 0.0089  -0.0120 376  ALA B N   
11806 C CA  . ALA B 378  ? 0.1883 0.2244 0.1835 -0.0062 0.0071  -0.0124 376  ALA B CA  
11807 C C   . ALA B 378  ? 0.2118 0.2467 0.2083 -0.0082 0.0060  -0.0118 376  ALA B C   
11808 O O   . ALA B 378  ? 0.2057 0.2377 0.2030 -0.0074 0.0048  -0.0125 376  ALA B O   
11809 C CB  . ALA B 378  ? 0.2251 0.2568 0.2163 -0.0067 0.0066  -0.0120 376  ALA B CB  
11810 N N   . GLU B 379  ? 0.1864 0.2235 0.1830 -0.0108 0.0065  -0.0106 377  GLU B N   
11811 C CA  . GLU B 379  ? 0.1857 0.2215 0.1832 -0.0128 0.0054  -0.0101 377  GLU B CA  
11812 C C   . GLU B 379  ? 0.2046 0.2435 0.2057 -0.0119 0.0052  -0.0108 377  GLU B C   
11813 O O   . GLU B 379  ? 0.2060 0.2422 0.2076 -0.0121 0.0040  -0.0111 377  GLU B O   
11814 C CB  . GLU B 379  ? 0.1909 0.2280 0.1876 -0.0161 0.0059  -0.0085 377  GLU B CB  
11815 C CG  . GLU B 379  ? 0.2116 0.2453 0.2045 -0.0174 0.0059  -0.0075 377  GLU B CG  
11816 C CD  . GLU B 379  ? 0.2260 0.2528 0.2164 -0.0175 0.0042  -0.0075 377  GLU B CD  
11817 O OE1 . GLU B 379  ? 0.2509 0.2752 0.2424 -0.0168 0.0030  -0.0083 377  GLU B OE1 
11818 O OE2 . GLU B 379  ? 0.2510 0.2745 0.2381 -0.0184 0.0041  -0.0066 377  GLU B OE2 
11819 N N   . ILE B 380  ? 0.1890 0.2333 0.1923 -0.0107 0.0065  -0.0110 378  ILE B N   
11820 C CA  . ILE B 380  ? 0.1792 0.2264 0.1858 -0.0096 0.0062  -0.0117 378  ILE B CA  
11821 C C   . ILE B 380  ? 0.1947 0.2381 0.2011 -0.0071 0.0053  -0.0129 378  ILE B C   
11822 O O   . ILE B 380  ? 0.1881 0.2301 0.1956 -0.0071 0.0042  -0.0133 378  ILE B O   
11823 C CB  . ILE B 380  ? 0.1957 0.2493 0.2047 -0.0083 0.0077  -0.0117 378  ILE B CB  
11824 C CG1 . ILE B 380  ? 0.1845 0.2425 0.1940 -0.0109 0.0088  -0.0103 378  ILE B CG1 
11825 C CG2 . ILE B 380  ? 0.1884 0.2448 0.2007 -0.0070 0.0072  -0.0123 378  ILE B CG2 
11826 C CD1 . ILE B 380  ? 0.2170 0.2755 0.2275 -0.0141 0.0078  -0.0094 378  ILE B CD1 
11827 N N   . LYS B 381  ? 0.1719 0.2135 0.1769 -0.0051 0.0056  -0.0136 379  LYS B N   
11828 C CA  . LYS B 381  ? 0.1729 0.2111 0.1779 -0.0030 0.0048  -0.0147 379  LYS B CA  
11829 C C   . LYS B 381  ? 0.1926 0.2260 0.1966 -0.0039 0.0034  -0.0146 379  LYS B C   
11830 O O   . LYS B 381  ? 0.1880 0.2200 0.1932 -0.0031 0.0026  -0.0152 379  LYS B O   
11831 C CB  . LYS B 381  ? 0.1888 0.2256 0.1921 -0.0011 0.0052  -0.0154 379  LYS B CB  
11832 C CG  . LYS B 381  ? 0.2095 0.2427 0.2128 0.0008  0.0042  -0.0164 379  LYS B CG  
11833 C CD  . LYS B 381  ? 0.1946 0.2267 0.1963 0.0026  0.0046  -0.0172 379  LYS B CD  
11834 C CE  . LYS B 381  ? 0.2131 0.2420 0.2152 0.0044  0.0036  -0.0182 379  LYS B CE  
11835 N NZ  . LYS B 381  ? 0.2134 0.2411 0.2137 0.0059  0.0038  -0.0190 379  LYS B NZ  
11836 N N   . ARG B 382  ? 0.1821 0.2127 0.1837 -0.0056 0.0031  -0.0139 380  ARG B N   
11837 C CA  . ARG B 382  ? 0.1942 0.2198 0.1946 -0.0062 0.0018  -0.0139 380  ARG B CA  
11838 C C   . ARG B 382  ? 0.1894 0.2149 0.1910 -0.0074 0.0012  -0.0138 380  ARG B C   
11839 O O   . ARG B 382  ? 0.2064 0.2290 0.2083 -0.0066 0.0004  -0.0143 380  ARG B O   
11840 C CB  . ARG B 382  ? 0.2211 0.2437 0.2185 -0.0078 0.0015  -0.0129 380  ARG B CB  
11841 C CG  . ARG B 382  ? 0.2856 0.3029 0.2817 -0.0080 0.0002  -0.0128 380  ARG B CG  
11842 C CD  . ARG B 382  ? 0.3245 0.3395 0.3212 -0.0056 -0.0004 -0.0138 380  ARG B CD  
11843 N NE  . ARG B 382  ? 0.4739 0.4841 0.4695 -0.0058 -0.0016 -0.0137 380  ARG B NE  
11844 C CZ  . ARG B 382  ? 0.5846 0.5916 0.5779 -0.0059 -0.0022 -0.0131 380  ARG B CZ  
11845 N NH1 . ARG B 382  ? 0.4990 0.5068 0.4907 -0.0060 -0.0018 -0.0127 380  ARG B NH1 
11846 N NH2 . ARG B 382  ? 0.5744 0.5773 0.5670 -0.0059 -0.0032 -0.0130 380  ARG B NH2 
11847 N N   . ALA B 383  ? 0.1884 0.2171 0.1907 -0.0093 0.0016  -0.0130 381  ALA B N   
11848 C CA  . ALA B 383  ? 0.1709 0.1994 0.1741 -0.0107 0.0008  -0.0130 381  ALA B CA  
11849 C C   . ALA B 383  ? 0.1865 0.2168 0.1920 -0.0088 0.0007  -0.0139 381  ALA B C   
11850 O O   . ALA B 383  ? 0.1925 0.2205 0.1980 -0.0088 -0.0001 -0.0143 381  ALA B O   
11851 C CB  . ALA B 383  ? 0.1938 0.2260 0.1975 -0.0133 0.0012  -0.0120 381  ALA B CB  
11852 N N   . GLN B 384  ? 0.1746 0.2087 0.1818 -0.0070 0.0015  -0.0142 382  GLN B N   
11853 C CA  . GLN B 384  ? 0.1920 0.2273 0.2012 -0.0051 0.0014  -0.0150 382  GLN B CA  
11854 C C   . GLN B 384  ? 0.1873 0.2182 0.1957 -0.0034 0.0008  -0.0158 382  GLN B C   
11855 O O   . GLN B 384  ? 0.1895 0.2192 0.1985 -0.0030 0.0002  -0.0161 382  GLN B O   
11856 C CB  . GLN B 384  ? 0.1768 0.2167 0.1878 -0.0033 0.0024  -0.0152 382  GLN B CB  
11857 C CG  . GLN B 384  ? 0.1676 0.2129 0.1804 -0.0047 0.0029  -0.0144 382  GLN B CG  
11858 C CD  . GLN B 384  ? 0.1842 0.2341 0.1989 -0.0026 0.0040  -0.0147 382  GLN B CD  
11859 O OE1 . GLN B 384  ? 0.2199 0.2683 0.2339 -0.0004 0.0045  -0.0154 382  GLN B OE1 
11860 N NE2 . GLN B 384  ? 0.1824 0.2376 0.1995 -0.0032 0.0043  -0.0141 382  GLN B NE2 
11861 N N   . LEU B 385  ? 0.1880 0.2166 0.1951 -0.0025 0.0010  -0.0160 383  LEU B N   
11862 C CA  . LEU B 385  ? 0.1882 0.2128 0.1948 -0.0011 0.0004  -0.0166 383  LEU B CA  
11863 C C   . LEU B 385  ? 0.2025 0.2236 0.2083 -0.0021 -0.0004 -0.0165 383  LEU B C   
11864 O O   . LEU B 385  ? 0.1983 0.2176 0.2047 -0.0010 -0.0008 -0.0170 383  LEU B O   
11865 C CB  . LEU B 385  ? 0.2072 0.2298 0.2123 -0.0005 0.0004  -0.0166 383  LEU B CB  
11866 C CG  . LEU B 385  ? 0.2590 0.2839 0.2645 0.0011  0.0011  -0.0171 383  LEU B CG  
11867 C CD1 . LEU B 385  ? 0.2682 0.2904 0.2716 0.0014  0.0009  -0.0171 383  LEU B CD1 
11868 C CD2 . LEU B 385  ? 0.3015 0.3264 0.3086 0.0031  0.0010  -0.0179 383  LEU B CD2 
11869 N N   . ASP B 386  ? 0.2011 0.2211 0.2054 -0.0042 -0.0007 -0.0158 384  ASP B N   
11870 C CA  . ASP B 386  ? 0.1894 0.2053 0.1924 -0.0050 -0.0014 -0.0158 384  ASP B CA  
11871 C C   . ASP B 386  ? 0.1906 0.2071 0.1939 -0.0061 -0.0017 -0.0159 384  ASP B C   
11872 O O   . ASP B 386  ? 0.2225 0.2355 0.2245 -0.0067 -0.0023 -0.0160 384  ASP B O   
11873 C CB  . ASP B 386  ? 0.2254 0.2388 0.2260 -0.0067 -0.0017 -0.0150 384  ASP B CB  
11874 C CG  . ASP B 386  ? 0.2897 0.3012 0.2893 -0.0055 -0.0017 -0.0149 384  ASP B CG  
11875 O OD1 . ASP B 386  ? 0.3068 0.3185 0.3076 -0.0035 -0.0017 -0.0156 384  ASP B OD1 
11876 O OD2 . ASP B 386  ? 0.3271 0.3368 0.3247 -0.0067 -0.0019 -0.0142 384  ASP B OD2 
11877 N N   . GLY B 387  ? 0.1905 0.2114 0.1956 -0.0062 -0.0014 -0.0159 385  GLY B N   
11878 C CA  . GLY B 387  ? 0.1974 0.2191 0.2028 -0.0071 -0.0019 -0.0160 385  GLY B CA  
11879 C C   . GLY B 387  ? 0.2362 0.2562 0.2399 -0.0098 -0.0025 -0.0154 385  GLY B C   
11880 O O   . GLY B 387  ? 0.2294 0.2472 0.2321 -0.0106 -0.0031 -0.0158 385  GLY B O   
11881 N N   . LEU B 388  ? 0.2056 0.2265 0.2087 -0.0114 -0.0022 -0.0147 386  LEU B N   
11882 C CA  . LEU B 388  ? 0.2266 0.2453 0.2277 -0.0142 -0.0029 -0.0141 386  LEU B CA  
11883 C C   . LEU B 388  ? 0.2291 0.2519 0.2314 -0.0163 -0.0031 -0.0136 386  LEU B C   
11884 O O   . LEU B 388  ? 0.2123 0.2402 0.2172 -0.0155 -0.0027 -0.0136 386  LEU B O   
11885 C CB  . LEU B 388  ? 0.2139 0.2308 0.2133 -0.0152 -0.0026 -0.0133 386  LEU B CB  
11886 C CG  . LEU B 388  ? 0.2074 0.2200 0.2056 -0.0131 -0.0027 -0.0137 386  LEU B CG  
11887 C CD1 . LEU B 388  ? 0.2560 0.2664 0.2522 -0.0140 -0.0026 -0.0129 386  LEU B CD1 
11888 C CD2 . LEU B 388  ? 0.2528 0.2605 0.2497 -0.0126 -0.0034 -0.0144 386  LEU B CD2 
11889 N N   . ALA B 389  ? 0.2317 0.2522 0.2322 -0.0190 -0.0039 -0.0132 387  ALA B N   
11890 C CA  . ALA B 389  ? 0.2286 0.2523 0.2301 -0.0212 -0.0046 -0.0129 387  ALA B CA  
11891 C C   . ALA B 389  ? 0.2133 0.2438 0.2175 -0.0222 -0.0039 -0.0120 387  ALA B C   
11892 O O   . ALA B 389  ? 0.2555 0.2908 0.2620 -0.0225 -0.0041 -0.0119 387  ALA B O   
11893 C CB  . ALA B 389  ? 0.2701 0.2894 0.2688 -0.0242 -0.0057 -0.0127 387  ALA B CB  
11894 N N   . ASP B 390  ? 0.2302 0.2612 0.2340 -0.0225 -0.0030 -0.0112 388  ASP B N   
11895 C CA  . ASP B 390  ? 0.2234 0.2608 0.2296 -0.0234 -0.0020 -0.0103 388  ASP B CA  
11896 C C   . ASP B 390  ? 0.1862 0.2225 0.1912 -0.0225 -0.0009 -0.0099 388  ASP B C   
11897 O O   . ASP B 390  ? 0.2102 0.2412 0.2129 -0.0213 -0.0011 -0.0104 388  ASP B O   
11898 C CB  . ASP B 390  ? 0.2086 0.2477 0.2148 -0.0273 -0.0027 -0.0092 388  ASP B CB  
11899 C CG  . ASP B 390  ? 0.2557 0.3030 0.2656 -0.0280 -0.0020 -0.0084 388  ASP B CG  
11900 O OD1 . ASP B 390  ? 0.2260 0.2770 0.2374 -0.0265 -0.0005 -0.0082 388  ASP B OD1 
11901 O OD2 . ASP B 390  ? 0.2825 0.3323 0.2937 -0.0302 -0.0030 -0.0081 388  ASP B OD2 
11902 N N   . PHE B 391  ? 0.2048 0.2463 0.2114 -0.0230 0.0003  -0.0091 389  PHE B N   
11903 C CA  . PHE B 391  ? 0.1939 0.2346 0.1990 -0.0225 0.0014  -0.0087 389  PHE B CA  
11904 C C   . PHE B 391  ? 0.1949 0.2325 0.1972 -0.0257 0.0011  -0.0075 389  PHE B C   
11905 O O   . PHE B 391  ? 0.2080 0.2462 0.2105 -0.0287 0.0004  -0.0068 389  PHE B O   
11906 C CB  . PHE B 391  ? 0.1986 0.2463 0.2063 -0.0217 0.0030  -0.0083 389  PHE B CB  
11907 C CG  . PHE B 391  ? 0.1809 0.2315 0.1911 -0.0185 0.0032  -0.0094 389  PHE B CG  
11908 C CD1 . PHE B 391  ? 0.1816 0.2293 0.1909 -0.0155 0.0034  -0.0104 389  PHE B CD1 
11909 C CD2 . PHE B 391  ? 0.2029 0.2587 0.2164 -0.0186 0.0030  -0.0093 389  PHE B CD2 
11910 C CE1 . PHE B 391  ? 0.1859 0.2356 0.1972 -0.0127 0.0035  -0.0114 389  PHE B CE1 
11911 C CE2 . PHE B 391  ? 0.2008 0.2587 0.2164 -0.0156 0.0031  -0.0103 389  PHE B CE2 
11912 C CZ  . PHE B 391  ? 0.1868 0.2415 0.2013 -0.0127 0.0034  -0.0113 389  PHE B CZ  
11913 N N   . PRO B 392  ? 0.1885 0.2225 0.1881 -0.0253 0.0015  -0.0072 390  PRO B N   
11914 C CA  . PRO B 392  ? 0.1729 0.2042 0.1698 -0.0283 0.0014  -0.0058 390  PRO B CA  
11915 C C   . PRO B 392  ? 0.2006 0.2371 0.1982 -0.0297 0.0029  -0.0045 390  PRO B C   
11916 O O   . PRO B 392  ? 0.2105 0.2451 0.2057 -0.0322 0.0030  -0.0032 390  PRO B O   
11917 C CB  . PRO B 392  ? 0.2103 0.2354 0.2041 -0.0265 0.0010  -0.0062 390  PRO B CB  
11918 C CG  . PRO B 392  ? 0.2056 0.2334 0.2010 -0.0231 0.0019  -0.0072 390  PRO B CG  
11919 C CD  . PRO B 392  ? 0.1787 0.2108 0.1776 -0.0220 0.0019  -0.0080 390  PRO B CD  
11920 N N   . VAL B 393  ? 0.1877 0.2307 0.1885 -0.0281 0.0042  -0.0049 391  VAL B N   
11921 C CA  . VAL B 393  ? 0.1887 0.2378 0.1907 -0.0291 0.0059  -0.0038 391  VAL B CA  
11922 C C   . VAL B 393  ? 0.1878 0.2441 0.1943 -0.0293 0.0062  -0.0038 391  VAL B C   
11923 O O   . VAL B 393  ? 0.2018 0.2582 0.2101 -0.0280 0.0052  -0.0049 391  VAL B O   
11924 C CB  . VAL B 393  ? 0.1946 0.2446 0.1957 -0.0262 0.0074  -0.0043 391  VAL B CB  
11925 C CG1 . VAL B 393  ? 0.2026 0.2460 0.1993 -0.0261 0.0069  -0.0041 391  VAL B CG1 
11926 C CG2 . VAL B 393  ? 0.2101 0.2612 0.2133 -0.0224 0.0073  -0.0060 391  VAL B CG2 
11927 N N   . PHE B 394  ? 0.1854 0.2478 0.1936 -0.0311 0.0077  -0.0026 392  PHE B N   
11928 C CA  . PHE B 394  ? 0.1840 0.2542 0.1968 -0.0310 0.0082  -0.0025 392  PHE B CA  
11929 C C   . PHE B 394  ? 0.1952 0.2686 0.2100 -0.0267 0.0092  -0.0038 392  PHE B C   
11930 O O   . PHE B 394  ? 0.1932 0.2637 0.2057 -0.0242 0.0099  -0.0045 392  PHE B O   
11931 C CB  . PHE B 394  ? 0.1780 0.2541 0.1923 -0.0341 0.0095  -0.0007 392  PHE B CB  
11932 C CG  . PHE B 394  ? 0.1839 0.2566 0.1962 -0.0385 0.0084  0.0006  392  PHE B CG  
11933 C CD1 . PHE B 394  ? 0.2082 0.2801 0.2217 -0.0406 0.0064  0.0006  392  PHE B CD1 
11934 C CD2 . PHE B 394  ? 0.1895 0.2591 0.1983 -0.0405 0.0091  0.0018  392  PHE B CD2 
11935 C CE1 . PHE B 394  ? 0.2288 0.2967 0.2400 -0.0447 0.0052  0.0016  392  PHE B CE1 
11936 C CE2 . PHE B 394  ? 0.1882 0.2538 0.1948 -0.0446 0.0079  0.0030  392  PHE B CE2 
11937 C CZ  . PHE B 394  ? 0.2036 0.2682 0.2113 -0.0467 0.0060  0.0029  392  PHE B CZ  
11938 N N   . THR B 395  ? 0.2015 0.2804 0.2204 -0.0258 0.0091  -0.0041 393  THR B N   
11939 C CA  . THR B 395  ? 0.1842 0.2661 0.2051 -0.0217 0.0099  -0.0052 393  THR B CA  
11940 C C   . THR B 395  ? 0.1651 0.2557 0.1897 -0.0210 0.0118  -0.0046 393  THR B C   
11941 O O   . THR B 395  ? 0.2153 0.3082 0.2411 -0.0175 0.0129  -0.0055 393  THR B O   
11942 C CB  . THR B 395  ? 0.1964 0.2772 0.2190 -0.0202 0.0082  -0.0063 393  THR B CB  
11943 O OG1 . THR B 395  ? 0.1993 0.2845 0.2249 -0.0226 0.0073  -0.0055 393  THR B OG1 
11944 C CG2 . THR B 395  ? 0.1960 0.2683 0.2151 -0.0202 0.0066  -0.0071 393  THR B CG2 
11945 N N   . ARG B 396  ? 0.1844 0.2799 0.2108 -0.0243 0.0123  -0.0030 394  ARG B N   
11946 C CA  . ARG B 396  ? 0.2010 0.3052 0.2309 -0.0239 0.0145  -0.0022 394  ARG B CA  
11947 C C   . ARG B 396  ? 0.1920 0.2958 0.2191 -0.0258 0.0162  -0.0011 394  ARG B C   
11948 O O   . ARG B 396  ? 0.2059 0.3062 0.2307 -0.0295 0.0155  0.0000  394  ARG B O   
11949 C CB  . ARG B 396  ? 0.1926 0.3038 0.2272 -0.0263 0.0138  -0.0010 394  ARG B CB  
11950 C CG  . ARG B 396  ? 0.2309 0.3428 0.2681 -0.0246 0.0120  -0.0020 394  ARG B CG  
11951 C CD  . ARG B 396  ? 0.2293 0.3497 0.2718 -0.0264 0.0116  -0.0008 394  ARG B CD  
11952 N NE  . ARG B 396  ? 0.2723 0.3925 0.3166 -0.0251 0.0095  -0.0016 394  ARG B NE  
11953 C CZ  . ARG B 396  ? 0.3145 0.4417 0.3635 -0.0231 0.0095  -0.0016 394  ARG B CZ  
11954 N NH1 . ARG B 396  ? 0.3031 0.4386 0.3558 -0.0222 0.0116  -0.0008 394  ARG B NH1 
11955 N NH2 . ARG B 396  ? 0.2977 0.4235 0.3474 -0.0219 0.0075  -0.0023 394  ARG B NH2 
11956 N N   . LYS B 397  ? 0.2034 0.3107 0.2306 -0.0233 0.0186  -0.0013 395  LYS B N   
11957 C CA  . LYS B 397  ? 0.2160 0.3228 0.2401 -0.0248 0.0205  -0.0003 395  LYS B CA  
11958 C C   . LYS B 397  ? 0.2150 0.3266 0.2410 -0.0294 0.0209  0.0018  395  LYS B C   
11959 O O   . LYS B 397  ? 0.2175 0.3257 0.2401 -0.0324 0.0211  0.0030  395  LYS B O   
11960 C CB  . LYS B 397  ? 0.2584 0.3688 0.2826 -0.0211 0.0230  -0.0011 395  LYS B CB  
11961 C CG  . LYS B 397  ? 0.2719 0.3799 0.2916 -0.0216 0.0248  -0.0006 395  LYS B CG  
11962 C CD  . LYS B 397  ? 0.3094 0.4244 0.3307 -0.0241 0.0270  0.0012  395  LYS B CD  
11963 C CE  . LYS B 397  ? 0.2710 0.3832 0.2872 -0.0244 0.0289  0.0017  395  LYS B CE  
11964 N NZ  . LYS B 397  ? 0.2484 0.3679 0.2663 -0.0271 0.0312  0.0037  395  LYS B NZ  
11965 N N   . ILE B 398  ? 0.2052 0.3245 0.2365 -0.0301 0.0210  0.0025  396  ILE B N   
11966 C CA  . ILE B 398  ? 0.2513 0.3758 0.2849 -0.0347 0.0213  0.0046  396  ILE B CA  
11967 C C   . ILE B 398  ? 0.1997 0.3176 0.2306 -0.0389 0.0188  0.0053  396  ILE B C   
11968 O O   . ILE B 398  ? 0.2253 0.3439 0.2555 -0.0431 0.0192  0.0071  396  ILE B O   
11969 C CB  . ILE B 398  ? 0.2987 0.4329 0.3390 -0.0343 0.0215  0.0050  396  ILE B CB  
11970 C CG1 . ILE B 398  ? 0.3601 0.5016 0.4033 -0.0385 0.0227  0.0073  396  ILE B CG1 
11971 C CG2 . ILE B 398  ? 0.2639 0.3961 0.3059 -0.0345 0.0185  0.0042  396  ILE B CG2 
11972 C CD1 . ILE B 398  ? 0.3921 0.5446 0.4420 -0.0374 0.0238  0.0078  396  ILE B CD1 
11973 N N   . HIS B 399  ? 0.2105 0.3213 0.2395 -0.0378 0.0164  0.0039  397  HIS B N   
11974 C CA  . HIS B 399  ? 0.2172 0.3210 0.2432 -0.0414 0.0142  0.0043  397  HIS B CA  
11975 C C   . HIS B 399  ? 0.1925 0.2896 0.2130 -0.0425 0.0147  0.0049  397  HIS B C   
11976 O O   . HIS B 399  ? 0.2216 0.3159 0.2401 -0.0466 0.0140  0.0063  397  HIS B O   
11977 C CB  . HIS B 399  ? 0.2125 0.3108 0.2378 -0.0394 0.0118  0.0026  397  HIS B CB  
11978 C CG  . HIS B 399  ? 0.2195 0.3234 0.2496 -0.0390 0.0107  0.0023  397  HIS B CG  
11979 N ND1 . HIS B 399  ? 0.2415 0.3422 0.2717 -0.0367 0.0089  0.0008  397  HIS B ND1 
11980 C CD2 . HIS B 399  ? 0.2452 0.3579 0.2802 -0.0407 0.0111  0.0034  397  HIS B CD2 
11981 C CE1 . HIS B 399  ? 0.2315 0.3385 0.2662 -0.0370 0.0082  0.0010  397  HIS B CE1 
11982 N NE2 . HIS B 399  ? 0.2357 0.3502 0.2735 -0.0393 0.0094  0.0026  397  HIS B NE2 
11983 N N   . THR B 400  ? 0.2055 0.2998 0.2233 -0.0390 0.0159  0.0038  398  THR B N   
11984 C CA  . THR B 400  ? 0.2075 0.2962 0.2202 -0.0399 0.0165  0.0044  398  THR B CA  
11985 C C   . THR B 400  ? 0.1902 0.2838 0.2031 -0.0430 0.0185  0.0065  398  THR B C   
11986 O O   . THR B 400  ? 0.2175 0.3067 0.2267 -0.0462 0.0183  0.0079  398  THR B O   
11987 C CB  . THR B 400  ? 0.2068 0.2927 0.2172 -0.0355 0.0174  0.0029  398  THR B CB  
11988 O OG1 . THR B 400  ? 0.1932 0.2731 0.2027 -0.0334 0.0152  0.0013  398  THR B OG1 
11989 C CG2 . THR B 400  ? 0.2251 0.3067 0.2304 -0.0362 0.0183  0.0037  398  THR B CG2 
11990 N N   . ASP B 401  ? 0.2069 0.3097 0.2240 -0.0422 0.0206  0.0069  399  ASP B N   
11991 C CA  . ASP B 401  ? 0.2396 0.3481 0.2574 -0.0451 0.0228  0.0090  399  ASP B CA  
11992 C C   . ASP B 401  ? 0.1995 0.3085 0.2184 -0.0506 0.0215  0.0108  399  ASP B C   
11993 O O   . ASP B 401  ? 0.2369 0.3445 0.2532 -0.0540 0.0222  0.0127  399  ASP B O   
11994 C CB  . ASP B 401  ? 0.2621 0.3811 0.2850 -0.0429 0.0253  0.0089  399  ASP B CB  
11995 C CG  . ASP B 401  ? 0.3036 0.4223 0.3246 -0.0381 0.0272  0.0074  399  ASP B CG  
11996 O OD1 . ASP B 401  ? 0.2912 0.4029 0.3067 -0.0374 0.0272  0.0071  399  ASP B OD1 
11997 O OD2 . ASP B 401  ? 0.3040 0.4294 0.3289 -0.0350 0.0286  0.0066  399  ASP B OD2 
11998 N N   . VAL B 402  ? 0.2154 0.3259 0.2379 -0.0514 0.0194  0.0104  400  VAL B N   
11999 C CA  . VAL B 402  ? 0.2364 0.3466 0.2596 -0.0567 0.0178  0.0120  400  VAL B CA  
12000 C C   . VAL B 402  ? 0.1899 0.2891 0.2071 -0.0587 0.0160  0.0121  400  VAL B C   
12001 O O   . VAL B 402  ? 0.2296 0.3270 0.2449 -0.0632 0.0158  0.0140  400  VAL B O   
12002 C CB  . VAL B 402  ? 0.2108 0.3244 0.2386 -0.0568 0.0158  0.0113  400  VAL B CB  
12003 C CG1 . VAL B 402  ? 0.2641 0.3755 0.2918 -0.0622 0.0136  0.0125  400  VAL B CG1 
12004 C CG2 . VAL B 402  ? 0.2211 0.3463 0.2553 -0.0552 0.0176  0.0115  400  VAL B CG2 
12005 N N   . SER B 403  ? 0.2051 0.2969 0.2193 -0.0555 0.0147  0.0103  401  SER B N   
12006 C CA  . SER B 403  ? 0.2502 0.3316 0.2588 -0.0568 0.0130  0.0103  401  SER B CA  
12007 C C   . SER B 403  ? 0.2002 0.2793 0.2047 -0.0583 0.0146  0.0119  401  SER B C   
12008 O O   . SER B 403  ? 0.2235 0.2972 0.2246 -0.0619 0.0137  0.0132  401  SER B O   
12009 C CB  . SER B 403  ? 0.2098 0.2851 0.2164 -0.0525 0.0118  0.0080  401  SER B CB  
12010 O OG  . SER B 403  ? 0.2240 0.2895 0.2253 -0.0533 0.0104  0.0081  401  SER B OG  
12011 N N   . TYR B 404  ? 0.2227 0.3059 0.2272 -0.0556 0.0171  0.0117  402  TYR B N   
12012 C CA  . TYR B 404  ? 0.2445 0.3258 0.2448 -0.0568 0.0188  0.0132  402  TYR B CA  
12013 C C   . TYR B 404  ? 0.2246 0.3098 0.2259 -0.0620 0.0196  0.0158  402  TYR B C   
12014 O O   . TYR B 404  ? 0.2480 0.3277 0.2449 -0.0651 0.0192  0.0174  402  TYR B O   
12015 C CB  . TYR B 404  ? 0.2445 0.3306 0.2453 -0.0529 0.0214  0.0125  402  TYR B CB  
12016 C CG  . TYR B 404  ? 0.2340 0.3168 0.2294 -0.0531 0.0229  0.0135  402  TYR B CG  
12017 C CD1 . TYR B 404  ? 0.2412 0.3284 0.2363 -0.0564 0.0250  0.0158  402  TYR B CD1 
12018 C CD2 . TYR B 404  ? 0.2445 0.3203 0.2354 -0.0501 0.0223  0.0123  402  TYR B CD2 
12019 C CE1 . TYR B 404  ? 0.2403 0.3245 0.2302 -0.0566 0.0265  0.0168  402  TYR B CE1 
12020 C CE2 . TYR B 404  ? 0.2417 0.3145 0.2276 -0.0503 0.0235  0.0132  402  TYR B CE2 
12021 C CZ  . TYR B 404  ? 0.2715 0.3483 0.2566 -0.0535 0.0256  0.0155  402  TYR B CZ  
12022 O OH  . TYR B 404  ? 0.2721 0.3458 0.2518 -0.0537 0.0268  0.0165  402  TYR B OH  
12023 N N   . ILE B 405  ? 0.2423 0.3370 0.2493 -0.0632 0.0207  0.0164  403  ILE B N   
12024 C CA  . ILE B 405  ? 0.2637 0.3631 0.2721 -0.0683 0.0216  0.0189  403  ILE B CA  
12025 C C   . ILE B 405  ? 0.2293 0.3225 0.2361 -0.0729 0.0188  0.0198  403  ILE B C   
12026 O O   . ILE B 405  ? 0.2724 0.3634 0.2766 -0.0772 0.0190  0.0220  403  ILE B O   
12027 C CB  . ILE B 405  ? 0.2640 0.3756 0.2795 -0.0681 0.0233  0.0193  403  ILE B CB  
12028 C CG1 . ILE B 405  ? 0.3019 0.4189 0.3180 -0.0639 0.0264  0.0186  403  ILE B CG1 
12029 C CG2 . ILE B 405  ? 0.2499 0.3670 0.2677 -0.0738 0.0240  0.0219  403  ILE B CG2 
12030 C CD1 . ILE B 405  ? 0.3976 0.5253 0.4205 -0.0617 0.0278  0.0180  403  ILE B CD1 
12031 N N   . ALA B 406  ? 0.2427 0.3325 0.2506 -0.0719 0.0162  0.0182  404  ALA B N   
12032 C CA  . ALA B 406  ? 0.2918 0.3748 0.2976 -0.0757 0.0134  0.0186  404  ALA B CA  
12033 C C   . ALA B 406  ? 0.2433 0.3154 0.2421 -0.0763 0.0126  0.0190  404  ALA B C   
12034 O O   . ALA B 406  ? 0.2808 0.3480 0.2768 -0.0807 0.0115  0.0206  404  ALA B O   
12035 C CB  . ALA B 406  ? 0.2701 0.3512 0.2778 -0.0738 0.0109  0.0165  404  ALA B CB  
12036 N N   . CYS B 407  ? 0.2552 0.3231 0.2511 -0.0718 0.0130  0.0176  405  CYS B N   
12037 C CA  . CYS B 407  ? 0.2742 0.3322 0.2637 -0.0720 0.0122  0.0180  405  CYS B CA  
12038 C C   . CYS B 407  ? 0.2533 0.3123 0.2401 -0.0746 0.0142  0.0205  405  CYS B C   
12039 O O   . CYS B 407  ? 0.2936 0.3451 0.2755 -0.0772 0.0133  0.0218  405  CYS B O   
12040 C CB  . CYS B 407  ? 0.2411 0.2948 0.2287 -0.0666 0.0119  0.0159  405  CYS B CB  
12041 S SG  . CYS B 407  ? 0.3105 0.3602 0.2997 -0.0643 0.0091  0.0133  405  CYS B SG  
12042 N N   . ALA B 408  ? 0.2301 0.2982 0.2198 -0.0740 0.0171  0.0211  406  ALA B N   
12043 C CA  . ALA B 408  ? 0.2680 0.3379 0.2553 -0.0769 0.0192  0.0236  406  ALA B CA  
12044 C C   . ALA B 408  ? 0.2605 0.3307 0.2483 -0.0830 0.0185  0.0259  406  ALA B C   
12045 O O   . ALA B 408  ? 0.2952 0.3607 0.2786 -0.0862 0.0187  0.0280  406  ALA B O   
12046 C CB  . ALA B 408  ? 0.2902 0.3705 0.2811 -0.0749 0.0226  0.0237  406  ALA B CB  
12047 N N   . ALA B 409  ? 0.2887 0.3638 0.2818 -0.0848 0.0175  0.0256  407  ALA B N   
12048 C CA  . ALA B 409  ? 0.3064 0.3814 0.2999 -0.0909 0.0164  0.0277  407  ALA B CA  
12049 C C   . ALA B 409  ? 0.2975 0.3599 0.2849 -0.0930 0.0138  0.0280  407  ALA B C   
12050 O O   . ALA B 409  ? 0.3610 0.4203 0.3456 -0.0976 0.0137  0.0304  407  ALA B O   
12051 C CB  . ALA B 409  ? 0.2838 0.3655 0.2837 -0.0920 0.0153  0.0270  407  ALA B CB  
12052 N N   . LYS B 410  ? 0.2881 0.3433 0.2735 -0.0895 0.0117  0.0257  408  LYS B N   
12053 C CA  . LYS B 410  ? 0.2739 0.3172 0.2536 -0.0908 0.0092  0.0258  408  LYS B CA  
12054 C C   . LYS B 410  ? 0.3327 0.3703 0.3067 -0.0907 0.0102  0.0273  408  LYS B C   
12055 O O   . LYS B 410  ? 0.3542 0.3846 0.3237 -0.0943 0.0091  0.0290  408  LYS B O   
12056 C CB  . LYS B 410  ? 0.2912 0.3292 0.2706 -0.0865 0.0072  0.0229  408  LYS B CB  
12057 C CG  . LYS B 410  ? 0.3244 0.3499 0.2981 -0.0872 0.0046  0.0227  408  LYS B CG  
12058 C CD  . LYS B 410  ? 0.3463 0.3672 0.3197 -0.0824 0.0031  0.0199  408  LYS B CD  
12059 C CE  . LYS B 410  ? 0.3553 0.3802 0.3333 -0.0819 0.0019  0.0182  408  LYS B CE  
12060 N NZ  . LYS B 410  ? 0.3764 0.3965 0.3532 -0.0862 -0.0004 0.0185  408  LYS B NZ  
12061 N N   . LEU B 411  ? 0.3115 0.3519 0.2851 -0.0866 0.0122  0.0266  409  LEU B N   
12062 C CA  . LEU B 411  ? 0.3213 0.3568 0.2892 -0.0863 0.0132  0.0280  409  LEU B CA  
12063 C C   . LEU B 411  ? 0.3123 0.3512 0.2793 -0.0913 0.0150  0.0312  409  LEU B C   
12064 O O   . LEU B 411  ? 0.3234 0.3551 0.2850 -0.0938 0.0144  0.0330  409  LEU B O   
12065 C CB  . LEU B 411  ? 0.2870 0.3257 0.2550 -0.0811 0.0149  0.0266  409  LEU B CB  
12066 C CG  . LEU B 411  ? 0.3127 0.3449 0.2793 -0.0764 0.0129  0.0240  409  LEU B CG  
12067 C CD1 . LEU B 411  ? 0.3089 0.3457 0.2768 -0.0714 0.0145  0.0223  409  LEU B CD1 
12068 C CD2 . LEU B 411  ? 0.3165 0.3375 0.2766 -0.0768 0.0111  0.0248  409  LEU B CD2 
12069 N N   . LEU B 412  ? 0.3321 0.3820 0.3045 -0.0928 0.0171  0.0318  410  LEU B N   
12070 C CA  . LEU B 412  ? 0.3169 0.3710 0.2888 -0.0975 0.0192  0.0349  410  LEU B CA  
12071 C C   . LEU B 412  ? 0.3420 0.3910 0.3124 -0.1035 0.0173  0.0368  410  LEU B C   
12072 O O   . LEU B 412  ? 0.4038 0.4514 0.3711 -0.1075 0.0183  0.0396  410  LEU B O   
12073 C CB  . LEU B 412  ? 0.3658 0.4333 0.3443 -0.0975 0.0220  0.0351  410  LEU B CB  
12074 C CG  . LEU B 412  ? 0.3403 0.4129 0.3191 -0.0925 0.0248  0.0340  410  LEU B CG  
12075 C CD1 . LEU B 412  ? 0.3939 0.4795 0.3799 -0.0916 0.0271  0.0336  410  LEU B CD1 
12076 C CD2 . LEU B 412  ? 0.3509 0.4210 0.3240 -0.0934 0.0268  0.0360  410  LEU B CD2 
12077 N N   . ALA B 413  ? 0.3322 0.3779 0.3043 -0.1041 0.0145  0.0354  411  ALA B N   
12078 C CA  . ALA B 413  ? 0.3890 0.4282 0.3587 -0.1095 0.0123  0.0370  411  ALA B CA  
12079 C C   . ALA B 413  ? 0.3985 0.4243 0.3607 -0.1092 0.0104  0.0373  411  ALA B C   
12080 O O   . ALA B 413  ? 0.4041 0.4229 0.3632 -0.1135 0.0085  0.0387  411  ALA B O   
12081 C CB  . ALA B 413  ? 0.3692 0.4095 0.3431 -0.1104 0.0099  0.0353  411  ALA B CB  
12082 N N   . ALA B 414  ? 0.3644 0.3864 0.3235 -0.1041 0.0107  0.0360  412  ALA B N   
12083 C CA  . ALA B 414  ? 0.3370 0.3466 0.2893 -0.1031 0.0088  0.0361  412  ALA B CA  
12084 C C   . ALA B 414  ? 0.3976 0.4055 0.3453 -0.1018 0.0105  0.0376  412  ALA B C   
12085 O O   . ALA B 414  ? 0.3676 0.3668 0.3105 -0.0990 0.0092  0.0371  412  ALA B O   
12086 C CB  . ALA B 414  ? 0.3576 0.3622 0.3101 -0.0982 0.0066  0.0329  412  ALA B CB  
12087 N N   . THR B 415  ? 0.3535 0.3693 0.3023 -0.1038 0.0135  0.0395  413  THR B N   
12088 C CA  . THR B 415  ? 0.3508 0.3652 0.2949 -0.1023 0.0152  0.0408  413  THR B CA  
12089 C C   . THR B 415  ? 0.3929 0.3964 0.3299 -0.1052 0.0138  0.0432  413  THR B C   
12090 O O   . THR B 415  ? 0.3883 0.3878 0.3202 -0.1033 0.0143  0.0440  413  THR B O   
12091 C CB  . THR B 415  ? 0.3526 0.3779 0.2993 -0.1040 0.0189  0.0425  413  THR B CB  
12092 O OG1 . THR B 415  ? 0.4109 0.4380 0.3584 -0.1104 0.0193  0.0452  413  THR B OG1 
12093 C CG2 . THR B 415  ? 0.3693 0.4053 0.3230 -0.1008 0.0204  0.0402  413  THR B CG2 
12094 N N   . ASP B 416  ? 0.4003 0.3988 0.3365 -0.1097 0.0119  0.0443  414  ASP B N   
12095 C CA  . ASP B 416  ? 0.4391 0.4258 0.3683 -0.1119 0.0100  0.0462  414  ASP B CA  
12096 C C   . ASP B 416  ? 0.3951 0.3720 0.3209 -0.1073 0.0074  0.0442  414  ASP B C   
12097 O O   . ASP B 416  ? 0.4469 0.4139 0.3664 -0.1079 0.0060  0.0456  414  ASP B O   
12098 C CB  . ASP B 416  ? 0.3774 0.3611 0.3068 -0.1180 0.0086  0.0478  414  ASP B CB  
12099 C CG  . ASP B 416  ? 0.5642 0.5495 0.4986 -0.1177 0.0067  0.0453  414  ASP B CG  
12100 O OD1 . ASP B 416  ? 0.5024 0.4970 0.4427 -0.1150 0.0079  0.0433  414  ASP B OD1 
12101 O OD2 . ASP B 416  ? 0.6105 0.5875 0.5427 -0.1201 0.0041  0.0453  414  ASP B OD2 
12102 N N   . VAL B 417  ? 0.3685 0.3478 0.2982 -0.1028 0.0067  0.0410  415  VAL B N   
12103 C CA  . VAL B 417  ? 0.3460 0.3164 0.2733 -0.0988 0.0041  0.0389  415  VAL B CA  
12104 C C   . VAL B 417  ? 0.3595 0.3325 0.2875 -0.0927 0.0048  0.0369  415  VAL B C   
12105 O O   . VAL B 417  ? 0.3529 0.3185 0.2774 -0.0894 0.0032  0.0362  415  VAL B O   
12106 C CB  . VAL B 417  ? 0.4275 0.3967 0.3583 -0.0992 0.0021  0.0369  415  VAL B CB  
12107 C CG1 . VAL B 417  ? 0.3832 0.3439 0.3118 -0.0949 -0.0003 0.0347  415  VAL B CG1 
12108 C CG2 . VAL B 417  ? 0.4110 0.3767 0.3405 -0.1054 0.0011  0.0389  415  VAL B CG2 
12109 N N   . VAL B 418  ? 0.3339 0.3175 0.2667 -0.0912 0.0071  0.0359  416  VAL B N   
12110 C CA  . VAL B 418  ? 0.3060 0.2927 0.2397 -0.0858 0.0080  0.0340  416  VAL B CA  
12111 C C   . VAL B 418  ? 0.3355 0.3310 0.2701 -0.0864 0.0113  0.0352  416  VAL B C   
12112 O O   . VAL B 418  ? 0.3165 0.3174 0.2526 -0.0906 0.0130  0.0371  416  VAL B O   
12113 C CB  . VAL B 418  ? 0.3176 0.3082 0.2569 -0.0822 0.0074  0.0308  416  VAL B CB  
12114 C CG1 . VAL B 418  ? 0.3196 0.3012 0.2575 -0.0811 0.0043  0.0294  416  VAL B CG1 
12115 C CG2 . VAL B 418  ? 0.3036 0.3038 0.2489 -0.0847 0.0088  0.0306  416  VAL B CG2 
12116 N N   . PHE B 419  ? 0.3071 0.3041 0.2406 -0.0820 0.0122  0.0341  417  PHE B N   
12117 C CA  . PHE B 419  ? 0.2848 0.2898 0.2187 -0.0818 0.0154  0.0348  417  PHE B CA  
12118 C C   . PHE B 419  ? 0.2845 0.2977 0.2241 -0.0780 0.0165  0.0321  417  PHE B C   
12119 O O   . PHE B 419  ? 0.2692 0.2807 0.2085 -0.0733 0.0158  0.0300  417  PHE B O   
12120 C CB  . PHE B 419  ? 0.2880 0.2881 0.2155 -0.0798 0.0155  0.0357  417  PHE B CB  
12121 C CG  . PHE B 419  ? 0.3217 0.3293 0.2489 -0.0790 0.0188  0.0361  417  PHE B CG  
12122 C CD1 . PHE B 419  ? 0.3384 0.3522 0.2663 -0.0830 0.0215  0.0384  417  PHE B CD1 
12123 C CD2 . PHE B 419  ? 0.3153 0.3236 0.2412 -0.0743 0.0192  0.0343  417  PHE B CD2 
12124 C CE1 . PHE B 419  ? 0.3337 0.3545 0.2612 -0.0821 0.0247  0.0388  417  PHE B CE1 
12125 C CE2 . PHE B 419  ? 0.3161 0.3309 0.2412 -0.0734 0.0223  0.0346  417  PHE B CE2 
12126 C CZ  . PHE B 419  ? 0.3067 0.3278 0.2326 -0.0772 0.0251  0.0368  417  PHE B CZ  
12127 N N   . PRO B 420  ? 0.2634 0.2855 0.2086 -0.0797 0.0182  0.0321  418  PRO B N   
12128 C CA  . PRO B 420  ? 0.2806 0.3102 0.2314 -0.0760 0.0191  0.0294  418  PRO B CA  
12129 C C   . PRO B 420  ? 0.2571 0.2919 0.2071 -0.0730 0.0218  0.0290  418  PRO B C   
12130 O O   . PRO B 420  ? 0.2769 0.3148 0.2247 -0.0750 0.0241  0.0310  418  PRO B O   
12131 C CB  . PRO B 420  ? 0.3014 0.3387 0.2580 -0.0795 0.0200  0.0301  418  PRO B CB  
12132 C CG  . PRO B 420  ? 0.2962 0.3278 0.2502 -0.0847 0.0185  0.0324  418  PRO B CG  
12133 C CD  . PRO B 420  ? 0.2646 0.2898 0.2116 -0.0853 0.0188  0.0343  418  PRO B CD  
12134 N N   . GLN B 421  ? 0.2658 0.3012 0.2172 -0.0681 0.0214  0.0263  419  GLN B N   
12135 C CA  . GLN B 421  ? 0.2684 0.3080 0.2189 -0.0647 0.0236  0.0254  419  GLN B CA  
12136 C C   . GLN B 421  ? 0.2502 0.2972 0.2071 -0.0617 0.0244  0.0230  419  GLN B C   
12137 O O   . GLN B 421  ? 0.2430 0.2873 0.2017 -0.0588 0.0224  0.0208  419  GLN B O   
12138 C CB  . GLN B 421  ? 0.2687 0.3003 0.2139 -0.0614 0.0219  0.0244  419  GLN B CB  
12139 C CG  . GLN B 421  ? 0.2818 0.3052 0.2209 -0.0642 0.0206  0.0268  419  GLN B CG  
12140 C CD  . GLN B 421  ? 0.2748 0.2897 0.2097 -0.0611 0.0181  0.0258  419  GLN B CD  
12141 O OE1 . GLN B 421  ? 0.3016 0.3132 0.2385 -0.0591 0.0159  0.0240  419  GLN B OE1 
12142 N NE2 . GLN B 421  ? 0.2793 0.2910 0.2083 -0.0608 0.0186  0.0270  419  GLN B NE2 
12143 N N   . PHE B 422  ? 0.2628 0.3192 0.2232 -0.0623 0.0273  0.0234  420  PHE B N   
12144 C CA  . PHE B 422  ? 0.2395 0.3032 0.2063 -0.0599 0.0279  0.0215  420  PHE B CA  
12145 C C   . PHE B 422  ? 0.2553 0.3217 0.2216 -0.0550 0.0295  0.0195  420  PHE B C   
12146 O O   . PHE B 422  ? 0.2539 0.3262 0.2200 -0.0546 0.0325  0.0200  420  PHE B O   
12147 C CB  . PHE B 422  ? 0.2214 0.2941 0.1931 -0.0633 0.0299  0.0231  420  PHE B CB  
12148 C CG  . PHE B 422  ? 0.2645 0.3344 0.2367 -0.0683 0.0281  0.0249  420  PHE B CG  
12149 C CD1 . PHE B 422  ? 0.2891 0.3557 0.2638 -0.0682 0.0252  0.0236  420  PHE B CD1 
12150 C CD2 . PHE B 422  ? 0.2687 0.3389 0.2387 -0.0730 0.0292  0.0278  420  PHE B CD2 
12151 C CE1 . PHE B 422  ? 0.3158 0.3793 0.2907 -0.0728 0.0235  0.0251  420  PHE B CE1 
12152 C CE2 . PHE B 422  ? 0.2890 0.3561 0.2593 -0.0776 0.0274  0.0294  420  PHE B CE2 
12153 C CZ  . PHE B 422  ? 0.3011 0.3647 0.2737 -0.0775 0.0245  0.0279  420  PHE B CZ  
12154 N N   . ALA B 423  ? 0.2490 0.3107 0.2149 -0.0514 0.0275  0.0172  421  ALA B N   
12155 C CA  . ALA B 423  ? 0.2429 0.3058 0.2081 -0.0467 0.0285  0.0151  421  ALA B CA  
12156 C C   . ALA B 423  ? 0.2673 0.3382 0.2389 -0.0445 0.0297  0.0135  421  ALA B C   
12157 O O   . ALA B 423  ? 0.2989 0.3692 0.2742 -0.0437 0.0277  0.0122  421  ALA B O   
12158 C CB  . ALA B 423  ? 0.2339 0.2884 0.1962 -0.0440 0.0257  0.0135  421  ALA B CB  
12159 N N   . THR B 424  ? 0.2569 0.3351 0.2297 -0.0433 0.0328  0.0135  422  THR B N   
12160 C CA  . THR B 424  ? 0.2471 0.3329 0.2258 -0.0407 0.0340  0.0119  422  THR B CA  
12161 C C   . THR B 424  ? 0.2419 0.3335 0.2197 -0.0385 0.0375  0.0117  422  THR B C   
12162 O O   . THR B 424  ? 0.2739 0.3664 0.2482 -0.0405 0.0395  0.0135  422  THR B O   
12163 C CB  . THR B 424  ? 0.2897 0.3818 0.2745 -0.0438 0.0340  0.0131  422  THR B CB  
12164 O OG1 . THR B 424  ? 0.2735 0.3728 0.2639 -0.0409 0.0350  0.0116  422  THR B OG1 
12165 C CG2 . THR B 424  ? 0.2938 0.3906 0.2782 -0.0479 0.0363  0.0159  422  THR B CG2 
12166 N N   . HIS B 425  ? 0.2535 0.3483 0.2339 -0.0343 0.0382  0.0095  423  HIS B N   
12167 C CA  . HIS B 425  ? 0.2599 0.3612 0.2405 -0.0318 0.0416  0.0089  423  HIS B CA  
12168 C C   . HIS B 425  ? 0.2939 0.4054 0.2816 -0.0318 0.0435  0.0092  423  HIS B C   
12169 O O   . HIS B 425  ? 0.3024 0.4201 0.2912 -0.0293 0.0465  0.0087  423  HIS B O   
12170 C CB  . HIS B 425  ? 0.2626 0.3604 0.2407 -0.0269 0.0413  0.0062  423  HIS B CB  
12171 C CG  . HIS B 425  ? 0.2897 0.3782 0.2608 -0.0266 0.0397  0.0059  423  HIS B CG  
12172 N ND1 . HIS B 425  ? 0.3197 0.4017 0.2894 -0.0239 0.0371  0.0039  423  HIS B ND1 
12173 C CD2 . HIS B 425  ? 0.2852 0.3700 0.2504 -0.0288 0.0401  0.0075  423  HIS B CD2 
12174 C CE1 . HIS B 425  ? 0.3145 0.3895 0.2780 -0.0244 0.0359  0.0042  423  HIS B CE1 
12175 N NE2 . HIS B 425  ? 0.2788 0.3551 0.2393 -0.0272 0.0377  0.0063  423  HIS B NE2 
12176 N N   . ASN B 426  ? 0.2879 0.4012 0.2804 -0.0344 0.0417  0.0101  424  ASN B N   
12177 C CA  . ASN B 426  ? 0.2549 0.3777 0.2547 -0.0345 0.0429  0.0103  424  ASN B CA  
12178 C C   . ASN B 426  ? 0.2651 0.3945 0.2664 -0.0387 0.0451  0.0131  424  ASN B C   
12179 O O   . ASN B 426  ? 0.2539 0.3805 0.2542 -0.0433 0.0438  0.0150  424  ASN B O   
12180 C CB  . ASN B 426  ? 0.2689 0.3897 0.2726 -0.0354 0.0395  0.0098  424  ASN B CB  
12181 C CG  . ASN B 426  ? 0.2827 0.4127 0.2940 -0.0347 0.0401  0.0097  424  ASN B CG  
12182 O OD1 . ASN B 426  ? 0.2990 0.4375 0.3137 -0.0364 0.0424  0.0113  424  ASN B OD1 
12183 N ND2 . ASN B 426  ? 0.2813 0.4098 0.2953 -0.0323 0.0379  0.0080  424  ASN B ND2 
12184 N N   . ALA B 427  ? 0.2890 0.4271 0.2927 -0.0372 0.0487  0.0133  425  ALA B N   
12185 C CA  . ALA B 427  ? 0.3171 0.4624 0.3225 -0.0410 0.0513  0.0160  425  ALA B CA  
12186 C C   . ALA B 427  ? 0.2314 0.3818 0.2432 -0.0449 0.0499  0.0176  425  ALA B C   
12187 O O   . ALA B 427  ? 0.2862 0.4388 0.2981 -0.0498 0.0506  0.0202  425  ALA B O   
12188 C CB  . ALA B 427  ? 0.3253 0.4794 0.3325 -0.0378 0.0554  0.0156  425  ALA B CB  
12189 N N   . GLN B 428  ? 0.2758 0.4280 0.2927 -0.0430 0.0479  0.0162  426  GLN B N   
12190 C CA  . GLN B 428  ? 0.3091 0.4655 0.3317 -0.0468 0.0462  0.0175  426  GLN B CA  
12191 C C   . GLN B 428  ? 0.2693 0.4168 0.2884 -0.0511 0.0430  0.0185  426  GLN B C   
12192 O O   . GLN B 428  ? 0.2981 0.4476 0.3186 -0.0562 0.0427  0.0208  426  GLN B O   
12193 C CB  . GLN B 428  ? 0.2941 0.4543 0.3226 -0.0436 0.0448  0.0158  426  GLN B CB  
12194 C CG  . GLN B 428  ? 0.3286 0.4961 0.3641 -0.0471 0.0437  0.0172  426  GLN B CG  
12195 C CD  . GLN B 428  ? 0.2986 0.4590 0.3326 -0.0514 0.0400  0.0179  426  GLN B CD  
12196 O OE1 . GLN B 428  ? 0.3364 0.4873 0.3663 -0.0501 0.0376  0.0164  426  GLN B OE1 
12197 N NE2 . GLN B 428  ? 0.3250 0.4901 0.3623 -0.0565 0.0397  0.0202  426  GLN B NE2 
12198 N N   . THR B 429  ? 0.2943 0.4317 0.3085 -0.0491 0.0407  0.0168  427  THR B N   
12199 C CA  . THR B 429  ? 0.3334 0.4616 0.3436 -0.0526 0.0378  0.0176  427  THR B CA  
12200 C C   . THR B 429  ? 0.2591 0.3856 0.2650 -0.0566 0.0392  0.0201  427  THR B C   
12201 O O   . THR B 429  ? 0.2807 0.4052 0.2863 -0.0615 0.0379  0.0220  427  THR B O   
12202 C CB  . THR B 429  ? 0.2762 0.3945 0.2818 -0.0492 0.0357  0.0154  427  THR B CB  
12203 O OG1 . THR B 429  ? 0.2777 0.3979 0.2872 -0.0452 0.0347  0.0131  427  THR B OG1 
12204 C CG2 . THR B 429  ? 0.3074 0.4167 0.3097 -0.0524 0.0326  0.0160  427  THR B CG2 
12205 N N   . LEU B 430  ? 0.3204 0.4471 0.3223 -0.0547 0.0419  0.0201  428  LEU B N   
12206 C CA  . LEU B 430  ? 0.2918 0.4168 0.2890 -0.0582 0.0435  0.0225  428  LEU B CA  
12207 C C   . LEU B 430  ? 0.2732 0.4067 0.2747 -0.0628 0.0452  0.0251  428  LEU B C   
12208 O O   . LEU B 430  ? 0.3076 0.4380 0.3069 -0.0678 0.0445  0.0274  428  LEU B O   
12209 C CB  . LEU B 430  ? 0.3176 0.4429 0.3104 -0.0547 0.0464  0.0218  428  LEU B CB  
12210 C CG  . LEU B 430  ? 0.2919 0.4137 0.2779 -0.0571 0.0481  0.0238  428  LEU B CG  
12211 C CD1 . LEU B 430  ? 0.3589 0.4803 0.3409 -0.0524 0.0502  0.0221  428  LEU B CD1 
12212 C CD2 . LEU B 430  ? 0.3674 0.4968 0.3555 -0.0616 0.0508  0.0268  428  LEU B CD2 
12213 N N   . ALA B 431  ? 0.3201 0.4645 0.3279 -0.0613 0.0475  0.0249  429  ALA B N   
12214 C CA  . ALA B 431  ? 0.3385 0.4922 0.3511 -0.0655 0.0494  0.0275  429  ALA B CA  
12215 C C   . ALA B 431  ? 0.3185 0.4706 0.3339 -0.0703 0.0462  0.0287  429  ALA B C   
12216 O O   . ALA B 431  ? 0.3446 0.4984 0.3602 -0.0757 0.0466  0.0313  429  ALA B O   
12217 C CB  . ALA B 431  ? 0.3134 0.4791 0.3329 -0.0624 0.0520  0.0267  429  ALA B CB  
12218 N N   . ALA B 432  ? 0.3242 0.4724 0.3414 -0.0686 0.0429  0.0267  430  ALA B N   
12219 C CA  . ALA B 432  ? 0.2973 0.4433 0.3167 -0.0728 0.0397  0.0275  430  ALA B CA  
12220 C C   . ALA B 432  ? 0.3121 0.4482 0.3251 -0.0770 0.0381  0.0290  430  ALA B C   
12221 O O   . ALA B 432  ? 0.3401 0.4767 0.3541 -0.0825 0.0373  0.0312  430  ALA B O   
12222 C CB  . ALA B 432  ? 0.3009 0.4435 0.3223 -0.0696 0.0367  0.0249  430  ALA B CB  
12223 N N   . ILE B 433  ? 0.3204 0.4471 0.3267 -0.0746 0.0375  0.0280  431  ILE B N   
12224 C CA  . ILE B 433  ? 0.3385 0.4551 0.3384 -0.0780 0.0359  0.0294  431  ILE B CA  
12225 C C   . ILE B 433  ? 0.2892 0.4085 0.2867 -0.0818 0.0386  0.0323  431  ILE B C   
12226 O O   . ILE B 433  ? 0.3026 0.4177 0.2977 -0.0869 0.0375  0.0345  431  ILE B O   
12227 C CB  . ILE B 433  ? 0.3207 0.4272 0.3146 -0.0740 0.0345  0.0274  431  ILE B CB  
12228 C CG1 . ILE B 433  ? 0.3969 0.4997 0.3930 -0.0714 0.0314  0.0249  431  ILE B CG1 
12229 C CG2 . ILE B 433  ? 0.3763 0.4731 0.3630 -0.0770 0.0334  0.0291  431  ILE B CG2 
12230 C CD1 . ILE B 433  ? 0.3998 0.4943 0.3911 -0.0672 0.0302  0.0229  431  ILE B CD1 
12231 N N   . TYR B 434  ? 0.3233 0.4492 0.3210 -0.0794 0.0422  0.0324  432  TYR B N   
12232 C CA  . TYR B 434  ? 0.3326 0.4618 0.3280 -0.0829 0.0452  0.0353  432  TYR B CA  
12233 C C   . TYR B 434  ? 0.3375 0.4730 0.3377 -0.0888 0.0453  0.0379  432  TYR B C   
12234 O O   . TYR B 434  ? 0.3334 0.4658 0.3303 -0.0937 0.0454  0.0405  432  TYR B O   
12235 C CB  . TYR B 434  ? 0.3225 0.4595 0.3188 -0.0789 0.0492  0.0346  432  TYR B CB  
12236 C CG  . TYR B 434  ? 0.3151 0.4580 0.3104 -0.0822 0.0529  0.0375  432  TYR B CG  
12237 C CD1 . TYR B 434  ? 0.3549 0.4909 0.3425 -0.0844 0.0535  0.0392  432  TYR B CD1 
12238 C CD2 . TYR B 434  ? 0.3532 0.5088 0.3552 -0.0831 0.0558  0.0385  432  TYR B CD2 
12239 C CE1 . TYR B 434  ? 0.4174 0.5588 0.4038 -0.0874 0.0570  0.0420  432  TYR B CE1 
12240 C CE2 . TYR B 434  ? 0.3562 0.5177 0.3575 -0.0861 0.0594  0.0413  432  TYR B CE2 
12241 C CZ  . TYR B 434  ? 0.3864 0.5406 0.3797 -0.0884 0.0600  0.0430  432  TYR B CZ  
12242 O OH  . TYR B 434  ? 0.4231 0.5831 0.4154 -0.0915 0.0637  0.0458  432  TYR B OH  
12243 N N   . HIS B 435  ? 0.3553 0.4992 0.3633 -0.0885 0.0450  0.0372  433  HIS B N   
12244 C CA  . HIS B 435  ? 0.3730 0.5233 0.3860 -0.0942 0.0449  0.0396  433  HIS B CA  
12245 C C   . HIS B 435  ? 0.3171 0.4593 0.3290 -0.0981 0.0407  0.0399  433  HIS B C   
12246 O O   . HIS B 435  ? 0.3804 0.5229 0.3925 -0.1041 0.0403  0.0425  433  HIS B O   
12247 C CB  . HIS B 435  ? 0.4058 0.5693 0.4277 -0.0925 0.0465  0.0390  433  HIS B CB  
12248 C CG  . HIS B 435  ? 0.4249 0.5978 0.4483 -0.0905 0.0512  0.0398  433  HIS B CG  
12249 N ND1 . HIS B 435  ? 0.3595 0.5393 0.3842 -0.0949 0.0540  0.0428  433  HIS B ND1 
12250 C CD2 . HIS B 435  ? 0.3650 0.5411 0.3884 -0.0845 0.0536  0.0378  433  HIS B CD2 
12251 C CE1 . HIS B 435  ? 0.4346 0.6218 0.4601 -0.0916 0.0581  0.0427  433  HIS B CE1 
12252 N NE2 . HIS B 435  ? 0.3092 0.4942 0.3338 -0.0852 0.0579  0.0396  433  HIS B NE2 
12253 N N   . MET B 436  ? 0.3186 0.4534 0.3291 -0.0949 0.0376  0.0373  434  MET B N   
12254 C CA  . MET B 436  ? 0.3288 0.4549 0.3375 -0.0982 0.0337  0.0373  434  MET B CA  
12255 C C   . MET B 436  ? 0.3290 0.4456 0.3305 -0.1021 0.0331  0.0394  434  MET B C   
12256 O O   . MET B 436  ? 0.3867 0.4989 0.3874 -0.1070 0.0308  0.0407  434  MET B O   
12257 C CB  . MET B 436  ? 0.3703 0.4897 0.3779 -0.0934 0.0310  0.0341  434  MET B CB  
12258 C CG  . MET B 436  ? 0.3646 0.4738 0.3693 -0.0959 0.0270  0.0337  434  MET B CG  
12259 S SD  . MET B 436  ? 0.4191 0.5206 0.4220 -0.0898 0.0246  0.0300  434  MET B SD  
12260 C CE  . MET B 436  ? 0.3392 0.4511 0.3509 -0.0879 0.0242  0.0285  434  MET B CE  
12261 N N   . ALA B 437  ? 0.3360 0.4491 0.3319 -0.1000 0.0350  0.0397  435  ALA B N   
12262 C CA  . ALA B 437  ? 0.3660 0.4695 0.3545 -0.1031 0.0344  0.0416  435  ALA B CA  
12263 C C   . ALA B 437  ? 0.3914 0.4993 0.3803 -0.1093 0.0363  0.0452  435  ALA B C   
12264 O O   . ALA B 437  ? 0.4533 0.5532 0.4366 -0.1131 0.0353  0.0472  435  ALA B O   
12265 C CB  . ALA B 437  ? 0.3864 0.4851 0.3688 -0.0988 0.0358  0.0408  435  ALA B CB  
12266 N N   . GLY B 438  ? 0.4067 0.5272 0.4021 -0.1105 0.0389  0.0461  436  GLY B N   
12267 C CA  . GLY B 438  ? 0.4063 0.5321 0.4031 -0.1167 0.0406  0.0496  436  GLY B CA  
12268 C C   . GLY B 438  ? 0.5280 0.6553 0.5203 -0.1169 0.0444  0.0516  436  GLY B C   
12269 O O   . GLY B 438  ? 0.4456 0.5695 0.4334 -0.1122 0.0456  0.0503  436  GLY B O   
12270 N N   . LYS B 439  ? 0.5150 0.6474 0.5085 -0.1227 0.0462  0.0549  437  LYS B N   
12271 C CA  . LYS B 439  ? 0.4635 0.5992 0.4537 -0.1235 0.0502  0.0572  437  LYS B CA  
12272 C C   . LYS B 439  ? 0.4827 0.6056 0.4629 -0.1243 0.0493  0.0583  437  LYS B C   
12273 O O   . LYS B 439  ? 0.5985 0.7220 0.5743 -0.1229 0.0523  0.0592  437  LYS B O   
12274 C CB  . LYS B 439  ? 0.4269 0.5721 0.4216 -0.1298 0.0524  0.0606  437  LYS B CB  
12275 N N   . ASP B 440  ? 0.4607 0.5722 0.4371 -0.1265 0.0454  0.0583  438  ASP B N   
12276 C CA  . ASP B 440  ? 0.5062 0.6056 0.4735 -0.1278 0.0443  0.0597  438  ASP B CA  
12277 C C   . ASP B 440  ? 0.4734 0.5655 0.4358 -0.1212 0.0434  0.0569  438  ASP B C   
12278 O O   . ASP B 440  ? 0.4963 0.5851 0.4605 -0.1177 0.0407  0.0540  438  ASP B O   
12279 C CB  . ASP B 440  ? 0.5459 0.6359 0.5112 -0.1327 0.0404  0.0608  438  ASP B CB  
12280 N N   . PHE B 441  ? 0.4484 0.5381 0.4046 -0.1196 0.0455  0.0578  439  PHE B N   
12281 C CA  . PHE B 441  ? 0.4235 0.5063 0.3749 -0.1137 0.0445  0.0553  439  PHE B CA  
12282 C C   . PHE B 441  ? 0.4382 0.5128 0.3804 -0.1146 0.0450  0.0573  439  PHE B C   
12283 O O   . PHE B 441  ? 0.4353 0.5135 0.3753 -0.1178 0.0480  0.0602  439  PHE B O   
12284 C CB  . PHE B 441  ? 0.3905 0.4818 0.3453 -0.1079 0.0471  0.0527  439  PHE B CB  
12285 C CG  . PHE B 441  ? 0.4270 0.5109 0.3772 -0.1021 0.0456  0.0500  439  PHE B CG  
12286 C CD1 . PHE B 441  ? 0.3665 0.4454 0.3184 -0.0992 0.0422  0.0472  439  PHE B CD1 
12287 C CD2 . PHE B 441  ? 0.3786 0.4601 0.3223 -0.1000 0.0475  0.0504  439  PHE B CD2 
12288 C CE1 . PHE B 441  ? 0.3704 0.4425 0.3183 -0.0941 0.0407  0.0448  439  PHE B CE1 
12289 C CE2 . PHE B 441  ? 0.3839 0.4585 0.3234 -0.0949 0.0459  0.0479  439  PHE B CE2 
12290 C CZ  . PHE B 441  ? 0.3908 0.4608 0.3326 -0.0920 0.0425  0.0452  439  PHE B CZ  
12291 N N   . HIS B 442  ? 0.4394 0.5032 0.3762 -0.1114 0.0421  0.0558  440  HIS B N   
12292 C CA  . HIS B 442  ? 0.4096 0.4655 0.3377 -0.1108 0.0423  0.0571  440  HIS B CA  
12293 C C   . HIS B 442  ? 0.3718 0.4214 0.2973 -0.1047 0.0401  0.0539  440  HIS B C   
12294 O O   . HIS B 442  ? 0.3930 0.4405 0.3221 -0.1024 0.0374  0.0514  440  HIS B O   
12295 C CB  . HIS B 442  ? 0.4227 0.4688 0.3456 -0.1159 0.0400  0.0600  440  HIS B CB  
12296 C CG  . HIS B 442  ? 0.4828 0.5214 0.4071 -0.1164 0.0358  0.0588  440  HIS B CG  
12297 N ND1 . HIS B 442  ? 0.5250 0.5535 0.4456 -0.1127 0.0325  0.0569  440  HIS B ND1 
12298 C CD2 . HIS B 442  ? 0.4778 0.5177 0.4070 -0.1202 0.0343  0.0591  440  HIS B CD2 
12299 C CE1 . HIS B 442  ? 0.5181 0.5419 0.4410 -0.1141 0.0294  0.0561  440  HIS B CE1 
12300 N NE2 . HIS B 442  ? 0.5110 0.5413 0.4389 -0.1186 0.0303  0.0574  440  HIS B NE2 
12301 N N   . VAL B 443  ? 0.4074 0.4540 0.3266 -0.1021 0.0412  0.0541  441  VAL B N   
12302 C CA  . VAL B 443  ? 0.3741 0.4140 0.2903 -0.0967 0.0389  0.0514  441  VAL B CA  
12303 C C   . VAL B 443  ? 0.3778 0.4064 0.2915 -0.0976 0.0345  0.0515  441  VAL B C   
12304 O O   . VAL B 443  ? 0.4298 0.4522 0.3392 -0.1018 0.0336  0.0543  441  VAL B O   
12305 C CB  . VAL B 443  ? 0.4361 0.4741 0.3451 -0.0944 0.0406  0.0519  441  VAL B CB  
12306 C CG1 . VAL B 443  ? 0.4143 0.4440 0.3196 -0.0896 0.0376  0.0495  441  VAL B CG1 
12307 C CG2 . VAL B 443  ? 0.4473 0.4965 0.3592 -0.0923 0.0448  0.0509  441  VAL B CG2 
12308 N N   . GLY B 444  ? 0.3708 0.3969 0.2874 -0.0938 0.0320  0.0484  442  GLY B N   
12309 C CA  . GLY B 444  ? 0.3835 0.4000 0.2990 -0.0942 0.0280  0.0481  442  GLY B CA  
12310 C C   . GLY B 444  ? 0.3573 0.3764 0.2795 -0.0961 0.0268  0.0471  442  GLY B C   
12311 O O   . GLY B 444  ? 0.3635 0.3755 0.2857 -0.0954 0.0235  0.0460  442  GLY B O   
12312 N N   . LYS B 445  ? 0.3624 0.3918 0.2903 -0.0984 0.0292  0.0476  443  LYS B N   
12313 C CA  . LYS B 445  ? 0.3662 0.3988 0.3007 -0.0999 0.0279  0.0465  443  LYS B CA  
12314 C C   . LYS B 445  ? 0.3434 0.3784 0.2824 -0.0946 0.0269  0.0428  443  LYS B C   
12315 O O   . LYS B 445  ? 0.3493 0.3792 0.2896 -0.0937 0.0240  0.0412  443  LYS B O   
12316 C CB  . LYS B 445  ? 0.3483 0.3915 0.2878 -0.1041 0.0308  0.0483  443  LYS B CB  
12317 C CG  . LYS B 445  ? 0.3846 0.4302 0.3301 -0.1068 0.0291  0.0478  443  LYS B CG  
12318 C CD  . LYS B 445  ? 0.4635 0.5202 0.4143 -0.1109 0.0318  0.0497  443  LYS B CD  
12319 C CE  . LYS B 445  ? 0.5265 0.5849 0.4828 -0.1141 0.0297  0.0494  443  LYS B CE  
12320 N NZ  . LYS B 445  ? 0.5560 0.6256 0.5178 -0.1184 0.0321  0.0514  443  LYS B NZ  
12321 N N   . TYR B 446  ? 0.3159 0.3584 0.2569 -0.0910 0.0295  0.0414  444  TYR B N   
12322 C CA  . TYR B 446  ? 0.2920 0.3365 0.2365 -0.0856 0.0288  0.0379  444  TYR B CA  
12323 C C   . TYR B 446  ? 0.3012 0.3509 0.2444 -0.0820 0.0317  0.0372  444  TYR B C   
12324 O O   . TYR B 446  ? 0.3114 0.3644 0.2521 -0.0840 0.0344  0.0393  444  TYR B O   
12325 C CB  . TYR B 446  ? 0.3252 0.3770 0.2777 -0.0860 0.0286  0.0366  444  TYR B CB  
12326 C CG  . TYR B 446  ? 0.3783 0.4422 0.3356 -0.0876 0.0321  0.0376  444  TYR B CG  
12327 C CD1 . TYR B 446  ? 0.3227 0.3944 0.2830 -0.0834 0.0345  0.0359  444  TYR B CD1 
12328 C CD2 . TYR B 446  ? 0.3602 0.4276 0.3192 -0.0932 0.0329  0.0403  444  TYR B CD2 
12329 C CE1 . TYR B 446  ? 0.4186 0.5015 0.3835 -0.0846 0.0378  0.0368  444  TYR B CE1 
12330 C CE2 . TYR B 446  ? 0.3897 0.4685 0.3535 -0.0947 0.0362  0.0413  444  TYR B CE2 
12331 C CZ  . TYR B 446  ? 0.3575 0.4441 0.3243 -0.0902 0.0386  0.0395  444  TYR B CZ  
12332 O OH  . TYR B 446  ? 0.4736 0.5720 0.4455 -0.0914 0.0419  0.0406  444  TYR B OH  
12333 N N   . GLU B 447  ? 0.3072 0.3574 0.2519 -0.0769 0.0312  0.0342  445  GLU B N   
12334 C CA  . GLU B 447  ? 0.2990 0.3545 0.2430 -0.0733 0.0339  0.0331  445  GLU B CA  
12335 C C   . GLU B 447  ? 0.2629 0.3238 0.2129 -0.0691 0.0340  0.0301  445  GLU B C   
12336 O O   . GLU B 447  ? 0.2609 0.3201 0.2146 -0.0686 0.0315  0.0287  445  GLU B O   
12337 C CB  . GLU B 447  ? 0.2670 0.3148 0.2037 -0.0708 0.0331  0.0329  445  GLU B CB  
12338 C CG  . GLU B 447  ? 0.2644 0.3049 0.2007 -0.0673 0.0297  0.0305  445  GLU B CG  
12339 C CD  . GLU B 447  ? 0.2947 0.3272 0.2238 -0.0654 0.0284  0.0306  445  GLU B CD  
12340 O OE1 . GLU B 447  ? 0.3126 0.3440 0.2364 -0.0672 0.0299  0.0327  445  GLU B OE1 
12341 O OE2 . GLU B 447  ? 0.3044 0.3319 0.2333 -0.0621 0.0259  0.0285  445  GLU B OE2 
12342 N N   . PHE B 448  ? 0.2778 0.3450 0.2285 -0.0661 0.0367  0.0290  446  PHE B N   
12343 C CA  . PHE B 448  ? 0.2582 0.3287 0.2127 -0.0613 0.0367  0.0259  446  PHE B CA  
12344 C C   . PHE B 448  ? 0.2341 0.2977 0.1834 -0.0573 0.0354  0.0242  446  PHE B C   
12345 O O   . PHE B 448  ? 0.2607 0.3184 0.2035 -0.0581 0.0351  0.0254  446  PHE B O   
12346 C CB  . PHE B 448  ? 0.2989 0.3803 0.2574 -0.0601 0.0404  0.0256  446  PHE B CB  
12347 C CG  . PHE B 448  ? 0.2550 0.3442 0.2197 -0.0637 0.0415  0.0271  446  PHE B CG  
12348 C CD1 . PHE B 448  ? 0.2827 0.3749 0.2539 -0.0631 0.0399  0.0257  446  PHE B CD1 
12349 C CD2 . PHE B 448  ? 0.2851 0.3784 0.2490 -0.0679 0.0439  0.0300  446  PHE B CD2 
12350 C CE1 . PHE B 448  ? 0.2779 0.3773 0.2548 -0.0665 0.0406  0.0272  446  PHE B CE1 
12351 C CE2 . PHE B 448  ? 0.3345 0.4353 0.3045 -0.0714 0.0447  0.0315  446  PHE B CE2 
12352 C CZ  . PHE B 448  ? 0.3101 0.4139 0.2866 -0.0707 0.0429  0.0300  446  PHE B CZ  
12353 N N   . GLN B 449  ? 0.2583 0.3224 0.2105 -0.0531 0.0344  0.0213  447  GLN B N   
12354 C CA  . GLN B 449  ? 0.2598 0.3186 0.2078 -0.0491 0.0334  0.0194  447  GLN B CA  
12355 C C   . GLN B 449  ? 0.2655 0.3299 0.2171 -0.0448 0.0348  0.0168  447  GLN B C   
12356 O O   . GLN B 449  ? 0.2537 0.3242 0.2116 -0.0444 0.0353  0.0160  447  GLN B O   
12357 C CB  . GLN B 449  ? 0.2663 0.3161 0.2130 -0.0484 0.0295  0.0186  447  GLN B CB  
12358 C CG  . GLN B 449  ? 0.2849 0.3283 0.2281 -0.0523 0.0278  0.0210  447  GLN B CG  
12359 C CD  . GLN B 449  ? 0.2739 0.3080 0.2140 -0.0507 0.0244  0.0202  447  GLN B CD  
12360 O OE1 . GLN B 449  ? 0.2968 0.3298 0.2387 -0.0471 0.0231  0.0178  447  GLN B OE1 
12361 N NE2 . GLN B 449  ? 0.2585 0.2858 0.1939 -0.0533 0.0230  0.0223  447  GLN B NE2 
12362 N N   . CYS B 450  ? 0.2348 0.2968 0.1821 -0.0415 0.0352  0.0154  448  CYS B N   
12363 C CA  . CYS B 450  ? 0.2658 0.3318 0.2156 -0.0371 0.0363  0.0127  448  CYS B CA  
12364 C C   . CYS B 450  ? 0.2387 0.2979 0.1836 -0.0338 0.0346  0.0109  448  CYS B C   
12365 O O   . CYS B 450  ? 0.2759 0.3282 0.2154 -0.0349 0.0330  0.0119  448  CYS B O   
12366 C CB  . CYS B 450  ? 0.2494 0.3236 0.1997 -0.0366 0.0404  0.0131  448  CYS B CB  
12367 S SG  . CYS B 450  ? 0.2966 0.3681 0.2381 -0.0365 0.0425  0.0140  448  CYS B SG  
12368 N N   . LEU B 451  ? 0.2560 0.3171 0.2028 -0.0299 0.0350  0.0084  449  LEU B N   
12369 C CA  . LEU B 451  ? 0.2560 0.3114 0.1987 -0.0266 0.0334  0.0064  449  LEU B CA  
12370 C C   . LEU B 451  ? 0.3198 0.3765 0.2572 -0.0252 0.0360  0.0062  449  LEU B C   
12371 O O   . LEU B 451  ? 0.3205 0.3843 0.2598 -0.0246 0.0393  0.0061  449  LEU B O   
12372 C CB  . LEU B 451  ? 0.2960 0.3525 0.2434 -0.0232 0.0324  0.0038  449  LEU B CB  
12373 C CG  . LEU B 451  ? 0.3562 0.4070 0.3005 -0.0198 0.0304  0.0015  449  LEU B CG  
12374 C CD1 . LEU B 451  ? 0.3146 0.3572 0.2554 -0.0211 0.0271  0.0023  449  LEU B CD1 
12375 C CD2 . LEU B 451  ? 0.4284 0.4811 0.3782 -0.0171 0.0296  -0.0007 449  LEU B CD2 
12376 N N   . HIS B 452  ? 0.2656 0.3157 0.1966 -0.0246 0.0346  0.0061  450  HIS B N   
12377 C CA  . HIS B 452  ? 0.3345 0.3848 0.2597 -0.0229 0.0367  0.0055  450  HIS B CA  
12378 C C   . HIS B 452  ? 0.3301 0.3845 0.2578 -0.0189 0.0382  0.0027  450  HIS B C   
12379 O O   . HIS B 452  ? 0.3669 0.4199 0.2981 -0.0167 0.0363  0.0007  450  HIS B O   
12380 C CB  . HIS B 452  ? 0.2845 0.3264 0.2032 -0.0222 0.0339  0.0051  450  HIS B CB  
12381 C CG  . HIS B 452  ? 0.3033 0.3444 0.2159 -0.0198 0.0354  0.0038  450  HIS B CG  
12382 N ND1 . HIS B 452  ? 0.3550 0.3967 0.2618 -0.0213 0.0377  0.0055  450  HIS B ND1 
12383 C CD2 . HIS B 452  ? 0.3252 0.3650 0.2366 -0.0162 0.0351  0.0011  450  HIS B CD2 
12384 C CE1 . HIS B 452  ? 0.3532 0.3939 0.2552 -0.0186 0.0387  0.0037  450  HIS B CE1 
12385 N NE2 . HIS B 452  ? 0.3212 0.3606 0.2258 -0.0154 0.0371  0.0009  450  HIS B NE2 
12386 N N   . GLY B 453  ? 0.4045 0.4637 0.3302 -0.0180 0.0418  0.0026  451  GLY B N   
12387 C CA  . GLY B 453  ? 0.4918 0.5542 0.4188 -0.0139 0.0435  -0.0001 451  GLY B CA  
12388 C C   . GLY B 453  ? 0.5459 0.6143 0.4812 -0.0127 0.0440  -0.0010 451  GLY B C   
12389 O O   . GLY B 453  ? 0.5848 0.6544 0.5217 -0.0091 0.0444  -0.0034 451  GLY B O   
12390 N N   . MET B 454  ? 0.3813 0.4532 0.3217 -0.0158 0.0439  0.0009  452  MET B N   
12391 C CA  . MET B 454  ? 0.3578 0.4360 0.3060 -0.0151 0.0445  0.0004  452  MET B CA  
12392 C C   . MET B 454  ? 0.3944 0.4795 0.3459 -0.0186 0.0467  0.0030  452  MET B C   
12393 O O   . MET B 454  ? 0.3674 0.4606 0.3235 -0.0177 0.0494  0.0029  452  MET B O   
12394 C CB  . MET B 454  ? 0.3162 0.3904 0.2682 -0.0153 0.0407  -0.0002 452  MET B CB  
12395 C CG  . MET B 454  ? 0.3916 0.4720 0.3515 -0.0152 0.0409  -0.0003 452  MET B CG  
12396 S SD  . MET B 454  ? 0.5055 0.5928 0.4686 -0.0107 0.0438  -0.0025 452  MET B SD  
12397 C CE  . MET B 454  ? 0.4839 0.5633 0.4435 -0.0067 0.0414  -0.0055 452  MET B CE  
12398 N N   . GLY B 455  ? 0.3041 0.3860 0.2533 -0.0226 0.0456  0.0054  453  GLY B N   
12399 C CA  . GLY B 455  ? 0.3311 0.4186 0.2835 -0.0266 0.0471  0.0081  453  GLY B CA  
12400 C C   . GLY B 455  ? 0.3797 0.4713 0.3286 -0.0282 0.0507  0.0099  453  GLY B C   
12401 O O   . GLY B 455  ? 0.3559 0.4537 0.3084 -0.0314 0.0525  0.0120  453  GLY B O   
12402 N N   . GLU B 456  ? 0.4124 0.5008 0.3545 -0.0264 0.0519  0.0092  454  GLU B N   
12403 C CA  . GLU B 456  ? 0.3925 0.4844 0.3306 -0.0280 0.0554  0.0110  454  GLU B CA  
12404 C C   . GLU B 456  ? 0.3844 0.4872 0.3277 -0.0275 0.0595  0.0113  454  GLU B C   
12405 O O   . GLU B 456  ? 0.4060 0.5135 0.3499 -0.0311 0.0617  0.0140  454  GLU B O   
12406 C CB  . GLU B 456  ? 0.4451 0.5315 0.3746 -0.0257 0.0559  0.0099  454  GLU B CB  
12407 C CG  . GLU B 456  ? 0.5225 0.5991 0.4459 -0.0274 0.0525  0.0107  454  GLU B CG  
12408 C CD  . GLU B 456  ? 0.5514 0.6216 0.4751 -0.0246 0.0487  0.0082  454  GLU B CD  
12409 O OE1 . GLU B 456  ? 0.5267 0.5999 0.4566 -0.0225 0.0482  0.0064  454  GLU B OE1 
12410 O OE2 . GLU B 456  ? 0.4286 0.4909 0.3463 -0.0244 0.0463  0.0080  454  GLU B OE2 
12411 N N   . PRO B 457  ? 0.3896 0.4968 0.3369 -0.0234 0.0606  0.0089  455  PRO B N   
12412 C CA  . PRO B 457  ? 0.3965 0.5147 0.3492 -0.0228 0.0645  0.0093  455  PRO B CA  
12413 C C   . PRO B 457  ? 0.4005 0.5247 0.3600 -0.0271 0.0645  0.0119  455  PRO B C   
12414 O O   . PRO B 457  ? 0.4151 0.5473 0.3766 -0.0289 0.0679  0.0137  455  PRO B O   
12415 C CB  . PRO B 457  ? 0.4217 0.5416 0.3781 -0.0177 0.0643  0.0062  455  PRO B CB  
12416 C CG  . PRO B 457  ? 0.4262 0.5365 0.3760 -0.0151 0.0621  0.0040  455  PRO B CG  
12417 C CD  . PRO B 457  ? 0.4187 0.5213 0.3651 -0.0188 0.0587  0.0056  455  PRO B CD  
12418 N N   . LEU B 458  ? 0.3596 0.4803 0.3224 -0.0287 0.0608  0.0120  456  LEU B N   
12419 C CA  . LEU B 458  ? 0.3275 0.4532 0.2963 -0.0330 0.0604  0.0143  456  LEU B CA  
12420 C C   . LEU B 458  ? 0.3242 0.4474 0.2887 -0.0381 0.0607  0.0174  456  LEU B C   
12421 O O   . LEU B 458  ? 0.3224 0.4526 0.2896 -0.0414 0.0631  0.0198  456  LEU B O   
12422 C CB  . LEU B 458  ? 0.3190 0.4408 0.2918 -0.0333 0.0563  0.0134  456  LEU B CB  
12423 C CG  . LEU B 458  ? 0.2916 0.4171 0.2701 -0.0378 0.0552  0.0156  456  LEU B CG  
12424 C CD1 . LEU B 458  ? 0.3412 0.4789 0.3266 -0.0379 0.0584  0.0164  456  LEU B CD1 
12425 C CD2 . LEU B 458  ? 0.3340 0.4550 0.3156 -0.0374 0.0512  0.0143  456  LEU B CD2 
12426 N N   . TYR B 459  ? 0.3264 0.4396 0.2841 -0.0388 0.0583  0.0175  457  TYR B N   
12427 C CA  . TYR B 459  ? 0.3072 0.4169 0.2610 -0.0438 0.0579  0.0205  457  TYR B CA  
12428 C C   . TYR B 459  ? 0.3161 0.4283 0.2646 -0.0448 0.0616  0.0222  457  TYR B C   
12429 O O   . TYR B 459  ? 0.3377 0.4495 0.2841 -0.0494 0.0622  0.0251  457  TYR B O   
12430 C CB  . TYR B 459  ? 0.3222 0.4207 0.2716 -0.0445 0.0536  0.0203  457  TYR B CB  
12431 C CG  . TYR B 459  ? 0.3048 0.4024 0.2602 -0.0456 0.0505  0.0200  457  TYR B CG  
12432 C CD1 . TYR B 459  ? 0.2873 0.3863 0.2455 -0.0505 0.0499  0.0224  457  TYR B CD1 
12433 C CD2 . TYR B 459  ? 0.2882 0.3841 0.2466 -0.0419 0.0484  0.0171  457  TYR B CD2 
12434 C CE1 . TYR B 459  ? 0.2786 0.3769 0.2419 -0.0516 0.0471  0.0220  457  TYR B CE1 
12435 C CE2 . TYR B 459  ? 0.2935 0.3888 0.2571 -0.0430 0.0457  0.0168  457  TYR B CE2 
12436 C CZ  . TYR B 459  ? 0.2662 0.3626 0.2321 -0.0478 0.0451  0.0193  457  TYR B CZ  
12437 O OH  . TYR B 459  ? 0.2843 0.3799 0.2550 -0.0489 0.0424  0.0189  457  TYR B OH  
12438 N N   . GLU B 460  ? 0.3237 0.4386 0.2700 -0.0408 0.0643  0.0204  458  GLU B N   
12439 C CA  . GLU B 460  ? 0.3868 0.5060 0.3291 -0.0418 0.0685  0.0220  458  GLU B CA  
12440 C C   . GLU B 460  ? 0.4550 0.5855 0.4041 -0.0442 0.0717  0.0240  458  GLU B C   
12441 O O   . GLU B 460  ? 0.4079 0.5426 0.3546 -0.0465 0.0751  0.0261  458  GLU B O   
12442 C CB  . GLU B 460  ? 0.4133 0.5319 0.3508 -0.0368 0.0705  0.0195  458  GLU B CB  
12443 C CG  . GLU B 460  ? 0.5362 0.6617 0.4796 -0.0322 0.0721  0.0169  458  GLU B CG  
12444 C CD  . GLU B 460  ? 0.6467 0.7699 0.5846 -0.0272 0.0737  0.0141  458  GLU B CD  
12445 O OE1 . GLU B 460  ? 0.5804 0.6960 0.5099 -0.0272 0.0729  0.0141  458  GLU B OE1 
12446 O OE2 . GLU B 460  ? 0.6185 0.7472 0.5603 -0.0232 0.0755  0.0120  458  GLU B OE2 
12447 N N   . GLU B 461  ? 0.3558 0.4915 0.3135 -0.0441 0.0707  0.0234  459  GLU B N   
12448 C CA  . GLU B 461  ? 0.4092 0.5554 0.3742 -0.0471 0.0728  0.0254  459  GLU B CA  
12449 C C   . GLU B 461  ? 0.4160 0.5599 0.3828 -0.0530 0.0703  0.0282  459  GLU B C   
12450 O O   . GLU B 461  ? 0.3705 0.5225 0.3438 -0.0560 0.0714  0.0299  459  GLU B O   
12451 C CB  . GLU B 461  ? 0.3718 0.5253 0.3452 -0.0436 0.0730  0.0234  459  GLU B CB  
12452 C CG  . GLU B 461  ? 0.3663 0.5211 0.3384 -0.0374 0.0749  0.0203  459  GLU B CG  
12453 C CD  . GLU B 461  ? 0.4887 0.6500 0.4582 -0.0365 0.0800  0.0211  459  GLU B CD  
12454 O OE1 . GLU B 461  ? 0.4571 0.6250 0.4287 -0.0405 0.0825  0.0240  459  GLU B OE1 
12455 O OE2 . GLU B 461  ? 0.5233 0.6827 0.4884 -0.0319 0.0816  0.0188  459  GLU B OE2 
12456 N N   . VAL B 462  ? 0.3907 0.5237 0.3518 -0.0546 0.0669  0.0285  460  VAL B N   
12457 C CA  . VAL B 462  ? 0.3503 0.4792 0.3123 -0.0597 0.0640  0.0306  460  VAL B CA  
12458 C C   . VAL B 462  ? 0.3620 0.4841 0.3161 -0.0634 0.0640  0.0332  460  VAL B C   
12459 O O   . VAL B 462  ? 0.3465 0.4706 0.3011 -0.0685 0.0647  0.0363  460  VAL B O   
12460 C CB  . VAL B 462  ? 0.3385 0.4603 0.3021 -0.0582 0.0594  0.0286  460  VAL B CB  
12461 C CG1 . VAL B 462  ? 0.3174 0.4337 0.2809 -0.0634 0.0563  0.0307  460  VAL B CG1 
12462 C CG2 . VAL B 462  ? 0.3406 0.4694 0.3123 -0.0552 0.0593  0.0265  460  VAL B CG2 
12463 N N   . VAL B 463  ? 0.3341 0.4479 0.2804 -0.0608 0.0631  0.0321  461  VAL B N   
12464 C CA  . VAL B 463  ? 0.3066 0.4132 0.2449 -0.0639 0.0628  0.0344  461  VAL B CA  
12465 C C   . VAL B 463  ? 0.3602 0.4732 0.2958 -0.0654 0.0675  0.0365  461  VAL B C   
12466 O O   . VAL B 463  ? 0.4141 0.5334 0.3502 -0.0619 0.0708  0.0351  461  VAL B O   
12467 C CB  . VAL B 463  ? 0.3332 0.4296 0.2643 -0.0604 0.0603  0.0325  461  VAL B CB  
12468 C CG1 . VAL B 463  ? 0.3846 0.4735 0.3072 -0.0633 0.0598  0.0350  461  VAL B CG1 
12469 C CG2 . VAL B 463  ? 0.3479 0.4385 0.2820 -0.0588 0.0558  0.0305  461  VAL B CG2 
12470 N N   . GLY B 464  ? 0.3782 0.4895 0.3108 -0.0707 0.0678  0.0400  462  GLY B N   
12471 C CA  . GLY B 464  ? 0.3660 0.4822 0.2951 -0.0726 0.0722  0.0423  462  GLY B CA  
12472 C C   . GLY B 464  ? 0.4481 0.5733 0.3830 -0.0776 0.0745  0.0453  462  GLY B C   
12473 O O   . GLY B 464  ? 0.4180 0.5496 0.3615 -0.0779 0.0740  0.0447  462  GLY B O   
12474 N N   . ARG B 465  ? 0.5035 0.6293 0.4339 -0.0816 0.0770  0.0486  463  ARG B N   
12475 C CA  . ARG B 465  ? 0.5227 0.6572 0.4583 -0.0867 0.0794  0.0517  463  ARG B CA  
12476 C C   . ARG B 465  ? 0.5271 0.6751 0.4707 -0.0844 0.0832  0.0506  463  ARG B C   
12477 O O   . ARG B 465  ? 0.5824 0.7384 0.5339 -0.0876 0.0837  0.0519  463  ARG B O   
12478 C CB  . ARG B 465  ? 0.6044 0.7373 0.5329 -0.0909 0.0820  0.0553  463  ARG B CB  
12479 N N   . GLY B 466  ? 0.4730 0.6238 0.4148 -0.0789 0.0857  0.0481  464  GLY B N   
12480 C CA  . GLY B 466  ? 0.5055 0.6685 0.4544 -0.0758 0.0892  0.0467  464  GLY B CA  
12481 C C   . GLY B 466  ? 0.5331 0.6986 0.4899 -0.0724 0.0868  0.0438  464  GLY B C   
12482 O O   . GLY B 466  ? 0.4958 0.6716 0.4592 -0.0697 0.0895  0.0426  464  GLY B O   
12483 N N   . LYS B 467  ? 0.4508 0.6071 0.4071 -0.0725 0.0818  0.0426  465  LYS B N   
12484 C CA  . LYS B 467  ? 0.4477 0.6055 0.4111 -0.0697 0.0792  0.0400  465  LYS B CA  
12485 C C   . LYS B 467  ? 0.4759 0.6329 0.4443 -0.0747 0.0759  0.0417  465  LYS B C   
12486 O O   . LYS B 467  ? 0.4476 0.6115 0.4199 -0.0793 0.0776  0.0445  465  LYS B O   
12487 C CB  . LYS B 467  ? 0.4091 0.5572 0.3679 -0.0647 0.0762  0.0366  465  LYS B CB  
12488 C CG  . LYS B 467  ? 0.4668 0.6155 0.4207 -0.0597 0.0791  0.0346  465  LYS B CG  
12489 C CD  . LYS B 467  ? 0.4613 0.6217 0.4220 -0.0562 0.0826  0.0332  465  LYS B CD  
12490 C CE  . LYS B 467  ? 0.4807 0.6421 0.4362 -0.0514 0.0860  0.0314  465  LYS B CE  
12491 N NZ  . LYS B 467  ? 0.5288 0.7000 0.4911 -0.0469 0.0887  0.0293  465  LYS B NZ  
12492 N N   . LEU B 468  ? 0.4035 0.5521 0.3717 -0.0738 0.0714  0.0400  466  LEU B N   
12493 C CA  . LEU B 468  ? 0.3817 0.5280 0.3535 -0.0785 0.0681  0.0415  466  LEU B CA  
12494 C C   . LEU B 468  ? 0.3662 0.5019 0.3307 -0.0827 0.0659  0.0437  466  LEU B C   
12495 O O   . LEU B 468  ? 0.3816 0.5146 0.3481 -0.0871 0.0633  0.0452  466  LEU B O   
12496 C CB  . LEU B 468  ? 0.3758 0.5195 0.3519 -0.0756 0.0644  0.0386  466  LEU B CB  
12497 C CG  . LEU B 468  ? 0.3852 0.5383 0.3686 -0.0711 0.0659  0.0363  466  LEU B CG  
12498 C CD1 . LEU B 468  ? 0.4122 0.5618 0.3994 -0.0691 0.0619  0.0339  466  LEU B CD1 
12499 C CD2 . LEU B 468  ? 0.4154 0.5815 0.4059 -0.0738 0.0691  0.0383  466  LEU B CD2 
12500 N N   . ASP B 469  ? 0.3671 0.4968 0.3232 -0.0815 0.0668  0.0439  467  ASP B N   
12501 C CA  . ASP B 469  ? 0.4519 0.5713 0.4006 -0.0851 0.0649  0.0462  467  ASP B CA  
12502 C C   . ASP B 469  ? 0.3310 0.4406 0.2793 -0.0853 0.0597  0.0450  467  ASP B C   
12503 O O   . ASP B 469  ? 0.3705 0.4746 0.3173 -0.0899 0.0576  0.0472  467  ASP B O   
12504 C CB  . ASP B 469  ? 0.4423 0.5655 0.3910 -0.0916 0.0669  0.0502  467  ASP B CB  
12505 C CG  . ASP B 469  ? 0.5392 0.6532 0.4786 -0.0943 0.0664  0.0526  467  ASP B CG  
12506 O OD1 . ASP B 469  ? 0.5083 0.6148 0.4408 -0.0908 0.0656  0.0512  467  ASP B OD1 
12507 O OD2 . ASP B 469  ? 0.5902 0.7041 0.5289 -0.1001 0.0669  0.0560  467  ASP B OD2 
12508 N N   . ARG B 470  ? 0.3706 0.4778 0.3201 -0.0802 0.0579  0.0416  468  ARG B N   
12509 C CA  . ARG B 470  ? 0.3325 0.4305 0.2816 -0.0794 0.0533  0.0402  468  ARG B CA  
12510 C C   . ARG B 470  ? 0.3400 0.4302 0.2829 -0.0747 0.0519  0.0379  468  ARG B C   
12511 O O   . ARG B 470  ? 0.3401 0.4341 0.2830 -0.0703 0.0539  0.0359  468  ARG B O   
12512 C CB  . ARG B 470  ? 0.3819 0.4846 0.3393 -0.0779 0.0518  0.0381  468  ARG B CB  
12513 C CG  . ARG B 470  ? 0.3478 0.4582 0.3118 -0.0826 0.0525  0.0401  468  ARG B CG  
12514 C CD  . ARG B 470  ? 0.3293 0.4327 0.2907 -0.0883 0.0501  0.0427  468  ARG B CD  
12515 N NE  . ARG B 470  ? 0.3708 0.4814 0.3383 -0.0931 0.0506  0.0446  468  ARG B NE  
12516 C CZ  . ARG B 470  ? 0.4586 0.5748 0.4263 -0.0975 0.0534  0.0477  468  ARG B CZ  
12517 N NH1 . ARG B 470  ? 0.3984 0.5141 0.3604 -0.0977 0.0562  0.0492  468  ARG B NH1 
12518 N NH2 . ARG B 470  ? 0.4534 0.5760 0.4273 -0.1020 0.0534  0.0493  468  ARG B NH2 
12519 N N   . PRO B 471  ? 0.3271 0.4064 0.2648 -0.0754 0.0486  0.0383  469  PRO B N   
12520 C CA  . PRO B 471  ? 0.3314 0.4033 0.2633 -0.0712 0.0471  0.0364  469  PRO B CA  
12521 C C   . PRO B 471  ? 0.2870 0.3584 0.2231 -0.0667 0.0450  0.0329  469  PRO B C   
12522 O O   . PRO B 471  ? 0.2737 0.3475 0.2161 -0.0671 0.0436  0.0321  469  PRO B O   
12523 C CB  . PRO B 471  ? 0.3299 0.3910 0.2562 -0.0741 0.0440  0.0383  469  PRO B CB  
12524 C CG  . PRO B 471  ? 0.3864 0.4479 0.3176 -0.0779 0.0424  0.0394  469  PRO B CG  
12525 C CD  . PRO B 471  ? 0.3447 0.4178 0.2819 -0.0800 0.0458  0.0403  469  PRO B CD  
12526 N N   . CYS B 472  ? 0.2838 0.3518 0.2159 -0.0623 0.0447  0.0308  470  CYS B N   
12527 C CA  . CYS B 472  ? 0.2698 0.3364 0.2048 -0.0578 0.0427  0.0275  470  CYS B CA  
12528 C C   . CYS B 472  ? 0.2883 0.3453 0.2166 -0.0555 0.0402  0.0266  470  CYS B C   
12529 O O   . CYS B 472  ? 0.3008 0.3561 0.2229 -0.0548 0.0416  0.0272  470  CYS B O   
12530 C CB  . CYS B 472  ? 0.3081 0.3830 0.2467 -0.0541 0.0455  0.0254  470  CYS B CB  
12531 S SG  . CYS B 472  ? 0.3272 0.4002 0.2694 -0.0489 0.0430  0.0215  470  CYS B SG  
12532 N N   . ARG B 473  ? 0.2798 0.3308 0.2094 -0.0543 0.0366  0.0253  471  ARG B N   
12533 C CA  . ARG B 473  ? 0.3121 0.3546 0.2365 -0.0517 0.0340  0.0242  471  ARG B CA  
12534 C C   . ARG B 473  ? 0.2745 0.3190 0.2014 -0.0467 0.0338  0.0208  471  ARG B C   
12535 O O   . ARG B 473  ? 0.2987 0.3463 0.2318 -0.0455 0.0332  0.0192  471  ARG B O   
12536 C CB  . ARG B 473  ? 0.2771 0.3118 0.2014 -0.0531 0.0302  0.0247  471  ARG B CB  
12537 C CG  . ARG B 473  ? 0.2798 0.3060 0.1988 -0.0506 0.0274  0.0239  471  ARG B CG  
12538 C CD  . ARG B 473  ? 0.2630 0.2813 0.1812 -0.0523 0.0240  0.0249  471  ARG B CD  
12539 N NE  . ARG B 473  ? 0.2930 0.3104 0.2098 -0.0571 0.0246  0.0280  471  ARG B NE  
12540 C CZ  . ARG B 473  ? 0.3226 0.3357 0.2331 -0.0593 0.0247  0.0305  471  ARG B CZ  
12541 N NH1 . ARG B 473  ? 0.3105 0.3193 0.2150 -0.0572 0.0241  0.0303  471  ARG B NH1 
12542 N NH2 . ARG B 473  ? 0.3235 0.3364 0.2332 -0.0639 0.0254  0.0333  471  ARG B NH2 
12543 N N   . ILE B 474  ? 0.2999 0.3420 0.2216 -0.0441 0.0342  0.0198  472  ILE B N   
12544 C CA  . ILE B 474  ? 0.2610 0.3043 0.1840 -0.0395 0.0341  0.0167  472  ILE B CA  
12545 C C   . ILE B 474  ? 0.2917 0.3272 0.2136 -0.0376 0.0301  0.0153  472  ILE B C   
12546 O O   . ILE B 474  ? 0.3119 0.3406 0.2281 -0.0381 0.0283  0.0163  472  ILE B O   
12547 C CB  . ILE B 474  ? 0.2805 0.3254 0.1981 -0.0376 0.0366  0.0162  472  ILE B CB  
12548 C CG1 . ILE B 474  ? 0.2780 0.3315 0.1974 -0.0392 0.0409  0.0175  472  ILE B CG1 
12549 C CG2 . ILE B 474  ? 0.2844 0.3289 0.2026 -0.0329 0.0360  0.0129  472  ILE B CG2 
12550 C CD1 . ILE B 474  ? 0.3438 0.3986 0.2571 -0.0379 0.0437  0.0174  472  ILE B CD1 
12551 N N   . TYR B 475  ? 0.2686 0.3052 0.1960 -0.0354 0.0288  0.0132  473  TYR B N   
12552 C CA  . TYR B 475  ? 0.2597 0.2901 0.1869 -0.0331 0.0254  0.0115  473  TYR B CA  
12553 C C   . TYR B 475  ? 0.2967 0.3263 0.2205 -0.0295 0.0257  0.0095  473  TYR B C   
12554 O O   . TYR B 475  ? 0.2746 0.3093 0.2008 -0.0272 0.0276  0.0077  473  TYR B O   
12555 C CB  . TYR B 475  ? 0.2836 0.3163 0.2180 -0.0321 0.0243  0.0100  473  TYR B CB  
12556 C CG  . TYR B 475  ? 0.2628 0.2894 0.1979 -0.0303 0.0209  0.0087  473  TYR B CG  
12557 C CD1 . TYR B 475  ? 0.3007 0.3267 0.2362 -0.0266 0.0201  0.0062  473  TYR B CD1 
12558 C CD2 . TYR B 475  ? 0.2690 0.2908 0.2045 -0.0323 0.0185  0.0098  473  TYR B CD2 
12559 C CE1 . TYR B 475  ? 0.2951 0.3162 0.2317 -0.0250 0.0171  0.0050  473  TYR B CE1 
12560 C CE2 . TYR B 475  ? 0.2448 0.2616 0.1814 -0.0304 0.0155  0.0086  473  TYR B CE2 
12561 C CZ  . TYR B 475  ? 0.3174 0.3341 0.2547 -0.0268 0.0149  0.0062  473  TYR B CZ  
12562 O OH  . TYR B 475  ? 0.3343 0.3465 0.2728 -0.0252 0.0121  0.0051  473  TYR B OH  
12563 N N   . ALA B 476  ? 0.2761 0.2992 0.1939 -0.0291 0.0238  0.0099  474  ALA B N   
12564 C CA  . ALA B 476  ? 0.3127 0.3346 0.2255 -0.0266 0.0243  0.0085  474  ALA B CA  
12565 C C   . ALA B 476  ? 0.3152 0.3316 0.2277 -0.0240 0.0209  0.0067  474  ALA B C   
12566 O O   . ALA B 476  ? 0.3030 0.3132 0.2123 -0.0247 0.0182  0.0078  474  ALA B O   
12567 C CB  . ALA B 476  ? 0.3175 0.3367 0.2230 -0.0286 0.0251  0.0108  474  ALA B CB  
12568 N N   . PRO B 477  ? 0.3144 0.3328 0.2302 -0.0209 0.0209  0.0040  475  PRO B N   
12569 C CA  . PRO B 477  ? 0.2849 0.2984 0.2002 -0.0185 0.0177  0.0023  475  PRO B CA  
12570 C C   . PRO B 477  ? 0.2941 0.3035 0.2020 -0.0177 0.0170  0.0022  475  PRO B C   
12571 O O   . PRO B 477  ? 0.3133 0.3249 0.2172 -0.0175 0.0195  0.0022  475  PRO B O   
12572 C CB  . PRO B 477  ? 0.3245 0.3420 0.2445 -0.0157 0.0186  -0.0004 475  PRO B CB  
12573 C CG  . PRO B 477  ? 0.3260 0.3502 0.2507 -0.0169 0.0215  0.0002  475  PRO B CG  
12574 C CD  . PRO B 477  ? 0.3157 0.3412 0.2364 -0.0196 0.0235  0.0026  475  PRO B CD  
12575 N N   . VAL B 478  ? 0.2954 0.2989 0.2016 -0.0172 0.0135  0.0022  476  VAL B N   
12576 C CA  . VAL B 478  ? 0.3089 0.3078 0.2082 -0.0165 0.0121  0.0021  476  VAL B CA  
12577 C C   . VAL B 478  ? 0.3192 0.3148 0.2200 -0.0140 0.0090  0.0001  476  VAL B C   
12578 O O   . VAL B 478  ? 0.3481 0.3415 0.2526 -0.0142 0.0065  0.0004  476  VAL B O   
12579 C CB  . VAL B 478  ? 0.3134 0.3078 0.2082 -0.0190 0.0107  0.0050  476  VAL B CB  
12580 C CG1 . VAL B 478  ? 0.3650 0.3548 0.2525 -0.0181 0.0090  0.0050  476  VAL B CG1 
12581 C CG2 . VAL B 478  ? 0.3296 0.3272 0.2234 -0.0218 0.0137  0.0073  476  VAL B CG2 
12582 N N   . GLY B 479  ? 0.3860 0.3814 0.2840 -0.0119 0.0090  -0.0019 477  GLY B N   
12583 C CA  . GLY B 479  ? 0.4306 0.4227 0.3296 -0.0098 0.0059  -0.0037 477  GLY B CA  
12584 C C   . GLY B 479  ? 0.4180 0.4110 0.3149 -0.0074 0.0068  -0.0064 477  GLY B C   
12585 O O   . GLY B 479  ? 0.3684 0.3646 0.2632 -0.0070 0.0099  -0.0069 477  GLY B O   
12586 N N   . THR B 480  ? 0.4746 0.4647 0.3726 -0.0058 0.0039  -0.0080 478  THR B N   
12587 C CA  . THR B 480  ? 0.5364 0.5256 0.4318 -0.0036 0.0038  -0.0105 478  THR B CA  
12588 C C   . THR B 480  ? 0.5301 0.5235 0.4309 -0.0019 0.0058  -0.0125 478  THR B C   
12589 O O   . THR B 480  ? 0.5192 0.5160 0.4258 -0.0025 0.0070  -0.0120 478  THR B O   
12590 C CB  . THR B 480  ? 0.5293 0.5139 0.4244 -0.0029 -0.0004 -0.0113 478  THR B CB  
12591 O OG1 . THR B 480  ? 0.6366 0.6219 0.5390 -0.0027 -0.0018 -0.0114 478  THR B OG1 
12592 C CG2 . THR B 480  ? 0.4801 0.4606 0.3700 -0.0043 -0.0026 -0.0092 478  THR B CG2 
12593 N N   . HIS B 481  ? 0.5863 0.5790 0.4847 0.0001  0.0060  -0.0149 479  HIS B N   
12594 C CA  . HIS B 481  ? 0.5724 0.5683 0.4753 0.0021  0.0077  -0.0170 479  HIS B CA  
12595 C C   . HIS B 481  ? 0.6179 0.6140 0.5280 0.0023  0.0058  -0.0173 479  HIS B C   
12596 O O   . HIS B 481  ? 0.6204 0.6204 0.5361 0.0026  0.0074  -0.0174 479  HIS B O   
12597 C CB  . HIS B 481  ? 0.5440 0.5378 0.4424 0.0042  0.0078  -0.0195 479  HIS B CB  
12598 C CG  . HIS B 481  ? 0.5798 0.5743 0.4715 0.0045  0.0104  -0.0196 479  HIS B CG  
12599 N ND1 . HIS B 481  ? 0.6467 0.6393 0.5334 0.0065  0.0111  -0.0220 479  HIS B ND1 
12600 C CD2 . HIS B 481  ? 0.5523 0.5489 0.4412 0.0029  0.0128  -0.0177 479  HIS B CD2 
12601 C CE1 . HIS B 481  ? 0.6611 0.6549 0.5422 0.0063  0.0138  -0.0215 479  HIS B CE1 
12602 N NE2 . HIS B 481  ? 0.6565 0.6529 0.5389 0.0041  0.0149  -0.0188 479  HIS B NE2 
12603 N N   . GLU B 482  ? 0.6362 0.6281 0.5462 0.0021  0.0022  -0.0173 480  GLU B N   
12604 C CA  . GLU B 482  ? 0.5408 0.5328 0.4575 0.0024  0.0003  -0.0176 480  GLU B CA  
12605 C C   . GLU B 482  ? 0.5940 0.5884 0.5153 0.0008  0.0010  -0.0156 480  GLU B C   
12606 O O   . GLU B 482  ? 0.6465 0.6435 0.5737 0.0012  0.0016  -0.0160 480  GLU B O   
12607 C CB  . GLU B 482  ? 0.6951 0.6825 0.6106 0.0023  -0.0036 -0.0177 480  GLU B CB  
12608 N N   . THR B 483  ? 0.6269 0.6205 0.5455 -0.0011 0.0010  -0.0134 481  THR B N   
12609 C CA  . THR B 483  ? 0.6495 0.6447 0.5720 -0.0028 0.0014  -0.0115 481  THR B CA  
12610 C C   . THR B 483  ? 0.5834 0.5840 0.5092 -0.0030 0.0047  -0.0115 481  THR B C   
12611 O O   . THR B 483  ? 0.6505 0.6531 0.5818 -0.0034 0.0049  -0.0113 481  THR B O   
12612 C CB  . THR B 483  ? 0.6230 0.6156 0.5413 -0.0048 0.0006  -0.0091 481  THR B CB  
12613 N N   . LEU B 484  ? 0.6186 0.6215 0.5409 -0.0027 0.0074  -0.0119 482  LEU B N   
12614 C CA  . LEU B 484  ? 0.6389 0.6474 0.5643 -0.0030 0.0107  -0.0116 482  LEU B CA  
12615 C C   . LEU B 484  ? 0.5772 0.5884 0.5078 -0.0009 0.0112  -0.0136 482  LEU B C   
12616 O O   . LEU B 484  ? 0.6223 0.6377 0.5579 -0.0013 0.0126  -0.0133 482  LEU B O   
12617 C CB  . LEU B 484  ? 0.6034 0.6140 0.5237 -0.0031 0.0135  -0.0113 482  LEU B CB  
12618 C CG  . LEU B 484  ? 0.5958 0.6064 0.5127 -0.0006 0.0147  -0.0136 482  LEU B CG  
12619 C CD1 . LEU B 484  ? 0.5669 0.5829 0.4878 0.0010  0.0176  -0.0149 482  LEU B CD1 
12620 C CD2 . LEU B 484  ? 0.5693 0.5787 0.4786 -0.0012 0.0159  -0.0129 482  LEU B CD2 
12621 N N   . LEU B 485  ? 0.5461 0.5549 0.4755 0.0012  0.0100  -0.0157 483  LEU B N   
12622 C CA  . LEU B 485  ? 0.6208 0.6316 0.5548 0.0033  0.0104  -0.0176 483  LEU B CA  
12623 C C   . LEU B 485  ? 0.6202 0.6311 0.5603 0.0028  0.0088  -0.0172 483  LEU B C   
12624 O O   . LEU B 485  ? 0.5700 0.5837 0.5147 0.0039  0.0096  -0.0180 483  LEU B O   
12625 C CB  . LEU B 485  ? 0.5500 0.5573 0.4809 0.0054  0.0092  -0.0198 483  LEU B CB  
12626 C CG  . LEU B 485  ? 0.5474 0.5551 0.4729 0.0068  0.0113  -0.0210 483  LEU B CG  
12627 C CD1 . LEU B 485  ? 0.5900 0.5931 0.5122 0.0085  0.0094  -0.0232 483  LEU B CD1 
12628 C CD2 . LEU B 485  ? 0.5846 0.5977 0.5129 0.0081  0.0147  -0.0216 483  LEU B CD2 
12629 N N   . ALA B 486  ? 0.6246 0.6324 0.5647 0.0012  0.0064  -0.0158 484  ALA B N   
12630 C CA  . ALA B 486  ? 0.5512 0.5583 0.4965 0.0010  0.0046  -0.0156 484  ALA B CA  
12631 C C   . ALA B 486  ? 0.6575 0.6687 0.6075 0.0000  0.0062  -0.0148 484  ALA B C   
12632 O O   . ALA B 486  ? 0.6343 0.6459 0.5890 0.0004  0.0054  -0.0152 484  ALA B O   
12633 C CB  . ALA B 486  ? 0.5913 0.5941 0.5350 -0.0003 0.0019  -0.0144 484  ALA B CB  
12634 N N   . TYR B 487  ? 0.6533 0.6675 0.6022 -0.0014 0.0084  -0.0135 485  TYR B N   
12635 C CA  . TYR B 487  ? 0.5858 0.6042 0.5392 -0.0025 0.0098  -0.0127 485  TYR B CA  
12636 C C   . TYR B 487  ? 0.6122 0.6358 0.5653 -0.0025 0.0130  -0.0125 485  TYR B C   
12637 O O   . TYR B 487  ? 0.4963 0.5236 0.4520 -0.0042 0.0143  -0.0112 485  TYR B O   
12638 C CB  . TYR B 487  ? 0.7125 0.7293 0.6665 -0.0051 0.0087  -0.0106 485  TYR B CB  
12639 C CG  . TYR B 487  ? 0.7364 0.7491 0.6922 -0.0049 0.0059  -0.0108 485  TYR B CG  
12640 C CD1 . TYR B 487  ? 0.7406 0.7544 0.7015 -0.0042 0.0054  -0.0116 485  TYR B CD1 
12641 C CD2 . TYR B 487  ? 0.7315 0.7394 0.6839 -0.0053 0.0038  -0.0101 485  TYR B CD2 
12642 C CE1 . TYR B 487  ? 0.7589 0.7693 0.7215 -0.0039 0.0030  -0.0117 485  TYR B CE1 
12643 C CE2 . TYR B 487  ? 0.7235 0.7281 0.6779 -0.0050 0.0014  -0.0102 485  TYR B CE2 
12644 C CZ  . TYR B 487  ? 0.7634 0.7693 0.7229 -0.0042 0.0011  -0.0110 485  TYR B CZ  
12645 O OH  . TYR B 487  ? 0.8059 0.8087 0.7673 -0.0038 -0.0011 -0.0111 485  TYR B OH  
12646 N N   . LEU B 488  ? 0.6204 0.6444 0.5703 -0.0007 0.0142  -0.0138 486  LEU B N   
12647 C CA  . LEU B 488  ? 0.5550 0.5844 0.5049 -0.0003 0.0175  -0.0138 486  LEU B CA  
12648 C C   . LEU B 488  ? 0.5178 0.5520 0.4737 0.0007  0.0186  -0.0144 486  LEU B C   
12649 O O   . LEU B 488  ? 0.4336 0.4733 0.3914 0.0002  0.0210  -0.0137 486  LEU B O   
12650 C CB  . LEU B 488  ? 0.5270 0.5553 0.4720 0.0018  0.0185  -0.0153 486  LEU B CB  
12651 C CG  . LEU B 488  ? 0.5331 0.5667 0.4771 0.0021  0.0221  -0.0151 486  LEU B CG  
12652 C CD1 . LEU B 488  ? 0.6291 0.6646 0.5721 -0.0010 0.0231  -0.0126 486  LEU B CD1 
12653 C CD2 . LEU B 488  ? 0.4407 0.4721 0.3787 0.0041  0.0229  -0.0166 486  LEU B CD2 
12654 N N   . VAL B 489  ? 0.5354 0.5679 0.4945 0.0022  0.0168  -0.0157 487  VAL B N   
12655 C CA  . VAL B 489  ? 0.4356 0.4724 0.4003 0.0033  0.0176  -0.0163 487  VAL B CA  
12656 C C   . VAL B 489  ? 0.4770 0.5175 0.4451 0.0007  0.0182  -0.0144 487  VAL B C   
12657 O O   . VAL B 489  ? 0.5388 0.5850 0.5096 0.0007  0.0203  -0.0141 487  VAL B O   
12658 C CB  . VAL B 489  ? 0.4913 0.5248 0.4584 0.0047  0.0153  -0.0176 487  VAL B CB  
12659 N N   . ARG B 490  ? 0.5412 0.5785 0.5092 -0.0015 0.0163  -0.0132 488  ARG B N   
12660 C CA  . ARG B 490  ? 0.5439 0.5839 0.5149 -0.0042 0.0166  -0.0115 488  ARG B CA  
12661 C C   . ARG B 490  ? 0.5412 0.5849 0.5104 -0.0060 0.0189  -0.0099 488  ARG B C   
12662 O O   . ARG B 490  ? 0.5286 0.5774 0.5013 -0.0074 0.0202  -0.0090 488  ARG B O   
12663 C CB  . ARG B 490  ? 0.5510 0.5858 0.5214 -0.0060 0.0141  -0.0106 488  ARG B CB  
12664 C CG  . ARG B 490  ? 0.5422 0.5786 0.5155 -0.0086 0.0138  -0.0091 488  ARG B CG  
12665 C CD  . ARG B 490  ? 0.5276 0.5582 0.4994 -0.0101 0.0115  -0.0082 488  ARG B CD  
12666 N NE  . ARG B 490  ? 0.5483 0.5758 0.5150 -0.0113 0.0114  -0.0071 488  ARG B NE  
12667 C CZ  . ARG B 490  ? 0.5256 0.5475 0.4896 -0.0113 0.0093  -0.0068 488  ARG B CZ  
12668 N NH1 . ARG B 490  ? 0.4830 0.5017 0.4487 -0.0101 0.0073  -0.0077 488  ARG B NH1 
12669 N NH2 . ARG B 490  ? 0.4503 0.4697 0.4095 -0.0125 0.0093  -0.0056 488  ARG B NH2 
12670 N N   . ARG B 491  ? 0.4827 0.5242 0.4467 -0.0062 0.0195  -0.0096 489  ARG B N   
12671 C CA  . ARG B 491  ? 0.5334 0.5783 0.4954 -0.0081 0.0218  -0.0081 489  ARG B CA  
12672 C C   . ARG B 491  ? 0.5627 0.6145 0.5270 -0.0066 0.0247  -0.0087 489  ARG B C   
12673 O O   . ARG B 491  ? 0.5555 0.6126 0.5218 -0.0084 0.0266  -0.0072 489  ARG B O   
12674 C CB  . ARG B 491  ? 0.6107 0.6514 0.5660 -0.0083 0.0216  -0.0077 489  ARG B CB  
12675 N N   . LEU B 492  ? 0.5939 0.6458 0.5582 -0.0032 0.0251  -0.0108 490  LEU B N   
12676 C CA  . LEU B 492  ? 0.5978 0.6559 0.5642 -0.0012 0.0279  -0.0115 490  LEU B CA  
12677 C C   . LEU B 492  ? 0.6045 0.6678 0.5776 -0.0012 0.0281  -0.0113 490  LEU B C   
12678 O O   . LEU B 492  ? 0.4618 0.5319 0.4377 -0.0012 0.0305  -0.0108 490  LEU B O   
12679 C CB  . LEU B 492  ? 0.5148 0.5706 0.4787 0.0025  0.0280  -0.0139 490  LEU B CB  
12680 N N   . LEU B 493  ? 0.6156 0.6761 0.5915 -0.0012 0.0256  -0.0118 491  LEU B N   
12681 C CA  . LEU B 493  ? 0.4419 0.5069 0.4239 -0.0014 0.0255  -0.0116 491  LEU B CA  
12682 C C   . LEU B 493  ? 0.5952 0.6645 0.5794 -0.0049 0.0263  -0.0094 491  LEU B C   
12683 O O   . LEU B 493  ? 0.6284 0.7034 0.6176 -0.0051 0.0270  -0.0090 491  LEU B O   
12684 C CB  . LEU B 493  ? 0.5640 0.6245 0.5478 -0.0011 0.0226  -0.0123 491  LEU B CB  
12685 C CG  . LEU B 493  ? 0.4710 0.5299 0.4555 0.0025  0.0221  -0.0144 491  LEU B CG  
12686 C CD1 . LEU B 493  ? 0.5301 0.5860 0.5173 0.0024  0.0196  -0.0148 491  LEU B CD1 
12687 C CD2 . LEU B 493  ? 0.5410 0.6060 0.5282 0.0049  0.0243  -0.0151 491  LEU B CD2 
12688 N N   . GLU B 494  ? 0.6028 0.6695 0.5834 -0.0077 0.0261  -0.0079 492  GLU B N   
12689 C CA  . GLU B 494  ? 0.5586 0.6288 0.5408 -0.0113 0.0269  -0.0057 492  GLU B CA  
12690 C C   . GLU B 494  ? 0.5147 0.5925 0.4981 -0.0112 0.0301  -0.0050 492  GLU B C   
12691 O O   . GLU B 494  ? 0.6160 0.6991 0.6028 -0.0136 0.0311  -0.0035 492  GLU B O   
12692 C CB  . GLU B 494  ? 0.4676 0.5324 0.4450 -0.0141 0.0258  -0.0042 492  GLU B CB  
12693 N N   . GLY B 496  ? 0.6586 0.7436 0.6442 -0.0018 0.0340  -0.0093 494  GLY B N   
12694 C CA  . GLY B 496  ? 0.6252 0.7125 0.6118 0.0024  0.0354  -0.0112 494  GLY B CA  
12695 C C   . GLY B 496  ? 0.7519 0.8414 0.7441 0.0041  0.0343  -0.0120 494  GLY B C   
12696 O O   . GLY B 496  ? 0.8130 0.9042 0.8064 0.0077  0.0352  -0.0136 494  GLY B O   
12697 N N   . ALA B 497  ? 0.7561 0.8451 0.7514 0.0016  0.0321  -0.0110 495  ALA B N   
12698 C CA  . ALA B 497  ? 0.6920 0.7833 0.6925 0.0028  0.0310  -0.0115 495  ALA B CA  
12699 C C   . ALA B 497  ? 0.5334 0.6340 0.5390 0.0029  0.0331  -0.0106 495  ALA B C   
12700 O O   . ALA B 497  ? 0.6159 0.7211 0.6218 0.0008  0.0350  -0.0091 495  ALA B O   
12701 C CB  . ALA B 497  ? 0.5570 0.6448 0.5589 0.0000  0.0281  -0.0107 495  ALA B CB  
12702 N N   . ASN B 498  ? 0.5794 0.6828 0.5893 0.0054  0.0327  -0.0115 496  ASN B N   
12703 C CA  . ASN B 498  ? 0.5542 0.6667 0.5693 0.0063  0.0346  -0.0108 496  ASN B CA  
12704 C C   . ASN B 498  ? 0.5514 0.6692 0.5696 0.0020  0.0348  -0.0085 496  ASN B C   
12705 O O   . ASN B 498  ? 0.4859 0.6113 0.5066 0.0017  0.0372  -0.0075 496  ASN B O   
12706 C CB  . ASN B 498  ? 0.5946 0.7084 0.6138 0.0092  0.0334  -0.0118 496  ASN B CB  
12707 N N   . SER B 499  ? 0.4298 0.5436 0.4477 -0.0012 0.0323  -0.0077 497  SER B N   
12708 C CA  . SER B 499  ? 0.4659 0.5837 0.4863 -0.0056 0.0321  -0.0056 497  SER B CA  
12709 C C   . SER B 499  ? 0.3666 0.4832 0.3831 -0.0086 0.0334  -0.0042 497  SER B C   
12710 O O   . SER B 499  ? 0.3927 0.5129 0.4109 -0.0124 0.0336  -0.0023 497  SER B O   
12711 C CB  . SER B 499  ? 0.4272 0.5405 0.4484 -0.0078 0.0289  -0.0054 497  SER B CB  
12712 O OG  . SER B 499  ? 0.4616 0.5659 0.4779 -0.0076 0.0273  -0.0063 497  SER B OG  
12713 N N   . SER B 500  ? 0.4015 0.5129 0.4125 -0.0072 0.0341  -0.0051 498  SER B N   
12714 C CA  . SER B 500  ? 0.3567 0.4659 0.3631 -0.0100 0.0351  -0.0038 498  SER B CA  
12715 C C   . SER B 500  ? 0.4212 0.5385 0.4289 -0.0104 0.0385  -0.0026 498  SER B C   
12716 O O   . SER B 500  ? 0.4763 0.5983 0.4857 -0.0070 0.0406  -0.0036 498  SER B O   
12717 C CB  . SER B 500  ? 0.4451 0.5466 0.4453 -0.0081 0.0346  -0.0051 498  SER B CB  
12718 O OG  . SER B 500  ? 0.5270 0.6209 0.5254 -0.0090 0.0315  -0.0056 498  SER B OG  
12719 N N   . PHE B 501  ? 0.3453 0.4638 0.3520 -0.0145 0.0391  -0.0005 499  PHE B N   
12720 C CA  . PHE B 501  ? 0.4041 0.5300 0.4114 -0.0153 0.0426  0.0008  499  PHE B CA  
12721 C C   . PHE B 501  ? 0.5015 0.6258 0.5039 -0.0120 0.0449  -0.0004 499  PHE B C   
12722 O O   . PHE B 501  ? 0.5497 0.6809 0.5537 -0.0102 0.0480  -0.0004 499  PHE B O   
12723 C CB  . PHE B 501  ? 0.3805 0.5062 0.3863 -0.0206 0.0426  0.0034  499  PHE B CB  
12724 C CG  . PHE B 501  ? 0.3516 0.4853 0.3584 -0.0219 0.0463  0.0051  499  PHE B CG  
12725 C CD1 . PHE B 501  ? 0.4312 0.5634 0.4325 -0.0213 0.0486  0.0052  499  PHE B CD1 
12726 C CD2 . PHE B 501  ? 0.3857 0.5285 0.3989 -0.0240 0.0473  0.0066  499  PHE B CD2 
12727 C CE1 . PHE B 501  ? 0.3943 0.5341 0.3964 -0.0225 0.0522  0.0068  499  PHE B CE1 
12728 C CE2 . PHE B 501  ? 0.4448 0.5955 0.4593 -0.0253 0.0507  0.0083  499  PHE B CE2 
12729 C CZ  . PHE B 501  ? 0.4017 0.5509 0.4106 -0.0245 0.0533  0.0084  499  PHE B CZ  
12730 N N   . VAL B 502  ? 0.5360 0.6514 0.5324 -0.0111 0.0434  -0.0016 500  VAL B N   
12731 C CA  . VAL B 502  ? 0.6659 0.7790 0.6569 -0.0083 0.0453  -0.0028 500  VAL B CA  
12732 C C   . VAL B 502  ? 0.6561 0.7709 0.6486 -0.0032 0.0462  -0.0052 500  VAL B C   
12733 O O   . VAL B 502  ? 0.7087 0.8246 0.6982 -0.0007 0.0487  -0.0061 500  VAL B O   
12734 C CB  . VAL B 502  ? 0.6784 0.7816 0.6626 -0.0091 0.0432  -0.0031 500  VAL B CB  
12735 C CG1 . VAL B 502  ? 0.6081 0.7097 0.5905 -0.0140 0.0426  -0.0006 500  VAL B CG1 
12736 C CG2 . VAL B 502  ? 0.5757 0.6726 0.5603 -0.0075 0.0399  -0.0048 500  VAL B CG2 
12737 N N   . HIS B 503  ? 0.5135 0.6284 0.5105 -0.0017 0.0442  -0.0062 501  HIS B N   
12738 C CA  . HIS B 503  ? 0.5396 0.6570 0.5387 0.0030  0.0452  -0.0082 501  HIS B CA  
12739 C C   . HIS B 503  ? 0.5778 0.7058 0.5831 0.0036  0.0478  -0.0073 501  HIS B C   
12740 O O   . HIS B 503  ? 0.5275 0.6595 0.5333 0.0072  0.0503  -0.0084 501  HIS B O   
12741 C CB  . HIS B 503  ? 0.5791 0.6917 0.5800 0.0046  0.0421  -0.0097 501  HIS B CB  
12742 C CG  . HIS B 503  ? 0.5671 0.6834 0.5717 0.0089  0.0428  -0.0112 501  HIS B CG  
12743 N ND1 . HIS B 503  ? 0.5641 0.6878 0.5755 0.0091  0.0431  -0.0104 501  HIS B ND1 
12744 C CD2 . HIS B 503  ? 0.5538 0.6670 0.5562 0.0132  0.0432  -0.0134 501  HIS B CD2 
12745 C CE1 . HIS B 503  ? 0.4845 0.6096 0.4978 0.0134  0.0436  -0.0121 501  HIS B CE1 
12746 N NE2 . HIS B 503  ? 0.5196 0.6383 0.5274 0.0160  0.0437  -0.0140 501  HIS B NE2 
12747 N N   . ARG B 504  ? 0.4587 0.5914 0.4689 0.0000  0.0471  -0.0053 502  ARG B N   
12748 C CA  . ARG B 504  ? 0.4257 0.5689 0.4424 0.0003  0.0490  -0.0043 502  ARG B CA  
12749 C C   . ARG B 504  ? 0.4797 0.6292 0.4955 0.0000  0.0530  -0.0032 502  ARG B C   
12750 O O   . ARG B 504  ? 0.4574 0.6152 0.4775 0.0023  0.0554  -0.0032 502  ARG B O   
12751 C CB  . ARG B 504  ? 0.4476 0.5936 0.4692 -0.0038 0.0469  -0.0024 502  ARG B CB  
12752 C CG  . ARG B 504  ? 0.4690 0.6107 0.4926 -0.0029 0.0435  -0.0035 502  ARG B CG  
12753 C CD  . ARG B 504  ? 0.3848 0.5260 0.4107 -0.0076 0.0409  -0.0019 502  ARG B CD  
12754 N NE  . ARG B 504  ? 0.3735 0.5242 0.4049 -0.0102 0.0421  0.0002  502  ARG B NE  
12755 C CZ  . ARG B 504  ? 0.4398 0.5981 0.4776 -0.0087 0.0424  0.0002  502  ARG B CZ  
12756 N NH1 . ARG B 504  ? 0.4508 0.6085 0.4901 -0.0042 0.0417  -0.0016 502  ARG B NH1 
12757 N NH2 . ARG B 504  ? 0.3995 0.5662 0.4423 -0.0117 0.0432  0.0022  502  ARG B NH2 
12758 N N   . ILE B 505  ? 0.4679 0.6137 0.4782 -0.0028 0.0536  -0.0022 503  ILE B N   
12759 C CA  . ILE B 505  ? 0.5112 0.6626 0.5201 -0.0033 0.0575  -0.0011 503  ILE B CA  
12760 C C   . ILE B 505  ? 0.5232 0.6759 0.5301 0.0020  0.0603  -0.0032 503  ILE B C   
12761 O O   . ILE B 505  ? 0.4604 0.6208 0.4688 0.0030  0.0639  -0.0026 503  ILE B O   
12762 C CB  . ILE B 505  ? 0.4517 0.5976 0.4543 -0.0073 0.0573  0.0004  503  ILE B CB  
12763 C CG1 . ILE B 505  ? 0.5111 0.6639 0.5130 -0.0089 0.0613  0.0022  503  ILE B CG1 
12764 C CG2 . ILE B 505  ? 0.5715 0.7072 0.5666 -0.0052 0.0560  -0.0015 503  ILE B CG2 
12765 C CD1 . ILE B 505  ? 0.4569 0.6188 0.4656 -0.0126 0.0621  0.0048  503  ILE B CD1 
12766 N N   . ASN B 506  ? 0.4971 0.6422 0.5003 0.0054  0.0586  -0.0056 504  ASN B N   
12767 C CA  . ASN B 506  ? 0.5590 0.7036 0.5594 0.0105  0.0607  -0.0079 504  ASN B CA  
12768 C C   . ASN B 506  ? 0.5866 0.7348 0.5925 0.0146  0.0605  -0.0094 504  ASN B C   
12769 O O   . ASN B 506  ? 0.5835 0.7301 0.5871 0.0192  0.0618  -0.0116 504  ASN B O   
12770 C CB  . ASN B 506  ? 0.5925 0.7262 0.5849 0.0116  0.0591  -0.0097 504  ASN B CB  
12771 C CG  . ASN B 506  ? 0.6095 0.7399 0.5958 0.0082  0.0597  -0.0084 504  ASN B CG  
12772 O OD1 . ASN B 506  ? 0.6304 0.7663 0.6160 0.0071  0.0630  -0.0070 504  ASN B OD1 
12773 N ND2 . ASN B 506  ? 0.7400 0.8613 0.7218 0.0065  0.0566  -0.0086 504  ASN B ND2 
12774 N N   . ASP B 507  ? 0.5430 0.6956 0.5558 0.0132  0.0589  -0.0083 505  ASP B N   
12775 C CA  . ASP B 507  ? 0.5623 0.7189 0.5807 0.0170  0.0586  -0.0094 505  ASP B CA  
12776 C C   . ASP B 507  ? 0.6444 0.8130 0.6688 0.0175  0.0618  -0.0080 505  ASP B C   
12777 O O   . ASP B 507  ? 0.5521 0.7265 0.5810 0.0135  0.0616  -0.0057 505  ASP B O   
12778 C CB  . ASP B 507  ? 0.6118 0.7658 0.6338 0.0154  0.0547  -0.0091 505  ASP B CB  
12779 C CG  . ASP B 507  ? 0.6756 0.8300 0.7010 0.0198  0.0537  -0.0108 505  ASP B CG  
12780 O OD1 . ASP B 507  ? 0.7572 0.9178 0.7853 0.0235  0.0562  -0.0114 505  ASP B OD1 
12781 O OD2 . ASP B 507  ? 0.7728 0.9211 0.7980 0.0197  0.0504  -0.0116 505  ASP B OD2 
12782 N N   . PRO B 508  ? 0.7101 0.8827 0.7350 0.0222  0.0648  -0.0093 506  PRO B N   
12783 C CA  . PRO B 508  ? 0.6359 0.8208 0.6671 0.0228  0.0680  -0.0079 506  PRO B CA  
12784 C C   . PRO B 508  ? 0.6773 0.8687 0.7171 0.0228  0.0662  -0.0070 506  PRO B C   
12785 O O   . PRO B 508  ? 0.6992 0.9013 0.7452 0.0221  0.0682  -0.0053 506  PRO B O   
12786 C CB  . PRO B 508  ? 0.7271 0.9129 0.7558 0.0286  0.0713  -0.0100 506  PRO B CB  
12787 C CG  . PRO B 508  ? 0.7428 0.9166 0.7627 0.0299  0.0701  -0.0122 506  PRO B CG  
12788 C CD  . PRO B 508  ? 0.6339 0.8003 0.6535 0.0271  0.0655  -0.0122 506  PRO B CD  
12789 N N   . LYS B 509  ? 0.6352 0.8207 0.6756 0.0237  0.0626  -0.0081 507  LYS B N   
12790 C CA  . LYS B 509  ? 0.6565 0.8476 0.7045 0.0234  0.0606  -0.0072 507  LYS B CA  
12791 C C   . LYS B 509  ? 0.6970 0.8911 0.7481 0.0172  0.0589  -0.0046 507  LYS B C   
12792 O O   . LYS B 509  ? 0.7471 0.9492 0.8054 0.0162  0.0583  -0.0032 507  LYS B O   
12793 C CB  . LYS B 509  ? 0.6080 0.7915 0.6552 0.0259  0.0572  -0.0090 507  LYS B CB  
12794 N N   . VAL B 510  ? 0.6833 0.8712 0.7292 0.0132  0.0581  -0.0040 508  VAL B N   
12795 C CA  . VAL B 510  ? 0.6043 0.7938 0.6521 0.0072  0.0565  -0.0016 508  VAL B CA  
12796 C C   . VAL B 510  ? 0.5644 0.7625 0.6138 0.0048  0.0600  0.0004  508  VAL B C   
12797 O O   . VAL B 510  ? 0.6034 0.7995 0.6475 0.0052  0.0626  0.0002  508  VAL B O   
12798 C CB  . VAL B 510  ? 0.5163 0.6947 0.5577 0.0041  0.0539  -0.0019 508  VAL B CB  
12799 N N   . SER B 511  ? 0.5224 0.7298 0.5789 0.0023  0.0601  0.0025  509  SER B N   
12800 C CA  . SER B 511  ? 0.5634 0.7799 0.6223 -0.0003 0.0634  0.0046  509  SER B CA  
12801 C C   . SER B 511  ? 0.5842 0.7971 0.6399 -0.0066 0.0625  0.0066  509  SER B C   
12802 O O   . SER B 511  ? 0.5579 0.7624 0.6106 -0.0092 0.0591  0.0065  509  SER B O   
12803 C CB  . SER B 511  ? 0.5748 0.8035 0.6433 -0.0006 0.0638  0.0062  509  SER B CB  
12804 O OG  . SER B 511  ? 0.5865 0.8155 0.6579 -0.0059 0.0606  0.0079  509  SER B OG  
12805 N N   . ILE B 512  ? 0.4922 0.7118 0.5485 -0.0091 0.0658  0.0086  510  ILE B N   
12806 C CA  . ILE B 512  ? 0.5078 0.7246 0.5612 -0.0153 0.0651  0.0108  510  ILE B CA  
12807 C C   . ILE B 512  ? 0.5636 0.7835 0.6227 -0.0199 0.0621  0.0125  510  ILE B C   
12808 O O   . ILE B 512  ? 0.4895 0.7026 0.5455 -0.0244 0.0595  0.0134  510  ILE B O   
12809 C CB  . ILE B 512  ? 0.4614 0.6845 0.5137 -0.0167 0.0696  0.0124  510  ILE B CB  
12810 C CG1 . ILE B 512  ? 0.4708 0.6887 0.5159 -0.0123 0.0721  0.0104  510  ILE B CG1 
12811 C CG2 . ILE B 512  ? 0.4754 0.6963 0.5253 -0.0235 0.0689  0.0150  510  ILE B CG2 
12812 C CD1 . ILE B 512  ? 0.4944 0.7189 0.5383 -0.0125 0.0769  0.0117  510  ILE B CD1 
12813 N N   . ASP B 513  ? 0.4989 0.7287 0.5661 -0.0188 0.0622  0.0130  511  ASP B N   
12814 C CA  . ASP B 513  ? 0.5200 0.7525 0.5926 -0.0229 0.0590  0.0145  511  ASP B CA  
12815 C C   . ASP B 513  ? 0.4702 0.6917 0.5394 -0.0231 0.0545  0.0130  511  ASP B C   
12816 O O   . ASP B 513  ? 0.4965 0.7142 0.5651 -0.0280 0.0518  0.0141  511  ASP B O   
12817 C CB  . ASP B 513  ? 0.5482 0.7926 0.6299 -0.0205 0.0595  0.0148  511  ASP B CB  
12818 C CG  . ASP B 513  ? 0.6385 0.8953 0.7252 -0.0221 0.0634  0.0170  511  ASP B CG  
12819 O OD1 . ASP B 513  ? 0.5820 0.8400 0.6678 -0.0276 0.0640  0.0193  511  ASP B OD1 
12820 O OD2 . ASP B 513  ? 0.7371 1.0026 0.8286 -0.0177 0.0658  0.0166  511  ASP B OD2 
12821 N N   . GLU B 514  ? 0.4678 0.6841 0.5348 -0.0178 0.0539  0.0104  512  GLU B N   
12822 C CA  . GLU B 514  ? 0.4829 0.6886 0.5464 -0.0177 0.0500  0.0089  512  GLU B CA  
12823 C C   . GLU B 514  ? 0.4692 0.6648 0.5252 -0.0210 0.0491  0.0092  512  GLU B C   
12824 O O   . GLU B 514  ? 0.4347 0.6242 0.4893 -0.0242 0.0458  0.0094  512  GLU B O   
12825 C CB  . GLU B 514  ? 0.4913 0.6931 0.5532 -0.0114 0.0499  0.0062  512  GLU B CB  
12826 C CG  . GLU B 514  ? 0.6467 0.8578 0.7154 -0.0073 0.0510  0.0058  512  GLU B CG  
12827 C CD  . GLU B 514  ? 0.6932 0.8999 0.7596 -0.0010 0.0513  0.0031  512  GLU B CD  
12828 O OE1 . GLU B 514  ? 0.7502 0.9471 0.8123 -0.0002 0.0488  0.0016  512  GLU B OE1 
12829 O OE2 . GLU B 514  ? 0.7096 0.9228 0.7786 0.0031  0.0542  0.0026  512  GLU B OE2 
12830 N N   . LEU B 515  ? 0.4295 0.6234 0.4806 -0.0203 0.0519  0.0091  513  LEU B N   
12831 C CA  . LEU B 515  ? 0.4079 0.5919 0.4515 -0.0230 0.0511  0.0093  513  LEU B CA  
12832 C C   . LEU B 515  ? 0.3929 0.5777 0.4369 -0.0294 0.0502  0.0119  513  LEU B C   
12833 O O   . LEU B 515  ? 0.4040 0.5799 0.4431 -0.0322 0.0481  0.0121  513  LEU B O   
12834 C CB  . LEU B 515  ? 0.3877 0.5701 0.4258 -0.0205 0.0544  0.0086  513  LEU B CB  
12835 C CG  . LEU B 515  ? 0.4076 0.5868 0.4434 -0.0143 0.0550  0.0058  513  LEU B CG  
12836 C CD1 . LEU B 515  ? 0.4547 0.6348 0.4861 -0.0123 0.0588  0.0055  513  LEU B CD1 
12837 C CD2 . LEU B 515  ? 0.4201 0.5877 0.4512 -0.0135 0.0516  0.0041  513  LEU B CD2 
12838 N N   . ILE B 516  ? 0.3544 0.5497 0.4042 -0.0319 0.0519  0.0140  514  ILE B N   
12839 C CA  . ILE B 516  ? 0.3270 0.5235 0.3775 -0.0384 0.0512  0.0166  514  ILE B CA  
12840 C C   . ILE B 516  ? 0.2980 0.4956 0.3534 -0.0411 0.0477  0.0171  514  ILE B C   
12841 O O   . ILE B 516  ? 0.3550 0.5540 0.4116 -0.0467 0.0467  0.0193  514  ILE B O   
12842 C CB  . ILE B 516  ? 0.3876 0.5943 0.4410 -0.0404 0.0551  0.0189  514  ILE B CB  
12843 C CG1 . ILE B 516  ? 0.3522 0.5716 0.4147 -0.0389 0.0562  0.0193  514  ILE B CG1 
12844 C CG2 . ILE B 516  ? 0.4274 0.6328 0.4754 -0.0375 0.0587  0.0183  514  ILE B CG2 
12845 C CD1 . ILE B 516  ? 0.4316 0.6622 0.4977 -0.0407 0.0602  0.0215  514  ILE B CD1 
12846 N N   . ALA B 517  ? 0.3741 0.5713 0.4322 -0.0375 0.0457  0.0152  515  ALA B N   
12847 C CA  . ALA B 517  ? 0.3999 0.5968 0.4617 -0.0399 0.0420  0.0155  515  ALA B CA  
12848 C C   . ALA B 517  ? 0.3406 0.5276 0.3972 -0.0445 0.0393  0.0160  515  ALA B C   
12849 O O   . ALA B 517  ? 0.3659 0.5433 0.4159 -0.0435 0.0389  0.0150  515  ALA B O   
12850 C CB  . ALA B 517  ? 0.3662 0.5608 0.4293 -0.0350 0.0401  0.0131  515  ALA B CB  
12851 N N   . ASP B 518  ? 0.3263 0.5157 0.3861 -0.0494 0.0374  0.0177  516  ASP B N   
12852 C CA  . ASP B 518  ? 0.3450 0.5255 0.4003 -0.0540 0.0347  0.0184  516  ASP B CA  
12853 C C   . ASP B 518  ? 0.2975 0.4704 0.3514 -0.0523 0.0311  0.0164  516  ASP B C   
12854 O O   . ASP B 518  ? 0.2968 0.4738 0.3556 -0.0523 0.0293  0.0161  516  ASP B O   
12855 C CB  . ASP B 518  ? 0.3150 0.5013 0.3741 -0.0602 0.0342  0.0210  516  ASP B CB  
12856 C CG  . ASP B 518  ? 0.4082 0.5851 0.4624 -0.0652 0.0316  0.0218  516  ASP B CG  
12857 O OD1 . ASP B 518  ? 0.3269 0.4929 0.3751 -0.0638 0.0301  0.0204  516  ASP B OD1 
12858 O OD2 . ASP B 518  ? 0.4225 0.6029 0.4789 -0.0706 0.0311  0.0240  516  ASP B OD2 
12859 N N   . PRO B 519  ? 0.2588 0.4209 0.3063 -0.0509 0.0301  0.0150  517  PRO B N   
12860 C CA  . PRO B 519  ? 0.3193 0.4743 0.3656 -0.0492 0.0268  0.0131  517  PRO B CA  
12861 C C   . PRO B 519  ? 0.2447 0.3983 0.2924 -0.0538 0.0238  0.0140  517  PRO B C   
12862 O O   . PRO B 519  ? 0.2674 0.4202 0.3171 -0.0526 0.0214  0.0128  517  PRO B O   
12863 C CB  . PRO B 519  ? 0.2934 0.4374 0.3324 -0.0477 0.0266  0.0120  517  PRO B CB  
12864 C CG  . PRO B 519  ? 0.3411 0.4852 0.3770 -0.0504 0.0288  0.0138  517  PRO B CG  
12865 C CD  . PRO B 519  ? 0.2849 0.4407 0.3260 -0.0507 0.0317  0.0151  517  PRO B CD  
12866 N N   . VAL B 520  ? 0.2734 0.4265 0.3199 -0.0591 0.0237  0.0161  518  VAL B N   
12867 C CA  . VAL B 520  ? 0.2746 0.4254 0.3216 -0.0639 0.0207  0.0169  518  VAL B CA  
12868 C C   . VAL B 520  ? 0.3009 0.4611 0.3551 -0.0645 0.0198  0.0172  518  VAL B C   
12869 O O   . VAL B 520  ? 0.2835 0.4414 0.3386 -0.0648 0.0168  0.0163  518  VAL B O   
12870 C CB  . VAL B 520  ? 0.2865 0.4352 0.3308 -0.0695 0.0212  0.0192  518  VAL B CB  
12871 C CG1 . VAL B 520  ? 0.3455 0.4903 0.3895 -0.0744 0.0178  0.0198  518  VAL B CG1 
12872 C CG2 . VAL B 520  ? 0.2721 0.4118 0.3092 -0.0685 0.0222  0.0189  518  VAL B CG2 
12873 N N   . GLU B 521  ? 0.2811 0.4524 0.3406 -0.0644 0.0223  0.0185  519  GLU B N   
12874 C CA  . GLU B 521  ? 0.2715 0.4527 0.3383 -0.0650 0.0214  0.0191  519  GLU B CA  
12875 C C   . GLU B 521  ? 0.2954 0.4780 0.3646 -0.0594 0.0207  0.0170  519  GLU B C   
12876 O O   . GLU B 521  ? 0.3354 0.5213 0.4085 -0.0598 0.0183  0.0168  519  GLU B O   
12877 C CB  . GLU B 521  ? 0.3120 0.5051 0.3841 -0.0666 0.0245  0.0212  519  GLU B CB  
12878 C CG  . GLU B 521  ? 0.3542 0.5468 0.4246 -0.0729 0.0249  0.0237  519  GLU B CG  
12879 C CD  . GLU B 521  ? 0.4557 0.6445 0.5259 -0.0782 0.0211  0.0243  519  GLU B CD  
12880 O OE1 . GLU B 521  ? 0.4698 0.6624 0.5444 -0.0779 0.0188  0.0238  519  GLU B OE1 
12881 O OE2 . GLU B 521  ? 0.5031 0.6849 0.5686 -0.0825 0.0204  0.0253  519  GLU B OE2 
12882 N N   . VAL B 522  ? 0.2890 0.4686 0.3556 -0.0542 0.0225  0.0154  520  VAL B N   
12883 C CA  . VAL B 522  ? 0.2689 0.4486 0.3371 -0.0489 0.0217  0.0134  520  VAL B CA  
12884 C C   . VAL B 522  ? 0.3340 0.5047 0.3991 -0.0494 0.0180  0.0120  520  VAL B C   
12885 O O   . VAL B 522  ? 0.3406 0.5135 0.4089 -0.0479 0.0161  0.0113  520  VAL B O   
12886 C CB  . VAL B 522  ? 0.3211 0.4990 0.3867 -0.0435 0.0243  0.0119  520  VAL B CB  
12887 C CG1 . VAL B 522  ? 0.3144 0.4908 0.3810 -0.0384 0.0232  0.0098  520  VAL B CG1 
12888 C CG2 . VAL B 522  ? 0.4234 0.6112 0.4926 -0.0427 0.0280  0.0131  520  VAL B CG2 
12889 N N   . VAL B 523  ? 0.2561 0.4166 0.3150 -0.0513 0.0171  0.0117  521  VAL B N   
12890 C CA  . VAL B 523  ? 0.2745 0.4263 0.3302 -0.0519 0.0138  0.0105  521  VAL B CA  
12891 C C   . VAL B 523  ? 0.2725 0.4272 0.3312 -0.0564 0.0112  0.0115  521  VAL B C   
12892 O O   . VAL B 523  ? 0.2862 0.4388 0.3454 -0.0557 0.0086  0.0105  521  VAL B O   
12893 C CB  . VAL B 523  ? 0.2843 0.4248 0.3328 -0.0528 0.0135  0.0100  521  VAL B CB  
12894 C CG1 . VAL B 523  ? 0.2797 0.4120 0.3252 -0.0545 0.0102  0.0092  521  VAL B CG1 
12895 C CG2 . VAL B 523  ? 0.3160 0.4528 0.3616 -0.0478 0.0152  0.0085  521  VAL B CG2 
12896 N N   . ARG B 524  ? 0.2776 0.4371 0.3381 -0.0611 0.0118  0.0137  522  ARG B N   
12897 C CA  . ARG B 524  ? 0.3375 0.4994 0.4006 -0.0659 0.0092  0.0147  522  ARG B CA  
12898 C C   . ARG B 524  ? 0.3460 0.5162 0.4153 -0.0641 0.0080  0.0144  522  ARG B C   
12899 O O   . ARG B 524  ? 0.3738 0.5425 0.4436 -0.0661 0.0049  0.0142  522  ARG B O   
12900 C CB  . ARG B 524  ? 0.3488 0.5159 0.4136 -0.0711 0.0105  0.0173  522  ARG B CB  
12901 C CG  . ARG B 524  ? 0.3898 0.5574 0.4559 -0.0770 0.0076  0.0184  522  ARG B CG  
12902 C CD  . ARG B 524  ? 0.4140 0.5895 0.4837 -0.0819 0.0090  0.0211  522  ARG B CD  
12903 N NE  . ARG B 524  ? 0.3757 0.5471 0.4410 -0.0830 0.0115  0.0220  522  ARG B NE  
12904 C CZ  . ARG B 524  ? 0.3989 0.5603 0.4580 -0.0864 0.0104  0.0224  522  ARG B CZ  
12905 N NH1 . ARG B 524  ? 0.3897 0.5437 0.4461 -0.0890 0.0070  0.0217  522  ARG B NH1 
12906 N NH2 . ARG B 524  ? 0.3906 0.5491 0.4460 -0.0871 0.0128  0.0234  522  ARG B NH2 
12907 N N   . ALA B 525  ? 0.3420 0.5204 0.4157 -0.0600 0.0104  0.0144  523  ALA B N   
12908 C CA  . ALA B 525  ? 0.3353 0.5229 0.4155 -0.0582 0.0095  0.0145  523  ALA B CA  
12909 C C   . ALA B 525  ? 0.4224 0.6063 0.5017 -0.0530 0.0083  0.0123  523  ALA B C   
12910 O O   . ALA B 525  ? 0.4131 0.6038 0.4974 -0.0511 0.0073  0.0123  523  ALA B O   
12911 C CB  . ALA B 525  ? 0.3532 0.5525 0.4391 -0.0565 0.0128  0.0157  523  ALA B CB  
12912 N N   . MET B 526  ? 0.3738 0.5472 0.4470 -0.0508 0.0081  0.0106  524  MET B N   
12913 C CA  A MET B 526  ? 0.3791 0.5483 0.4511 -0.0463 0.0069  0.0087  524  MET B CA  
12914 C CA  B MET B 526  ? 0.3791 0.5485 0.4512 -0.0462 0.0069  0.0087  524  MET B CA  
12915 C C   . MET B 526  ? 0.3712 0.5389 0.4437 -0.0484 0.0032  0.0085  524  MET B C   
12916 O O   . MET B 526  ? 0.3478 0.5128 0.4187 -0.0534 0.0014  0.0092  524  MET B O   
12917 C CB  A MET B 526  ? 0.3814 0.5396 0.4467 -0.0441 0.0074  0.0071  524  MET B CB  
12918 C CB  B MET B 526  ? 0.3815 0.5400 0.4469 -0.0440 0.0075  0.0071  524  MET B CB  
12919 C CG  A MET B 526  ? 0.4126 0.5716 0.4768 -0.0412 0.0108  0.0069  524  MET B CG  
12920 C CG  B MET B 526  ? 0.4187 0.5785 0.4837 -0.0396 0.0107  0.0065  524  MET B CG  
12921 S SD  A MET B 526  ? 0.4767 0.6449 0.5464 -0.0354 0.0128  0.0065  524  MET B SD  
12922 S SD  B MET B 526  ? 0.4875 0.6349 0.5448 -0.0377 0.0112  0.0049  524  MET B SD  
12923 C CE  A MET B 526  ? 0.4034 0.5649 0.4710 -0.0312 0.0106  0.0043  524  MET B CE  
12924 C CE  B MET B 526  ? 0.4644 0.6145 0.5227 -0.0313 0.0139  0.0037  524  MET B CE  
12925 N N   . PRO B 527  ? 0.3870 0.5561 0.4615 -0.0448 0.0020  0.0074  525  PRO B N   
12926 C CA  . PRO B 527  ? 0.4910 0.6589 0.5658 -0.0468 -0.0016 0.0073  525  PRO B CA  
12927 C C   . PRO B 527  ? 0.3850 0.5412 0.4531 -0.0489 -0.0035 0.0062  525  PRO B C   
12928 O O   . PRO B 527  ? 0.3571 0.5117 0.4245 -0.0529 -0.0061 0.0066  525  PRO B O   
12929 C CB  . PRO B 527  ? 0.4917 0.6624 0.5690 -0.0416 -0.0020 0.0063  525  PRO B CB  
12930 C CG  . PRO B 527  ? 0.5005 0.6684 0.5758 -0.0369 0.0008  0.0052  525  PRO B CG  
12931 C CD  . PRO B 527  ? 0.4804 0.6513 0.5561 -0.0387 0.0036  0.0063  525  PRO B CD  
12932 N N   . VAL B 528  ? 0.3606 0.5086 0.4238 -0.0463 -0.0023 0.0049  526  VAL B N   
12933 C CA  . VAL B 528  ? 0.3342 0.4711 0.3910 -0.0479 -0.0037 0.0039  526  VAL B CA  
12934 C C   . VAL B 528  ? 0.2885 0.4213 0.3420 -0.0485 -0.0014 0.0041  526  VAL B C   
12935 O O   . VAL B 528  ? 0.3461 0.4769 0.3982 -0.0446 0.0006  0.0033  526  VAL B O   
12936 C CB  . VAL B 528  ? 0.3615 0.4920 0.4155 -0.0439 -0.0046 0.0020  526  VAL B CB  
12937 C CG1 . VAL B 528  ? 0.3397 0.4589 0.3872 -0.0452 -0.0056 0.0009  526  VAL B CG1 
12938 C CG2 . VAL B 528  ? 0.3698 0.5040 0.4265 -0.0435 -0.0070 0.0018  526  VAL B CG2 
12939 N N   . VAL B 529  ? 0.2608 0.3922 0.3129 -0.0533 -0.0017 0.0053  527  VAL B N   
12940 C CA  . VAL B 529  ? 0.2351 0.3626 0.2838 -0.0542 0.0003  0.0058  527  VAL B CA  
12941 C C   . VAL B 529  ? 0.2830 0.3999 0.3260 -0.0516 0.0002  0.0041  527  VAL B C   
12942 O O   . VAL B 529  ? 0.2840 0.3939 0.3237 -0.0523 -0.0020 0.0031  527  VAL B O   
12943 C CB  . VAL B 529  ? 0.2304 0.3573 0.2783 -0.0602 -0.0004 0.0074  527  VAL B CB  
12944 C CG1 . VAL B 529  ? 0.2498 0.3715 0.2934 -0.0610 0.0015  0.0080  527  VAL B CG1 
12945 C CG2 . VAL B 529  ? 0.2930 0.4313 0.3471 -0.0627 0.0000  0.0093  527  VAL B CG2 
12946 N N   . GLY B 530  ? 0.2531 0.3692 0.2949 -0.0484 0.0026  0.0037  528  GLY B N   
12947 C CA  . GLY B 530  ? 0.2607 0.3674 0.2973 -0.0461 0.0026  0.0024  528  GLY B CA  
12948 C C   . GLY B 530  ? 0.2499 0.3540 0.2862 -0.0418 0.0019  0.0005  528  GLY B C   
12949 O O   . GLY B 530  ? 0.2450 0.3408 0.2770 -0.0404 0.0014  -0.0006 528  GLY B O   
12950 N N   . ALA B 531  ? 0.2483 0.3590 0.2889 -0.0395 0.0018  0.0003  529  ALA B N   
12951 C CA  . ALA B 531  ? 0.2492 0.3574 0.2895 -0.0354 0.0012  -0.0013 529  ALA B CA  
12952 C C   . ALA B 531  ? 0.2231 0.3277 0.2611 -0.0316 0.0031  -0.0022 529  ALA B C   
12953 O O   . ALA B 531  ? 0.2569 0.3649 0.2957 -0.0310 0.0053  -0.0017 529  ALA B O   
12954 C CB  . ALA B 531  ? 0.2872 0.4037 0.3327 -0.0334 0.0010  -0.0011 529  ALA B CB  
12955 N N   . LYS B 532  ? 0.2270 0.3247 0.2620 -0.0293 0.0022  -0.0037 530  LYS B N   
12956 C CA  . LYS B 532  ? 0.2425 0.3365 0.2754 -0.0257 0.0036  -0.0047 530  LYS B CA  
12957 C C   . LYS B 532  ? 0.2199 0.3205 0.2562 -0.0223 0.0053  -0.0048 530  LYS B C   
12958 O O   . LYS B 532  ? 0.2224 0.3295 0.2628 -0.0218 0.0050  -0.0045 530  LYS B O   
12959 C CB  . LYS B 532  ? 0.2687 0.3558 0.2990 -0.0238 0.0021  -0.0062 530  LYS B CB  
12960 C CG  . LYS B 532  ? 0.2847 0.3678 0.3131 -0.0200 0.0031  -0.0074 530  LYS B CG  
12961 C CD  . LYS B 532  ? 0.3010 0.3784 0.3276 -0.0184 0.0017  -0.0086 530  LYS B CD  
12962 C CE  . LYS B 532  ? 0.2668 0.3480 0.2964 -0.0170 0.0007  -0.0088 530  LYS B CE  
12963 N NZ  . LYS B 532  ? 0.2653 0.3516 0.2978 -0.0135 0.0020  -0.0090 530  LYS B NZ  
12964 N N   . HIS B 533  ? 0.2021 0.3010 0.2367 -0.0199 0.0071  -0.0054 531  HIS B N   
12965 C CA  . HIS B 533  ? 0.2056 0.3091 0.2426 -0.0161 0.0087  -0.0059 531  HIS B CA  
12966 C C   . HIS B 533  ? 0.2324 0.3358 0.2710 -0.0133 0.0074  -0.0068 531  HIS B C   
12967 O O   . HIS B 533  ? 0.2272 0.3242 0.2633 -0.0128 0.0060  -0.0077 531  HIS B O   
12968 C CB  . HIS B 533  ? 0.2024 0.3015 0.2360 -0.0139 0.0102  -0.0067 531  HIS B CB  
12969 C CG  . HIS B 533  ? 0.2543 0.3584 0.2897 -0.0107 0.0123  -0.0070 531  HIS B CG  
12970 N ND1 . HIS B 533  ? 0.2792 0.3852 0.3167 -0.0070 0.0123  -0.0079 531  HIS B ND1 
12971 C CD2 . HIS B 533  ? 0.3248 0.4319 0.3599 -0.0105 0.0146  -0.0066 531  HIS B CD2 
12972 C CE1 . HIS B 533  ? 0.3765 0.4866 0.4151 -0.0046 0.0145  -0.0081 531  HIS B CE1 
12973 N NE2 . HIS B 533  ? 0.3860 0.4969 0.4231 -0.0066 0.0159  -0.0073 531  HIS B NE2 
12974 N N   . ASP B 534  ? 0.2360 0.3466 0.2789 -0.0115 0.0079  -0.0065 532  ASP B N   
12975 C CA  . ASP B 534  ? 0.2946 0.4057 0.3392 -0.0088 0.0067  -0.0072 532  ASP B CA  
12976 C C   . ASP B 534  ? 0.2682 0.3735 0.3101 -0.0051 0.0070  -0.0087 532  ASP B C   
12977 O O   . ASP B 534  ? 0.3140 0.4167 0.3558 -0.0035 0.0057  -0.0093 532  ASP B O   
12978 C CB  . ASP B 534  ? 0.2999 0.4201 0.3496 -0.0071 0.0074  -0.0065 532  ASP B CB  
12979 C CG  . ASP B 534  ? 0.4196 0.5458 0.4726 -0.0106 0.0064  -0.0051 532  ASP B CG  
12980 O OD1 . ASP B 534  ? 0.5228 0.6457 0.5745 -0.0134 0.0042  -0.0049 532  ASP B OD1 
12981 O OD2 . ASP B 534  ? 0.5275 0.6618 0.5845 -0.0106 0.0076  -0.0041 532  ASP B OD2 
12982 N N   . ARG B 535  ? 0.2292 0.3324 0.2690 -0.0038 0.0088  -0.0092 533  ARG B N   
12983 C CA  . ARG B 535  ? 0.2363 0.3349 0.2740 -0.0003 0.0092  -0.0106 533  ARG B CA  
12984 C C   . ARG B 535  ? 0.2552 0.3456 0.2884 -0.0011 0.0088  -0.0113 533  ARG B C   
12985 O O   . ARG B 535  ? 0.2768 0.3634 0.3079 0.0015  0.0093  -0.0123 533  ARG B O   
12986 C CB  . ARG B 535  ? 0.3258 0.4282 0.3644 0.0026  0.0115  -0.0108 533  ARG B CB  
12987 N N   . ILE B 536  ? 0.2052 0.2929 0.2367 -0.0045 0.0078  -0.0107 534  ILE B N   
12988 C CA  . ILE B 536  ? 0.1899 0.2701 0.2175 -0.0053 0.0072  -0.0112 534  ILE B CA  
12989 C C   . ILE B 536  ? 0.2138 0.2905 0.2408 -0.0067 0.0051  -0.0113 534  ILE B C   
12990 O O   . ILE B 536  ? 0.2437 0.3224 0.2717 -0.0095 0.0043  -0.0105 534  ILE B O   
12991 C CB  . ILE B 536  ? 0.2137 0.2928 0.2391 -0.0080 0.0079  -0.0104 534  ILE B CB  
12992 C CG1 . ILE B 536  ? 0.2373 0.3196 0.2627 -0.0065 0.0101  -0.0104 534  ILE B CG1 
12993 C CG2 . ILE B 536  ? 0.2173 0.2885 0.2387 -0.0086 0.0070  -0.0110 534  ILE B CG2 
12994 C CD1 . ILE B 536  ? 0.2904 0.3719 0.3135 -0.0092 0.0109  -0.0095 534  ILE B CD1 
12995 N N   . ALA B 537  ? 0.1950 0.2668 0.2205 -0.0048 0.0044  -0.0123 535  ALA B N   
12996 C CA  . ALA B 537  ? 0.1946 0.2630 0.2194 -0.0058 0.0027  -0.0125 535  ALA B CA  
12997 C C   . ALA B 537  ? 0.1864 0.2495 0.2081 -0.0084 0.0020  -0.0124 535  ALA B C   
12998 O O   . ALA B 537  ? 0.1999 0.2594 0.2194 -0.0081 0.0026  -0.0126 535  ALA B O   
12999 C CB  . ALA B 537  ? 0.2074 0.2727 0.2318 -0.0028 0.0023  -0.0135 535  ALA B CB  
13000 N N   . LEU B 538  ? 0.1863 0.2490 0.2079 -0.0109 0.0007  -0.0120 536  LEU B N   
13001 C CA  . LEU B 538  ? 0.1839 0.2403 0.2022 -0.0126 -0.0001 -0.0122 536  LEU B CA  
13002 C C   . LEU B 538  ? 0.1958 0.2471 0.2126 -0.0102 -0.0003 -0.0132 536  LEU B C   
13003 O O   . LEU B 538  ? 0.2093 0.2617 0.2274 -0.0078 -0.0003 -0.0137 536  LEU B O   
13004 C CB  . LEU B 538  ? 0.2255 0.2816 0.2437 -0.0152 -0.0016 -0.0119 536  LEU B CB  
13005 C CG  . LEU B 538  ? 0.2669 0.3268 0.2861 -0.0186 -0.0018 -0.0107 536  LEU B CG  
13006 C CD1 . LEU B 538  ? 0.3032 0.3627 0.3222 -0.0207 -0.0036 -0.0107 536  LEU B CD1 
13007 C CD2 . LEU B 538  ? 0.2603 0.3169 0.2770 -0.0206 -0.0013 -0.0102 536  LEU B CD2 
13008 N N   . PRO B 539  ? 0.1841 0.2298 0.1981 -0.0107 -0.0004 -0.0135 537  PRO B N   
13009 C CA  . PRO B 539  ? 0.1802 0.2213 0.1929 -0.0085 -0.0006 -0.0144 537  PRO B CA  
13010 C C   . PRO B 539  ? 0.1906 0.2311 0.2038 -0.0077 -0.0015 -0.0149 537  PRO B C   
13011 O O   . PRO B 539  ? 0.1964 0.2363 0.2102 -0.0053 -0.0013 -0.0155 537  PRO B O   
13012 C CB  . PRO B 539  ? 0.2103 0.2460 0.2202 -0.0097 -0.0009 -0.0144 537  PRO B CB  
13013 C CG  . PRO B 539  ? 0.2128 0.2506 0.2224 -0.0117 -0.0003 -0.0134 537  PRO B CG  
13014 C CD  . PRO B 539  ? 0.2158 0.2593 0.2277 -0.0131 -0.0003 -0.0128 537  PRO B CD  
13015 N N   . ALA B 540  ? 0.2025 0.2433 0.2154 -0.0098 -0.0024 -0.0146 538  ALA B N   
13016 C CA  . ALA B 540  ? 0.2101 0.2501 0.2230 -0.0092 -0.0033 -0.0151 538  ALA B CA  
13017 C C   . ALA B 540  ? 0.2293 0.2741 0.2449 -0.0073 -0.0032 -0.0150 538  ALA B C   
13018 O O   . ALA B 540  ? 0.2202 0.2640 0.2357 -0.0061 -0.0037 -0.0154 538  ALA B O   
13019 C CB  . ALA B 540  ? 0.2250 0.2645 0.2367 -0.0121 -0.0045 -0.0148 538  ALA B CB  
13020 N N   . GLU B 541  ? 0.2201 0.2699 0.2380 -0.0071 -0.0024 -0.0145 539  GLU B N   
13021 C CA  . GLU B 541  ? 0.1912 0.2461 0.2119 -0.0054 -0.0024 -0.0142 539  GLU B CA  
13022 C C   . GLU B 541  ? 0.1764 0.2320 0.1981 -0.0024 -0.0012 -0.0146 539  GLU B C   
13023 O O   . GLU B 541  ? 0.2131 0.2733 0.2372 -0.0008 -0.0009 -0.0144 539  GLU B O   
13024 C CB  . GLU B 541  ? 0.2366 0.2974 0.2595 -0.0074 -0.0026 -0.0133 539  GLU B CB  
13025 C CG  . GLU B 541  ? 0.2985 0.3580 0.3201 -0.0105 -0.0041 -0.0130 539  GLU B CG  
13026 C CD  . GLU B 541  ? 0.4475 0.5126 0.4713 -0.0131 -0.0046 -0.0120 539  GLU B CD  
13027 O OE1 . GLU B 541  ? 0.4512 0.5215 0.4776 -0.0127 -0.0036 -0.0114 539  GLU B OE1 
13028 O OE2 . GLU B 541  ? 0.4736 0.5377 0.4963 -0.0157 -0.0060 -0.0119 539  GLU B OE2 
13029 N N   . LEU B 542  ? 0.1877 0.2388 0.2075 -0.0015 -0.0007 -0.0152 540  LEU B N   
13030 C CA  . LEU B 542  ? 0.2097 0.2608 0.2300 0.0012  0.0003  -0.0157 540  LEU B CA  
13031 C C   . LEU B 542  ? 0.2004 0.2527 0.2221 0.0036  0.0001  -0.0159 540  LEU B C   
13032 O O   . LEU B 542  ? 0.2457 0.2999 0.2686 0.0058  0.0009  -0.0161 540  LEU B O   
13033 C CB  . LEU B 542  ? 0.2300 0.2757 0.2481 0.0017  0.0005  -0.0163 540  LEU B CB  
13034 C CG  . LEU B 542  ? 0.2585 0.3024 0.2749 0.0002  0.0009  -0.0162 540  LEU B CG  
13035 C CD1 . LEU B 542  ? 0.2394 0.2786 0.2542 0.0015  0.0010  -0.0168 540  LEU B CD1 
13036 C CD2 . LEU B 542  ? 0.2522 0.3004 0.2696 0.0002  0.0019  -0.0158 540  LEU B CD2 
13037 N N   . PHE B 543  ? 0.2003 0.2512 0.2217 0.0034  -0.0009 -0.0159 541  PHE B N   
13038 C CA  . PHE B 543  ? 0.2163 0.2676 0.2386 0.0056  -0.0012 -0.0160 541  PHE B CA  
13039 C C   . PHE B 543  ? 0.2174 0.2734 0.2416 0.0054  -0.0020 -0.0153 541  PHE B C   
13040 O O   . PHE B 543  ? 0.2407 0.2971 0.2656 0.0070  -0.0025 -0.0152 541  PHE B O   
13041 C CB  . PHE B 543  ? 0.1921 0.2382 0.2124 0.0059  -0.0017 -0.0164 541  PHE B CB  
13042 C CG  . PHE B 543  ? 0.1958 0.2377 0.2146 0.0059  -0.0011 -0.0170 541  PHE B CG  
13043 C CD1 . PHE B 543  ? 0.2466 0.2883 0.2657 0.0075  -0.0003 -0.0173 541  PHE B CD1 
13044 C CD2 . PHE B 543  ? 0.1967 0.2349 0.2136 0.0043  -0.0014 -0.0171 541  PHE B CD2 
13045 C CE1 . PHE B 543  ? 0.2513 0.2893 0.2690 0.0074  0.0000  -0.0178 541  PHE B CE1 
13046 C CE2 . PHE B 543  ? 0.1998 0.2346 0.2155 0.0044  -0.0010 -0.0176 541  PHE B CE2 
13047 C CZ  . PHE B 543  ? 0.2276 0.2624 0.2438 0.0059  -0.0003 -0.0178 541  PHE B CZ  
13048 N N   . GLY B 544  ? 0.2102 0.2700 0.2356 0.0033  -0.0021 -0.0148 542  GLY B N   
13049 C CA  . GLY B 544  ? 0.2041 0.2692 0.2318 0.0030  -0.0029 -0.0140 542  GLY B CA  
13050 C C   . GLY B 544  ? 0.2294 0.2929 0.2561 0.0025  -0.0044 -0.0139 542  GLY B C   
13051 O O   . GLY B 544  ? 0.2775 0.3367 0.3016 0.0009  -0.0050 -0.0142 542  GLY B O   
13052 N N   . ASP B 545  ? 0.2577 0.3244 0.2862 0.0042  -0.0050 -0.0135 543  ASP B N   
13053 C CA  . ASP B 545  ? 0.2854 0.3513 0.3130 0.0037  -0.0066 -0.0133 543  ASP B CA  
13054 C C   . ASP B 545  ? 0.2845 0.3444 0.3093 0.0050  -0.0065 -0.0138 543  ASP B C   
13055 O O   . ASP B 545  ? 0.2927 0.3508 0.3157 0.0042  -0.0077 -0.0137 543  ASP B O   
13056 C CB  . ASP B 545  ? 0.2960 0.3673 0.3264 0.0053  -0.0073 -0.0125 543  ASP B CB  
13057 C CG  . ASP B 545  ? 0.5320 0.6100 0.5656 0.0040  -0.0075 -0.0117 543  ASP B CG  
13058 O OD1 . ASP B 545  ? 0.4973 0.5755 0.5303 0.0010  -0.0076 -0.0117 543  ASP B OD1 
13059 O OD2 . ASP B 545  ? 0.6787 0.7618 0.7154 0.0060  -0.0074 -0.0112 543  ASP B OD2 
13060 N N   . ALA B 546  ? 0.2631 0.3200 0.2873 0.0067  -0.0053 -0.0144 544  ALA B N   
13061 C CA  . ALA B 546  ? 0.2443 0.2961 0.2664 0.0078  -0.0052 -0.0148 544  ALA B CA  
13062 C C   . ALA B 546  ? 0.2480 0.2955 0.2673 0.0058  -0.0055 -0.0152 544  ALA B C   
13063 O O   . ALA B 546  ? 0.2415 0.2863 0.2589 0.0059  -0.0060 -0.0152 544  ALA B O   
13064 C CB  . ALA B 546  ? 0.2562 0.3057 0.2784 0.0098  -0.0040 -0.0153 544  ALA B CB  
13065 N N   . ARG B 547  ? 0.2021 0.2487 0.2208 0.0040  -0.0051 -0.0155 545  ARG B N   
13066 C CA  . ARG B 547  ? 0.2099 0.2521 0.2259 0.0023  -0.0052 -0.0160 545  ARG B CA  
13067 C C   . ARG B 547  ? 0.2014 0.2436 0.2172 0.0004  -0.0049 -0.0161 545  ARG B C   
13068 O O   . ARG B 547  ? 0.2111 0.2562 0.2287 0.0006  -0.0043 -0.0159 545  ARG B O   
13069 C CB  . ARG B 547  ? 0.2544 0.2919 0.2690 0.0038  -0.0044 -0.0165 545  ARG B CB  
13070 C CG  . ARG B 547  ? 0.2087 0.2456 0.2243 0.0049  -0.0034 -0.0168 545  ARG B CG  
13071 C CD  . ARG B 547  ? 0.2321 0.2648 0.2466 0.0062  -0.0028 -0.0172 545  ARG B CD  
13072 N NE  . ARG B 547  ? 0.2229 0.2556 0.2386 0.0077  -0.0021 -0.0174 545  ARG B NE  
13073 C CZ  . ARG B 547  ? 0.2250 0.2557 0.2404 0.0075  -0.0015 -0.0178 545  ARG B CZ  
13074 N NH1 . ARG B 547  ? 0.2094 0.2379 0.2235 0.0061  -0.0016 -0.0180 545  ARG B NH1 
13075 N NH2 . ARG B 547  ? 0.2382 0.2692 0.2545 0.0089  -0.0010 -0.0180 545  ARG B NH2 
13076 N N   . THR B 548  ? 0.1947 0.2336 0.2082 -0.0015 -0.0053 -0.0164 546  THR B N   
13077 C CA  . THR B 548  ? 0.1749 0.2127 0.1876 -0.0034 -0.0051 -0.0164 546  THR B CA  
13078 C C   . THR B 548  ? 0.1877 0.2216 0.1995 -0.0025 -0.0042 -0.0169 546  THR B C   
13079 O O   . THR B 548  ? 0.2006 0.2308 0.2110 -0.0015 -0.0040 -0.0174 546  THR B O   
13080 C CB  . THR B 548  ? 0.2175 0.2530 0.2277 -0.0058 -0.0062 -0.0166 546  THR B CB  
13081 O OG1 . THR B 548  ? 0.2593 0.2986 0.2705 -0.0069 -0.0073 -0.0161 546  THR B OG1 
13082 C CG2 . THR B 548  ? 0.2514 0.2852 0.2606 -0.0079 -0.0061 -0.0166 546  THR B CG2 
13083 N N   . ASN B 549  ? 0.1784 0.2132 0.1909 -0.0027 -0.0035 -0.0168 547  ASN B N   
13084 C CA  . ASN B 549  ? 0.1567 0.1880 0.1683 -0.0019 -0.0028 -0.0171 547  ASN B CA  
13085 C C   . ASN B 549  ? 0.1777 0.2044 0.1868 -0.0033 -0.0031 -0.0174 547  ASN B C   
13086 O O   . ASN B 549  ? 0.2047 0.2311 0.2126 -0.0054 -0.0038 -0.0173 547  ASN B O   
13087 C CB  . ASN B 549  ? 0.1868 0.2203 0.1993 -0.0023 -0.0022 -0.0168 547  ASN B CB  
13088 C CG  . ASN B 549  ? 0.1802 0.2108 0.1921 -0.0011 -0.0016 -0.0171 547  ASN B CG  
13089 O OD1 . ASN B 549  ? 0.1805 0.2084 0.1921 0.0003  -0.0015 -0.0176 547  ASN B OD1 
13090 N ND2 . ASN B 549  ? 0.1868 0.2183 0.1986 -0.0017 -0.0011 -0.0169 547  ASN B ND2 
13091 N N   . SER B 550  ? 0.1717 0.1948 0.1800 -0.0021 -0.0027 -0.0179 548  SER B N   
13092 C CA  . SER B 550  ? 0.1814 0.2000 0.1874 -0.0030 -0.0029 -0.0182 548  SER B CA  
13093 C C   . SER B 550  ? 0.1984 0.2166 0.2038 -0.0047 -0.0030 -0.0178 548  SER B C   
13094 O O   . SER B 550  ? 0.2009 0.2215 0.2074 -0.0045 -0.0026 -0.0174 548  SER B O   
13095 C CB  . SER B 550  ? 0.1794 0.1949 0.1853 -0.0012 -0.0024 -0.0186 548  SER B CB  
13096 O OG  . SER B 550  ? 0.1801 0.1962 0.1872 -0.0003 -0.0019 -0.0185 548  SER B OG  
13097 N N   . ALA B 551  ? 0.2084 0.2233 0.2115 -0.0063 -0.0035 -0.0179 549  ALA B N   
13098 C CA  . ALA B 551  ? 0.2217 0.2354 0.2236 -0.0081 -0.0037 -0.0174 549  ALA B CA  
13099 C C   . ALA B 551  ? 0.2238 0.2327 0.2242 -0.0073 -0.0035 -0.0177 549  ALA B C   
13100 O O   . ALA B 551  ? 0.2223 0.2281 0.2218 -0.0062 -0.0035 -0.0183 549  ALA B O   
13101 C CB  . ALA B 551  ? 0.2293 0.2423 0.2296 -0.0107 -0.0045 -0.0172 549  ALA B CB  
13102 N N   . GLY B 552  ? 0.2047 0.2133 0.2049 -0.0077 -0.0034 -0.0171 550  GLY B N   
13103 C CA  . GLY B 552  ? 0.2266 0.2309 0.2254 -0.0071 -0.0034 -0.0172 550  GLY B CA  
13104 C C   . GLY B 552  ? 0.2112 0.2120 0.2073 -0.0093 -0.0040 -0.0168 550  GLY B C   
13105 O O   . GLY B 552  ? 0.2495 0.2504 0.2447 -0.0112 -0.0045 -0.0168 550  GLY B O   
13106 N N   . LEU B 553  ? 0.2323 0.2298 0.2272 -0.0090 -0.0042 -0.0165 551  LEU B N   
13107 C CA  . LEU B 553  ? 0.2506 0.2439 0.2426 -0.0109 -0.0048 -0.0161 551  LEU B CA  
13108 C C   . LEU B 553  ? 0.2293 0.2226 0.2209 -0.0112 -0.0048 -0.0151 551  LEU B C   
13109 O O   . LEU B 553  ? 0.2667 0.2607 0.2595 -0.0093 -0.0045 -0.0151 551  LEU B O   
13110 C CB  . LEU B 553  ? 0.2531 0.2410 0.2433 -0.0097 -0.0051 -0.0167 551  LEU B CB  
13111 C CG  . LEU B 553  ? 0.2676 0.2545 0.2573 -0.0094 -0.0051 -0.0177 551  LEU B CG  
13112 C CD1 . LEU B 553  ? 0.3015 0.2837 0.2900 -0.0076 -0.0050 -0.0184 551  LEU B CD1 
13113 C CD2 . LEU B 553  ? 0.3005 0.2867 0.2883 -0.0123 -0.0058 -0.0176 551  LEU B CD2 
13114 N N   . ASP B 554  ? 0.2399 0.2324 0.2298 -0.0138 -0.0051 -0.0143 552  ASP B N   
13115 C CA  . ASP B 554  ? 0.2323 0.2249 0.2214 -0.0144 -0.0050 -0.0132 552  ASP B CA  
13116 C C   . ASP B 554  ? 0.2283 0.2149 0.2148 -0.0141 -0.0057 -0.0129 552  ASP B C   
13117 O O   . ASP B 554  ? 0.2410 0.2237 0.2251 -0.0159 -0.0063 -0.0126 552  ASP B O   
13118 C CB  . ASP B 554  ? 0.2551 0.2503 0.2438 -0.0175 -0.0049 -0.0123 552  ASP B CB  
13119 C CG  . ASP B 554  ? 0.2539 0.2496 0.2417 -0.0183 -0.0046 -0.0111 552  ASP B CG  
13120 O OD1 . ASP B 554  ? 0.2652 0.2593 0.2525 -0.0165 -0.0046 -0.0110 552  ASP B OD1 
13121 O OD2 . ASP B 554  ? 0.2811 0.2789 0.2684 -0.0209 -0.0044 -0.0101 552  ASP B OD2 
13122 N N   . LEU B 555  ? 0.2294 0.2151 0.2165 -0.0118 -0.0056 -0.0130 553  LEU B N   
13123 C CA  . LEU B 555  ? 0.2465 0.2268 0.2316 -0.0110 -0.0064 -0.0127 553  LEU B CA  
13124 C C   . LEU B 555  ? 0.2674 0.2462 0.2502 -0.0126 -0.0067 -0.0113 553  LEU B C   
13125 O O   . LEU B 555  ? 0.2537 0.2282 0.2348 -0.0118 -0.0074 -0.0108 553  LEU B O   
13126 C CB  . LEU B 555  ? 0.2286 0.2089 0.2155 -0.0079 -0.0063 -0.0132 553  LEU B CB  
13127 C CG  . LEU B 555  ? 0.2537 0.2353 0.2428 -0.0063 -0.0059 -0.0145 553  LEU B CG  
13128 C CD1 . LEU B 555  ? 0.2971 0.2786 0.2880 -0.0035 -0.0059 -0.0148 553  LEU B CD1 
13129 C CD2 . LEU B 555  ? 0.3081 0.2862 0.2955 -0.0069 -0.0061 -0.0150 553  LEU B CD2 
13130 N N   . SER B 556  ? 0.2421 0.2242 0.2248 -0.0148 -0.0063 -0.0106 554  SER B N   
13131 C CA  . SER B 556  ? 0.2449 0.2254 0.2251 -0.0170 -0.0065 -0.0091 554  SER B CA  
13132 C C   . SER B 556  ? 0.2602 0.2387 0.2384 -0.0201 -0.0068 -0.0086 554  SER B C   
13133 O O   . SER B 556  ? 0.2852 0.2618 0.2610 -0.0222 -0.0070 -0.0073 554  SER B O   
13134 C CB  . SER B 556  ? 0.2600 0.2456 0.2411 -0.0174 -0.0056 -0.0085 554  SER B CB  
13135 O OG  . SER B 556  ? 0.2683 0.2587 0.2510 -0.0190 -0.0048 -0.0086 554  SER B OG  
13136 N N   . ASN B 557  ? 0.2286 0.2074 0.2077 -0.0205 -0.0069 -0.0096 555  ASN B N   
13137 C CA  . ASN B 557  ? 0.2559 0.2330 0.2333 -0.0236 -0.0073 -0.0092 555  ASN B CA  
13138 C C   . ASN B 557  ? 0.2554 0.2249 0.2298 -0.0234 -0.0084 -0.0095 555  ASN B C   
13139 O O   . ASN B 557  ? 0.2546 0.2222 0.2294 -0.0211 -0.0085 -0.0108 555  ASN B O   
13140 C CB  . ASN B 557  ? 0.2446 0.2263 0.2245 -0.0240 -0.0070 -0.0101 555  ASN B CB  
13141 C CG  . ASN B 557  ? 0.2639 0.2444 0.2423 -0.0274 -0.0077 -0.0098 555  ASN B CG  
13142 O OD1 . ASN B 557  ? 0.2706 0.2450 0.2460 -0.0283 -0.0086 -0.0100 555  ASN B OD1 
13143 N ND2 . ASN B 557  ? 0.2714 0.2578 0.2519 -0.0293 -0.0073 -0.0095 555  ASN B ND2 
13144 N N   . GLU B 558  ? 0.2694 0.2345 0.2405 -0.0257 -0.0090 -0.0084 556  GLU B N   
13145 C CA  . GLU B 558  ? 0.2776 0.2349 0.2455 -0.0253 -0.0100 -0.0086 556  GLU B CA  
13146 C C   . GLU B 558  ? 0.2815 0.2367 0.2488 -0.0258 -0.0104 -0.0100 556  GLU B C   
13147 O O   . GLU B 558  ? 0.2979 0.2478 0.2635 -0.0239 -0.0108 -0.0109 556  GLU B O   
13148 C CB  . GLU B 558  ? 0.3292 0.2817 0.2934 -0.0279 -0.0107 -0.0070 556  GLU B CB  
13149 C CG  . GLU B 558  ? 0.3424 0.2947 0.3060 -0.0271 -0.0106 -0.0057 556  GLU B CG  
13150 C CD  . GLU B 558  ? 0.3248 0.2742 0.2885 -0.0233 -0.0109 -0.0061 556  GLU B CD  
13151 O OE1 . GLU B 558  ? 0.3080 0.2541 0.2717 -0.0211 -0.0113 -0.0074 556  GLU B OE1 
13152 O OE2 . GLU B 558  ? 0.3198 0.2703 0.2835 -0.0225 -0.0108 -0.0052 556  GLU B OE2 
13153 N N   . GLU B 559  ? 0.2669 0.2260 0.2352 -0.0283 -0.0103 -0.0101 557  GLU B N   
13154 C CA  . GLU B 559  ? 0.2610 0.2184 0.2286 -0.0287 -0.0108 -0.0114 557  GLU B CA  
13155 C C   . GLU B 559  ? 0.2718 0.2308 0.2416 -0.0250 -0.0101 -0.0129 557  GLU B C   
13156 O O   . GLU B 559  ? 0.2892 0.2437 0.2573 -0.0237 -0.0104 -0.0141 557  GLU B O   
13157 C CB  . GLU B 559  ? 0.3355 0.2979 0.3045 -0.0319 -0.0109 -0.0112 557  GLU B CB  
13158 C CG  . GLU B 559  ? 0.3738 0.3352 0.3409 -0.0361 -0.0115 -0.0098 557  GLU B CG  
13159 C CD  . GLU B 559  ? 0.4983 0.4650 0.4672 -0.0390 -0.0118 -0.0097 557  GLU B CD  
13160 O OE1 . GLU B 559  ? 0.5156 0.4838 0.4856 -0.0381 -0.0120 -0.0110 557  GLU B OE1 
13161 O OE2 . GLU B 559  ? 0.4432 0.4129 0.4127 -0.0421 -0.0117 -0.0083 557  GLU B OE2 
13162 N N   . THR B 560  ? 0.2557 0.2209 0.2290 -0.0235 -0.0092 -0.0128 558  THR B N   
13163 C CA  . THR B 560  ? 0.2301 0.1972 0.2057 -0.0202 -0.0086 -0.0141 558  THR B CA  
13164 C C   . THR B 560  ? 0.2554 0.2176 0.2299 -0.0173 -0.0086 -0.0145 558  THR B C   
13165 O O   . THR B 560  ? 0.2646 0.2247 0.2389 -0.0153 -0.0085 -0.0157 558  THR B O   
13166 C CB  . THR B 560  ? 0.2379 0.2120 0.2172 -0.0191 -0.0077 -0.0138 558  THR B CB  
13167 O OG1 . THR B 560  ? 0.2682 0.2472 0.2488 -0.0216 -0.0077 -0.0134 558  THR B OG1 
13168 C CG2 . THR B 560  ? 0.2596 0.2356 0.2412 -0.0160 -0.0071 -0.0150 558  THR B CG2 
13169 N N   . LEU B 561  ? 0.2305 0.1908 0.2042 -0.0171 -0.0089 -0.0134 559  LEU B N   
13170 C CA  . LEU B 561  ? 0.2338 0.1898 0.2068 -0.0143 -0.0090 -0.0136 559  LEU B CA  
13171 C C   . LEU B 561  ? 0.2721 0.2211 0.2417 -0.0142 -0.0096 -0.0143 559  LEU B C   
13172 O O   . LEU B 561  ? 0.2511 0.1977 0.2209 -0.0114 -0.0094 -0.0152 559  LEU B O   
13173 C CB  . LEU B 561  ? 0.2509 0.2059 0.2232 -0.0143 -0.0094 -0.0121 559  LEU B CB  
13174 C CG  . LEU B 561  ? 0.2380 0.1992 0.2134 -0.0135 -0.0088 -0.0117 559  LEU B CG  
13175 C CD1 . LEU B 561  ? 0.2800 0.2398 0.2539 -0.0139 -0.0092 -0.0102 559  LEU B CD1 
13176 C CD2 . LEU B 561  ? 0.2422 0.2055 0.2205 -0.0102 -0.0083 -0.0127 559  LEU B CD2 
13177 N N   . ALA B 562  ? 0.2624 0.2081 0.2290 -0.0173 -0.0103 -0.0139 560  ALA B N   
13178 C CA  . ALA B 562  ? 0.2839 0.2223 0.2468 -0.0174 -0.0109 -0.0146 560  ALA B CA  
13179 C C   . ALA B 562  ? 0.2875 0.2263 0.2506 -0.0165 -0.0105 -0.0164 560  ALA B C   
13180 O O   . ALA B 562  ? 0.2914 0.2256 0.2529 -0.0143 -0.0104 -0.0174 560  ALA B O   
13181 C CB  . ALA B 562  ? 0.3022 0.2371 0.2616 -0.0214 -0.0119 -0.0137 560  ALA B CB  
13182 N N   . SER B 563  ? 0.2663 0.2108 0.2314 -0.0179 -0.0102 -0.0166 561  SER B N   
13183 C CA  . SER B 563  ? 0.2580 0.2028 0.2231 -0.0171 -0.0099 -0.0182 561  SER B CA  
13184 C C   . SER B 563  ? 0.2908 0.2381 0.2587 -0.0133 -0.0088 -0.0189 561  SER B C   
13185 O O   . SER B 563  ? 0.2878 0.2324 0.2547 -0.0114 -0.0084 -0.0202 561  SER B O   
13186 C CB  . SER B 563  ? 0.2996 0.2496 0.2659 -0.0198 -0.0101 -0.0182 561  SER B CB  
13187 O OG  . SER B 563  ? 0.3348 0.2921 0.3053 -0.0192 -0.0094 -0.0175 561  SER B OG  
13188 N N   . LEU B 564  ? 0.2468 0.1988 0.2181 -0.0121 -0.0083 -0.0181 562  LEU B N   
13189 C CA  . LEU B 564  ? 0.2589 0.2132 0.2331 -0.0087 -0.0073 -0.0187 562  LEU B CA  
13190 C C   . LEU B 564  ? 0.2743 0.2233 0.2471 -0.0061 -0.0073 -0.0190 562  LEU B C   
13191 O O   . LEU B 564  ? 0.2782 0.2266 0.2516 -0.0037 -0.0065 -0.0200 562  LEU B O   
13192 C CB  . LEU B 564  ? 0.2755 0.2354 0.2532 -0.0082 -0.0070 -0.0177 562  LEU B CB  
13193 C CG  . LEU B 564  ? 0.3121 0.2751 0.2931 -0.0051 -0.0062 -0.0181 562  LEU B CG  
13194 C CD1 . LEU B 564  ? 0.3239 0.2890 0.3059 -0.0044 -0.0054 -0.0192 562  LEU B CD1 
13195 C CD2 . LEU B 564  ? 0.3212 0.2892 0.3050 -0.0051 -0.0061 -0.0172 562  LEU B CD2 
13196 N N   . THR B 565  ? 0.2795 0.2244 0.2503 -0.0067 -0.0081 -0.0181 563  THR B N   
13197 C CA  . THR B 565  ? 0.2694 0.2088 0.2388 -0.0042 -0.0081 -0.0183 563  THR B CA  
13198 C C   . THR B 565  ? 0.3097 0.2448 0.2766 -0.0033 -0.0078 -0.0198 563  THR B C   
13199 O O   . THR B 565  ? 0.2819 0.2159 0.2496 -0.0002 -0.0070 -0.0206 563  THR B O   
13200 C CB  . THR B 565  ? 0.2814 0.2160 0.2480 -0.0055 -0.0093 -0.0171 563  THR B CB  
13201 O OG1 . THR B 565  ? 0.3039 0.2424 0.2726 -0.0058 -0.0095 -0.0157 563  THR B OG1 
13202 C CG2 . THR B 565  ? 0.3174 0.2459 0.2822 -0.0029 -0.0095 -0.0173 563  THR B CG2 
13203 N N   . GLU B 566  ? 0.2803 0.2129 0.2440 -0.0061 -0.0083 -0.0203 564  GLU B N   
13204 C CA  . GLU B 566  ? 0.2675 0.1954 0.2281 -0.0054 -0.0081 -0.0218 564  GLU B CA  
13205 C C   . GLU B 566  ? 0.2711 0.2032 0.2340 -0.0036 -0.0068 -0.0230 564  GLU B C   
13206 O O   . GLU B 566  ? 0.2857 0.2149 0.2476 -0.0011 -0.0060 -0.0241 564  GLU B O   
13207 C CB  . GLU B 566  ? 0.3455 0.2699 0.3021 -0.0091 -0.0092 -0.0220 564  GLU B CB  
13208 C CG  . GLU B 566  ? 0.4358 0.3546 0.3894 -0.0109 -0.0104 -0.0209 564  GLU B CG  
13209 C CD  . GLU B 566  ? 0.5920 0.5054 0.5445 -0.0077 -0.0102 -0.0209 564  GLU B CD  
13210 O OE1 . GLU B 566  ? 0.5580 0.4676 0.5090 -0.0051 -0.0096 -0.0223 564  GLU B OE1 
13211 O OE2 . GLU B 566  ? 0.5568 0.4698 0.5100 -0.0076 -0.0108 -0.0194 564  GLU B OE2 
13212 N N   . ALA B 567  ? 0.2709 0.2096 0.2367 -0.0048 -0.0066 -0.0226 565  ALA B N   
13213 C CA  . ALA B 567  ? 0.2746 0.2173 0.2425 -0.0032 -0.0055 -0.0235 565  ALA B CA  
13214 C C   . ALA B 567  ? 0.2710 0.2154 0.2421 0.0004  -0.0044 -0.0235 565  ALA B C   
13215 O O   . ALA B 567  ? 0.2624 0.2070 0.2338 0.0025  -0.0032 -0.0245 565  ALA B O   
13216 C CB  . ALA B 567  ? 0.2621 0.2114 0.2326 -0.0051 -0.0056 -0.0229 565  ALA B CB  
13217 N N   . LEU B 568  ? 0.2416 0.1873 0.2150 0.0011  -0.0047 -0.0223 566  LEU B N   
13218 C CA  . LEU B 568  ? 0.2440 0.1914 0.2205 0.0043  -0.0038 -0.0222 566  LEU B CA  
13219 C C   . LEU B 568  ? 0.2628 0.2048 0.2374 0.0068  -0.0034 -0.0229 566  LEU B C   
13220 O O   . LEU B 568  ? 0.2563 0.1994 0.2327 0.0094  -0.0022 -0.0236 566  LEU B O   
13221 C CB  . LEU B 568  ? 0.2372 0.1871 0.2163 0.0043  -0.0045 -0.0208 566  LEU B CB  
13222 C CG  . LEU B 568  ? 0.2344 0.1901 0.2157 0.0024  -0.0047 -0.0201 566  LEU B CG  
13223 C CD1 . LEU B 568  ? 0.2706 0.2274 0.2532 0.0022  -0.0055 -0.0188 566  LEU B CD1 
13224 C CD2 . LEU B 568  ? 0.2794 0.2402 0.2641 0.0037  -0.0037 -0.0206 566  LEU B CD2 
13225 N N   . ARG B 569  ? 0.2728 0.2088 0.2438 0.0059  -0.0043 -0.0228 567  ARG B N   
13226 C CA  . ARG B 569  ? 0.2909 0.2210 0.2595 0.0084  -0.0040 -0.0236 567  ARG B CA  
13227 C C   . ARG B 569  ? 0.3020 0.2307 0.2687 0.0092  -0.0028 -0.0253 567  ARG B C   
13228 O O   . ARG B 569  ? 0.3415 0.2693 0.3089 0.0123  -0.0015 -0.0260 567  ARG B O   
13229 C CB  . ARG B 569  ? 0.3042 0.2274 0.2685 0.0069  -0.0053 -0.0233 567  ARG B CB  
13230 C CG  . ARG B 569  ? 0.3716 0.2950 0.3373 0.0068  -0.0063 -0.0216 567  ARG B CG  
13231 C CD  . ARG B 569  ? 0.4026 0.3190 0.3637 0.0050  -0.0077 -0.0211 567  ARG B CD  
13232 N NE  . ARG B 569  ? 0.4495 0.3664 0.4118 0.0048  -0.0087 -0.0194 567  ARG B NE  
13233 C CZ  . ARG B 569  ? 0.5225 0.4348 0.4815 0.0027  -0.0099 -0.0183 567  ARG B CZ  
13234 N NH1 . ARG B 569  ? 0.5422 0.4490 0.4967 0.0004  -0.0105 -0.0188 567  ARG B NH1 
13235 N NH2 . ARG B 569  ? 0.5373 0.4506 0.4975 0.0028  -0.0107 -0.0167 567  ARG B NH2 
13236 N N   . GLU B 570  ? 0.2799 0.2088 0.2443 0.0064  -0.0031 -0.0258 568  GLU B N   
13237 C CA  . GLU B 570  ? 0.2889 0.2164 0.2510 0.0069  -0.0022 -0.0274 568  GLU B CA  
13238 C C   . GLU B 570  ? 0.3258 0.2589 0.2916 0.0090  -0.0006 -0.0276 568  GLU B C   
13239 O O   . GLU B 570  ? 0.3189 0.2505 0.2835 0.0110  0.0007  -0.0288 568  GLU B O   
13240 C CB  . GLU B 570  ? 0.3161 0.2433 0.2753 0.0032  -0.0032 -0.0277 568  GLU B CB  
13241 C CG  . GLU B 570  ? 0.3334 0.2539 0.2879 0.0009  -0.0047 -0.0277 568  GLU B CG  
13242 C CD  . GLU B 570  ? 0.4928 0.4148 0.4461 -0.0033 -0.0060 -0.0273 568  GLU B CD  
13243 O OE1 . GLU B 570  ? 0.4836 0.4115 0.4393 -0.0042 -0.0058 -0.0272 568  GLU B OE1 
13244 O OE2 . GLU B 570  ? 0.5215 0.4390 0.4718 -0.0057 -0.0074 -0.0270 568  GLU B OE2 
13245 N N   . SER B 571  ? 0.2841 0.2237 0.2545 0.0086  -0.0007 -0.0265 569  SER B N   
13246 C CA  . SER B 571  ? 0.3077 0.2525 0.2817 0.0104  0.0008  -0.0266 569  SER B CA  
13247 C C   . SER B 571  ? 0.3541 0.2982 0.3300 0.0140  0.0020  -0.0267 569  SER B C   
13248 O O   . SER B 571  ? 0.3145 0.2607 0.2918 0.0158  0.0035  -0.0273 569  SER B O   
13249 C CB  . SER B 571  ? 0.2760 0.2273 0.2543 0.0093  0.0003  -0.0254 569  SER B CB  
13250 O OG  . SER B 571  ? 0.2901 0.2423 0.2712 0.0105  -0.0001 -0.0243 569  SER B OG  
13251 N N   . ALA B 572  ? 0.2825 0.2239 0.2587 0.0150  0.0013  -0.0261 570  ALA B N   
13252 C CA  . ALA B 572  ? 0.2876 0.2287 0.2660 0.0185  0.0023  -0.0262 570  ALA B CA  
13253 C C   . ALA B 572  ? 0.3506 0.2863 0.3253 0.0205  0.0034  -0.0276 570  ALA B C   
13254 O O   . ALA B 572  ? 0.3834 0.3197 0.3602 0.0236  0.0048  -0.0279 570  ALA B O   
13255 C CB  . ALA B 572  ? 0.3117 0.2518 0.2915 0.0190  0.0010  -0.0250 570  ALA B CB  
13256 N N   . ALA B 573  ? 0.3114 0.2420 0.2809 0.0186  0.0029  -0.0286 571  ALA B N   
13257 C CA  . ALA B 573  ? 0.3540 0.2791 0.3193 0.0204  0.0040  -0.0302 571  ALA B CA  
13258 C C   . ALA B 573  ? 0.3635 0.2908 0.3281 0.0206  0.0056  -0.0313 571  ALA B C   
13259 O O   . ALA B 573  ? 0.3629 0.2862 0.3242 0.0224  0.0068  -0.0327 571  ALA B O   
13260 C CB  . ALA B 573  ? 0.3607 0.2784 0.3202 0.0183  0.0025  -0.0308 571  ALA B CB  
13261 N N   . MET B 574  ? 0.3003 0.2337 0.2676 0.0190  0.0056  -0.0307 572  MET B N   
13262 C CA  . MET B 574  ? 0.2981 0.2335 0.2645 0.0191  0.0070  -0.0315 572  MET B CA  
13263 C C   . MET B 574  ? 0.3096 0.2486 0.2797 0.0223  0.0092  -0.0315 572  MET B C   
13264 O O   . MET B 574  ? 0.3150 0.2574 0.2899 0.0238  0.0093  -0.0304 572  MET B O   
13265 C CB  . MET B 574  ? 0.3235 0.2640 0.2916 0.0163  0.0061  -0.0308 572  MET B CB  
13266 C CG  . MET B 574  ? 0.3575 0.2954 0.3222 0.0128  0.0041  -0.0308 572  MET B CG  
13267 S SD  . MET B 574  ? 0.3490 0.2936 0.3170 0.0100  0.0030  -0.0295 572  MET B SD  
13268 C CE  . MET B 574  ? 0.3572 0.2978 0.3206 0.0062  0.0009  -0.0298 572  MET B CE  
13269 N N   . LYS B 575  ? 0.2770 0.2153 0.2448 0.0234  0.0109  -0.0326 573  LYS B N   
13270 C CA  . LYS B 575  ? 0.2758 0.2181 0.2471 0.0262  0.0131  -0.0325 573  LYS B CA  
13271 C C   . LYS B 575  ? 0.2840 0.2329 0.2588 0.0246  0.0132  -0.0315 573  LYS B C   
13272 O O   . LYS B 575  ? 0.2835 0.2326 0.2556 0.0231  0.0133  -0.0320 573  LYS B O   
13273 C CB  . LYS B 575  ? 0.3115 0.2501 0.2784 0.0280  0.0151  -0.0341 573  LYS B CB  
13274 C CG  . LYS B 575  ? 0.3557 0.2985 0.3260 0.0307  0.0177  -0.0340 573  LYS B CG  
13275 C CD  . LYS B 575  ? 0.4215 0.3598 0.3870 0.0329  0.0198  -0.0357 573  LYS B CD  
13276 C CE  . LYS B 575  ? 0.6081 0.5505 0.5770 0.0359  0.0227  -0.0355 573  LYS B CE  
13277 N NZ  . LYS B 575  ? 0.5575 0.5037 0.5262 0.0348  0.0239  -0.0354 573  LYS B NZ  
13278 N N   . TRP B 576  ? 0.2727 0.2265 0.2531 0.0249  0.0129  -0.0301 574  TRP B N   
13279 C CA  . TRP B 576  ? 0.2420 0.2018 0.2260 0.0237  0.0129  -0.0291 574  TRP B CA  
13280 C C   . TRP B 576  ? 0.2318 0.1952 0.2188 0.0259  0.0152  -0.0289 574  TRP B C   
13281 O O   . TRP B 576  ? 0.2520 0.2163 0.2420 0.0282  0.0162  -0.0287 574  TRP B O   
13282 C CB  . TRP B 576  ? 0.2436 0.2065 0.2318 0.0228  0.0113  -0.0278 574  TRP B CB  
13283 C CG  . TRP B 576  ? 0.2251 0.1855 0.2109 0.0204  0.0092  -0.0277 574  TRP B CG  
13284 C CD1 . TRP B 576  ? 0.2795 0.2367 0.2647 0.0204  0.0079  -0.0275 574  TRP B CD1 
13285 C CD2 . TRP B 576  ? 0.2224 0.1835 0.2063 0.0175  0.0080  -0.0276 574  TRP B CD2 
13286 N NE1 . TRP B 576  ? 0.2671 0.2230 0.2501 0.0176  0.0062  -0.0273 574  TRP B NE1 
13287 C CE2 . TRP B 576  ? 0.2565 0.2150 0.2389 0.0158  0.0062  -0.0274 574  TRP B CE2 
13288 C CE3 . TRP B 576  ? 0.2347 0.1984 0.2181 0.0163  0.0083  -0.0277 574  TRP B CE3 
13289 C CZ2 . TRP B 576  ? 0.2883 0.2472 0.2690 0.0129  0.0048  -0.0272 574  TRP B CZ2 
13290 C CZ3 . TRP B 576  ? 0.2512 0.2153 0.2330 0.0136  0.0068  -0.0275 574  TRP B CZ3 
13291 C CH2 . TRP B 576  ? 0.2511 0.2130 0.2317 0.0119  0.0051  -0.0273 574  TRP B CH2 
13292 N N   . THR B 577  ? 0.2486 0.2141 0.2346 0.0250  0.0161  -0.0290 575  THR B N   
13293 C CA  . THR B 577  ? 0.2189 0.1879 0.2074 0.0267  0.0184  -0.0287 575  THR B CA  
13294 C C   . THR B 577  ? 0.2189 0.1925 0.2097 0.0249  0.0181  -0.0277 575  THR B C   
13295 O O   . THR B 577  ? 0.2283 0.2018 0.2176 0.0226  0.0164  -0.0275 575  THR B O   
13296 C CB  . THR B 577  ? 0.2694 0.2351 0.2532 0.0279  0.0203  -0.0301 575  THR B CB  
13297 O OG1 . THR B 577  ? 0.3225 0.2866 0.3017 0.0257  0.0195  -0.0306 575  THR B OG1 
13298 C CG2 . THR B 577  ? 0.2752 0.2354 0.2559 0.0297  0.0206  -0.0313 575  THR B CG2 
13299 N N   . ALA B 578  ? 0.2255 0.2032 0.2200 0.0261  0.0197  -0.0269 576  ALA B N   
13300 C CA  . ALA B 578  ? 0.2158 0.1974 0.2121 0.0247  0.0198  -0.0260 576  ALA B CA  
13301 C C   . ALA B 578  ? 0.2163 0.1997 0.2131 0.0262  0.0225  -0.0259 576  ALA B C   
13302 O O   . ALA B 578  ? 0.2336 0.2185 0.2335 0.0282  0.0240  -0.0257 576  ALA B O   
13303 C CB  . ALA B 578  ? 0.2124 0.1981 0.2141 0.0240  0.0186  -0.0247 576  ALA B CB  
13304 N N   . LEU B 579  ? 0.2280 0.2111 0.2215 0.0253  0.0231  -0.0260 577  LEU B N   
13305 C CA  . LEU B 579  ? 0.2200 0.2041 0.2127 0.0266  0.0258  -0.0261 577  LEU B CA  
13306 C C   . LEU B 579  ? 0.2177 0.2052 0.2117 0.0251  0.0260  -0.0248 577  LEU B C   
13307 O O   . LEU B 579  ? 0.2050 0.1929 0.1987 0.0231  0.0240  -0.0244 577  LEU B O   
13308 C CB  . LEU B 579  ? 0.2621 0.2414 0.2479 0.0269  0.0266  -0.0276 577  LEU B CB  
13309 C CG  . LEU B 579  ? 0.2971 0.2714 0.2797 0.0277  0.0259  -0.0290 577  LEU B CG  
13310 C CD1 . LEU B 579  ? 0.3217 0.2911 0.2970 0.0277  0.0265  -0.0306 577  LEU B CD1 
13311 C CD2 . LEU B 579  ? 0.2837 0.2587 0.2697 0.0304  0.0275  -0.0291 577  LEU B CD2 
13312 N N   . PRO B 580  ? 0.2034 0.1933 0.1986 0.0260  0.0284  -0.0242 578  PRO B N   
13313 C CA  . PRO B 580  ? 0.2053 0.1974 0.2003 0.0246  0.0286  -0.0231 578  PRO B CA  
13314 C C   . PRO B 580  ? 0.2009 0.1894 0.1892 0.0237  0.0282  -0.0240 578  PRO B C   
13315 O O   . PRO B 580  ? 0.2531 0.2395 0.2373 0.0247  0.0300  -0.0248 578  PRO B O   
13316 C CB  . PRO B 580  ? 0.2342 0.2292 0.2316 0.0260  0.0316  -0.0224 578  PRO B CB  
13317 C CG  . PRO B 580  ? 0.2407 0.2363 0.2414 0.0281  0.0325  -0.0228 578  PRO B CG  
13318 C CD  . PRO B 580  ? 0.2232 0.2140 0.2199 0.0284  0.0311  -0.0244 578  PRO B CD  
13319 N N   . GLN B 581  ? 0.2044 0.1924 0.1917 0.0218  0.0257  -0.0238 579  GLN B N   
13320 C CA  . GLN B 581  ? 0.2322 0.2171 0.2135 0.0206  0.0247  -0.0246 579  GLN B CA  
13321 C C   . GLN B 581  ? 0.2377 0.2247 0.2185 0.0196  0.0250  -0.0234 579  GLN B C   
13322 O O   . GLN B 581  ? 0.2407 0.2295 0.2233 0.0183  0.0233  -0.0225 579  GLN B O   
13323 C CB  . GLN B 581  ? 0.2409 0.2246 0.2219 0.0191  0.0218  -0.0250 579  GLN B CB  
13324 C CG  . GLN B 581  ? 0.2359 0.2170 0.2168 0.0199  0.0214  -0.0261 579  GLN B CG  
13325 C CD  . GLN B 581  ? 0.3322 0.3086 0.3072 0.0206  0.0222  -0.0277 579  GLN B CD  
13326 O OE1 . GLN B 581  ? 0.2896 0.2647 0.2603 0.0205  0.0231  -0.0281 579  GLN B OE1 
13327 N NE2 . GLN B 581  ? 0.3679 0.3415 0.3425 0.0213  0.0218  -0.0287 579  GLN B NE2 
13328 N N   . LEU B 582  ? 0.2207 0.2072 0.1987 0.0205  0.0273  -0.0234 580  LEU B N   
13329 C CA  . LEU B 582  ? 0.2115 0.1993 0.1881 0.0196  0.0278  -0.0222 580  LEU B CA  
13330 C C   . LEU B 582  ? 0.2431 0.2278 0.2134 0.0185  0.0263  -0.0229 580  LEU B C   
13331 O O   . LEU B 582  ? 0.2821 0.2636 0.2490 0.0184  0.0253  -0.0244 580  LEU B O   
13332 C CB  . LEU B 582  ? 0.2365 0.2255 0.2132 0.0209  0.0310  -0.0217 580  LEU B CB  
13333 C CG  . LEU B 582  ? 0.3094 0.3028 0.2930 0.0212  0.0320  -0.0202 580  LEU B CG  
13334 C CD1 . LEU B 582  ? 0.2817 0.2760 0.2699 0.0223  0.0319  -0.0207 580  LEU B CD1 
13335 C CD2 . LEU B 582  ? 0.3331 0.3282 0.3167 0.0220  0.0352  -0.0193 580  LEU B CD2 
13336 N N   . ALA B 583  ? 0.2461 0.2317 0.2149 0.0176  0.0261  -0.0217 581  ALA B N   
13337 C CA  . ALA B 583  ? 0.2891 0.2723 0.2523 0.0164  0.0244  -0.0222 581  ALA B CA  
13338 C C   . ALA B 583  ? 0.3425 0.3219 0.2995 0.0172  0.0257  -0.0238 581  ALA B C   
13339 O O   . ALA B 583  ? 0.3800 0.3565 0.3323 0.0162  0.0239  -0.0248 581  ALA B O   
13340 C CB  . ALA B 583  ? 0.2938 0.2786 0.2563 0.0156  0.0243  -0.0205 581  ALA B CB  
13341 N N   . THR B 584  ? 0.2852 0.2645 0.2419 0.0188  0.0287  -0.0239 582  THR B N   
13342 C CA  . THR B 584  ? 0.3045 0.2801 0.2551 0.0198  0.0304  -0.0254 582  THR B CA  
13343 C C   . THR B 584  ? 0.2655 0.2384 0.2159 0.0210  0.0306  -0.0272 582  THR B C   
13344 O O   . THR B 584  ? 0.3058 0.2752 0.2512 0.0221  0.0321  -0.0287 582  THR B O   
13345 C CB  . THR B 584  ? 0.3480 0.3250 0.2982 0.0211  0.0338  -0.0246 582  THR B CB  
13346 O OG1 . THR B 584  ? 0.3553 0.3363 0.3127 0.0220  0.0353  -0.0236 582  THR B OG1 
13347 C CG2 . THR B 584  ? 0.4477 0.4257 0.3956 0.0198  0.0335  -0.0231 582  THR B CG2 
13348 N N   . GLY B 585  ? 0.2761 0.2504 0.2316 0.0209  0.0293  -0.0272 583  GLY B N   
13349 C CA  . GLY B 585  ? 0.2716 0.2432 0.2271 0.0219  0.0292  -0.0287 583  GLY B CA  
13350 C C   . GLY B 585  ? 0.2765 0.2515 0.2389 0.0234  0.0304  -0.0280 583  GLY B C   
13351 O O   . GLY B 585  ? 0.2793 0.2584 0.2463 0.0234  0.0313  -0.0264 583  GLY B O   
13352 N N   . PRO B 586  ? 0.2505 0.2234 0.2137 0.0245  0.0303  -0.0291 584  PRO B N   
13353 C CA  . PRO B 586  ? 0.2407 0.2168 0.2105 0.0259  0.0312  -0.0284 584  PRO B CA  
13354 C C   . PRO B 586  ? 0.2658 0.2439 0.2370 0.0281  0.0347  -0.0281 584  PRO B C   
13355 O O   . PRO B 586  ? 0.2984 0.2737 0.2648 0.0294  0.0367  -0.0292 584  PRO B O   
13356 C CB  . PRO B 586  ? 0.3081 0.2806 0.2771 0.0266  0.0301  -0.0298 584  PRO B CB  
13357 C CG  . PRO B 586  ? 0.3392 0.3062 0.3005 0.0265  0.0301  -0.0315 584  PRO B CG  
13358 C CD  . PRO B 586  ? 0.3185 0.2861 0.2768 0.0244  0.0290  -0.0309 584  PRO B CD  
13359 N N   . ALA B 587  ? 0.2401 0.2230 0.2178 0.0284  0.0354  -0.0266 585  ALA B N   
13360 C CA  . ALA B 587  ? 0.2550 0.2409 0.2354 0.0302  0.0387  -0.0260 585  ALA B CA  
13361 C C   . ALA B 587  ? 0.2544 0.2410 0.2387 0.0325  0.0395  -0.0265 585  ALA B C   
13362 O O   . ALA B 587  ? 0.2630 0.2492 0.2499 0.0323  0.0374  -0.0266 585  ALA B O   
13363 C CB  . ALA B 587  ? 0.2749 0.2660 0.2601 0.0290  0.0390  -0.0239 585  ALA B CB  
13364 N N   . ALA B 588  ? 0.2599 0.2478 0.2448 0.0348  0.0428  -0.0266 586  ALA B N   
13365 C CA  . ALA B 588  ? 0.2480 0.2375 0.2375 0.0372  0.0438  -0.0267 586  ALA B CA  
13366 C C   . ALA B 588  ? 0.2518 0.2473 0.2495 0.0365  0.0432  -0.0248 586  ALA B C   
13367 O O   . ALA B 588  ? 0.2846 0.2833 0.2843 0.0347  0.0432  -0.0234 586  ALA B O   
13368 C CB  . ALA B 588  ? 0.2495 0.2394 0.2376 0.0399  0.0477  -0.0273 586  ALA B CB  
13369 N N   . GLY B 589  ? 0.2489 0.2455 0.2511 0.0380  0.0427  -0.0249 587  GLY B N   
13370 C CA  . GLY B 589  ? 0.2480 0.2503 0.2580 0.0377  0.0423  -0.0232 587  GLY B CA  
13371 C C   . GLY B 589  ? 0.3011 0.3040 0.3151 0.0398  0.0419  -0.0235 587  GLY B C   
13372 O O   . GLY B 589  ? 0.2939 0.2928 0.3047 0.0419  0.0424  -0.0250 587  GLY B O   
13373 N N   . GLU B 590  ? 0.2799 0.2875 0.3008 0.0393  0.0409  -0.0220 588  GLU B N   
13374 C CA  . GLU B 590  ? 0.2822 0.2910 0.3076 0.0413  0.0401  -0.0220 588  GLU B CA  
13375 C C   . GLU B 590  ? 0.2432 0.2477 0.2663 0.0405  0.0369  -0.0228 588  GLU B C   
13376 O O   . GLU B 590  ? 0.2468 0.2510 0.2696 0.0378  0.0345  -0.0223 588  GLU B O   
13377 C CB  . GLU B 590  ? 0.3121 0.3275 0.3455 0.0407  0.0399  -0.0201 588  GLU B CB  
13378 C CG  . GLU B 590  ? 0.4123 0.4327 0.4488 0.0414  0.0431  -0.0191 588  GLU B CG  
13379 C CD  . GLU B 590  ? 0.5218 0.5427 0.5590 0.0450  0.0460  -0.0199 588  GLU B CD  
13380 O OE1 . GLU B 590  ? 0.5871 0.6072 0.6261 0.0470  0.0450  -0.0203 588  GLU B OE1 
13381 O OE2 . GLU B 590  ? 0.6851 0.7072 0.7208 0.0459  0.0492  -0.0199 588  GLU B OE2 
13382 N N   . THR B 591  ? 0.2506 0.2516 0.2721 0.0427  0.0368  -0.0239 589  THR B N   
13383 C CA  . THR B 591  ? 0.2730 0.2691 0.2915 0.0420  0.0339  -0.0247 589  THR B CA  
13384 C C   . THR B 591  ? 0.2538 0.2514 0.2772 0.0433  0.0324  -0.0241 589  THR B C   
13385 O O   . THR B 591  ? 0.2621 0.2623 0.2894 0.0460  0.0340  -0.0238 589  THR B O   
13386 C CB  . THR B 591  ? 0.2850 0.2746 0.2964 0.0432  0.0347  -0.0266 589  THR B CB  
13387 O OG1 . THR B 591  ? 0.3128 0.3013 0.3195 0.0419  0.0359  -0.0271 589  THR B OG1 
13388 C CG2 . THR B 591  ? 0.3018 0.2863 0.3098 0.0421  0.0318  -0.0273 589  THR B CG2 
13389 N N   . ARG B 592  ? 0.2507 0.2470 0.2741 0.0414  0.0294  -0.0238 590  ARG B N   
13390 C CA  . ARG B 592  ? 0.2834 0.2803 0.3106 0.0424  0.0276  -0.0232 590  ARG B CA  
13391 C C   . ARG B 592  ? 0.2651 0.2569 0.2881 0.0409  0.0248  -0.0238 590  ARG B C   
13392 O O   . ARG B 592  ? 0.2447 0.2339 0.2634 0.0386  0.0241  -0.0243 590  ARG B O   
13393 C CB  . ARG B 592  ? 0.2692 0.2724 0.3032 0.0413  0.0266  -0.0215 590  ARG B CB  
13394 C CG  . ARG B 592  ? 0.2656 0.2694 0.2990 0.0380  0.0247  -0.0210 590  ARG B CG  
13395 C CD  . ARG B 592  ? 0.3737 0.3824 0.4133 0.0371  0.0232  -0.0195 590  ARG B CD  
13396 N NE  . ARG B 592  ? 0.3589 0.3687 0.3982 0.0341  0.0219  -0.0190 590  ARG B NE  
13397 C CZ  . ARG B 592  ? 0.3693 0.3767 0.4064 0.0323  0.0194  -0.0191 590  ARG B CZ  
13398 N NH1 . ARG B 592  ? 0.3308 0.3345 0.3657 0.0330  0.0180  -0.0197 590  ARG B NH1 
13399 N NH2 . ARG B 592  ? 0.3392 0.3478 0.3762 0.0299  0.0184  -0.0187 590  ARG B NH2 
13400 N N   . THR B 593  ? 0.2677 0.2582 0.2923 0.0421  0.0233  -0.0236 591  THR B N   
13401 C CA  . THR B 593  ? 0.2588 0.2447 0.2799 0.0406  0.0207  -0.0239 591  THR B CA  
13402 C C   . THR B 593  ? 0.2602 0.2492 0.2838 0.0378  0.0184  -0.0228 591  THR B C   
13403 O O   . THR B 593  ? 0.2660 0.2603 0.2949 0.0376  0.0185  -0.0216 591  THR B O   
13404 C CB  . THR B 593  ? 0.3195 0.3026 0.3410 0.0429  0.0198  -0.0239 591  THR B CB  
13405 O OG1 . THR B 593  ? 0.3557 0.3440 0.3839 0.0442  0.0195  -0.0226 591  THR B OG1 
13406 C CG2 . THR B 593  ? 0.4118 0.3908 0.4299 0.0457  0.0218  -0.0253 591  THR B CG2 
13407 N N   . VAL B 594  ? 0.2446 0.2300 0.2644 0.0357  0.0165  -0.0231 592  VAL B N   
13408 C CA  . VAL B 594  ? 0.2092 0.1964 0.2304 0.0333  0.0143  -0.0222 592  VAL B CA  
13409 C C   . VAL B 594  ? 0.2449 0.2290 0.2653 0.0337  0.0123  -0.0220 592  VAL B C   
13410 O O   . VAL B 594  ? 0.2650 0.2437 0.2807 0.0338  0.0119  -0.0229 592  VAL B O   
13411 C CB  . VAL B 594  ? 0.2551 0.2411 0.2726 0.0306  0.0139  -0.0226 592  VAL B CB  
13412 C CG1 . VAL B 594  ? 0.2592 0.2468 0.2779 0.0283  0.0116  -0.0218 592  VAL B CG1 
13413 C CG2 . VAL B 594  ? 0.2508 0.2395 0.2687 0.0304  0.0159  -0.0227 592  VAL B CG2 
13414 N N   . LEU B 595  ? 0.2451 0.2321 0.2698 0.0339  0.0109  -0.0209 593  LEU B N   
13415 C CA  . LEU B 595  ? 0.2253 0.2097 0.2497 0.0346  0.0090  -0.0205 593  LEU B CA  
13416 C C   . LEU B 595  ? 0.2370 0.2217 0.2608 0.0319  0.0067  -0.0199 593  LEU B C   
13417 O O   . LEU B 595  ? 0.2608 0.2493 0.2868 0.0303  0.0064  -0.0194 593  LEU B O   
13418 C CB  . LEU B 595  ? 0.2503 0.2380 0.2801 0.0370  0.0089  -0.0196 593  LEU B CB  
13419 C CG  . LEU B 595  ? 0.2710 0.2595 0.3023 0.0399  0.0114  -0.0201 593  LEU B CG  
13420 C CD1 . LEU B 595  ? 0.2880 0.2803 0.3251 0.0422  0.0109  -0.0190 593  LEU B CD1 
13421 C CD2 . LEU B 595  ? 0.2719 0.2541 0.2979 0.0413  0.0122  -0.0213 593  LEU B CD2 
13422 N N   . ASN B 596  ? 0.2311 0.2116 0.2518 0.0315  0.0051  -0.0199 594  ASN B N   
13423 C CA  . ASN B 596  ? 0.2182 0.1988 0.2381 0.0291  0.0031  -0.0192 594  ASN B CA  
13424 C C   . ASN B 596  ? 0.2286 0.2135 0.2534 0.0295  0.0019  -0.0181 594  ASN B C   
13425 O O   . ASN B 596  ? 0.2107 0.1956 0.2377 0.0316  0.0014  -0.0176 594  ASN B O   
13426 C CB  . ASN B 596  ? 0.2214 0.1964 0.2372 0.0291  0.0018  -0.0193 594  ASN B CB  
13427 C CG  . ASN B 596  ? 0.2218 0.1962 0.2358 0.0265  0.0000  -0.0187 594  ASN B CG  
13428 O OD1 . ASN B 596  ? 0.2370 0.2150 0.2535 0.0255  -0.0009 -0.0180 594  ASN B OD1 
13429 N ND2 . ASN B 596  ? 0.2639 0.2333 0.2732 0.0254  -0.0006 -0.0190 594  ASN B ND2 
13430 N N   . PRO B 597  ? 0.1965 0.1849 0.2230 0.0276  0.0013  -0.0177 595  PRO B N   
13431 C CA  . PRO B 597  ? 0.2083 0.2006 0.2392 0.0279  0.0000  -0.0167 595  PRO B CA  
13432 C C   . PRO B 597  ? 0.2043 0.1946 0.2345 0.0281  -0.0022 -0.0160 595  PRO B C   
13433 O O   . PRO B 597  ? 0.2202 0.2131 0.2541 0.0291  -0.0033 -0.0152 595  PRO B O   
13434 C CB  . PRO B 597  ? 0.2048 0.1999 0.2362 0.0255  -0.0002 -0.0167 595  PRO B CB  
13435 C CG  . PRO B 597  ? 0.2183 0.2102 0.2448 0.0239  0.0001  -0.0175 595  PRO B CG  
13436 C CD  . PRO B 597  ? 0.2054 0.1944 0.2299 0.0253  0.0017  -0.0182 595  PRO B CD  
13437 N N   . GLY B 598  ? 0.2175 0.2033 0.2430 0.0271  -0.0028 -0.0162 596  GLY B N   
13438 C CA  . GLY B 598  ? 0.2231 0.2065 0.2473 0.0273  -0.0048 -0.0154 596  GLY B CA  
13439 C C   . GLY B 598  ? 0.2209 0.2011 0.2448 0.0298  -0.0049 -0.0152 596  GLY B C   
13440 O O   . GLY B 598  ? 0.2471 0.2255 0.2704 0.0303  -0.0066 -0.0144 596  GLY B O   
13441 N N   . ASP B 599  ? 0.2149 0.1943 0.2390 0.0315  -0.0030 -0.0160 597  ASP B N   
13442 C CA  . ASP B 599  ? 0.2265 0.2029 0.2504 0.0343  -0.0028 -0.0160 597  ASP B CA  
13443 C C   . ASP B 599  ? 0.2485 0.2258 0.2736 0.0361  -0.0003 -0.0169 597  ASP B C   
13444 O O   . ASP B 599  ? 0.2433 0.2175 0.2647 0.0356  0.0011  -0.0180 597  ASP B O   
13445 C CB  . ASP B 599  ? 0.2427 0.2124 0.2609 0.0337  -0.0035 -0.0162 597  ASP B CB  
13446 C CG  . ASP B 599  ? 0.3006 0.2663 0.3181 0.0366  -0.0037 -0.0160 597  ASP B CG  
13447 O OD1 . ASP B 599  ? 0.2712 0.2392 0.2924 0.0394  -0.0026 -0.0161 597  ASP B OD1 
13448 O OD2 . ASP B 599  ? 0.3183 0.2787 0.3317 0.0361  -0.0049 -0.0158 597  ASP B OD2 
13449 N N   . HIS B 600  ? 0.2218 0.2036 0.2522 0.0383  0.0004  -0.0165 598  HIS B N   
13450 C CA  . HIS B 600  ? 0.2466 0.2299 0.2784 0.0398  0.0030  -0.0173 598  HIS B CA  
13451 C C   . HIS B 600  ? 0.2553 0.2334 0.2837 0.0421  0.0043  -0.0183 598  HIS B C   
13452 O O   . HIS B 600  ? 0.2971 0.2754 0.3251 0.0432  0.0066  -0.0192 598  HIS B O   
13453 C CB  . HIS B 600  ? 0.2693 0.2591 0.3079 0.0415  0.0036  -0.0165 598  HIS B CB  
13454 C CG  . HIS B 600  ? 0.2610 0.2559 0.3026 0.0391  0.0030  -0.0160 598  HIS B CG  
13455 N ND1 . HIS B 600  ? 0.3243 0.3251 0.3720 0.0397  0.0031  -0.0151 598  HIS B ND1 
13456 C CD2 . HIS B 600  ? 0.2591 0.2538 0.2984 0.0360  0.0022  -0.0161 598  HIS B CD2 
13457 C CE1 . HIS B 600  ? 0.3602 0.3639 0.4089 0.0371  0.0024  -0.0148 598  HIS B CE1 
13458 N NE2 . HIS B 600  ? 0.3006 0.3005 0.3442 0.0350  0.0019  -0.0154 598  HIS B NE2 
13459 N N   . ARG B 601  ? 0.2578 0.2308 0.2832 0.0428  0.0028  -0.0180 599  ARG B N   
13460 C CA  . ARG B 601  ? 0.2657 0.2326 0.2870 0.0447  0.0038  -0.0190 599  ARG B CA  
13461 C C   . ARG B 601  ? 0.2622 0.2249 0.2777 0.0424  0.0045  -0.0203 599  ARG B C   
13462 O O   . ARG B 601  ? 0.3055 0.2636 0.3174 0.0438  0.0059  -0.0215 599  ARG B O   
13463 C CB  . ARG B 601  ? 0.3295 0.2917 0.3490 0.0459  0.0018  -0.0183 599  ARG B CB  
13464 C CG  . ARG B 601  ? 0.3219 0.2880 0.3470 0.0484  0.0008  -0.0170 599  ARG B CG  
13465 C CD  . ARG B 601  ? 0.3434 0.3050 0.3664 0.0489  -0.0017 -0.0160 599  ARG B CD  
13466 N NE  . ARG B 601  ? 0.3171 0.2774 0.3371 0.0453  -0.0036 -0.0155 599  ARG B NE  
13467 C CZ  . ARG B 601  ? 0.3714 0.3276 0.3887 0.0448  -0.0058 -0.0145 599  ARG B CZ  
13468 N NH1 . ARG B 601  ? 0.3902 0.3430 0.4074 0.0478  -0.0066 -0.0140 599  ARG B NH1 
13469 N NH2 . ARG B 601  ? 0.3748 0.3302 0.3894 0.0414  -0.0072 -0.0141 599  ARG B NH2 
13470 N N   . ASP B 602  ? 0.2716 0.2356 0.2859 0.0390  0.0036  -0.0201 600  ASP B N   
13471 C CA  . ASP B 602  ? 0.2755 0.2361 0.2847 0.0365  0.0040  -0.0211 600  ASP B CA  
13472 C C   . ASP B 602  ? 0.2758 0.2400 0.2862 0.0362  0.0061  -0.0219 600  ASP B C   
13473 O O   . ASP B 602  ? 0.2780 0.2474 0.2914 0.0347  0.0060  -0.0214 600  ASP B O   
13474 C CB  . ASP B 602  ? 0.2835 0.2440 0.2911 0.0332  0.0020  -0.0204 600  ASP B CB  
13475 C CG  . ASP B 602  ? 0.3139 0.2717 0.3168 0.0305  0.0022  -0.0213 600  ASP B CG  
13476 O OD1 . ASP B 602  ? 0.3164 0.2701 0.3158 0.0311  0.0033  -0.0225 600  ASP B OD1 
13477 O OD2 . ASP B 602  ? 0.3114 0.2711 0.3141 0.0278  0.0012  -0.0208 600  ASP B OD2 
13478 N N   . VAL B 603  ? 0.2779 0.2394 0.2858 0.0377  0.0080  -0.0231 601  VAL B N   
13479 C CA  . VAL B 603  ? 0.2689 0.2331 0.2771 0.0375  0.0101  -0.0239 601  VAL B CA  
13480 C C   . VAL B 603  ? 0.2754 0.2377 0.2792 0.0343  0.0096  -0.0245 601  VAL B C   
13481 O O   . VAL B 603  ? 0.3043 0.2610 0.3030 0.0335  0.0091  -0.0253 601  VAL B O   
13482 C CB  . VAL B 603  ? 0.2922 0.2541 0.2990 0.0406  0.0124  -0.0250 601  VAL B CB  
13483 C CG1 . VAL B 603  ? 0.3045 0.2691 0.3112 0.0402  0.0146  -0.0257 601  VAL B CG1 
13484 C CG2 . VAL B 603  ? 0.3035 0.2677 0.3152 0.0440  0.0128  -0.0243 601  VAL B CG2 
13485 N N   . VAL B 604  ? 0.2460 0.2131 0.2520 0.0324  0.0097  -0.0241 602  VAL B N   
13486 C CA  . VAL B 604  ? 0.2176 0.1837 0.2201 0.0293  0.0091  -0.0245 602  VAL B CA  
13487 C C   . VAL B 604  ? 0.2485 0.2136 0.2481 0.0295  0.0110  -0.0256 602  VAL B C   
13488 O O   . VAL B 604  ? 0.2606 0.2222 0.2555 0.0278  0.0106  -0.0265 602  VAL B O   
13489 C CB  . VAL B 604  ? 0.2140 0.1853 0.2198 0.0273  0.0081  -0.0234 602  VAL B CB  
13490 C CG1 . VAL B 604  ? 0.2272 0.1975 0.2296 0.0244  0.0073  -0.0237 602  VAL B CG1 
13491 C CG2 . VAL B 604  ? 0.2174 0.1896 0.2259 0.0274  0.0063  -0.0223 602  VAL B CG2 
13492 N N   . GLY B 605  ? 0.2355 0.2038 0.2379 0.0313  0.0130  -0.0257 603  GLY B N   
13493 C CA  . GLY B 605  ? 0.2649 0.2326 0.2644 0.0313  0.0148  -0.0267 603  GLY B CA  
13494 C C   . GLY B 605  ? 0.2400 0.2120 0.2434 0.0335  0.0170  -0.0264 603  GLY B C   
13495 O O   . GLY B 605  ? 0.2443 0.2188 0.2521 0.0354  0.0173  -0.0257 603  GLY B O   
13496 N N   . SER B 606  ? 0.2338 0.2066 0.2354 0.0331  0.0187  -0.0269 604  SER B N   
13497 C CA  A SER B 606  ? 0.2470 0.2237 0.2517 0.0349  0.0211  -0.0267 604  SER B CA  
13498 C CA  B SER B 606  ? 0.2465 0.2231 0.2510 0.0349  0.0212  -0.0267 604  SER B CA  
13499 C C   . SER B 606  ? 0.2387 0.2189 0.2437 0.0329  0.0216  -0.0262 604  SER B C   
13500 O O   . SER B 606  ? 0.2529 0.2309 0.2538 0.0309  0.0208  -0.0267 604  SER B O   
13501 C CB  A SER B 606  ? 0.3242 0.2975 0.3255 0.0374  0.0234  -0.0280 604  SER B CB  
13502 C CB  B SER B 606  ? 0.3233 0.2962 0.3240 0.0372  0.0234  -0.0281 604  SER B CB  
13503 O OG  A SER B 606  ? 0.3344 0.3040 0.3296 0.0360  0.0237  -0.0292 604  SER B OG  
13504 O OG  B SER B 606  ? 0.4065 0.3764 0.4073 0.0396  0.0233  -0.0285 604  SER B OG  
13505 N N   . VAL B 607  ? 0.2190 0.2045 0.2290 0.0335  0.0228  -0.0252 605  VAL B N   
13506 C CA  . VAL B 607  ? 0.2059 0.1947 0.2166 0.0318  0.0234  -0.0245 605  VAL B CA  
13507 C C   . VAL B 607  ? 0.2233 0.2144 0.2351 0.0335  0.0264  -0.0245 605  VAL B C   
13508 O O   . VAL B 607  ? 0.2232 0.2168 0.2390 0.0356  0.0276  -0.0241 605  VAL B O   
13509 C CB  . VAL B 607  ? 0.2026 0.1955 0.2180 0.0302  0.0217  -0.0231 605  VAL B CB  
13510 C CG1 . VAL B 607  ? 0.2279 0.2245 0.2494 0.0318  0.0219  -0.0222 605  VAL B CG1 
13511 C CG2 . VAL B 607  ? 0.2275 0.2232 0.2432 0.0286  0.0224  -0.0225 605  VAL B CG2 
13512 N N   . THR B 608  ? 0.2151 0.2056 0.2234 0.0326  0.0275  -0.0248 606  THR B N   
13513 C CA  . THR B 608  ? 0.2079 0.2009 0.2169 0.0337  0.0304  -0.0245 606  THR B CA  
13514 C C   . THR B 608  ? 0.1945 0.1918 0.2065 0.0317  0.0301  -0.0231 606  THR B C   
13515 O O   . THR B 608  ? 0.2254 0.2215 0.2346 0.0296  0.0288  -0.0230 606  THR B O   
13516 C CB  . THR B 608  ? 0.2481 0.2370 0.2504 0.0342  0.0319  -0.0259 606  THR B CB  
13517 O OG1 . THR B 608  ? 0.2424 0.2270 0.2421 0.0362  0.0321  -0.0273 606  THR B OG1 
13518 C CG2 . THR B 608  ? 0.2478 0.2393 0.2504 0.0351  0.0350  -0.0255 606  THR B CG2 
13519 N N   . GLU B 609  ? 0.2070 0.2092 0.2247 0.0323  0.0313  -0.0218 607  GLU B N   
13520 C CA  . GLU B 609  ? 0.2474 0.2533 0.2681 0.0303  0.0307  -0.0204 607  GLU B CA  
13521 C C   . GLU B 609  ? 0.2145 0.2217 0.2337 0.0300  0.0331  -0.0200 607  GLU B C   
13522 O O   . GLU B 609  ? 0.2292 0.2357 0.2464 0.0317  0.0357  -0.0205 607  GLU B O   
13523 C CB  . GLU B 609  ? 0.2458 0.2560 0.2735 0.0305  0.0300  -0.0192 607  GLU B CB  
13524 C CG  . GLU B 609  ? 0.2854 0.2940 0.3138 0.0301  0.0271  -0.0196 607  GLU B CG  
13525 C CD  . GLU B 609  ? 0.3706 0.3830 0.4053 0.0303  0.0261  -0.0185 607  GLU B CD  
13526 O OE1 . GLU B 609  ? 0.4546 0.4708 0.4937 0.0316  0.0278  -0.0178 607  GLU B OE1 
13527 O OE2 . GLU B 609  ? 0.3357 0.3476 0.3712 0.0291  0.0235  -0.0183 607  GLU B OE2 
13528 N N   . THR B 610  ? 0.2076 0.2163 0.2273 0.0278  0.0323  -0.0189 608  THR B N   
13529 C CA  . THR B 610  ? 0.2004 0.2093 0.2174 0.0270  0.0340  -0.0184 608  THR B CA  
13530 C C   . THR B 610  ? 0.2157 0.2294 0.2376 0.0273  0.0362  -0.0170 608  THR B C   
13531 O O   . THR B 610  ? 0.2439 0.2610 0.2713 0.0266  0.0353  -0.0159 608  THR B O   
13532 C CB  . THR B 610  ? 0.2141 0.2223 0.2296 0.0246  0.0319  -0.0179 608  THR B CB  
13533 O OG1 . THR B 610  ? 0.2190 0.2236 0.2311 0.0241  0.0296  -0.0190 608  THR B OG1 
13534 C CG2 . THR B 610  ? 0.2288 0.2365 0.2406 0.0239  0.0333  -0.0174 608  THR B CG2 
13535 N N   . SER B 611  ? 0.2039 0.2179 0.2236 0.0283  0.0391  -0.0169 609  SER B N   
13536 C CA  . SER B 611  ? 0.2077 0.2264 0.2316 0.0281  0.0413  -0.0154 609  SER B CA  
13537 C C   . SER B 611  ? 0.2577 0.2773 0.2818 0.0255  0.0403  -0.0139 609  SER B C   
13538 O O   . SER B 611  ? 0.2271 0.2434 0.2466 0.0243  0.0388  -0.0143 609  SER B O   
13539 C CB  . SER B 611  ? 0.2638 0.2823 0.2847 0.0297  0.0449  -0.0157 609  SER B CB  
13540 O OG  . SER B 611  ? 0.2591 0.2745 0.2736 0.0287  0.0452  -0.0159 609  SER B OG  
13541 N N   . GLU B 612  ? 0.2482 0.2721 0.2777 0.0246  0.0411  -0.0123 610  GLU B N   
13542 C CA  . GLU B 612  ? 0.2692 0.2935 0.2987 0.0222  0.0402  -0.0109 610  GLU B CA  
13543 C C   . GLU B 612  ? 0.2910 0.3133 0.3147 0.0218  0.0419  -0.0107 610  GLU B C   
13544 O O   . GLU B 612  ? 0.2660 0.2862 0.2868 0.0202  0.0405  -0.0102 610  GLU B O   
13545 C CB  . GLU B 612  ? 0.3048 0.3341 0.3411 0.0212  0.0407  -0.0091 610  GLU B CB  
13546 C CG  . GLU B 612  ? 0.3530 0.3841 0.3947 0.0213  0.0385  -0.0093 610  GLU B CG  
13547 C CD  . GLU B 612  ? 0.4406 0.4767 0.4891 0.0202  0.0388  -0.0075 610  GLU B CD  
13548 O OE1 . GLU B 612  ? 0.5793 0.6165 0.6282 0.0184  0.0396  -0.0061 610  GLU B OE1 
13549 O OE2 . GLU B 612  ? 0.4644 0.5032 0.5179 0.0210  0.0381  -0.0076 610  GLU B OE2 
13550 N N   . GLU B 613  ? 0.2514 0.2739 0.2730 0.0235  0.0450  -0.0111 611  GLU B N   
13551 C CA  . GLU B 613  ? 0.2688 0.2888 0.2841 0.0232  0.0466  -0.0111 611  GLU B CA  
13552 C C   . GLU B 613  ? 0.2804 0.2953 0.2894 0.0230  0.0443  -0.0125 611  GLU B C   
13553 O O   . GLU B 613  ? 0.2854 0.2983 0.2903 0.0217  0.0437  -0.0120 611  GLU B O   
13554 C CB  . GLU B 613  ? 0.3273 0.3484 0.3413 0.0253  0.0503  -0.0115 611  GLU B CB  
13555 N N   . ASP B 614  ? 0.2379 0.2507 0.2462 0.0243  0.0430  -0.0142 612  ASP B N   
13556 C CA  . ASP B 614  ? 0.2271 0.2354 0.2298 0.0238  0.0408  -0.0155 612  ASP B CA  
13557 C C   . ASP B 614  ? 0.2231 0.2312 0.2270 0.0218  0.0377  -0.0149 612  ASP B C   
13558 O O   . ASP B 614  ? 0.2381 0.2433 0.2375 0.0209  0.0361  -0.0153 612  ASP B O   
13559 C CB  . ASP B 614  ? 0.2529 0.2587 0.2541 0.0255  0.0404  -0.0175 612  ASP B CB  
13560 C CG  . ASP B 614  ? 0.3090 0.3130 0.3059 0.0275  0.0433  -0.0186 612  ASP B CG  
13561 O OD1 . ASP B 614  ? 0.3520 0.3553 0.3449 0.0271  0.0449  -0.0182 612  ASP B OD1 
13562 O OD2 . ASP B 614  ? 0.3224 0.3254 0.3198 0.0294  0.0439  -0.0198 612  ASP B OD2 
13563 N N   . ALA B 615  ? 0.2213 0.2324 0.2313 0.0212  0.0367  -0.0140 613  ALA B N   
13564 C CA  . ALA B 615  ? 0.2125 0.2234 0.2237 0.0194  0.0339  -0.0133 613  ALA B CA  
13565 C C   . ALA B 615  ? 0.2231 0.2336 0.2317 0.0180  0.0343  -0.0120 613  ALA B C   
13566 O O   . ALA B 615  ? 0.2228 0.2311 0.2283 0.0171  0.0324  -0.0120 613  ALA B O   
13567 C CB  . ALA B 615  ? 0.2546 0.2687 0.2724 0.0190  0.0330  -0.0125 613  ALA B CB  
13568 N N   . ARG B 616  ? 0.2548 0.2676 0.2647 0.0180  0.0368  -0.0107 614  ARG B N   
13569 C CA  . ARG B 616  ? 0.2318 0.2439 0.2389 0.0167  0.0373  -0.0093 614  ARG B CA  
13570 C C   . ARG B 616  ? 0.2272 0.2358 0.2271 0.0171  0.0375  -0.0101 614  ARG B C   
13571 O O   . ARG B 616  ? 0.2374 0.2442 0.2341 0.0160  0.0362  -0.0095 614  ARG B O   
13572 C CB  . ARG B 616  ? 0.2815 0.2968 0.2915 0.0165  0.0401  -0.0077 614  ARG B CB  
13573 C CG  . ARG B 616  ? 0.2952 0.3135 0.3118 0.0153  0.0393  -0.0065 614  ARG B CG  
13574 C CD  . ARG B 616  ? 0.3929 0.4144 0.4122 0.0146  0.0419  -0.0046 614  ARG B CD  
13575 N NE  . ARG B 616  ? 0.3883 0.4126 0.4100 0.0162  0.0446  -0.0051 614  ARG B NE  
13576 C CZ  . ARG B 616  ? 0.4210 0.4485 0.4487 0.0168  0.0443  -0.0053 614  ARG B CZ  
13577 N NH1 . ARG B 616  ? 0.3390 0.3669 0.3704 0.0158  0.0415  -0.0051 614  ARG B NH1 
13578 N NH2 . ARG B 616  ? 0.3844 0.4144 0.4140 0.0186  0.0468  -0.0057 614  ARG B NH2 
13579 N N   . ARG B 617  ? 0.2269 0.2344 0.2241 0.0186  0.0391  -0.0115 615  ARG B N   
13580 C CA  . ARG B 617  ? 0.2594 0.2633 0.2494 0.0189  0.0391  -0.0125 615  ARG B CA  
13581 C C   . ARG B 617  ? 0.2350 0.2364 0.2229 0.0181  0.0357  -0.0133 615  ARG B C   
13582 O O   . ARG B 617  ? 0.2499 0.2492 0.2332 0.0173  0.0347  -0.0131 615  ARG B O   
13583 C CB  . ARG B 617  ? 0.2869 0.2896 0.2745 0.0209  0.0412  -0.0142 615  ARG B CB  
13584 C CG  . ARG B 617  ? 0.3226 0.3213 0.3023 0.0211  0.0413  -0.0153 615  ARG B CG  
13585 C CD  . ARG B 617  ? 0.3962 0.3940 0.3731 0.0231  0.0444  -0.0165 615  ARG B CD  
13586 N NE  . ARG B 617  ? 0.3937 0.3904 0.3719 0.0245  0.0440  -0.0182 615  ARG B NE  
13587 C CZ  . ARG B 617  ? 0.4898 0.4824 0.4635 0.0248  0.0423  -0.0200 615  ARG B CZ  
13588 N NH1 . ARG B 617  ? 0.4563 0.4459 0.4241 0.0236  0.0408  -0.0204 615  ARG B NH1 
13589 N NH2 . ARG B 617  ? 0.5120 0.5035 0.4870 0.0261  0.0421  -0.0215 615  ARG B NH2 
13590 N N   . ALA B 618  ? 0.2243 0.2261 0.2157 0.0183  0.0339  -0.0141 616  ALA B N   
13591 C CA  . ALA B 618  ? 0.1945 0.1944 0.1843 0.0175  0.0308  -0.0149 616  ALA B CA  
13592 C C   . ALA B 618  ? 0.2103 0.2108 0.2005 0.0160  0.0292  -0.0134 616  ALA B C   
13593 O O   . ALA B 618  ? 0.2136 0.2121 0.2001 0.0154  0.0274  -0.0137 616  ALA B O   
13594 C CB  . ALA B 618  ? 0.2071 0.2078 0.2011 0.0178  0.0294  -0.0157 616  ALA B CB  
13595 N N   . VAL B 619  ? 0.2272 0.2300 0.2217 0.0155  0.0297  -0.0119 617  VAL B N   
13596 C CA  . VAL B 619  ? 0.2156 0.2185 0.2103 0.0142  0.0282  -0.0106 617  VAL B CA  
13597 C C   . VAL B 619  ? 0.2399 0.2410 0.2293 0.0139  0.0289  -0.0098 617  VAL B C   
13598 O O   . VAL B 619  ? 0.2368 0.2366 0.2238 0.0133  0.0270  -0.0095 617  VAL B O   
13599 C CB  . VAL B 619  ? 0.2098 0.2151 0.2100 0.0136  0.0286  -0.0092 617  VAL B CB  
13600 C CG1 . VAL B 619  ? 0.2713 0.2760 0.2712 0.0124  0.0270  -0.0078 617  VAL B CG1 
13601 C CG2 . VAL B 619  ? 0.2368 0.2436 0.2418 0.0139  0.0274  -0.0100 617  VAL B CG2 
13602 N N   . ARG B 620  ? 0.2507 0.2519 0.2380 0.0144  0.0316  -0.0096 618  ARG B N   
13603 C CA  . ARG B 620  ? 0.2837 0.2830 0.2653 0.0142  0.0324  -0.0089 618  ARG B CA  
13604 C C   . ARG B 620  ? 0.2440 0.2406 0.2203 0.0143  0.0307  -0.0103 618  ARG B C   
13605 O O   . ARG B 620  ? 0.2561 0.2512 0.2287 0.0137  0.0293  -0.0097 618  ARG B O   
13606 C CB  . ARG B 620  ? 0.2953 0.2953 0.2757 0.0148  0.0359  -0.0085 618  ARG B CB  
13607 C CG  . ARG B 620  ? 0.4843 0.4865 0.4677 0.0139  0.0375  -0.0063 618  ARG B CG  
13608 C CD  . ARG B 620  ? 0.5200 0.5234 0.5022 0.0145  0.0412  -0.0059 618  ARG B CD  
13609 N NE  . ARG B 620  ? 0.6253 0.6317 0.6129 0.0154  0.0429  -0.0063 618  ARG B NE  
13610 C CZ  . ARG B 620  ? 0.5394 0.5458 0.5261 0.0171  0.0445  -0.0079 618  ARG B CZ  
13611 N NH1 . ARG B 620  ? 0.5610 0.5642 0.5412 0.0179  0.0448  -0.0093 618  ARG B NH1 
13612 N NH2 . ARG B 620  ? 0.4775 0.4869 0.4697 0.0179  0.0457  -0.0082 618  ARG B NH2 
13613 N N   . LEU B 621  ? 0.2391 0.2349 0.2150 0.0152  0.0305  -0.0122 619  LEU B N   
13614 C CA  . LEU B 621  ? 0.2346 0.2277 0.2057 0.0151  0.0287  -0.0136 619  LEU B CA  
13615 C C   . LEU B 621  ? 0.2624 0.2557 0.2347 0.0141  0.0254  -0.0133 619  LEU B C   
13616 O O   . LEU B 621  ? 0.2814 0.2731 0.2496 0.0136  0.0238  -0.0135 619  LEU B O   
13617 C CB  . LEU B 621  ? 0.2567 0.2487 0.2276 0.0160  0.0291  -0.0156 619  LEU B CB  
13618 C CG  . LEU B 621  ? 0.2840 0.2753 0.2525 0.0173  0.0322  -0.0162 619  LEU B CG  
13619 C CD1 . LEU B 621  ? 0.2770 0.2673 0.2465 0.0185  0.0324  -0.0180 619  LEU B CD1 
13620 C CD2 . LEU B 621  ? 0.3474 0.3357 0.3085 0.0172  0.0326  -0.0165 619  LEU B CD2 
13621 N N   . ALA B 622  ? 0.2201 0.2154 0.1981 0.0139  0.0245  -0.0129 620  ALA B N   
13622 C CA  . ALA B 622  ? 0.2247 0.2205 0.2041 0.0132  0.0217  -0.0126 620  ALA B CA  
13623 C C   . ALA B 622  ? 0.2415 0.2371 0.2193 0.0126  0.0211  -0.0109 620  ALA B C   
13624 O O   . ALA B 622  ? 0.2399 0.2349 0.2157 0.0122  0.0189  -0.0109 620  ALA B O   
13625 C CB  . ALA B 622  ? 0.2193 0.2171 0.2047 0.0132  0.0211  -0.0126 620  ALA B CB  
13626 N N   . ALA B 623  ? 0.2198 0.2160 0.1983 0.0126  0.0230  -0.0095 621  ALA B N   
13627 C CA  . ALA B 623  ? 0.2235 0.2191 0.2002 0.0120  0.0225  -0.0078 621  ALA B CA  
13628 C C   . ALA B 623  ? 0.2630 0.2565 0.2333 0.0120  0.0221  -0.0079 621  ALA B C   
13629 O O   . ALA B 623  ? 0.2487 0.2415 0.2170 0.0117  0.0202  -0.0071 621  ALA B O   
13630 C CB  . ALA B 623  ? 0.2345 0.2310 0.2132 0.0118  0.0249  -0.0062 621  ALA B CB  
13631 N N   . ASP B 624  ? 0.2694 0.2618 0.2362 0.0124  0.0238  -0.0089 622  ASP B N   
13632 C CA  . ASP B 624  ? 0.2824 0.2726 0.2426 0.0123  0.0235  -0.0092 622  ASP B CA  
13633 C C   . ASP B 624  ? 0.3051 0.2946 0.2638 0.0120  0.0204  -0.0101 622  ASP B C   
13634 O O   . ASP B 624  ? 0.3864 0.3747 0.3409 0.0116  0.0188  -0.0096 622  ASP B O   
13635 C CB  . ASP B 624  ? 0.3633 0.3522 0.3202 0.0130  0.0259  -0.0104 622  ASP B CB  
13636 C CG  . ASP B 624  ? 0.4217 0.4115 0.3795 0.0134  0.0293  -0.0094 622  ASP B CG  
13637 O OD1 . ASP B 624  ? 0.4961 0.4869 0.4556 0.0128  0.0297  -0.0074 622  ASP B OD1 
13638 O OD2 . ASP B 624  ? 0.4702 0.4597 0.4270 0.0142  0.0316  -0.0105 622  ASP B OD2 
13639 N N   . ALA B 625  ? 0.3046 0.2950 0.2666 0.0121  0.0194  -0.0115 623  ALA B N   
13640 C CA  . ALA B 625  ? 0.3764 0.3666 0.3376 0.0116  0.0166  -0.0125 623  ALA B CA  
13641 C C   . ALA B 625  ? 0.3266 0.3187 0.2914 0.0113  0.0143  -0.0115 623  ALA B C   
13642 O O   . ALA B 625  ? 0.3156 0.3081 0.2800 0.0109  0.0119  -0.0120 623  ALA B O   
13643 C CB  . ALA B 625  ? 0.4232 0.4133 0.3863 0.0118  0.0167  -0.0143 623  ALA B CB  
13644 N N   . ALA B 626  ? 0.2665 0.2596 0.2347 0.0115  0.0150  -0.0101 624  ALA B N   
13645 C CA  . ALA B 626  ? 0.2433 0.2379 0.2150 0.0115  0.0130  -0.0094 624  ALA B CA  
13646 C C   . ALA B 626  ? 0.2561 0.2505 0.2250 0.0113  0.0107  -0.0087 624  ALA B C   
13647 O O   . ALA B 626  ? 0.2817 0.2775 0.2525 0.0113  0.0086  -0.0091 624  ALA B O   
13648 C CB  . ALA B 626  ? 0.2336 0.2289 0.2091 0.0116  0.0141  -0.0080 624  ALA B CB  
13649 N N   . PRO B 627  ? 0.2611 0.2541 0.2256 0.0113  0.0109  -0.0077 625  PRO B N   
13650 C CA  . PRO B 627  ? 0.3018 0.2948 0.2638 0.0112  0.0084  -0.0070 625  PRO B CA  
13651 C C   . PRO B 627  ? 0.2709 0.2644 0.2313 0.0107  0.0065  -0.0085 625  PRO B C   
13652 O O   . PRO B 627  ? 0.2750 0.2701 0.2366 0.0107  0.0041  -0.0082 625  PRO B O   
13653 C CB  . PRO B 627  ? 0.3144 0.3054 0.2712 0.0112  0.0093  -0.0057 625  PRO B CB  
13654 C CG  . PRO B 627  ? 0.3783 0.3687 0.3363 0.0112  0.0123  -0.0052 625  PRO B CG  
13655 C CD  . PRO B 627  ? 0.2977 0.2891 0.2593 0.0113  0.0134  -0.0069 625  PRO B CD  
13656 N N   . ASP B 628  ? 0.2620 0.2543 0.2199 0.0103  0.0075  -0.0100 626  ASP B N   
13657 C CA  . ASP B 628  ? 0.2815 0.2738 0.2374 0.0096  0.0056  -0.0113 626  ASP B CA  
13658 C C   . ASP B 628  ? 0.2902 0.2848 0.2512 0.0094  0.0043  -0.0121 626  ASP B C   
13659 O O   . ASP B 628  ? 0.2964 0.2923 0.2573 0.0088  0.0020  -0.0124 626  ASP B O   
13660 C CB  . ASP B 628  ? 0.3277 0.3175 0.2797 0.0092  0.0070  -0.0129 626  ASP B CB  
13661 C CG  . ASP B 628  ? 0.4324 0.4198 0.3783 0.0093  0.0080  -0.0124 626  ASP B CG  
13662 O OD1 . ASP B 628  ? 0.4347 0.4224 0.3787 0.0092  0.0067  -0.0110 626  ASP B OD1 
13663 O OD2 . ASP B 628  ? 0.4945 0.4798 0.4376 0.0095  0.0101  -0.0134 626  ASP B OD2 
13664 N N   . TRP B 629  ? 0.2494 0.2447 0.2147 0.0098  0.0057  -0.0123 627  TRP B N   
13665 C CA  . TRP B 629  ? 0.2378 0.2351 0.2075 0.0097  0.0046  -0.0130 627  TRP B CA  
13666 C C   . TRP B 629  ? 0.2089 0.2084 0.1815 0.0101  0.0030  -0.0118 627  TRP B C   
13667 O O   . TRP B 629  ? 0.2279 0.2294 0.2023 0.0098  0.0012  -0.0121 627  TRP B O   
13668 C CB  . TRP B 629  ? 0.2360 0.2332 0.2090 0.0101  0.0065  -0.0136 627  TRP B CB  
13669 C CG  . TRP B 629  ? 0.2080 0.2071 0.1852 0.0099  0.0055  -0.0142 627  TRP B CG  
13670 C CD1 . TRP B 629  ? 0.2325 0.2330 0.2143 0.0104  0.0057  -0.0138 627  TRP B CD1 
13671 C CD2 . TRP B 629  ? 0.2018 0.2014 0.1788 0.0091  0.0039  -0.0153 627  TRP B CD2 
13672 N NE1 . TRP B 629  ? 0.2308 0.2328 0.2151 0.0101  0.0045  -0.0145 627  TRP B NE1 
13673 C CE2 . TRP B 629  ? 0.2148 0.2163 0.1963 0.0092  0.0035  -0.0154 627  TRP B CE2 
13674 C CE3 . TRP B 629  ? 0.2301 0.2286 0.2033 0.0081  0.0029  -0.0162 627  TRP B CE3 
13675 C CZ2 . TRP B 629  ? 0.2202 0.2227 0.2026 0.0084  0.0021  -0.0163 627  TRP B CZ2 
13676 C CZ3 . TRP B 629  ? 0.2431 0.2426 0.2175 0.0071  0.0014  -0.0170 627  TRP B CZ3 
13677 C CH2 . TRP B 629  ? 0.2607 0.2623 0.2397 0.0073  0.0011  -0.0170 627  TRP B CH2 
13678 N N   . ALA B 630  ? 0.2437 0.2428 0.2166 0.0108  0.0037  -0.0103 628  ALA B N   
13679 C CA  . ALA B 630  ? 0.2305 0.2312 0.2058 0.0115  0.0022  -0.0091 628  ALA B CA  
13680 C C   . ALA B 630  ? 0.2586 0.2605 0.2316 0.0113  -0.0002 -0.0089 628  ALA B C   
13681 O O   . ALA B 630  ? 0.2746 0.2787 0.2503 0.0117  -0.0019 -0.0085 628  ALA B O   
13682 C CB  . ALA B 630  ? 0.2682 0.2676 0.2433 0.0121  0.0033  -0.0075 628  ALA B CB  
13683 N N   . ALA B 631  ? 0.2437 0.2441 0.2119 0.0106  -0.0004 -0.0091 629  ALA B N   
13684 C CA  . ALA B 631  ? 0.2495 0.2510 0.2153 0.0103  -0.0029 -0.0087 629  ALA B CA  
13685 C C   . ALA B 631  ? 0.2693 0.2727 0.2363 0.0093  -0.0044 -0.0100 629  ALA B C   
13686 O O   . ALA B 631  ? 0.2829 0.2881 0.2490 0.0089  -0.0067 -0.0097 629  ALA B O   
13687 C CB  . ALA B 631  ? 0.2844 0.2833 0.2442 0.0099  -0.0026 -0.0084 629  ALA B CB  
13688 N N   . VAL B 632  ? 0.2526 0.2559 0.2216 0.0088  -0.0034 -0.0114 630  VAL B N   
13689 C CA  . VAL B 632  ? 0.2401 0.2454 0.2105 0.0078  -0.0049 -0.0124 630  VAL B CA  
13690 C C   . VAL B 632  ? 0.2579 0.2667 0.2332 0.0085  -0.0061 -0.0117 630  VAL B C   
13691 O O   . VAL B 632  ? 0.2565 0.2655 0.2351 0.0095  -0.0049 -0.0114 630  VAL B O   
13692 C CB  . VAL B 632  ? 0.2557 0.2595 0.2269 0.0072  -0.0035 -0.0139 630  VAL B CB  
13693 C CG1 . VAL B 632  ? 0.2528 0.2586 0.2257 0.0060  -0.0050 -0.0148 630  VAL B CG1 
13694 C CG2 . VAL B 632  ? 0.2597 0.2600 0.2260 0.0067  -0.0022 -0.0147 630  VAL B CG2 
13695 N N   . PRO B 633  ? 0.2478 0.2595 0.2237 0.0081  -0.0084 -0.0114 631  PRO B N   
13696 C CA  . PRO B 633  ? 0.2413 0.2565 0.2217 0.0091  -0.0093 -0.0107 631  PRO B CA  
13697 C C   . PRO B 633  ? 0.2445 0.2606 0.2289 0.0091  -0.0083 -0.0115 631  PRO B C   
13698 O O   . PRO B 633  ? 0.2291 0.2445 0.2132 0.0079  -0.0078 -0.0127 631  PRO B O   
13699 C CB  . PRO B 633  ? 0.2293 0.2476 0.2094 0.0082  -0.0119 -0.0105 631  PRO B CB  
13700 C CG  . PRO B 633  ? 0.2868 0.3027 0.2615 0.0072  -0.0125 -0.0106 631  PRO B CG  
13701 C CD  . PRO B 633  ? 0.2315 0.2433 0.2037 0.0067  -0.0102 -0.0117 631  PRO B CD  
13702 N N   . PRO B 634  ? 0.2280 0.2456 0.2160 0.0106  -0.0080 -0.0109 632  PRO B N   
13703 C CA  . PRO B 634  ? 0.2422 0.2607 0.2338 0.0107  -0.0070 -0.0116 632  PRO B CA  
13704 C C   . PRO B 634  ? 0.2262 0.2470 0.2191 0.0093  -0.0079 -0.0125 632  PRO B C   
13705 O O   . PRO B 634  ? 0.2039 0.2238 0.1976 0.0086  -0.0069 -0.0134 632  PRO B O   
13706 C CB  . PRO B 634  ? 0.2395 0.2594 0.2341 0.0125  -0.0072 -0.0107 632  PRO B CB  
13707 C CG  . PRO B 634  ? 0.2605 0.2786 0.2527 0.0134  -0.0074 -0.0095 632  PRO B CG  
13708 C CD  . PRO B 634  ? 0.2480 0.2656 0.2362 0.0123  -0.0083 -0.0094 632  PRO B CD  
13709 N N   . SER B 635  ? 0.2400 0.2639 0.2330 0.0088  -0.0098 -0.0121 633  SER B N   
13710 C CA  . SER B 635  ? 0.2509 0.2771 0.2451 0.0072  -0.0106 -0.0129 633  SER B CA  
13711 C C   . SER B 635  ? 0.2151 0.2383 0.2061 0.0053  -0.0103 -0.0140 633  SER B C   
13712 O O   . SER B 635  ? 0.2188 0.2423 0.2109 0.0041  -0.0100 -0.0148 633  SER B O   
13713 C CB  . SER B 635  ? 0.3056 0.3361 0.3008 0.0069  -0.0128 -0.0121 633  SER B CB  
13714 O OG  . SER B 635  ? 0.4004 0.4296 0.3918 0.0063  -0.0140 -0.0118 633  SER B OG  
13715 N N   . GLU B 636  ? 0.2155 0.2356 0.2024 0.0051  -0.0101 -0.0140 634  GLU B N   
13716 C CA  . GLU B 636  ? 0.2295 0.2463 0.2130 0.0036  -0.0097 -0.0152 634  GLU B CA  
13717 C C   . GLU B 636  ? 0.2136 0.2274 0.1975 0.0042  -0.0074 -0.0159 634  GLU B C   
13718 O O   . GLU B 636  ? 0.2234 0.2354 0.2065 0.0031  -0.0069 -0.0169 634  GLU B O   
13719 C CB  . GLU B 636  ? 0.2422 0.2566 0.2207 0.0032  -0.0102 -0.0151 634  GLU B CB  
13720 C CG  . GLU B 636  ? 0.3384 0.3487 0.3128 0.0019  -0.0096 -0.0165 634  GLU B CG  
13721 C CD  . GLU B 636  ? 0.4481 0.4590 0.4232 -0.0001 -0.0106 -0.0174 634  GLU B CD  
13722 O OE1 . GLU B 636  ? 0.4162 0.4306 0.3928 -0.0012 -0.0126 -0.0170 634  GLU B OE1 
13723 O OE2 . GLU B 636  ? 0.4003 0.4084 0.3745 -0.0005 -0.0093 -0.0185 634  GLU B OE2 
13724 N N   . ARG B 637  ? 0.1979 0.2112 0.1832 0.0058  -0.0061 -0.0152 635  ARG B N   
13725 C CA  . ARG B 637  ? 0.2045 0.2158 0.1911 0.0064  -0.0041 -0.0158 635  ARG B CA  
13726 C C   . ARG B 637  ? 0.2020 0.2152 0.1921 0.0060  -0.0043 -0.0162 635  ARG B C   
13727 O O   . ARG B 637  ? 0.2146 0.2260 0.2046 0.0055  -0.0034 -0.0171 635  ARG B O   
13728 C CB  . ARG B 637  ? 0.1833 0.1941 0.1711 0.0080  -0.0029 -0.0149 635  ARG B CB  
13729 C CG  . ARG B 637  ? 0.2012 0.2102 0.1855 0.0084  -0.0027 -0.0142 635  ARG B CG  
13730 C CD  . ARG B 637  ? 0.2203 0.2280 0.2054 0.0096  -0.0011 -0.0134 635  ARG B CD  
13731 N NE  . ARG B 637  ? 0.2192 0.2289 0.2078 0.0106  -0.0017 -0.0126 635  ARG B NE  
13732 C CZ  . ARG B 637  ? 0.2234 0.2331 0.2116 0.0116  -0.0021 -0.0113 635  ARG B CZ  
13733 N NH1 . ARG B 637  ? 0.2852 0.2937 0.2699 0.0115  -0.0023 -0.0106 635  ARG B NH1 
13734 N NH2 . ARG B 637  ? 0.2282 0.2391 0.2196 0.0127  -0.0023 -0.0107 635  ARG B NH2 
13735 N N   . ALA B 638  ? 0.1876 0.2043 0.1805 0.0063  -0.0054 -0.0157 636  ALA B N   
13736 C CA  . ALA B 638  ? 0.1730 0.1917 0.1689 0.0059  -0.0055 -0.0160 636  ALA B CA  
13737 C C   . ALA B 638  ? 0.1985 0.2169 0.1930 0.0038  -0.0062 -0.0168 636  ALA B C   
13738 O O   . ALA B 638  ? 0.1928 0.2108 0.1885 0.0032  -0.0057 -0.0174 636  ALA B O   
13739 C CB  . ALA B 638  ? 0.1858 0.2086 0.1848 0.0067  -0.0064 -0.0152 636  ALA B CB  
13740 N N   . ALA B 639  ? 0.1979 0.2164 0.1898 0.0027  -0.0075 -0.0168 637  ALA B N   
13741 C CA  . ALA B 639  ? 0.2132 0.2309 0.2033 0.0005  -0.0084 -0.0176 637  ALA B CA  
13742 C C   . ALA B 639  ? 0.1941 0.2073 0.1818 0.0002  -0.0071 -0.0186 637  ALA B C   
13743 O O   . ALA B 639  ? 0.2068 0.2190 0.1943 -0.0012 -0.0072 -0.0193 637  ALA B O   
13744 C CB  . ALA B 639  ? 0.2061 0.2245 0.1935 -0.0007 -0.0102 -0.0174 637  ALA B CB  
13745 N N   . CYS B 640  ? 0.1985 0.2089 0.1845 0.0015  -0.0057 -0.0187 638  CYS B N   
13746 C CA  . CYS B 640  ? 0.2103 0.2168 0.1946 0.0016  -0.0042 -0.0197 638  CYS B CA  
13747 C C   . CYS B 640  ? 0.1710 0.1779 0.1586 0.0021  -0.0034 -0.0198 638  CYS B C   
13748 O O   . CYS B 640  ? 0.2003 0.2049 0.1872 0.0014  -0.0030 -0.0206 638  CYS B O   
13749 C CB  . CYS B 640  ? 0.1874 0.1916 0.1700 0.0031  -0.0027 -0.0195 638  CYS B CB  
13750 S SG  . CYS B 640  ? 0.2295 0.2320 0.2070 0.0027  -0.0033 -0.0196 638  CYS B SG  
13751 N N   . LEU B 641  ? 0.1744 0.1839 0.1656 0.0033  -0.0030 -0.0190 639  LEU B N   
13752 C CA  . LEU B 641  ? 0.1833 0.1932 0.1774 0.0037  -0.0024 -0.0191 639  LEU B CA  
13753 C C   . LEU B 641  ? 0.1908 0.2020 0.1856 0.0021  -0.0034 -0.0194 639  LEU B C   
13754 O O   . LEU B 641  ? 0.1849 0.1945 0.1799 0.0017  -0.0029 -0.0199 639  LEU B O   
13755 C CB  . LEU B 641  ? 0.1926 0.2050 0.1899 0.0051  -0.0021 -0.0183 639  LEU B CB  
13756 C CG  . LEU B 641  ? 0.2003 0.2112 0.1983 0.0066  -0.0007 -0.0181 639  LEU B CG  
13757 C CD1 . LEU B 641  ? 0.2367 0.2459 0.2318 0.0069  -0.0003 -0.0179 639  LEU B CD1 
13758 C CD2 . LEU B 641  ? 0.1802 0.1933 0.1811 0.0077  -0.0007 -0.0174 639  LEU B CD2 
13759 N N   . ASP B 642  ? 0.1755 0.1897 0.1706 0.0012  -0.0048 -0.0190 640  ASP B N   
13760 C CA  . ASP B 642  ? 0.1931 0.2089 0.1890 -0.0006 -0.0057 -0.0190 640  ASP B CA  
13761 C C   . ASP B 642  ? 0.1833 0.1955 0.1760 -0.0023 -0.0060 -0.0199 640  ASP B C   
13762 O O   . ASP B 642  ? 0.1972 0.2087 0.1902 -0.0034 -0.0060 -0.0201 640  ASP B O   
13763 C CB  . ASP B 642  ? 0.1822 0.2023 0.1794 -0.0013 -0.0072 -0.0184 640  ASP B CB  
13764 C CG  . ASP B 642  ? 0.2283 0.2523 0.2292 0.0002  -0.0069 -0.0176 640  ASP B CG  
13765 O OD1 . ASP B 642  ? 0.2195 0.2431 0.2221 0.0012  -0.0058 -0.0177 640  ASP B OD1 
13766 O OD2 . ASP B 642  ? 0.2252 0.2526 0.2271 0.0004  -0.0079 -0.0170 640  ASP B OD2 
13767 N N   . ARG B 643  ? 0.1881 0.1975 0.1773 -0.0025 -0.0062 -0.0203 641  ARG B N   
13768 C CA  . ARG B 643  ? 0.2156 0.2210 0.2013 -0.0039 -0.0064 -0.0213 641  ARG B CA  
13769 C C   . ARG B 643  ? 0.1992 0.2013 0.1849 -0.0029 -0.0048 -0.0219 641  ARG B C   
13770 O O   . ARG B 643  ? 0.2082 0.2078 0.1927 -0.0041 -0.0050 -0.0224 641  ARG B O   
13771 C CB  . ARG B 643  ? 0.2094 0.2123 0.1909 -0.0041 -0.0067 -0.0218 641  ARG B CB  
13772 C CG  . ARG B 643  ? 0.2310 0.2361 0.2114 -0.0060 -0.0088 -0.0215 641  ARG B CG  
13773 C CD  . ARG B 643  ? 0.2481 0.2499 0.2235 -0.0064 -0.0093 -0.0222 641  ARG B CD  
13774 N NE  . ARG B 643  ? 0.2613 0.2629 0.2361 -0.0043 -0.0082 -0.0218 641  ARG B NE  
13775 C CZ  . ARG B 643  ? 0.2749 0.2795 0.2502 -0.0039 -0.0091 -0.0209 641  ARG B CZ  
13776 N NH1 . ARG B 643  ? 0.2770 0.2855 0.2539 -0.0052 -0.0110 -0.0203 641  ARG B NH1 
13777 N NH2 . ARG B 643  ? 0.3058 0.3096 0.2802 -0.0021 -0.0079 -0.0206 641  ARG B NH2 
13778 N N   . ALA B 644  ? 0.1748 0.1767 0.1619 -0.0008 -0.0034 -0.0217 642  ALA B N   
13779 C CA  . ALA B 644  ? 0.1935 0.1928 0.1811 0.0002  -0.0021 -0.0221 642  ALA B CA  
13780 C C   . ALA B 644  ? 0.1933 0.1939 0.1835 -0.0003 -0.0023 -0.0218 642  ALA B C   
13781 O O   . ALA B 644  ? 0.1949 0.1929 0.1846 -0.0004 -0.0020 -0.0222 642  ALA B O   
13782 C CB  . ALA B 644  ? 0.1744 0.1741 0.1635 0.0023  -0.0006 -0.0217 642  ALA B CB  
13783 N N   . ALA B 645  ? 0.1827 0.1874 0.1758 -0.0005 -0.0029 -0.0210 643  ALA B N   
13784 C CA  . ALA B 645  ? 0.1938 0.2000 0.1891 -0.0010 -0.0031 -0.0207 643  ALA B CA  
13785 C C   . ALA B 645  ? 0.1895 0.1944 0.1830 -0.0032 -0.0040 -0.0210 643  ALA B C   
13786 O O   . ALA B 645  ? 0.1991 0.2024 0.1928 -0.0036 -0.0039 -0.0211 643  ALA B O   
13787 C CB  . ALA B 645  ? 0.1908 0.2017 0.1891 -0.0006 -0.0034 -0.0200 643  ALA B CB  
13788 N N   . GLU B 646  ? 0.1983 0.2035 0.1899 -0.0047 -0.0052 -0.0211 644  GLU B N   
13789 C CA  . GLU B 646  ? 0.2072 0.2109 0.1969 -0.0072 -0.0062 -0.0213 644  GLU B CA  
13790 C C   . GLU B 646  ? 0.2139 0.2118 0.2006 -0.0071 -0.0057 -0.0222 644  GLU B C   
13791 O O   . GLU B 646  ? 0.2186 0.2145 0.2045 -0.0084 -0.0060 -0.0223 644  GLU B O   
13792 C CB  . GLU B 646  ? 0.2454 0.2501 0.2333 -0.0089 -0.0076 -0.0214 644  GLU B CB  
13793 C CG  . GLU B 646  ? 0.3028 0.3134 0.2937 -0.0092 -0.0084 -0.0205 644  GLU B CG  
13794 C CD  . GLU B 646  ? 0.4075 0.4213 0.4011 -0.0104 -0.0087 -0.0198 644  GLU B CD  
13795 O OE1 . GLU B 646  ? 0.5142 0.5259 0.5064 -0.0125 -0.0092 -0.0199 644  GLU B OE1 
13796 O OE2 . GLU B 646  ? 0.4577 0.4758 0.4547 -0.0093 -0.0083 -0.0191 644  GLU B OE2 
13797 N N   . LEU B 647  ? 0.2151 0.2102 0.1999 -0.0056 -0.0048 -0.0228 645  LEU B N   
13798 C CA  . LEU B 647  ? 0.2298 0.2196 0.2118 -0.0051 -0.0042 -0.0237 645  LEU B CA  
13799 C C   . LEU B 647  ? 0.2283 0.2174 0.2125 -0.0039 -0.0033 -0.0235 645  LEU B C   
13800 O O   . LEU B 647  ? 0.2342 0.2197 0.2168 -0.0044 -0.0034 -0.0238 645  LEU B O   
13801 C CB  . LEU B 647  ? 0.2142 0.2018 0.1940 -0.0035 -0.0032 -0.0244 645  LEU B CB  
13802 C CG  . LEU B 647  ? 0.2231 0.2103 0.1997 -0.0047 -0.0042 -0.0248 645  LEU B CG  
13803 C CD1 . LEU B 647  ? 0.2447 0.2298 0.2191 -0.0029 -0.0029 -0.0254 645  LEU B CD1 
13804 C CD2 . LEU B 647  ? 0.2781 0.2617 0.2510 -0.0070 -0.0055 -0.0255 645  LEU B CD2 
13805 N N   . MET B 648  ? 0.1919 0.1842 0.1795 -0.0023 -0.0025 -0.0229 646  MET B N   
13806 C CA  . MET B 648  ? 0.1901 0.1820 0.1798 -0.0012 -0.0018 -0.0226 646  MET B CA  
13807 C C   . MET B 648  ? 0.2000 0.1926 0.1903 -0.0029 -0.0027 -0.0221 646  MET B C   
13808 O O   . MET B 648  ? 0.2280 0.2181 0.2181 -0.0028 -0.0026 -0.0221 646  MET B O   
13809 C CB  . MET B 648  ? 0.2290 0.2242 0.2222 0.0006  -0.0010 -0.0221 646  MET B CB  
13810 C CG  . MET B 648  ? 0.2372 0.2314 0.2301 0.0023  0.0001  -0.0224 646  MET B CG  
13811 S SD  . MET B 648  ? 0.2476 0.2447 0.2446 0.0041  0.0009  -0.0217 646  MET B SD  
13812 C CE  . MET B 648  ? 0.2610 0.2570 0.2573 0.0057  0.0023  -0.0220 646  MET B CE  
13813 N N   . GLN B 649  ? 0.1957 0.1917 0.1868 -0.0045 -0.0036 -0.0217 647  GLN B N   
13814 C CA  . GLN B 649  ? 0.2102 0.2071 0.2019 -0.0063 -0.0043 -0.0211 647  GLN B CA  
13815 C C   . GLN B 649  ? 0.2102 0.2025 0.1985 -0.0080 -0.0050 -0.0215 647  GLN B C   
13816 O O   . GLN B 649  ? 0.2396 0.2301 0.2277 -0.0086 -0.0050 -0.0212 647  GLN B O   
13817 C CB  . GLN B 649  ? 0.2049 0.2067 0.1981 -0.0076 -0.0050 -0.0205 647  GLN B CB  
13818 C CG  . GLN B 649  ? 0.2084 0.2122 0.2027 -0.0094 -0.0055 -0.0198 647  GLN B CG  
13819 C CD  . GLN B 649  ? 0.2082 0.2137 0.2049 -0.0080 -0.0047 -0.0193 647  GLN B CD  
13820 O OE1 . GLN B 649  ? 0.2185 0.2280 0.2178 -0.0069 -0.0043 -0.0190 647  GLN B OE1 
13821 N NE2 . GLN B 649  ? 0.2251 0.2273 0.2209 -0.0079 -0.0044 -0.0193 647  GLN B NE2 
13822 N N   . ALA B 650  ? 0.2176 0.2078 0.2030 -0.0089 -0.0055 -0.0222 648  ALA B N   
13823 C CA  . ALA B 650  ? 0.2308 0.2161 0.2126 -0.0107 -0.0063 -0.0226 648  ALA B CA  
13824 C C   . ALA B 650  ? 0.2702 0.2502 0.2503 -0.0091 -0.0055 -0.0232 648  ALA B C   
13825 O O   . ALA B 650  ? 0.2844 0.2605 0.2624 -0.0103 -0.0060 -0.0233 648  ALA B O   
13826 C CB  . ALA B 650  ? 0.2541 0.2382 0.2329 -0.0120 -0.0071 -0.0234 648  ALA B CB  
13827 N N   . ARG B 651  ? 0.2327 0.2128 0.2139 -0.0064 -0.0042 -0.0236 649  ARG B N   
13828 C CA  . ARG B 651  ? 0.2282 0.2038 0.2082 -0.0045 -0.0034 -0.0241 649  ARG B CA  
13829 C C   . ARG B 651  ? 0.2292 0.2063 0.2124 -0.0031 -0.0028 -0.0234 649  ARG B C   
13830 O O   . ARG B 651  ? 0.2448 0.2192 0.2279 -0.0012 -0.0020 -0.0237 649  ARG B O   
13831 C CB  . ARG B 651  ? 0.2428 0.2175 0.2218 -0.0026 -0.0023 -0.0250 649  ARG B CB  
13832 C CG  . ARG B 651  ? 0.2653 0.2378 0.2404 -0.0041 -0.0030 -0.0258 649  ARG B CG  
13833 C CD  . ARG B 651  ? 0.2775 0.2493 0.2512 -0.0024 -0.0019 -0.0265 649  ARG B CD  
13834 N NE  . ARG B 651  ? 0.2921 0.2626 0.2622 -0.0042 -0.0029 -0.0271 649  ARG B NE  
13835 C CZ  . ARG B 651  ? 0.2806 0.2507 0.2486 -0.0034 -0.0024 -0.0277 649  ARG B CZ  
13836 N NH1 . ARG B 651  ? 0.2927 0.2635 0.2620 -0.0009 -0.0007 -0.0278 649  ARG B NH1 
13837 N NH2 . ARG B 651  ? 0.2775 0.2466 0.2422 -0.0053 -0.0036 -0.0282 649  ARG B NH2 
13838 N N   . MET B 652  ? 0.2206 0.2018 0.2064 -0.0039 -0.0032 -0.0225 650  MET B N   
13839 C CA  . MET B 652  ? 0.2218 0.2044 0.2104 -0.0026 -0.0028 -0.0219 650  MET B CA  
13840 C C   . MET B 652  ? 0.2352 0.2132 0.2223 -0.0021 -0.0029 -0.0219 650  MET B C   
13841 O O   . MET B 652  ? 0.2465 0.2243 0.2353 0.0000  -0.0022 -0.0218 650  MET B O   
13842 C CB  . MET B 652  ? 0.2198 0.2067 0.2105 -0.0039 -0.0033 -0.0210 650  MET B CB  
13843 C CG  . MET B 652  ? 0.2122 0.2003 0.2051 -0.0028 -0.0030 -0.0203 650  MET B CG  
13844 S SD  . MET B 652  ? 0.2564 0.2494 0.2513 -0.0042 -0.0034 -0.0194 650  MET B SD  
13845 C CE  . MET B 652  ? 0.2341 0.2316 0.2315 -0.0029 -0.0028 -0.0196 650  MET B CE  
13846 N N   . PRO B 653  ? 0.2345 0.2089 0.2187 -0.0039 -0.0037 -0.0219 651  PRO B N   
13847 C CA  . PRO B 653  ? 0.2623 0.2321 0.2451 -0.0032 -0.0038 -0.0218 651  PRO B CA  
13848 C C   . PRO B 653  ? 0.2433 0.2101 0.2256 -0.0005 -0.0029 -0.0226 651  PRO B C   
13849 O O   . PRO B 653  ? 0.2521 0.2180 0.2358 0.0013  -0.0026 -0.0223 651  PRO B O   
13850 C CB  . PRO B 653  ? 0.2635 0.2294 0.2426 -0.0058 -0.0049 -0.0218 651  PRO B CB  
13851 C CG  . PRO B 653  ? 0.2690 0.2395 0.2492 -0.0082 -0.0054 -0.0213 651  PRO B CG  
13852 C CD  . PRO B 653  ? 0.2486 0.2230 0.2308 -0.0068 -0.0047 -0.0218 651  PRO B CD  
13853 N N   . THR B 654  ? 0.2469 0.2124 0.2275 -0.0002 -0.0024 -0.0236 652  THR B N   
13854 C CA  . THR B 654  ? 0.2533 0.2165 0.2336 0.0025  -0.0013 -0.0244 652  THR B CA  
13855 C C   . THR B 654  ? 0.2509 0.2184 0.2353 0.0046  -0.0002 -0.0240 652  THR B C   
13856 O O   . THR B 654  ? 0.2453 0.2119 0.2311 0.0068  0.0004  -0.0240 652  THR B O   
13857 C CB  . THR B 654  ? 0.2572 0.2180 0.2341 0.0022  -0.0009 -0.0255 652  THR B CB  
13858 O OG1 . THR B 654  ? 0.3035 0.2599 0.2764 0.0000  -0.0021 -0.0259 652  THR B OG1 
13859 C CG2 . THR B 654  ? 0.2479 0.2064 0.2243 0.0050  0.0005  -0.0264 652  THR B CG2 
13860 N N   . LEU B 655  ? 0.2202 0.1925 0.2067 0.0040  -0.0002 -0.0237 653  LEU B N   
13861 C CA  . LEU B 655  ? 0.2154 0.1916 0.2057 0.0057  0.0007  -0.0233 653  LEU B CA  
13862 C C   . LEU B 655  ? 0.2398 0.2169 0.2327 0.0064  0.0003  -0.0225 653  LEU B C   
13863 O O   . LEU B 655  ? 0.2399 0.2180 0.2353 0.0084  0.0010  -0.0223 653  LEU B O   
13864 C CB  . LEU B 655  ? 0.2263 0.2070 0.2181 0.0047  0.0006  -0.0230 653  LEU B CB  
13865 C CG  . LEU B 655  ? 0.2539 0.2342 0.2433 0.0039  0.0007  -0.0236 653  LEU B CG  
13866 C CD1 . LEU B 655  ? 0.2562 0.2411 0.2473 0.0031  0.0004  -0.0231 653  LEU B CD1 
13867 C CD2 . LEU B 655  ? 0.2880 0.2668 0.2767 0.0058  0.0020  -0.0242 653  LEU B CD2 
13868 N N   . LEU B 656  ? 0.2574 0.2341 0.2496 0.0048  -0.0008 -0.0219 654  LEU B N   
13869 C CA  . LEU B 656  ? 0.2605 0.2377 0.2546 0.0054  -0.0013 -0.0211 654  LEU B CA  
13870 C C   . LEU B 656  ? 0.2611 0.2348 0.2549 0.0073  -0.0010 -0.0213 654  LEU B C   
13871 O O   . LEU B 656  ? 0.2685 0.2436 0.2650 0.0089  -0.0009 -0.0208 654  LEU B O   
13872 C CB  . LEU B 656  ? 0.2829 0.2592 0.2753 0.0032  -0.0024 -0.0205 654  LEU B CB  
13873 C CG  . LEU B 656  ? 0.3364 0.3162 0.3291 0.0011  -0.0027 -0.0202 654  LEU B CG  
13874 C CD1 . LEU B 656  ? 0.3005 0.2794 0.2919 -0.0007 -0.0036 -0.0194 654  LEU B CD1 
13875 C CD2 . LEU B 656  ? 0.3133 0.2978 0.3093 0.0021  -0.0023 -0.0200 654  LEU B CD2 
13876 N N   . GLY B 657  ? 0.2542 0.2233 0.2447 0.0071  -0.0011 -0.0218 655  GLY B N   
13877 C CA  . GLY B 657  ? 0.2905 0.2559 0.2806 0.0092  -0.0008 -0.0220 655  GLY B CA  
13878 C C   . GLY B 657  ? 0.2715 0.2390 0.2644 0.0118  0.0005  -0.0223 655  GLY B C   
13879 O O   . GLY B 657  ? 0.2645 0.2321 0.2596 0.0136  0.0005  -0.0219 655  GLY B O   
13880 N N   . LEU B 658  ? 0.2302 0.1997 0.2233 0.0118  0.0015  -0.0229 656  LEU B N   
13881 C CA  . LEU B 658  ? 0.2174 0.1891 0.2132 0.0140  0.0028  -0.0231 656  LEU B CA  
13882 C C   . LEU B 658  ? 0.2441 0.2204 0.2444 0.0144  0.0026  -0.0222 656  LEU B C   
13883 O O   . LEU B 658  ? 0.2448 0.2221 0.2479 0.0163  0.0031  -0.0219 656  LEU B O   
13884 C CB  . LEU B 658  ? 0.2255 0.1980 0.2200 0.0137  0.0039  -0.0238 656  LEU B CB  
13885 C CG  . LEU B 658  ? 0.2136 0.1883 0.2105 0.0158  0.0056  -0.0240 656  LEU B CG  
13886 C CD1 . LEU B 658  ? 0.2271 0.1990 0.2240 0.0182  0.0065  -0.0243 656  LEU B CD1 
13887 C CD2 . LEU B 658  ? 0.2292 0.2043 0.2241 0.0153  0.0065  -0.0246 656  LEU B CD2 
13888 N N   . ILE B 659  ? 0.2135 0.1925 0.2144 0.0127  0.0019  -0.0217 657  ILE B N   
13889 C CA  . ILE B 659  ? 0.1934 0.1764 0.1981 0.0130  0.0016  -0.0210 657  ILE B CA  
13890 C C   . ILE B 659  ? 0.2240 0.2063 0.2300 0.0137  0.0006  -0.0204 657  ILE B C   
13891 O O   . ILE B 659  ? 0.2156 0.2001 0.2248 0.0149  0.0006  -0.0199 657  ILE B O   
13892 C CB  . ILE B 659  ? 0.2010 0.1866 0.2056 0.0111  0.0010  -0.0208 657  ILE B CB  
13893 C CG1 . ILE B 659  ? 0.2092 0.1960 0.2131 0.0107  0.0019  -0.0213 657  ILE B CG1 
13894 C CG2 . ILE B 659  ? 0.2145 0.2032 0.2221 0.0112  0.0004  -0.0201 657  ILE B CG2 
13895 C CD1 . ILE B 659  ? 0.2264 0.2150 0.2293 0.0088  0.0012  -0.0211 657  ILE B CD1 
13896 N N   . ILE B 660  ? 0.2217 0.2007 0.2249 0.0128  -0.0003 -0.0202 658  ILE B N   
13897 C CA  . ILE B 660  ? 0.2150 0.1927 0.2188 0.0134  -0.0014 -0.0195 658  ILE B CA  
13898 C C   . ILE B 660  ? 0.2305 0.2075 0.2363 0.0160  -0.0008 -0.0195 658  ILE B C   
13899 O O   . ILE B 660  ? 0.2354 0.2142 0.2441 0.0171  -0.0014 -0.0189 658  ILE B O   
13900 C CB  . ILE B 660  ? 0.2274 0.2011 0.2275 0.0120  -0.0023 -0.0193 658  ILE B CB  
13901 C CG1 . ILE B 660  ? 0.2393 0.2147 0.2384 0.0096  -0.0030 -0.0189 658  ILE B CG1 
13902 C CG2 . ILE B 660  ? 0.2498 0.2208 0.2498 0.0133  -0.0032 -0.0187 658  ILE B CG2 
13903 C CD1 . ILE B 660  ? 0.2641 0.2358 0.2594 0.0077  -0.0037 -0.0187 658  ILE B CD1 
13904 N N   . ARG B 661  ? 0.2120 0.1866 0.2163 0.0171  0.0003  -0.0203 659  ARG B N   
13905 C CA  . ARG B 661  ? 0.2062 0.1798 0.2121 0.0197  0.0009  -0.0204 659  ARG B CA  
13906 C C   . ARG B 661  ? 0.2273 0.2051 0.2372 0.0211  0.0022  -0.0204 659  ARG B C   
13907 O O   . ARG B 661  ? 0.2483 0.2274 0.2613 0.0231  0.0023  -0.0200 659  ARG B O   
13908 C CB  . ARG B 661  ? 0.2311 0.1996 0.2333 0.0205  0.0015  -0.0213 659  ARG B CB  
13909 C CG  . ARG B 661  ? 0.2514 0.2152 0.2502 0.0195  0.0001  -0.0209 659  ARG B CG  
13910 C CD  . ARG B 661  ? 0.2693 0.2274 0.2639 0.0199  0.0006  -0.0219 659  ARG B CD  
13911 N NE  . ARG B 661  ? 0.2761 0.2330 0.2716 0.0230  0.0019  -0.0225 659  ARG B NE  
13912 C CZ  . ARG B 661  ? 0.2894 0.2450 0.2833 0.0239  0.0035  -0.0236 659  ARG B CZ  
13913 N NH1 . ARG B 661  ? 0.3058 0.2613 0.2971 0.0220  0.0038  -0.0243 659  ARG B NH1 
13914 N NH2 . ARG B 661  ? 0.3006 0.2551 0.2955 0.0270  0.0047  -0.0241 659  ARG B NH2 
13915 N N   . GLU B 662  ? 0.2109 0.1910 0.2208 0.0200  0.0030  -0.0208 660  GLU B N   
13916 C CA  . GLU B 662  ? 0.2305 0.2144 0.2439 0.0212  0.0044  -0.0207 660  GLU B CA  
13917 C C   . GLU B 662  ? 0.2342 0.2223 0.2515 0.0207  0.0035  -0.0199 660  GLU B C   
13918 O O   . GLU B 662  ? 0.2380 0.2289 0.2591 0.0219  0.0041  -0.0195 660  GLU B O   
13919 C CB  . GLU B 662  ? 0.2493 0.2335 0.2609 0.0204  0.0057  -0.0214 660  GLU B CB  
13920 C CG  . GLU B 662  ? 0.2438 0.2317 0.2587 0.0215  0.0072  -0.0212 660  GLU B CG  
13921 C CD  . GLU B 662  ? 0.2347 0.2228 0.2475 0.0208  0.0085  -0.0218 660  GLU B CD  
13922 O OE1 . GLU B 662  ? 0.2553 0.2425 0.2654 0.0190  0.0078  -0.0221 660  GLU B OE1 
13923 O OE2 . GLU B 662  ? 0.2489 0.2382 0.2629 0.0221  0.0102  -0.0219 660  GLU B OE2 
13924 N N   . ALA B 663  ? 0.2036 0.1923 0.2200 0.0188  0.0023  -0.0196 661  ALA B N   
13925 C CA  . ALA B 663  ? 0.2092 0.2014 0.2285 0.0182  0.0016  -0.0190 661  ALA B CA  
13926 C C   . ALA B 663  ? 0.2310 0.2231 0.2509 0.0178  -0.0002 -0.0184 661  ALA B C   
13927 O O   . ALA B 663  ? 0.2957 0.2903 0.3172 0.0171  -0.0010 -0.0180 661  ALA B O   
13928 C CB  . ALA B 663  ? 0.2159 0.2096 0.2342 0.0165  0.0018  -0.0192 661  ALA B CB  
13929 N N   . GLY B 664  ? 0.2468 0.2358 0.2649 0.0183  -0.0009 -0.0182 662  GLY B N   
13930 C CA  . GLY B 664  ? 0.2733 0.2620 0.2916 0.0181  -0.0026 -0.0175 662  GLY B CA  
13931 C C   . GLY B 664  ? 0.2542 0.2428 0.2702 0.0160  -0.0035 -0.0174 662  GLY B C   
13932 O O   . GLY B 664  ? 0.2587 0.2483 0.2754 0.0156  -0.0048 -0.0168 662  GLY B O   
13933 N N   . LYS B 665  ? 0.2279 0.2156 0.2413 0.0146  -0.0029 -0.0179 663  LYS B N   
13934 C CA  . LYS B 665  ? 0.2272 0.2156 0.2388 0.0127  -0.0035 -0.0178 663  LYS B CA  
13935 C C   . LYS B 665  ? 0.2073 0.1923 0.2156 0.0118  -0.0043 -0.0175 663  LYS B C   
13936 O O   . LYS B 665  ? 0.2307 0.2124 0.2371 0.0122  -0.0041 -0.0176 663  LYS B O   
13937 C CB  . LYS B 665  ? 0.2275 0.2170 0.2382 0.0117  -0.0025 -0.0184 663  LYS B CB  
13938 C CG  . LYS B 665  ? 0.2493 0.2417 0.2627 0.0124  -0.0016 -0.0186 663  LYS B CG  
13939 C CD  . LYS B 665  ? 0.2824 0.2774 0.2982 0.0124  -0.0023 -0.0183 663  LYS B CD  
13940 C CE  . LYS B 665  ? 0.3465 0.3441 0.3649 0.0129  -0.0014 -0.0184 663  LYS B CE  
13941 N NZ  . LYS B 665  ? 0.3357 0.3355 0.3565 0.0129  -0.0022 -0.0181 663  LYS B NZ  
13942 N N   . SER B 666  ? 0.2424 0.2281 0.2498 0.0105  -0.0052 -0.0170 664  SER B N   
13943 C CA  . SER B 666  ? 0.2362 0.2191 0.2402 0.0091  -0.0058 -0.0166 664  SER B CA  
13944 C C   . SER B 666  ? 0.2510 0.2338 0.2531 0.0075  -0.0050 -0.0170 664  SER B C   
13945 O O   . SER B 666  ? 0.2530 0.2383 0.2562 0.0074  -0.0042 -0.0176 664  SER B O   
13946 C CB  . SER B 666  ? 0.2838 0.2678 0.2872 0.0082  -0.0067 -0.0159 664  SER B CB  
13947 O OG  . SER B 666  ? 0.2946 0.2820 0.2987 0.0072  -0.0062 -0.0162 664  SER B OG  
13948 N N   . ALA B 667  ? 0.2520 0.2319 0.2509 0.0061  -0.0054 -0.0167 665  ALA B N   
13949 C CA  . ALA B 667  ? 0.2434 0.2233 0.2406 0.0042  -0.0050 -0.0171 665  ALA B CA  
13950 C C   . ALA B 667  ? 0.2299 0.2142 0.2281 0.0032  -0.0047 -0.0171 665  ALA B C   
13951 O O   . ALA B 667  ? 0.2334 0.2195 0.2321 0.0027  -0.0040 -0.0176 665  ALA B O   
13952 C CB  . ALA B 667  ? 0.2622 0.2384 0.2559 0.0025  -0.0056 -0.0165 665  ALA B CB  
13953 N N   . LEU B 668  ? 0.2320 0.2180 0.2306 0.0029  -0.0051 -0.0165 666  LEU B N   
13954 C CA  . LEU B 668  ? 0.2469 0.2369 0.2465 0.0021  -0.0047 -0.0166 666  LEU B CA  
13955 C C   . LEU B 668  ? 0.2333 0.2259 0.2355 0.0035  -0.0041 -0.0173 666  LEU B C   
13956 O O   . LEU B 668  ? 0.2455 0.2406 0.2483 0.0029  -0.0036 -0.0176 666  LEU B O   
13957 C CB  . LEU B 668  ? 0.2782 0.2693 0.2775 0.0018  -0.0053 -0.0160 666  LEU B CB  
13958 C CG  . LEU B 668  ? 0.3605 0.3506 0.3571 -0.0001 -0.0055 -0.0152 666  LEU B CG  
13959 C CD1 . LEU B 668  ? 0.4374 0.4284 0.4334 -0.0001 -0.0059 -0.0146 666  LEU B CD1 
13960 C CD2 . LEU B 668  ? 0.3795 0.3721 0.3759 -0.0018 -0.0048 -0.0153 666  LEU B CD2 
13961 N N   . ASN B 669  ? 0.2396 0.2317 0.2436 0.0052  -0.0043 -0.0174 667  ASN B N   
13962 C CA  . ASN B 669  ? 0.2402 0.2348 0.2468 0.0063  -0.0037 -0.0179 667  ASN B CA  
13963 C C   . ASN B 669  ? 0.2327 0.2267 0.2392 0.0065  -0.0028 -0.0184 667  ASN B C   
13964 O O   . ASN B 669  ? 0.2443 0.2406 0.2522 0.0067  -0.0022 -0.0187 667  ASN B O   
13965 C CB  . ASN B 669  ? 0.3028 0.2975 0.3115 0.0077  -0.0041 -0.0177 667  ASN B CB  
13966 C CG  . ASN B 669  ? 0.3176 0.3133 0.3262 0.0074  -0.0050 -0.0174 667  ASN B CG  
13967 O OD1 . ASN B 669  ? 0.3969 0.3945 0.4049 0.0066  -0.0048 -0.0175 667  ASN B OD1 
13968 N ND2 . ASN B 669  ? 0.4070 0.4016 0.4160 0.0082  -0.0059 -0.0170 667  ASN B ND2 
13969 N N   . ALA B 670  ? 0.2105 0.2014 0.2153 0.0064  -0.0028 -0.0185 668  ALA B N   
13970 C CA  . ALA B 670  ? 0.2158 0.2058 0.2197 0.0064  -0.0021 -0.0191 668  ALA B CA  
13971 C C   . ALA B 670  ? 0.2173 0.2088 0.2199 0.0047  -0.0020 -0.0192 668  ALA B C   
13972 O O   . ALA B 670  ? 0.2085 0.2011 0.2113 0.0047  -0.0014 -0.0196 668  ALA B O   
13973 C CB  . ALA B 670  ? 0.2211 0.2070 0.2231 0.0068  -0.0021 -0.0193 668  ALA B CB  
13974 N N   . ILE B 671  ? 0.2050 0.1964 0.2062 0.0031  -0.0026 -0.0188 669  ILE B N   
13975 C CA  . ILE B 671  ? 0.2015 0.1951 0.2021 0.0014  -0.0026 -0.0187 669  ILE B CA  
13976 C C   . ILE B 671  ? 0.1936 0.1913 0.1965 0.0021  -0.0022 -0.0188 669  ILE B C   
13977 O O   . ILE B 671  ? 0.2152 0.2145 0.2182 0.0018  -0.0019 -0.0191 669  ILE B O   
13978 C CB  . ILE B 671  ? 0.1930 0.1865 0.1921 -0.0004 -0.0032 -0.0181 669  ILE B CB  
13979 C CG1 . ILE B 671  ? 0.2309 0.2201 0.2272 -0.0015 -0.0036 -0.0180 669  ILE B CG1 
13980 C CG2 . ILE B 671  ? 0.2353 0.2324 0.2347 -0.0018 -0.0031 -0.0179 669  ILE B CG2 
13981 C CD1 . ILE B 671  ? 0.2561 0.2442 0.2508 -0.0030 -0.0042 -0.0171 669  ILE B CD1 
13982 N N   . ALA B 672  ? 0.2033 0.2023 0.2078 0.0030  -0.0023 -0.0186 670  ALA B N   
13983 C CA  . ALA B 672  ? 0.2001 0.2023 0.2065 0.0038  -0.0020 -0.0188 670  ALA B CA  
13984 C C   . ALA B 672  ? 0.1990 0.2013 0.2065 0.0048  -0.0014 -0.0192 670  ALA B C   
13985 O O   . ALA B 672  ? 0.2183 0.2229 0.2266 0.0050  -0.0011 -0.0193 670  ALA B O   
13986 C CB  . ALA B 672  ? 0.2490 0.2517 0.2565 0.0046  -0.0023 -0.0186 670  ALA B CB  
13987 N N   . GLU B 673  ? 0.1983 0.1983 0.2060 0.0057  -0.0012 -0.0193 671  GLU B N   
13988 C CA  . GLU B 673  ? 0.2122 0.2123 0.2208 0.0067  -0.0005 -0.0196 671  GLU B CA  
13989 C C   . GLU B 673  ? 0.2033 0.2034 0.2102 0.0060  -0.0002 -0.0199 671  GLU B C   
13990 O O   . GLU B 673  ? 0.1977 0.1994 0.2053 0.0063  0.0002  -0.0200 671  GLU B O   
13991 C CB  . GLU B 673  ? 0.2302 0.2278 0.2390 0.0078  -0.0002 -0.0197 671  GLU B CB  
13992 C CG  . GLU B 673  ? 0.2369 0.2347 0.2468 0.0089  0.0007  -0.0200 671  GLU B CG  
13993 C CD  . GLU B 673  ? 0.2682 0.2682 0.2810 0.0098  0.0009  -0.0197 671  GLU B CD  
13994 O OE1 . GLU B 673  ? 0.2774 0.2781 0.2914 0.0099  0.0002  -0.0194 671  GLU B OE1 
13995 O OE2 . GLU B 673  ? 0.2206 0.2213 0.2343 0.0104  0.0017  -0.0197 671  GLU B OE2 
13996 N N   . VAL B 674  ? 0.1805 0.1786 0.1850 0.0048  -0.0005 -0.0200 672  VAL B N   
13997 C CA  . VAL B 674  ? 0.1857 0.1836 0.1884 0.0039  -0.0005 -0.0204 672  VAL B CA  
13998 C C   . VAL B 674  ? 0.1787 0.1801 0.1821 0.0030  -0.0008 -0.0201 672  VAL B C   
13999 O O   . VAL B 674  ? 0.1862 0.1890 0.1895 0.0030  -0.0007 -0.0202 672  VAL B O   
14000 C CB  . VAL B 674  ? 0.1841 0.1787 0.1841 0.0027  -0.0009 -0.0206 672  VAL B CB  
14001 C CG1 . VAL B 674  ? 0.1956 0.1899 0.1935 0.0016  -0.0010 -0.0210 672  VAL B CG1 
14002 C CG2 . VAL B 674  ? 0.1891 0.1802 0.1885 0.0041  -0.0004 -0.0209 672  VAL B CG2 
14003 N N   . ARG B 675  ? 0.1766 0.1796 0.1807 0.0023  -0.0012 -0.0197 673  ARG B N   
14004 C CA  . ARG B 675  ? 0.1730 0.1796 0.1780 0.0017  -0.0014 -0.0194 673  ARG B CA  
14005 C C   . ARG B 675  ? 0.1811 0.1898 0.1880 0.0032  -0.0010 -0.0194 673  ARG B C   
14006 O O   . ARG B 675  ? 0.1770 0.1878 0.1841 0.0031  -0.0011 -0.0194 673  ARG B O   
14007 C CB  . ARG B 675  ? 0.1807 0.1886 0.1861 0.0011  -0.0017 -0.0190 673  ARG B CB  
14008 C CG  . ARG B 675  ? 0.2036 0.2101 0.2071 -0.0008 -0.0021 -0.0187 673  ARG B CG  
14009 C CD  . ARG B 675  ? 0.1825 0.1912 0.1865 -0.0015 -0.0022 -0.0181 673  ARG B CD  
14010 N NE  . ARG B 675  ? 0.1816 0.1946 0.1871 -0.0016 -0.0020 -0.0180 673  ARG B NE  
14011 C CZ  . ARG B 675  ? 0.1943 0.2101 0.2007 -0.0015 -0.0017 -0.0177 673  ARG B CZ  
14012 N NH1 . ARG B 675  ? 0.2171 0.2317 0.2229 -0.0013 -0.0016 -0.0175 673  ARG B NH1 
14013 N NH2 . ARG B 675  ? 0.1889 0.2086 0.1966 -0.0015 -0.0015 -0.0176 673  ARG B NH2 
14014 N N   . GLU B 676  ? 0.1775 0.1854 0.1857 0.0045  -0.0007 -0.0195 674  GLU B N   
14015 C CA  A GLU B 676  ? 0.1763 0.1857 0.1861 0.0058  -0.0003 -0.0195 674  GLU B CA  
14016 C CA  B GLU B 676  ? 0.1762 0.1856 0.1859 0.0058  -0.0003 -0.0195 674  GLU B CA  
14017 C C   . GLU B 676  ? 0.1615 0.1705 0.1707 0.0061  0.0000  -0.0196 674  GLU B C   
14018 O O   . GLU B 676  ? 0.1790 0.1898 0.1889 0.0065  0.0001  -0.0194 674  GLU B O   
14019 C CB  A GLU B 676  ? 0.2042 0.2127 0.2154 0.0069  -0.0002 -0.0195 674  GLU B CB  
14020 C CB  B GLU B 676  ? 0.2042 0.2128 0.2155 0.0069  -0.0002 -0.0195 674  GLU B CB  
14021 C CG  A GLU B 676  ? 0.2196 0.2292 0.2324 0.0080  0.0001  -0.0194 674  GLU B CG  
14022 C CG  B GLU B 676  ? 0.2169 0.2269 0.2298 0.0079  0.0000  -0.0194 674  GLU B CG  
14023 C CD  A GLU B 676  ? 0.2516 0.2630 0.2652 0.0082  -0.0003 -0.0194 674  GLU B CD  
14024 C CD  B GLU B 676  ? 0.2790 0.2884 0.2933 0.0087  -0.0001 -0.0194 674  GLU B CD  
14025 O OE1 A GLU B 676  ? 0.3281 0.3405 0.3410 0.0074  -0.0005 -0.0193 674  GLU B OE1 
14026 O OE1 B GLU B 676  ? 0.3305 0.3397 0.3446 0.0084  -0.0006 -0.0194 674  GLU B OE1 
14027 O OE2 A GLU B 676  ? 0.2504 0.2622 0.2652 0.0091  -0.0002 -0.0194 674  GLU B OE2 
14028 O OE2 B GLU B 676  ? 0.3190 0.3282 0.3346 0.0094  0.0002  -0.0193 674  GLU B OE2 
14029 N N   . ALA B 677  ? 0.1652 0.1717 0.1731 0.0060  0.0003  -0.0198 675  ALA B N   
14030 C CA  . ALA B 677  ? 0.1605 0.1664 0.1673 0.0062  0.0007  -0.0200 675  ALA B CA  
14031 C C   . ALA B 677  ? 0.1766 0.1840 0.1821 0.0051  0.0001  -0.0199 675  ALA B C   
14032 O O   . ALA B 677  ? 0.1737 0.1823 0.1791 0.0055  0.0002  -0.0197 675  ALA B O   
14033 C CB  . ALA B 677  ? 0.1943 0.1970 0.1994 0.0063  0.0012  -0.0204 675  ALA B CB  
14034 N N   . ILE B 678  ? 0.1758 0.1833 0.1803 0.0037  -0.0005 -0.0200 676  ILE B N   
14035 C CA  . ILE B 678  ? 0.1599 0.1694 0.1636 0.0024  -0.0013 -0.0198 676  ILE B CA  
14036 C C   . ILE B 678  ? 0.1574 0.1706 0.1632 0.0031  -0.0014 -0.0194 676  ILE B C   
14037 O O   . ILE B 678  ? 0.1802 0.1950 0.1858 0.0031  -0.0017 -0.0192 676  ILE B O   
14038 C CB  . ILE B 678  ? 0.1680 0.1771 0.1706 0.0006  -0.0019 -0.0198 676  ILE B CB  
14039 C CG1 . ILE B 678  ? 0.1908 0.1957 0.1908 -0.0001 -0.0019 -0.0203 676  ILE B CG1 
14040 C CG2 . ILE B 678  ? 0.1803 0.1927 0.1831 -0.0008 -0.0027 -0.0194 676  ILE B CG2 
14041 C CD1 . ILE B 678  ? 0.1891 0.1925 0.1882 -0.0015 -0.0024 -0.0202 676  ILE B CD1 
14042 N N   . ASP B 679  ? 0.1602 0.1744 0.1678 0.0038  -0.0012 -0.0192 677  ASP B N   
14043 C CA  . ASP B 679  ? 0.1689 0.1864 0.1783 0.0046  -0.0012 -0.0189 677  ASP B CA  
14044 C C   . ASP B 679  ? 0.1674 0.1847 0.1773 0.0061  -0.0009 -0.0188 677  ASP B C   
14045 O O   . ASP B 679  ? 0.1716 0.1911 0.1822 0.0066  -0.0012 -0.0184 677  ASP B O   
14046 C CB  . ASP B 679  ? 0.1623 0.1804 0.1730 0.0051  -0.0010 -0.0188 677  ASP B CB  
14047 C CG  . ASP B 679  ? 0.1974 0.2165 0.2077 0.0036  -0.0013 -0.0187 677  ASP B CG  
14048 O OD1 . ASP B 679  ? 0.2097 0.2304 0.2195 0.0023  -0.0017 -0.0185 677  ASP B OD1 
14049 O OD2 . ASP B 679  ? 0.2268 0.2448 0.2371 0.0036  -0.0011 -0.0188 677  ASP B OD2 
14050 N N   . PHE B 680  ? 0.1630 0.1777 0.1728 0.0068  -0.0003 -0.0189 678  PHE B N   
14051 C CA  . PHE B 680  ? 0.1663 0.1808 0.1764 0.0079  0.0001  -0.0187 678  PHE B CA  
14052 C C   . PHE B 680  ? 0.1622 0.1770 0.1707 0.0075  -0.0002 -0.0185 678  PHE B C   
14053 O O   . PHE B 680  ? 0.1604 0.1765 0.1692 0.0082  -0.0004 -0.0181 678  PHE B O   
14054 C CB  . PHE B 680  ? 0.1559 0.1678 0.1661 0.0084  0.0008  -0.0188 678  PHE B CB  
14055 C CG  . PHE B 680  ? 0.1644 0.1761 0.1765 0.0092  0.0010  -0.0188 678  PHE B CG  
14056 C CD1 . PHE B 680  ? 0.1643 0.1772 0.1777 0.0100  0.0009  -0.0185 678  PHE B CD1 
14057 C CD2 . PHE B 680  ? 0.1695 0.1797 0.1820 0.0091  0.0013  -0.0190 678  PHE B CD2 
14058 C CE1 . PHE B 680  ? 0.1811 0.1935 0.1960 0.0105  0.0009  -0.0186 678  PHE B CE1 
14059 C CE2 . PHE B 680  ? 0.1783 0.1883 0.1926 0.0097  0.0013  -0.0190 678  PHE B CE2 
14060 C CZ  . PHE B 680  ? 0.1944 0.2054 0.2098 0.0103  0.0011  -0.0188 678  PHE B CZ  
14061 N N   . LEU B 681  ? 0.1497 0.1630 0.1561 0.0064  -0.0004 -0.0189 679  LEU B N   
14062 C CA  . LEU B 681  ? 0.1572 0.1706 0.1617 0.0058  -0.0008 -0.0188 679  LEU B CA  
14063 C C   . LEU B 681  ? 0.1598 0.1766 0.1650 0.0055  -0.0018 -0.0184 679  LEU B C   
14064 O O   . LEU B 681  ? 0.1665 0.1842 0.1713 0.0060  -0.0021 -0.0179 679  LEU B O   
14065 C CB  . LEU B 681  ? 0.1638 0.1748 0.1658 0.0045  -0.0010 -0.0194 679  LEU B CB  
14066 C CG  . LEU B 681  ? 0.1629 0.1705 0.1638 0.0051  0.0001  -0.0198 679  LEU B CG  
14067 C CD1 . LEU B 681  ? 0.1735 0.1786 0.1724 0.0040  -0.0001 -0.0205 679  LEU B CD1 
14068 C CD2 . LEU B 681  ? 0.1780 0.1847 0.1772 0.0058  0.0007  -0.0197 679  LEU B CD2 
14069 N N   . ARG B 682  ? 0.1503 0.1689 0.1565 0.0046  -0.0023 -0.0184 680  ARG B N   
14070 C CA  . ARG B 682  ? 0.1527 0.1751 0.1600 0.0043  -0.0031 -0.0179 680  ARG B CA  
14071 C C   . ARG B 682  ? 0.1482 0.1727 0.1576 0.0060  -0.0030 -0.0175 680  ARG B C   
14072 O O   . ARG B 682  ? 0.1640 0.1911 0.1740 0.0064  -0.0036 -0.0170 680  ARG B O   
14073 C CB  . ARG B 682  ? 0.1553 0.1792 0.1631 0.0028  -0.0035 -0.0180 680  ARG B CB  
14074 C CG  . ARG B 682  ? 0.1708 0.1926 0.1762 0.0008  -0.0040 -0.0184 680  ARG B CG  
14075 C CD  . ARG B 682  ? 0.1845 0.2076 0.1905 -0.0008 -0.0043 -0.0183 680  ARG B CD  
14076 N NE  . ARG B 682  ? 0.1957 0.2166 0.1992 -0.0029 -0.0050 -0.0186 680  ARG B NE  
14077 C CZ  . ARG B 682  ? 0.1958 0.2160 0.1988 -0.0046 -0.0052 -0.0186 680  ARG B CZ  
14078 N NH1 . ARG B 682  ? 0.2013 0.2230 0.2061 -0.0044 -0.0046 -0.0183 680  ARG B NH1 
14079 N NH2 . ARG B 682  ? 0.2399 0.2575 0.2404 -0.0065 -0.0059 -0.0189 680  ARG B NH2 
14080 N N   . TYR B 683  ? 0.1467 0.1701 0.1572 0.0071  -0.0022 -0.0176 681  TYR B N   
14081 C CA  . TYR B 683  ? 0.1688 0.1936 0.1810 0.0088  -0.0020 -0.0173 681  TYR B CA  
14082 C C   . TYR B 683  ? 0.1766 0.2003 0.1882 0.0099  -0.0020 -0.0169 681  TYR B C   
14083 O O   . TYR B 683  ? 0.1763 0.2019 0.1886 0.0109  -0.0025 -0.0164 681  TYR B O   
14084 C CB  . TYR B 683  ? 0.1604 0.1838 0.1737 0.0095  -0.0013 -0.0177 681  TYR B CB  
14085 C CG  . TYR B 683  ? 0.1487 0.1727 0.1633 0.0113  -0.0012 -0.0175 681  TYR B CG  
14086 C CD1 . TYR B 683  ? 0.1688 0.1957 0.1846 0.0120  -0.0013 -0.0175 681  TYR B CD1 
14087 C CD2 . TYR B 683  ? 0.1821 0.2036 0.1965 0.0122  -0.0008 -0.0174 681  TYR B CD2 
14088 C CE1 . TYR B 683  ? 0.1765 0.2034 0.1932 0.0137  -0.0012 -0.0174 681  TYR B CE1 
14089 C CE2 . TYR B 683  ? 0.1656 0.1870 0.1809 0.0137  -0.0008 -0.0173 681  TYR B CE2 
14090 C CZ  . TYR B 683  ? 0.1680 0.1919 0.1843 0.0145  -0.0010 -0.0174 681  TYR B CZ  
14091 O OH  . TYR B 683  ? 0.1960 0.2193 0.2129 0.0161  -0.0010 -0.0173 681  TYR B OH  
14092 N N   . TYR B 684  ? 0.1587 0.1794 0.1689 0.0097  -0.0015 -0.0170 682  TYR B N   
14093 C CA  . TYR B 684  ? 0.1666 0.1863 0.1760 0.0106  -0.0014 -0.0165 682  TYR B CA  
14094 C C   . TYR B 684  ? 0.1754 0.1964 0.1833 0.0101  -0.0023 -0.0161 682  TYR B C   
14095 O O   . TYR B 684  ? 0.1773 0.1986 0.1848 0.0110  -0.0027 -0.0154 682  TYR B O   
14096 C CB  . TYR B 684  ? 0.1627 0.1791 0.1710 0.0105  -0.0004 -0.0166 682  TYR B CB  
14097 C CG  . TYR B 684  ? 0.1544 0.1697 0.1644 0.0111  0.0002  -0.0169 682  TYR B CG  
14098 C CD1 . TYR B 684  ? 0.1868 0.2029 0.1985 0.0121  0.0001  -0.0167 682  TYR B CD1 
14099 C CD2 . TYR B 684  ? 0.1556 0.1691 0.1655 0.0106  0.0009  -0.0173 682  TYR B CD2 
14100 C CE1 . TYR B 684  ? 0.1778 0.1928 0.1909 0.0124  0.0005  -0.0169 682  TYR B CE1 
14101 C CE2 . TYR B 684  ? 0.1554 0.1682 0.1671 0.0110  0.0013  -0.0174 682  TYR B CE2 
14102 C CZ  . TYR B 684  ? 0.1778 0.1912 0.1909 0.0118  0.0010  -0.0173 682  TYR B CZ  
14103 O OH  . TYR B 684  ? 0.1743 0.1869 0.1889 0.0120  0.0012  -0.0175 682  TYR B OH  
14104 N N   . ALA B 685  ? 0.1620 0.1836 0.1688 0.0086  -0.0029 -0.0165 683  ALA B N   
14105 C CA  . ALA B 685  ? 0.1738 0.1971 0.1793 0.0079  -0.0040 -0.0161 683  ALA B CA  
14106 C C   . ALA B 685  ? 0.1723 0.1995 0.1800 0.0087  -0.0049 -0.0155 683  ALA B C   
14107 O O   . ALA B 685  ? 0.1747 0.2029 0.1820 0.0095  -0.0056 -0.0148 683  ALA B O   
14108 C CB  . ALA B 685  ? 0.1828 0.2059 0.1868 0.0059  -0.0045 -0.0167 683  ALA B CB  
14109 N N   . GLU B 686  ? 0.1653 0.1946 0.1752 0.0088  -0.0047 -0.0157 684  GLU B N   
14110 C CA  . GLU B 686  ? 0.1803 0.2135 0.1925 0.0098  -0.0053 -0.0152 684  GLU B CA  
14111 C C   . GLU B 686  ? 0.1946 0.2271 0.2075 0.0121  -0.0050 -0.0147 684  GLU B C   
14112 O O   . GLU B 686  ? 0.1845 0.2192 0.1980 0.0132  -0.0058 -0.0140 684  GLU B O   
14113 C CB  . GLU B 686  ? 0.2040 0.2397 0.2183 0.0094  -0.0050 -0.0155 684  GLU B CB  
14114 C CG  . GLU B 686  ? 0.2203 0.2602 0.2371 0.0109  -0.0052 -0.0150 684  GLU B CG  
14115 C CD  . GLU B 686  ? 0.2869 0.3307 0.3043 0.0105  -0.0065 -0.0143 684  GLU B CD  
14116 O OE1 . GLU B 686  ? 0.2659 0.3094 0.2818 0.0087  -0.0074 -0.0143 684  GLU B OE1 
14117 O OE2 . GLU B 686  ? 0.3042 0.3515 0.3239 0.0121  -0.0068 -0.0138 684  GLU B OE2 
14118 N N   . GLN B 687  ? 0.1754 0.2049 0.1882 0.0128  -0.0040 -0.0150 685  GLN B N   
14119 C CA  . GLN B 687  ? 0.1697 0.1980 0.1829 0.0147  -0.0038 -0.0146 685  GLN B CA  
14120 C C   . GLN B 687  ? 0.1780 0.2051 0.1894 0.0150  -0.0043 -0.0138 685  GLN B C   
14121 O O   . GLN B 687  ? 0.1910 0.2186 0.2028 0.0166  -0.0048 -0.0131 685  GLN B O   
14122 C CB  . GLN B 687  ? 0.1789 0.2038 0.1921 0.0150  -0.0027 -0.0151 685  GLN B CB  
14123 C CG  . GLN B 687  ? 0.2121 0.2380 0.2269 0.0150  -0.0023 -0.0157 685  GLN B CG  
14124 C CD  . GLN B 687  ? 0.2289 0.2573 0.2453 0.0166  -0.0026 -0.0156 685  GLN B CD  
14125 O OE1 . GLN B 687  ? 0.2154 0.2427 0.2319 0.0182  -0.0026 -0.0153 685  GLN B OE1 
14126 N NE2 . GLN B 687  ? 0.2480 0.2798 0.2655 0.0162  -0.0027 -0.0158 685  GLN B NE2 
14127 N N   . THR B 688  ? 0.1680 0.1935 0.1772 0.0136  -0.0043 -0.0139 686  THR B N   
14128 C CA  . THR B 688  ? 0.1831 0.2076 0.1901 0.0137  -0.0048 -0.0132 686  THR B CA  
14129 C C   . THR B 688  ? 0.1840 0.2119 0.1914 0.0140  -0.0063 -0.0125 686  THR B C   
14130 O O   . THR B 688  ? 0.1963 0.2243 0.2032 0.0153  -0.0069 -0.0116 686  THR B O   
14131 C CB  . THR B 688  ? 0.1809 0.2032 0.1853 0.0122  -0.0044 -0.0136 686  THR B CB  
14132 O OG1 . THR B 688  ? 0.1939 0.2132 0.1982 0.0122  -0.0030 -0.0140 686  THR B OG1 
14133 C CG2 . THR B 688  ? 0.1857 0.2071 0.1873 0.0121  -0.0051 -0.0129 686  THR B CG2 
14134 N N   . ARG B 689  ? 0.1796 0.2105 0.1879 0.0128  -0.0070 -0.0129 687  ARG B N   
14135 C CA  . ARG B 689  ? 0.1658 0.2007 0.1749 0.0129  -0.0085 -0.0123 687  ARG B CA  
14136 C C   . ARG B 689  ? 0.1935 0.2309 0.2053 0.0152  -0.0087 -0.0117 687  ARG B C   
14137 O O   . ARG B 689  ? 0.2120 0.2519 0.2243 0.0160  -0.0100 -0.0109 687  ARG B O   
14138 C CB  . ARG B 689  ? 0.1780 0.2157 0.1880 0.0109  -0.0090 -0.0128 687  ARG B CB  
14139 C CG  . ARG B 689  ? 0.2359 0.2713 0.2428 0.0088  -0.0094 -0.0133 687  ARG B CG  
14140 C CD  . ARG B 689  ? 0.2252 0.2635 0.2329 0.0067  -0.0102 -0.0136 687  ARG B CD  
14141 N NE  . ARG B 689  ? 0.2401 0.2789 0.2498 0.0064  -0.0091 -0.0142 687  ARG B NE  
14142 C CZ  . ARG B 689  ? 0.2356 0.2716 0.2440 0.0050  -0.0084 -0.0150 687  ARG B CZ  
14143 N NH1 . ARG B 689  ? 0.2282 0.2605 0.2333 0.0039  -0.0084 -0.0154 687  ARG B NH1 
14144 N NH2 . ARG B 689  ? 0.2301 0.2669 0.2403 0.0048  -0.0076 -0.0153 687  ARG B NH2 
14145 N N   . ARG B 690  ? 0.1737 0.2102 0.1870 0.0163  -0.0076 -0.0121 688  ARG B N   
14146 C CA  . ARG B 690  ? 0.1851 0.2233 0.2006 0.0186  -0.0076 -0.0117 688  ARG B CA  
14147 C C   . ARG B 690  ? 0.1846 0.2195 0.1989 0.0204  -0.0076 -0.0110 688  ARG B C   
14148 O O   . ARG B 690  ? 0.1889 0.2249 0.2044 0.0225  -0.0080 -0.0105 688  ARG B O   
14149 C CB  . ARG B 690  ? 0.2206 0.2586 0.2378 0.0190  -0.0064 -0.0126 688  ARG B CB  
14150 C CG  . ARG B 690  ? 0.2005 0.2421 0.2193 0.0176  -0.0063 -0.0131 688  ARG B CG  
14151 C CD  . ARG B 690  ? 0.2441 0.2911 0.2654 0.0186  -0.0070 -0.0126 688  ARG B CD  
14152 N NE  . ARG B 690  ? 0.2626 0.3101 0.2855 0.0213  -0.0065 -0.0126 688  ARG B NE  
14153 C CZ  . ARG B 690  ? 0.2781 0.3264 0.3015 0.0235  -0.0072 -0.0118 688  ARG B CZ  
14154 N NH1 . ARG B 690  ? 0.2906 0.3399 0.3134 0.0232  -0.0086 -0.0109 688  ARG B NH1 
14155 N NH2 . ARG B 690  ? 0.2421 0.2901 0.2666 0.0260  -0.0066 -0.0120 688  ARG B NH2 
14156 N N   . THR B 691  ? 0.1854 0.2162 0.1972 0.0196  -0.0071 -0.0110 689  THR B N   
14157 C CA  . THR B 691  ? 0.2051 0.2326 0.2160 0.0211  -0.0068 -0.0103 689  THR B CA  
14158 C C   . THR B 691  ? 0.2054 0.2305 0.2134 0.0207  -0.0072 -0.0094 689  THR B C   
14159 O O   . THR B 691  ? 0.2435 0.2674 0.2508 0.0222  -0.0077 -0.0084 689  THR B O   
14160 C CB  . THR B 691  ? 0.1919 0.2160 0.2030 0.0210  -0.0054 -0.0110 689  THR B CB  
14161 O OG1 . THR B 691  ? 0.2110 0.2337 0.2209 0.0190  -0.0047 -0.0116 689  THR B OG1 
14162 C CG2 . THR B 691  ? 0.2288 0.2547 0.2424 0.0218  -0.0051 -0.0118 689  THR B CG2 
14163 N N   . LEU B 692  ? 0.1894 0.2132 0.1953 0.0188  -0.0068 -0.0097 690  LEU B N   
14164 C CA  . LEU B 692  ? 0.1932 0.2139 0.1962 0.0185  -0.0066 -0.0090 690  LEU B CA  
14165 C C   . LEU B 692  ? 0.1973 0.2191 0.1983 0.0188  -0.0081 -0.0079 690  LEU B C   
14166 O O   . LEU B 692  ? 0.2396 0.2641 0.2403 0.0178  -0.0091 -0.0082 690  LEU B O   
14167 C CB  . LEU B 692  ? 0.2056 0.2242 0.2069 0.0167  -0.0054 -0.0097 690  LEU B CB  
14168 C CG  . LEU B 692  ? 0.2239 0.2410 0.2269 0.0166  -0.0040 -0.0105 690  LEU B CG  
14169 C CD1 . LEU B 692  ? 0.2486 0.2635 0.2499 0.0151  -0.0028 -0.0111 690  LEU B CD1 
14170 C CD2 . LEU B 692  ? 0.2324 0.2473 0.2362 0.0179  -0.0035 -0.0099 690  LEU B CD2 
14171 N N   . GLY B 693  ? 0.2292 0.2488 0.2287 0.0199  -0.0082 -0.0068 691  GLY B N   
14172 C CA  . GLY B 693  ? 0.2296 0.2496 0.2269 0.0203  -0.0097 -0.0056 691  GLY B CA  
14173 C C   . GLY B 693  ? 0.2479 0.2638 0.2415 0.0200  -0.0090 -0.0047 691  GLY B C   
14174 O O   . GLY B 693  ? 0.2566 0.2697 0.2498 0.0193  -0.0073 -0.0051 691  GLY B O   
14175 N N   . PRO B 694  ? 0.2976 0.3133 0.2887 0.0205  -0.0103 -0.0034 692  PRO B N   
14176 C CA  . PRO B 694  ? 0.2809 0.2929 0.2680 0.0199  -0.0096 -0.0026 692  PRO B CA  
14177 C C   . PRO B 694  ? 0.2966 0.3049 0.2836 0.0206  -0.0081 -0.0018 692  PRO B C   
14178 O O   . PRO B 694  ? 0.3544 0.3600 0.3391 0.0196  -0.0067 -0.0016 692  PRO B O   
14179 C CB  . PRO B 694  ? 0.3214 0.3343 0.3060 0.0205  -0.0116 -0.0012 692  PRO B CB  
14180 C CG  . PRO B 694  ? 0.3599 0.3768 0.3481 0.0220  -0.0133 -0.0012 692  PRO B CG  
14181 C CD  . PRO B 694  ? 0.3007 0.3199 0.2924 0.0214  -0.0125 -0.0028 692  PRO B CD  
14182 N N   . GLY B 695  ? 0.2767 0.2851 0.2665 0.0222  -0.0084 -0.0015 693  GLY B N   
14183 C CA  . GLY B 695  ? 0.2937 0.2983 0.2835 0.0227  -0.0072 -0.0009 693  GLY B CA  
14184 C C   . GLY B 695  ? 0.2950 0.2987 0.2869 0.0217  -0.0055 -0.0021 693  GLY B C   
14185 O O   . GLY B 695  ? 0.3444 0.3452 0.3367 0.0219  -0.0046 -0.0016 693  GLY B O   
14186 N N   . HIS B 696  ? 0.2857 0.2919 0.2791 0.0207  -0.0051 -0.0036 694  HIS B N   
14187 C CA  . HIS B 696  ? 0.2426 0.2481 0.2380 0.0198  -0.0036 -0.0047 694  HIS B CA  
14188 C C   . HIS B 696  ? 0.2544 0.2588 0.2476 0.0181  -0.0022 -0.0049 694  HIS B C   
14189 O O   . HIS B 696  ? 0.3233 0.3293 0.3167 0.0171  -0.0020 -0.0061 694  HIS B O   
14190 C CB  . HIS B 696  ? 0.2409 0.2494 0.2393 0.0199  -0.0039 -0.0061 694  HIS B CB  
14191 C CG  . HIS B 696  ? 0.2245 0.2347 0.2247 0.0217  -0.0052 -0.0059 694  HIS B CG  
14192 N ND1 . HIS B 696  ? 0.2351 0.2490 0.2363 0.0221  -0.0064 -0.0062 694  HIS B ND1 
14193 C CD2 . HIS B 696  ? 0.2475 0.2559 0.2486 0.0233  -0.0054 -0.0054 694  HIS B CD2 
14194 C CE1 . HIS B 696  ? 0.2504 0.2653 0.2533 0.0240  -0.0072 -0.0059 694  HIS B CE1 
14195 N NE2 . HIS B 696  ? 0.2456 0.2569 0.2483 0.0248  -0.0066 -0.0055 694  HIS B NE2 
14196 N N   . GLY B 697  ? 0.2886 0.2902 0.2798 0.0178  -0.0013 -0.0038 695  GLY B N   
14197 C CA  . GLY B 697  ? 0.2716 0.2722 0.2605 0.0165  0.0001  -0.0039 695  GLY B CA  
14198 C C   . GLY B 697  ? 0.2298 0.2303 0.2208 0.0156  0.0018  -0.0049 695  GLY B C   
14199 O O   . GLY B 697  ? 0.2600 0.2600 0.2539 0.0159  0.0021  -0.0051 695  GLY B O   
14200 N N   . PRO B 698  ? 0.2706 0.2713 0.2603 0.0147  0.0028  -0.0057 696  PRO B N   
14201 C CA  . PRO B 698  ? 0.2558 0.2566 0.2476 0.0140  0.0043  -0.0066 696  PRO B CA  
14202 C C   . PRO B 698  ? 0.2258 0.2247 0.2181 0.0137  0.0059  -0.0057 696  PRO B C   
14203 O O   . PRO B 698  ? 0.2494 0.2467 0.2396 0.0137  0.0062  -0.0042 696  PRO B O   
14204 C CB  . PRO B 698  ? 0.2778 0.2789 0.2673 0.0133  0.0050  -0.0075 696  PRO B CB  
14205 C CG  . PRO B 698  ? 0.3577 0.3578 0.3430 0.0133  0.0045  -0.0066 696  PRO B CG  
14206 C CD  . PRO B 698  ? 0.3078 0.3086 0.2936 0.0142  0.0025  -0.0057 696  PRO B CD  
14207 N N   . LEU B 699  ? 0.2097 0.2091 0.2051 0.0133  0.0069  -0.0063 697  LEU B N   
14208 C CA  . LEU B 699  ? 0.2025 0.2008 0.1990 0.0127  0.0085  -0.0055 697  LEU B CA  
14209 C C   . LEU B 699  ? 0.2104 0.2083 0.2043 0.0121  0.0103  -0.0052 697  LEU B C   
14210 O O   . LEU B 699  ? 0.2505 0.2471 0.2434 0.0117  0.0115  -0.0039 697  LEU B O   
14211 C CB  . LEU B 699  ? 0.2092 0.2083 0.2097 0.0124  0.0089  -0.0064 697  LEU B CB  
14212 C CG  . LEU B 699  ? 0.2403 0.2396 0.2432 0.0129  0.0073  -0.0068 697  LEU B CG  
14213 C CD1 . LEU B 699  ? 0.2491 0.2493 0.2555 0.0125  0.0077  -0.0077 697  LEU B CD1 
14214 C CD2 . LEU B 699  ? 0.3067 0.3040 0.3093 0.0132  0.0068  -0.0055 697  LEU B CD2 
14215 N N   . GLY B 700  ? 0.2056 0.2044 0.1984 0.0121  0.0106  -0.0065 698  GLY B N   
14216 C CA  . GLY B 700  ? 0.2093 0.2078 0.2002 0.0118  0.0126  -0.0066 698  GLY B CA  
14217 C C   . GLY B 700  ? 0.1989 0.1986 0.1922 0.0117  0.0134  -0.0080 698  GLY B C   
14218 O O   . GLY B 700  ? 0.1994 0.2000 0.1949 0.0119  0.0121  -0.0090 698  GLY B O   
14219 N N   . PRO B 701  ? 0.2037 0.2034 0.1968 0.0116  0.0155  -0.0081 699  PRO B N   
14220 C CA  . PRO B 701  ? 0.1911 0.1919 0.1864 0.0118  0.0162  -0.0094 699  PRO B CA  
14221 C C   . PRO B 701  ? 0.1860 0.1880 0.1862 0.0117  0.0156  -0.0095 699  PRO B C   
14222 O O   . PRO B 701  ? 0.2073 0.2096 0.2098 0.0113  0.0159  -0.0084 699  PRO B O   
14223 C CB  . PRO B 701  ? 0.2018 0.2025 0.1963 0.0119  0.0188  -0.0091 699  PRO B CB  
14224 C CG  . PRO B 701  ? 0.2321 0.2314 0.2222 0.0117  0.0193  -0.0080 699  PRO B CG  
14225 C CD  . PRO B 701  ? 0.2119 0.2108 0.2025 0.0114  0.0174  -0.0070 699  PRO B CD  
14226 N N   . ILE B 702  ? 0.1868 0.1893 0.1883 0.0119  0.0144  -0.0108 700  ILE B N   
14227 C CA  A ILE B 702  ? 0.1825 0.1861 0.1882 0.0118  0.0137  -0.0111 700  ILE B CA  
14228 C CA  B ILE B 702  ? 0.1823 0.1860 0.1880 0.0118  0.0136  -0.0111 700  ILE B CA  
14229 C C   . ILE B 702  ? 0.1883 0.1927 0.1958 0.0121  0.0146  -0.0120 700  ILE B C   
14230 O O   . ILE B 702  ? 0.1842 0.1881 0.1897 0.0124  0.0148  -0.0130 700  ILE B O   
14231 C CB  A ILE B 702  ? 0.1708 0.1745 0.1766 0.0119  0.0115  -0.0116 700  ILE B CB  
14232 C CB  B ILE B 702  ? 0.1712 0.1750 0.1769 0.0119  0.0115  -0.0117 700  ILE B CB  
14233 C CG1 A ILE B 702  ? 0.1909 0.1940 0.1959 0.0119  0.0106  -0.0106 700  ILE B CG1 
14234 C CG1 B ILE B 702  ? 0.1846 0.1877 0.1885 0.0120  0.0105  -0.0108 700  ILE B CG1 
14235 C CG2 A ILE B 702  ? 0.1877 0.1924 0.1971 0.0119  0.0109  -0.0123 700  ILE B CG2 
14236 C CG2 B ILE B 702  ? 0.1865 0.1911 0.1961 0.0119  0.0108  -0.0120 700  ILE B CG2 
14237 C CD1 A ILE B 702  ? 0.1896 0.1932 0.1948 0.0122  0.0087  -0.0110 700  ILE B CD1 
14238 C CD1 B ILE B 702  ? 0.1942 0.1968 0.1998 0.0118  0.0108  -0.0095 700  ILE B CD1 
14239 N N   . VAL B 703  ? 0.1712 0.1767 0.1824 0.0120  0.0152  -0.0116 701  VAL B N   
14240 C CA  . VAL B 703  ? 0.1621 0.1686 0.1757 0.0124  0.0159  -0.0123 701  VAL B CA  
14241 C C   . VAL B 703  ? 0.1782 0.1851 0.1939 0.0123  0.0141  -0.0130 701  VAL B C   
14242 O O   . VAL B 703  ? 0.1783 0.1856 0.1960 0.0119  0.0130  -0.0126 701  VAL B O   
14243 C CB  . VAL B 703  ? 0.1662 0.1743 0.1831 0.0121  0.0175  -0.0113 701  VAL B CB  
14244 C CG1 . VAL B 703  ? 0.1896 0.1992 0.2098 0.0126  0.0178  -0.0119 701  VAL B CG1 
14245 C CG2 . VAL B 703  ? 0.1938 0.2016 0.2083 0.0123  0.0196  -0.0106 701  VAL B CG2 
14246 N N   . CYS B 704  ? 0.1646 0.1712 0.1795 0.0127  0.0137  -0.0141 702  CYS B N   
14247 C CA  . CYS B 704  ? 0.1615 0.1684 0.1780 0.0127  0.0121  -0.0148 702  CYS B CA  
14248 C C   . CYS B 704  ? 0.1700 0.1776 0.1891 0.0131  0.0126  -0.0152 702  CYS B C   
14249 O O   . CYS B 704  ? 0.1710 0.1781 0.1889 0.0137  0.0136  -0.0157 702  CYS B O   
14250 C CB  . CYS B 704  ? 0.1684 0.1742 0.1818 0.0126  0.0111  -0.0157 702  CYS B CB  
14251 S SG  . CYS B 704  ? 0.1841 0.1894 0.1947 0.0122  0.0102  -0.0153 702  CYS B SG  
14252 N N   . ILE B 705  ? 0.1555 0.1643 0.1781 0.0129  0.0119  -0.0148 703  ILE B N   
14253 C CA  . ILE B 705  ? 0.1735 0.1834 0.1991 0.0133  0.0122  -0.0150 703  ILE B CA  
14254 C C   . ILE B 705  ? 0.1644 0.1741 0.1908 0.0131  0.0103  -0.0155 703  ILE B C   
14255 O O   . ILE B 705  ? 0.1679 0.1776 0.1948 0.0125  0.0091  -0.0154 703  ILE B O   
14256 C CB  . ILE B 705  ? 0.1612 0.1729 0.1903 0.0129  0.0129  -0.0139 703  ILE B CB  
14257 C CG1 . ILE B 705  ? 0.1693 0.1813 0.1976 0.0132  0.0151  -0.0133 703  ILE B CG1 
14258 C CG2 . ILE B 705  ? 0.1650 0.1782 0.1977 0.0133  0.0126  -0.0140 703  ILE B CG2 
14259 C CD1 . ILE B 705  ? 0.1951 0.2088 0.2264 0.0124  0.0159  -0.0120 703  ILE B CD1 
14260 N N   . SER B 706  ? 0.1679 0.1772 0.1942 0.0137  0.0102  -0.0162 704  SER B N   
14261 C CA  . SER B 706  ? 0.1918 0.2004 0.2177 0.0135  0.0085  -0.0168 704  SER B CA  
14262 C C   . SER B 706  ? 0.1618 0.1712 0.1905 0.0140  0.0081  -0.0168 704  SER B C   
14263 O O   . SER B 706  ? 0.1796 0.1898 0.2100 0.0148  0.0092  -0.0166 704  SER B O   
14264 C CB  . SER B 706  ? 0.1838 0.1907 0.2061 0.0135  0.0083  -0.0175 704  SER B CB  
14265 O OG  . SER B 706  ? 0.1773 0.1834 0.1985 0.0143  0.0096  -0.0179 704  SER B OG  
14266 N N   . PRO B 707  ? 0.1660 0.1752 0.1951 0.0137  0.0065  -0.0170 705  PRO B N   
14267 C CA  . PRO B 707  ? 0.1803 0.1901 0.2118 0.0141  0.0058  -0.0170 705  PRO B CA  
14268 C C   . PRO B 707  ? 0.1795 0.1877 0.2092 0.0147  0.0057  -0.0175 705  PRO B C   
14269 O O   . PRO B 707  ? 0.1984 0.2049 0.2249 0.0146  0.0059  -0.0180 705  PRO B O   
14270 C CB  . PRO B 707  ? 0.1976 0.2075 0.2295 0.0133  0.0040  -0.0170 705  PRO B CB  
14271 C CG  . PRO B 707  ? 0.1989 0.2076 0.2275 0.0128  0.0038  -0.0174 705  PRO B CG  
14272 C CD  . PRO B 707  ? 0.1892 0.1978 0.2166 0.0129  0.0053  -0.0173 705  PRO B CD  
14273 N N   . TRP B 708  ? 0.1666 0.1752 0.1984 0.0155  0.0053  -0.0174 706  TRP B N   
14274 C CA  . TRP B 708  ? 0.1730 0.1797 0.2031 0.0162  0.0052  -0.0178 706  TRP B CA  
14275 C C   . TRP B 708  ? 0.1814 0.1865 0.2092 0.0154  0.0036  -0.0181 706  TRP B C   
14276 O O   . TRP B 708  ? 0.1911 0.1940 0.2164 0.0156  0.0036  -0.0186 706  TRP B O   
14277 C CB  . TRP B 708  ? 0.1723 0.1797 0.2052 0.0175  0.0053  -0.0175 706  TRP B CB  
14278 C CG  . TRP B 708  ? 0.1730 0.1815 0.2082 0.0172  0.0035  -0.0171 706  TRP B CG  
14279 C CD1 . TRP B 708  ? 0.2161 0.2270 0.2547 0.0169  0.0029  -0.0165 706  TRP B CD1 
14280 C CD2 . TRP B 708  ? 0.1913 0.1981 0.2249 0.0171  0.0019  -0.0172 706  TRP B CD2 
14281 N NE1 . TRP B 708  ? 0.1959 0.2068 0.2351 0.0165  0.0010  -0.0163 706  TRP B NE1 
14282 C CE2 . TRP B 708  ? 0.1872 0.1956 0.2233 0.0167  0.0004  -0.0168 706  TRP B CE2 
14283 C CE3 . TRP B 708  ? 0.2109 0.2148 0.2411 0.0171  0.0016  -0.0177 706  TRP B CE3 
14284 C CZ2 . TRP B 708  ? 0.1851 0.1923 0.2202 0.0165  -0.0013 -0.0167 706  TRP B CZ2 
14285 C CZ3 . TRP B 708  ? 0.1965 0.1993 0.2259 0.0168  -0.0001 -0.0175 706  TRP B CZ3 
14286 C CH2 . TRP B 708  ? 0.2091 0.2136 0.2408 0.0166  -0.0015 -0.0170 706  TRP B CH2 
14287 N N   . ASN B 709  ? 0.1752 0.1813 0.2038 0.0146  0.0024  -0.0179 707  ASN B N   
14288 C CA  . ASN B 709  ? 0.1790 0.1840 0.2063 0.0141  0.0009  -0.0180 707  ASN B CA  
14289 C C   . ASN B 709  ? 0.1957 0.1995 0.2196 0.0132  0.0008  -0.0185 707  ASN B C   
14290 O O   . ASN B 709  ? 0.2233 0.2257 0.2454 0.0128  -0.0001 -0.0185 707  ASN B O   
14291 C CB  . ASN B 709  ? 0.1958 0.2022 0.2250 0.0137  -0.0004 -0.0177 707  ASN B CB  
14292 C CG  . ASN B 709  ? 0.2070 0.2141 0.2357 0.0128  -0.0004 -0.0178 707  ASN B CG  
14293 O OD1 . ASN B 709  ? 0.2337 0.2418 0.2636 0.0129  0.0005  -0.0177 707  ASN B OD1 
14294 N ND2 . ASN B 709  ? 0.2193 0.2259 0.2463 0.0122  -0.0014 -0.0181 707  ASN B ND2 
14295 N N   . PHE B 710  ? 0.1843 0.1886 0.2073 0.0128  0.0016  -0.0186 708  PHE B N   
14296 C CA  . PHE B 710  ? 0.1933 0.1967 0.2132 0.0120  0.0016  -0.0190 708  PHE B CA  
14297 C C   . PHE B 710  ? 0.2022 0.2049 0.2211 0.0124  0.0029  -0.0192 708  PHE B C   
14298 O O   . PHE B 710  ? 0.1959 0.1994 0.2144 0.0122  0.0035  -0.0192 708  PHE B O   
14299 C CB  . PHE B 710  ? 0.1950 0.1999 0.2149 0.0114  0.0012  -0.0190 708  PHE B CB  
14300 C CG  . PHE B 710  ? 0.2221 0.2274 0.2426 0.0111  0.0001  -0.0189 708  PHE B CG  
14301 C CD1 . PHE B 710  ? 0.2299 0.2343 0.2496 0.0109  -0.0008 -0.0189 708  PHE B CD1 
14302 C CD2 . PHE B 710  ? 0.2160 0.2226 0.2378 0.0111  -0.0002 -0.0188 708  PHE B CD2 
14303 C CE1 . PHE B 710  ? 0.2749 0.2796 0.2947 0.0106  -0.0018 -0.0188 708  PHE B CE1 
14304 C CE2 . PHE B 710  ? 0.2350 0.2417 0.2569 0.0109  -0.0013 -0.0189 708  PHE B CE2 
14305 C CZ  . PHE B 710  ? 0.2667 0.2726 0.2876 0.0106  -0.0020 -0.0189 708  PHE B CZ  
14306 N N   . PRO B 711  ? 0.2069 0.2078 0.2248 0.0130  0.0033  -0.0194 709  PRO B N   
14307 C CA  . PRO B 711  ? 0.2147 0.2149 0.2319 0.0137  0.0047  -0.0197 709  PRO B CA  
14308 C C   . PRO B 711  ? 0.1848 0.1839 0.1988 0.0129  0.0050  -0.0201 709  PRO B C   
14309 O O   . PRO B 711  ? 0.1916 0.1902 0.2046 0.0134  0.0062  -0.0203 709  PRO B O   
14310 C CB  . PRO B 711  ? 0.2011 0.1994 0.2183 0.0147  0.0049  -0.0199 709  PRO B CB  
14311 C CG  . PRO B 711  ? 0.2211 0.2180 0.2370 0.0139  0.0034  -0.0199 709  PRO B CG  
14312 C CD  . PRO B 711  ? 0.2106 0.2099 0.2282 0.0132  0.0025  -0.0195 709  PRO B CD  
14313 N N   . LEU B 712  ? 0.1876 0.1863 0.1997 0.0117  0.0040  -0.0203 710  LEU B N   
14314 C CA  . LEU B 712  ? 0.1833 0.1816 0.1928 0.0108  0.0040  -0.0206 710  LEU B CA  
14315 C C   . LEU B 712  ? 0.1862 0.1869 0.1964 0.0101  0.0035  -0.0202 710  LEU B C   
14316 O O   . LEU B 712  ? 0.2030 0.2043 0.2122 0.0099  0.0039  -0.0202 710  LEU B O   
14317 C CB  . LEU B 712  ? 0.1943 0.1904 0.2010 0.0098  0.0033  -0.0210 710  LEU B CB  
14318 C CG  . LEU B 712  ? 0.1711 0.1668 0.1750 0.0087  0.0032  -0.0213 710  LEU B CG  
14319 C CD1 . LEU B 712  ? 0.1896 0.1839 0.1918 0.0094  0.0043  -0.0217 710  LEU B CD1 
14320 C CD2 . LEU B 712  ? 0.2277 0.2213 0.2291 0.0074  0.0022  -0.0216 710  LEU B CD2 
14321 N N   . ALA B 713  ? 0.1803 0.1824 0.1921 0.0099  0.0027  -0.0199 711  ALA B N   
14322 C CA  . ALA B 713  ? 0.1781 0.1822 0.1902 0.0094  0.0022  -0.0197 711  ALA B CA  
14323 C C   . ALA B 713  ? 0.1948 0.2002 0.2084 0.0100  0.0027  -0.0194 711  ALA B C   
14324 O O   . ALA B 713  ? 0.1933 0.1994 0.2059 0.0099  0.0028  -0.0193 711  ALA B O   
14325 C CB  . ALA B 713  ? 0.2114 0.2163 0.2243 0.0090  0.0013  -0.0196 711  ALA B CB  
14326 N N   . ILE B 714  ? 0.1894 0.1950 0.2052 0.0107  0.0030  -0.0191 712  ILE B N   
14327 C CA  . ILE B 714  ? 0.2000 0.2066 0.2172 0.0111  0.0035  -0.0187 712  ILE B CA  
14328 C C   . ILE B 714  ? 0.1968 0.2028 0.2129 0.0114  0.0046  -0.0186 712  ILE B C   
14329 O O   . ILE B 714  ? 0.1817 0.1882 0.1974 0.0114  0.0049  -0.0183 712  ILE B O   
14330 C CB  . ILE B 714  ? 0.1843 0.1913 0.2042 0.0115  0.0033  -0.0184 712  ILE B CB  
14331 C CG1 . ILE B 714  ? 0.2215 0.2290 0.2417 0.0112  0.0021  -0.0186 712  ILE B CG1 
14332 C CG2 . ILE B 714  ? 0.1918 0.1994 0.2131 0.0118  0.0040  -0.0179 712  ILE B CG2 
14333 C CD1 . ILE B 714  ? 0.3046 0.3124 0.3271 0.0114  0.0016  -0.0184 712  ILE B CD1 
14334 N N   . PHE B 715  ? 0.1739 0.1786 0.1893 0.0117  0.0053  -0.0189 713  PHE B N   
14335 C CA  . PHE B 715  ? 0.1764 0.1803 0.1902 0.0120  0.0065  -0.0190 713  PHE B CA  
14336 C C   . PHE B 715  ? 0.1830 0.1867 0.1940 0.0114  0.0062  -0.0191 713  PHE B C   
14337 O O   . PHE B 715  ? 0.1784 0.1824 0.1887 0.0115  0.0067  -0.0187 713  PHE B O   
14338 C CB  . PHE B 715  ? 0.1986 0.2007 0.2114 0.0125  0.0070  -0.0196 713  PHE B CB  
14339 C CG  . PHE B 715  ? 0.1809 0.1816 0.1914 0.0129  0.0083  -0.0198 713  PHE B CG  
14340 C CD1 . PHE B 715  ? 0.1751 0.1766 0.1870 0.0138  0.0098  -0.0195 713  PHE B CD1 
14341 C CD2 . PHE B 715  ? 0.1885 0.1874 0.1953 0.0123  0.0081  -0.0205 713  PHE B CD2 
14342 C CE1 . PHE B 715  ? 0.1898 0.1900 0.1993 0.0143  0.0111  -0.0197 713  PHE B CE1 
14343 C CE2 . PHE B 715  ? 0.1854 0.1828 0.1896 0.0127  0.0092  -0.0208 713  PHE B CE2 
14344 C CZ  . PHE B 715  ? 0.1849 0.1830 0.1904 0.0138  0.0109  -0.0205 713  PHE B CZ  
14345 N N   . THR B 716  ? 0.1728 0.1761 0.1823 0.0106  0.0051  -0.0195 714  THR B N   
14346 C CA  . THR B 716  ? 0.1775 0.1810 0.1846 0.0099  0.0046  -0.0196 714  THR B CA  
14347 C C   . THR B 716  ? 0.1674 0.1729 0.1755 0.0099  0.0041  -0.0190 714  THR B C   
14348 O O   . THR B 716  ? 0.1777 0.1836 0.1844 0.0098  0.0041  -0.0188 714  THR B O   
14349 C CB  . THR B 716  ? 0.1711 0.1740 0.1767 0.0088  0.0036  -0.0201 714  THR B CB  
14350 O OG1 . THR B 716  ? 0.2071 0.2074 0.2112 0.0089  0.0040  -0.0207 714  THR B OG1 
14351 C CG2 . THR B 716  ? 0.2005 0.2041 0.2040 0.0079  0.0029  -0.0201 714  THR B CG2 
14352 N N   . GLY B 717  ? 0.1730 0.1797 0.1834 0.0100  0.0036  -0.0188 715  GLY B N   
14353 C CA  . GLY B 717  ? 0.1640 0.1723 0.1753 0.0102  0.0031  -0.0184 715  GLY B CA  
14354 C C   . GLY B 717  ? 0.1631 0.1713 0.1746 0.0108  0.0038  -0.0178 715  GLY B C   
14355 O O   . GLY B 717  ? 0.1656 0.1744 0.1761 0.0109  0.0035  -0.0174 715  GLY B O   
14356 N N   . GLN B 718  ? 0.1653 0.1727 0.1780 0.0112  0.0047  -0.0176 716  GLN B N   
14357 C CA  . GLN B 718  ? 0.1615 0.1688 0.1745 0.0116  0.0055  -0.0169 716  GLN B CA  
14358 C C   . GLN B 718  ? 0.1595 0.1661 0.1696 0.0115  0.0060  -0.0168 716  GLN B C   
14359 O O   . GLN B 718  ? 0.1637 0.1705 0.1728 0.0116  0.0059  -0.0162 716  GLN B O   
14360 C CB  . GLN B 718  ? 0.1683 0.1753 0.1834 0.0118  0.0064  -0.0166 716  GLN B CB  
14361 C CG  . GLN B 718  ? 0.1603 0.1678 0.1781 0.0118  0.0057  -0.0167 716  GLN B CG  
14362 C CD  . GLN B 718  ? 0.1820 0.1897 0.2023 0.0119  0.0064  -0.0163 716  GLN B CD  
14363 O OE1 . GLN B 718  ? 0.1927 0.2008 0.2150 0.0118  0.0060  -0.0159 716  GLN B OE1 
14364 N NE2 . GLN B 718  ? 0.1842 0.1918 0.2046 0.0122  0.0075  -0.0164 716  GLN B NE2 
14365 N N   . ILE B 719  ? 0.1687 0.1743 0.1772 0.0113  0.0065  -0.0174 717  ILE B N   
14366 C CA  . ILE B 719  ? 0.1737 0.1783 0.1791 0.0112  0.0070  -0.0174 717  ILE B CA  
14367 C C   . ILE B 719  ? 0.1766 0.1818 0.1800 0.0107  0.0058  -0.0174 717  ILE B C   
14368 O O   . ILE B 719  ? 0.1792 0.1842 0.1807 0.0107  0.0058  -0.0169 717  ILE B O   
14369 C CB  . ILE B 719  ? 0.1895 0.1925 0.1933 0.0112  0.0077  -0.0183 717  ILE B CB  
14370 C CG1 . ILE B 719  ? 0.1872 0.1899 0.1930 0.0120  0.0091  -0.0182 717  ILE B CG1 
14371 C CG2 . ILE B 719  ? 0.2667 0.2683 0.2666 0.0109  0.0079  -0.0186 717  ILE B CG2 
14372 C CD1 . ILE B 719  ? 0.2696 0.2708 0.2746 0.0122  0.0096  -0.0190 717  ILE B CD1 
14373 N N   . ALA B 720  ? 0.1695 0.1755 0.1734 0.0102  0.0046  -0.0178 718  ALA B N   
14374 C CA  . ALA B 720  ? 0.1644 0.1716 0.1670 0.0096  0.0034  -0.0178 718  ALA B CA  
14375 C C   . ALA B 720  ? 0.1761 0.1847 0.1795 0.0102  0.0030  -0.0169 718  ALA B C   
14376 O O   . ALA B 720  ? 0.1747 0.1838 0.1764 0.0101  0.0024  -0.0165 718  ALA B O   
14377 C CB  . ALA B 720  ? 0.1964 0.2047 0.2000 0.0089  0.0024  -0.0182 718  ALA B CB  
14378 N N   . ALA B 721  ? 0.1717 0.1807 0.1777 0.0108  0.0031  -0.0166 719  ALA B N   
14379 C CA  . ALA B 721  ? 0.1756 0.1855 0.1824 0.0115  0.0027  -0.0158 719  ALA B CA  
14380 C C   . ALA B 721  ? 0.1631 0.1717 0.1682 0.0118  0.0034  -0.0150 719  ALA B C   
14381 O O   . ALA B 721  ? 0.1709 0.1799 0.1748 0.0121  0.0028  -0.0144 719  ALA B O   
14382 C CB  . ALA B 721  ? 0.1707 0.1806 0.1802 0.0120  0.0028  -0.0157 719  ALA B CB  
14383 N N   . ALA B 722  ? 0.1574 0.1647 0.1626 0.0117  0.0048  -0.0150 720  ALA B N   
14384 C CA  . ALA B 722  ? 0.1561 0.1622 0.1596 0.0119  0.0057  -0.0142 720  ALA B CA  
14385 C C   . ALA B 722  ? 0.1731 0.1788 0.1730 0.0116  0.0053  -0.0143 720  ALA B C   
14386 O O   . ALA B 722  ? 0.1736 0.1791 0.1718 0.0118  0.0051  -0.0134 720  ALA B O   
14387 C CB  . ALA B 722  ? 0.1672 0.1724 0.1715 0.0119  0.0073  -0.0142 720  ALA B CB  
14388 N N   . LEU B 723  ? 0.1727 0.1782 0.1713 0.0110  0.0052  -0.0152 721  LEU B N   
14389 C CA  . LEU B 723  ? 0.1696 0.1745 0.1645 0.0105  0.0047  -0.0154 721  LEU B CA  
14390 C C   . LEU B 723  ? 0.1852 0.1917 0.1797 0.0105  0.0030  -0.0150 721  LEU B C   
14391 O O   . LEU B 723  ? 0.1921 0.1983 0.1840 0.0105  0.0026  -0.0144 721  LEU B O   
14392 C CB  . LEU B 723  ? 0.1828 0.1869 0.1765 0.0098  0.0046  -0.0166 721  LEU B CB  
14393 C CG  . LEU B 723  ? 0.1782 0.1803 0.1712 0.0101  0.0063  -0.0172 721  LEU B CG  
14394 C CD1 . LEU B 723  ? 0.1878 0.1889 0.1800 0.0095  0.0059  -0.0184 721  LEU B CD1 
14395 C CD2 . LEU B 723  ? 0.1957 0.1962 0.1853 0.0103  0.0075  -0.0170 721  LEU B CD2 
14396 N N   . VAL B 724  ? 0.1743 0.1827 0.1713 0.0104  0.0020  -0.0152 722  VAL B N   
14397 C CA  . VAL B 724  ? 0.1675 0.1779 0.1643 0.0104  0.0004  -0.0148 722  VAL B CA  
14398 C C   . VAL B 724  ? 0.1726 0.1834 0.1699 0.0115  0.0001  -0.0136 722  VAL B C   
14399 O O   . VAL B 724  ? 0.1821 0.1940 0.1782 0.0117  -0.0011 -0.0130 722  VAL B O   
14400 C CB  . VAL B 724  ? 0.1666 0.1793 0.1659 0.0100  -0.0005 -0.0153 722  VAL B CB  
14401 C CG1 . VAL B 724  ? 0.1859 0.1995 0.1884 0.0111  -0.0003 -0.0150 722  VAL B CG1 
14402 C CG2 . VAL B 724  ? 0.1761 0.1911 0.1746 0.0095  -0.0021 -0.0152 722  VAL B CG2 
14403 N N   . ALA B 725  ? 0.1857 0.1953 0.1845 0.0122  0.0012  -0.0132 723  ALA B N   
14404 C CA  . ALA B 725  ? 0.1719 0.1809 0.1707 0.0131  0.0011  -0.0120 723  ALA B CA  
14405 C C   . ALA B 725  ? 0.1993 0.2066 0.1947 0.0129  0.0017  -0.0113 723  ALA B C   
14406 O O   . ALA B 725  ? 0.2297 0.2362 0.2245 0.0136  0.0016  -0.0101 723  ALA B O   
14407 C CB  . ALA B 725  ? 0.1974 0.2055 0.1987 0.0136  0.0020  -0.0118 723  ALA B CB  
14408 N N   . GLY B 726  ? 0.1841 0.1906 0.1770 0.0121  0.0022  -0.0119 724  GLY B N   
14409 C CA  . GLY B 726  ? 0.2007 0.2055 0.1898 0.0119  0.0027  -0.0113 724  GLY B CA  
14410 C C   . GLY B 726  ? 0.2047 0.2077 0.1933 0.0119  0.0048  -0.0111 724  GLY B C   
14411 O O   . GLY B 726  ? 0.2271 0.2287 0.2126 0.0119  0.0055  -0.0104 724  GLY B O   
14412 N N   . ASN B 727  ? 0.1939 0.1969 0.1852 0.0119  0.0059  -0.0117 725  ASN B N   
14413 C CA  . ASN B 727  ? 0.1902 0.1921 0.1818 0.0119  0.0080  -0.0115 725  ASN B CA  
14414 C C   . ASN B 727  ? 0.1829 0.1841 0.1732 0.0116  0.0090  -0.0127 725  ASN B C   
14415 O O   . ASN B 727  ? 0.2060 0.2078 0.1976 0.0114  0.0083  -0.0138 725  ASN B O   
14416 C CB  . ASN B 727  ? 0.1916 0.1941 0.1875 0.0121  0.0083  -0.0113 725  ASN B CB  
14417 C CG  . ASN B 727  ? 0.2117 0.2144 0.2088 0.0125  0.0072  -0.0103 725  ASN B CG  
14418 O OD1 . ASN B 727  ? 0.2086 0.2103 0.2049 0.0126  0.0076  -0.0091 725  ASN B OD1 
14419 N ND2 . ASN B 727  ? 0.1866 0.1905 0.1857 0.0128  0.0058  -0.0108 725  ASN B ND2 
14420 N N   . PRO B 728  ? 0.1799 0.1798 0.1678 0.0116  0.0107  -0.0126 726  PRO B N   
14421 C CA  . PRO B 728  ? 0.1902 0.1893 0.1775 0.0117  0.0120  -0.0138 726  PRO B CA  
14422 C C   . PRO B 728  ? 0.2040 0.2042 0.1958 0.0120  0.0129  -0.0138 726  PRO B C   
14423 O O   . PRO B 728  ? 0.1972 0.1982 0.1917 0.0121  0.0132  -0.0128 726  PRO B O   
14424 C CB  . PRO B 728  ? 0.2179 0.2155 0.2015 0.0119  0.0138  -0.0134 726  PRO B CB  
14425 C CG  . PRO B 728  ? 0.2192 0.2173 0.2036 0.0119  0.0141  -0.0117 726  PRO B CG  
14426 C CD  . PRO B 728  ? 0.2145 0.2135 0.2004 0.0117  0.0117  -0.0112 726  PRO B CD  
14427 N N   . VAL B 729  ? 0.1770 0.1769 0.1694 0.0122  0.0133  -0.0150 727  VAL B N   
14428 C CA  . VAL B 729  ? 0.1754 0.1764 0.1722 0.0124  0.0136  -0.0152 727  VAL B CA  
14429 C C   . VAL B 729  ? 0.2002 0.2007 0.1971 0.0131  0.0156  -0.0157 727  VAL B C   
14430 O O   . VAL B 729  ? 0.1929 0.1917 0.1866 0.0133  0.0162  -0.0166 727  VAL B O   
14431 C CB  . VAL B 729  ? 0.1906 0.1919 0.1886 0.0121  0.0119  -0.0161 727  VAL B CB  
14432 C CG1 . VAL B 729  ? 0.1969 0.1988 0.1984 0.0125  0.0123  -0.0165 727  VAL B CG1 
14433 C CG2 . VAL B 729  ? 0.1813 0.1838 0.1804 0.0118  0.0102  -0.0155 727  VAL B CG2 
14434 N N   . LEU B 730  ? 0.1773 0.1793 0.1781 0.0134  0.0167  -0.0151 728  LEU B N   
14435 C CA  . LEU B 730  ? 0.1773 0.1796 0.1797 0.0142  0.0183  -0.0155 728  LEU B CA  
14436 C C   . LEU B 730  ? 0.1661 0.1693 0.1722 0.0142  0.0172  -0.0160 728  LEU B C   
14437 O O   . LEU B 730  ? 0.1837 0.1884 0.1932 0.0139  0.0165  -0.0152 728  LEU B O   
14438 C CB  . LEU B 730  ? 0.1944 0.1981 0.1989 0.0143  0.0202  -0.0143 728  LEU B CB  
14439 C CG  . LEU B 730  ? 0.1984 0.2015 0.1996 0.0142  0.0217  -0.0135 728  LEU B CG  
14440 C CD1 . LEU B 730  ? 0.2194 0.2203 0.2156 0.0148  0.0224  -0.0147 728  LEU B CD1 
14441 C CD2 . LEU B 730  ? 0.2095 0.2121 0.2094 0.0133  0.0204  -0.0125 728  LEU B CD2 
14442 N N   . ALA B 731  ? 0.1684 0.1705 0.1736 0.0147  0.0169  -0.0171 729  ALA B N   
14443 C CA  . ALA B 731  ? 0.1574 0.1599 0.1653 0.0146  0.0155  -0.0176 729  ALA B CA  
14444 C C   . ALA B 731  ? 0.1906 0.1940 0.2015 0.0157  0.0168  -0.0176 729  ALA B C   
14445 O O   . ALA B 731  ? 0.1871 0.1892 0.1962 0.0166  0.0181  -0.0183 729  ALA B O   
14446 C CB  . ALA B 731  ? 0.2068 0.2074 0.2118 0.0143  0.0142  -0.0186 729  ALA B CB  
14447 N N   . LYS B 732  ? 0.1739 0.1793 0.1891 0.0156  0.0164  -0.0170 730  LYS B N   
14448 C CA  . LYS B 732  ? 0.1754 0.1823 0.1942 0.0165  0.0173  -0.0168 730  LYS B CA  
14449 C C   . LYS B 732  ? 0.1626 0.1696 0.1835 0.0164  0.0156  -0.0172 730  LYS B C   
14450 O O   . LYS B 732  ? 0.1775 0.1859 0.2011 0.0157  0.0144  -0.0166 730  LYS B O   
14451 C CB  . LYS B 732  ? 0.1790 0.1884 0.2012 0.0162  0.0184  -0.0156 730  LYS B CB  
14452 C CG  . LYS B 732  ? 0.1779 0.1891 0.2027 0.0173  0.0204  -0.0153 730  LYS B CG  
14453 C CD  . LYS B 732  ? 0.1803 0.1921 0.2079 0.0182  0.0197  -0.0158 730  LYS B CD  
14454 C CE  . LYS B 732  ? 0.1745 0.1884 0.2065 0.0174  0.0181  -0.0151 730  LYS B CE  
14455 N NZ  . LYS B 732  ? 0.1809 0.1952 0.2151 0.0183  0.0173  -0.0155 730  LYS B NZ  
14456 N N   . PRO B 733  ? 0.1570 0.1623 0.1765 0.0171  0.0153  -0.0181 731  PRO B N   
14457 C CA  . PRO B 733  ? 0.1773 0.1825 0.1983 0.0170  0.0135  -0.0183 731  PRO B CA  
14458 C C   . PRO B 733  ? 0.1604 0.1676 0.1858 0.0179  0.0139  -0.0178 731  PRO B C   
14459 O O   . PRO B 733  ? 0.1780 0.1864 0.2050 0.0188  0.0156  -0.0175 731  PRO B O   
14460 C CB  . PRO B 733  ? 0.1986 0.2008 0.2161 0.0174  0.0134  -0.0194 731  PRO B CB  
14461 C CG  . PRO B 733  ? 0.1936 0.1950 0.2095 0.0186  0.0155  -0.0197 731  PRO B CG  
14462 C CD  . PRO B 733  ? 0.1936 0.1966 0.2095 0.0180  0.0165  -0.0189 731  PRO B CD  
14463 N N   . ALA B 734  ? 0.1701 0.1777 0.1974 0.0175  0.0121  -0.0178 732  ALA B N   
14464 C CA  . ALA B 734  ? 0.1743 0.1839 0.2058 0.0182  0.0120  -0.0173 732  ALA B CA  
14465 C C   . ALA B 734  ? 0.1809 0.1898 0.2125 0.0200  0.0132  -0.0177 732  ALA B C   
14466 O O   . ALA B 734  ? 0.1923 0.1983 0.2204 0.0205  0.0133  -0.0185 732  ALA B O   
14467 C CB  . ALA B 734  ? 0.1835 0.1930 0.2160 0.0176  0.0098  -0.0173 732  ALA B CB  
14468 N N   . GLU B 735  ? 0.1798 0.1914 0.2155 0.0209  0.0140  -0.0170 733  GLU B N   
14469 C CA  . GLU B 735  ? 0.1922 0.2034 0.2282 0.0229  0.0154  -0.0174 733  GLU B CA  
14470 C C   . GLU B 735  ? 0.1959 0.2047 0.2310 0.0237  0.0140  -0.0179 733  GLU B C   
14471 O O   . GLU B 735  ? 0.2008 0.2074 0.2340 0.0253  0.0149  -0.0186 733  GLU B O   
14472 C CB  . GLU B 735  ? 0.1960 0.2112 0.2372 0.0238  0.0166  -0.0165 733  GLU B CB  
14473 C CG  . GLU B 735  ? 0.2585 0.2764 0.3043 0.0232  0.0148  -0.0156 733  GLU B CG  
14474 C CD  . GLU B 735  ? 0.2621 0.2820 0.3095 0.0212  0.0143  -0.0148 733  GLU B CD  
14475 O OE1 . GLU B 735  ? 0.2431 0.2614 0.2873 0.0201  0.0146  -0.0151 733  GLU B OE1 
14476 O OE2 . GLU B 735  ? 0.2731 0.2961 0.3250 0.0207  0.0137  -0.0140 733  GLU B OE2 
14477 N N   . GLU B 736  ? 0.1813 0.1900 0.2170 0.0227  0.0117  -0.0177 734  GLU B N   
14478 C CA  . GLU B 736  ? 0.1910 0.1975 0.2257 0.0233  0.0103  -0.0180 734  GLU B CA  
14479 C C   . GLU B 736  ? 0.1823 0.1846 0.2117 0.0229  0.0101  -0.0190 734  GLU B C   
14480 O O   . GLU B 736  ? 0.2284 0.2280 0.2562 0.0238  0.0096  -0.0194 734  GLU B O   
14481 C CB  . GLU B 736  ? 0.1939 0.2015 0.2306 0.0222  0.0081  -0.0175 734  GLU B CB  
14482 C CG  . GLU B 736  ? 0.2222 0.2337 0.2641 0.0225  0.0077  -0.0165 734  GLU B CG  
14483 C CD  . GLU B 736  ? 0.2530 0.2670 0.2967 0.0210  0.0079  -0.0160 734  GLU B CD  
14484 O OE1 . GLU B 736  ? 0.2027 0.2159 0.2439 0.0201  0.0089  -0.0163 734  GLU B OE1 
14485 O OE2 . GLU B 736  ? 0.2841 0.3009 0.3317 0.0205  0.0070  -0.0153 734  GLU B OE2 
14486 N N   . THR B 737  ? 0.1863 0.1879 0.2129 0.0214  0.0103  -0.0193 735  THR B N   
14487 C CA  . THR B 737  ? 0.1888 0.1870 0.2108 0.0205  0.0095  -0.0200 735  THR B CA  
14488 C C   . THR B 737  ? 0.1966 0.1936 0.2152 0.0202  0.0109  -0.0206 735  THR B C   
14489 O O   . THR B 737  ? 0.2097 0.2063 0.2261 0.0187  0.0103  -0.0207 735  THR B O   
14490 C CB  . THR B 737  ? 0.1964 0.1951 0.2182 0.0187  0.0077  -0.0197 735  THR B CB  
14491 O OG1 . THR B 737  ? 0.1971 0.1986 0.2207 0.0179  0.0079  -0.0192 735  THR B OG1 
14492 C CG2 . THR B 737  ? 0.2151 0.2141 0.2390 0.0190  0.0062  -0.0193 735  THR B CG2 
14493 N N   . PRO B 738  ? 0.1867 0.1830 0.2048 0.0216  0.0127  -0.0210 736  PRO B N   
14494 C CA  . PRO B 738  ? 0.1787 0.1737 0.1933 0.0213  0.0140  -0.0216 736  PRO B CA  
14495 C C   . PRO B 738  ? 0.2105 0.2013 0.2200 0.0207  0.0134  -0.0226 736  PRO B C   
14496 O O   . PRO B 738  ? 0.2015 0.1914 0.2078 0.0198  0.0137  -0.0229 736  PRO B O   
14497 C CB  . PRO B 738  ? 0.1850 0.1806 0.2006 0.0234  0.0163  -0.0217 736  PRO B CB  
14498 C CG  . PRO B 738  ? 0.2033 0.1982 0.2209 0.0249  0.0158  -0.0217 736  PRO B CG  
14499 C CD  . PRO B 738  ? 0.1836 0.1804 0.2043 0.0238  0.0137  -0.0209 736  PRO B CD  
14500 N N   . LEU B 739  ? 0.1819 0.1701 0.1904 0.0211  0.0124  -0.0229 737  LEU B N   
14501 C CA  . LEU B 739  ? 0.1830 0.1668 0.1865 0.0205  0.0119  -0.0239 737  LEU B CA  
14502 C C   . LEU B 739  ? 0.1932 0.1769 0.1947 0.0181  0.0104  -0.0239 737  LEU B C   
14503 O O   . LEU B 739  ? 0.2025 0.1843 0.2002 0.0171  0.0104  -0.0245 737  LEU B O   
14504 C CB  . LEU B 739  ? 0.2051 0.1857 0.2080 0.0215  0.0113  -0.0243 737  LEU B CB  
14505 C CG  . LEU B 739  ? 0.2121 0.1927 0.2170 0.0242  0.0128  -0.0244 737  LEU B CG  
14506 C CD1 . LEU B 739  ? 0.2292 0.2064 0.2335 0.0250  0.0117  -0.0245 737  LEU B CD1 
14507 C CD2 . LEU B 739  ? 0.2159 0.1947 0.2179 0.0254  0.0149  -0.0253 737  LEU B CD2 
14508 N N   . ILE B 740  ? 0.2015 0.1874 0.2055 0.0171  0.0090  -0.0231 738  ILE B N   
14509 C CA  . ILE B 740  ? 0.1785 0.1647 0.1809 0.0150  0.0076  -0.0230 738  ILE B CA  
14510 C C   . ILE B 740  ? 0.1811 0.1696 0.1834 0.0144  0.0082  -0.0229 738  ILE B C   
14511 O O   . ILE B 740  ? 0.2070 0.1952 0.2068 0.0130  0.0076  -0.0231 738  ILE B O   
14512 C CB  . ILE B 740  ? 0.2265 0.2141 0.2310 0.0142  0.0061  -0.0224 738  ILE B CB  
14513 C CG1 . ILE B 740  ? 0.2110 0.1989 0.2136 0.0121  0.0049  -0.0223 738  ILE B CG1 
14514 C CG2 . ILE B 740  ? 0.2355 0.2269 0.2442 0.0147  0.0063  -0.0216 738  ILE B CG2 
14515 C CD1 . ILE B 740  ? 0.2307 0.2150 0.2294 0.0110  0.0044  -0.0230 738  ILE B CD1 
14516 N N   . ALA B 741  ? 0.1782 0.1691 0.1832 0.0155  0.0094  -0.0224 739  ALA B N   
14517 C CA  . ALA B 741  ? 0.1700 0.1627 0.1747 0.0151  0.0101  -0.0221 739  ALA B CA  
14518 C C   . ALA B 741  ? 0.1910 0.1813 0.1915 0.0151  0.0110  -0.0229 739  ALA B C   
14519 O O   . ALA B 741  ? 0.1944 0.1849 0.1928 0.0140  0.0106  -0.0229 739  ALA B O   
14520 C CB  . ALA B 741  ? 0.2156 0.2111 0.2241 0.0161  0.0113  -0.0214 739  ALA B CB  
14521 N N   . ALA B 742  ? 0.1860 0.1740 0.1853 0.0165  0.0122  -0.0235 740  ALA B N   
14522 C CA  . ALA B 742  ? 0.1909 0.1759 0.1855 0.0166  0.0130  -0.0245 740  ALA B CA  
14523 C C   . ALA B 742  ? 0.2095 0.1921 0.2004 0.0148  0.0113  -0.0251 740  ALA B C   
14524 O O   . ALA B 742  ? 0.2147 0.1963 0.2022 0.0139  0.0112  -0.0254 740  ALA B O   
14525 C CB  . ALA B 742  ? 0.2041 0.1866 0.1979 0.0185  0.0145  -0.0252 740  ALA B CB  
14526 N N   . GLU B 743  ? 0.2076 0.1894 0.1992 0.0141  0.0099  -0.0250 741  GLU B N   
14527 C CA  . GLU B 743  ? 0.1922 0.1720 0.1806 0.0122  0.0082  -0.0255 741  GLU B CA  
14528 C C   . GLU B 743  ? 0.2069 0.1898 0.1959 0.0106  0.0072  -0.0248 741  GLU B C   
14529 O O   . GLU B 743  ? 0.2196 0.2017 0.2056 0.0092  0.0064  -0.0252 741  GLU B O   
14530 C CB  . GLU B 743  ? 0.2203 0.1986 0.2095 0.0118  0.0071  -0.0254 741  GLU B CB  
14531 C CG  . GLU B 743  ? 0.2403 0.2168 0.2266 0.0096  0.0055  -0.0257 741  GLU B CG  
14532 C CD  . GLU B 743  ? 0.2607 0.2326 0.2419 0.0091  0.0055  -0.0268 741  GLU B CD  
14533 O OE1 . GLU B 743  ? 0.2585 0.2281 0.2381 0.0108  0.0069  -0.0276 741  GLU B OE1 
14534 O OE2 . GLU B 743  ? 0.2892 0.2600 0.2681 0.0070  0.0040  -0.0270 741  GLU B OE2 
14535 N N   . GLY B 744  ? 0.2050 0.1917 0.1981 0.0109  0.0072  -0.0239 742  GLY B N   
14536 C CA  . GLY B 744  ? 0.2030 0.1925 0.1968 0.0098  0.0065  -0.0233 742  GLY B CA  
14537 C C   . GLY B 744  ? 0.2018 0.1913 0.1932 0.0099  0.0072  -0.0234 742  GLY B C   
14538 O O   . GLY B 744  ? 0.1984 0.1885 0.1881 0.0086  0.0062  -0.0233 742  GLY B O   
14539 N N   . VAL B 745  ? 0.1916 0.1804 0.1828 0.0113  0.0089  -0.0235 743  VAL B N   
14540 C CA  . VAL B 745  ? 0.1861 0.1746 0.1745 0.0114  0.0097  -0.0236 743  VAL B CA  
14541 C C   . VAL B 745  ? 0.2201 0.2051 0.2034 0.0105  0.0092  -0.0246 743  VAL B C   
14542 O O   . VAL B 745  ? 0.2136 0.1988 0.1944 0.0096  0.0085  -0.0246 743  VAL B O   
14543 C CB  . VAL B 745  ? 0.2007 0.1895 0.1902 0.0131  0.0119  -0.0234 743  VAL B CB  
14544 C CG1 . VAL B 745  ? 0.2111 0.1986 0.1967 0.0132  0.0129  -0.0236 743  VAL B CG1 
14545 C CG2 . VAL B 745  ? 0.2052 0.1976 0.1993 0.0133  0.0121  -0.0222 743  VAL B CG2 
14546 N N   . ARG B 746  ? 0.1982 0.1800 0.1799 0.0108  0.0092  -0.0256 744  ARG B N   
14547 C CA  . ARG B 746  ? 0.2084 0.1865 0.1852 0.0097  0.0084  -0.0266 744  ARG B CA  
14548 C C   . ARG B 746  ? 0.1991 0.1785 0.1753 0.0074  0.0063  -0.0263 744  ARG B C   
14549 O O   . ARG B 746  ? 0.2187 0.1970 0.1912 0.0063  0.0055  -0.0268 744  ARG B O   
14550 C CB  . ARG B 746  ? 0.2293 0.2036 0.2049 0.0101  0.0084  -0.0275 744  ARG B CB  
14551 C CG  . ARG B 746  ? 0.2464 0.2186 0.2216 0.0124  0.0105  -0.0281 744  ARG B CG  
14552 C CD  . ARG B 746  ? 0.2285 0.1964 0.2019 0.0126  0.0101  -0.0290 744  ARG B CD  
14553 N NE  . ARG B 746  ? 0.2734 0.2401 0.2477 0.0152  0.0121  -0.0294 744  ARG B NE  
14554 C CZ  . ARG B 746  ? 0.2409 0.2093 0.2195 0.0166  0.0126  -0.0287 744  ARG B CZ  
14555 N NH1 . ARG B 746  ? 0.2471 0.2176 0.2290 0.0157  0.0111  -0.0279 744  ARG B NH1 
14556 N NH2 . ARG B 746  ? 0.2574 0.2259 0.2373 0.0191  0.0146  -0.0289 744  ARG B NH2 
14557 N N   . ILE B 747  ? 0.1921 0.1741 0.1718 0.0068  0.0052  -0.0256 745  ILE B N   
14558 C CA  . ILE B 747  ? 0.1996 0.1833 0.1793 0.0047  0.0033  -0.0253 745  ILE B CA  
14559 C C   . ILE B 747  ? 0.2048 0.1917 0.1850 0.0045  0.0030  -0.0245 745  ILE B C   
14560 O O   . ILE B 747  ? 0.1871 0.1742 0.1650 0.0030  0.0017  -0.0246 745  ILE B O   
14561 C CB  . ILE B 747  ? 0.1967 0.1822 0.1799 0.0043  0.0026  -0.0247 745  ILE B CB  
14562 C CG1 . ILE B 747  ? 0.2110 0.1926 0.1925 0.0039  0.0023  -0.0254 745  ILE B CG1 
14563 C CG2 . ILE B 747  ? 0.1991 0.1877 0.1832 0.0026  0.0010  -0.0241 745  ILE B CG2 
14564 C CD1 . ILE B 747  ? 0.2356 0.2185 0.2203 0.0039  0.0020  -0.0248 745  ILE B CD1 
14565 N N   . LEU B 748  ? 0.1860 0.1752 0.1689 0.0059  0.0041  -0.0238 746  LEU B N   
14566 C CA  . LEU B 748  ? 0.1920 0.1838 0.1752 0.0058  0.0038  -0.0230 746  LEU B CA  
14567 C C   . LEU B 748  ? 0.1914 0.1811 0.1700 0.0057  0.0040  -0.0235 746  LEU B C   
14568 O O   . LEU B 748  ? 0.2036 0.1946 0.1809 0.0048  0.0028  -0.0231 746  LEU B O   
14569 C CB  . LEU B 748  ? 0.1948 0.1889 0.1815 0.0073  0.0050  -0.0221 746  LEU B CB  
14570 C CG  . LEU B 748  ? 0.2423 0.2392 0.2330 0.0071  0.0042  -0.0215 746  LEU B CG  
14571 C CD1 . LEU B 748  ? 0.2497 0.2478 0.2438 0.0085  0.0054  -0.0209 746  LEU B CD1 
14572 C CD2 . LEU B 748  ? 0.2656 0.2652 0.2566 0.0064  0.0028  -0.0208 746  LEU B CD2 
14573 N N   . ARG B 749  ? 0.2006 0.1872 0.1769 0.0066  0.0055  -0.0243 747  ARG B N   
14574 C CA  . ARG B 749  ? 0.2004 0.1846 0.1717 0.0065  0.0058  -0.0249 747  ARG B CA  
14575 C C   . ARG B 749  ? 0.1980 0.1801 0.1657 0.0046  0.0039  -0.0257 747  ARG B C   
14576 O O   . ARG B 749  ? 0.2065 0.1886 0.1711 0.0036  0.0029  -0.0257 747  ARG B O   
14577 C CB  . ARG B 749  ? 0.2104 0.1916 0.1799 0.0081  0.0080  -0.0257 747  ARG B CB  
14578 C CG  . ARG B 749  ? 0.2224 0.2058 0.1947 0.0097  0.0099  -0.0247 747  ARG B CG  
14579 C CD  . ARG B 749  ? 0.2507 0.2314 0.2208 0.0113  0.0122  -0.0255 747  ARG B CD  
14580 N NE  . ARG B 749  ? 0.2324 0.2153 0.2048 0.0126  0.0142  -0.0246 747  ARG B NE  
14581 C CZ  . ARG B 749  ? 0.3185 0.3000 0.2893 0.0140  0.0165  -0.0250 747  ARG B CZ  
14582 N NH1 . ARG B 749  ? 0.3359 0.3135 0.3025 0.0145  0.0171  -0.0264 747  ARG B NH1 
14583 N NH2 . ARG B 749  ? 0.3226 0.3065 0.2960 0.0149  0.0182  -0.0239 747  ARG B NH2 
14584 N N   . GLU B 750  ? 0.1985 0.1790 0.1665 0.0038  0.0032  -0.0263 748  GLU B N   
14585 C CA  . GLU B 750  ? 0.2091 0.1876 0.1739 0.0017  0.0013  -0.0270 748  GLU B CA  
14586 C C   . GLU B 750  ? 0.1925 0.1750 0.1588 0.0001  -0.0006 -0.0261 748  GLU B C   
14587 O O   . GLU B 750  ? 0.2258 0.2077 0.1890 -0.0016 -0.0022 -0.0264 748  GLU B O   
14588 C CB  . GLU B 750  ? 0.2313 0.2076 0.1967 0.0011  0.0010  -0.0276 748  GLU B CB  
14589 C CG  . GLU B 750  ? 0.2394 0.2132 0.2013 -0.0013 -0.0010 -0.0283 748  GLU B CG  
14590 C CD  . GLU B 750  ? 0.2676 0.2384 0.2296 -0.0018 -0.0012 -0.0288 748  GLU B CD  
14591 O OE1 . GLU B 750  ? 0.2802 0.2502 0.2441 0.0000  0.0003  -0.0288 748  GLU B OE1 
14592 O OE2 . GLU B 750  ? 0.3424 0.3116 0.3024 -0.0041 -0.0029 -0.0291 748  GLU B OE2 
14593 N N   . ALA B 751  ? 0.2046 0.1914 0.1758 0.0007  -0.0006 -0.0249 749  ALA B N   
14594 C CA  . ALA B 751  ? 0.2019 0.1929 0.1752 -0.0004 -0.0022 -0.0240 749  ALA B CA  
14595 C C   . ALA B 751  ? 0.2074 0.1999 0.1794 0.0000  -0.0024 -0.0234 749  ALA B C   
14596 O O   . ALA B 751  ? 0.2313 0.2273 0.2049 -0.0007 -0.0039 -0.0226 749  ALA B O   
14597 C CB  . ALA B 751  ? 0.1969 0.1913 0.1754 0.0004  -0.0018 -0.0231 749  ALA B CB  
14598 N N   . GLY B 752  ? 0.2060 0.1961 0.1753 0.0013  -0.0010 -0.0237 750  GLY B N   
14599 C CA  . GLY B 752  ? 0.2147 0.2057 0.1820 0.0015  -0.0013 -0.0231 750  GLY B CA  
14600 C C   . GLY B 752  ? 0.2219 0.2138 0.1908 0.0035  0.0006  -0.0223 750  GLY B C   
14601 O O   . GLY B 752  ? 0.2418 0.2341 0.2087 0.0038  0.0004  -0.0216 750  GLY B O   
14602 N N   . ILE B 753  ? 0.2157 0.2078 0.1879 0.0047  0.0021  -0.0221 751  ILE B N   
14603 C CA  . ILE B 753  ? 0.2250 0.2180 0.1987 0.0062  0.0038  -0.0213 751  ILE B CA  
14604 C C   . ILE B 753  ? 0.2331 0.2227 0.2026 0.0069  0.0055  -0.0219 751  ILE B C   
14605 O O   . ILE B 753  ? 0.2425 0.2295 0.2108 0.0072  0.0065  -0.0230 751  ILE B O   
14606 C CB  . ILE B 753  ? 0.1880 0.1823 0.1665 0.0072  0.0049  -0.0210 751  ILE B CB  
14607 C CG1 . ILE B 753  ? 0.2297 0.2269 0.2118 0.0066  0.0033  -0.0205 751  ILE B CG1 
14608 C CG2 . ILE B 753  ? 0.2207 0.2158 0.2007 0.0085  0.0065  -0.0200 751  ILE B CG2 
14609 C CD1 . ILE B 753  ? 0.2252 0.2253 0.2084 0.0066  0.0023  -0.0193 751  ILE B CD1 
14610 N N   . PRO B 754  ? 0.2253 0.2149 0.1925 0.0073  0.0060  -0.0213 752  PRO B N   
14611 C CA  . PRO B 754  ? 0.2338 0.2203 0.1966 0.0080  0.0078  -0.0219 752  PRO B CA  
14612 C C   . PRO B 754  ? 0.2449 0.2310 0.2100 0.0094  0.0104  -0.0220 752  PRO B C   
14613 O O   . PRO B 754  ? 0.2299 0.2185 0.1998 0.0100  0.0109  -0.0211 752  PRO B O   
14614 C CB  . PRO B 754  ? 0.2624 0.2496 0.2229 0.0080  0.0077  -0.0208 752  PRO B CB  
14615 C CG  . PRO B 754  ? 0.3020 0.2921 0.2648 0.0072  0.0054  -0.0198 752  PRO B CG  
14616 C CD  . PRO B 754  ? 0.2239 0.2159 0.1916 0.0071  0.0048  -0.0199 752  PRO B CD  
14617 N N   . ALA B 755  ? 0.2715 0.2545 0.2332 0.0101  0.0119  -0.0231 753  ALA B N   
14618 C CA  . ALA B 755  ? 0.2801 0.2631 0.2442 0.0116  0.0144  -0.0232 753  ALA B CA  
14619 C C   . ALA B 755  ? 0.2343 0.2198 0.2008 0.0124  0.0160  -0.0217 753  ALA B C   
14620 O O   . ALA B 755  ? 0.2744 0.2617 0.2455 0.0132  0.0172  -0.0212 753  ALA B O   
14621 C CB  . ALA B 755  ? 0.3235 0.3027 0.2830 0.0125  0.0161  -0.0247 753  ALA B CB  
14622 N N   . SER B 756  ? 0.2342 0.2199 0.1980 0.0120  0.0157  -0.0208 754  SER B N   
14623 C CA  . SER B 756  ? 0.2437 0.2314 0.2096 0.0125  0.0171  -0.0192 754  SER B CA  
14624 C C   . SER B 756  ? 0.2267 0.2173 0.1978 0.0121  0.0158  -0.0181 754  SER B C   
14625 O O   . SER B 756  ? 0.2473 0.2396 0.2214 0.0126  0.0170  -0.0168 754  SER B O   
14626 C CB  . SER B 756  ? 0.2989 0.2855 0.2599 0.0122  0.0172  -0.0186 754  SER B CB  
14627 O OG  . SER B 756  ? 0.3194 0.3063 0.2790 0.0111  0.0144  -0.0184 754  SER B OG  
14628 N N   . ALA B 757  ? 0.1993 0.1906 0.1715 0.0113  0.0134  -0.0184 755  ALA B N   
14629 C CA  . ALA B 757  ? 0.2010 0.1950 0.1779 0.0111  0.0122  -0.0175 755  ALA B CA  
14630 C C   . ALA B 757  ? 0.1984 0.1934 0.1798 0.0115  0.0126  -0.0179 755  ALA B C   
14631 O O   . ALA B 757  ? 0.2102 0.2072 0.1956 0.0115  0.0120  -0.0172 755  ALA B O   
14632 C CB  . ALA B 757  ? 0.2091 0.2038 0.1852 0.0102  0.0096  -0.0175 755  ALA B CB  
14633 N N   . LEU B 758  ? 0.2015 0.1949 0.1822 0.0119  0.0134  -0.0191 756  LEU B N   
14634 C CA  . LEU B 758  ? 0.1995 0.1937 0.1843 0.0122  0.0135  -0.0195 756  LEU B CA  
14635 C C   . LEU B 758  ? 0.1844 0.1770 0.1686 0.0133  0.0155  -0.0203 756  LEU B C   
14636 O O   . LEU B 758  ? 0.2279 0.2179 0.2088 0.0133  0.0155  -0.0215 756  LEU B O   
14637 C CB  . LEU B 758  ? 0.1875 0.1815 0.1725 0.0113  0.0114  -0.0202 756  LEU B CB  
14638 C CG  . LEU B 758  ? 0.1892 0.1836 0.1778 0.0117  0.0114  -0.0205 756  LEU B CG  
14639 C CD1 . LEU B 758  ? 0.2071 0.2042 0.2005 0.0121  0.0117  -0.0195 756  LEU B CD1 
14640 C CD2 . LEU B 758  ? 0.2117 0.2059 0.2000 0.0106  0.0095  -0.0211 756  LEU B CD2 
14641 N N   . GLN B 759  ? 0.1831 0.1773 0.1706 0.0142  0.0172  -0.0195 757  GLN B N   
14642 C CA  . GLN B 759  ? 0.1873 0.1807 0.1751 0.0154  0.0193  -0.0201 757  GLN B CA  
14643 C C   . GLN B 759  ? 0.1957 0.1908 0.1887 0.0159  0.0191  -0.0200 757  GLN B C   
14644 O O   . GLN B 759  ? 0.2110 0.2084 0.2077 0.0154  0.0183  -0.0190 757  GLN B O   
14645 C CB  . GLN B 759  ? 0.1904 0.1848 0.1779 0.0160  0.0216  -0.0192 757  GLN B CB  
14646 C CG  . GLN B 759  ? 0.1981 0.1905 0.1798 0.0157  0.0219  -0.0193 757  GLN B CG  
14647 C CD  . GLN B 759  ? 0.2112 0.2045 0.1925 0.0161  0.0241  -0.0182 757  GLN B CD  
14648 O OE1 . GLN B 759  ? 0.2433 0.2358 0.2228 0.0171  0.0264  -0.0186 757  GLN B OE1 
14649 N NE2 . GLN B 759  ? 0.2079 0.2029 0.1908 0.0153  0.0234  -0.0167 757  GLN B NE2 
14650 N N   . LEU B 760  ? 0.1825 0.1762 0.1754 0.0169  0.0198  -0.0210 758  LEU B N   
14651 C CA  . LEU B 760  ? 0.1805 0.1755 0.1779 0.0175  0.0196  -0.0209 758  LEU B CA  
14652 C C   . LEU B 760  ? 0.2055 0.2020 0.2055 0.0190  0.0219  -0.0206 758  LEU B C   
14653 O O   . LEU B 760  ? 0.2018 0.1968 0.1992 0.0201  0.0237  -0.0213 758  LEU B O   
14654 C CB  . LEU B 760  ? 0.2056 0.1979 0.2013 0.0177  0.0186  -0.0222 758  LEU B CB  
14655 C CG  . LEU B 760  ? 0.1941 0.1874 0.1940 0.0184  0.0181  -0.0221 758  LEU B CG  
14656 C CD1 . LEU B 760  ? 0.2189 0.2140 0.2215 0.0171  0.0161  -0.0214 758  LEU B CD1 
14657 C CD2 . LEU B 760  ? 0.2452 0.2351 0.2428 0.0192  0.0180  -0.0233 758  LEU B CD2 
14658 N N   . LEU B 761  ? 0.2075 0.2072 0.2126 0.0190  0.0220  -0.0195 759  LEU B N   
14659 C CA  . LEU B 761  ? 0.1843 0.1862 0.1928 0.0202  0.0241  -0.0189 759  LEU B CA  
14660 C C   . LEU B 761  ? 0.1855 0.1889 0.1986 0.0208  0.0233  -0.0189 759  LEU B C   
14661 O O   . LEU B 761  ? 0.2051 0.2111 0.2223 0.0201  0.0224  -0.0179 759  LEU B O   
14662 C CB  . LEU B 761  ? 0.2079 0.2125 0.2183 0.0195  0.0250  -0.0175 759  LEU B CB  
14663 C CG  . LEU B 761  ? 0.2272 0.2306 0.2332 0.0189  0.0260  -0.0172 759  LEU B CG  
14664 C CD1 . LEU B 761  ? 0.2536 0.2545 0.2550 0.0200  0.0276  -0.0183 759  LEU B CD1 
14665 C CD2 . LEU B 761  ? 0.2671 0.2694 0.2710 0.0175  0.0237  -0.0171 759  LEU B CD2 
14666 N N   . PRO B 762  ? 0.1886 0.1903 0.2011 0.0221  0.0234  -0.0199 760  PRO B N   
14667 C CA  . PRO B 762  ? 0.1836 0.1867 0.2004 0.0228  0.0225  -0.0197 760  PRO B CA  
14668 C C   . PRO B 762  ? 0.1862 0.1931 0.2079 0.0237  0.0242  -0.0187 760  PRO B C   
14669 O O   . PRO B 762  ? 0.1987 0.2065 0.2199 0.0244  0.0266  -0.0185 760  PRO B O   
14670 C CB  . PRO B 762  ? 0.1856 0.1854 0.1998 0.0242  0.0227  -0.0210 760  PRO B CB  
14671 C CG  . PRO B 762  ? 0.2104 0.2066 0.2185 0.0236  0.0227  -0.0219 760  PRO B CG  
14672 C CD  . PRO B 762  ? 0.1993 0.1972 0.2067 0.0230  0.0241  -0.0212 760  PRO B CD  
14673 N N   . GLY B 763  ? 0.1896 0.1988 0.2160 0.0236  0.0230  -0.0181 761  GLY B N   
14674 C CA  . GLY B 763  ? 0.1934 0.2066 0.2251 0.0244  0.0242  -0.0171 761  GLY B CA  
14675 C C   . GLY B 763  ? 0.1669 0.1826 0.2029 0.0231  0.0223  -0.0161 761  GLY B C   
14676 O O   . GLY B 763  ? 0.1919 0.2062 0.2268 0.0219  0.0201  -0.0163 761  GLY B O   
14677 N N   . ASP B 764  ? 0.2009 0.2206 0.2420 0.0234  0.0232  -0.0151 762  ASP B N   
14678 C CA  . ASP B 764  ? 0.2050 0.2271 0.2504 0.0222  0.0213  -0.0142 762  ASP B CA  
14679 C C   . ASP B 764  ? 0.2192 0.2423 0.2650 0.0201  0.0212  -0.0133 762  ASP B C   
14680 O O   . ASP B 764  ? 0.2060 0.2274 0.2480 0.0195  0.0221  -0.0134 762  ASP B O   
14681 C CB  . ASP B 764  ? 0.2474 0.2731 0.2983 0.0235  0.0217  -0.0136 762  ASP B CB  
14682 C CG  . ASP B 764  ? 0.2979 0.3273 0.3519 0.0239  0.0244  -0.0127 762  ASP B CG  
14683 O OD1 . ASP B 764  ? 0.2435 0.2729 0.2958 0.0228  0.0257  -0.0122 762  ASP B OD1 
14684 O OD2 . ASP B 764  ? 0.3750 0.4074 0.4333 0.0254  0.0251  -0.0123 762  ASP B OD2 
14685 N N   . GLY B 765  ? 0.2069 0.2327 0.2571 0.0190  0.0200  -0.0123 763  GLY B N   
14686 C CA  . GLY B 765  ? 0.2062 0.2324 0.2566 0.0170  0.0196  -0.0115 763  GLY B CA  
14687 C C   . GLY B 765  ? 0.2178 0.2454 0.2683 0.0167  0.0222  -0.0106 763  GLY B C   
14688 O O   . GLY B 765  ? 0.2230 0.2497 0.2718 0.0153  0.0221  -0.0100 763  GLY B O   
14689 N N   . ARG B 766  ? 0.2069 0.2368 0.2592 0.0182  0.0245  -0.0104 764  ARG B N   
14690 C CA  . ARG B 766  ? 0.2349 0.2662 0.2868 0.0180  0.0272  -0.0095 764  ARG B CA  
14691 C C   . ARG B 766  ? 0.1825 0.2101 0.2280 0.0181  0.0280  -0.0102 764  ARG B C   
14692 O O   . ARG B 766  ? 0.2039 0.2314 0.2478 0.0171  0.0292  -0.0094 764  ARG B O   
14693 C CB  . ARG B 766  ? 0.2298 0.2644 0.2848 0.0199  0.0296  -0.0093 764  ARG B CB  
14694 C CG  . ARG B 766  ? 0.2806 0.3196 0.3425 0.0198  0.0290  -0.0084 764  ARG B CG  
14695 C CD  . ARG B 766  ? 0.3630 0.4048 0.4275 0.0222  0.0312  -0.0086 764  ARG B CD  
14696 N NE  . ARG B 766  ? 0.4305 0.4690 0.4916 0.0244  0.0308  -0.0102 764  ARG B NE  
14697 C CZ  . ARG B 766  ? 0.5100 0.5495 0.5719 0.0269  0.0326  -0.0107 764  ARG B CZ  
14698 N NH1 . ARG B 766  ? 0.4942 0.5383 0.5606 0.0279  0.0350  -0.0098 764  ARG B NH1 
14699 N NH2 . ARG B 766  ? 0.5086 0.5441 0.5668 0.0286  0.0320  -0.0122 764  ARG B NH2 
14700 N N   . VAL B 767  ? 0.1778 0.2022 0.2195 0.0192  0.0272  -0.0117 765  VAL B N   
14701 C CA  . VAL B 767  ? 0.1872 0.2081 0.2229 0.0191  0.0275  -0.0124 765  VAL B CA  
14702 C C   . VAL B 767  ? 0.1884 0.2078 0.2226 0.0172  0.0256  -0.0119 765  VAL B C   
14703 O O   . VAL B 767  ? 0.2104 0.2286 0.2415 0.0165  0.0263  -0.0115 765  VAL B O   
14704 C CB  . VAL B 767  ? 0.1784 0.1962 0.2106 0.0205  0.0270  -0.0140 765  VAL B CB  
14705 C CG1 . VAL B 767  ? 0.2009 0.2153 0.2269 0.0202  0.0271  -0.0147 765  VAL B CG1 
14706 C CG2 . VAL B 767  ? 0.2141 0.2331 0.2477 0.0226  0.0290  -0.0144 765  VAL B CG2 
14707 N N   . GLY B 768  ? 0.1741 0.1936 0.2104 0.0165  0.0232  -0.0120 766  GLY B N   
14708 C CA  . GLY B 768  ? 0.1923 0.2106 0.2276 0.0149  0.0214  -0.0117 766  GLY B CA  
14709 C C   . GLY B 768  ? 0.1958 0.2155 0.2327 0.0137  0.0223  -0.0102 766  GLY B C   
14710 O O   . GLY B 768  ? 0.1922 0.2102 0.2261 0.0129  0.0222  -0.0097 766  GLY B O   
14711 N N   . ALA B 769  ? 0.2022 0.2251 0.2438 0.0135  0.0232  -0.0093 767  ALA B N   
14712 C CA  . ALA B 769  ? 0.1986 0.2230 0.2420 0.0120  0.0241  -0.0077 767  ALA B CA  
14713 C C   . ALA B 769  ? 0.2020 0.2257 0.2420 0.0122  0.0265  -0.0072 767  ALA B C   
14714 O O   . ALA B 769  ? 0.2000 0.2226 0.2385 0.0109  0.0266  -0.0061 767  ALA B O   
14715 C CB  . ALA B 769  ? 0.1901 0.2185 0.2396 0.0117  0.0246  -0.0068 767  ALA B CB  
14716 N N   . ALA B 770  ? 0.1911 0.2151 0.2295 0.0138  0.0284  -0.0078 768  ALA B N   
14717 C CA  . ALA B 770  ? 0.1890 0.2122 0.2236 0.0140  0.0308  -0.0074 768  ALA B CA  
14718 C C   . ALA B 770  ? 0.2024 0.2218 0.2315 0.0136  0.0296  -0.0078 768  ALA B C   
14719 O O   . ALA B 770  ? 0.2227 0.2412 0.2491 0.0128  0.0306  -0.0069 768  ALA B O   
14720 C CB  . ALA B 770  ? 0.2001 0.2237 0.2337 0.0161  0.0329  -0.0084 768  ALA B CB  
14721 N N   . LEU B 771  ? 0.1917 0.2089 0.2189 0.0140  0.0275  -0.0091 769  LEU B N   
14722 C CA  . LEU B 771  ? 0.2062 0.2204 0.2287 0.0135  0.0261  -0.0094 769  LEU B CA  
14723 C C   . LEU B 771  ? 0.1938 0.2076 0.2171 0.0120  0.0248  -0.0082 769  LEU B C   
14724 O O   . LEU B 771  ? 0.2186 0.2307 0.2385 0.0115  0.0249  -0.0076 769  LEU B O   
14725 C CB  . LEU B 771  ? 0.2027 0.2151 0.2237 0.0141  0.0241  -0.0110 769  LEU B CB  
14726 C CG  . LEU B 771  ? 0.1929 0.2044 0.2117 0.0156  0.0252  -0.0123 769  LEU B CG  
14727 C CD1 . LEU B 771  ? 0.2078 0.2179 0.2260 0.0158  0.0231  -0.0136 769  LEU B CD1 
14728 C CD2 . LEU B 771  ? 0.2078 0.2173 0.2212 0.0158  0.0265  -0.0125 769  LEU B CD2 
14729 N N   . VAL B 772  ? 0.1910 0.2061 0.2186 0.0113  0.0235  -0.0079 770  VAL B N   
14730 C CA  . VAL B 772  ? 0.1946 0.2090 0.2230 0.0099  0.0221  -0.0070 770  VAL B CA  
14731 C C   . VAL B 772  ? 0.2377 0.2524 0.2660 0.0089  0.0238  -0.0053 770  VAL B C   
14732 O O   . VAL B 772  ? 0.2487 0.2615 0.2748 0.0081  0.0231  -0.0044 770  VAL B O   
14733 C CB  . VAL B 772  ? 0.2017 0.2174 0.2346 0.0093  0.0205  -0.0071 770  VAL B CB  
14734 C CG1 . VAL B 772  ? 0.2234 0.2383 0.2575 0.0078  0.0194  -0.0059 770  VAL B CG1 
14735 C CG2 . VAL B 772  ? 0.2009 0.2155 0.2331 0.0101  0.0185  -0.0086 770  VAL B CG2 
14736 N N   . ALA B 773  ? 0.2193 0.2367 0.2500 0.0090  0.0260  -0.0046 771  ALA B N   
14737 C CA  . ALA B 773  ? 0.2325 0.2507 0.2635 0.0079  0.0279  -0.0028 771  ALA B CA  
14738 C C   . ALA B 773  ? 0.2664 0.2829 0.2922 0.0083  0.0296  -0.0025 771  ALA B C   
14739 O O   . ALA B 773  ? 0.2828 0.2993 0.3079 0.0073  0.0309  -0.0009 771  ALA B O   
14740 C CB  . ALA B 773  ? 0.2404 0.2626 0.2763 0.0078  0.0298  -0.0022 771  ALA B CB  
14741 N N   . ALA B 774  ? 0.2308 0.2457 0.2527 0.0097  0.0295  -0.0039 772  ALA B N   
14742 C CA  . ALA B 774  ? 0.2196 0.2330 0.2363 0.0102  0.0311  -0.0038 772  ALA B CA  
14743 C C   . ALA B 774  ? 0.2536 0.2645 0.2671 0.0091  0.0301  -0.0026 772  ALA B C   
14744 O O   . ALA B 774  ? 0.2593 0.2687 0.2730 0.0087  0.0276  -0.0027 772  ALA B O   
14745 C CB  . ALA B 774  ? 0.2602 0.2719 0.2733 0.0116  0.0306  -0.0057 772  ALA B CB  
14746 N N   . ALA B 775  ? 0.3001 0.3105 0.3104 0.0088  0.0321  -0.0014 773  ALA B N   
14747 C CA  . ALA B 775  ? 0.3175 0.3257 0.3252 0.0077  0.0315  0.0002  773  ALA B CA  
14748 C C   . ALA B 775  ? 0.2705 0.2757 0.2744 0.0082  0.0288  -0.0006 773  ALA B C   
14749 O O   . ALA B 775  ? 0.3015 0.3050 0.3052 0.0074  0.0272  0.0004  773  ALA B O   
14750 C CB  . ALA B 775  ? 0.3616 0.3696 0.3657 0.0075  0.0342  0.0014  773  ALA B CB  
14751 N N   . GLU B 776  ? 0.2706 0.2751 0.2717 0.0093  0.0284  -0.0022 774  GLU B N   
14752 C CA  . GLU B 776  ? 0.2484 0.2506 0.2458 0.0097  0.0261  -0.0028 774  GLU B CA  
14753 C C   . GLU B 776  ? 0.2114 0.2137 0.2114 0.0100  0.0236  -0.0040 774  GLU B C   
14754 O O   . GLU B 776  ? 0.2279 0.2289 0.2255 0.0103  0.0217  -0.0045 774  GLU B O   
14755 C CB  . GLU B 776  ? 0.2466 0.2477 0.2389 0.0106  0.0269  -0.0038 774  GLU B CB  
14756 C CG  . GLU B 776  ? 0.3429 0.3435 0.3316 0.0104  0.0294  -0.0027 774  GLU B CG  
14757 C CD  . GLU B 776  ? 0.4460 0.4487 0.4367 0.0108  0.0323  -0.0030 774  GLU B CD  
14758 O OE1 . GLU B 776  ? 0.3413 0.3459 0.3363 0.0113  0.0323  -0.0041 774  GLU B OE1 
14759 O OE2 . GLU B 776  ? 0.4510 0.4538 0.4391 0.0108  0.0348  -0.0021 774  GLU B OE2 
14760 N N   . THR B 777  ? 0.2120 0.2163 0.2168 0.0099  0.0236  -0.0045 775  THR B N   
14761 C CA  . THR B 777  ? 0.1986 0.2029 0.2057 0.0101  0.0213  -0.0055 775  THR B CA  
14762 C C   . THR B 777  ? 0.2103 0.2132 0.2174 0.0095  0.0195  -0.0047 775  THR B C   
14763 O O   . THR B 777  ? 0.2273 0.2300 0.2359 0.0087  0.0199  -0.0033 775  THR B O   
14764 C CB  . THR B 777  ? 0.2159 0.2225 0.2281 0.0100  0.0218  -0.0059 775  THR B CB  
14765 O OG1 . THR B 777  ? 0.2423 0.2500 0.2542 0.0109  0.0233  -0.0069 775  THR B OG1 
14766 C CG2 . THR B 777  ? 0.2084 0.2150 0.2229 0.0100  0.0194  -0.0069 775  THR B CG2 
14767 N N   . ALA B 778  ? 0.1794 0.1813 0.1847 0.0101  0.0175  -0.0055 776  ALA B N   
14768 C CA  . ALA B 778  ? 0.1958 0.1961 0.2005 0.0100  0.0157  -0.0047 776  ALA B CA  
14769 C C   . ALA B 778  ? 0.1888 0.1895 0.1964 0.0102  0.0139  -0.0056 776  ALA B C   
14770 O O   . ALA B 778  ? 0.2075 0.2069 0.2150 0.0103  0.0125  -0.0052 776  ALA B O   
14771 C CB  . ALA B 778  ? 0.2165 0.2157 0.2167 0.0106  0.0149  -0.0048 776  ALA B CB  
14772 N N   . GLY B 779  ? 0.1846 0.1869 0.1946 0.0103  0.0139  -0.0069 777  GLY B N   
14773 C CA  . GLY B 779  ? 0.1921 0.1947 0.2047 0.0104  0.0124  -0.0077 777  GLY B CA  
14774 C C   . GLY B 779  ? 0.1978 0.2021 0.2126 0.0105  0.0128  -0.0088 777  GLY B C   
14775 O O   . GLY B 779  ? 0.1866 0.1914 0.2002 0.0108  0.0140  -0.0093 777  GLY B O   
14776 N N   . VAL B 780  ? 0.1793 0.1841 0.1972 0.0104  0.0118  -0.0093 778  VAL B N   
14777 C CA  . VAL B 780  ? 0.1741 0.1804 0.1943 0.0105  0.0119  -0.0102 778  VAL B CA  
14778 C C   . VAL B 780  ? 0.1819 0.1881 0.2027 0.0108  0.0101  -0.0112 778  VAL B C   
14779 O O   . VAL B 780  ? 0.1809 0.1863 0.2023 0.0106  0.0089  -0.0110 778  VAL B O   
14780 C CB  . VAL B 780  ? 0.1692 0.1768 0.1931 0.0098  0.0128  -0.0096 778  VAL B CB  
14781 C CG1 . VAL B 780  ? 0.1975 0.2067 0.2238 0.0102  0.0128  -0.0105 778  VAL B CG1 
14782 C CG2 . VAL B 780  ? 0.1987 0.2067 0.2220 0.0096  0.0149  -0.0085 778  VAL B CG2 
14783 N N   . MET B 781  ? 0.1563 0.1631 0.1766 0.0112  0.0099  -0.0123 779  MET B N   
14784 C CA  . MET B 781  ? 0.1528 0.1597 0.1737 0.0114  0.0084  -0.0132 779  MET B CA  
14785 C C   . MET B 781  ? 0.1679 0.1759 0.1914 0.0114  0.0087  -0.0137 779  MET B C   
14786 O O   . MET B 781  ? 0.1759 0.1843 0.1990 0.0117  0.0097  -0.0140 779  MET B O   
14787 C CB  . MET B 781  ? 0.1597 0.1665 0.1779 0.0118  0.0079  -0.0140 779  MET B CB  
14788 C CG  . MET B 781  ? 0.1891 0.1952 0.2049 0.0119  0.0076  -0.0134 779  MET B CG  
14789 S SD  . MET B 781  ? 0.1863 0.1926 0.1991 0.0121  0.0069  -0.0141 779  MET B SD  
14790 C CE  . MET B 781  ? 0.1726 0.1798 0.1869 0.0122  0.0053  -0.0148 779  MET B CE  
14791 N N   . PHE B 782  ? 0.1635 0.1718 0.1895 0.0110  0.0078  -0.0136 780  PHE B N   
14792 C CA  . PHE B 782  ? 0.1733 0.1827 0.2021 0.0110  0.0078  -0.0138 780  PHE B CA  
14793 C C   . PHE B 782  ? 0.1580 0.1673 0.1872 0.0110  0.0062  -0.0146 780  PHE B C   
14794 O O   . PHE B 782  ? 0.1745 0.1830 0.2034 0.0108  0.0051  -0.0147 780  PHE B O   
14795 C CB  . PHE B 782  ? 0.1628 0.1731 0.1946 0.0103  0.0082  -0.0129 780  PHE B CB  
14796 C CG  . PHE B 782  ? 0.1576 0.1694 0.1927 0.0102  0.0078  -0.0131 780  PHE B CG  
14797 C CD1 . PHE B 782  ? 0.1749 0.1881 0.2112 0.0109  0.0090  -0.0131 780  PHE B CD1 
14798 C CD2 . PHE B 782  ? 0.1640 0.1756 0.2007 0.0097  0.0061  -0.0133 780  PHE B CD2 
14799 C CE1 . PHE B 782  ? 0.1738 0.1886 0.2132 0.0110  0.0086  -0.0131 780  PHE B CE1 
14800 C CE2 . PHE B 782  ? 0.1912 0.2044 0.2309 0.0097  0.0056  -0.0133 780  PHE B CE2 
14801 C CZ  . PHE B 782  ? 0.1719 0.1867 0.2130 0.0103  0.0068  -0.0132 780  PHE B CZ  
14802 N N   . THR B 783  ? 0.1561 0.1659 0.1857 0.0114  0.0061  -0.0152 781  THR B N   
14803 C CA  . THR B 783  ? 0.1683 0.1780 0.1986 0.0113  0.0046  -0.0158 781  THR B CA  
14804 C C   . THR B 783  ? 0.1711 0.1820 0.2041 0.0115  0.0047  -0.0157 781  THR B C   
14805 O O   . THR B 783  ? 0.1764 0.1876 0.2094 0.0121  0.0058  -0.0157 781  THR B O   
14806 C CB  . THR B 783  ? 0.1830 0.1921 0.2106 0.0116  0.0041  -0.0165 781  THR B CB  
14807 O OG1 . THR B 783  ? 0.1785 0.1870 0.2040 0.0115  0.0040  -0.0165 781  THR B OG1 
14808 C CG2 . THR B 783  ? 0.1778 0.1867 0.2058 0.0115  0.0026  -0.0170 781  THR B CG2 
14809 N N   . GLY B 784  ? 0.1651 0.1764 0.2003 0.0111  0.0035  -0.0155 782  GLY B N   
14810 C CA  . GLY B 784  ? 0.1656 0.1784 0.2039 0.0112  0.0035  -0.0152 782  GLY B CA  
14811 C C   . GLY B 784  ? 0.1772 0.1905 0.2178 0.0104  0.0021  -0.0149 782  GLY B C   
14812 O O   . GLY B 784  ? 0.1838 0.1958 0.2231 0.0098  0.0010  -0.0152 782  GLY B O   
14813 N N   . SER B 785  ? 0.2011 0.2164 0.2453 0.0103  0.0022  -0.0144 783  SER B N   
14814 C CA  . SER B 785  ? 0.2087 0.2245 0.2553 0.0093  0.0006  -0.0141 783  SER B CA  
14815 C C   . SER B 785  ? 0.2414 0.2567 0.2884 0.0081  0.0008  -0.0135 783  SER B C   
14816 O O   . SER B 785  ? 0.2127 0.2283 0.2595 0.0081  0.0024  -0.0130 783  SER B O   
14817 C CB  . SER B 785  ? 0.2104 0.2290 0.2612 0.0094  0.0006  -0.0135 783  SER B CB  
14818 O OG  . SER B 785  ? 0.2128 0.2333 0.2657 0.0095  0.0025  -0.0126 783  SER B OG  
14819 N N   . THR B 786  ? 0.2166 0.2309 0.2638 0.0071  -0.0009 -0.0137 784  THR B N   
14820 C CA  . THR B 786  ? 0.2206 0.2339 0.2681 0.0059  -0.0010 -0.0132 784  THR B CA  
14821 C C   . THR B 786  ? 0.2060 0.2217 0.2573 0.0051  0.0001  -0.0119 784  THR B C   
14822 O O   . THR B 786  ? 0.2364 0.2516 0.2875 0.0045  0.0012  -0.0112 784  THR B O   
14823 C CB  . THR B 786  ? 0.2170 0.2285 0.2641 0.0050  -0.0032 -0.0137 784  THR B CB  
14824 O OG1 . THR B 786  ? 0.2564 0.2661 0.3001 0.0059  -0.0040 -0.0148 784  THR B OG1 
14825 C CG2 . THR B 786  ? 0.2824 0.2920 0.3289 0.0039  -0.0034 -0.0133 784  THR B CG2 
14826 N N   . GLU B 787  ? 0.2429 0.2615 0.2977 0.0052  -0.0001 -0.0116 785  GLU B N   
14827 C CA  . GLU B 787  ? 0.2186 0.2402 0.2776 0.0045  0.0010  -0.0103 785  GLU B CA  
14828 C C   . GLU B 787  ? 0.2453 0.2676 0.3035 0.0052  0.0037  -0.0098 785  GLU B C   
14829 O O   . GLU B 787  ? 0.2283 0.2514 0.2879 0.0043  0.0049  -0.0088 785  GLU B O   
14830 C CB  . GLU B 787  ? 0.2955 0.3203 0.3584 0.0049  0.0004  -0.0101 785  GLU B CB  
14831 N N   . VAL B 788  ? 0.2003 0.2220 0.2560 0.0069  0.0046  -0.0106 786  VAL B N   
14832 C CA  . VAL B 788  ? 0.2049 0.2269 0.2593 0.0076  0.0070  -0.0102 786  VAL B CA  
14833 C C   . VAL B 788  ? 0.1809 0.2003 0.2320 0.0070  0.0074  -0.0101 786  VAL B C   
14834 O O   . VAL B 788  ? 0.2011 0.2208 0.2520 0.0067  0.0091  -0.0092 786  VAL B O   
14835 C CB  . VAL B 788  ? 0.1854 0.2070 0.2377 0.0094  0.0077  -0.0111 786  VAL B CB  
14836 C CG1 . VAL B 788  ? 0.2059 0.2268 0.2555 0.0101  0.0099  -0.0110 786  VAL B CG1 
14837 C CG2 . VAL B 788  ? 0.2187 0.2431 0.2746 0.0103  0.0077  -0.0110 786  VAL B CG2 
14838 N N   . ALA B 789  ? 0.1791 0.1958 0.2274 0.0069  0.0058  -0.0109 787  ALA B N   
14839 C CA  . ALA B 789  ? 0.1731 0.1874 0.2184 0.0065  0.0060  -0.0107 787  ALA B CA  
14840 C C   . ALA B 789  ? 0.1798 0.1940 0.2269 0.0050  0.0062  -0.0095 787  ALA B C   
14841 O O   . ALA B 789  ? 0.2042 0.2174 0.2496 0.0048  0.0074  -0.0088 787  ALA B O   
14842 C CB  . ALA B 789  ? 0.1816 0.1934 0.2243 0.0067  0.0041  -0.0117 787  ALA B CB  
14843 N N   . ARG B 790  ? 0.1903 0.2057 0.2408 0.0038  0.0051  -0.0091 788  ARG B N   
14844 C CA  . ARG B 790  ? 0.2108 0.2260 0.2630 0.0021  0.0052  -0.0079 788  ARG B CA  
14845 C C   . ARG B 790  ? 0.2262 0.2440 0.2802 0.0019  0.0077  -0.0066 788  ARG B C   
14846 O O   . ARG B 790  ? 0.2348 0.2517 0.2883 0.0008  0.0085  -0.0055 788  ARG B O   
14847 C CB  . ARG B 790  ? 0.2669 0.2835 0.3229 0.0007  0.0035  -0.0077 788  ARG B CB  
14848 C CG  . ARG B 790  ? 0.2888 0.3025 0.3430 0.0004  0.0011  -0.0088 788  ARG B CG  
14849 C CD  . ARG B 790  ? 0.3456 0.3604 0.4034 -0.0014 -0.0006 -0.0084 788  ARG B CD  
14850 N NE  . ARG B 790  ? 0.4626 0.4748 0.5184 -0.0014 -0.0029 -0.0097 788  ARG B NE  
14851 C CZ  . ARG B 790  ? 0.4487 0.4569 0.5013 -0.0018 -0.0040 -0.0102 788  ARG B CZ  
14852 N NH1 . ARG B 790  ? 0.3990 0.4052 0.4504 -0.0024 -0.0031 -0.0094 788  ARG B NH1 
14853 N NH2 . ARG B 790  ? 0.5150 0.5211 0.5656 -0.0015 -0.0059 -0.0115 788  ARG B NH2 
14854 N N   . LEU B 791  ? 0.2075 0.2283 0.2633 0.0030  0.0089  -0.0067 789  LEU B N   
14855 C CA  . LEU B 791  ? 0.2332 0.2565 0.2905 0.0031  0.0115  -0.0057 789  LEU B CA  
14856 C C   . LEU B 791  ? 0.2370 0.2580 0.2898 0.0037  0.0129  -0.0056 789  LEU B C   
14857 O O   . LEU B 791  ? 0.2406 0.2620 0.2933 0.0030  0.0146  -0.0044 789  LEU B O   
14858 C CB  . LEU B 791  ? 0.2496 0.2761 0.3093 0.0045  0.0124  -0.0060 789  LEU B CB  
14859 C CG  . LEU B 791  ? 0.2569 0.2862 0.3213 0.0041  0.0110  -0.0059 789  LEU B CG  
14860 C CD1 . LEU B 791  ? 0.2605 0.2927 0.3269 0.0059  0.0121  -0.0063 789  LEU B CD1 
14861 C CD2 . LEU B 791  ? 0.2698 0.3014 0.3383 0.0019  0.0111  -0.0044 789  LEU B CD2 
14862 N N   . ILE B 792  ? 0.2285 0.2473 0.2775 0.0051  0.0123  -0.0068 790  ILE B N   
14863 C CA  . ILE B 792  ? 0.2121 0.2288 0.2568 0.0057  0.0134  -0.0068 790  ILE B CA  
14864 C C   . ILE B 792  ? 0.1920 0.2061 0.2350 0.0045  0.0128  -0.0060 790  ILE B C   
14865 O O   . ILE B 792  ? 0.2295 0.2428 0.2705 0.0043  0.0142  -0.0051 790  ILE B O   
14866 C CB  . ILE B 792  ? 0.1985 0.2137 0.2401 0.0071  0.0125  -0.0083 790  ILE B CB  
14867 C CG1 . ILE B 792  ? 0.1896 0.2068 0.2322 0.0084  0.0134  -0.0090 790  ILE B CG1 
14868 C CG2 . ILE B 792  ? 0.1953 0.2081 0.2324 0.0075  0.0128  -0.0084 790  ILE B CG2 
14869 C CD1 . ILE B 792  ? 0.2160 0.2319 0.2563 0.0094  0.0123  -0.0104 790  ILE B CD1 
14870 N N   . GLN B 793  ? 0.2079 0.2203 0.2512 0.0038  0.0106  -0.0064 791  GLN B N   
14871 C CA  . GLN B 793  ? 0.2168 0.2262 0.2585 0.0028  0.0099  -0.0057 791  GLN B CA  
14872 C C   . GLN B 793  ? 0.1891 0.1993 0.2328 0.0012  0.0112  -0.0039 791  GLN B C   
14873 O O   . GLN B 793  ? 0.2310 0.2391 0.2724 0.0007  0.0117  -0.0029 791  GLN B O   
14874 C CB  . GLN B 793  ? 0.2204 0.2282 0.2628 0.0023  0.0075  -0.0065 791  GLN B CB  
14875 C CG  . GLN B 793  ? 0.2472 0.2515 0.2880 0.0014  0.0065  -0.0059 791  GLN B CG  
14876 C CD  . GLN B 793  ? 0.2883 0.2913 0.3305 0.0004  0.0044  -0.0065 791  GLN B CD  
14877 O OE1 . GLN B 793  ? 0.2996 0.3049 0.3453 -0.0005 0.0039  -0.0065 791  GLN B OE1 
14878 N NE2 . GLN B 793  ? 0.3410 0.3403 0.3804 0.0008  0.0030  -0.0071 791  GLN B NE2 
14879 N N   . ALA B 794  ? 0.2182 0.2317 0.2664 0.0003  0.0116  -0.0034 792  ALA B N   
14880 C CA  . ALA B 794  ? 0.2311 0.2460 0.2817 -0.0015 0.0129  -0.0017 792  ALA B CA  
14881 C C   . ALA B 794  ? 0.2498 0.2656 0.2985 -0.0008 0.0156  -0.0008 792  ALA B C   
14882 O O   . ALA B 794  ? 0.2695 0.2843 0.3173 -0.0020 0.0167  0.0007  792  ALA B O   
14883 C CB  . ALA B 794  ? 0.2583 0.2772 0.3144 -0.0024 0.0128  -0.0014 792  ALA B CB  
14884 N N   . GLN B 795  ? 0.2383 0.2559 0.2863 0.0010  0.0168  -0.0017 793  GLN B N   
14885 C CA  . GLN B 795  ? 0.2475 0.2656 0.2931 0.0017  0.0193  -0.0011 793  GLN B CA  
14886 C C   . GLN B 795  ? 0.2283 0.2425 0.2689 0.0017  0.0191  -0.0008 793  GLN B C   
14887 O O   . GLN B 795  ? 0.2397 0.2535 0.2787 0.0011  0.0208  0.0006  793  GLN B O   
14888 C CB  . GLN B 795  ? 0.2792 0.2986 0.3237 0.0038  0.0201  -0.0025 793  GLN B CB  
14889 C CG  . GLN B 795  ? 0.3204 0.3437 0.3691 0.0044  0.0211  -0.0027 793  GLN B CG  
14890 C CD  . GLN B 795  ? 0.3114 0.3349 0.3581 0.0065  0.0218  -0.0041 793  GLN B CD  
14891 O OE1 . GLN B 795  ? 0.3352 0.3575 0.3810 0.0074  0.0201  -0.0055 793  GLN B OE1 
14892 N NE2 . GLN B 795  ? 0.3032 0.3279 0.3489 0.0073  0.0244  -0.0038 793  GLN B NE2 
14893 N N   . LEU B 796  ? 0.2184 0.2298 0.2564 0.0025  0.0171  -0.0019 794  LEU B N   
14894 C CA  . LEU B 796  ? 0.2407 0.2489 0.2741 0.0029  0.0167  -0.0017 794  LEU B CA  
14895 C C   . LEU B 796  ? 0.2603 0.2660 0.2933 0.0014  0.0162  -0.0002 794  LEU B C   
14896 O O   . LEU B 796  ? 0.2787 0.2822 0.3083 0.0014  0.0167  0.0007  794  LEU B O   
14897 C CB  . LEU B 796  ? 0.2332 0.2396 0.2645 0.0042  0.0147  -0.0033 794  LEU B CB  
14898 C CG  . LEU B 796  ? 0.2335 0.2414 0.2639 0.0057  0.0151  -0.0047 794  LEU B CG  
14899 C CD1 . LEU B 796  ? 0.2279 0.2342 0.2565 0.0066  0.0131  -0.0060 794  LEU B CD1 
14900 C CD2 . LEU B 796  ? 0.2283 0.2360 0.2552 0.0064  0.0169  -0.0042 794  LEU B CD2 
14901 N N   . ALA B 797  ? 0.2713 0.2770 0.3076 0.0000  0.0150  0.0000  795  ALA B N   
14902 C CA  . ALA B 797  ? 0.3088 0.3115 0.3447 -0.0016 0.0143  0.0013  795  ALA B CA  
14903 C C   . ALA B 797  ? 0.2729 0.2764 0.3091 -0.0031 0.0164  0.0034  795  ALA B C   
14904 O O   . ALA B 797  ? 0.3443 0.3448 0.3790 -0.0042 0.0161  0.0047  795  ALA B O   
14905 C CB  . ALA B 797  ? 0.3165 0.3191 0.3558 -0.0029 0.0124  0.0009  795  ALA B CB  
14906 N N   . ASP B 798  ? 0.2822 0.2895 0.3201 -0.0029 0.0186  0.0037  796  ASP B N   
14907 C CA  . ASP B 798  ? 0.3760 0.3843 0.4137 -0.0041 0.0210  0.0056  796  ASP B CA  
14908 C C   . ASP B 798  ? 0.3763 0.3823 0.4086 -0.0030 0.0220  0.0060  796  ASP B C   
14909 O O   . ASP B 798  ? 0.3872 0.3930 0.4182 -0.0039 0.0239  0.0078  796  ASP B O   
14910 C CB  . ASP B 798  ? 0.3391 0.3525 0.3805 -0.0040 0.0232  0.0057  796  ASP B CB  
14911 C CG  . ASP B 798  ? 0.5187 0.5350 0.5661 -0.0054 0.0224  0.0059  796  ASP B CG  
14912 O OD1 . ASP B 798  ? 0.5692 0.5837 0.6178 -0.0074 0.0210  0.0067  796  ASP B OD1 
14913 O OD2 . ASP B 798  ? 0.5811 0.6014 0.6318 -0.0046 0.0232  0.0051  796  ASP B OD2 
14914 N N   . ARG B 799  ? 0.3296 0.3337 0.3586 -0.0011 0.0208  0.0046  797  ARG B N   
14915 C CA  A ARG B 799  ? 0.3565 0.3592 0.3806 0.0002  0.0216  0.0047  797  ARG B CA  
14916 C CA  B ARG B 799  ? 0.3566 0.3593 0.3807 0.0001  0.0216  0.0047  797  ARG B CA  
14917 C C   . ARG B 799  ? 0.3244 0.3229 0.3449 0.0007  0.0195  0.0047  797  ARG B C   
14918 O O   . ARG B 799  ? 0.3033 0.3003 0.3250 0.0007  0.0174  0.0039  797  ARG B O   
14919 C CB  A ARG B 799  ? 0.3772 0.3820 0.4006 0.0020  0.0220  0.0028  797  ARG B CB  
14920 C CB  B ARG B 799  ? 0.3787 0.3836 0.4021 0.0019  0.0222  0.0030  797  ARG B CB  
14921 C CG  A ARG B 799  ? 0.3881 0.3970 0.4155 0.0021  0.0236  0.0024  797  ARG B CG  
14922 C CG  B ARG B 799  ? 0.3886 0.3976 0.4161 0.0018  0.0239  0.0026  797  ARG B CG  
14923 C CD  A ARG B 799  ? 0.3614 0.3714 0.3874 0.0040  0.0240  0.0006  797  ARG B CD  
14924 C CD  B ARG B 799  ? 0.3740 0.3844 0.3991 0.0030  0.0262  0.0024  797  ARG B CD  
14925 N NE  A ARG B 799  ? 0.4202 0.4281 0.4407 0.0049  0.0244  0.0005  797  ARG B NE  
14926 N NE  B ARG B 799  ? 0.4228 0.4307 0.4429 0.0043  0.0253  0.0015  797  ARG B NE  
14927 C CZ  A ARG B 799  ? 0.3641 0.3707 0.3818 0.0061  0.0230  -0.0009 797  ARG B CZ  
14928 C CZ  B ARG B 799  ? 0.4088 0.4168 0.4280 0.0058  0.0244  -0.0003 797  ARG B CZ  
14929 N NH1 A ARG B 799  ? 0.3032 0.3103 0.3227 0.0068  0.0215  -0.0024 797  ARG B NH1 
14930 N NH1 B ARG B 799  ? 0.3454 0.3557 0.3680 0.0063  0.0244  -0.0015 797  ARG B NH1 
14931 N NH2 A ARG B 799  ? 0.3494 0.3541 0.3623 0.0067  0.0232  -0.0006 797  ARG B NH2 
14932 N NH2 B ARG B 799  ? 0.3740 0.3797 0.3889 0.0066  0.0233  -0.0009 797  ARG B NH2 
14933 N N   . LEU B 800  ? 0.2929 0.2896 0.3089 0.0012  0.0202  0.0055  798  LEU B N   
14934 C CA  . LEU B 800  ? 0.3136 0.3069 0.3260 0.0022  0.0183  0.0054  798  LEU B CA  
14935 C C   . LEU B 800  ? 0.2997 0.2932 0.3080 0.0037  0.0189  0.0049  798  LEU B C   
14936 O O   . LEU B 800  ? 0.3410 0.3363 0.3484 0.0036  0.0210  0.0052  798  LEU B O   
14937 C CB  . LEU B 800  ? 0.3500 0.3398 0.3604 0.0010  0.0182  0.0076  798  LEU B CB  
14938 C CG  . LEU B 800  ? 0.3528 0.3409 0.3662 -0.0006 0.0172  0.0082  798  LEU B CG  
14939 C CD1 . LEU B 800  ? 0.4135 0.3978 0.4242 -0.0017 0.0173  0.0105  798  LEU B CD1 
14940 C CD2 . LEU B 800  ? 0.3028 0.2895 0.3170 0.0004  0.0146  0.0066  798  LEU B CD2 
14941 N N   . SER B 801  ? 0.3029 0.2948 0.3089 0.0050  0.0169  0.0041  799  SER B N   
14942 C CA  . SER B 801  ? 0.3328 0.3245 0.3346 0.0062  0.0170  0.0038  799  SER B CA  
14943 C C   . SER B 801  ? 0.3767 0.3664 0.3747 0.0056  0.0181  0.0059  799  SER B C   
14944 O O   . SER B 801  ? 0.3686 0.3566 0.3672 0.0045  0.0183  0.0075  799  SER B O   
14945 C CB  . SER B 801  ? 0.3551 0.3457 0.3557 0.0076  0.0146  0.0029  799  SER B CB  
14946 O OG  . SER B 801  ? 0.3547 0.3421 0.3539 0.0076  0.0134  0.0042  799  SER B OG  
14947 N N   . PRO B 802  ? 0.4112 0.4010 0.4052 0.0064  0.0187  0.0059  800  PRO B N   
14948 C CA  . PRO B 802  ? 0.4364 0.4240 0.4262 0.0060  0.0194  0.0079  800  PRO B CA  
14949 C C   . PRO B 802  ? 0.4560 0.4401 0.4443 0.0062  0.0173  0.0091  800  PRO B C   
14950 O O   . PRO B 802  ? 0.4990 0.4808 0.4851 0.0054  0.0179  0.0112  800  PRO B O   
14951 C CB  . PRO B 802  ? 0.3895 0.3776 0.3750 0.0070  0.0197  0.0071  800  PRO B CB  
14952 C CG  . PRO B 802  ? 0.4465 0.4377 0.4347 0.0074  0.0204  0.0051  800  PRO B CG  
14953 C CD  . PRO B 802  ? 0.3768 0.3686 0.3697 0.0074  0.0189  0.0041  800  PRO B CD  
14954 N N   . ALA B 803  ? 0.4466 0.4304 0.4362 0.0073  0.0150  0.0079  801  ALA B N   
14955 C CA  . ALA B 803  ? 0.4233 0.4040 0.4123 0.0078  0.0130  0.0088  801  ALA B CA  
14956 C C   . ALA B 803  ? 0.4489 0.4279 0.4411 0.0066  0.0130  0.0094  801  ALA B C   
14957 O O   . ALA B 803  ? 0.4868 0.4625 0.4782 0.0069  0.0115  0.0102  801  ALA B O   
14958 C CB  . ALA B 803  ? 0.4589 0.4402 0.4483 0.0096  0.0108  0.0072  801  ALA B CB  
14959 N N   . GLY B 804  ? 0.4177 0.3988 0.4132 0.0052  0.0146  0.0091  802  GLY B N   
14960 C CA  . GLY B 804  ? 0.3793 0.3590 0.3779 0.0037  0.0145  0.0098  802  GLY B CA  
14961 C C   . GLY B 804  ? 0.3718 0.3514 0.3735 0.0042  0.0126  0.0082  802  GLY B C   
14962 O O   . GLY B 804  ? 0.3926 0.3693 0.3952 0.0035  0.0116  0.0087  802  GLY B O   
14963 N N   . ARG B 805  ? 0.3612 0.3436 0.3642 0.0054  0.0121  0.0061  803  ARG B N   
14964 C CA  . ARG B 805  ? 0.3126 0.2950 0.3181 0.0061  0.0104  0.0045  803  ARG B CA  
14965 C C   . ARG B 805  ? 0.2975 0.2836 0.3065 0.0057  0.0112  0.0030  803  ARG B C   
14966 O O   . ARG B 805  ? 0.2998 0.2885 0.3089 0.0055  0.0128  0.0029  803  ARG B O   
14967 C CB  . ARG B 805  ? 0.3690 0.3509 0.3723 0.0083  0.0088  0.0035  803  ARG B CB  
14968 C CG  . ARG B 805  ? 0.3786 0.3570 0.3786 0.0090  0.0078  0.0050  803  ARG B CG  
14969 C CD  . ARG B 805  ? 0.4521 0.4267 0.4529 0.0084  0.0069  0.0057  803  ARG B CD  
14970 N NE  . ARG B 805  ? 0.5169 0.4875 0.5143 0.0094  0.0058  0.0071  803  ARG B NE  
14971 C CZ  . ARG B 805  ? 0.4354 0.4033 0.4308 0.0082  0.0065  0.0092  803  ARG B CZ  
14972 N NH1 . ARG B 805  ? 0.4440 0.4125 0.4404 0.0060  0.0083  0.0102  803  ARG B NH1 
14973 N NH2 . ARG B 805  ? 0.5028 0.4671 0.4949 0.0094  0.0053  0.0105  803  ARG B NH2 
14974 N N   . PRO B 806  ? 0.2631 0.2492 0.2750 0.0056  0.0100  0.0019  804  PRO B N   
14975 C CA  . PRO B 806  ? 0.2622 0.2516 0.2774 0.0052  0.0104  0.0005  804  PRO B CA  
14976 C C   . PRO B 806  ? 0.2296 0.2216 0.2439 0.0066  0.0107  -0.0008 804  PRO B C   
14977 O O   . PRO B 806  ? 0.2555 0.2467 0.2674 0.0080  0.0097  -0.0014 804  PRO B O   
14978 C CB  . PRO B 806  ? 0.2656 0.2537 0.2828 0.0052  0.0086  -0.0005 804  PRO B CB  
14979 C CG  . PRO B 806  ? 0.3094 0.2934 0.3252 0.0047  0.0078  0.0008  804  PRO B CG  
14980 C CD  . PRO B 806  ? 0.3026 0.2853 0.3145 0.0058  0.0081  0.0017  804  PRO B CD  
14981 N N   . ILE B 807  ? 0.2285 0.2235 0.2448 0.0062  0.0120  -0.0013 805  ILE B N   
14982 C CA  . ILE B 807  ? 0.2149 0.2120 0.2305 0.0073  0.0123  -0.0027 805  ILE B CA  
14983 C C   . ILE B 807  ? 0.2248 0.2224 0.2422 0.0080  0.0106  -0.0043 805  ILE B C   
14984 O O   . ILE B 807  ? 0.2249 0.2231 0.2454 0.0072  0.0103  -0.0046 805  ILE B O   
14985 C CB  . ILE B 807  ? 0.1986 0.1985 0.2160 0.0068  0.0143  -0.0027 805  ILE B CB  
14986 C CG1 . ILE B 807  ? 0.2769 0.2765 0.2928 0.0061  0.0162  -0.0011 805  ILE B CG1 
14987 C CG2 . ILE B 807  ? 0.2223 0.2238 0.2388 0.0080  0.0144  -0.0042 805  ILE B CG2 
14988 C CD1 . ILE B 807  ? 0.3186 0.3169 0.3297 0.0069  0.0164  -0.0008 805  ILE B CD1 
14989 N N   . PRO B 808  ? 0.1889 0.1864 0.2044 0.0092  0.0095  -0.0053 806  PRO B N   
14990 C CA  . PRO B 808  ? 0.2099 0.2078 0.2268 0.0098  0.0081  -0.0067 806  PRO B CA  
14991 C C   . PRO B 808  ? 0.2189 0.2192 0.2382 0.0095  0.0085  -0.0077 806  PRO B C   
14992 O O   . PRO B 808  ? 0.1970 0.1988 0.2158 0.0096  0.0097  -0.0079 806  PRO B O   
14993 C CB  . PRO B 808  ? 0.2192 0.2171 0.2334 0.0111  0.0072  -0.0072 806  PRO B CB  
14994 C CG  . PRO B 808  ? 0.2736 0.2700 0.2851 0.0112  0.0076  -0.0059 806  PRO B CG  
14995 C CD  . PRO B 808  ? 0.2132 0.2100 0.2250 0.0101  0.0094  -0.0049 806  PRO B CD  
14996 N N   . LEU B 809  ? 0.1828 0.1831 0.2044 0.0093  0.0075  -0.0084 807  LEU B N   
14997 C CA  . LEU B 809  ? 0.1922 0.1946 0.2161 0.0092  0.0076  -0.0094 807  LEU B CA  
14998 C C   . LEU B 809  ? 0.1718 0.1739 0.1956 0.0099  0.0060  -0.0106 807  LEU B C   
14999 O O   . LEU B 809  ? 0.2107 0.2112 0.2347 0.0098  0.0048  -0.0107 807  LEU B O   
15000 C CB  . LEU B 809  ? 0.1926 0.1955 0.2198 0.0080  0.0079  -0.0088 807  LEU B CB  
15001 C CG  . LEU B 809  ? 0.1978 0.2027 0.2277 0.0079  0.0075  -0.0097 807  LEU B CG  
15002 C CD1 . LEU B 809  ? 0.2104 0.2172 0.2401 0.0086  0.0087  -0.0101 807  LEU B CD1 
15003 C CD2 . LEU B 809  ? 0.2214 0.2269 0.2547 0.0066  0.0075  -0.0090 807  LEU B CD2 
15004 N N   . ILE B 810  ? 0.1682 0.1718 0.1915 0.0105  0.0059  -0.0116 808  ILE B N   
15005 C CA  . ILE B 810  ? 0.1820 0.1858 0.2056 0.0109  0.0047  -0.0127 808  ILE B CA  
15006 C C   . ILE B 810  ? 0.1813 0.1864 0.2074 0.0104  0.0049  -0.0131 808  ILE B C   
15007 O O   . ILE B 810  ? 0.1973 0.2036 0.2237 0.0104  0.0059  -0.0130 808  ILE B O   
15008 C CB  . ILE B 810  ? 0.1861 0.1906 0.2076 0.0117  0.0044  -0.0134 808  ILE B CB  
15009 C CG1 . ILE B 810  ? 0.1846 0.1883 0.2039 0.0122  0.0043  -0.0129 808  ILE B CG1 
15010 C CG2 . ILE B 810  ? 0.2212 0.2261 0.2431 0.0120  0.0033  -0.0145 808  ILE B CG2 
15011 C CD1 . ILE B 810  ? 0.2274 0.2322 0.2449 0.0129  0.0038  -0.0135 808  ILE B CD1 
15012 N N   . ALA B 811  ? 0.1741 0.1788 0.2020 0.0099  0.0038  -0.0133 809  ALA B N   
15013 C CA  . ALA B 811  ? 0.1812 0.1872 0.2116 0.0095  0.0037  -0.0135 809  ALA B CA  
15014 C C   . ALA B 811  ? 0.2059 0.2117 0.2363 0.0097  0.0022  -0.0146 809  ALA B C   
15015 O O   . ALA B 811  ? 0.2075 0.2119 0.2379 0.0094  0.0011  -0.0148 809  ALA B O   
15016 C CB  . ALA B 811  ? 0.1953 0.2014 0.2283 0.0084  0.0039  -0.0126 809  ALA B CB  
15017 N N   . GLU B 812  ? 0.1717 0.1785 0.2015 0.0102  0.0023  -0.0152 810  GLU B N   
15018 C CA  . GLU B 812  ? 0.1701 0.1768 0.1994 0.0104  0.0011  -0.0161 810  GLU B CA  
15019 C C   . GLU B 812  ? 0.1901 0.1978 0.2216 0.0101  0.0007  -0.0162 810  GLU B C   
15020 O O   . GLU B 812  ? 0.2011 0.2099 0.2333 0.0103  0.0015  -0.0160 810  GLU B O   
15021 C CB  . GLU B 812  ? 0.2012 0.2082 0.2282 0.0111  0.0013  -0.0166 810  GLU B CB  
15022 C CG  . GLU B 812  ? 0.2180 0.2243 0.2431 0.0115  0.0015  -0.0164 810  GLU B CG  
15023 C CD  . GLU B 812  ? 0.2598 0.2647 0.2845 0.0116  0.0005  -0.0166 810  GLU B CD  
15024 O OE1 . GLU B 812  ? 0.2331 0.2381 0.2570 0.0120  -0.0002 -0.0174 810  GLU B OE1 
15025 O OE2 . GLU B 812  ? 0.2372 0.2409 0.2624 0.0114  0.0006  -0.0161 810  GLU B OE2 
15026 N N   . THR B 813  ? 0.1828 0.1900 0.2154 0.0096  -0.0005 -0.0163 811  THR B N   
15027 C CA  . THR B 813  ? 0.1678 0.1761 0.2032 0.0091  -0.0010 -0.0161 811  THR B CA  
15028 C C   . THR B 813  ? 0.1792 0.1873 0.2143 0.0091  -0.0025 -0.0168 811  THR B C   
15029 O O   . THR B 813  ? 0.1962 0.2038 0.2289 0.0096  -0.0027 -0.0174 811  THR B O   
15030 C CB  . THR B 813  ? 0.1991 0.2074 0.2368 0.0081  -0.0010 -0.0153 811  THR B CB  
15031 O OG1 . THR B 813  ? 0.2093 0.2155 0.2456 0.0077  -0.0020 -0.0156 811  THR B OG1 
15032 C CG2 . THR B 813  ? 0.2067 0.2158 0.2449 0.0081  0.0008  -0.0144 811  THR B CG2 
15033 N N   . GLY B 814  ? 0.1977 0.2065 0.2352 0.0085  -0.0036 -0.0166 812  GLY B N   
15034 C CA  . GLY B 814  ? 0.2074 0.2161 0.2446 0.0086  -0.0049 -0.0170 812  GLY B CA  
15035 C C   . GLY B 814  ? 0.2061 0.2129 0.2408 0.0084  -0.0063 -0.0179 812  GLY B C   
15036 O O   . GLY B 814  ? 0.2270 0.2323 0.2602 0.0083  -0.0062 -0.0181 812  GLY B O   
15037 N N   . GLY B 815  ? 0.2056 0.2124 0.2398 0.0084  -0.0075 -0.0182 813  GLY B N   
15038 C CA  . GLY B 815  ? 0.2167 0.2217 0.2483 0.0083  -0.0087 -0.0191 813  GLY B CA  
15039 C C   . GLY B 815  ? 0.2022 0.2072 0.2347 0.0077  -0.0106 -0.0191 813  GLY B C   
15040 O O   . GLY B 815  ? 0.2209 0.2276 0.2560 0.0076  -0.0108 -0.0184 813  GLY B O   
15041 N N   . GLN B 816  ? 0.1852 0.1884 0.2156 0.0074  -0.0119 -0.0198 814  GLN B N   
15042 C CA  . GLN B 816  ? 0.1883 0.1911 0.2184 0.0068  -0.0139 -0.0200 814  GLN B CA  
15043 C C   . GLN B 816  ? 0.1832 0.1841 0.2090 0.0073  -0.0142 -0.0210 814  GLN B C   
15044 O O   . GLN B 816  ? 0.2134 0.2121 0.2371 0.0070  -0.0152 -0.0218 814  GLN B O   
15045 C CB  . GLN B 816  ? 0.2161 0.2184 0.2481 0.0056  -0.0153 -0.0199 814  GLN B CB  
15046 C CG  . GLN B 816  ? 0.2072 0.2097 0.2397 0.0050  -0.0176 -0.0199 814  GLN B CG  
15047 C CD  . GLN B 816  ? 0.2087 0.2140 0.2445 0.0052  -0.0175 -0.0189 814  GLN B CD  
15048 O OE1 . GLN B 816  ? 0.2301 0.2359 0.2648 0.0062  -0.0170 -0.0188 814  GLN B OE1 
15049 N NE2 . GLN B 816  ? 0.2020 0.2093 0.2420 0.0044  -0.0181 -0.0181 814  GLN B NE2 
15050 N N   . ASN B 817  ? 0.1674 0.1689 0.1916 0.0081  -0.0133 -0.0210 815  ASN B N   
15051 C CA  . ASN B 817  ? 0.1688 0.1691 0.1893 0.0086  -0.0127 -0.0218 815  ASN B CA  
15052 C C   . ASN B 817  ? 0.1940 0.1932 0.2118 0.0085  -0.0142 -0.0223 815  ASN B C   
15053 O O   . ASN B 817  ? 0.2007 0.2006 0.2190 0.0082  -0.0150 -0.0218 815  ASN B O   
15054 C CB  . ASN B 817  ? 0.1807 0.1825 0.2009 0.0093  -0.0111 -0.0214 815  ASN B CB  
15055 C CG  . ASN B 817  ? 0.1817 0.1846 0.2043 0.0094  -0.0098 -0.0209 815  ASN B CG  
15056 O OD1 . ASN B 817  ? 0.1763 0.1787 0.1992 0.0095  -0.0093 -0.0210 815  ASN B OD1 
15057 N ND2 . ASN B 817  ? 0.1806 0.1849 0.2048 0.0095  -0.0092 -0.0202 815  ASN B ND2 
15058 N N   . ALA B 818  ? 0.1819 0.1793 0.1966 0.0087  -0.0143 -0.0233 816  ALA B N   
15059 C CA  . ALA B 818  ? 0.1825 0.1784 0.1940 0.0085  -0.0156 -0.0239 816  ALA B CA  
15060 C C   . ALA B 818  ? 0.1899 0.1860 0.1980 0.0093  -0.0143 -0.0243 816  ALA B C   
15061 O O   . ALA B 818  ? 0.1940 0.1908 0.2020 0.0100  -0.0126 -0.0244 816  ALA B O   
15062 C CB  . ALA B 818  ? 0.1937 0.1871 0.2037 0.0082  -0.0169 -0.0249 816  ALA B CB  
15063 N N   . MET B 819  ? 0.1796 0.1750 0.1850 0.0091  -0.0152 -0.0244 817  MET B N   
15064 C CA  . MET B 819  ? 0.1872 0.1824 0.1888 0.0097  -0.0142 -0.0249 817  MET B CA  
15065 C C   . MET B 819  ? 0.1947 0.1875 0.1928 0.0095  -0.0156 -0.0259 817  MET B C   
15066 O O   . MET B 819  ? 0.2068 0.1988 0.2047 0.0088  -0.0175 -0.0256 817  MET B O   
15067 C CB  . MET B 819  ? 0.2089 0.2056 0.2102 0.0095  -0.0136 -0.0240 817  MET B CB  
15068 C CG  . MET B 819  ? 0.2257 0.2225 0.2231 0.0098  -0.0125 -0.0244 817  MET B CG  
15069 S SD  . MET B 819  ? 0.2395 0.2373 0.2360 0.0092  -0.0122 -0.0231 817  MET B SD  
15070 C CE  . MET B 819  ? 0.2575 0.2576 0.2573 0.0093  -0.0105 -0.0225 817  MET B CE  
15071 N N   . ILE B 820  ? 0.2022 0.1939 0.1974 0.0103  -0.0148 -0.0270 818  ILE B N   
15072 C CA  . ILE B 820  ? 0.1911 0.1802 0.1820 0.0103  -0.0159 -0.0281 818  ILE B CA  
15073 C C   . ILE B 820  ? 0.2096 0.1993 0.1969 0.0108  -0.0147 -0.0281 818  ILE B C   
15074 O O   . ILE B 820  ? 0.2095 0.2011 0.1968 0.0116  -0.0126 -0.0281 818  ILE B O   
15075 C CB  . ILE B 820  ? 0.2047 0.1915 0.1944 0.0111  -0.0157 -0.0294 818  ILE B CB  
15076 C CG1 . ILE B 820  ? 0.2116 0.1976 0.2048 0.0103  -0.0170 -0.0292 818  ILE B CG1 
15077 C CG2 . ILE B 820  ? 0.2181 0.2019 0.2026 0.0112  -0.0167 -0.0308 818  ILE B CG2 
15078 C CD1 . ILE B 820  ? 0.2532 0.2364 0.2452 0.0108  -0.0170 -0.0304 818  ILE B CD1 
15079 N N   . VAL B 821  ? 0.2148 0.2032 0.1990 0.0102  -0.0161 -0.0281 819  VAL B N   
15080 C CA  . VAL B 821  ? 0.2050 0.1939 0.1855 0.0103  -0.0152 -0.0279 819  VAL B CA  
15081 C C   . VAL B 821  ? 0.2390 0.2251 0.2146 0.0105  -0.0161 -0.0292 819  VAL B C   
15082 O O   . VAL B 821  ? 0.2434 0.2273 0.2181 0.0098  -0.0185 -0.0294 819  VAL B O   
15083 C CB  . VAL B 821  ? 0.2016 0.1914 0.1829 0.0093  -0.0161 -0.0264 819  VAL B CB  
15084 C CG1 . VAL B 821  ? 0.2266 0.2166 0.2037 0.0092  -0.0152 -0.0261 819  VAL B CG1 
15085 C CG2 . VAL B 821  ? 0.2198 0.2119 0.2058 0.0091  -0.0154 -0.0253 819  VAL B CG2 
15086 N N   . ASP B 822  ? 0.2289 0.2148 0.2010 0.0116  -0.0143 -0.0302 820  ASP B N   
15087 C CA  . ASP B 822  ? 0.2482 0.2312 0.2149 0.0119  -0.0150 -0.0315 820  ASP B CA  
15088 C C   . ASP B 822  ? 0.2551 0.2386 0.2179 0.0115  -0.0146 -0.0309 820  ASP B C   
15089 O O   . ASP B 822  ? 0.2511 0.2370 0.2154 0.0109  -0.0139 -0.0294 820  ASP B O   
15090 C CB  . ASP B 822  ? 0.2612 0.2430 0.2262 0.0135  -0.0136 -0.0332 820  ASP B CB  
15091 C CG  . ASP B 822  ? 0.2725 0.2570 0.2367 0.0147  -0.0106 -0.0332 820  ASP B CG  
15092 O OD1 . ASP B 822  ? 0.2498 0.2368 0.2137 0.0142  -0.0096 -0.0320 820  ASP B OD1 
15093 O OD2 . ASP B 822  ? 0.3020 0.2860 0.2657 0.0163  -0.0093 -0.0343 820  ASP B OD2 
15094 N N   . SER B 823  ? 0.2521 0.2329 0.2093 0.0118  -0.0151 -0.0320 821  SER B N   
15095 C CA  . SER B 823  ? 0.2791 0.2599 0.2320 0.0113  -0.0149 -0.0314 821  SER B CA  
15096 C C   . SER B 823  ? 0.2831 0.2668 0.2349 0.0120  -0.0118 -0.0311 821  SER B C   
15097 O O   . SER B 823  ? 0.3105 0.2945 0.2590 0.0114  -0.0113 -0.0302 821  SER B O   
15098 C CB  . SER B 823  ? 0.2828 0.2596 0.2298 0.0113  -0.0165 -0.0328 821  SER B CB  
15099 O OG  . SER B 823  ? 0.3076 0.2830 0.2519 0.0128  -0.0151 -0.0347 821  SER B OG  
15100 N N   . SER B 824  ? 0.2425 0.2283 0.1970 0.0132  -0.0096 -0.0315 822  SER B N   
15101 C CA  . SER B 824  ? 0.2615 0.2507 0.2157 0.0137  -0.0067 -0.0310 822  SER B CA  
15102 C C   . SER B 824  ? 0.2643 0.2568 0.2230 0.0127  -0.0061 -0.0292 822  SER B C   
15103 O O   . SER B 824  ? 0.2910 0.2866 0.2497 0.0126  -0.0040 -0.0284 822  SER B O   
15104 C CB  . SER B 824  ? 0.2657 0.2558 0.2203 0.0157  -0.0047 -0.0324 822  SER B CB  
15105 O OG  . SER B 824  ? 0.2466 0.2381 0.2067 0.0160  -0.0047 -0.0322 822  SER B OG  
15106 N N   . ALA B 825  ? 0.2547 0.2468 0.2172 0.0118  -0.0079 -0.0284 823  ALA B N   
15107 C CA  . ALA B 825  ? 0.2546 0.2494 0.2213 0.0110  -0.0074 -0.0269 823  ALA B CA  
15108 C C   . ALA B 825  ? 0.2655 0.2606 0.2302 0.0097  -0.0075 -0.0254 823  ALA B C   
15109 O O   . ALA B 825  ? 0.2974 0.2902 0.2582 0.0092  -0.0089 -0.0253 823  ALA B O   
15110 C CB  . ALA B 825  ? 0.2706 0.2645 0.2416 0.0106  -0.0093 -0.0266 823  ALA B CB  
15111 N N   . LEU B 826  ? 0.2744 0.2722 0.2415 0.0090  -0.0062 -0.0241 824  LEU B N   
15112 C CA  . LEU B 826  ? 0.2879 0.2858 0.2532 0.0076  -0.0063 -0.0225 824  LEU B CA  
15113 C C   . LEU B 826  ? 0.2972 0.2935 0.2649 0.0068  -0.0085 -0.0215 824  LEU B C   
15114 O O   . LEU B 826  ? 0.2698 0.2673 0.2419 0.0067  -0.0084 -0.0211 824  LEU B O   
15115 C CB  . LEU B 826  ? 0.3148 0.3162 0.2816 0.0071  -0.0039 -0.0216 824  LEU B CB  
15116 C CG  . LEU B 826  ? 0.3895 0.3909 0.3544 0.0054  -0.0037 -0.0199 824  LEU B CG  
15117 C CD1 . LEU B 826  ? 0.4054 0.4051 0.3646 0.0052  -0.0038 -0.0198 824  LEU B CD1 
15118 C CD2 . LEU B 826  ? 0.4786 0.4837 0.4454 0.0048  -0.0015 -0.0191 824  LEU B CD2 
15119 N N   . ALA B 827  ? 0.2791 0.2728 0.2439 0.0062  -0.0104 -0.0210 825  ALA B N   
15120 C CA  . ALA B 827  ? 0.2621 0.2543 0.2293 0.0058  -0.0127 -0.0202 825  ALA B CA  
15121 C C   . ALA B 827  ? 0.2657 0.2591 0.2361 0.0051  -0.0121 -0.0188 825  ALA B C   
15122 O O   . ALA B 827  ? 0.2691 0.2626 0.2435 0.0054  -0.0129 -0.0187 825  ALA B O   
15123 C CB  . ALA B 827  ? 0.2672 0.2567 0.2303 0.0053  -0.0147 -0.0196 825  ALA B CB  
15124 N N   . GLU B 828  ? 0.2593 0.2535 0.2278 0.0042  -0.0107 -0.0178 826  GLU B N   
15125 C CA  . GLU B 828  ? 0.2743 0.2692 0.2453 0.0034  -0.0103 -0.0165 826  GLU B CA  
15126 C C   . GLU B 828  ? 0.2941 0.2912 0.2697 0.0039  -0.0092 -0.0172 826  GLU B C   
15127 O O   . GLU B 828  ? 0.2692 0.2661 0.2480 0.0038  -0.0097 -0.0166 826  GLU B O   
15128 C CB  . GLU B 828  ? 0.3236 0.3192 0.2918 0.0022  -0.0088 -0.0154 826  GLU B CB  
15129 C CG  . GLU B 828  ? 0.3596 0.3525 0.3233 0.0014  -0.0100 -0.0142 826  GLU B CG  
15130 C CD  . GLU B 828  ? 0.3929 0.3851 0.3521 0.0018  -0.0100 -0.0150 826  GLU B CD  
15131 O OE1 . GLU B 828  ? 0.3704 0.3641 0.3298 0.0028  -0.0091 -0.0165 826  GLU B OE1 
15132 O OE2 . GLU B 828  ? 0.4232 0.4131 0.3783 0.0011  -0.0111 -0.0140 826  GLU B OE2 
15133 N N   . GLN B 829  ? 0.2439 0.2432 0.2199 0.0046  -0.0076 -0.0183 827  GLN B N   
15134 C CA  . GLN B 829  ? 0.2596 0.2610 0.2397 0.0052  -0.0067 -0.0188 827  GLN B CA  
15135 C C   . GLN B 829  ? 0.2546 0.2547 0.2375 0.0060  -0.0082 -0.0195 827  GLN B C   
15136 O O   . GLN B 829  ? 0.2442 0.2449 0.2306 0.0060  -0.0082 -0.0192 827  GLN B O   
15137 C CB  . GLN B 829  ? 0.3184 0.3222 0.2979 0.0060  -0.0048 -0.0198 827  GLN B CB  
15138 N N   . VAL B 830  ? 0.2421 0.2405 0.2235 0.0066  -0.0095 -0.0203 828  VAL B N   
15139 C CA  . VAL B 830  ? 0.2268 0.2241 0.2109 0.0071  -0.0111 -0.0208 828  VAL B CA  
15140 C C   . VAL B 830  ? 0.2504 0.2470 0.2367 0.0066  -0.0123 -0.0196 828  VAL B C   
15141 O O   . VAL B 830  ? 0.2288 0.2259 0.2188 0.0069  -0.0125 -0.0196 828  VAL B O   
15142 C CB  . VAL B 830  ? 0.2169 0.2121 0.1983 0.0074  -0.0126 -0.0216 828  VAL B CB  
15143 C CG1 . VAL B 830  ? 0.2505 0.2447 0.2349 0.0076  -0.0145 -0.0218 828  VAL B CG1 
15144 C CG2 . VAL B 830  ? 0.2404 0.2360 0.2197 0.0082  -0.0113 -0.0230 828  VAL B CG2 
15145 N N   . VAL B 831  ? 0.2251 0.2202 0.2089 0.0060  -0.0132 -0.0186 829  VAL B N   
15146 C CA  . VAL B 831  ? 0.2007 0.1948 0.1864 0.0058  -0.0146 -0.0175 829  VAL B CA  
15147 C C   . VAL B 831  ? 0.2340 0.2291 0.2224 0.0056  -0.0133 -0.0170 829  VAL B C   
15148 O O   . VAL B 831  ? 0.2333 0.2284 0.2251 0.0061  -0.0138 -0.0168 829  VAL B O   
15149 C CB  . VAL B 831  ? 0.2260 0.2181 0.2080 0.0052  -0.0158 -0.0164 829  VAL B CB  
15150 C CG1 . VAL B 831  ? 0.2437 0.2346 0.2275 0.0051  -0.0167 -0.0152 829  VAL B CG1 
15151 C CG2 . VAL B 831  ? 0.2455 0.2362 0.2255 0.0055  -0.0176 -0.0170 829  VAL B CG2 
15152 N N   . GLY B 832  ? 0.2164 0.2127 0.2035 0.0050  -0.0115 -0.0168 830  GLY B N   
15153 C CA  . GLY B 832  ? 0.2338 0.2310 0.2233 0.0047  -0.0104 -0.0164 830  GLY B CA  
15154 C C   . GLY B 832  ? 0.2217 0.2204 0.2149 0.0055  -0.0099 -0.0173 830  GLY B C   
15155 O O   . GLY B 832  ? 0.2317 0.2303 0.2275 0.0057  -0.0100 -0.0170 830  GLY B O   
15156 N N   . ASP B 833  ? 0.2083 0.2082 0.2015 0.0061  -0.0095 -0.0183 831  ASP B N   
15157 C CA  . ASP B 833  ? 0.2107 0.2118 0.2072 0.0068  -0.0090 -0.0191 831  ASP B CA  
15158 C C   . ASP B 833  ? 0.2251 0.2251 0.2240 0.0073  -0.0105 -0.0192 831  ASP B C   
15159 O O   . ASP B 833  ? 0.2155 0.2163 0.2175 0.0077  -0.0101 -0.0193 831  ASP B O   
15160 C CB  . ASP B 833  ? 0.2144 0.2168 0.2101 0.0074  -0.0081 -0.0201 831  ASP B CB  
15161 C CG  . ASP B 833  ? 0.2305 0.2349 0.2249 0.0070  -0.0064 -0.0200 831  ASP B CG  
15162 O OD1 . ASP B 833  ? 0.2561 0.2610 0.2509 0.0061  -0.0058 -0.0191 831  ASP B OD1 
15163 O OD2 . ASP B 833  ? 0.2568 0.2622 0.2499 0.0076  -0.0055 -0.0207 831  ASP B OD2 
15164 N N   . VAL B 834  ? 0.2078 0.2064 0.2055 0.0073  -0.0121 -0.0190 832  VAL B N   
15165 C CA  . VAL B 834  ? 0.1970 0.1950 0.1973 0.0077  -0.0136 -0.0190 832  VAL B CA  
15166 C C   . VAL B 834  ? 0.2195 0.2172 0.2218 0.0078  -0.0138 -0.0180 832  VAL B C   
15167 O O   . VAL B 834  ? 0.2282 0.2265 0.2340 0.0082  -0.0139 -0.0180 832  VAL B O   
15168 C CB  . VAL B 834  ? 0.2163 0.2127 0.2144 0.0076  -0.0155 -0.0190 832  VAL B CB  
15169 C CG1 . VAL B 834  ? 0.2270 0.2232 0.2280 0.0078  -0.0173 -0.0186 832  VAL B CG1 
15170 C CG2 . VAL B 834  ? 0.2394 0.2357 0.2361 0.0078  -0.0155 -0.0203 832  VAL B CG2 
15171 N N   . ILE B 835  ? 0.2189 0.2156 0.2191 0.0073  -0.0138 -0.0172 833  ILE B N   
15172 C CA  . ILE B 835  ? 0.2605 0.2564 0.2623 0.0075  -0.0140 -0.0163 833  ILE B CA  
15173 C C   . ILE B 835  ? 0.2551 0.2522 0.2592 0.0077  -0.0124 -0.0166 833  ILE B C   
15174 O O   . ILE B 835  ? 0.2761 0.2734 0.2831 0.0083  -0.0125 -0.0165 833  ILE B O   
15175 C CB  . ILE B 835  ? 0.2773 0.2714 0.2759 0.0069  -0.0143 -0.0153 833  ILE B CB  
15176 C CG1 . ILE B 835  ? 0.3252 0.3180 0.3217 0.0069  -0.0162 -0.0149 833  ILE B CG1 
15177 C CG2 . ILE B 835  ? 0.3302 0.3231 0.3301 0.0071  -0.0142 -0.0146 833  ILE B CG2 
15178 C CD1 . ILE B 835  ? 0.3512 0.3418 0.3447 0.0064  -0.0167 -0.0137 833  ILE B CD1 
15179 N N   . THR B 836  ? 0.2201 0.2182 0.2230 0.0071  -0.0109 -0.0170 834  THR B N   
15180 C CA  . THR B 836  ? 0.2431 0.2423 0.2478 0.0072  -0.0096 -0.0173 834  THR B CA  
15181 C C   . THR B 836  ? 0.2709 0.2713 0.2788 0.0080  -0.0095 -0.0179 834  THR B C   
15182 O O   . THR B 836  ? 0.3088 0.3093 0.3190 0.0084  -0.0092 -0.0178 834  THR B O   
15183 C CB  . THR B 836  ? 0.2453 0.2460 0.2484 0.0065  -0.0082 -0.0176 834  THR B CB  
15184 O OG1 . THR B 836  ? 0.3301 0.3299 0.3306 0.0055  -0.0081 -0.0169 834  THR B OG1 
15185 C CG2 . THR B 836  ? 0.2926 0.2947 0.2976 0.0066  -0.0070 -0.0179 834  THR B CG2 
15186 N N   . SER B 837  ? 0.2182 0.2192 0.2260 0.0082  -0.0099 -0.0185 835  SER B N   
15187 C CA  . SER B 837  ? 0.2157 0.2175 0.2261 0.0087  -0.0098 -0.0190 835  SER B CA  
15188 C C   . SER B 837  ? 0.2047 0.2063 0.2178 0.0091  -0.0109 -0.0187 835  SER B C   
15189 O O   . SER B 837  ? 0.2020 0.2044 0.2179 0.0095  -0.0104 -0.0187 835  SER B O   
15190 C CB  . SER B 837  ? 0.2029 0.2050 0.2122 0.0088  -0.0099 -0.0198 835  SER B CB  
15191 O OG  . SER B 837  ? 0.2024 0.2052 0.2095 0.0086  -0.0088 -0.0201 835  SER B OG  
15192 N N   . ALA B 838  ? 0.2022 0.2028 0.2146 0.0091  -0.0124 -0.0182 836  ALA B N   
15193 C CA  . ALA B 838  ? 0.1858 0.1866 0.2011 0.0095  -0.0137 -0.0179 836  ALA B CA  
15194 C C   . ALA B 838  ? 0.2014 0.2021 0.2184 0.0100  -0.0136 -0.0171 836  ALA B C   
15195 O O   . ALA B 838  ? 0.2279 0.2296 0.2483 0.0106  -0.0137 -0.0169 836  ALA B O   
15196 C CB  . ALA B 838  ? 0.1857 0.1858 0.1997 0.0092  -0.0157 -0.0178 836  ALA B CB  
15197 N N   . PHE B 839  ? 0.2352 0.2345 0.2498 0.0099  -0.0134 -0.0167 837  PHE B N   
15198 C CA  . PHE B 839  ? 0.2365 0.2349 0.2521 0.0106  -0.0137 -0.0159 837  PHE B CA  
15199 C C   . PHE B 839  ? 0.2535 0.2511 0.2685 0.0107  -0.0122 -0.0158 837  PHE B C   
15200 O O   . PHE B 839  ? 0.2763 0.2731 0.2927 0.0115  -0.0121 -0.0154 837  PHE B O   
15201 C CB  . PHE B 839  ? 0.2358 0.2325 0.2492 0.0105  -0.0154 -0.0152 837  PHE B CB  
15202 C CG  . PHE B 839  ? 0.2457 0.2430 0.2595 0.0104  -0.0171 -0.0152 837  PHE B CG  
15203 C CD1 . PHE B 839  ? 0.2205 0.2193 0.2381 0.0110  -0.0181 -0.0151 837  PHE B CD1 
15204 C CD2 . PHE B 839  ? 0.2519 0.2482 0.2621 0.0097  -0.0179 -0.0154 837  PHE B CD2 
15205 C CE1 . PHE B 839  ? 0.2149 0.2142 0.2328 0.0107  -0.0199 -0.0152 837  PHE B CE1 
15206 C CE2 . PHE B 839  ? 0.2698 0.2663 0.2799 0.0095  -0.0197 -0.0155 837  PHE B CE2 
15207 C CZ  . PHE B 839  ? 0.2540 0.2519 0.2679 0.0100  -0.0208 -0.0154 837  PHE B CZ  
15208 N N   . ASP B 840  ? 0.2654 0.2630 0.2783 0.0098  -0.0110 -0.0163 838  ASP B N   
15209 C CA  . ASP B 840  ? 0.2864 0.2835 0.2989 0.0097  -0.0096 -0.0163 838  ASP B CA  
15210 C C   . ASP B 840  ? 0.3117 0.3098 0.3274 0.0106  -0.0088 -0.0166 838  ASP B C   
15211 O O   . ASP B 840  ? 0.2528 0.2528 0.2708 0.0109  -0.0088 -0.0169 838  ASP B O   
15212 C CB  . ASP B 840  ? 0.3408 0.3387 0.3514 0.0087  -0.0086 -0.0168 838  ASP B CB  
15213 C CG  . ASP B 840  ? 0.4898 0.4876 0.5002 0.0083  -0.0073 -0.0170 838  ASP B CG  
15214 O OD1 . ASP B 840  ? 0.4848 0.4837 0.4971 0.0088  -0.0065 -0.0174 838  ASP B OD1 
15215 O OD2 . ASP B 840  ? 0.5574 0.5537 0.5653 0.0075  -0.0072 -0.0166 838  ASP B OD2 
15216 N N   . SER B 841  ? 0.2429 0.2398 0.2587 0.0111  -0.0082 -0.0165 839  SER B N   
15217 C CA  . SER B 841  ? 0.2368 0.2345 0.2554 0.0121  -0.0073 -0.0167 839  SER B CA  
15218 C C   . SER B 841  ? 0.2202 0.2192 0.2420 0.0131  -0.0082 -0.0163 839  SER B C   
15219 O O   . SER B 841  ? 0.2157 0.2165 0.2404 0.0137  -0.0074 -0.0165 839  SER B O   
15220 C CB  . SER B 841  ? 0.3053 0.3046 0.3244 0.0117  -0.0060 -0.0173 839  SER B CB  
15221 O OG  . SER B 841  ? 0.3232 0.3217 0.3395 0.0107  -0.0054 -0.0175 839  SER B OG  
15222 N N   . ALA B 842  ? 0.2114 0.2097 0.2329 0.0132  -0.0097 -0.0158 840  ALA B N   
15223 C CA  . ALA B 842  ? 0.1964 0.1962 0.2210 0.0140  -0.0110 -0.0154 840  ALA B CA  
15224 C C   . ALA B 842  ? 0.1951 0.1974 0.2219 0.0135  -0.0109 -0.0158 840  ALA B C   
15225 O O   . ALA B 842  ? 0.2006 0.2048 0.2310 0.0140  -0.0110 -0.0156 840  ALA B O   
15226 C CB  . ALA B 842  ? 0.2098 0.2097 0.2371 0.0155  -0.0107 -0.0150 840  ALA B CB  
15227 N N   . GLY B 843  ? 0.1976 0.1998 0.2222 0.0124  -0.0106 -0.0163 841  GLY B N   
15228 C CA  . GLY B 843  ? 0.1962 0.2000 0.2224 0.0119  -0.0106 -0.0167 841  GLY B CA  
15229 C C   . GLY B 843  ? 0.1872 0.1923 0.2156 0.0122  -0.0091 -0.0169 841  GLY B C   
15230 O O   . GLY B 843  ? 0.2003 0.2068 0.2305 0.0119  -0.0091 -0.0171 841  GLY B O   
15231 N N   . GLN B 844  ? 0.1777 0.1824 0.2058 0.0127  -0.0077 -0.0169 842  GLN B N   
15232 C CA  . GLN B 844  ? 0.1930 0.1988 0.2230 0.0131  -0.0062 -0.0170 842  GLN B CA  
15233 C C   . GLN B 844  ? 0.1941 0.1996 0.2220 0.0124  -0.0051 -0.0175 842  GLN B C   
15234 O O   . GLN B 844  ? 0.2031 0.2082 0.2301 0.0126  -0.0039 -0.0177 842  GLN B O   
15235 C CB  . GLN B 844  ? 0.1735 0.1789 0.2044 0.0142  -0.0053 -0.0168 842  GLN B CB  
15236 C CG  . GLN B 844  ? 0.1781 0.1845 0.2120 0.0150  -0.0064 -0.0162 842  GLN B CG  
15237 C CD  . GLN B 844  ? 0.1917 0.1971 0.2260 0.0165  -0.0058 -0.0159 842  GLN B CD  
15238 O OE1 . GLN B 844  ? 0.1994 0.2065 0.2370 0.0175  -0.0052 -0.0156 842  GLN B OE1 
15239 N NE2 . GLN B 844  ? 0.2118 0.2145 0.2428 0.0165  -0.0060 -0.0160 842  GLN B NE2 
15240 N N   . ARG B 845  ? 0.1947 0.2005 0.2217 0.0117  -0.0057 -0.0178 843  ARG B N   
15241 C CA  . ARG B 845  ? 0.1581 0.1641 0.1837 0.0112  -0.0049 -0.0182 843  ARG B CA  
15242 C C   . ARG B 845  ? 0.1658 0.1726 0.1930 0.0110  -0.0053 -0.0183 843  ARG B C   
15243 O O   . ARG B 845  ? 0.1785 0.1853 0.2063 0.0108  -0.0066 -0.0183 843  ARG B O   
15244 C CB  . ARG B 845  ? 0.2010 0.2062 0.2235 0.0107  -0.0052 -0.0186 843  ARG B CB  
15245 C CG  . ARG B 845  ? 0.2291 0.2332 0.2496 0.0106  -0.0050 -0.0184 843  ARG B CG  
15246 C CD  . ARG B 845  ? 0.3001 0.3041 0.3179 0.0098  -0.0051 -0.0187 843  ARG B CD  
15247 N NE  . ARG B 845  ? 0.3366 0.3394 0.3523 0.0094  -0.0052 -0.0184 843  ARG B NE  
15248 C CZ  . ARG B 845  ? 0.4705 0.4732 0.4848 0.0088  -0.0043 -0.0185 843  ARG B CZ  
15249 N NH1 . ARG B 845  ? 0.4904 0.4943 0.5053 0.0089  -0.0034 -0.0188 843  ARG B NH1 
15250 N NH2 . ARG B 845  ? 0.5539 0.5552 0.5663 0.0082  -0.0045 -0.0182 843  ARG B NH2 
15251 N N   . CYS B 846  ? 0.1912 0.1985 0.2187 0.0110  -0.0042 -0.0184 844  CYS B N   
15252 C CA  . CYS B 846  ? 0.1993 0.2069 0.2280 0.0107  -0.0046 -0.0185 844  CYS B CA  
15253 C C   . CYS B 846  ? 0.1547 0.1614 0.1813 0.0104  -0.0057 -0.0190 844  CYS B C   
15254 O O   . CYS B 846  ? 0.1877 0.1941 0.2150 0.0101  -0.0066 -0.0192 844  CYS B O   
15255 C CB  . CYS B 846  ? 0.2010 0.2089 0.2298 0.0107  -0.0034 -0.0184 844  CYS B CB  
15256 S SG  . CYS B 846  ? 0.1950 0.2026 0.2208 0.0109  -0.0025 -0.0188 844  CYS B SG  
15257 N N   . SER B 847  ? 0.1705 0.1769 0.1945 0.0104  -0.0054 -0.0193 845  SER B N   
15258 C CA  . SER B 847  ? 0.1743 0.1802 0.1961 0.0103  -0.0060 -0.0199 845  SER B CA  
15259 C C   . SER B 847  ? 0.1862 0.1914 0.2071 0.0101  -0.0073 -0.0199 845  SER B C   
15260 O O   . SER B 847  ? 0.1766 0.1812 0.1953 0.0100  -0.0078 -0.0204 845  SER B O   
15261 C CB  . SER B 847  ? 0.1837 0.1899 0.2033 0.0104  -0.0051 -0.0200 845  SER B CB  
15262 O OG  . SER B 847  ? 0.2076 0.2138 0.2271 0.0102  -0.0048 -0.0196 845  SER B OG  
15263 N N   . ALA B 848  ? 0.1700 0.1752 0.1924 0.0101  -0.0079 -0.0194 846  ALA B N   
15264 C CA  . ALA B 848  ? 0.1686 0.1731 0.1899 0.0099  -0.0092 -0.0192 846  ALA B CA  
15265 C C   . ALA B 848  ? 0.1790 0.1828 0.1997 0.0096  -0.0106 -0.0196 846  ALA B C   
15266 O O   . ALA B 848  ? 0.1861 0.1901 0.2085 0.0095  -0.0109 -0.0198 846  ALA B O   
15267 C CB  . ALA B 848  ? 0.1773 0.1821 0.2009 0.0102  -0.0096 -0.0185 846  ALA B CB  
15268 N N   . LEU B 849  ? 0.1824 0.1853 0.2005 0.0094  -0.0115 -0.0197 847  LEU B N   
15269 C CA  . LEU B 849  ? 0.1731 0.1751 0.1900 0.0091  -0.0130 -0.0202 847  LEU B CA  
15270 C C   . LEU B 849  ? 0.1772 0.1794 0.1968 0.0089  -0.0146 -0.0197 847  LEU B C   
15271 O O   . LEU B 849  ? 0.1940 0.1964 0.2143 0.0091  -0.0152 -0.0190 847  LEU B O   
15272 C CB  . LEU B 849  ? 0.1886 0.1895 0.2017 0.0090  -0.0133 -0.0203 847  LEU B CB  
15273 C CG  . LEU B 849  ? 0.1965 0.1961 0.2076 0.0087  -0.0150 -0.0208 847  LEU B CG  
15274 C CD1 . LEU B 849  ? 0.2232 0.2222 0.2338 0.0087  -0.0149 -0.0218 847  LEU B CD1 
15275 C CD2 . LEU B 849  ? 0.2048 0.2036 0.2120 0.0085  -0.0151 -0.0207 847  LEU B CD2 
15276 N N   . ARG B 850  ? 0.1654 0.1675 0.1864 0.0085  -0.0154 -0.0200 848  ARG B N   
15277 C CA  . ARG B 850  ? 0.1773 0.1801 0.2012 0.0081  -0.0170 -0.0196 848  ARG B CA  
15278 C C   . ARG B 850  ? 0.1918 0.1932 0.2136 0.0075  -0.0192 -0.0200 848  ARG B C   
15279 O O   . ARG B 850  ? 0.2004 0.2024 0.2239 0.0072  -0.0209 -0.0195 848  ARG B O   
15280 C CB  . ARG B 850  ? 0.1897 0.1936 0.2171 0.0078  -0.0165 -0.0194 848  ARG B CB  
15281 C CG  . ARG B 850  ? 0.2072 0.2123 0.2362 0.0083  -0.0144 -0.0191 848  ARG B CG  
15282 C CD  . ARG B 850  ? 0.1852 0.1913 0.2154 0.0090  -0.0140 -0.0183 848  ARG B CD  
15283 N NE  . ARG B 850  ? 0.1997 0.2068 0.2313 0.0095  -0.0121 -0.0181 848  ARG B NE  
15284 C CZ  . ARG B 850  ? 0.1910 0.1986 0.2231 0.0102  -0.0113 -0.0176 848  ARG B CZ  
15285 N NH1 . ARG B 850  ? 0.2014 0.2086 0.2329 0.0106  -0.0122 -0.0173 848  ARG B NH1 
15286 N NH2 . ARG B 850  ? 0.1893 0.1975 0.2223 0.0106  -0.0095 -0.0175 848  ARG B NH2 
15287 N N   . VAL B 851  ? 0.1940 0.1936 0.2124 0.0073  -0.0191 -0.0210 849  VAL B N   
15288 C CA  . VAL B 851  ? 0.1908 0.1886 0.2068 0.0067  -0.0211 -0.0217 849  VAL B CA  
15289 C C   . VAL B 851  ? 0.2049 0.2010 0.2159 0.0071  -0.0205 -0.0224 849  VAL B C   
15290 O O   . VAL B 851  ? 0.2082 0.2037 0.2175 0.0075  -0.0191 -0.0232 849  VAL B O   
15291 C CB  . VAL B 851  ? 0.2113 0.2080 0.2282 0.0060  -0.0217 -0.0223 849  VAL B CB  
15292 C CG1 . VAL B 851  ? 0.2516 0.2461 0.2657 0.0053  -0.0240 -0.0231 849  VAL B CG1 
15293 C CG2 . VAL B 851  ? 0.2478 0.2465 0.2699 0.0055  -0.0219 -0.0215 849  VAL B CG2 
15294 N N   . LEU B 852  ? 0.2185 0.2140 0.2272 0.0070  -0.0217 -0.0222 850  LEU B N   
15295 C CA  . LEU B 852  ? 0.2012 0.1952 0.2049 0.0072  -0.0213 -0.0228 850  LEU B CA  
15296 C C   . LEU B 852  ? 0.1981 0.1898 0.1988 0.0068  -0.0231 -0.0238 850  LEU B C   
15297 O O   . LEU B 852  ? 0.2100 0.2013 0.2112 0.0061  -0.0254 -0.0235 850  LEU B O   
15298 C CB  . LEU B 852  ? 0.2091 0.2035 0.2116 0.0073  -0.0216 -0.0218 850  LEU B CB  
15299 C CG  . LEU B 852  ? 0.2063 0.1994 0.2036 0.0074  -0.0212 -0.0222 850  LEU B CG  
15300 C CD1 . LEU B 852  ? 0.2231 0.2168 0.2192 0.0079  -0.0187 -0.0228 850  LEU B CD1 
15301 C CD2 . LEU B 852  ? 0.2409 0.2341 0.2373 0.0073  -0.0216 -0.0210 850  LEU B CD2 
15302 N N   . CYS B 853  ? 0.2049 0.1952 0.2027 0.0071  -0.0222 -0.0250 851  CYS B N   
15303 C CA  . CYS B 853  ? 0.2134 0.2009 0.2078 0.0068  -0.0237 -0.0263 851  CYS B CA  
15304 C C   . CYS B 853  ? 0.2062 0.1924 0.1952 0.0073  -0.0232 -0.0268 851  CYS B C   
15305 O O   . CYS B 853  ? 0.2221 0.2088 0.2094 0.0081  -0.0210 -0.0273 851  CYS B O   
15306 C CB  . CYS B 853  ? 0.2165 0.2027 0.2113 0.0071  -0.0230 -0.0273 851  CYS B CB  
15307 S SG  . CYS B 853  ? 0.2495 0.2375 0.2506 0.0065  -0.0230 -0.0265 851  CYS B SG  
15308 N N   . LEU B 854  ? 0.2198 0.2047 0.2061 0.0067  -0.0252 -0.0267 852  LEU B N   
15309 C CA  . LEU B 854  ? 0.2186 0.2025 0.1996 0.0069  -0.0248 -0.0270 852  LEU B CA  
15310 C C   . LEU B 854  ? 0.2447 0.2253 0.2210 0.0068  -0.0261 -0.0285 852  LEU B C   
15311 O O   . LEU B 854  ? 0.2409 0.2201 0.2175 0.0059  -0.0287 -0.0287 852  LEU B O   
15312 C CB  . LEU B 854  ? 0.2188 0.2033 0.1997 0.0064  -0.0262 -0.0256 852  LEU B CB  
15313 C CG  . LEU B 854  ? 0.2184 0.2056 0.2035 0.0066  -0.0250 -0.0241 852  LEU B CG  
15314 C CD1 . LEU B 854  ? 0.2331 0.2203 0.2176 0.0062  -0.0267 -0.0227 852  LEU B CD1 
15315 C CD2 . LEU B 854  ? 0.2531 0.2415 0.2371 0.0072  -0.0221 -0.0241 852  LEU B CD2 
15316 N N   . GLN B 855  ? 0.2312 0.2108 0.2032 0.0077  -0.0244 -0.0296 853  GLN B N   
15317 C CA  . GLN B 855  ? 0.2249 0.2009 0.1914 0.0077  -0.0256 -0.0311 853  GLN B CA  
15318 C C   . GLN B 855  ? 0.2663 0.2413 0.2301 0.0067  -0.0281 -0.0305 853  GLN B C   
15319 O O   . GLN B 855  ? 0.2566 0.2332 0.2202 0.0065  -0.0278 -0.0291 853  GLN B O   
15320 C CB  . GLN B 855  ? 0.2284 0.2039 0.1906 0.0090  -0.0231 -0.0322 853  GLN B CB  
15321 C CG  . GLN B 855  ? 0.2739 0.2454 0.2307 0.0093  -0.0239 -0.0341 853  GLN B CG  
15322 C CD  . GLN B 855  ? 0.3309 0.3021 0.2835 0.0109  -0.0213 -0.0353 853  GLN B CD  
15323 O OE1 . GLN B 855  ? 0.3696 0.3433 0.3245 0.0119  -0.0187 -0.0351 853  GLN B OE1 
15324 N NE2 . GLN B 855  ? 0.3572 0.3255 0.3035 0.0111  -0.0218 -0.0364 853  GLN B NE2 
15325 N N   . GLU B 856  ? 0.2678 0.2399 0.2295 0.0059  -0.0307 -0.0314 854  GLU B N   
15326 C CA  . GLU B 856  ? 0.2673 0.2386 0.2274 0.0048  -0.0337 -0.0307 854  GLU B CA  
15327 C C   . GLU B 856  ? 0.2922 0.2631 0.2471 0.0051  -0.0331 -0.0302 854  GLU B C   
15328 O O   . GLU B 856  ? 0.3165 0.2883 0.2717 0.0045  -0.0346 -0.0287 854  GLU B O   
15329 C CB  . GLU B 856  ? 0.3607 0.3286 0.3184 0.0039  -0.0365 -0.0321 854  GLU B CB  
15330 N N   . ASP B 857  ? 0.2987 0.2683 0.2487 0.0060  -0.0309 -0.0314 855  ASP B N   
15331 C CA  . ASP B 857  ? 0.3267 0.2958 0.2711 0.0062  -0.0303 -0.0310 855  ASP B CA  
15332 C C   . ASP B 857  ? 0.3039 0.2761 0.2504 0.0062  -0.0286 -0.0291 855  ASP B C   
15333 O O   . ASP B 857  ? 0.3604 0.3321 0.3030 0.0059  -0.0287 -0.0282 855  ASP B O   
15334 C CB  . ASP B 857  ? 0.3816 0.3490 0.3206 0.0073  -0.0280 -0.0328 855  ASP B CB  
15335 N N   . VAL B 858  ? 0.2559 0.2310 0.2083 0.0066  -0.0270 -0.0284 856  VAL B N   
15336 C CA  . VAL B 858  ? 0.2776 0.2552 0.2319 0.0065  -0.0255 -0.0266 856  VAL B CA  
15337 C C   . VAL B 858  ? 0.2308 0.2100 0.1908 0.0060  -0.0270 -0.0251 856  VAL B C   
15338 O O   . VAL B 858  ? 0.2643 0.2451 0.2260 0.0059  -0.0261 -0.0236 856  VAL B O   
15339 C CB  . VAL B 858  ? 0.2813 0.2612 0.2370 0.0074  -0.0220 -0.0269 856  VAL B CB  
15340 C CG1 . VAL B 858  ? 0.3168 0.2957 0.2667 0.0080  -0.0202 -0.0281 856  VAL B CG1 
15341 C CG2 . VAL B 858  ? 0.2744 0.2553 0.2350 0.0079  -0.0215 -0.0276 856  VAL B CG2 
15342 N N   . ALA B 859  ? 0.2579 0.2365 0.2209 0.0056  -0.0293 -0.0255 857  ALA B N   
15343 C CA  . ALA B 859  ? 0.2395 0.2202 0.2086 0.0053  -0.0302 -0.0242 857  ALA B CA  
15344 C C   . ALA B 859  ? 0.2532 0.2341 0.2221 0.0050  -0.0316 -0.0224 857  ALA B C   
15345 O O   . ALA B 859  ? 0.2551 0.2379 0.2276 0.0052  -0.0307 -0.0212 857  ALA B O   
15346 C CB  . ALA B 859  ? 0.2380 0.2182 0.2101 0.0048  -0.0325 -0.0249 857  ALA B CB  
15347 N N   . ASP B 860  ? 0.2631 0.2420 0.2275 0.0045  -0.0338 -0.0223 858  ASP B N   
15348 C CA  . ASP B 860  ? 0.2635 0.2424 0.2276 0.0043  -0.0354 -0.0205 858  ASP B CA  
15349 C C   . ASP B 860  ? 0.2656 0.2450 0.2283 0.0045  -0.0330 -0.0194 858  ASP B C   
15350 O O   . ASP B 860  ? 0.2740 0.2544 0.2396 0.0047  -0.0332 -0.0178 858  ASP B O   
15351 C CB  . ASP B 860  ? 0.2701 0.2464 0.2289 0.0037  -0.0381 -0.0206 858  ASP B CB  
15352 C CG  . ASP B 860  ? 0.3886 0.3644 0.3492 0.0032  -0.0412 -0.0213 858  ASP B CG  
15353 O OD1 . ASP B 860  ? 0.4113 0.3893 0.3783 0.0032  -0.0419 -0.0208 858  ASP B OD1 
15354 O OD2 . ASP B 860  ? 0.4132 0.3866 0.3690 0.0027  -0.0429 -0.0223 858  ASP B OD2 
15355 N N   . ARG B 861  ? 0.2552 0.2340 0.2135 0.0046  -0.0308 -0.0201 859  ARG B N   
15356 C CA  . ARG B 861  ? 0.2869 0.2663 0.2437 0.0045  -0.0285 -0.0190 859  ARG B CA  
15357 C C   . ARG B 861  ? 0.2564 0.2383 0.2188 0.0049  -0.0266 -0.0186 859  ARG B C   
15358 O O   . ARG B 861  ? 0.2658 0.2482 0.2293 0.0047  -0.0261 -0.0171 859  ARG B O   
15359 C CB  . ARG B 861  ? 0.3276 0.3064 0.2790 0.0046  -0.0264 -0.0199 859  ARG B CB  
15360 C CG  . ARG B 861  ? 0.4415 0.4214 0.3917 0.0042  -0.0240 -0.0187 859  ARG B CG  
15361 C CD  . ARG B 861  ? 0.4995 0.4790 0.4438 0.0042  -0.0220 -0.0193 859  ARG B CD  
15362 N NE  . ARG B 861  ? 0.6289 0.6098 0.5728 0.0036  -0.0196 -0.0180 859  ARG B NE  
15363 C CZ  . ARG B 861  ? 0.5630 0.5466 0.5093 0.0039  -0.0169 -0.0184 859  ARG B CZ  
15364 N NH1 . ARG B 861  ? 0.5980 0.5828 0.5468 0.0048  -0.0160 -0.0201 859  ARG B NH1 
15365 N NH2 . ARG B 861  ? 0.6055 0.5905 0.5517 0.0031  -0.0150 -0.0171 859  ARG B NH2 
15366 N N   . ILE B 862  ? 0.2390 0.2223 0.2048 0.0053  -0.0256 -0.0199 860  ILE B N   
15367 C CA  . ILE B 862  ? 0.2346 0.2201 0.2054 0.0056  -0.0239 -0.0195 860  ILE B CA  
15368 C C   . ILE B 862  ? 0.2276 0.2136 0.2029 0.0057  -0.0256 -0.0183 860  ILE B C   
15369 O O   . ILE B 862  ? 0.2444 0.2312 0.2219 0.0057  -0.0245 -0.0173 860  ILE B O   
15370 C CB  . ILE B 862  ? 0.2420 0.2285 0.2151 0.0062  -0.0226 -0.0210 860  ILE B CB  
15371 C CG1 . ILE B 862  ? 0.2769 0.2635 0.2460 0.0064  -0.0204 -0.0220 860  ILE B CG1 
15372 C CG2 . ILE B 862  ? 0.2505 0.2392 0.2291 0.0064  -0.0214 -0.0206 860  ILE B CG2 
15373 C CD1 . ILE B 862  ? 0.3158 0.3028 0.2861 0.0072  -0.0193 -0.0236 860  ILE B CD1 
15374 N N   . LEU B 863  ? 0.2450 0.2303 0.2215 0.0056  -0.0282 -0.0184 861  LEU B N   
15375 C CA  . LEU B 863  ? 0.2512 0.2374 0.2323 0.0059  -0.0297 -0.0173 861  LEU B CA  
15376 C C   . LEU B 863  ? 0.2884 0.2736 0.2677 0.0059  -0.0304 -0.0156 861  LEU B C   
15377 O O   . LEU B 863  ? 0.2637 0.2496 0.2464 0.0063  -0.0302 -0.0146 861  LEU B O   
15378 C CB  . LEU B 863  ? 0.2506 0.2369 0.2337 0.0057  -0.0324 -0.0177 861  LEU B CB  
15379 C CG  . LEU B 863  ? 0.2500 0.2373 0.2361 0.0057  -0.0317 -0.0191 861  LEU B CG  
15380 C CD1 . LEU B 863  ? 0.3064 0.2932 0.2931 0.0051  -0.0346 -0.0195 861  LEU B CD1 
15381 C CD2 . LEU B 863  ? 0.2848 0.2744 0.2766 0.0062  -0.0302 -0.0186 861  LEU B CD2 
15382 N N   . THR B 864  ? 0.2441 0.2273 0.2180 0.0054  -0.0313 -0.0153 862  THR B N   
15383 C CA  . THR B 864  ? 0.2563 0.2380 0.2279 0.0053  -0.0319 -0.0136 862  THR B CA  
15384 C C   . THR B 864  ? 0.2726 0.2548 0.2447 0.0053  -0.0293 -0.0130 862  THR B C   
15385 O O   . THR B 864  ? 0.2776 0.2594 0.2513 0.0055  -0.0295 -0.0117 862  THR B O   
15386 C CB  . THR B 864  ? 0.3189 0.2984 0.2839 0.0047  -0.0330 -0.0135 862  THR B CB  
15387 O OG1 . THR B 864  ? 0.3319 0.3107 0.2965 0.0047  -0.0359 -0.0139 862  THR B OG1 
15388 C CG2 . THR B 864  ? 0.3438 0.3216 0.3060 0.0045  -0.0333 -0.0115 862  THR B CG2 
15389 N N   . MET B 865  ? 0.2349 0.2180 0.2057 0.0049  -0.0268 -0.0140 863  MET B N   
15390 C CA  . MET B 865  ? 0.2513 0.2350 0.2224 0.0046  -0.0243 -0.0134 863  MET B CA  
15391 C C   . MET B 865  ? 0.2605 0.2457 0.2373 0.0052  -0.0237 -0.0134 863  MET B C   
15392 O O   . MET B 865  ? 0.2301 0.2149 0.2078 0.0051  -0.0230 -0.0124 863  MET B O   
15393 C CB  . MET B 865  ? 0.2387 0.2236 0.2075 0.0043  -0.0219 -0.0145 863  MET B CB  
15394 C CG  . MET B 865  ? 0.2569 0.2427 0.2257 0.0037  -0.0195 -0.0139 863  MET B CG  
15395 S SD  . MET B 865  ? 0.2985 0.2864 0.2653 0.0035  -0.0167 -0.0151 863  MET B SD  
15396 C CE  . MET B 865  ? 0.3344 0.3203 0.2944 0.0031  -0.0175 -0.0151 863  MET B CE  
15397 N N   . LEU B 866  ? 0.2346 0.2214 0.2151 0.0058  -0.0240 -0.0145 864  LEU B N   
15398 C CA  . LEU B 866  ? 0.2282 0.2165 0.2140 0.0064  -0.0233 -0.0146 864  LEU B CA  
15399 C C   . LEU B 866  ? 0.2379 0.2254 0.2257 0.0069  -0.0249 -0.0132 864  LEU B C   
15400 O O   . LEU B 866  ? 0.2336 0.2211 0.2234 0.0072  -0.0239 -0.0126 864  LEU B O   
15401 C CB  . LEU B 866  ? 0.2242 0.2139 0.2130 0.0067  -0.0237 -0.0158 864  LEU B CB  
15402 C CG  . LEU B 866  ? 0.2120 0.2034 0.2063 0.0073  -0.0232 -0.0158 864  LEU B CG  
15403 C CD1 . LEU B 866  ? 0.2451 0.2373 0.2401 0.0073  -0.0207 -0.0158 864  LEU B CD1 
15404 C CD2 . LEU B 866  ? 0.2597 0.2523 0.2567 0.0075  -0.0237 -0.0168 864  LEU B CD2 
15405 N N   . LYS B 867  ? 0.2387 0.2253 0.2259 0.0071  -0.0275 -0.0128 865  LYS B N   
15406 C CA  . LYS B 867  ? 0.2462 0.2322 0.2355 0.0079  -0.0291 -0.0115 865  LYS B CA  
15407 C C   . LYS B 867  ? 0.2696 0.2533 0.2560 0.0077  -0.0287 -0.0102 865  LYS B C   
15408 O O   . LYS B 867  ? 0.2559 0.2391 0.2445 0.0084  -0.0286 -0.0093 865  LYS B O   
15409 C CB  . LYS B 867  ? 0.2666 0.2525 0.2559 0.0080  -0.0321 -0.0112 865  LYS B CB  
15410 C CG  . LYS B 867  ? 0.3081 0.2963 0.3015 0.0081  -0.0326 -0.0124 865  LYS B CG  
15411 C CD  . LYS B 867  ? 0.2990 0.2869 0.2916 0.0079  -0.0356 -0.0124 865  LYS B CD  
15412 C CE  . LYS B 867  ? 0.4133 0.4032 0.4092 0.0075  -0.0360 -0.0136 865  LYS B CE  
15413 N NZ  . LYS B 867  ? 0.4435 0.4329 0.4380 0.0069  -0.0389 -0.0138 865  LYS B NZ  
15414 N N   . GLY B 868  ? 0.2476 0.2298 0.2286 0.0067  -0.0282 -0.0100 866  GLY B N   
15415 C CA  . GLY B 868  ? 0.2478 0.2277 0.2258 0.0062  -0.0276 -0.0086 866  GLY B CA  
15416 C C   . GLY B 868  ? 0.2562 0.2367 0.2361 0.0060  -0.0252 -0.0088 866  GLY B C   
15417 O O   . GLY B 868  ? 0.2702 0.2488 0.2501 0.0062  -0.0251 -0.0077 866  GLY B O   
15418 N N   . ALA B 869  ? 0.2420 0.2248 0.2233 0.0057  -0.0233 -0.0101 867  ALA B N   
15419 C CA  . ALA B 869  ? 0.2605 0.2440 0.2437 0.0055  -0.0212 -0.0103 867  ALA B CA  
15420 C C   . ALA B 869  ? 0.2167 0.2005 0.2046 0.0067  -0.0215 -0.0103 867  ALA B C   
15421 O O   . ALA B 869  ? 0.2356 0.2183 0.2241 0.0067  -0.0206 -0.0098 867  ALA B O   
15422 C CB  . ALA B 869  ? 0.2423 0.2283 0.2260 0.0051  -0.0193 -0.0117 867  ALA B CB  
15423 N N   . LEU B 870  ? 0.2240 0.2091 0.2150 0.0077  -0.0229 -0.0107 868  LEU B N   
15424 C CA  . LEU B 870  ? 0.2287 0.2145 0.2244 0.0089  -0.0230 -0.0106 868  LEU B CA  
15425 C C   . LEU B 870  ? 0.2299 0.2131 0.2250 0.0097  -0.0242 -0.0093 868  LEU B C   
15426 O O   . LEU B 870  ? 0.2549 0.2379 0.2526 0.0106  -0.0236 -0.0091 868  LEU B O   
15427 C CB  . LEU B 870  ? 0.2498 0.2378 0.2491 0.0096  -0.0243 -0.0112 868  LEU B CB  
15428 C CG  . LEU B 870  ? 0.2874 0.2777 0.2884 0.0093  -0.0230 -0.0126 868  LEU B CG  
15429 C CD1 . LEU B 870  ? 0.2810 0.2730 0.2851 0.0097  -0.0246 -0.0130 868  LEU B CD1 
15430 C CD2 . LEU B 870  ? 0.2872 0.2784 0.2908 0.0096  -0.0209 -0.0130 868  LEU B CD2 
15431 N N   . HIS B 871  ? 0.2267 0.2079 0.2184 0.0094  -0.0259 -0.0083 869  HIS B N   
15432 C CA  A HIS B 871  ? 0.2506 0.2290 0.2415 0.0102  -0.0271 -0.0068 869  HIS B CA  
15433 C CA  B HIS B 871  ? 0.2507 0.2291 0.2415 0.0102  -0.0271 -0.0068 869  HIS B CA  
15434 C C   . HIS B 871  ? 0.2706 0.2466 0.2595 0.0096  -0.0255 -0.0064 869  HIS B C   
15435 O O   . HIS B 871  ? 0.2994 0.2728 0.2883 0.0105  -0.0262 -0.0054 869  HIS B O   
15436 C CB  A HIS B 871  ? 0.2618 0.2386 0.2492 0.0100  -0.0294 -0.0058 869  HIS B CB  
15437 C CB  B HIS B 871  ? 0.2625 0.2392 0.2493 0.0098  -0.0293 -0.0058 869  HIS B CB  
15438 C CG  A HIS B 871  ? 0.3001 0.2785 0.2904 0.0111  -0.0318 -0.0057 869  HIS B CG  
15439 C CG  B HIS B 871  ? 0.3108 0.2842 0.2963 0.0106  -0.0308 -0.0041 869  HIS B CG  
15440 N ND1 A HIS B 871  ? 0.3110 0.2913 0.3010 0.0105  -0.0326 -0.0065 869  HIS B ND1 
15441 N ND1 B HIS B 871  ? 0.3588 0.3324 0.3475 0.0124  -0.0328 -0.0035 869  HIS B ND1 
15442 C CD2 A HIS B 871  ? 0.3488 0.3273 0.3422 0.0128  -0.0335 -0.0049 869  HIS B CD2 
15443 C CD2 B HIS B 871  ? 0.3335 0.3033 0.3147 0.0099  -0.0306 -0.0029 869  HIS B CD2 
15444 C CE1 A HIS B 871  ? 0.3513 0.3329 0.3443 0.0115  -0.0349 -0.0062 869  HIS B CE1 
15445 C CE1 B HIS B 871  ? 0.3124 0.2826 0.2989 0.0130  -0.0338 -0.0020 869  HIS B CE1 
15446 N NE2 A HIS B 871  ? 0.3127 0.2936 0.3081 0.0129  -0.0354 -0.0052 869  HIS B NE2 
15447 N NE2 B HIS B 871  ? 0.3423 0.3098 0.3240 0.0114  -0.0326 -0.0016 869  HIS B NE2 
15448 N N   . GLU B 872  ? 0.2299 0.2065 0.2171 0.0082  -0.0235 -0.0070 870  GLU B N   
15449 C CA  . GLU B 872  ? 0.2464 0.2209 0.2317 0.0072  -0.0221 -0.0066 870  GLU B CA  
15450 C C   . GLU B 872  ? 0.2401 0.2154 0.2287 0.0078  -0.0205 -0.0075 870  GLU B C   
15451 O O   . GLU B 872  ? 0.2657 0.2393 0.2530 0.0069  -0.0194 -0.0073 870  GLU B O   
15452 C CB  . GLU B 872  ? 0.2435 0.2183 0.2251 0.0052  -0.0208 -0.0067 870  GLU B CB  
15453 C CG  . GLU B 872  ? 0.2582 0.2319 0.2358 0.0047  -0.0221 -0.0058 870  GLU B CG  
15454 C CD  . GLU B 872  ? 0.2933 0.2629 0.2682 0.0048  -0.0236 -0.0041 870  GLU B CD  
15455 O OE1 . GLU B 872  ? 0.3221 0.2894 0.2969 0.0046  -0.0230 -0.0035 870  GLU B OE1 
15456 O OE2 . GLU B 872  ? 0.3095 0.2779 0.2819 0.0050  -0.0254 -0.0032 870  GLU B OE2 
15457 N N   . LEU B 873  ? 0.2488 0.2269 0.2418 0.0090  -0.0205 -0.0084 871  LEU B N   
15458 C CA  . LEU B 873  ? 0.2433 0.2224 0.2392 0.0095  -0.0189 -0.0093 871  LEU B CA  
15459 C C   . LEU B 873  ? 0.2612 0.2379 0.2585 0.0111  -0.0194 -0.0088 871  LEU B C   
15460 O O   . LEU B 873  ? 0.2761 0.2521 0.2743 0.0124  -0.0211 -0.0080 871  LEU B O   
15461 C CB  . LEU B 873  ? 0.2509 0.2337 0.2507 0.0101  -0.0185 -0.0104 871  LEU B CB  
15462 C CG  . LEU B 873  ? 0.2808 0.2658 0.2795 0.0089  -0.0178 -0.0112 871  LEU B CG  
15463 C CD1 . LEU B 873  ? 0.2967 0.2847 0.2993 0.0095  -0.0172 -0.0123 871  LEU B CD1 
15464 C CD2 . LEU B 873  ? 0.2695 0.2540 0.2654 0.0073  -0.0162 -0.0113 871  LEU B CD2 
15465 N N   . HIS B 874  ? 0.2452 0.2208 0.2427 0.0110  -0.0179 -0.0092 872  HIS B N   
15466 C CA  . HIS B 874  ? 0.2682 0.2415 0.2669 0.0127  -0.0180 -0.0090 872  HIS B CA  
15467 C C   . HIS B 874  ? 0.2430 0.2192 0.2461 0.0139  -0.0168 -0.0101 872  HIS B C   
15468 O O   . HIS B 874  ? 0.2342 0.2119 0.2376 0.0130  -0.0152 -0.0110 872  HIS B O   
15469 C CB  . HIS B 874  ? 0.2868 0.2562 0.2820 0.0115  -0.0171 -0.0087 872  HIS B CB  
15470 C CG  . HIS B 874  ? 0.2734 0.2395 0.2690 0.0131  -0.0171 -0.0086 872  HIS B CG  
15471 N ND1 . HIS B 874  ? 0.3662 0.3280 0.3585 0.0123  -0.0166 -0.0085 872  HIS B ND1 
15472 C CD2 . HIS B 874  ? 0.3373 0.3036 0.3361 0.0156  -0.0174 -0.0087 872  HIS B CD2 
15473 C CE1 . HIS B 874  ? 0.3690 0.3282 0.3622 0.0143  -0.0166 -0.0085 872  HIS B CE1 
15474 N NE2 . HIS B 874  ? 0.3623 0.3244 0.3596 0.0164  -0.0170 -0.0087 872  HIS B NE2 
15475 N N   . ILE B 875  ? 0.2417 0.2190 0.2482 0.0159  -0.0176 -0.0099 873  ILE B N   
15476 C CA  . ILE B 875  ? 0.2408 0.2209 0.2517 0.0172  -0.0166 -0.0107 873  ILE B CA  
15477 C C   . ILE B 875  ? 0.2589 0.2363 0.2700 0.0189  -0.0159 -0.0106 873  ILE B C   
15478 O O   . ILE B 875  ? 0.2537 0.2287 0.2644 0.0203  -0.0172 -0.0097 873  ILE B O   
15479 C CB  . ILE B 875  ? 0.2779 0.2614 0.2926 0.0183  -0.0179 -0.0104 873  ILE B CB  
15480 C CG1 . ILE B 875  ? 0.3422 0.3276 0.3560 0.0167  -0.0188 -0.0104 873  ILE B CG1 
15481 C CG2 . ILE B 875  ? 0.2709 0.2576 0.2903 0.0195  -0.0166 -0.0111 873  ILE B CG2 
15482 C CD1 . ILE B 875  ? 0.3828 0.3701 0.3989 0.0174  -0.0209 -0.0098 873  ILE B CD1 
15483 N N   . GLY B 876  ? 0.2196 0.1973 0.2315 0.0191  -0.0140 -0.0116 874  GLY B N   
15484 C CA  . GLY B 876  ? 0.2485 0.2235 0.2605 0.0209  -0.0133 -0.0118 874  GLY B CA  
15485 C C   . GLY B 876  ? 0.2242 0.1994 0.2361 0.0206  -0.0112 -0.0129 874  GLY B C   
15486 O O   . GLY B 876  ? 0.2237 0.2016 0.2362 0.0193  -0.0104 -0.0136 874  GLY B O   
15487 N N   . ARG B 877  ? 0.2487 0.2205 0.2596 0.0220  -0.0105 -0.0132 875  ARG B N   
15488 C CA  . ARG B 877  ? 0.2419 0.2131 0.2520 0.0218  -0.0086 -0.0144 875  ARG B CA  
15489 C C   . ARG B 877  ? 0.2467 0.2163 0.2528 0.0190  -0.0085 -0.0147 875  ARG B C   
15490 O O   . ARG B 877  ? 0.2628 0.2294 0.2658 0.0178  -0.0095 -0.0140 875  ARG B O   
15491 C CB  . ARG B 877  ? 0.2708 0.2378 0.2796 0.0239  -0.0081 -0.0146 875  ARG B CB  
15492 C CG  . ARG B 877  ? 0.2922 0.2592 0.3010 0.0244  -0.0061 -0.0159 875  ARG B CG  
15493 C CD  . ARG B 877  ? 0.3540 0.3166 0.3616 0.0268  -0.0055 -0.0162 875  ARG B CD  
15494 N NE  . ARG B 877  ? 0.3207 0.2773 0.3230 0.0256  -0.0059 -0.0164 875  ARG B NE  
15495 C CZ  . ARG B 877  ? 0.4287 0.3804 0.4287 0.0273  -0.0054 -0.0170 875  ARG B CZ  
15496 N NH1 . ARG B 877  ? 0.3846 0.3369 0.3873 0.0305  -0.0045 -0.0172 875  ARG B NH1 
15497 N NH2 . ARG B 877  ? 0.4328 0.3789 0.4277 0.0258  -0.0057 -0.0172 875  ARG B NH2 
15498 N N   . THR B 878  ? 0.2132 0.1852 0.2198 0.0180  -0.0071 -0.0155 876  THR B N   
15499 C CA  . THR B 878  ? 0.2381 0.2105 0.2423 0.0153  -0.0071 -0.0156 876  THR B CA  
15500 C C   . THR B 878  ? 0.2118 0.1802 0.2119 0.0139  -0.0067 -0.0161 876  THR B C   
15501 O O   . THR B 878  ? 0.2334 0.2027 0.2319 0.0117  -0.0066 -0.0162 876  THR B O   
15502 C CB  . THR B 878  ? 0.2410 0.2180 0.2476 0.0148  -0.0061 -0.0163 876  THR B CB  
15503 O OG1 . THR B 878  ? 0.2564 0.2338 0.2645 0.0162  -0.0047 -0.0170 876  THR B OG1 
15504 C CG2 . THR B 878  ? 0.2690 0.2496 0.2788 0.0153  -0.0069 -0.0158 876  THR B CG2 
15505 N N   . ASP B 879  ? 0.2269 0.1910 0.2254 0.0151  -0.0066 -0.0162 877  ASP B N   
15506 C CA  . ASP B 879  ? 0.2334 0.1932 0.2277 0.0137  -0.0064 -0.0167 877  ASP B CA  
15507 C C   . ASP B 879  ? 0.2502 0.2064 0.2412 0.0121  -0.0078 -0.0157 877  ASP B C   
15508 O O   . ASP B 879  ? 0.2695 0.2206 0.2570 0.0115  -0.0079 -0.0158 877  ASP B O   
15509 C CB  . ASP B 879  ? 0.2818 0.2380 0.2752 0.0157  -0.0055 -0.0176 877  ASP B CB  
15510 C CG  . ASP B 879  ? 0.3322 0.2856 0.3261 0.0182  -0.0062 -0.0170 877  ASP B CG  
15511 O OD1 . ASP B 879  ? 0.3517 0.3077 0.3484 0.0192  -0.0070 -0.0161 877  ASP B OD1 
15512 O OD2 . ASP B 879  ? 0.3351 0.2835 0.3265 0.0193  -0.0059 -0.0175 877  ASP B OD2 
15513 N N   . ARG B 880  ? 0.2551 0.2136 0.2470 0.0114  -0.0087 -0.0147 878  ARG B N   
15514 C CA  . ARG B 880  ? 0.2583 0.2142 0.2471 0.0095  -0.0098 -0.0136 878  ARG B CA  
15515 C C   . ARG B 880  ? 0.2426 0.2029 0.2320 0.0075  -0.0098 -0.0133 878  ARG B C   
15516 O O   . ARG B 880  ? 0.2479 0.2126 0.2404 0.0083  -0.0097 -0.0134 878  ARG B O   
15517 C CB  . ARG B 880  ? 0.2950 0.2488 0.2838 0.0111  -0.0112 -0.0124 878  ARG B CB  
15518 C CG  . ARG B 880  ? 0.3900 0.3387 0.3776 0.0132  -0.0115 -0.0125 878  ARG B CG  
15519 C CD  . ARG B 880  ? 0.4504 0.3978 0.4386 0.0149  -0.0130 -0.0112 878  ARG B CD  
15520 N NE  . ARG B 880  ? 0.6748 0.6179 0.6626 0.0175  -0.0132 -0.0112 878  ARG B NE  
15521 C CZ  . ARG B 880  ? 0.7353 0.6723 0.7194 0.0175  -0.0142 -0.0105 878  ARG B CZ  
15522 N NH1 . ARG B 880  ? 0.7449 0.6795 0.7253 0.0149  -0.0150 -0.0095 878  ARG B NH1 
15523 N NH2 . ARG B 880  ? 0.7175 0.6506 0.7014 0.0203  -0.0142 -0.0107 878  ARG B NH2 
15524 N N   . LEU B 881  ? 0.2420 0.2012 0.2285 0.0048  -0.0099 -0.0129 879  LEU B N   
15525 C CA  . LEU B 881  ? 0.2412 0.2045 0.2280 0.0029  -0.0097 -0.0126 879  LEU B CA  
15526 C C   . LEU B 881  ? 0.2298 0.1948 0.2174 0.0035  -0.0105 -0.0117 879  LEU B C   
15527 O O   . LEU B 881  ? 0.2480 0.2173 0.2372 0.0031  -0.0102 -0.0119 879  LEU B O   
15528 C CB  . LEU B 881  ? 0.2575 0.2190 0.2410 0.0000  -0.0097 -0.0122 879  LEU B CB  
15529 C CG  . LEU B 881  ? 0.2884 0.2543 0.2722 -0.0021 -0.0093 -0.0118 879  LEU B CG  
15530 C CD1 . LEU B 881  ? 0.2848 0.2552 0.2712 -0.0019 -0.0082 -0.0129 879  LEU B CD1 
15531 C CD2 . LEU B 881  ? 0.2856 0.2492 0.2660 -0.0050 -0.0094 -0.0110 879  LEU B CD2 
15532 N N   . SER B 882  ? 0.2151 0.1766 0.2014 0.0045  -0.0117 -0.0108 880  SER B N   
15533 C CA  . SER B 882  ? 0.2280 0.1907 0.2146 0.0050  -0.0128 -0.0099 880  SER B CA  
15534 C C   . SER B 882  ? 0.2575 0.2238 0.2481 0.0071  -0.0129 -0.0105 880  SER B C   
15535 O O   . SER B 882  ? 0.2521 0.2197 0.2430 0.0075  -0.0139 -0.0098 880  SER B O   
15536 C CB  . SER B 882  ? 0.2616 0.2192 0.2456 0.0055  -0.0141 -0.0087 880  SER B CB  
15537 O OG  . SER B 882  ? 0.3114 0.2671 0.2971 0.0081  -0.0144 -0.0090 880  SER B OG  
15538 N N   . VAL B 883  ? 0.2449 0.2128 0.2384 0.0085  -0.0120 -0.0115 881  VAL B N   
15539 C CA  . VAL B 883  ? 0.2287 0.2000 0.2261 0.0103  -0.0122 -0.0119 881  VAL B CA  
15540 C C   . VAL B 883  ? 0.2437 0.2195 0.2425 0.0093  -0.0115 -0.0125 881  VAL B C   
15541 O O   . VAL B 883  ? 0.2719 0.2490 0.2704 0.0081  -0.0104 -0.0131 881  VAL B O   
15542 C CB  . VAL B 883  ? 0.2289 0.2000 0.2288 0.0124  -0.0114 -0.0126 881  VAL B CB  
15543 C CG1 . VAL B 883  ? 0.2668 0.2422 0.2710 0.0138  -0.0113 -0.0130 881  VAL B CG1 
15544 C CG2 . VAL B 883  ? 0.2673 0.2341 0.2662 0.0139  -0.0122 -0.0120 881  VAL B CG2 
15545 N N   . ASP B 884  ? 0.2204 0.1984 0.2205 0.0098  -0.0124 -0.0122 882  ASP B N   
15546 C CA  . ASP B 884  ? 0.2228 0.2046 0.2241 0.0090  -0.0120 -0.0127 882  ASP B CA  
15547 C C   . ASP B 884  ? 0.2759 0.2607 0.2812 0.0104  -0.0117 -0.0135 882  ASP B C   
15548 O O   . ASP B 884  ? 0.3114 0.2987 0.3177 0.0098  -0.0106 -0.0142 882  ASP B O   
15549 C CB  . ASP B 884  ? 0.2412 0.2234 0.2410 0.0085  -0.0133 -0.0121 882  ASP B CB  
15550 C CG  . ASP B 884  ? 0.2619 0.2413 0.2576 0.0070  -0.0136 -0.0112 882  ASP B CG  
15551 O OD1 . ASP B 884  ? 0.2605 0.2402 0.2546 0.0055  -0.0124 -0.0114 882  ASP B OD1 
15552 O OD2 . ASP B 884  ? 0.2551 0.2322 0.2491 0.0073  -0.0150 -0.0102 882  ASP B OD2 
15553 N N   . VAL B 885  ? 0.2408 0.2255 0.2485 0.0121  -0.0125 -0.0132 883  VAL B N   
15554 C CA  . VAL B 885  ? 0.2502 0.2379 0.2620 0.0132  -0.0122 -0.0137 883  VAL B CA  
15555 C C   . VAL B 885  ? 0.2143 0.2011 0.2281 0.0149  -0.0116 -0.0137 883  VAL B C   
15556 O O   . VAL B 885  ? 0.2290 0.2136 0.2425 0.0160  -0.0125 -0.0130 883  VAL B O   
15557 C CB  . VAL B 885  ? 0.2436 0.2329 0.2570 0.0136  -0.0139 -0.0132 883  VAL B CB  
15558 C CG1 . VAL B 885  ? 0.2657 0.2582 0.2835 0.0145  -0.0137 -0.0136 883  VAL B CG1 
15559 C CG2 . VAL B 885  ? 0.3099 0.2996 0.3206 0.0121  -0.0145 -0.0132 883  VAL B CG2 
15560 N N   . GLY B 886  ? 0.2276 0.2161 0.2433 0.0152  -0.0101 -0.0145 884  GLY B N   
15561 C CA  . GLY B 886  ? 0.2197 0.2076 0.2372 0.0169  -0.0092 -0.0147 884  GLY B CA  
15562 C C   . GLY B 886  ? 0.2031 0.1940 0.2251 0.0183  -0.0094 -0.0145 884  GLY B C   
15563 O O   . GLY B 886  ? 0.2185 0.2116 0.2422 0.0181  -0.0106 -0.0141 884  GLY B O   
15564 N N   . PRO B 887  ? 0.1915 0.1829 0.2156 0.0198  -0.0081 -0.0148 885  PRO B N   
15565 C CA  . PRO B 887  ? 0.1833 0.1778 0.2122 0.0213  -0.0081 -0.0145 885  PRO B CA  
15566 C C   . PRO B 887  ? 0.1768 0.1749 0.2080 0.0204  -0.0073 -0.0148 885  PRO B C   
15567 O O   . PRO B 887  ? 0.1862 0.1843 0.2156 0.0191  -0.0065 -0.0154 885  PRO B O   
15568 C CB  . PRO B 887  ? 0.1840 0.1771 0.2132 0.0232  -0.0066 -0.0148 885  PRO B CB  
15569 C CG  . PRO B 887  ? 0.1972 0.1876 0.2224 0.0220  -0.0053 -0.0156 885  PRO B CG  
15570 C CD  . PRO B 887  ? 0.1998 0.1882 0.2215 0.0202  -0.0067 -0.0154 885  PRO B CD  
15571 N N   . VAL B 888  ? 0.1859 0.1873 0.2215 0.0212  -0.0077 -0.0144 886  VAL B N   
15572 C CA  . VAL B 888  ? 0.1910 0.1956 0.2294 0.0207  -0.0066 -0.0147 886  VAL B CA  
15573 C C   . VAL B 888  ? 0.2096 0.2144 0.2490 0.0220  -0.0044 -0.0150 886  VAL B C   
15574 O O   . VAL B 888  ? 0.1997 0.2030 0.2389 0.0237  -0.0040 -0.0149 886  VAL B O   
15575 C CB  . VAL B 888  ? 0.2250 0.2330 0.2676 0.0206  -0.0080 -0.0140 886  VAL B CB  
15576 C CG1 . VAL B 888  ? 0.2204 0.2276 0.2611 0.0192  -0.0101 -0.0139 886  VAL B CG1 
15577 C CG2 . VAL B 888  ? 0.3068 0.3163 0.3530 0.0226  -0.0084 -0.0133 886  VAL B CG2 
15578 N N   . ILE B 889  ? 0.1971 0.2036 0.2372 0.0213  -0.0030 -0.0154 887  ILE B N   
15579 C CA  . ILE B 889  ? 0.1879 0.1936 0.2272 0.0221  -0.0007 -0.0159 887  ILE B CA  
15580 C C   . ILE B 889  ? 0.1927 0.2002 0.2355 0.0242  0.0003  -0.0155 887  ILE B C   
15581 O O   . ILE B 889  ? 0.1935 0.1991 0.2348 0.0256  0.0018  -0.0160 887  ILE B O   
15582 C CB  . ILE B 889  ? 0.1972 0.2041 0.2359 0.0208  0.0005  -0.0163 887  ILE B CB  
15583 C CG1 . ILE B 889  ? 0.2004 0.2060 0.2372 0.0215  0.0026  -0.0169 887  ILE B CG1 
15584 C CG2 . ILE B 889  ? 0.2093 0.2200 0.2523 0.0203  0.0004  -0.0157 887  ILE B CG2 
15585 C CD1 . ILE B 889  ? 0.1917 0.1931 0.2239 0.0215  0.0026  -0.0175 887  ILE B CD1 
15586 N N   . THR B 890  ? 0.1843 0.1955 0.2318 0.0246  -0.0003 -0.0148 888  THR B N   
15587 C CA  . THR B 890  ? 0.1924 0.2061 0.2439 0.0266  0.0009  -0.0144 888  THR B CA  
15588 C C   . THR B 890  ? 0.1968 0.2134 0.2527 0.0271  -0.0011 -0.0134 888  THR B C   
15589 O O   . THR B 890  ? 0.2004 0.2174 0.2564 0.0256  -0.0031 -0.0131 888  THR B O   
15590 C CB  . THR B 890  ? 0.2305 0.2475 0.2847 0.0262  0.0029  -0.0143 888  THR B CB  
15591 O OG1 . THR B 890  ? 0.2258 0.2453 0.2820 0.0243  0.0017  -0.0138 888  THR B OG1 
15592 C CG2 . THR B 890  ? 0.2157 0.2303 0.2658 0.0259  0.0049  -0.0152 888  THR B CG2 
15593 N N   . SER B 891  ? 0.2174 0.2361 0.2769 0.0292  -0.0003 -0.0129 889  SER B N   
15594 C CA  A SER B 891  ? 0.2011 0.2235 0.2656 0.0298  -0.0021 -0.0119 889  SER B CA  
15595 C CA  B SER B 891  ? 0.2009 0.2232 0.2654 0.0298  -0.0021 -0.0119 889  SER B CA  
15596 C CA  C SER B 891  ? 0.2013 0.2236 0.2658 0.0298  -0.0021 -0.0119 889  SER B CA  
15597 C C   . SER B 891  ? 0.2079 0.2344 0.2761 0.0279  -0.0025 -0.0113 889  SER B C   
15598 O O   . SER B 891  ? 0.2114 0.2397 0.2818 0.0270  -0.0049 -0.0107 889  SER B O   
15599 C CB  A SER B 891  ? 0.2181 0.2425 0.2863 0.0327  -0.0008 -0.0115 889  SER B CB  
15600 C CB  B SER B 891  ? 0.2182 0.2425 0.2863 0.0327  -0.0009 -0.0114 889  SER B CB  
15601 C CB  C SER B 891  ? 0.2183 0.2427 0.2864 0.0327  -0.0009 -0.0115 889  SER B CB  
15602 O OG  A SER B 891  ? 0.2390 0.2590 0.3037 0.0346  -0.0007 -0.0119 889  SER B OG  
15603 O OG  B SER B 891  ? 0.2217 0.2493 0.2927 0.0331  0.0017  -0.0115 889  SER B OG  
15604 O OG  C SER B 891  ? 0.2390 0.2667 0.3119 0.0334  -0.0029 -0.0104 889  SER B OG  
15605 N N   . GLU B 892  ? 0.1928 0.2207 0.2615 0.0271  -0.0003 -0.0116 890  GLU B N   
15606 C CA  . GLU B 892  ? 0.2071 0.2384 0.2787 0.0251  -0.0007 -0.0111 890  GLU B CA  
15607 C C   . GLU B 892  ? 0.2075 0.2366 0.2761 0.0228  -0.0028 -0.0114 890  GLU B C   
15608 O O   . GLU B 892  ? 0.2260 0.2572 0.2972 0.0214  -0.0046 -0.0108 890  GLU B O   
15609 C CB  . GLU B 892  ? 0.2462 0.2784 0.3178 0.0246  0.0021  -0.0113 890  GLU B CB  
15610 N N   . ALA B 893  ? 0.2004 0.2252 0.2635 0.0224  -0.0026 -0.0123 891  ALA B N   
15611 C CA  . ALA B 893  ? 0.2028 0.2256 0.2630 0.0205  -0.0044 -0.0126 891  ALA B CA  
15612 C C   . ALA B 893  ? 0.1951 0.2177 0.2557 0.0206  -0.0071 -0.0122 891  ALA B C   
15613 O O   . ALA B 893  ? 0.2130 0.2363 0.2740 0.0191  -0.0090 -0.0120 891  ALA B O   
15614 C CB  . ALA B 893  ? 0.2360 0.2548 0.2906 0.0201  -0.0036 -0.0135 891  ALA B CB  
15615 N N   . LYS B 894  ? 0.1907 0.2122 0.2511 0.0224  -0.0074 -0.0120 892  LYS B N   
15616 C CA  . LYS B 894  ? 0.2121 0.2334 0.2728 0.0228  -0.0100 -0.0114 892  LYS B CA  
15617 C C   . LYS B 894  ? 0.2011 0.2268 0.2672 0.0224  -0.0116 -0.0106 892  LYS B C   
15618 O O   . LYS B 894  ? 0.2156 0.2413 0.2814 0.0211  -0.0140 -0.0103 892  LYS B O   
15619 C CB  . LYS B 894  ? 0.2196 0.2390 0.2797 0.0251  -0.0098 -0.0112 892  LYS B CB  
15620 C CG  . LYS B 894  ? 0.2143 0.2333 0.2747 0.0257  -0.0125 -0.0105 892  LYS B CG  
15621 C CD  . LYS B 894  ? 0.2867 0.3034 0.3461 0.0282  -0.0121 -0.0103 892  LYS B CD  
15622 C CE  . LYS B 894  ? 0.3816 0.3992 0.4432 0.0294  -0.0146 -0.0092 892  LYS B CE  
15623 N NZ  . LYS B 894  ? 0.4362 0.4496 0.4929 0.0287  -0.0166 -0.0091 892  LYS B NZ  
15624 N N   . ASP B 895  ? 0.2059 0.2353 0.2769 0.0233  -0.0101 -0.0100 893  ASP B N   
15625 C CA  . ASP B 895  ? 0.2102 0.2443 0.2868 0.0227  -0.0115 -0.0091 893  ASP B CA  
15626 C C   . ASP B 895  ? 0.2184 0.2529 0.2947 0.0199  -0.0125 -0.0093 893  ASP B C   
15627 O O   . ASP B 895  ? 0.2314 0.2678 0.3099 0.0188  -0.0149 -0.0088 893  ASP B O   
15628 C CB  . ASP B 895  ? 0.2324 0.2707 0.3141 0.0240  -0.0092 -0.0086 893  ASP B CB  
15629 C CG  . ASP B 895  ? 0.2739 0.3125 0.3571 0.0270  -0.0086 -0.0082 893  ASP B CG  
15630 O OD1 . ASP B 895  ? 0.3129 0.3492 0.3942 0.0280  -0.0104 -0.0081 893  ASP B OD1 
15631 O OD2 . ASP B 895  ? 0.3039 0.3450 0.3899 0.0285  -0.0061 -0.0081 893  ASP B OD2 
15632 N N   . ASN B 896  ? 0.1980 0.2307 0.2714 0.0189  -0.0107 -0.0101 894  ASN B N   
15633 C CA  . ASN B 896  ? 0.2050 0.2376 0.2778 0.0164  -0.0114 -0.0103 894  ASN B CA  
15634 C C   . ASN B 896  ? 0.2282 0.2578 0.2972 0.0154  -0.0140 -0.0108 894  ASN B C   
15635 O O   . ASN B 896  ? 0.2185 0.2490 0.2886 0.0137  -0.0160 -0.0106 894  ASN B O   
15636 C CB  . ASN B 896  ? 0.2225 0.2534 0.2925 0.0159  -0.0089 -0.0110 894  ASN B CB  
15637 C CG  . ASN B 896  ? 0.3529 0.3831 0.4219 0.0137  -0.0094 -0.0112 894  ASN B CG  
15638 O OD1 . ASN B 896  ? 0.3832 0.4109 0.4490 0.0126  -0.0112 -0.0118 894  ASN B OD1 
15639 N ND2 . ASN B 896  ? 0.4957 0.5278 0.5670 0.0129  -0.0078 -0.0109 894  ASN B ND2 
15640 N N   . ILE B 897  ? 0.2026 0.2288 0.2670 0.0162  -0.0139 -0.0113 895  ILE B N   
15641 C CA  . ILE B 897  ? 0.2071 0.2304 0.2676 0.0153  -0.0161 -0.0117 895  ILE B CA  
15642 C C   . ILE B 897  ? 0.2020 0.2269 0.2648 0.0156  -0.0188 -0.0110 895  ILE B C   
15643 O O   . ILE B 897  ? 0.2133 0.2378 0.2753 0.0141  -0.0210 -0.0111 895  ILE B O   
15644 C CB  . ILE B 897  ? 0.2059 0.2255 0.2614 0.0162  -0.0152 -0.0123 895  ILE B CB  
15645 C CG1 . ILE B 897  ? 0.1941 0.2122 0.2471 0.0158  -0.0129 -0.0131 895  ILE B CG1 
15646 C CG2 . ILE B 897  ? 0.2193 0.2363 0.2710 0.0156  -0.0174 -0.0125 895  ILE B CG2 
15647 C CD1 . ILE B 897  ? 0.2013 0.2167 0.2509 0.0169  -0.0116 -0.0134 895  ILE B CD1 
15648 N N   . GLU B 898  ? 0.2027 0.2293 0.2685 0.0174  -0.0187 -0.0102 896  GLU B N   
15649 C CA  . GLU B 898  ? 0.1901 0.2184 0.2583 0.0179  -0.0215 -0.0093 896  GLU B CA  
15650 C C   . GLU B 898  ? 0.1915 0.2238 0.2645 0.0164  -0.0229 -0.0088 896  GLU B C   
15651 O O   . GLU B 898  ? 0.2156 0.2484 0.2890 0.0156  -0.0258 -0.0084 896  GLU B O   
15652 C CB  . GLU B 898  ? 0.2373 0.2665 0.3077 0.0205  -0.0210 -0.0086 896  GLU B CB  
15653 C CG  . GLU B 898  ? 0.2476 0.2721 0.3126 0.0215  -0.0205 -0.0090 896  GLU B CG  
15654 C CD  . GLU B 898  ? 0.3592 0.3837 0.4257 0.0242  -0.0199 -0.0084 896  GLU B CD  
15655 O OE1 . GLU B 898  ? 0.3805 0.4089 0.4523 0.0255  -0.0192 -0.0078 896  GLU B OE1 
15656 O OE2 . GLU B 898  ? 0.4325 0.4531 0.4948 0.0250  -0.0202 -0.0085 896  GLU B OE2 
15657 N N   . LYS B 899  ? 0.1937 0.2287 0.2701 0.0158  -0.0210 -0.0087 897  LYS B N   
15658 C CA  . LYS B 899  ? 0.2232 0.2617 0.3040 0.0141  -0.0224 -0.0082 897  LYS B CA  
15659 C C   . LYS B 899  ? 0.1971 0.2329 0.2743 0.0117  -0.0243 -0.0089 897  LYS B C   
15660 O O   . LYS B 899  ? 0.2032 0.2405 0.2823 0.0104  -0.0270 -0.0085 897  LYS B O   
15661 C CB  . LYS B 899  ? 0.2394 0.2807 0.3238 0.0137  -0.0197 -0.0079 897  LYS B CB  
15662 C CG  . LYS B 899  ? 0.2573 0.3023 0.3464 0.0116  -0.0210 -0.0073 897  LYS B CG  
15663 C CD  . LYS B 899  ? 0.3702 0.4188 0.4637 0.0115  -0.0183 -0.0066 897  LYS B CD  
15664 C CE  . LYS B 899  ? 0.4189 0.4648 0.5091 0.0099  -0.0166 -0.0074 897  LYS B CE  
15665 N NZ  . LYS B 899  ? 0.3846 0.4343 0.4795 0.0090  -0.0147 -0.0065 897  LYS B NZ  
15666 N N   . HIS B 900  ? 0.2021 0.2338 0.2739 0.0113  -0.0231 -0.0100 898  HIS B N   
15667 C CA  . HIS B 900  ? 0.2015 0.2304 0.2694 0.0094  -0.0248 -0.0108 898  HIS B CA  
15668 C C   . HIS B 900  ? 0.1997 0.2269 0.2649 0.0095  -0.0275 -0.0108 898  HIS B C   
15669 O O   . HIS B 900  ? 0.2087 0.2355 0.2733 0.0080  -0.0300 -0.0110 898  HIS B O   
15670 C CB  . HIS B 900  ? 0.2004 0.2257 0.2634 0.0093  -0.0227 -0.0119 898  HIS B CB  
15671 C CG  . HIS B 900  ? 0.1979 0.2198 0.2561 0.0079  -0.0241 -0.0129 898  HIS B CG  
15672 N ND1 . HIS B 900  ? 0.2491 0.2707 0.3076 0.0060  -0.0253 -0.0132 898  HIS B ND1 
15673 C CD2 . HIS B 900  ? 0.2267 0.2453 0.2796 0.0082  -0.0246 -0.0135 898  HIS B CD2 
15674 C CE1 . HIS B 900  ? 0.2250 0.2431 0.2784 0.0054  -0.0264 -0.0142 898  HIS B CE1 
15675 N NE2 . HIS B 900  ? 0.2230 0.2395 0.2731 0.0067  -0.0259 -0.0144 898  HIS B NE2 
15676 N N   . ILE B 901  ? 0.2053 0.2310 0.2683 0.0113  -0.0272 -0.0107 899  ILE B N   
15677 C CA  . ILE B 901  ? 0.2059 0.2297 0.2659 0.0115  -0.0297 -0.0105 899  ILE B CA  
15678 C C   . ILE B 901  ? 0.2093 0.2363 0.2736 0.0112  -0.0326 -0.0096 899  ILE B C   
15679 O O   . ILE B 901  ? 0.2276 0.2536 0.2899 0.0100  -0.0353 -0.0097 899  ILE B O   
15680 C CB  . ILE B 901  ? 0.2080 0.2298 0.2655 0.0135  -0.0287 -0.0103 899  ILE B CB  
15681 C CG1 . ILE B 901  ? 0.1992 0.2176 0.2519 0.0133  -0.0264 -0.0113 899  ILE B CG1 
15682 C CG2 . ILE B 901  ? 0.2201 0.2403 0.2750 0.0138  -0.0315 -0.0098 899  ILE B CG2 
15683 C CD1 . ILE B 901  ? 0.2375 0.2541 0.2883 0.0151  -0.0250 -0.0111 899  ILE B CD1 
15684 N N   . GLU B 902  ? 0.2355 0.2667 0.3058 0.0123  -0.0320 -0.0086 900  GLU B N   
15685 C CA  . GLU B 902  ? 0.2395 0.2745 0.3147 0.0121  -0.0347 -0.0075 900  GLU B CA  
15686 C C   . GLU B 902  ? 0.2098 0.2464 0.2870 0.0095  -0.0362 -0.0077 900  GLU B C   
15687 O O   . GLU B 902  ? 0.2549 0.2930 0.3337 0.0086  -0.0393 -0.0072 900  GLU B O   
15688 C CB  . GLU B 902  ? 0.2509 0.2903 0.3322 0.0142  -0.0334 -0.0064 900  GLU B CB  
15689 C CG  . GLU B 902  ? 0.3416 0.3790 0.4209 0.0169  -0.0326 -0.0061 900  GLU B CG  
15690 C CD  . GLU B 902  ? 0.4333 0.4678 0.5085 0.0172  -0.0355 -0.0059 900  GLU B CD  
15691 O OE1 . GLU B 902  ? 0.4011 0.4379 0.4788 0.0167  -0.0386 -0.0051 900  GLU B OE1 
15692 O OE2 . GLU B 902  ? 0.4213 0.4513 0.4909 0.0178  -0.0347 -0.0064 900  GLU B OE2 
15693 N N   . ARG B 903  ? 0.2271 0.2632 0.3040 0.0083  -0.0341 -0.0084 901  ARG B N   
15694 C CA  . ARG B 903  ? 0.2574 0.2940 0.3353 0.0056  -0.0356 -0.0086 901  ARG B CA  
15695 C C   . ARG B 903  ? 0.2648 0.2971 0.3368 0.0043  -0.0381 -0.0096 901  ARG B C   
15696 O O   . ARG B 903  ? 0.2751 0.3081 0.3481 0.0026  -0.0410 -0.0095 901  ARG B O   
15697 C CB  . ARG B 903  ? 0.2773 0.3137 0.3557 0.0047  -0.0329 -0.0091 901  ARG B CB  
15698 C CG  . ARG B 903  ? 0.3932 0.4300 0.4730 0.0019  -0.0343 -0.0092 901  ARG B CG  
15699 C CD  . ARG B 903  ? 0.4363 0.4728 0.5167 0.0010  -0.0316 -0.0095 901  ARG B CD  
15700 N NE  . ARG B 903  ? 0.5179 0.5493 0.5919 0.0009  -0.0304 -0.0109 901  ARG B NE  
15701 C CZ  . ARG B 903  ? 0.5388 0.5669 0.6094 -0.0009 -0.0317 -0.0118 901  ARG B CZ  
15702 N NH1 . ARG B 903  ? 0.5239 0.5527 0.5963 -0.0030 -0.0344 -0.0116 901  ARG B NH1 
15703 N NH2 . ARG B 903  ? 0.5223 0.5461 0.5874 -0.0006 -0.0303 -0.0130 901  ARG B NH2 
15704 N N   . MET B 904  ? 0.2412 0.2692 0.3071 0.0051  -0.0369 -0.0106 902  MET B N   
15705 C CA  . MET B 904  ? 0.2200 0.2439 0.2799 0.0041  -0.0390 -0.0116 902  MET B CA  
15706 C C   . MET B 904  ? 0.2773 0.3018 0.3371 0.0045  -0.0422 -0.0108 902  MET B C   
15707 O O   . MET B 904  ? 0.2798 0.3031 0.3376 0.0029  -0.0450 -0.0112 902  MET B O   
15708 C CB  . MET B 904  ? 0.2564 0.2763 0.3104 0.0051  -0.0368 -0.0125 902  MET B CB  
15709 C CG  . MET B 904  ? 0.2515 0.2705 0.3050 0.0048  -0.0338 -0.0133 902  MET B CG  
15710 S SD  . MET B 904  ? 0.3796 0.3966 0.4313 0.0023  -0.0350 -0.0144 902  MET B SD  
15711 C CE  . MET B 904  ? 0.3668 0.3881 0.4258 0.0013  -0.0345 -0.0134 902  MET B CE  
15712 N N   . ARG B 905  ? 0.2529 0.2791 0.3146 0.0065  -0.0418 -0.0098 903  ARG B N   
15713 C CA  . ARG B 905  ? 0.2801 0.3070 0.3420 0.0071  -0.0450 -0.0089 903  ARG B CA  
15714 C C   . ARG B 905  ? 0.3006 0.3313 0.3676 0.0056  -0.0478 -0.0082 903  ARG B C   
15715 O O   . ARG B 905  ? 0.2942 0.3241 0.3593 0.0046  -0.0511 -0.0081 903  ARG B O   
15716 C CB  . ARG B 905  ? 0.3024 0.3305 0.3661 0.0097  -0.0439 -0.0078 903  ARG B CB  
15717 C CG  . ARG B 905  ? 0.3930 0.4194 0.4538 0.0107  -0.0465 -0.0071 903  ARG B CG  
15718 C CD  . ARG B 905  ? 0.4059 0.4340 0.4697 0.0133  -0.0458 -0.0059 903  ARG B CD  
15719 N NE  . ARG B 905  ? 0.3827 0.4091 0.4451 0.0147  -0.0421 -0.0064 903  ARG B NE  
15720 C CZ  . ARG B 905  ? 0.3347 0.3567 0.3914 0.0153  -0.0411 -0.0068 903  ARG B CZ  
15721 N NH1 . ARG B 905  ? 0.3886 0.4074 0.4400 0.0147  -0.0431 -0.0068 903  ARG B NH1 
15722 N NH2 . ARG B 905  ? 0.3709 0.3918 0.4271 0.0165  -0.0380 -0.0071 903  ARG B NH2 
15723 N N   . GLY B 906  ? 0.2604 0.2954 0.3338 0.0054  -0.0466 -0.0076 904  GLY B N   
15724 C CA  . GLY B 906  ? 0.2751 0.3145 0.3543 0.0039  -0.0492 -0.0067 904  GLY B CA  
15725 C C   . GLY B 906  ? 0.3153 0.3527 0.3921 0.0009  -0.0512 -0.0077 904  GLY B C   
15726 O O   . GLY B 906  ? 0.3508 0.3905 0.4304 -0.0006 -0.0545 -0.0071 904  GLY B O   
15727 N N   . LEU B 907  ? 0.3173 0.3504 0.3891 0.0000  -0.0494 -0.0091 905  LEU B N   
15728 C CA  . LEU B 907  ? 0.3491 0.3790 0.4173 -0.0025 -0.0512 -0.0103 905  LEU B CA  
15729 C C   . LEU B 907  ? 0.3201 0.3458 0.3815 -0.0027 -0.0537 -0.0111 905  LEU B C   
15730 O O   . LEU B 907  ? 0.3407 0.3632 0.3983 -0.0046 -0.0554 -0.0122 905  LEU B O   
15731 C CB  . LEU B 907  ? 0.3713 0.3982 0.4368 -0.0031 -0.0482 -0.0115 905  LEU B CB  
15732 C CG  . LEU B 907  ? 0.4275 0.4580 0.4990 -0.0036 -0.0460 -0.0108 905  LEU B CG  
15733 C CD1 . LEU B 907  ? 0.4882 0.5154 0.5565 -0.0040 -0.0432 -0.0119 905  LEU B CD1 
15734 C CD2 . LEU B 907  ? 0.4253 0.4593 0.5021 -0.0059 -0.0485 -0.0101 905  LEU B CD2 
15735 N N   . GLY B 908  ? 0.2915 0.3169 0.3512 -0.0007 -0.0540 -0.0105 906  GLY B N   
15736 C CA  . GLY B 908  ? 0.3239 0.3457 0.3773 -0.0007 -0.0564 -0.0110 906  GLY B CA  
15737 C C   . GLY B 908  ? 0.3801 0.3967 0.4261 0.0000  -0.0544 -0.0123 906  GLY B C   
15738 O O   . GLY B 908  ? 0.3187 0.3320 0.3588 -0.0002 -0.0561 -0.0128 906  GLY B O   
15739 N N   . ARG B 909  ? 0.2772 0.2933 0.3232 0.0008  -0.0507 -0.0127 907  ARG B N   
15740 C CA  . ARG B 909  ? 0.2622 0.2740 0.3016 0.0014  -0.0487 -0.0138 907  ARG B CA  
15741 C C   . ARG B 909  ? 0.2755 0.2866 0.3126 0.0033  -0.0485 -0.0131 907  ARG B C   
15742 O O   . ARG B 909  ? 0.3198 0.3337 0.3611 0.0047  -0.0484 -0.0117 907  ARG B O   
15743 C CB  . ARG B 909  ? 0.2778 0.2895 0.3182 0.0019  -0.0449 -0.0144 907  ARG B CB  
15744 C CG  . ARG B 909  ? 0.3405 0.3535 0.3844 0.0003  -0.0446 -0.0148 907  ARG B CG  
15745 C CD  . ARG B 909  ? 0.4859 0.4952 0.5251 -0.0014 -0.0459 -0.0162 907  ARG B CD  
15746 N NE  . ARG B 909  ? 0.5643 0.5748 0.6073 -0.0032 -0.0462 -0.0163 907  ARG B NE  
15747 C CZ  . ARG B 909  ? 0.6558 0.6633 0.6959 -0.0049 -0.0474 -0.0175 907  ARG B CZ  
15748 N NH1 . ARG B 909  ? 0.7399 0.7430 0.7733 -0.0050 -0.0482 -0.0189 907  ARG B NH1 
15749 N NH2 . ARG B 909  ? 0.6750 0.6838 0.7190 -0.0066 -0.0477 -0.0174 907  ARG B NH2 
15750 N N   . LYS B 910  ? 0.2729 0.2800 0.3031 0.0034  -0.0482 -0.0139 908  LYS B N   
15751 C CA  . LYS B 910  ? 0.2854 0.2913 0.3128 0.0049  -0.0478 -0.0131 908  LYS B CA  
15752 C C   . LYS B 910  ? 0.2666 0.2731 0.2957 0.0063  -0.0443 -0.0129 908  LYS B C   
15753 O O   . LYS B 910  ? 0.2693 0.2744 0.2966 0.0060  -0.0418 -0.0139 908  LYS B O   
15754 C CB  . LYS B 910  ? 0.3135 0.3150 0.3331 0.0044  -0.0483 -0.0140 908  LYS B CB  
15755 C CG  . LYS B 910  ? 0.3808 0.3809 0.3972 0.0057  -0.0485 -0.0130 908  LYS B CG  
15756 C CD  . LYS B 910  ? 0.4675 0.4636 0.4760 0.0051  -0.0484 -0.0138 908  LYS B CD  
15757 C CE  . LYS B 910  ? 0.5916 0.5862 0.5968 0.0061  -0.0489 -0.0126 908  LYS B CE  
15758 N NZ  . LYS B 910  ? 0.5790 0.5701 0.5770 0.0058  -0.0477 -0.0133 908  LYS B NZ  
15759 N N   . VAL B 911  ? 0.2685 0.2768 0.3008 0.0078  -0.0441 -0.0116 909  VAL B N   
15760 C CA  . VAL B 911  ? 0.2545 0.2632 0.2883 0.0092  -0.0410 -0.0113 909  VAL B CA  
15761 C C   . VAL B 911  ? 0.2636 0.2702 0.2941 0.0105  -0.0412 -0.0105 909  VAL B C   
15762 O O   . VAL B 911  ? 0.2770 0.2841 0.3085 0.0112  -0.0435 -0.0094 909  VAL B O   
15763 C CB  . VAL B 911  ? 0.2309 0.2437 0.2720 0.0100  -0.0404 -0.0106 909  VAL B CB  
15764 C CG1 . VAL B 911  ? 0.2503 0.2631 0.2924 0.0116  -0.0374 -0.0103 909  VAL B CG1 
15765 C CG2 . VAL B 911  ? 0.2595 0.2744 0.3038 0.0085  -0.0403 -0.0112 909  VAL B CG2 
15766 N N   . GLU B 912  ? 0.2386 0.2426 0.2652 0.0108  -0.0388 -0.0110 910  GLU B N   
15767 C CA  . GLU B 912  ? 0.2362 0.2378 0.2596 0.0118  -0.0386 -0.0102 910  GLU B CA  
15768 C C   . GLU B 912  ? 0.2659 0.2674 0.2905 0.0128  -0.0355 -0.0102 910  GLU B C   
15769 O O   . GLU B 912  ? 0.2590 0.2607 0.2835 0.0122  -0.0333 -0.0112 910  GLU B O   
15770 C CB  . GLU B 912  ? 0.3092 0.3074 0.3256 0.0108  -0.0388 -0.0106 910  GLU B CB  
15771 C CG  . GLU B 912  ? 0.3836 0.3814 0.3979 0.0098  -0.0419 -0.0107 910  GLU B CG  
15772 C CD  . GLU B 912  ? 0.5221 0.5166 0.5293 0.0088  -0.0417 -0.0114 910  GLU B CD  
15773 O OE1 . GLU B 912  ? 0.5914 0.5836 0.5946 0.0091  -0.0416 -0.0107 910  GLU B OE1 
15774 O OE2 . GLU B 912  ? 0.5902 0.5844 0.5959 0.0077  -0.0415 -0.0128 910  GLU B OE2 
15775 N N   . GLN B 913  ? 0.2515 0.2526 0.2770 0.0143  -0.0356 -0.0091 911  GLN B N   
15776 C CA  . GLN B 913  ? 0.2661 0.2664 0.2920 0.0152  -0.0329 -0.0091 911  GLN B CA  
15777 C C   . GLN B 913  ? 0.2815 0.2782 0.3029 0.0157  -0.0331 -0.0084 911  GLN B C   
15778 O O   . GLN B 913  ? 0.3292 0.3249 0.3496 0.0163  -0.0354 -0.0073 911  GLN B O   
15779 C CB  . GLN B 913  ? 0.2728 0.2760 0.3048 0.0169  -0.0325 -0.0086 911  GLN B CB  
15780 C CG  . GLN B 913  ? 0.2861 0.2929 0.3227 0.0162  -0.0320 -0.0092 911  GLN B CG  
15781 C CD  . GLN B 913  ? 0.3217 0.3315 0.3641 0.0178  -0.0310 -0.0087 911  GLN B CD  
15782 O OE1 . GLN B 913  ? 0.3914 0.4025 0.4367 0.0192  -0.0324 -0.0077 911  GLN B OE1 
15783 N NE2 . GLN B 913  ? 0.2899 0.3008 0.3340 0.0177  -0.0284 -0.0095 911  GLN B NE2 
15784 N N   . ILE B 914  ? 0.2929 0.2876 0.3114 0.0153  -0.0308 -0.0089 912  ILE B N   
15785 C CA  . ILE B 914  ? 0.3871 0.3781 0.4010 0.0153  -0.0307 -0.0082 912  ILE B CA  
15786 C C   . ILE B 914  ? 0.3995 0.3897 0.4149 0.0164  -0.0288 -0.0081 912  ILE B C   
15787 O O   . ILE B 914  ? 0.3906 0.3808 0.4057 0.0159  -0.0265 -0.0089 912  ILE B O   
15788 C CB  . ILE B 914  ? 0.3744 0.3637 0.3830 0.0135  -0.0298 -0.0088 912  ILE B CB  
15789 C CG1 . ILE B 914  ? 0.4115 0.4014 0.4185 0.0126  -0.0319 -0.0090 912  ILE B CG1 
15790 C CG2 . ILE B 914  ? 0.3929 0.3786 0.3969 0.0133  -0.0295 -0.0079 912  ILE B CG2 
15791 C CD1 . ILE B 914  ? 0.4251 0.4140 0.4274 0.0110  -0.0309 -0.0099 912  ILE B CD1 
15792 N N   . GLY B 915  ? 0.5727 0.5621 0.5898 0.0182  -0.0298 -0.0070 913  GLY B N   
15793 C CA  . GLY B 915  ? 0.6226 0.6130 0.6438 0.0200  -0.0285 -0.0070 913  GLY B CA  
15794 C C   . GLY B 915  ? 0.6088 0.5955 0.6275 0.0207  -0.0272 -0.0068 913  GLY B C   
15795 O O   . GLY B 915  ? 0.7563 0.7399 0.7702 0.0193  -0.0266 -0.0068 913  GLY B O   
15796 N N   . LEU B 916  ? 0.7425 0.7295 0.7645 0.0228  -0.0266 -0.0066 914  LEU B N   
15797 C CA  . LEU B 916  ? 0.6890 0.6728 0.7094 0.0235  -0.0248 -0.0068 914  LEU B CA  
15798 C C   . LEU B 916  ? 0.7928 0.7741 0.8136 0.0259  -0.0258 -0.0057 914  LEU B C   
15799 O O   . LEU B 916  ? 0.7481 0.7309 0.7714 0.0272  -0.0279 -0.0048 914  LEU B O   
15800 C CB  . LEU B 916  ? 0.7087 0.6948 0.7322 0.0238  -0.0223 -0.0080 914  LEU B CB  
15801 N N   . ALA B 917  ? 0.6727 0.6501 0.6910 0.0264  -0.0244 -0.0059 915  ALA B N   
15802 C CA  . ALA B 917  ? 0.6328 0.6063 0.6501 0.0285  -0.0252 -0.0050 915  ALA B CA  
15803 C C   . ALA B 917  ? 0.6539 0.6289 0.6757 0.0313  -0.0241 -0.0054 915  ALA B C   
15804 O O   . ALA B 917  ? 0.5635 0.5424 0.5889 0.0314  -0.0224 -0.0063 915  ALA B O   
15805 C CB  . ALA B 917  ? 0.7061 0.6739 0.7177 0.0273  -0.0245 -0.0050 915  ALA B CB  
15806 N N   . SER B 918  ? 0.5791 0.5507 0.6004 0.0336  -0.0248 -0.0045 916  SER B N   
15807 C CA  . SER B 918  ? 0.5718 0.5448 0.5974 0.0368  -0.0239 -0.0047 916  SER B CA  
15808 C C   . SER B 918  ? 0.5746 0.5469 0.5999 0.0368  -0.0209 -0.0063 916  SER B C   
15809 O O   . SER B 918  ? 0.5202 0.4960 0.5500 0.0386  -0.0195 -0.0068 916  SER B O   
15810 C CB  . SER B 918  ? 0.5055 0.4742 0.5298 0.0394  -0.0253 -0.0036 916  SER B CB  
15811 N N   . GLU B 919  ? 0.5261 0.4941 0.5463 0.0348  -0.0199 -0.0069 917  GLU B N   
15812 C CA  . GLU B 919  ? 0.5361 0.5029 0.5552 0.0347  -0.0173 -0.0083 917  GLU B CA  
15813 C C   . GLU B 919  ? 0.5534 0.5259 0.5763 0.0338  -0.0157 -0.0093 917  GLU B C   
15814 O O   . GLU B 919  ? 0.4608 0.4331 0.4838 0.0343  -0.0135 -0.0104 917  GLU B O   
15815 C CB  . GLU B 919  ? 0.4839 0.4456 0.4969 0.0322  -0.0170 -0.0086 917  GLU B CB  
15816 N N   . THR B 920  ? 0.4618 0.4389 0.4873 0.0326  -0.0168 -0.0089 918  THR B N   
15817 C CA  . THR B 920  ? 0.4234 0.4055 0.4523 0.0317  -0.0154 -0.0097 918  THR B CA  
15818 C C   . THR B 920  ? 0.4345 0.4204 0.4690 0.0343  -0.0144 -0.0098 918  THR B C   
15819 O O   . THR B 920  ? 0.3985 0.3875 0.4352 0.0339  -0.0126 -0.0106 918  THR B O   
15820 C CB  . THR B 920  ? 0.5059 0.4912 0.5355 0.0296  -0.0169 -0.0094 918  THR B CB  
15821 O OG1 . THR B 920  ? 0.4474 0.4343 0.4795 0.0307  -0.0192 -0.0082 918  THR B OG1 
15822 C CG2 . THR B 920  ? 0.3771 0.3592 0.4013 0.0270  -0.0173 -0.0095 918  THR B CG2 
15823 N N   . GLY B 921  ? 0.4391 0.4250 0.4759 0.0369  -0.0155 -0.0089 919  GLY B N   
15824 C CA  . GLY B 921  ? 0.4421 0.4324 0.4849 0.0394  -0.0147 -0.0088 919  GLY B CA  
15825 C C   . GLY B 921  ? 0.4372 0.4274 0.4805 0.0407  -0.0117 -0.0099 919  GLY B C   
15826 O O   . GLY B 921  ? 0.4803 0.4751 0.5287 0.0422  -0.0105 -0.0099 919  GLY B O   
15827 N N   . VAL B 922  ? 0.2922 0.2771 0.3303 0.0401  -0.0105 -0.0108 920  VAL B N   
15828 C CA  . VAL B 922  ? 0.2641 0.2483 0.3017 0.0411  -0.0077 -0.0121 920  VAL B CA  
15829 C C   . VAL B 922  ? 0.2777 0.2647 0.3155 0.0387  -0.0061 -0.0129 920  VAL B C   
15830 O O   . VAL B 922  ? 0.2771 0.2645 0.3151 0.0395  -0.0037 -0.0139 920  VAL B O   
15831 C CB  . VAL B 922  ? 0.2997 0.2767 0.3315 0.0416  -0.0072 -0.0127 920  VAL B CB  
15832 C CG1 . VAL B 922  ? 0.3221 0.2962 0.3542 0.0447  -0.0083 -0.0119 920  VAL B CG1 
15833 C CG2 . VAL B 922  ? 0.3145 0.2879 0.3411 0.0384  -0.0083 -0.0127 920  VAL B CG2 
15834 N N   . GLY B 923  ? 0.2603 0.2490 0.2976 0.0360  -0.0074 -0.0126 921  GLY B N   
15835 C CA  . GLY B 923  ? 0.2513 0.2427 0.2889 0.0339  -0.0061 -0.0133 921  GLY B CA  
15836 C C   . GLY B 923  ? 0.2554 0.2522 0.2975 0.0329  -0.0073 -0.0126 921  GLY B C   
15837 O O   . GLY B 923  ? 0.2683 0.2673 0.3138 0.0341  -0.0088 -0.0117 921  GLY B O   
15838 N N   . THR B 924  ? 0.1963 0.1951 0.2382 0.0307  -0.0067 -0.0131 922  THR B N   
15839 C CA  . THR B 924  ? 0.2048 0.2083 0.2506 0.0296  -0.0077 -0.0125 922  THR B CA  
15840 C C   . THR B 924  ? 0.2121 0.2142 0.2546 0.0271  -0.0093 -0.0126 922  THR B C   
15841 O O   . THR B 924  ? 0.2365 0.2379 0.2765 0.0254  -0.0083 -0.0133 922  THR B O   
15842 C CB  . THR B 924  ? 0.2007 0.2077 0.2493 0.0292  -0.0057 -0.0130 922  THR B CB  
15843 O OG1 . THR B 924  ? 0.2202 0.2248 0.2650 0.0281  -0.0040 -0.0140 922  THR B OG1 
15844 C CG2 . THR B 924  ? 0.2199 0.2294 0.2726 0.0317  -0.0042 -0.0127 922  THR B CG2 
15845 N N   . PHE B 925  ? 0.2104 0.2123 0.2529 0.0269  -0.0117 -0.0118 923  PHE B N   
15846 C CA  . PHE B 925  ? 0.2271 0.2275 0.2662 0.0248  -0.0132 -0.0118 923  PHE B CA  
15847 C C   . PHE B 925  ? 0.2086 0.2124 0.2506 0.0241  -0.0151 -0.0112 923  PHE B C   
15848 O O   . PHE B 925  ? 0.2273 0.2336 0.2733 0.0254  -0.0162 -0.0105 923  PHE B O   
15849 C CB  . PHE B 925  ? 0.2071 0.2032 0.2422 0.0251  -0.0144 -0.0113 923  PHE B CB  
15850 C CG  . PHE B 925  ? 0.2068 0.1988 0.2380 0.0252  -0.0129 -0.0119 923  PHE B CG  
15851 C CD1 . PHE B 925  ? 0.2043 0.1948 0.2362 0.0274  -0.0119 -0.0120 923  PHE B CD1 
15852 C CD2 . PHE B 925  ? 0.1924 0.1821 0.2192 0.0231  -0.0126 -0.0124 923  PHE B CD2 
15853 C CE1 . PHE B 925  ? 0.2339 0.2202 0.2618 0.0273  -0.0106 -0.0126 923  PHE B CE1 
15854 C CE2 . PHE B 925  ? 0.2174 0.2035 0.2407 0.0230  -0.0113 -0.0129 923  PHE B CE2 
15855 C CZ  . PHE B 925  ? 0.2268 0.2109 0.2505 0.0250  -0.0104 -0.0130 923  PHE B CZ  
15856 N N   . VAL B 926  ? 0.2057 0.2095 0.2456 0.0220  -0.0156 -0.0116 924  VAL B N   
15857 C CA  . VAL B 926  ? 0.2141 0.2197 0.2551 0.0209  -0.0177 -0.0113 924  VAL B CA  
15858 C C   . VAL B 926  ? 0.1986 0.2010 0.2343 0.0195  -0.0187 -0.0114 924  VAL B C   
15859 O O   . VAL B 926  ? 0.2093 0.2102 0.2419 0.0185  -0.0173 -0.0121 924  VAL B O   
15860 C CB  . VAL B 926  ? 0.2105 0.2192 0.2541 0.0197  -0.0170 -0.0118 924  VAL B CB  
15861 C CG1 . VAL B 926  ? 0.2315 0.2414 0.2753 0.0183  -0.0193 -0.0116 924  VAL B CG1 
15862 C CG2 . VAL B 926  ? 0.2484 0.2606 0.2973 0.0209  -0.0158 -0.0115 924  VAL B CG2 
15863 N N   . PRO B 927  ? 0.2366 0.2383 0.2712 0.0195  -0.0210 -0.0107 925  PRO B N   
15864 C CA  . PRO B 927  ? 0.2366 0.2354 0.2660 0.0182  -0.0218 -0.0107 925  PRO B CA  
15865 C C   . PRO B 927  ? 0.2604 0.2603 0.2887 0.0164  -0.0220 -0.0115 925  PRO B C   
15866 O O   . PRO B 927  ? 0.2481 0.2508 0.2798 0.0161  -0.0224 -0.0117 925  PRO B O   
15867 C CB  . PRO B 927  ? 0.3043 0.3021 0.3332 0.0189  -0.0244 -0.0096 925  PRO B CB  
15868 C CG  . PRO B 927  ? 0.2602 0.2618 0.2946 0.0197  -0.0255 -0.0092 925  PRO B CG  
15869 C CD  . PRO B 927  ? 0.2575 0.2613 0.2957 0.0206  -0.0231 -0.0097 925  PRO B CD  
15870 N N   . PRO B 928  ? 0.2342 0.2319 0.2579 0.0151  -0.0216 -0.0119 926  PRO B N   
15871 C CA  . PRO B 928  ? 0.2151 0.2135 0.2373 0.0137  -0.0220 -0.0126 926  PRO B CA  
15872 C C   . PRO B 928  ? 0.2276 0.2273 0.2512 0.0135  -0.0244 -0.0122 926  PRO B C   
15873 O O   . PRO B 928  ? 0.2495 0.2482 0.2723 0.0140  -0.0263 -0.0114 926  PRO B O   
15874 C CB  . PRO B 928  ? 0.2400 0.2356 0.2568 0.0128  -0.0217 -0.0126 926  PRO B CB  
15875 C CG  . PRO B 928  ? 0.3079 0.3019 0.3240 0.0133  -0.0202 -0.0123 926  PRO B CG  
15876 C CD  . PRO B 928  ? 0.2442 0.2388 0.2640 0.0150  -0.0207 -0.0117 926  PRO B CD  
15877 N N   . THR B 929  ? 0.2284 0.2300 0.2539 0.0128  -0.0245 -0.0129 927  THR B N   
15878 C CA  . THR B 929  ? 0.1936 0.1968 0.2212 0.0125  -0.0268 -0.0127 927  THR B CA  
15879 C C   . THR B 929  ? 0.2152 0.2178 0.2402 0.0110  -0.0271 -0.0137 927  THR B C   
15880 O O   . THR B 929  ? 0.2272 0.2298 0.2517 0.0105  -0.0253 -0.0146 927  THR B O   
15881 C CB  . THR B 929  ? 0.2221 0.2286 0.2558 0.0131  -0.0265 -0.0125 927  THR B CB  
15882 O OG1 . THR B 929  ? 0.2333 0.2402 0.2692 0.0147  -0.0259 -0.0116 927  THR B OG1 
15883 C CG2 . THR B 929  ? 0.2297 0.2382 0.2661 0.0124  -0.0290 -0.0122 927  THR B CG2 
15884 N N   . ILE B 930  ? 0.2139 0.2157 0.2369 0.0104  -0.0295 -0.0136 928  ILE B N   
15885 C CA  . ILE B 930  ? 0.2342 0.2350 0.2543 0.0092  -0.0302 -0.0147 928  ILE B CA  
15886 C C   . ILE B 930  ? 0.2314 0.2337 0.2544 0.0085  -0.0326 -0.0146 928  ILE B C   
15887 O O   . ILE B 930  ? 0.2352 0.2381 0.2591 0.0088  -0.0349 -0.0137 928  ILE B O   
15888 C CB  . ILE B 930  ? 0.2334 0.2314 0.2475 0.0088  -0.0308 -0.0147 928  ILE B CB  
15889 C CG1 . ILE B 930  ? 0.2322 0.2289 0.2437 0.0092  -0.0284 -0.0147 928  ILE B CG1 
15890 C CG2 . ILE B 930  ? 0.2451 0.2419 0.2560 0.0077  -0.0315 -0.0159 928  ILE B CG2 
15891 C CD1 . ILE B 930  ? 0.3127 0.3070 0.3185 0.0087  -0.0288 -0.0145 928  ILE B CD1 
15892 N N   . ILE B 931  ? 0.2220 0.2250 0.2462 0.0076  -0.0323 -0.0155 929  ILE B N   
15893 C CA  . ILE B 931  ? 0.2065 0.2108 0.2335 0.0067  -0.0345 -0.0155 929  ILE B CA  
15894 C C   . ILE B 931  ? 0.2434 0.2454 0.2664 0.0054  -0.0353 -0.0168 929  ILE B C   
15895 O O   . ILE B 931  ? 0.2285 0.2294 0.2499 0.0053  -0.0333 -0.0178 929  ILE B O   
15896 C CB  . ILE B 931  ? 0.2099 0.2173 0.2429 0.0067  -0.0334 -0.0152 929  ILE B CB  
15897 C CG1 . ILE B 931  ? 0.2401 0.2496 0.2767 0.0082  -0.0323 -0.0141 929  ILE B CG1 
15898 C CG2 . ILE B 931  ? 0.2294 0.2384 0.2655 0.0054  -0.0358 -0.0151 929  ILE B CG2 
15899 C CD1 . ILE B 931  ? 0.2426 0.2554 0.2851 0.0083  -0.0312 -0.0137 929  ILE B CD1 
15900 N N   . GLU B 932  ? 0.2331 0.2341 0.2543 0.0046  -0.0382 -0.0168 930  GLU B N   
15901 C CA  . GLU B 932  ? 0.2344 0.2327 0.2513 0.0035  -0.0390 -0.0182 930  GLU B CA  
15902 C C   . GLU B 932  ? 0.2478 0.2472 0.2683 0.0022  -0.0400 -0.0186 930  GLU B C   
15903 O O   . GLU B 932  ? 0.2557 0.2576 0.2806 0.0017  -0.0420 -0.0177 930  GLU B O   
15904 C CB  . GLU B 932  ? 0.3006 0.2970 0.3131 0.0031  -0.0417 -0.0182 930  GLU B CB  
15905 C CG  . GLU B 932  ? 0.3436 0.3384 0.3516 0.0041  -0.0406 -0.0179 930  GLU B CG  
15906 C CD  . GLU B 932  ? 0.5450 0.5371 0.5471 0.0036  -0.0426 -0.0182 930  GLU B CD  
15907 O OE1 . GLU B 932  ? 0.5577 0.5491 0.5592 0.0025  -0.0453 -0.0187 930  GLU B OE1 
15908 O OE2 . GLU B 932  ? 0.4562 0.4467 0.4539 0.0042  -0.0416 -0.0180 930  GLU B OE2 
15909 N N   . LEU B 933  ? 0.2568 0.2546 0.2758 0.0018  -0.0386 -0.0198 931  LEU B N   
15910 C CA  . LEU B 933  ? 0.2431 0.2412 0.2649 0.0004  -0.0393 -0.0202 931  LEU B CA  
15911 C C   . LEU B 933  ? 0.2984 0.2929 0.3154 -0.0008 -0.0413 -0.0216 931  LEU B C   
15912 O O   . LEU B 933  ? 0.3509 0.3424 0.3620 -0.0002 -0.0409 -0.0226 931  LEU B O   
15913 C CB  . LEU B 933  ? 0.2813 0.2795 0.3046 0.0008  -0.0364 -0.0206 931  LEU B CB  
15914 C CG  . LEU B 933  ? 0.2927 0.2940 0.3202 0.0019  -0.0341 -0.0195 931  LEU B CG  
15915 C CD1 . LEU B 933  ? 0.3380 0.3389 0.3661 0.0020  -0.0316 -0.0200 931  LEU B CD1 
15916 C CD2 . LEU B 933  ? 0.3688 0.3739 0.4023 0.0016  -0.0354 -0.0181 931  LEU B CD2 
15917 N N   . GLU B 934  ? 0.3398 0.3345 0.3592 -0.0024 -0.0435 -0.0217 932  GLU B N   
15918 C CA  . GLU B 934  ? 0.3940 0.3848 0.4088 -0.0037 -0.0452 -0.0232 932  GLU B CA  
15919 C C   . GLU B 934  ? 0.3876 0.3759 0.4009 -0.0036 -0.0430 -0.0244 932  GLU B C   
15920 O O   . GLU B 934  ? 0.4527 0.4370 0.4602 -0.0034 -0.0429 -0.0259 932  GLU B O   
15921 C CB  . GLU B 934  ? 0.4300 0.4217 0.4477 -0.0057 -0.0486 -0.0229 932  GLU B CB  
15922 N N   . LYS B 935  ? 0.3386 0.3292 0.3567 -0.0036 -0.0412 -0.0237 933  LYS B N   
15923 C CA  . LYS B 935  ? 0.3327 0.3211 0.3499 -0.0035 -0.0392 -0.0246 933  LYS B CA  
15924 C C   . LYS B 935  ? 0.3012 0.2927 0.3223 -0.0023 -0.0362 -0.0236 933  LYS B C   
15925 O O   . LYS B 935  ? 0.3352 0.3305 0.3610 -0.0022 -0.0361 -0.0222 933  LYS B O   
15926 C CB  . LYS B 935  ? 0.4027 0.3898 0.4217 -0.0056 -0.0409 -0.0249 933  LYS B CB  
15927 N N   . LEU B 936  ? 0.2914 0.2811 0.3104 -0.0014 -0.0338 -0.0243 934  LEU B N   
15928 C CA  . LEU B 936  ? 0.2898 0.2820 0.3120 -0.0004 -0.0311 -0.0234 934  LEU B CA  
15929 C C   . LEU B 936  ? 0.3019 0.2966 0.3299 -0.0015 -0.0312 -0.0223 934  LEU B C   
15930 O O   . LEU B 936  ? 0.3084 0.3064 0.3402 -0.0009 -0.0296 -0.0212 934  LEU B O   
15931 C CB  . LEU B 936  ? 0.3396 0.3294 0.3585 0.0007  -0.0289 -0.0244 934  LEU B CB  
15932 C CG  . LEU B 936  ? 0.3433 0.3351 0.3624 0.0024  -0.0262 -0.0239 934  LEU B CG  
15933 C CD1 . LEU B 936  ? 0.3905 0.3798 0.4050 0.0036  -0.0247 -0.0251 934  LEU B CD1 
15934 C CD2 . LEU B 936  ? 0.3837 0.3779 0.4075 0.0023  -0.0247 -0.0229 934  LEU B CD2 
15935 N N   . SER B 937  ? 0.2955 0.2888 0.3242 -0.0033 -0.0330 -0.0226 935  SER B N   
15936 C CA  . SER B 937  ? 0.3243 0.3201 0.3586 -0.0047 -0.0331 -0.0214 935  SER B CA  
15937 C C   . SER B 937  ? 0.3404 0.3409 0.3798 -0.0050 -0.0341 -0.0200 935  SER B C   
15938 O O   . SER B 937  ? 0.3205 0.3240 0.3651 -0.0058 -0.0337 -0.0188 935  SER B O   
15939 C CB  . SER B 937  ? 0.3740 0.3668 0.4076 -0.0068 -0.0350 -0.0220 935  SER B CB  
15940 O OG  . SER B 937  ? 0.3941 0.3851 0.4250 -0.0077 -0.0380 -0.0228 935  SER B OG  
15941 N N   . ASP B 938  ? 0.3248 0.3259 0.3627 -0.0042 -0.0353 -0.0200 936  ASP B N   
15942 C CA  . ASP B 938  ? 0.2937 0.2993 0.3364 -0.0039 -0.0359 -0.0186 936  ASP B CA  
15943 C C   . ASP B 938  ? 0.3054 0.3138 0.3512 -0.0024 -0.0329 -0.0176 936  ASP B C   
15944 O O   . ASP B 938  ? 0.3149 0.3274 0.3658 -0.0022 -0.0328 -0.0164 936  ASP B O   
15945 C CB  . ASP B 938  ? 0.3774 0.3826 0.4172 -0.0030 -0.0375 -0.0187 936  ASP B CB  
15946 C CG  . ASP B 938  ? 0.4895 0.4921 0.5261 -0.0044 -0.0407 -0.0195 936  ASP B CG  
15947 O OD1 . ASP B 938  ? 0.4265 0.4286 0.4646 -0.0064 -0.0423 -0.0197 936  ASP B OD1 
15948 O OD2 . ASP B 938  ? 0.5202 0.5213 0.5528 -0.0037 -0.0418 -0.0199 936  ASP B OD2 
15949 N N   . LEU B 939  ? 0.2795 0.2859 0.3221 -0.0012 -0.0305 -0.0183 937  LEU B N   
15950 C CA  . LEU B 939  ? 0.3157 0.3242 0.3603 0.0002  -0.0277 -0.0176 937  LEU B CA  
15951 C C   . LEU B 939  ? 0.3348 0.3438 0.3820 -0.0006 -0.0262 -0.0173 937  LEU B C   
15952 O O   . LEU B 939  ? 0.4351 0.4410 0.4795 -0.0012 -0.0259 -0.0182 937  LEU B O   
15953 C CB  . LEU B 939  ? 0.3193 0.3253 0.3590 0.0016  -0.0260 -0.0185 937  LEU B CB  
15954 C CG  . LEU B 939  ? 0.4499 0.4569 0.4887 0.0032  -0.0252 -0.0181 937  LEU B CG  
15955 C CD1 . LEU B 939  ? 0.3188 0.3235 0.3532 0.0041  -0.0234 -0.0190 937  LEU B CD1 
15956 C CD2 . LEU B 939  ? 0.4088 0.4192 0.4523 0.0040  -0.0237 -0.0170 937  LEU B CD2 
15957 N N   . GLN B 940  ? 0.2941 0.3068 0.3463 -0.0005 -0.0251 -0.0161 938  GLN B N   
15958 C CA  . GLN B 940  ? 0.3793 0.3928 0.4342 -0.0015 -0.0237 -0.0155 938  GLN B CA  
15959 C C   . GLN B 940  ? 0.3139 0.3284 0.3693 -0.0001 -0.0206 -0.0151 938  GLN B C   
15960 O O   . GLN B 940  ? 0.3237 0.3383 0.3803 -0.0008 -0.0192 -0.0147 938  GLN B O   
15961 C CB  . GLN B 940  ? 0.4638 0.4811 0.5246 -0.0030 -0.0249 -0.0143 938  GLN B CB  
15962 N N   . ARG B 941  ? 0.2507 0.2658 0.3049 0.0017  -0.0195 -0.0152 939  ARG B N   
15963 C CA  . ARG B 941  ? 0.2707 0.2869 0.3255 0.0029  -0.0168 -0.0148 939  ARG B CA  
15964 C C   . ARG B 941  ? 0.2267 0.2415 0.2778 0.0045  -0.0161 -0.0155 939  ARG B C   
15965 O O   . ARG B 941  ? 0.2353 0.2493 0.2847 0.0049  -0.0176 -0.0158 939  ARG B O   
15966 C CB  . ARG B 941  ? 0.2871 0.3076 0.3474 0.0032  -0.0159 -0.0136 939  ARG B CB  
15967 C CG  . ARG B 941  ? 0.3255 0.3481 0.3876 0.0042  -0.0171 -0.0132 939  ARG B CG  
15968 C CD  . ARG B 941  ? 0.3063 0.3334 0.3742 0.0046  -0.0162 -0.0119 939  ARG B CD  
15969 N NE  . ARG B 941  ? 0.3082 0.3373 0.3780 0.0059  -0.0172 -0.0115 939  ARG B NE  
15970 C CZ  . ARG B 941  ? 0.3260 0.3551 0.3950 0.0079  -0.0158 -0.0115 939  ARG B CZ  
15971 N NH1 . ARG B 941  ? 0.3320 0.3594 0.3983 0.0087  -0.0134 -0.0120 939  ARG B NH1 
15972 N NH2 . ARG B 941  ? 0.3087 0.3397 0.3799 0.0091  -0.0169 -0.0110 939  ARG B NH2 
15973 N N   . GLU B 942  ? 0.2443 0.2587 0.2942 0.0054  -0.0138 -0.0156 940  GLU B N   
15974 C CA  . GLU B 942  ? 0.2043 0.2176 0.2510 0.0068  -0.0129 -0.0160 940  GLU B CA  
15975 C C   . GLU B 942  ? 0.2293 0.2448 0.2784 0.0078  -0.0128 -0.0154 940  GLU B C   
15976 O O   . GLU B 942  ? 0.2764 0.2943 0.3290 0.0082  -0.0116 -0.0146 940  GLU B O   
15977 C CB  . GLU B 942  ? 0.2237 0.2363 0.2689 0.0073  -0.0106 -0.0162 940  GLU B CB  
15978 C CG  . GLU B 942  ? 0.2295 0.2413 0.2718 0.0085  -0.0097 -0.0166 940  GLU B CG  
15979 C CD  . GLU B 942  ? 0.2388 0.2505 0.2803 0.0090  -0.0075 -0.0166 940  GLU B CD  
15980 O OE1 . GLU B 942  ? 0.2614 0.2747 0.3055 0.0090  -0.0063 -0.0159 940  GLU B OE1 
15981 O OE2 . GLU B 942  ? 0.2075 0.2177 0.2457 0.0094  -0.0069 -0.0171 940  GLU B OE2 
15982 N N   . VAL B 943  ? 0.1995 0.2141 0.2467 0.0083  -0.0141 -0.0156 941  VAL B N   
15983 C CA  . VAL B 943  ? 0.1886 0.2046 0.2375 0.0095  -0.0142 -0.0150 941  VAL B CA  
15984 C C   . VAL B 943  ? 0.2084 0.2226 0.2539 0.0105  -0.0129 -0.0154 941  VAL B C   
15985 O O   . VAL B 943  ? 0.2045 0.2165 0.2461 0.0104  -0.0136 -0.0160 941  VAL B O   
15986 C CB  . VAL B 943  ? 0.2104 0.2266 0.2597 0.0092  -0.0169 -0.0148 941  VAL B CB  
15987 C CG1 . VAL B 943  ? 0.2344 0.2519 0.2855 0.0107  -0.0170 -0.0141 941  VAL B CG1 
15988 C CG2 . VAL B 943  ? 0.2751 0.2931 0.3279 0.0079  -0.0183 -0.0144 941  VAL B CG2 
15989 N N   . PHE B 944  ? 0.1943 0.2094 0.2410 0.0115  -0.0110 -0.0151 942  PHE B N   
15990 C CA  . PHE B 944  ? 0.1967 0.2099 0.2400 0.0121  -0.0095 -0.0156 942  PHE B CA  
15991 C C   . PHE B 944  ? 0.2032 0.2156 0.2457 0.0132  -0.0099 -0.0154 942  PHE B C   
15992 O O   . PHE B 944  ? 0.2178 0.2306 0.2613 0.0143  -0.0087 -0.0151 942  PHE B O   
15993 C CB  . PHE B 944  ? 0.1946 0.2087 0.2391 0.0124  -0.0072 -0.0155 942  PHE B CB  
15994 C CG  . PHE B 944  ? 0.1968 0.2090 0.2376 0.0125  -0.0059 -0.0161 942  PHE B CG  
15995 C CD1 . PHE B 944  ? 0.1981 0.2091 0.2364 0.0117  -0.0060 -0.0166 942  PHE B CD1 
15996 C CD2 . PHE B 944  ? 0.1889 0.2006 0.2288 0.0135  -0.0046 -0.0161 942  PHE B CD2 
15997 C CE1 . PHE B 944  ? 0.2003 0.2102 0.2357 0.0118  -0.0049 -0.0171 942  PHE B CE1 
15998 C CE2 . PHE B 944  ? 0.2014 0.2114 0.2380 0.0134  -0.0035 -0.0167 942  PHE B CE2 
15999 C CZ  . PHE B 944  ? 0.2042 0.2136 0.2387 0.0125  -0.0037 -0.0171 942  PHE B CZ  
16000 N N   . GLY B 945  ? 0.1974 0.2085 0.2377 0.0129  -0.0116 -0.0154 943  GLY B N   
16001 C CA  . GLY B 945  ? 0.2060 0.2160 0.2453 0.0138  -0.0124 -0.0151 943  GLY B CA  
16002 C C   . GLY B 945  ? 0.2047 0.2127 0.2403 0.0130  -0.0139 -0.0153 943  GLY B C   
16003 O O   . GLY B 945  ? 0.2103 0.2178 0.2441 0.0120  -0.0142 -0.0159 943  GLY B O   
16004 N N   . PRO B 946  ? 0.1984 0.2052 0.2328 0.0136  -0.0149 -0.0148 944  PRO B N   
16005 C CA  . PRO B 946  ? 0.2014 0.2060 0.2316 0.0130  -0.0161 -0.0150 944  PRO B CA  
16006 C C   . PRO B 946  ? 0.1987 0.2038 0.2293 0.0124  -0.0184 -0.0148 944  PRO B C   
16007 O O   . PRO B 946  ? 0.2190 0.2233 0.2487 0.0127  -0.0201 -0.0142 944  PRO B O   
16008 C CB  . PRO B 946  ? 0.1946 0.1974 0.2234 0.0139  -0.0161 -0.0144 944  PRO B CB  
16009 C CG  . PRO B 946  ? 0.2021 0.2066 0.2352 0.0153  -0.0163 -0.0138 944  PRO B CG  
16010 C CD  . PRO B 946  ? 0.1984 0.2054 0.2348 0.0151  -0.0148 -0.0142 944  PRO B CD  
16011 N N   . VAL B 947  ? 0.1940 0.2003 0.2259 0.0116  -0.0186 -0.0153 945  VAL B N   
16012 C CA  . VAL B 947  ? 0.2045 0.2114 0.2373 0.0109  -0.0209 -0.0152 945  VAL B CA  
16013 C C   . VAL B 947  ? 0.2327 0.2382 0.2622 0.0098  -0.0211 -0.0162 945  VAL B C   
16014 O O   . VAL B 947  ? 0.2121 0.2181 0.2424 0.0093  -0.0200 -0.0168 945  VAL B O   
16015 C CB  . VAL B 947  ? 0.2118 0.2217 0.2499 0.0109  -0.0213 -0.0148 945  VAL B CB  
16016 C CG1 . VAL B 947  ? 0.2286 0.2390 0.2675 0.0100  -0.0240 -0.0146 945  VAL B CG1 
16017 C CG2 . VAL B 947  ? 0.2073 0.2188 0.2488 0.0124  -0.0208 -0.0139 945  VAL B CG2 
16018 N N   . LEU B 948  ? 0.1937 0.1973 0.2193 0.0095  -0.0223 -0.0163 946  LEU B N   
16019 C CA  . LEU B 948  ? 0.2145 0.2165 0.2364 0.0087  -0.0224 -0.0173 946  LEU B CA  
16020 C C   . LEU B 948  ? 0.2113 0.2132 0.2334 0.0079  -0.0249 -0.0175 946  LEU B C   
16021 O O   . LEU B 948  ? 0.2169 0.2189 0.2391 0.0079  -0.0269 -0.0169 946  LEU B O   
16022 C CB  . LEU B 948  ? 0.2085 0.2086 0.2256 0.0087  -0.0222 -0.0174 946  LEU B CB  
16023 C CG  . LEU B 948  ? 0.2048 0.2034 0.2178 0.0081  -0.0221 -0.0184 946  LEU B CG  
16024 C CD1 . LEU B 948  ? 0.1903 0.1895 0.2040 0.0082  -0.0200 -0.0192 946  LEU B CD1 
16025 C CD2 . LEU B 948  ? 0.2642 0.2613 0.2728 0.0081  -0.0219 -0.0182 946  LEU B CD2 
16026 N N   . HIS B 949  ? 0.1924 0.1940 0.2145 0.0072  -0.0248 -0.0184 947  HIS B N   
16027 C CA  . HIS B 949  ? 0.1959 0.1969 0.2177 0.0062  -0.0272 -0.0188 947  HIS B CA  
16028 C C   . HIS B 949  ? 0.2164 0.2146 0.2325 0.0059  -0.0274 -0.0199 947  HIS B C   
16029 O O   . HIS B 949  ? 0.2402 0.2375 0.2539 0.0063  -0.0254 -0.0205 947  HIS B O   
16030 C CB  . HIS B 949  ? 0.2183 0.2203 0.2435 0.0055  -0.0270 -0.0190 947  HIS B CB  
16031 C CG  . HIS B 949  ? 0.1912 0.1962 0.2220 0.0058  -0.0263 -0.0180 947  HIS B CG  
16032 N ND1 . HIS B 949  ? 0.2215 0.2275 0.2536 0.0066  -0.0238 -0.0178 947  HIS B ND1 
16033 C CD2 . HIS B 949  ? 0.2145 0.2219 0.2496 0.0056  -0.0277 -0.0170 947  HIS B CD2 
16034 C CE1 . HIS B 949  ? 0.2066 0.2151 0.2434 0.0070  -0.0235 -0.0168 947  HIS B CE1 
16035 N NE2 . HIS B 949  ? 0.2211 0.2308 0.2600 0.0064  -0.0258 -0.0163 947  HIS B NE2 
16036 N N   . VAL B 950  ? 0.2315 0.2284 0.2454 0.0053  -0.0298 -0.0201 948  VAL B N   
16037 C CA  . VAL B 950  ? 0.2349 0.2291 0.2430 0.0051  -0.0301 -0.0210 948  VAL B CA  
16038 C C   . VAL B 950  ? 0.2308 0.2233 0.2377 0.0041  -0.0319 -0.0221 948  VAL B C   
16039 O O   . VAL B 950  ? 0.2383 0.2315 0.2475 0.0033  -0.0343 -0.0216 948  VAL B O   
16040 C CB  . VAL B 950  ? 0.2249 0.2183 0.2299 0.0054  -0.0312 -0.0204 948  VAL B CB  
16041 C CG1 . VAL B 950  ? 0.2608 0.2514 0.2594 0.0051  -0.0315 -0.0214 948  VAL B CG1 
16042 C CG2 . VAL B 950  ? 0.2551 0.2495 0.2606 0.0062  -0.0292 -0.0194 948  VAL B CG2 
16043 N N   . ILE B 951  ? 0.2248 0.2151 0.2281 0.0042  -0.0309 -0.0234 949  ILE B N   
16044 C CA  . ILE B 951  ? 0.2296 0.2174 0.2306 0.0033  -0.0325 -0.0247 949  ILE B CA  
16045 C C   . ILE B 951  ? 0.2238 0.2088 0.2182 0.0037  -0.0324 -0.0257 949  ILE B C   
16046 O O   . ILE B 951  ? 0.2480 0.2332 0.2404 0.0047  -0.0301 -0.0258 949  ILE B O   
16047 C CB  . ILE B 951  ? 0.2619 0.2492 0.2646 0.0033  -0.0311 -0.0254 949  ILE B CB  
16048 C CG1 . ILE B 951  ? 0.3586 0.3484 0.3675 0.0026  -0.0315 -0.0244 949  ILE B CG1 
16049 C CG2 . ILE B 951  ? 0.3768 0.3604 0.3754 0.0028  -0.0321 -0.0270 949  ILE B CG2 
16050 C CD1 . ILE B 951  ? 0.4804 0.4696 0.4910 0.0024  -0.0302 -0.0249 949  ILE B CD1 
16051 N N   . ARG B 952  ? 0.2268 0.2095 0.2179 0.0029  -0.0349 -0.0264 950  ARG B N   
16052 C CA  . ARG B 952  ? 0.2414 0.2211 0.2258 0.0033  -0.0347 -0.0276 950  ARG B CA  
16053 C C   . ARG B 952  ? 0.2507 0.2274 0.2329 0.0030  -0.0349 -0.0294 950  ARG B C   
16054 O O   . ARG B 952  ? 0.3202 0.2962 0.3048 0.0019  -0.0367 -0.0296 950  ARG B O   
16055 C CB  . ARG B 952  ? 0.2659 0.2445 0.2473 0.0026  -0.0375 -0.0273 950  ARG B CB  
16056 C CG  . ARG B 952  ? 0.2795 0.2606 0.2627 0.0029  -0.0375 -0.0255 950  ARG B CG  
16057 C CD  . ARG B 952  ? 0.3809 0.3615 0.3629 0.0021  -0.0409 -0.0248 950  ARG B CD  
16058 N NE  . ARG B 952  ? 0.4271 0.4101 0.4118 0.0025  -0.0411 -0.0230 950  ARG B NE  
16059 C CZ  . ARG B 952  ? 0.3603 0.3424 0.3411 0.0029  -0.0412 -0.0223 950  ARG B CZ  
16060 N NH1 . ARG B 952  ? 0.3752 0.3546 0.3494 0.0028  -0.0410 -0.0232 950  ARG B NH1 
16061 N NH2 . ARG B 952  ? 0.4115 0.3955 0.3951 0.0033  -0.0415 -0.0205 950  ARG B NH2 
16062 N N   . TYR B 953  ? 0.2410 0.2157 0.2186 0.0041  -0.0330 -0.0307 951  TYR B N   
16063 C CA  . TYR B 953  ? 0.2497 0.2211 0.2249 0.0042  -0.0331 -0.0324 951  TYR B CA  
16064 C C   . TYR B 953  ? 0.2555 0.2237 0.2234 0.0049  -0.0327 -0.0339 951  TYR B C   
16065 O O   . TYR B 953  ? 0.2766 0.2459 0.2419 0.0058  -0.0312 -0.0336 951  TYR B O   
16066 C CB  . TYR B 953  ? 0.2526 0.2249 0.2308 0.0051  -0.0305 -0.0325 951  TYR B CB  
16067 C CG  . TYR B 953  ? 0.2328 0.2063 0.2091 0.0068  -0.0274 -0.0327 951  TYR B CG  
16068 C CD1 . TYR B 953  ? 0.2328 0.2099 0.2119 0.0072  -0.0259 -0.0312 951  TYR B CD1 
16069 C CD2 . TYR B 953  ? 0.2355 0.2065 0.2074 0.0080  -0.0261 -0.0343 951  TYR B CD2 
16070 C CE1 . TYR B 953  ? 0.2410 0.2195 0.2186 0.0084  -0.0232 -0.0313 951  TYR B CE1 
16071 C CE2 . TYR B 953  ? 0.2635 0.2361 0.2342 0.0095  -0.0233 -0.0343 951  TYR B CE2 
16072 C CZ  . TYR B 953  ? 0.2483 0.2248 0.2219 0.0096  -0.0219 -0.0328 951  TYR B CZ  
16073 O OH  . TYR B 953  ? 0.2581 0.2364 0.2305 0.0109  -0.0192 -0.0328 951  TYR B OH  
16074 N N   . ARG B 954  ? 0.3048 0.2690 0.2693 0.0046  -0.0340 -0.0356 952  ARG B N   
16075 C CA  . ARG B 954  ? 0.3673 0.3280 0.3247 0.0056  -0.0333 -0.0374 952  ARG B CA  
16076 C C   . ARG B 954  ? 0.3366 0.2971 0.2940 0.0074  -0.0302 -0.0383 952  ARG B C   
16077 O O   . ARG B 954  ? 0.2920 0.2526 0.2532 0.0074  -0.0298 -0.0382 952  ARG B O   
16078 C CB  . ARG B 954  ? 0.3707 0.3267 0.3244 0.0045  -0.0362 -0.0389 952  ARG B CB  
16079 N N   . ARG B 955  ? 0.3471 0.3074 0.3000 0.0090  -0.0280 -0.0390 953  ARG B N   
16080 C CA  . ARG B 955  ? 0.3686 0.3294 0.3217 0.0109  -0.0250 -0.0397 953  ARG B CA  
16081 C C   . ARG B 955  ? 0.3328 0.2896 0.2851 0.0114  -0.0254 -0.0413 953  ARG B C   
16082 O O   . ARG B 955  ? 0.3460 0.3037 0.3013 0.0124  -0.0237 -0.0412 953  ARG B O   
16083 C CB  . ARG B 955  ? 0.4139 0.3751 0.3620 0.0125  -0.0227 -0.0403 953  ARG B CB  
16084 C CG  . ARG B 955  ? 0.4583 0.4206 0.4068 0.0147  -0.0195 -0.0409 953  ARG B CG  
16085 C CD  . ARG B 955  ? 0.4626 0.4292 0.4178 0.0148  -0.0181 -0.0393 953  ARG B CD  
16086 N NE  . ARG B 955  ? 0.4787 0.4468 0.4344 0.0168  -0.0152 -0.0398 953  ARG B NE  
16087 C CZ  . ARG B 955  ? 0.4871 0.4526 0.4424 0.0182  -0.0147 -0.0411 953  ARG B CZ  
16088 N NH1 . ARG B 955  ? 0.4967 0.4577 0.4509 0.0174  -0.0169 -0.0421 953  ARG B NH1 
16089 N NH2 . ARG B 955  ? 0.4206 0.3880 0.3766 0.0202  -0.0121 -0.0413 953  ARG B NH2 
16090 N N   . ASP B 956  ? 0.3375 0.2896 0.2855 0.0106  -0.0278 -0.0427 954  ASP B N   
16091 C CA  A ASP B 956  ? 0.3794 0.3270 0.3262 0.0108  -0.0285 -0.0443 954  ASP B CA  
16092 C CA  B ASP B 956  ? 0.3795 0.3272 0.3264 0.0108  -0.0284 -0.0443 954  ASP B CA  
16093 C C   . ASP B 956  ? 0.3751 0.3237 0.3283 0.0094  -0.0295 -0.0432 954  ASP B C   
16094 O O   . ASP B 956  ? 0.4106 0.3559 0.3637 0.0097  -0.0296 -0.0441 954  ASP B O   
16095 C CB  A ASP B 956  ? 0.3919 0.3341 0.3327 0.0098  -0.0312 -0.0460 954  ASP B CB  
16096 C CB  B ASP B 956  ? 0.3941 0.3360 0.3343 0.0103  -0.0306 -0.0463 954  ASP B CB  
16097 C CG  A ASP B 956  ? 0.4443 0.3845 0.3778 0.0115  -0.0298 -0.0475 954  ASP B CG  
16098 C CG  B ASP B 956  ? 0.3398 0.2811 0.2805 0.0076  -0.0343 -0.0456 954  ASP B CG  
16099 O OD1 A ASP B 956  ? 0.4881 0.4303 0.4212 0.0137  -0.0266 -0.0477 954  ASP B OD1 
16100 O OD1 B ASP B 956  ? 0.4224 0.3679 0.3689 0.0063  -0.0351 -0.0437 954  ASP B OD1 
16101 O OD2 A ASP B 956  ? 0.5008 0.4375 0.4291 0.0106  -0.0320 -0.0486 954  ASP B OD2 
16102 O OD2 B ASP B 956  ? 0.4697 0.4065 0.4049 0.0069  -0.0364 -0.0472 954  ASP B OD2 
16103 N N   . ASP B 957  ? 0.3133 0.2660 0.2716 0.0080  -0.0303 -0.0412 955  ASP B N   
16104 C CA  . ASP B 957  ? 0.3448 0.2990 0.3094 0.0067  -0.0311 -0.0400 955  ASP B CA  
16105 C C   . ASP B 957  ? 0.3051 0.2636 0.2744 0.0078  -0.0283 -0.0386 955  ASP B C   
16106 O O   . ASP B 957  ? 0.3022 0.2629 0.2770 0.0068  -0.0286 -0.0373 955  ASP B O   
16107 C CB  . ASP B 957  ? 0.3656 0.3217 0.3332 0.0044  -0.0338 -0.0387 955  ASP B CB  
16108 C CG  . ASP B 957  ? 0.4927 0.4446 0.4566 0.0028  -0.0371 -0.0399 955  ASP B CG  
16109 O OD1 . ASP B 957  ? 0.4676 0.4148 0.4283 0.0028  -0.0375 -0.0415 955  ASP B OD1 
16110 O OD2 . ASP B 957  ? 0.5397 0.4929 0.5039 0.0014  -0.0393 -0.0391 955  ASP B OD2 
16111 N N   . LEU B 958  ? 0.2810 0.2408 0.2484 0.0098  -0.0256 -0.0389 956  LEU B N   
16112 C CA  . LEU B 958  ? 0.2715 0.2356 0.2433 0.0108  -0.0232 -0.0376 956  LEU B CA  
16113 C C   . LEU B 958  ? 0.2713 0.2347 0.2465 0.0109  -0.0228 -0.0374 956  LEU B C   
16114 O O   . LEU B 958  ? 0.2532 0.2199 0.2336 0.0103  -0.0223 -0.0359 956  LEU B O   
16115 C CB  . LEU B 958  ? 0.2812 0.2465 0.2500 0.0129  -0.0205 -0.0382 956  LEU B CB  
16116 C CG  . LEU B 958  ? 0.2807 0.2504 0.2536 0.0139  -0.0181 -0.0369 956  LEU B CG  
16117 C CD1 . LEU B 958  ? 0.2793 0.2529 0.2563 0.0125  -0.0184 -0.0350 956  LEU B CD1 
16118 C CD2 . LEU B 958  ? 0.3234 0.2943 0.2932 0.0158  -0.0156 -0.0375 956  LEU B CD2 
16119 N N   . ASP B 959  ? 0.2625 0.2215 0.2349 0.0115  -0.0230 -0.0389 957  ASP B N   
16120 C CA  . ASP B 959  ? 0.2595 0.2175 0.2348 0.0117  -0.0226 -0.0386 957  ASP B CA  
16121 C C   . ASP B 959  ? 0.2624 0.2211 0.2423 0.0092  -0.0245 -0.0374 957  ASP B C   
16122 O O   . ASP B 959  ? 0.2562 0.2172 0.2406 0.0090  -0.0236 -0.0361 957  ASP B O   
16123 C CB  . ASP B 959  ? 0.2688 0.2212 0.2397 0.0129  -0.0227 -0.0405 957  ASP B CB  
16124 C CG  . ASP B 959  ? 0.2736 0.2254 0.2469 0.0139  -0.0214 -0.0402 957  ASP B CG  
16125 O OD1 . ASP B 959  ? 0.2848 0.2406 0.2608 0.0152  -0.0192 -0.0392 957  ASP B OD1 
16126 O OD2 . ASP B 959  ? 0.3081 0.2552 0.2803 0.0134  -0.0226 -0.0409 957  ASP B OD2 
16127 N N   . ARG B 960  ? 0.2738 0.2306 0.2525 0.0074  -0.0271 -0.0377 958  ARG B N   
16128 C CA  . ARG B 960  ? 0.2509 0.2089 0.2341 0.0050  -0.0291 -0.0364 958  ARG B CA  
16129 C C   . ARG B 960  ? 0.2702 0.2341 0.2584 0.0047  -0.0282 -0.0345 958  ARG B C   
16130 O O   . ARG B 960  ? 0.2532 0.2194 0.2465 0.0037  -0.0283 -0.0331 958  ARG B O   
16131 C CB  . ARG B 960  ? 0.3339 0.2893 0.3147 0.0031  -0.0322 -0.0372 958  ARG B CB  
16132 N N   . LEU B 961  ? 0.2291 0.1953 0.2158 0.0057  -0.0273 -0.0344 959  LEU B N   
16133 C CA  . LEU B 961  ? 0.2250 0.1962 0.2159 0.0056  -0.0264 -0.0327 959  LEU B CA  
16134 C C   . LEU B 961  ? 0.2275 0.2010 0.2218 0.0066  -0.0240 -0.0318 959  LEU B C   
16135 O O   . LEU B 961  ? 0.2307 0.2072 0.2298 0.0059  -0.0238 -0.0304 959  LEU B O   
16136 C CB  . LEU B 961  ? 0.2498 0.2225 0.2379 0.0065  -0.0258 -0.0327 959  LEU B CB  
16137 C CG  . LEU B 961  ? 0.2352 0.2124 0.2268 0.0067  -0.0246 -0.0311 959  LEU B CG  
16138 C CD1 . LEU B 961  ? 0.3078 0.2869 0.3036 0.0050  -0.0266 -0.0298 959  LEU B CD1 
16139 C CD2 . LEU B 961  ? 0.2607 0.2389 0.2490 0.0076  -0.0237 -0.0311 959  LEU B CD2 
16140 N N   . VAL B 962  ? 0.2093 0.1813 0.2011 0.0083  -0.0222 -0.0327 960  VAL B N   
16141 C CA  . VAL B 962  ? 0.2327 0.2066 0.2274 0.0092  -0.0202 -0.0320 960  VAL B CA  
16142 C C   . VAL B 962  ? 0.2363 0.2093 0.2345 0.0079  -0.0210 -0.0313 960  VAL B C   
16143 O O   . VAL B 962  ? 0.2287 0.2046 0.2309 0.0076  -0.0201 -0.0299 960  VAL B O   
16144 C CB  . VAL B 962  ? 0.2419 0.2142 0.2333 0.0113  -0.0184 -0.0331 960  VAL B CB  
16145 C CG1 . VAL B 962  ? 0.2723 0.2459 0.2667 0.0121  -0.0168 -0.0323 960  VAL B CG1 
16146 C CG2 . VAL B 962  ? 0.2571 0.2317 0.2463 0.0125  -0.0171 -0.0333 960  VAL B CG2 
16147 N N   . ASP B 963  ? 0.2279 0.1968 0.2243 0.0069  -0.0228 -0.0322 961  ASP B N   
16148 C CA  . ASP B 963  ? 0.2560 0.2241 0.2558 0.0052  -0.0238 -0.0314 961  ASP B CA  
16149 C C   . ASP B 963  ? 0.2518 0.2239 0.2564 0.0036  -0.0245 -0.0298 961  ASP B C   
16150 O O   . ASP B 963  ? 0.2558 0.2298 0.2645 0.0030  -0.0239 -0.0285 961  ASP B O   
16151 C CB  . ASP B 963  ? 0.2598 0.2229 0.2568 0.0040  -0.0261 -0.0326 961  ASP B CB  
16152 C CG  . ASP B 963  ? 0.3431 0.3015 0.3359 0.0055  -0.0255 -0.0340 961  ASP B CG  
16153 O OD1 . ASP B 963  ? 0.3437 0.3028 0.3367 0.0073  -0.0233 -0.0338 961  ASP B OD1 
16154 O OD2 . ASP B 963  ? 0.3521 0.3058 0.3411 0.0048  -0.0272 -0.0354 961  ASP B OD2 
16155 N N   . ASP B 964  ? 0.2453 0.2187 0.2495 0.0030  -0.0259 -0.0298 962  ASP B N   
16156 C CA  . ASP B 964  ? 0.2385 0.2158 0.2472 0.0018  -0.0267 -0.0284 962  ASP B CA  
16157 C C   . ASP B 964  ? 0.2517 0.2330 0.2636 0.0029  -0.0243 -0.0271 962  ASP B C   
16158 O O   . ASP B 964  ? 0.2345 0.2186 0.2510 0.0021  -0.0241 -0.0258 962  ASP B O   
16159 C CB  . ASP B 964  ? 0.2549 0.2327 0.2618 0.0014  -0.0285 -0.0286 962  ASP B CB  
16160 C CG  . ASP B 964  ? 0.3523 0.3265 0.3567 -0.0001 -0.0312 -0.0296 962  ASP B CG  
16161 O OD1 . ASP B 964  ? 0.3160 0.2875 0.3208 -0.0011 -0.0319 -0.0300 962  ASP B OD1 
16162 O OD2 . ASP B 964  ? 0.3970 0.3709 0.3991 -0.0004 -0.0328 -0.0301 962  ASP B OD2 
16163 N N   . VAL B 965  ? 0.2158 0.1976 0.2252 0.0046  -0.0226 -0.0275 963  VAL B N   
16164 C CA  . VAL B 965  ? 0.1949 0.1801 0.2069 0.0055  -0.0204 -0.0265 963  VAL B CA  
16165 C C   . VAL B 965  ? 0.2127 0.1980 0.2271 0.0055  -0.0192 -0.0259 963  VAL B C   
16166 O O   . VAL B 965  ? 0.2220 0.2101 0.2403 0.0051  -0.0185 -0.0247 963  VAL B O   
16167 C CB  . VAL B 965  ? 0.2124 0.1981 0.2212 0.0072  -0.0189 -0.0271 963  VAL B CB  
16168 C CG1 . VAL B 965  ? 0.2056 0.1943 0.2167 0.0079  -0.0168 -0.0261 963  VAL B CG1 
16169 C CG2 . VAL B 965  ? 0.2322 0.2181 0.2387 0.0070  -0.0200 -0.0273 963  VAL B CG2 
16170 N N   . ASN B 966  ? 0.2123 0.1943 0.2244 0.0059  -0.0191 -0.0268 964  ASN B N   
16171 C CA  . ASN B 966  ? 0.2144 0.1960 0.2284 0.0059  -0.0180 -0.0261 964  ASN B CA  
16172 C C   . ASN B 966  ? 0.2284 0.2103 0.2461 0.0039  -0.0192 -0.0251 964  ASN B C   
16173 O O   . ASN B 966  ? 0.2617 0.2447 0.2820 0.0037  -0.0180 -0.0241 964  ASN B O   
16174 C CB  . ASN B 966  ? 0.2268 0.2042 0.2373 0.0068  -0.0179 -0.0273 964  ASN B CB  
16175 C CG  . ASN B 966  ? 0.2175 0.1952 0.2251 0.0090  -0.0163 -0.0280 964  ASN B CG  
16176 O OD1 . ASN B 966  ? 0.2312 0.2124 0.2401 0.0098  -0.0149 -0.0274 964  ASN B OD1 
16177 N ND2 . ASN B 966  ? 0.2423 0.2164 0.2461 0.0101  -0.0165 -0.0294 964  ASN B ND2 
16178 N N   . ALA B 967  ? 0.2087 0.1897 0.2265 0.0024  -0.0213 -0.0254 965  ALA B N   
16179 C CA  . ALA B 967  ? 0.2294 0.2105 0.2506 0.0003  -0.0226 -0.0245 965  ALA B CA  
16180 C C   . ALA B 967  ? 0.2393 0.2252 0.2656 -0.0002 -0.0219 -0.0229 965  ALA B C   
16181 O O   . ALA B 967  ? 0.2515 0.2383 0.2813 -0.0019 -0.0224 -0.0220 965  ALA B O   
16182 C CB  . ALA B 967  ? 0.2353 0.2145 0.2552 -0.0012 -0.0254 -0.0253 965  ALA B CB  
16183 N N   . THR B 968  ? 0.2102 0.1992 0.2370 0.0011  -0.0207 -0.0226 966  THR B N   
16184 C CA  . THR B 968  ? 0.2193 0.2124 0.2506 0.0008  -0.0198 -0.0212 966  THR B CA  
16185 C C   . THR B 968  ? 0.2302 0.2239 0.2634 0.0009  -0.0178 -0.0203 966  THR B C   
16186 O O   . THR B 968  ? 0.2325 0.2293 0.2697 0.0004  -0.0171 -0.0191 966  THR B O   
16187 C CB  . THR B 968  ? 0.2209 0.2164 0.2519 0.0023  -0.0188 -0.0211 966  THR B CB  
16188 O OG1 . THR B 968  ? 0.2228 0.2178 0.2515 0.0038  -0.0168 -0.0215 966  THR B OG1 
16189 C CG2 . THR B 968  ? 0.2433 0.2380 0.2717 0.0024  -0.0206 -0.0219 966  THR B CG2 
16190 N N   . GLY B 969  ? 0.2128 0.2037 0.2430 0.0017  -0.0169 -0.0209 967  GLY B N   
16191 C CA  . GLY B 969  ? 0.2148 0.2060 0.2460 0.0021  -0.0151 -0.0201 967  GLY B CA  
16192 C C   . GLY B 969  ? 0.2215 0.2148 0.2523 0.0038  -0.0131 -0.0199 967  GLY B C   
16193 O O   . GLY B 969  ? 0.2127 0.2058 0.2433 0.0043  -0.0117 -0.0194 967  GLY B O   
16194 N N   . TYR B 970  ? 0.2248 0.2200 0.2552 0.0045  -0.0131 -0.0202 968  TYR B N   
16195 C CA  . TYR B 970  ? 0.1999 0.1968 0.2295 0.0059  -0.0115 -0.0201 968  TYR B CA  
16196 C C   . TYR B 970  ? 0.1906 0.1855 0.2163 0.0072  -0.0112 -0.0212 968  TYR B C   
16197 O O   . TYR B 970  ? 0.2190 0.2113 0.2424 0.0071  -0.0123 -0.0222 968  TYR B O   
16198 C CB  . TYR B 970  ? 0.1947 0.1941 0.2255 0.0060  -0.0117 -0.0199 968  TYR B CB  
16199 C CG  . TYR B 970  ? 0.2107 0.2128 0.2457 0.0054  -0.0114 -0.0188 968  TYR B CG  
16200 C CD1 . TYR B 970  ? 0.2465 0.2503 0.2828 0.0059  -0.0095 -0.0181 968  TYR B CD1 
16201 C CD2 . TYR B 970  ? 0.2443 0.2473 0.2818 0.0043  -0.0130 -0.0185 968  TYR B CD2 
16202 C CE1 . TYR B 970  ? 0.3020 0.3083 0.3420 0.0055  -0.0090 -0.0171 968  TYR B CE1 
16203 C CE2 . TYR B 970  ? 0.2702 0.2761 0.3118 0.0038  -0.0125 -0.0173 968  TYR B CE2 
16204 C CZ  . TYR B 970  ? 0.3094 0.3169 0.3522 0.0045  -0.0104 -0.0167 968  TYR B CZ  
16205 O OH  . TYR B 970  ? 0.4393 0.4498 0.4860 0.0043  -0.0096 -0.0156 968  TYR B OH  
16206 N N   . GLY B 971  ? 0.1802 0.1765 0.2052 0.0083  -0.0097 -0.0211 969  GLY B N   
16207 C CA  . GLY B 971  ? 0.1786 0.1738 0.2004 0.0096  -0.0093 -0.0220 969  GLY B CA  
16208 C C   . GLY B 971  ? 0.1813 0.1788 0.2029 0.0105  -0.0078 -0.0217 969  GLY B C   
16209 O O   . GLY B 971  ? 0.1833 0.1808 0.2040 0.0113  -0.0068 -0.0217 969  GLY B O   
16210 N N   . LEU B 972  ? 0.1643 0.1637 0.1865 0.0102  -0.0078 -0.0215 970  LEU B N   
16211 C CA  . LEU B 972  ? 0.1679 0.1693 0.1900 0.0108  -0.0065 -0.0212 970  LEU B CA  
16212 C C   . LEU B 972  ? 0.1609 0.1625 0.1804 0.0114  -0.0065 -0.0219 970  LEU B C   
16213 O O   . LEU B 972  ? 0.1788 0.1803 0.1967 0.0122  -0.0059 -0.0223 970  LEU B O   
16214 C CB  . LEU B 972  ? 0.1825 0.1855 0.2069 0.0103  -0.0063 -0.0204 970  LEU B CB  
16215 C CG  . LEU B 972  ? 0.1687 0.1733 0.1929 0.0107  -0.0051 -0.0201 970  LEU B CG  
16216 C CD1 . LEU B 972  ? 0.2133 0.2179 0.2372 0.0111  -0.0040 -0.0199 970  LEU B CD1 
16217 C CD2 . LEU B 972  ? 0.2008 0.2065 0.2272 0.0103  -0.0048 -0.0194 970  LEU B CD2 
16218 N N   . THR B 973  ? 0.1749 0.1770 0.1940 0.0110  -0.0071 -0.0219 971  THR B N   
16219 C CA  . THR B 973  ? 0.1752 0.1775 0.1917 0.0114  -0.0070 -0.0224 971  THR B CA  
16220 C C   . THR B 973  ? 0.1539 0.1545 0.1686 0.0112  -0.0083 -0.0231 971  THR B C   
16221 O O   . THR B 973  ? 0.1772 0.1768 0.1930 0.0106  -0.0096 -0.0231 971  THR B O   
16222 C CB  . THR B 973  ? 0.1715 0.1753 0.1881 0.0111  -0.0067 -0.0219 971  THR B CB  
16223 O OG1 . THR B 973  ? 0.1607 0.1642 0.1786 0.0105  -0.0077 -0.0215 971  THR B OG1 
16224 C CG2 . THR B 973  ? 0.1874 0.1926 0.2050 0.0112  -0.0054 -0.0214 971  THR B CG2 
16225 N N   . PHE B 974  ? 0.1657 0.1662 0.1777 0.0118  -0.0080 -0.0238 972  PHE B N   
16226 C CA  . PHE B 974  ? 0.1624 0.1611 0.1720 0.0118  -0.0091 -0.0246 972  PHE B CA  
16227 C C   . PHE B 974  ? 0.1576 0.1572 0.1644 0.0123  -0.0083 -0.0249 972  PHE B C   
16228 O O   . PHE B 974  ? 0.1716 0.1726 0.1780 0.0130  -0.0070 -0.0250 972  PHE B O   
16229 C CB  . PHE B 974  ? 0.1689 0.1653 0.1775 0.0124  -0.0094 -0.0255 972  PHE B CB  
16230 C CG  . PHE B 974  ? 0.1726 0.1668 0.1778 0.0125  -0.0103 -0.0266 972  PHE B CG  
16231 C CD1 . PHE B 974  ? 0.2040 0.1966 0.2090 0.0115  -0.0121 -0.0267 972  PHE B CD1 
16232 C CD2 . PHE B 974  ? 0.1963 0.1904 0.1986 0.0137  -0.0093 -0.0274 972  PHE B CD2 
16233 C CE1 . PHE B 974  ? 0.2025 0.1930 0.2040 0.0116  -0.0131 -0.0277 972  PHE B CE1 
16234 C CE2 . PHE B 974  ? 0.2012 0.1932 0.2001 0.0139  -0.0101 -0.0284 972  PHE B CE2 
16235 C CZ  . PHE B 974  ? 0.2162 0.2062 0.2144 0.0128  -0.0120 -0.0286 972  PHE B CZ  
16236 N N   . GLY B 975  ? 0.1732 0.1720 0.1781 0.0118  -0.0093 -0.0251 973  GLY B N   
16237 C CA  . GLY B 975  ? 0.1935 0.1930 0.1955 0.0120  -0.0086 -0.0253 973  GLY B CA  
16238 C C   . GLY B 975  ? 0.1933 0.1908 0.1919 0.0123  -0.0093 -0.0263 973  GLY B C   
16239 O O   . GLY B 975  ? 0.1963 0.1916 0.1944 0.0119  -0.0108 -0.0267 973  GLY B O   
16240 N N   . LEU B 976  ? 0.1874 0.1857 0.1834 0.0130  -0.0080 -0.0268 974  LEU B N   
16241 C CA  . LEU B 976  ? 0.1904 0.1869 0.1825 0.0135  -0.0084 -0.0278 974  LEU B CA  
16242 C C   . LEU B 976  ? 0.2057 0.2039 0.1955 0.0134  -0.0073 -0.0274 974  LEU B C   
16243 O O   . LEU B 976  ? 0.2053 0.2062 0.1959 0.0138  -0.0056 -0.0271 974  LEU B O   
16244 C CB  . LEU B 976  ? 0.2048 0.2001 0.1957 0.0150  -0.0076 -0.0290 974  LEU B CB  
16245 C CG  . LEU B 976  ? 0.2327 0.2260 0.2191 0.0158  -0.0075 -0.0303 974  LEU B CG  
16246 C CD1 . LEU B 976  ? 0.2631 0.2530 0.2477 0.0149  -0.0098 -0.0309 974  LEU B CD1 
16247 C CD2 . LEU B 976  ? 0.2465 0.2390 0.2322 0.0176  -0.0064 -0.0314 974  LEU B CD2 
16248 N N   . HIS B 977  ? 0.1854 0.1822 0.1723 0.0127  -0.0083 -0.0275 975  HIS B N   
16249 C CA  . HIS B 977  ? 0.2017 0.1996 0.1857 0.0125  -0.0073 -0.0271 975  HIS B CA  
16250 C C   . HIS B 977  ? 0.2142 0.2102 0.1937 0.0133  -0.0073 -0.0284 975  HIS B C   
16251 O O   . HIS B 977  ? 0.2155 0.2086 0.1928 0.0129  -0.0091 -0.0290 975  HIS B O   
16252 C CB  . HIS B 977  ? 0.2112 0.2088 0.1949 0.0111  -0.0085 -0.0259 975  HIS B CB  
16253 C CG  . HIS B 977  ? 0.2371 0.2371 0.2235 0.0104  -0.0076 -0.0246 975  HIS B CG  
16254 N ND1 . HIS B 977  ? 0.3122 0.3139 0.2971 0.0098  -0.0064 -0.0238 975  HIS B ND1 
16255 C CD2 . HIS B 977  ? 0.3118 0.3127 0.3021 0.0101  -0.0078 -0.0240 975  HIS B CD2 
16256 C CE1 . HIS B 977  ? 0.2903 0.2935 0.2780 0.0092  -0.0060 -0.0228 975  HIS B CE1 
16257 N NE2 . HIS B 977  ? 0.3059 0.3086 0.2967 0.0094  -0.0068 -0.0229 975  HIS B NE2 
16258 N N   . THR B 978  ? 0.2108 0.2084 0.1888 0.0145  -0.0053 -0.0290 976  THR B N   
16259 C CA  . THR B 978  ? 0.2132 0.2092 0.1867 0.0155  -0.0048 -0.0303 976  THR B CA  
16260 C C   . THR B 978  ? 0.2313 0.2306 0.2042 0.0165  -0.0021 -0.0303 976  THR B C   
16261 O O   . THR B 978  ? 0.2535 0.2560 0.2300 0.0167  -0.0009 -0.0296 976  THR B O   
16262 C CB  . THR B 978  ? 0.2460 0.2389 0.2190 0.0167  -0.0055 -0.0319 976  THR B CB  
16263 O OG1 . THR B 978  ? 0.2293 0.2204 0.1975 0.0179  -0.0048 -0.0333 976  THR B OG1 
16264 C CG2 . THR B 978  ? 0.2739 0.2686 0.2505 0.0178  -0.0043 -0.0319 976  THR B CG2 
16265 N N   . ARG B 979  ? 0.2421 0.2409 0.2106 0.0170  -0.0013 -0.0309 977  ARG B N   
16266 C CA  . ARG B 979  ? 0.2487 0.2509 0.2166 0.0182  0.0014  -0.0311 977  ARG B CA  
16267 C C   . ARG B 979  ? 0.2711 0.2723 0.2378 0.0206  0.0024  -0.0328 977  ARG B C   
16268 O O   . ARG B 979  ? 0.2616 0.2659 0.2281 0.0219  0.0047  -0.0330 977  ARG B O   
16269 C CB  . ARG B 979  ? 0.2960 0.2990 0.2598 0.0174  0.0023  -0.0306 977  ARG B CB  
16270 C CG  . ARG B 979  ? 0.3756 0.3803 0.3411 0.0153  0.0019  -0.0286 977  ARG B CG  
16271 C CD  . ARG B 979  ? 0.4732 0.4778 0.4342 0.0143  0.0024  -0.0281 977  ARG B CD  
16272 N NE  . ARG B 979  ? 0.5317 0.5380 0.4943 0.0123  0.0023  -0.0261 977  ARG B NE  
16273 C CZ  . ARG B 979  ? 0.6546 0.6611 0.6138 0.0111  0.0027  -0.0251 977  ARG B CZ  
16274 N NH1 . ARG B 979  ? 0.5003 0.5056 0.4544 0.0117  0.0033  -0.0259 977  ARG B NH1 
16275 N NH2 . ARG B 979  ? 0.6361 0.6437 0.5968 0.0093  0.0025  -0.0234 977  ARG B NH2 
16276 N N   . LEU B 980  ? 0.2325 0.2295 0.1984 0.0211  0.0007  -0.0340 978  LEU B N   
16277 C CA  . LEU B 980  ? 0.2262 0.2208 0.1894 0.0233  0.0013  -0.0359 978  LEU B CA  
16278 C C   . LEU B 980  ? 0.2393 0.2341 0.2062 0.0247  0.0015  -0.0362 978  LEU B C   
16279 O O   . LEU B 980  ? 0.2471 0.2399 0.2165 0.0238  -0.0003 -0.0359 978  LEU B O   
16280 C CB  . LEU B 980  ? 0.2546 0.2436 0.2137 0.0228  -0.0010 -0.0371 978  LEU B CB  
16281 C CG  . LEU B 980  ? 0.2803 0.2688 0.2355 0.0214  -0.0016 -0.0367 978  LEU B CG  
16282 C CD1 . LEU B 980  ? 0.2861 0.2691 0.2373 0.0209  -0.0041 -0.0379 978  LEU B CD1 
16283 C CD2 . LEU B 980  ? 0.2617 0.2526 0.2136 0.0224  0.0010  -0.0369 978  LEU B CD2 
16284 N N   . ASP B 981  ? 0.2419 0.2390 0.2090 0.0269  0.0037  -0.0367 979  ASP B N   
16285 C CA  . ASP B 981  ? 0.2294 0.2269 0.2000 0.0283  0.0039  -0.0368 979  ASP B CA  
16286 C C   . ASP B 981  ? 0.2374 0.2292 0.2067 0.0289  0.0021  -0.0381 979  ASP B C   
16287 O O   . ASP B 981  ? 0.2409 0.2322 0.2135 0.0288  0.0013  -0.0377 979  ASP B O   
16288 C CB  . ASP B 981  ? 0.2447 0.2454 0.2154 0.0309  0.0065  -0.0373 979  ASP B CB  
16289 C CG  . ASP B 981  ? 0.2659 0.2731 0.2395 0.0303  0.0082  -0.0358 979  ASP B CG  
16290 O OD1 . ASP B 981  ? 0.3002 0.3092 0.2765 0.0280  0.0074  -0.0343 979  ASP B OD1 
16291 O OD2 . ASP B 981  ? 0.3017 0.3120 0.2749 0.0322  0.0105  -0.0361 979  ASP B OD2 
16292 N N   . GLU B 982  ? 0.2269 0.2143 0.1911 0.0293  0.0015  -0.0397 980  GLU B N   
16293 C CA  . GLU B 982  ? 0.2418 0.2236 0.2046 0.0296  -0.0004 -0.0409 980  GLU B CA  
16294 C C   . GLU B 982  ? 0.2432 0.2236 0.2087 0.0270  -0.0029 -0.0399 980  GLU B C   
16295 O O   . GLU B 982  ? 0.2505 0.2283 0.2179 0.0269  -0.0041 -0.0400 980  GLU B O   
16296 C CB  . GLU B 982  ? 0.2686 0.2457 0.2251 0.0303  -0.0008 -0.0429 980  GLU B CB  
16297 C CG  . GLU B 982  ? 0.3157 0.2865 0.2704 0.0304  -0.0029 -0.0442 980  GLU B CG  
16298 C CD  . GLU B 982  ? 0.3897 0.3555 0.3381 0.0301  -0.0041 -0.0459 980  GLU B CD  
16299 O OE1 . GLU B 982  ? 0.4623 0.4290 0.4086 0.0286  -0.0046 -0.0455 980  GLU B OE1 
16300 O OE2 . GLU B 982  ? 0.3748 0.3353 0.3201 0.0314  -0.0048 -0.0477 980  GLU B OE2 
16301 N N   . THR B 983  ? 0.2400 0.2220 0.2057 0.0249  -0.0036 -0.0389 981  THR B N   
16302 C CA  . THR B 983  ? 0.2235 0.2048 0.1921 0.0226  -0.0058 -0.0378 981  THR B CA  
16303 C C   . THR B 983  ? 0.2265 0.2110 0.2006 0.0224  -0.0053 -0.0364 981  THR B C   
16304 O O   . THR B 983  ? 0.2344 0.2174 0.2112 0.0214  -0.0067 -0.0359 981  THR B O   
16305 C CB  . THR B 983  ? 0.2413 0.2236 0.2085 0.0208  -0.0066 -0.0370 981  THR B CB  
16306 O OG1 . THR B 983  ? 0.2688 0.2475 0.2305 0.0210  -0.0074 -0.0384 981  THR B OG1 
16307 C CG2 . THR B 983  ? 0.2479 0.2300 0.2185 0.0187  -0.0088 -0.0358 981  THR B CG2 
16308 N N   . ILE B 984  ? 0.2146 0.2036 0.1905 0.0231  -0.0032 -0.0356 982  ILE B N   
16309 C CA  . ILE B 984  ? 0.2126 0.2046 0.1934 0.0230  -0.0027 -0.0343 982  ILE B CA  
16310 C C   . ILE B 984  ? 0.2183 0.2080 0.2001 0.0244  -0.0028 -0.0350 982  ILE B C   
16311 O O   . ILE B 984  ? 0.2299 0.2191 0.2147 0.0236  -0.0038 -0.0342 982  ILE B O   
16312 C CB  . ILE B 984  ? 0.2102 0.2073 0.1923 0.0235  -0.0006 -0.0335 982  ILE B CB  
16313 C CG1 . ILE B 984  ? 0.2732 0.2722 0.2547 0.0217  -0.0007 -0.0325 982  ILE B CG1 
16314 C CG2 . ILE B 984  ? 0.2334 0.2334 0.2201 0.0236  -0.0001 -0.0324 982  ILE B CG2 
16315 C CD1 . ILE B 984  ? 0.2554 0.2591 0.2374 0.0220  0.0014  -0.0318 982  ILE B CD1 
16316 N N   . ALA B 985  ? 0.2226 0.2107 0.2016 0.0266  -0.0019 -0.0363 983  ALA B N   
16317 C CA  . ALA B 985  ? 0.2356 0.2213 0.2153 0.0282  -0.0020 -0.0369 983  ALA B CA  
16318 C C   . ALA B 985  ? 0.2325 0.2131 0.2117 0.0269  -0.0042 -0.0373 983  ALA B C   
16319 O O   . ALA B 985  ? 0.2415 0.2212 0.2234 0.0267  -0.0048 -0.0367 983  ALA B O   
16320 C CB  . ALA B 985  ? 0.2308 0.2153 0.2073 0.0311  -0.0005 -0.0384 983  ALA B CB  
16321 N N   . HIS B 986  ? 0.2395 0.2169 0.2153 0.0259  -0.0056 -0.0382 984  HIS B N   
16322 C CA  . HIS B 986  ? 0.2529 0.2257 0.2282 0.0244  -0.0079 -0.0386 984  HIS B CA  
16323 C C   . HIS B 986  ? 0.2462 0.2210 0.2261 0.0222  -0.0089 -0.0369 984  HIS B C   
16324 O O   . HIS B 986  ? 0.2393 0.2125 0.2215 0.0218  -0.0096 -0.0365 984  HIS B O   
16325 C CB  . HIS B 986  ? 0.2674 0.2373 0.2383 0.0235  -0.0092 -0.0397 984  HIS B CB  
16326 C CG  . HIS B 986  ? 0.2876 0.2533 0.2581 0.0216  -0.0119 -0.0400 984  HIS B CG  
16327 N ND1 . HIS B 986  ? 0.3535 0.3159 0.3199 0.0207  -0.0135 -0.0411 984  HIS B ND1 
16328 C CD2 . HIS B 986  ? 0.2899 0.2543 0.2637 0.0203  -0.0132 -0.0393 984  HIS B CD2 
16329 C CE1 . HIS B 986  ? 0.3293 0.2886 0.2965 0.0188  -0.0159 -0.0411 984  HIS B CE1 
16330 N NE2 . HIS B 986  ? 0.3100 0.2706 0.2818 0.0185  -0.0157 -0.0399 984  HIS B NE2 
16331 N N   . VAL B 987  ? 0.2170 0.1953 0.1983 0.0209  -0.0088 -0.0358 985  VAL B N   
16332 C CA  . VAL B 987  ? 0.2248 0.2047 0.2102 0.0189  -0.0099 -0.0343 985  VAL B CA  
16333 C C   . VAL B 987  ? 0.2311 0.2133 0.2203 0.0194  -0.0088 -0.0333 985  VAL B C   
16334 O O   . VAL B 987  ? 0.2403 0.2217 0.2322 0.0183  -0.0098 -0.0326 985  VAL B O   
16335 C CB  . VAL B 987  ? 0.2254 0.2081 0.2109 0.0177  -0.0100 -0.0335 985  VAL B CB  
16336 C CG1 . VAL B 987  ? 0.2447 0.2295 0.2346 0.0161  -0.0107 -0.0320 985  VAL B CG1 
16337 C CG2 . VAL B 987  ? 0.2213 0.2011 0.2030 0.0169  -0.0117 -0.0344 985  VAL B CG2 
16338 N N   . THR B 988  ? 0.2298 0.2151 0.2195 0.0209  -0.0069 -0.0330 986  THR B N   
16339 C CA  . THR B 988  ? 0.2327 0.2203 0.2260 0.0213  -0.0061 -0.0320 986  THR B CA  
16340 C C   . THR B 988  ? 0.2452 0.2296 0.2385 0.0223  -0.0063 -0.0324 986  THR B C   
16341 O O   . THR B 988  ? 0.3042 0.2893 0.3003 0.0219  -0.0063 -0.0314 986  THR B O   
16342 C CB  . THR B 988  ? 0.2658 0.2579 0.2598 0.0224  -0.0041 -0.0315 986  THR B CB  
16343 O OG1 . THR B 988  ? 0.2957 0.2872 0.2870 0.0245  -0.0031 -0.0327 986  THR B OG1 
16344 C CG2 . THR B 988  ? 0.2944 0.2893 0.2884 0.0211  -0.0039 -0.0309 986  THR B CG2 
16345 N N   . SER B 989  ? 0.2477 0.2282 0.2375 0.0235  -0.0067 -0.0339 987  SER B N   
16346 C CA  . SER B 989  ? 0.2811 0.2577 0.2705 0.0244  -0.0071 -0.0343 987  SER B CA  
16347 C C   . SER B 989  ? 0.2927 0.2662 0.2832 0.0222  -0.0090 -0.0340 987  SER B C   
16348 O O   . SER B 989  ? 0.3780 0.3491 0.3694 0.0224  -0.0094 -0.0337 987  SER B O   
16349 C CB  . SER B 989  ? 0.3104 0.2835 0.2956 0.0265  -0.0068 -0.0361 987  SER B CB  
16350 O OG  . SER B 989  ? 0.4060 0.3756 0.3878 0.0256  -0.0081 -0.0373 987  SER B OG  
16351 N N   . ARG B 990  ? 0.2449 0.2185 0.2354 0.0202  -0.0103 -0.0339 988  ARG B N   
16352 C CA  . ARG B 990  ? 0.2419 0.2127 0.2333 0.0182  -0.0123 -0.0337 988  ARG B CA  
16353 C C   . ARG B 990  ? 0.2351 0.2092 0.2308 0.0163  -0.0126 -0.0320 988  ARG B C   
16354 O O   . ARG B 990  ? 0.2409 0.2134 0.2385 0.0147  -0.0137 -0.0314 988  ARG B O   
16355 C CB  . ARG B 990  ? 0.2671 0.2349 0.2551 0.0173  -0.0139 -0.0349 988  ARG B CB  
16356 C CG  . ARG B 990  ? 0.3426 0.3069 0.3256 0.0193  -0.0135 -0.0368 988  ARG B CG  
16357 C CD  . ARG B 990  ? 0.3678 0.3268 0.3493 0.0197  -0.0142 -0.0376 988  ARG B CD  
16358 N NE  . ARG B 990  ? 0.2970 0.2516 0.2764 0.0179  -0.0166 -0.0384 988  ARG B NE  
16359 C CZ  . ARG B 990  ? 0.2991 0.2483 0.2769 0.0176  -0.0178 -0.0392 988  ARG B CZ  
16360 N NH1 . ARG B 990  ? 0.3557 0.3031 0.3338 0.0192  -0.0168 -0.0391 988  ARG B NH1 
16361 N NH2 . ARG B 990  ? 0.3060 0.2513 0.2817 0.0158  -0.0201 -0.0400 988  ARG B NH2 
16362 N N   . ILE B 991  ? 0.2105 0.1889 0.2076 0.0163  -0.0116 -0.0312 989  ILE B N   
16363 C CA  . ILE B 991  ? 0.2278 0.2091 0.2287 0.0147  -0.0117 -0.0298 989  ILE B CA  
16364 C C   . ILE B 991  ? 0.2270 0.2092 0.2306 0.0150  -0.0108 -0.0287 989  ILE B C   
16365 O O   . ILE B 991  ? 0.2519 0.2340 0.2548 0.0167  -0.0097 -0.0289 989  ILE B O   
16366 C CB  . ILE B 991  ? 0.2308 0.2160 0.2320 0.0148  -0.0109 -0.0293 989  ILE B CB  
16367 C CG1 . ILE B 991  ? 0.2642 0.2516 0.2687 0.0132  -0.0114 -0.0280 989  ILE B CG1 
16368 C CG2 . ILE B 991  ? 0.2531 0.2408 0.2545 0.0164  -0.0090 -0.0291 989  ILE B CG2 
16369 C CD1 . ILE B 991  ? 0.3038 0.2897 0.3085 0.0117  -0.0134 -0.0281 989  ILE B CD1 
16370 N N   . LYS B 992  ? 0.2017 0.1848 0.2086 0.0135  -0.0113 -0.0276 990  LYS B N   
16371 C CA  . LYS B 992  ? 0.2225 0.2063 0.2317 0.0135  -0.0105 -0.0266 990  LYS B CA  
16372 C C   . LYS B 992  ? 0.2352 0.2229 0.2473 0.0128  -0.0098 -0.0254 990  LYS B C   
16373 O O   . LYS B 992  ? 0.2776 0.2660 0.2923 0.0114  -0.0103 -0.0245 990  LYS B O   
16374 C CB  . LYS B 992  ? 0.2300 0.2107 0.2401 0.0123  -0.0116 -0.0263 990  LYS B CB  
16375 C CG  . LYS B 992  ? 0.2897 0.2657 0.2966 0.0130  -0.0124 -0.0275 990  LYS B CG  
16376 C CD  . LYS B 992  ? 0.3696 0.3424 0.3773 0.0113  -0.0137 -0.0272 990  LYS B CD  
16377 C CE  . LYS B 992  ? 0.4331 0.4069 0.4436 0.0109  -0.0128 -0.0257 990  LYS B CE  
16378 N NZ  . LYS B 992  ? 0.5285 0.5001 0.5407 0.0087  -0.0141 -0.0250 990  LYS B NZ  
16379 N N   . ALA B 993  ? 0.2131 0.2035 0.2248 0.0138  -0.0086 -0.0253 991  ALA B N   
16380 C CA  . ALA B 993  ? 0.1925 0.1862 0.2065 0.0133  -0.0079 -0.0243 991  ALA B CA  
16381 C C   . ALA B 993  ? 0.1906 0.1863 0.2045 0.0145  -0.0064 -0.0240 991  ALA B C   
16382 O O   . ALA B 993  ? 0.2111 0.2064 0.2231 0.0158  -0.0059 -0.0247 991  ALA B O   
16383 C CB  . ALA B 993  ? 0.2305 0.2255 0.2440 0.0127  -0.0083 -0.0245 991  ALA B CB  
16384 N N   . GLY B 994  ? 0.1787 0.1765 0.1946 0.0140  -0.0057 -0.0230 992  GLY B N   
16385 C CA  . GLY B 994  ? 0.1859 0.1856 0.2019 0.0149  -0.0045 -0.0227 992  GLY B CA  
16386 C C   . GLY B 994  ? 0.1846 0.1868 0.1997 0.0152  -0.0039 -0.0229 992  GLY B C   
16387 O O   . GLY B 994  ? 0.1662 0.1698 0.1809 0.0162  -0.0032 -0.0228 992  GLY B O   
16388 N N   . ASN B 995  ? 0.1757 0.1784 0.1905 0.0145  -0.0043 -0.0230 993  ASN B N   
16389 C CA  . ASN B 995  ? 0.1670 0.1718 0.1808 0.0145  -0.0038 -0.0231 993  ASN B CA  
16390 C C   . ASN B 995  ? 0.1681 0.1719 0.1801 0.0144  -0.0044 -0.0238 993  ASN B C   
16391 O O   . ASN B 995  ? 0.1730 0.1758 0.1853 0.0135  -0.0054 -0.0237 993  ASN B O   
16392 C CB  . ASN B 995  ? 0.1735 0.1798 0.1888 0.0135  -0.0035 -0.0223 993  ASN B CB  
16393 C CG  . ASN B 995  ? 0.1925 0.2002 0.2087 0.0137  -0.0027 -0.0217 993  ASN B CG  
16394 O OD1 . ASN B 995  ? 0.1732 0.1801 0.1907 0.0137  -0.0027 -0.0213 993  ASN B OD1 
16395 N ND2 . ASN B 995  ? 0.1865 0.1962 0.2021 0.0139  -0.0021 -0.0216 993  ASN B ND2 
16396 N N   . LEU B 996  ? 0.1684 0.1729 0.1786 0.0153  -0.0039 -0.0244 994  LEU B N   
16397 C CA  . LEU B 996  ? 0.1604 0.1639 0.1681 0.0154  -0.0043 -0.0251 994  LEU B CA  
16398 C C   . LEU B 996  ? 0.1616 0.1677 0.1686 0.0151  -0.0035 -0.0248 994  LEU B C   
16399 O O   . LEU B 996  ? 0.1703 0.1789 0.1782 0.0153  -0.0025 -0.0244 994  LEU B O   
16400 C CB  . LEU B 996  ? 0.1817 0.1838 0.1875 0.0169  -0.0041 -0.0262 994  LEU B CB  
16401 C CG  . LEU B 996  ? 0.1962 0.1956 0.2027 0.0173  -0.0047 -0.0264 994  LEU B CG  
16402 C CD1 . LEU B 996  ? 0.2530 0.2506 0.2572 0.0190  -0.0044 -0.0275 994  LEU B CD1 
16403 C CD2 . LEU B 996  ? 0.2098 0.2069 0.2170 0.0160  -0.0061 -0.0263 994  LEU B CD2 
16404 N N   . TYR B 997  ? 0.1679 0.1733 0.1730 0.0145  -0.0040 -0.0250 995  TYR B N   
16405 C CA  . TYR B 997  ? 0.1775 0.1849 0.1816 0.0139  -0.0034 -0.0246 995  TYR B CA  
16406 C C   . TYR B 997  ? 0.1719 0.1783 0.1728 0.0141  -0.0036 -0.0253 995  TYR B C   
16407 O O   . TYR B 997  ? 0.2009 0.2048 0.2007 0.0138  -0.0049 -0.0257 995  TYR B O   
16408 C CB  . TYR B 997  ? 0.1950 0.2024 0.2002 0.0125  -0.0040 -0.0237 995  TYR B CB  
16409 C CG  . TYR B 997  ? 0.1798 0.1878 0.1878 0.0123  -0.0039 -0.0231 995  TYR B CG  
16410 C CD1 . TYR B 997  ? 0.1685 0.1749 0.1781 0.0123  -0.0047 -0.0231 995  TYR B CD1 
16411 C CD2 . TYR B 997  ? 0.1941 0.2043 0.2030 0.0120  -0.0030 -0.0225 995  TYR B CD2 
16412 C CE1 . TYR B 997  ? 0.1977 0.2046 0.2096 0.0122  -0.0044 -0.0226 995  TYR B CE1 
16413 C CE2 . TYR B 997  ? 0.1941 0.2045 0.2051 0.0118  -0.0029 -0.0221 995  TYR B CE2 
16414 C CZ  . TYR B 997  ? 0.2023 0.2110 0.2146 0.0120  -0.0035 -0.0221 995  TYR B CZ  
16415 O OH  . TYR B 997  ? 0.2373 0.2463 0.2515 0.0119  -0.0032 -0.0216 995  TYR B OH  
16416 N N   . ILE B 998  ? 0.1813 0.1897 0.1808 0.0147  -0.0023 -0.0255 996  ILE B N   
16417 C CA  . ILE B 998  ? 0.1735 0.1811 0.1697 0.0151  -0.0021 -0.0262 996  ILE B CA  
16418 C C   . ILE B 998  ? 0.2068 0.2161 0.2017 0.0139  -0.0016 -0.0254 996  ILE B C   
16419 O O   . ILE B 998  ? 0.1939 0.2064 0.1899 0.0137  -0.0004 -0.0248 996  ILE B O   
16420 C CB  . ILE B 998  ? 0.2123 0.2208 0.2075 0.0169  -0.0009 -0.0271 996  ILE B CB  
16421 C CG1 . ILE B 998  ? 0.2566 0.2629 0.2529 0.0180  -0.0014 -0.0278 996  ILE B CG1 
16422 C CG2 . ILE B 998  ? 0.2205 0.2279 0.2117 0.0174  -0.0006 -0.0280 996  ILE B CG2 
16423 C CD1 . ILE B 998  ? 0.2997 0.3020 0.2948 0.0177  -0.0031 -0.0285 996  ILE B CD1 
16424 N N   . ASN B 999  ? 0.1801 0.1874 0.1728 0.0131  -0.0027 -0.0253 997  ASN B N   
16425 C CA  . ASN B 999  ? 0.1998 0.2080 0.1905 0.0120  -0.0023 -0.0245 997  ASN B CA  
16426 C C   . ASN B 999  ? 0.1817 0.1915 0.1748 0.0107  -0.0022 -0.0232 997  ASN B C   
16427 O O   . ASN B 999  ? 0.2022 0.2139 0.1946 0.0099  -0.0013 -0.0225 997  ASN B O   
16428 C CB  . ASN B 999  ? 0.1974 0.2076 0.1858 0.0127  -0.0006 -0.0249 997  ASN B CB  
16429 C CG  . ASN B 999  ? 0.2078 0.2158 0.1930 0.0138  -0.0009 -0.0262 997  ASN B CG  
16430 O OD1 . ASN B 999  ? 0.2129 0.2177 0.1965 0.0135  -0.0025 -0.0266 997  ASN B OD1 
16431 N ND2 . ASN B 999  ? 0.2203 0.2298 0.2045 0.0153  0.0007  -0.0270 997  ASN B ND2 
16432 N N   . ARG B 1000 ? 0.1985 0.2073 0.1941 0.0105  -0.0032 -0.0230 998  ARG B N   
16433 C CA  . ARG B 1000 ? 0.1919 0.2014 0.1894 0.0094  -0.0032 -0.0219 998  ARG B CA  
16434 C C   . ARG B 1000 ? 0.2094 0.2168 0.2088 0.0093  -0.0046 -0.0218 998  ARG B C   
16435 O O   . ARG B 1000 ? 0.2167 0.2224 0.2160 0.0099  -0.0056 -0.0224 998  ARG B O   
16436 C CB  . ARG B 1000 ? 0.1916 0.2039 0.1913 0.0096  -0.0019 -0.0218 998  ARG B CB  
16437 C CG  . ARG B 1000 ? 0.2041 0.2165 0.2054 0.0109  -0.0018 -0.0226 998  ARG B CG  
16438 C CD  . ARG B 1000 ? 0.1921 0.2065 0.1961 0.0109  -0.0012 -0.0221 998  ARG B CD  
16439 N NE  . ARG B 1000 ? 0.1606 0.1737 0.1659 0.0100  -0.0019 -0.0215 998  ARG B NE  
16440 C CZ  . ARG B 1000 ? 0.1712 0.1855 0.1782 0.0096  -0.0016 -0.0211 998  ARG B CZ  
16441 N NH1 . ARG B 1000 ? 0.2017 0.2185 0.2095 0.0099  -0.0007 -0.0210 998  ARG B NH1 
16442 N NH2 . ARG B 1000 ? 0.1950 0.2078 0.2028 0.0089  -0.0022 -0.0206 998  ARG B NH2 
16443 N N   . ASN B 1001 ? 0.1733 0.1808 0.1742 0.0085  -0.0047 -0.0210 999  ASN B N   
16444 C CA  . ASN B 1001 ? 0.1843 0.1904 0.1874 0.0086  -0.0058 -0.0208 999  ASN B CA  
16445 C C   . ASN B 1001 ? 0.1796 0.1862 0.1850 0.0094  -0.0055 -0.0214 999  ASN B C   
16446 O O   . ASN B 1001 ? 0.1994 0.2074 0.2049 0.0100  -0.0045 -0.0217 999  ASN B O   
16447 C CB  . ASN B 1001 ? 0.2027 0.2084 0.2065 0.0078  -0.0059 -0.0199 999  ASN B CB  
16448 C CG  . ASN B 1001 ? 0.2280 0.2353 0.2330 0.0076  -0.0047 -0.0197 999  ASN B CG  
16449 O OD1 . ASN B 1001 ? 0.2188 0.2271 0.2256 0.0082  -0.0042 -0.0201 999  ASN B OD1 
16450 N ND2 . ASN B 1001 ? 0.3410 0.3485 0.3450 0.0066  -0.0044 -0.0191 999  ASN B ND2 
16451 N N   . ILE B 1002 ? 0.1892 0.1946 0.1966 0.0096  -0.0063 -0.0213 1000 ILE B N   
16452 C CA  . ILE B 1002 ? 0.1902 0.1958 0.1996 0.0102  -0.0061 -0.0217 1000 ILE B CA  
16453 C C   . ILE B 1002 ? 0.1959 0.2021 0.2076 0.0101  -0.0056 -0.0211 1000 ILE B C   
16454 O O   . ILE B 1002 ? 0.1995 0.2056 0.2132 0.0104  -0.0056 -0.0212 1000 ILE B O   
16455 C CB  . ILE B 1002 ? 0.1967 0.2007 0.2065 0.0104  -0.0074 -0.0221 1000 ILE B CB  
16456 C CG1 . ILE B 1002 ? 0.1860 0.1892 0.1974 0.0099  -0.0085 -0.0215 1000 ILE B CG1 
16457 C CG2 . ILE B 1002 ? 0.2027 0.2058 0.2097 0.0106  -0.0078 -0.0228 1000 ILE B CG2 
16458 C CD1 . ILE B 1002 ? 0.1868 0.1890 0.1996 0.0099  -0.0098 -0.0218 1000 ILE B CD1 
16459 N N   . ILE B 1003 ? 0.1971 0.2039 0.2085 0.0095  -0.0051 -0.0206 1001 ILE B N   
16460 C CA  . ILE B 1003 ? 0.2122 0.2192 0.2254 0.0095  -0.0047 -0.0202 1001 ILE B CA  
16461 C C   . ILE B 1003 ? 0.3082 0.3167 0.3213 0.0094  -0.0036 -0.0202 1001 ILE B C   
16462 O O   . ILE B 1003 ? 0.2891 0.2977 0.3030 0.0092  -0.0032 -0.0199 1001 ILE B O   
16463 C CB  . ILE B 1003 ? 0.2509 0.2568 0.2643 0.0091  -0.0052 -0.0197 1001 ILE B CB  
16464 C CG1 . ILE B 1003 ? 0.3028 0.3084 0.3138 0.0083  -0.0052 -0.0193 1001 ILE B CG1 
16465 C CG2 . ILE B 1003 ? 0.2443 0.2492 0.2587 0.0093  -0.0064 -0.0196 1001 ILE B CG2 
16466 C CD1 . ILE B 1003 ? 0.3897 0.3938 0.4007 0.0081  -0.0057 -0.0188 1001 ILE B CD1 
16467 N N   . GLY B 1004 ? 0.2563 0.2661 0.2684 0.0096  -0.0031 -0.0205 1002 GLY B N   
16468 C CA  . GLY B 1004 ? 0.2393 0.2510 0.2515 0.0095  -0.0023 -0.0204 1002 GLY B CA  
16469 C C   . GLY B 1004 ? 0.2445 0.2565 0.2583 0.0102  -0.0019 -0.0205 1002 GLY B C   
16470 O O   . GLY B 1004 ? 0.2714 0.2829 0.2857 0.0110  -0.0021 -0.0208 1002 GLY B O   
16471 N N   . ALA B 1005 ? 0.2331 0.2456 0.2473 0.0098  -0.0016 -0.0201 1003 ALA B N   
16472 C CA  . ALA B 1005 ? 0.2578 0.2706 0.2731 0.0103  -0.0012 -0.0201 1003 ALA B CA  
16473 C C   . ALA B 1005 ? 0.2473 0.2617 0.2621 0.0098  -0.0008 -0.0198 1003 ALA B C   
16474 O O   . ALA B 1005 ? 0.2554 0.2696 0.2704 0.0097  -0.0006 -0.0196 1003 ALA B O   
16475 C CB  . ALA B 1005 ? 0.2387 0.2498 0.2550 0.0102  -0.0013 -0.0199 1003 ALA B CB  
16476 N N   . VAL B 1006 ? 0.1909 0.2072 0.2049 0.0095  -0.0007 -0.0198 1004 VAL B N   
16477 C CA  . VAL B 1006 ? 0.2034 0.2216 0.2172 0.0088  -0.0005 -0.0196 1004 VAL B CA  
16478 C C   . VAL B 1006 ? 0.1984 0.2178 0.2131 0.0097  -0.0003 -0.0195 1004 VAL B C   
16479 O O   . VAL B 1006 ? 0.1876 0.2078 0.2028 0.0108  -0.0002 -0.0197 1004 VAL B O   
16480 C CB  . VAL B 1006 ? 0.2108 0.2312 0.2240 0.0082  -0.0003 -0.0195 1004 VAL B CB  
16481 C CG1 . VAL B 1006 ? 0.2165 0.2395 0.2299 0.0073  -0.0002 -0.0191 1004 VAL B CG1 
16482 C CG2 . VAL B 1006 ? 0.2236 0.2426 0.2356 0.0071  -0.0005 -0.0194 1004 VAL B CG2 
16483 N N   . VAL B 1007 ? 0.2001 0.2192 0.2146 0.0092  -0.0003 -0.0193 1005 VAL B N   
16484 C CA  . VAL B 1007 ? 0.1941 0.2137 0.2091 0.0099  -0.0003 -0.0191 1005 VAL B CA  
16485 C C   . VAL B 1007 ? 0.1878 0.2105 0.2034 0.0105  -0.0003 -0.0189 1005 VAL B C   
16486 O O   . VAL B 1007 ? 0.1904 0.2154 0.2059 0.0097  -0.0004 -0.0188 1005 VAL B O   
16487 C CB  . VAL B 1007 ? 0.1937 0.2127 0.2079 0.0091  -0.0003 -0.0189 1005 VAL B CB  
16488 C CG1 . VAL B 1007 ? 0.1926 0.2123 0.2068 0.0098  -0.0004 -0.0186 1005 VAL B CG1 
16489 C CG2 . VAL B 1007 ? 0.2166 0.2327 0.2304 0.0089  -0.0001 -0.0190 1005 VAL B CG2 
16490 N N   . GLY B 1008 ? 0.1833 0.2061 0.1995 0.0120  -0.0003 -0.0189 1006 GLY B N   
16491 C CA  . GLY B 1008 ? 0.1759 0.2015 0.1928 0.0130  -0.0003 -0.0188 1006 GLY B CA  
16492 C C   . GLY B 1008 ? 0.1936 0.2209 0.2108 0.0134  0.0001  -0.0192 1006 GLY B C   
16493 O O   . GLY B 1008 ? 0.2251 0.2551 0.2430 0.0144  0.0002  -0.0191 1006 GLY B O   
16494 N N   . VAL B 1009 ? 0.1810 0.2066 0.1974 0.0127  0.0002  -0.0195 1007 VAL B N   
16495 C CA  . VAL B 1009 ? 0.1881 0.2148 0.2042 0.0131  0.0005  -0.0199 1007 VAL B CA  
16496 C C   . VAL B 1009 ? 0.1971 0.2208 0.2126 0.0139  0.0005  -0.0205 1007 VAL B C   
16497 O O   . VAL B 1009 ? 0.1998 0.2237 0.2151 0.0152  0.0007  -0.0209 1007 VAL B O   
16498 C CB  . VAL B 1009 ? 0.1950 0.2227 0.2105 0.0113  0.0006  -0.0197 1007 VAL B CB  
16499 C CG1 . VAL B 1009 ? 0.1955 0.2243 0.2103 0.0116  0.0012  -0.0200 1007 VAL B CG1 
16500 C CG2 . VAL B 1009 ? 0.1865 0.2171 0.2026 0.0102  0.0006  -0.0191 1007 VAL B CG2 
16501 N N   . GLN B 1010 ? 0.1827 0.2037 0.1979 0.0131  0.0001  -0.0205 1008 GLN B N   
16502 C CA  . GLN B 1010 ? 0.1779 0.1959 0.1929 0.0137  -0.0003 -0.0209 1008 GLN B CA  
16503 C C   . GLN B 1010 ? 0.1862 0.2027 0.2021 0.0137  -0.0005 -0.0205 1008 GLN B C   
16504 O O   . GLN B 1010 ? 0.2050 0.2200 0.2211 0.0129  -0.0007 -0.0204 1008 GLN B O   
16505 C CB  . GLN B 1010 ? 0.2016 0.2180 0.2159 0.0129  -0.0006 -0.0211 1008 GLN B CB  
16506 C CG  . GLN B 1010 ? 0.2179 0.2355 0.2309 0.0127  -0.0004 -0.0213 1008 GLN B CG  
16507 C CD  . GLN B 1010 ? 0.2165 0.2354 0.2290 0.0113  -0.0003 -0.0208 1008 GLN B CD  
16508 O OE1 . GLN B 1010 ? 0.2234 0.2410 0.2362 0.0104  -0.0006 -0.0205 1008 GLN B OE1 
16509 N NE2 . GLN B 1010 ? 0.2043 0.2256 0.2163 0.0111  0.0003  -0.0208 1008 GLN B NE2 
16510 N N   . PRO B 1011 ? 0.1690 0.1859 0.1854 0.0147  -0.0004 -0.0203 1009 PRO B N   
16511 C CA  . PRO B 1011 ? 0.1826 0.1977 0.1995 0.0147  -0.0005 -0.0199 1009 PRO B CA  
16512 C C   . PRO B 1011 ? 0.1624 0.1750 0.1796 0.0145  -0.0008 -0.0202 1009 PRO B C   
16513 O O   . PRO B 1011 ? 0.1708 0.1824 0.1876 0.0149  -0.0011 -0.0207 1009 PRO B O   
16514 C CB  . PRO B 1011 ? 0.1836 0.1989 0.2006 0.0161  -0.0004 -0.0198 1009 PRO B CB  
16515 C CG  . PRO B 1011 ? 0.2017 0.2201 0.2186 0.0166  -0.0002 -0.0199 1009 PRO B CG  
16516 C CD  . PRO B 1011 ? 0.2020 0.2209 0.2184 0.0159  -0.0001 -0.0204 1009 PRO B CD  
16517 N N   . PHE B 1012 ? 0.1652 0.1768 0.1830 0.0137  -0.0007 -0.0198 1010 PHE B N   
16518 C CA  . PHE B 1012 ? 0.1652 0.1752 0.1835 0.0132  -0.0011 -0.0200 1010 PHE B CA  
16519 C C   . PHE B 1012 ? 0.1721 0.1806 0.1916 0.0132  -0.0011 -0.0196 1010 PHE B C   
16520 O O   . PHE B 1012 ? 0.1823 0.1909 0.2021 0.0131  -0.0006 -0.0190 1010 PHE B O   
16521 C CB  . PHE B 1012 ? 0.1758 0.1862 0.1943 0.0123  -0.0010 -0.0198 1010 PHE B CB  
16522 C CG  . PHE B 1012 ? 0.1633 0.1725 0.1825 0.0119  -0.0015 -0.0199 1010 PHE B CG  
16523 C CD1 . PHE B 1012 ? 0.1809 0.1899 0.1993 0.0118  -0.0021 -0.0204 1010 PHE B CD1 
16524 C CD2 . PHE B 1012 ? 0.1831 0.1915 0.2038 0.0117  -0.0014 -0.0196 1010 PHE B CD2 
16525 C CE1 . PHE B 1012 ? 0.1887 0.1966 0.2077 0.0115  -0.0029 -0.0204 1010 PHE B CE1 
16526 C CE2 . PHE B 1012 ? 0.1882 0.1959 0.2100 0.0114  -0.0021 -0.0196 1010 PHE B CE2 
16527 C CZ  . PHE B 1012 ? 0.2036 0.2110 0.2246 0.0112  -0.0029 -0.0200 1010 PHE B CZ  
16528 N N   . GLY B 1013 ? 0.1768 0.1838 0.1967 0.0132  -0.0017 -0.0199 1011 GLY B N   
16529 C CA  . GLY B 1013 ? 0.1599 0.1655 0.1811 0.0129  -0.0018 -0.0194 1011 GLY B CA  
16530 C C   . GLY B 1013 ? 0.1797 0.1834 0.2007 0.0131  -0.0026 -0.0199 1011 GLY B C   
16531 O O   . GLY B 1013 ? 0.1912 0.1945 0.2107 0.0139  -0.0029 -0.0205 1011 GLY B O   
16532 N N   . GLY B 1014 ? 0.1899 0.1925 0.2123 0.0123  -0.0031 -0.0196 1012 GLY B N   
16533 C CA  . GLY B 1014 ? 0.2184 0.2189 0.2405 0.0122  -0.0041 -0.0201 1012 GLY B CA  
16534 C C   . GLY B 1014 ? 0.1937 0.1923 0.2164 0.0118  -0.0042 -0.0196 1012 GLY B C   
16535 O O   . GLY B 1014 ? 0.2304 0.2293 0.2536 0.0119  -0.0034 -0.0188 1012 GLY B O   
16536 N N   . ARG B 1015 ? 0.1996 0.1961 0.2223 0.0113  -0.0053 -0.0200 1013 ARG B N   
16537 C CA  . ARG B 1015 ? 0.2188 0.2127 0.2417 0.0108  -0.0057 -0.0196 1013 ARG B CA  
16538 C C   . ARG B 1015 ? 0.2047 0.1983 0.2297 0.0092  -0.0066 -0.0193 1013 ARG B C   
16539 O O   . ARG B 1015 ? 0.1937 0.1890 0.2199 0.0087  -0.0071 -0.0195 1013 ARG B O   
16540 C CB  . ARG B 1015 ? 0.2022 0.1932 0.2225 0.0118  -0.0063 -0.0206 1013 ARG B CB  
16541 C CG  . ARG B 1015 ? 0.2306 0.2208 0.2495 0.0118  -0.0074 -0.0218 1013 ARG B CG  
16542 C CD  . ARG B 1015 ? 0.2793 0.2655 0.2961 0.0120  -0.0085 -0.0226 1013 ARG B CD  
16543 N NE  . ARG B 1015 ? 0.3024 0.2867 0.3206 0.0103  -0.0096 -0.0222 1013 ARG B NE  
16544 C CZ  . ARG B 1015 ? 0.2970 0.2817 0.3163 0.0089  -0.0107 -0.0224 1013 ARG B CZ  
16545 N NH1 . ARG B 1015 ? 0.2721 0.2585 0.2909 0.0091  -0.0110 -0.0230 1013 ARG B NH1 
16546 N NH2 . ARG B 1015 ? 0.3453 0.3287 0.3663 0.0072  -0.0117 -0.0218 1013 ARG B NH2 
16547 N N   . GLY B 1016 ? 0.2189 0.2102 0.2443 0.0083  -0.0071 -0.0189 1014 GLY B N   
16548 C CA  . GLY B 1016 ? 0.2113 0.2026 0.2391 0.0066  -0.0081 -0.0185 1014 GLY B CA  
16549 C C   . GLY B 1016 ? 0.2019 0.1967 0.2329 0.0060  -0.0072 -0.0175 1014 GLY B C   
16550 O O   . GLY B 1016 ? 0.2269 0.2229 0.2584 0.0063  -0.0057 -0.0166 1014 GLY B O   
16551 N N   . LEU B 1017 ? 0.1903 0.1868 0.2234 0.0051  -0.0080 -0.0175 1015 LEU B N   
16552 C CA  . LEU B 1017 ? 0.2145 0.2144 0.2507 0.0048  -0.0072 -0.0166 1015 LEU B CA  
16553 C C   . LEU B 1017 ? 0.2064 0.2081 0.2416 0.0062  -0.0060 -0.0168 1015 LEU B C   
16554 O O   . LEU B 1017 ? 0.2038 0.2080 0.2412 0.0062  -0.0050 -0.0162 1015 LEU B O   
16555 C CB  . LEU B 1017 ? 0.2023 0.2035 0.2408 0.0038  -0.0086 -0.0166 1015 LEU B CB  
16556 C CG  . LEU B 1017 ? 0.2381 0.2380 0.2782 0.0020  -0.0100 -0.0163 1015 LEU B CG  
16557 C CD1 . LEU B 1017 ? 0.2551 0.2566 0.2975 0.0011  -0.0117 -0.0164 1015 LEU B CD1 
16558 C CD2 . LEU B 1017 ? 0.2592 0.2599 0.3017 0.0011  -0.0088 -0.0150 1015 LEU B CD2 
16559 N N   . SER B 1018 ? 0.1695 0.1701 0.2017 0.0073  -0.0059 -0.0177 1016 SER B N   
16560 C CA  . SER B 1018 ? 0.1641 0.1662 0.1952 0.0083  -0.0050 -0.0179 1016 SER B CA  
16561 C C   . SER B 1018 ? 0.1616 0.1640 0.1917 0.0090  -0.0035 -0.0175 1016 SER B C   
16562 O O   . SER B 1018 ? 0.1908 0.1946 0.2204 0.0097  -0.0027 -0.0175 1016 SER B O   
16563 C CB  . SER B 1018 ? 0.1812 0.1825 0.2097 0.0090  -0.0058 -0.0190 1016 SER B CB  
16564 O OG  . SER B 1018 ? 0.1903 0.1915 0.2194 0.0084  -0.0072 -0.0193 1016 SER B OG  
16565 N N   . GLY B 1019 ? 0.1648 0.1657 0.1945 0.0089  -0.0032 -0.0171 1017 GLY B N   
16566 C CA  . GLY B 1019 ? 0.1806 0.1819 0.2092 0.0096  -0.0020 -0.0166 1017 GLY B CA  
16567 C C   . GLY B 1019 ? 0.1800 0.1792 0.2078 0.0096  -0.0019 -0.0161 1017 GLY B C   
16568 O O   . GLY B 1019 ? 0.2122 0.2091 0.2394 0.0094  -0.0029 -0.0164 1017 GLY B O   
16569 N N   . THR B 1020 ? 0.2028 0.2025 0.2301 0.0099  -0.0007 -0.0153 1018 THR B N   
16570 C CA  . THR B 1020 ? 0.1926 0.1903 0.2185 0.0102  -0.0006 -0.0147 1018 THR B CA  
16571 C C   . THR B 1020 ? 0.2088 0.2062 0.2323 0.0117  -0.0007 -0.0153 1018 THR B C   
16572 O O   . THR B 1020 ? 0.2147 0.2101 0.2368 0.0123  -0.0010 -0.0151 1018 THR B O   
16573 C CB  . THR B 1020 ? 0.1861 0.1844 0.2123 0.0098  0.0008  -0.0135 1018 THR B CB  
16574 O OG1 . THR B 1020 ? 0.1865 0.1871 0.2122 0.0104  0.0016  -0.0137 1018 THR B OG1 
16575 C CG2 . THR B 1020 ? 0.2010 0.2001 0.2300 0.0084  0.0012  -0.0127 1018 THR B CG2 
16576 N N   . GLY B 1021 ? 0.1878 0.1873 0.2109 0.0122  -0.0005 -0.0159 1019 GLY B N   
16577 C CA  . GLY B 1021 ? 0.2011 0.2013 0.2224 0.0134  -0.0003 -0.0161 1019 GLY B CA  
16578 C C   . GLY B 1021 ? 0.1919 0.1925 0.2126 0.0135  0.0005  -0.0151 1019 GLY B C   
16579 O O   . GLY B 1021 ? 0.1977 0.1978 0.2191 0.0127  0.0011  -0.0143 1019 GLY B O   
16580 N N   . PRO B 1022 ? 0.1742 0.1756 0.1933 0.0145  0.0005  -0.0152 1020 PRO B N   
16581 C CA  . PRO B 1022 ? 0.1881 0.1908 0.2066 0.0155  0.0000  -0.0160 1020 PRO B CA  
16582 C C   . PRO B 1022 ? 0.2107 0.2155 0.2297 0.0149  0.0001  -0.0167 1020 PRO B C   
16583 O O   . PRO B 1022 ? 0.2044 0.2097 0.2241 0.0140  0.0007  -0.0165 1020 PRO B O   
16584 C CB  . PRO B 1022 ? 0.2183 0.2218 0.2355 0.0164  0.0000  -0.0155 1020 PRO B CB  
16585 C CG  . PRO B 1022 ? 0.2031 0.2068 0.2201 0.0156  0.0008  -0.0147 1020 PRO B CG  
16586 C CD  . PRO B 1022 ? 0.1876 0.1894 0.2057 0.0147  0.0011  -0.0143 1020 PRO B CD  
16587 N N   . LYS B 1023 ? 0.1763 0.1822 0.1950 0.0154  -0.0003 -0.0175 1021 LYS B N   
16588 C CA  . LYS B 1023 ? 0.1877 0.1951 0.2066 0.0148  -0.0002 -0.0180 1021 LYS B CA  
16589 C C   . LYS B 1023 ? 0.1695 0.1786 0.1879 0.0144  0.0002  -0.0177 1021 LYS B C   
16590 O O   . LYS B 1023 ? 0.1831 0.1934 0.2007 0.0150  0.0002  -0.0175 1021 LYS B O   
16591 C CB  . LYS B 1023 ? 0.1826 0.1910 0.2009 0.0155  -0.0006 -0.0188 1021 LYS B CB  
16592 C CG  . LYS B 1023 ? 0.1782 0.1848 0.1965 0.0157  -0.0012 -0.0194 1021 LYS B CG  
16593 C CD  . LYS B 1023 ? 0.1704 0.1782 0.1878 0.0166  -0.0013 -0.0201 1021 LYS B CD  
16594 C CE  . LYS B 1023 ? 0.1898 0.1959 0.2066 0.0168  -0.0018 -0.0209 1021 LYS B CE  
16595 N NZ  . LYS B 1023 ? 0.1889 0.1952 0.2059 0.0156  -0.0021 -0.0211 1021 LYS B NZ  
16596 N N   . ALA B 1024 ? 0.1790 0.1884 0.1978 0.0136  0.0005  -0.0178 1022 ALA B N   
16597 C CA  . ALA B 1024 ? 0.1876 0.1982 0.2055 0.0131  0.0008  -0.0178 1022 ALA B CA  
16598 C C   . ALA B 1024 ? 0.1852 0.1975 0.2026 0.0132  0.0004  -0.0182 1022 ALA B C   
16599 O O   . ALA B 1024 ? 0.2025 0.2149 0.2201 0.0134  0.0001  -0.0187 1022 ALA B O   
16600 C CB  . ALA B 1024 ? 0.1915 0.2015 0.2099 0.0123  0.0012  -0.0179 1022 ALA B CB  
16601 N N   . GLY B 1025 ? 0.1664 0.1801 0.1828 0.0129  0.0004  -0.0181 1023 GLY B N   
16602 C CA  . GLY B 1025 ? 0.1881 0.2039 0.2043 0.0128  0.0001  -0.0184 1023 GLY B CA  
16603 C C   . GLY B 1025 ? 0.1714 0.1884 0.1880 0.0139  -0.0001 -0.0184 1023 GLY B C   
16604 O O   . GLY B 1025 ? 0.1864 0.2053 0.2031 0.0140  -0.0002 -0.0187 1023 GLY B O   
16605 N N   . GLY B 1026 ? 0.1809 0.1969 0.1976 0.0149  -0.0002 -0.0181 1024 GLY B N   
16606 C CA  . GLY B 1026 ? 0.1715 0.1881 0.1884 0.0163  -0.0004 -0.0181 1024 GLY B CA  
16607 C C   . GLY B 1026 ? 0.1737 0.1905 0.1903 0.0170  -0.0006 -0.0173 1024 GLY B C   
16608 O O   . GLY B 1026 ? 0.1761 0.1923 0.1921 0.0163  -0.0004 -0.0168 1024 GLY B O   
16609 N N   . PRO B 1027 ? 0.1824 0.2001 0.1992 0.0185  -0.0008 -0.0172 1025 PRO B N   
16610 C CA  . PRO B 1027 ? 0.1641 0.1827 0.1806 0.0193  -0.0012 -0.0165 1025 PRO B CA  
16611 C C   . PRO B 1027 ? 0.1717 0.1872 0.1875 0.0198  -0.0012 -0.0158 1025 PRO B C   
16612 O O   . PRO B 1027 ? 0.1768 0.1927 0.1920 0.0203  -0.0016 -0.0150 1025 PRO B O   
16613 C CB  . PRO B 1027 ? 0.1865 0.2073 0.2038 0.0209  -0.0014 -0.0167 1025 PRO B CB  
16614 C CG  . PRO B 1027 ? 0.2072 0.2263 0.2246 0.0214  -0.0011 -0.0175 1025 PRO B CG  
16615 C CD  . PRO B 1027 ? 0.1975 0.2158 0.2148 0.0195  -0.0008 -0.0179 1025 PRO B CD  
16616 N N   . LEU B 1028 ? 0.1761 0.1887 0.1919 0.0195  -0.0009 -0.0160 1026 LEU B N   
16617 C CA  . LEU B 1028 ? 0.1746 0.1842 0.1898 0.0197  -0.0009 -0.0152 1026 LEU B CA  
16618 C C   . LEU B 1028 ? 0.1892 0.1981 0.2040 0.0182  -0.0004 -0.0148 1026 LEU B C   
16619 O O   . LEU B 1028 ? 0.2066 0.2135 0.2208 0.0182  -0.0002 -0.0139 1026 LEU B O   
16620 C CB  . LEU B 1028 ? 0.1777 0.1844 0.1932 0.0200  -0.0010 -0.0156 1026 LEU B CB  
16621 C CG  . LEU B 1028 ? 0.2140 0.2208 0.2295 0.0216  -0.0013 -0.0163 1026 LEU B CG  
16622 C CD1 . LEU B 1028 ? 0.2386 0.2418 0.2540 0.0217  -0.0015 -0.0166 1026 LEU B CD1 
16623 C CD2 . LEU B 1028 ? 0.2595 0.2671 0.2746 0.0232  -0.0017 -0.0156 1026 LEU B CD2 
16624 N N   . TYR B 1029 ? 0.1749 0.1853 0.1899 0.0171  -0.0001 -0.0152 1027 TYR B N   
16625 C CA  . TYR B 1029 ? 0.1760 0.1855 0.1909 0.0159  0.0006  -0.0150 1027 TYR B CA  
16626 C C   . TYR B 1029 ? 0.1738 0.1830 0.1871 0.0158  0.0008  -0.0142 1027 TYR B C   
16627 O O   . TYR B 1029 ? 0.1680 0.1755 0.1810 0.0154  0.0014  -0.0136 1027 TYR B O   
16628 C CB  . TYR B 1029 ? 0.1792 0.1902 0.1943 0.0150  0.0007  -0.0158 1027 TYR B CB  
16629 C CG  . TYR B 1029 ? 0.1777 0.1877 0.1932 0.0140  0.0015  -0.0159 1027 TYR B CG  
16630 C CD1 . TYR B 1029 ? 0.1682 0.1769 0.1851 0.0138  0.0017  -0.0160 1027 TYR B CD1 
16631 C CD2 . TYR B 1029 ? 0.1704 0.1809 0.1848 0.0133  0.0018  -0.0159 1027 TYR B CD2 
16632 C CE1 . TYR B 1029 ? 0.1800 0.1884 0.1975 0.0131  0.0023  -0.0161 1027 TYR B CE1 
16633 C CE2 . TYR B 1029 ? 0.1848 0.1944 0.1995 0.0127  0.0026  -0.0161 1027 TYR B CE2 
16634 C CZ  . TYR B 1029 ? 0.1773 0.1861 0.1937 0.0126  0.0028  -0.0161 1027 TYR B CZ  
16635 O OH  . TYR B 1029 ? 0.1936 0.2020 0.2107 0.0122  0.0035  -0.0163 1027 TYR B OH  
16636 N N   . LEU B 1030 ? 0.1770 0.1881 0.1893 0.0160  0.0003  -0.0141 1028 LEU B N   
16637 C CA  . LEU B 1030 ? 0.1610 0.1718 0.1714 0.0157  0.0004  -0.0134 1028 LEU B CA  
16638 C C   . LEU B 1030 ? 0.1796 0.1886 0.1894 0.0165  0.0004  -0.0123 1028 LEU B C   
16639 O O   . LEU B 1030 ? 0.1748 0.1825 0.1829 0.0160  0.0009  -0.0116 1028 LEU B O   
16640 C CB  . LEU B 1030 ? 0.1755 0.1888 0.1851 0.0157  -0.0004 -0.0134 1028 LEU B CB  
16641 C CG  . LEU B 1030 ? 0.1857 0.2005 0.1954 0.0146  -0.0004 -0.0143 1028 LEU B CG  
16642 C CD1 . LEU B 1030 ? 0.2149 0.2322 0.2238 0.0143  -0.0014 -0.0142 1028 LEU B CD1 
16643 C CD2 . LEU B 1030 ? 0.2266 0.2396 0.2352 0.0135  0.0005  -0.0145 1028 LEU B CD2 
16644 N N   . GLY B 1031 ? 0.1781 0.1865 0.1887 0.0176  -0.0001 -0.0122 1029 GLY B N   
16645 C CA  . GLY B 1031 ? 0.2058 0.2121 0.2156 0.0184  -0.0003 -0.0111 1029 GLY B CA  
16646 C C   . GLY B 1031 ? 0.1702 0.1738 0.1799 0.0176  0.0006  -0.0106 1029 GLY B C   
16647 O O   . GLY B 1031 ? 0.2069 0.2084 0.2153 0.0178  0.0006  -0.0094 1029 GLY B O   
16648 N N   . ARG B 1032 ? 0.1688 0.1723 0.1798 0.0166  0.0013  -0.0113 1030 ARG B N   
16649 C CA  . ARG B 1032 ? 0.1777 0.1794 0.1892 0.0156  0.0022  -0.0107 1030 ARG B CA  
16650 C C   . ARG B 1032 ? 0.1957 0.1975 0.2057 0.0149  0.0032  -0.0101 1030 ARG B C   
16651 O O   . ARG B 1032 ? 0.2062 0.2067 0.2163 0.0141  0.0041  -0.0093 1030 ARG B O   
16652 C CB  . ARG B 1032 ? 0.1745 0.1766 0.1882 0.0150  0.0024  -0.0117 1030 ARG B CB  
16653 C CG  . ARG B 1032 ? 0.2073 0.2077 0.2222 0.0140  0.0031  -0.0111 1030 ARG B CG  
16654 C CD  . ARG B 1032 ? 0.2108 0.2087 0.2257 0.0143  0.0025  -0.0105 1030 ARG B CD  
16655 N NE  . ARG B 1032 ? 0.2199 0.2165 0.2364 0.0131  0.0030  -0.0101 1030 ARG B NE  
16656 C CZ  . ARG B 1032 ? 0.2614 0.2559 0.2775 0.0125  0.0033  -0.0089 1030 ARG B CZ  
16657 N NH1 . ARG B 1032 ? 0.2702 0.2632 0.2842 0.0131  0.0033  -0.0079 1030 ARG B NH1 
16658 N NH2 . ARG B 1032 ? 0.2605 0.2543 0.2786 0.0112  0.0037  -0.0086 1030 ARG B NH2 
16659 N N   . LEU B 1033 ? 0.1763 0.1798 0.1849 0.0149  0.0030  -0.0104 1031 LEU B N   
16660 C CA  . LEU B 1033 ? 0.1819 0.1855 0.1888 0.0142  0.0040  -0.0102 1031 LEU B CA  
16661 C C   . LEU B 1033 ? 0.1962 0.1993 0.2003 0.0145  0.0037  -0.0093 1031 LEU B C   
16662 O O   . LEU B 1033 ? 0.2035 0.2068 0.2054 0.0141  0.0042  -0.0093 1031 LEU B O   
16663 C CB  . LEU B 1033 ? 0.1812 0.1865 0.1882 0.0138  0.0040  -0.0114 1031 LEU B CB  
16664 C CG  . LEU B 1033 ? 0.1913 0.1971 0.2009 0.0136  0.0040  -0.0124 1031 LEU B CG  
16665 C CD1 . LEU B 1033 ? 0.2016 0.2088 0.2110 0.0132  0.0039  -0.0134 1031 LEU B CD1 
16666 C CD2 . LEU B 1033 ? 0.2137 0.2186 0.2250 0.0131  0.0051  -0.0121 1031 LEU B CD2 
16667 N N   . VAL B 1034 ? 0.2027 0.2050 0.2064 0.0154  0.0028  -0.0085 1032 VAL B N   
16668 C CA  . VAL B 1034 ? 0.2267 0.2282 0.2277 0.0159  0.0023  -0.0073 1032 VAL B CA  
16669 C C   . VAL B 1034 ? 0.2075 0.2065 0.2087 0.0163  0.0024  -0.0061 1032 VAL B C   
16670 O O   . VAL B 1034 ? 0.2423 0.2404 0.2456 0.0163  0.0024  -0.0063 1032 VAL B O   
16671 C CB  . VAL B 1034 ? 0.2076 0.2111 0.2082 0.0168  0.0007  -0.0075 1032 VAL B CB  
16672 C CG1 . VAL B 1034 ? 0.2337 0.2394 0.2336 0.0161  0.0006  -0.0085 1032 VAL B CG1 
16673 C CG2 . VAL B 1034 ? 0.2094 0.2136 0.2126 0.0179  -0.0001 -0.0081 1032 VAL B CG2 
16674 N N   . THR B 1035 ? 0.2415 0.2390 0.2400 0.0165  0.0023  -0.0047 1033 THR B N   
16675 C CA  . THR B 1035 ? 0.2723 0.2668 0.2705 0.0166  0.0025  -0.0034 1033 THR B CA  
16676 C C   . THR B 1035 ? 0.2949 0.2885 0.2937 0.0181  0.0009  -0.0031 1033 THR B C   
16677 O O   . THR B 1035 ? 0.3552 0.3460 0.3543 0.0183  0.0009  -0.0024 1033 THR B O   
16678 C CB  . THR B 1035 ? 0.3483 0.3411 0.3432 0.0161  0.0032  -0.0018 1033 THR B CB  
16679 O OG1 . THR B 1035 ? 0.3839 0.3780 0.3763 0.0167  0.0022  -0.0016 1033 THR B OG1 
16680 C CG2 . THR B 1035 ? 0.4031 0.3962 0.3981 0.0146  0.0051  -0.0019 1033 THR B CG2 
16681 N N   . THR B 1036 ? 0.2594 0.2552 0.2582 0.0193  -0.0003 -0.0037 1034 THR B N   
16682 C CA  . THR B 1036 ? 0.2982 0.2938 0.2980 0.0211  -0.0016 -0.0037 1034 THR B CA  
16683 C C   . THR B 1036 ? 0.2577 0.2566 0.2597 0.0214  -0.0020 -0.0053 1034 THR B C   
16684 O O   . THR B 1036 ? 0.2560 0.2577 0.2576 0.0211  -0.0023 -0.0058 1034 THR B O   
16685 C CB  . THR B 1036 ? 0.3270 0.3225 0.3245 0.0223  -0.0028 -0.0024 1034 THR B CB  
16686 O OG1 . THR B 1036 ? 0.4169 0.4092 0.4118 0.0218  -0.0024 -0.0008 1034 THR B OG1 
16687 C CG2 . THR B 1036 ? 0.3668 0.3623 0.3655 0.0245  -0.0041 -0.0025 1034 THR B CG2 
16688 N N   . ALA B 1037 ? 0.2687 0.2670 0.2727 0.0220  -0.0021 -0.0062 1035 ALA B N   
16689 C CA  . ALA B 1037 ? 0.2648 0.2662 0.2709 0.0222  -0.0022 -0.0076 1035 ALA B CA  
16690 C C   . ALA B 1037 ? 0.2250 0.2289 0.2314 0.0239  -0.0034 -0.0076 1035 ALA B C   
16691 O O   . ALA B 1037 ? 0.2445 0.2470 0.2503 0.0255  -0.0042 -0.0069 1035 ALA B O   
16692 C CB  . ALA B 1037 ? 0.2789 0.2787 0.2867 0.0223  -0.0020 -0.0085 1035 ALA B CB  
16693 N N   . PRO B 1038 ? 0.2066 0.2143 0.2138 0.0235  -0.0036 -0.0084 1036 PRO B N   
16694 C CA  . PRO B 1038 ? 0.2161 0.2269 0.2242 0.0250  -0.0047 -0.0085 1036 PRO B CA  
16695 C C   . PRO B 1038 ? 0.2072 0.2184 0.2174 0.0263  -0.0046 -0.0095 1036 PRO B C   
16696 O O   . PRO B 1038 ? 0.2162 0.2253 0.2268 0.0257  -0.0038 -0.0102 1036 PRO B O   
16697 C CB  . PRO B 1038 ? 0.2423 0.2568 0.2508 0.0236  -0.0048 -0.0091 1036 PRO B CB  
16698 C CG  . PRO B 1038 ? 0.2408 0.2540 0.2495 0.0219  -0.0036 -0.0100 1036 PRO B CG  
16699 C CD  . PRO B 1038 ? 0.2147 0.2238 0.2221 0.0216  -0.0029 -0.0092 1036 PRO B CD  
16700 N N   . VAL B 1039 ? 0.2192 0.2332 0.2305 0.0281  -0.0054 -0.0094 1037 VAL B N   
16701 C CA  . VAL B 1039 ? 0.2118 0.2269 0.2248 0.0294  -0.0052 -0.0105 1037 VAL B CA  
16702 C C   . VAL B 1039 ? 0.1894 0.2084 0.2039 0.0280  -0.0048 -0.0115 1037 VAL B C   
16703 O O   . VAL B 1039 ? 0.2133 0.2362 0.2284 0.0277  -0.0053 -0.0112 1037 VAL B O   
16704 C CB  . VAL B 1039 ? 0.2032 0.2199 0.2170 0.0321  -0.0060 -0.0099 1037 VAL B CB  
16705 C CG1 . VAL B 1039 ? 0.2556 0.2735 0.2710 0.0336  -0.0055 -0.0111 1037 VAL B CG1 
16706 C CG2 . VAL B 1039 ? 0.2503 0.2627 0.2624 0.0334  -0.0065 -0.0088 1037 VAL B CG2 
16707 N N   . PRO B 1040 ? 0.1998 0.2177 0.2147 0.0271  -0.0039 -0.0125 1038 PRO B N   
16708 C CA  . PRO B 1040 ? 0.2090 0.2301 0.2250 0.0257  -0.0036 -0.0133 1038 PRO B CA  
16709 C C   . PRO B 1040 ? 0.2037 0.2290 0.2214 0.0269  -0.0038 -0.0137 1038 PRO B C   
16710 O O   . PRO B 1040 ? 0.2123 0.2376 0.2306 0.0292  -0.0039 -0.0137 1038 PRO B O   
16711 C CB  . PRO B 1040 ? 0.2457 0.2641 0.2616 0.0248  -0.0028 -0.0143 1038 PRO B CB  
16712 C CG  . PRO B 1040 ? 0.2690 0.2830 0.2838 0.0250  -0.0027 -0.0138 1038 PRO B CG  
16713 C CD  . PRO B 1040 ? 0.2316 0.2452 0.2459 0.0270  -0.0034 -0.0129 1038 PRO B CD  
16714 N N   . PRO B 1041 ? 0.2141 0.2431 0.2327 0.0255  -0.0037 -0.0140 1039 PRO B N   
16715 C CA  . PRO B 1041 ? 0.2058 0.2393 0.2264 0.0265  -0.0037 -0.0143 1039 PRO B CA  
16716 C C   . PRO B 1041 ? 0.2013 0.2335 0.2222 0.0278  -0.0028 -0.0152 1039 PRO B C   
16717 O O   . PRO B 1041 ? 0.2159 0.2449 0.2359 0.0270  -0.0023 -0.0159 1039 PRO B O   
16718 C CB  . PRO B 1041 ? 0.2374 0.2735 0.2583 0.0240  -0.0036 -0.0146 1039 PRO B CB  
16719 C CG  . PRO B 1041 ? 0.2612 0.2949 0.2804 0.0223  -0.0039 -0.0142 1039 PRO B CG  
16720 C CD  . PRO B 1041 ? 0.2666 0.2955 0.2845 0.0230  -0.0036 -0.0141 1039 PRO B CD  
16721 N N   . GLN B 1042 ? 0.2013 0.2360 0.2235 0.0301  -0.0028 -0.0152 1040 GLN B N   
16722 C CA  . GLN B 1042 ? 0.2091 0.2432 0.2316 0.0317  -0.0020 -0.0162 1040 GLN B CA  
16723 C C   . GLN B 1042 ? 0.2174 0.2457 0.2381 0.0327  -0.0019 -0.0166 1040 GLN B C   
16724 O O   . GLN B 1042 ? 0.2160 0.2426 0.2362 0.0336  -0.0013 -0.0176 1040 GLN B O   
16725 C CB  . GLN B 1042 ? 0.2461 0.2819 0.2689 0.0301  -0.0011 -0.0171 1040 GLN B CB  
16726 C CG  . GLN B 1042 ? 0.2888 0.3303 0.3134 0.0290  -0.0011 -0.0167 1040 GLN B CG  
16727 C CD  . GLN B 1042 ? 0.3699 0.4124 0.3944 0.0273  -0.0003 -0.0174 1040 GLN B CD  
16728 O OE1 . GLN B 1042 ? 0.5629 0.6029 0.5862 0.0252  -0.0004 -0.0176 1040 GLN B OE1 
16729 N NE2 . GLN B 1042 ? 0.4824 0.5285 0.5081 0.0282  0.0005  -0.0177 1040 GLN B NE2 
16730 N N   . HIS B 1043 ? 0.2086 0.2335 0.2281 0.0324  -0.0025 -0.0158 1041 HIS B N   
16731 C CA  . HIS B 1043 ? 0.1955 0.2147 0.2134 0.0327  -0.0025 -0.0161 1041 HIS B CA  
16732 C C   . HIS B 1043 ? 0.2079 0.2252 0.2253 0.0355  -0.0029 -0.0159 1041 HIS B C   
16733 O O   . HIS B 1043 ? 0.2349 0.2509 0.2518 0.0362  -0.0036 -0.0148 1041 HIS B O   
16734 C CB  . HIS B 1043 ? 0.1987 0.2154 0.2156 0.0307  -0.0028 -0.0153 1041 HIS B CB  
16735 C CG  . HIS B 1043 ? 0.2102 0.2214 0.2256 0.0305  -0.0028 -0.0154 1041 HIS B CG  
16736 N ND1 . HIS B 1043 ? 0.2116 0.2207 0.2267 0.0290  -0.0024 -0.0162 1041 HIS B ND1 
16737 C CD2 . HIS B 1043 ? 0.2272 0.2347 0.2414 0.0314  -0.0032 -0.0146 1041 HIS B CD2 
16738 C CE1 . HIS B 1043 ? 0.2223 0.2268 0.2363 0.0289  -0.0026 -0.0160 1041 HIS B CE1 
16739 N NE2 . HIS B 1043 ? 0.2171 0.2204 0.2305 0.0303  -0.0031 -0.0150 1041 HIS B NE2 
16740 N N   . SER B 1044 ? 0.1856 0.2023 0.2029 0.0373  -0.0024 -0.0169 1042 SER B N   
16741 C CA  . SER B 1044 ? 0.2061 0.2203 0.2227 0.0402  -0.0026 -0.0169 1042 SER B CA  
16742 C C   . SER B 1044 ? 0.2032 0.2156 0.2190 0.0413  -0.0018 -0.0185 1042 SER B C   
16743 O O   . SER B 1044 ? 0.2055 0.2198 0.2216 0.0400  -0.0012 -0.0194 1042 SER B O   
16744 C CB  . SER B 1044 ? 0.2037 0.2224 0.2220 0.0425  -0.0029 -0.0162 1042 SER B CB  
16745 O OG  . SER B 1044 ? 0.2146 0.2385 0.2348 0.0430  -0.0021 -0.0169 1042 SER B OG  
16746 N N   . SER B 1045 ? 0.1831 0.1918 0.1977 0.0439  -0.0020 -0.0188 1043 SER B N   
16747 C CA  . SER B 1045 ? 0.1703 0.1772 0.1837 0.0453  -0.0013 -0.0204 1043 SER B CA  
16748 C C   . SER B 1045 ? 0.1998 0.2051 0.2127 0.0491  -0.0014 -0.0205 1043 SER B C   
16749 O O   . SER B 1045 ? 0.2233 0.2256 0.2355 0.0500  -0.0023 -0.0195 1043 SER B O   
16750 C CB  . SER B 1045 ? 0.2169 0.2176 0.2280 0.0436  -0.0016 -0.0211 1043 SER B CB  
16751 O OG  . SER B 1045 ? 0.2206 0.2187 0.2300 0.0451  -0.0011 -0.0227 1043 SER B OG  
16752 N N   . VAL B 1046 ? 0.2070 0.2141 0.2199 0.0513  -0.0004 -0.0217 1044 VAL B N   
16753 C CA  . VAL B 1046 ? 0.2250 0.2302 0.2372 0.0552  -0.0003 -0.0220 1044 VAL B CA  
16754 C C   . VAL B 1046 ? 0.2189 0.2161 0.2277 0.0560  -0.0006 -0.0232 1044 VAL B C   
16755 O O   . VAL B 1046 ? 0.2429 0.2371 0.2505 0.0592  -0.0007 -0.0235 1044 VAL B O   
16756 C CB  . VAL B 1046 ? 0.2487 0.2596 0.2626 0.0577  0.0010  -0.0228 1044 VAL B CB  
16757 C CG1 . VAL B 1046 ? 0.2820 0.3008 0.2995 0.0570  0.0010  -0.0215 1044 VAL B CG1 
16758 C CG2 . VAL B 1046 ? 0.2448 0.2554 0.2572 0.0568  0.0021  -0.0245 1044 VAL B CG2 
16759 N N   . HIS B 1047 ? 0.2364 0.2302 0.2436 0.0531  -0.0008 -0.0238 1045 HIS B N   
16760 C CA  A HIS B 1047 ? 0.2444 0.2307 0.2483 0.0534  -0.0012 -0.0250 1045 HIS B CA  
16761 C CA  B HIS B 1047 ? 0.2443 0.2305 0.2481 0.0532  -0.0012 -0.0250 1045 HIS B CA  
16762 C C   . HIS B 1047 ? 0.2242 0.2049 0.2269 0.0525  -0.0025 -0.0238 1045 HIS B C   
16763 O O   . HIS B 1047 ? 0.2587 0.2408 0.2627 0.0501  -0.0030 -0.0224 1045 HIS B O   
16764 C CB  A HIS B 1047 ? 0.2523 0.2380 0.2551 0.0508  -0.0009 -0.0262 1045 HIS B CB  
16765 C CB  B HIS B 1047 ? 0.2493 0.2349 0.2522 0.0501  -0.0011 -0.0260 1045 HIS B CB  
16766 C CG  A HIS B 1047 ? 0.2490 0.2404 0.2529 0.0513  0.0004  -0.0271 1045 HIS B CG  
16767 C CG  B HIS B 1047 ? 0.2533 0.2315 0.2534 0.0489  -0.0020 -0.0268 1045 HIS B CG  
16768 N ND1 A HIS B 1047 ? 0.2955 0.2870 0.2981 0.0544  0.0014  -0.0285 1045 HIS B ND1 
16769 N ND1 B HIS B 1047 ? 0.2955 0.2687 0.2925 0.0508  -0.0019 -0.0284 1045 HIS B ND1 
16770 C CD2 A HIS B 1047 ? 0.2450 0.2423 0.2510 0.0493  0.0009  -0.0267 1045 HIS B CD2 
16771 C CD2 B HIS B 1047 ? 0.2607 0.2356 0.2604 0.0459  -0.0029 -0.0261 1045 HIS B CD2 
16772 C CE1 A HIS B 1047 ? 0.3252 0.3226 0.3292 0.0541  0.0026  -0.0288 1045 HIS B CE1 
16773 C CE1 B HIS B 1047 ? 0.2953 0.2623 0.2901 0.0489  -0.0030 -0.0287 1045 HIS B CE1 
16774 N NE2 A HIS B 1047 ? 0.2799 0.2807 0.2859 0.0510  0.0023  -0.0277 1045 HIS B NE2 
16775 N NE2 B HIS B 1047 ? 0.3151 0.2833 0.3118 0.0458  -0.0036 -0.0273 1045 HIS B NE2 
16776 N N   . THR B 1048 ? 0.2179 0.1920 0.2178 0.0543  -0.0030 -0.0245 1046 THR B N   
16777 C CA  . THR B 1048 ? 0.2468 0.2148 0.2452 0.0534  -0.0042 -0.0235 1046 THR B CA  
16778 C C   . THR B 1048 ? 0.2387 0.2000 0.2341 0.0519  -0.0047 -0.0248 1046 THR B C   
16779 O O   . THR B 1048 ? 0.2509 0.2094 0.2442 0.0538  -0.0044 -0.0266 1046 THR B O   
16780 C CB  . THR B 1048 ? 0.2966 0.2619 0.2942 0.0570  -0.0046 -0.0228 1046 THR B CB  
16781 O OG1 . THR B 1048 ? 0.2729 0.2450 0.2733 0.0589  -0.0041 -0.0218 1046 THR B OG1 
16782 C CG2 . THR B 1048 ? 0.2806 0.2402 0.2768 0.0556  -0.0058 -0.0213 1046 THR B CG2 
16783 N N   . ASP B 1049 ? 0.2472 0.2062 0.2427 0.0485  -0.0054 -0.0240 1047 ASP B N   
16784 C CA  . ASP B 1049 ? 0.2392 0.1922 0.2322 0.0466  -0.0061 -0.0251 1047 ASP B CA  
16785 C C   . ASP B 1049 ? 0.2290 0.1744 0.2187 0.0490  -0.0068 -0.0257 1047 ASP B C   
16786 O O   . ASP B 1049 ? 0.2612 0.2042 0.2506 0.0502  -0.0073 -0.0244 1047 ASP B O   
16787 C CB  . ASP B 1049 ? 0.2234 0.1755 0.2174 0.0428  -0.0068 -0.0237 1047 ASP B CB  
16788 C CG  . ASP B 1049 ? 0.2528 0.1993 0.2448 0.0405  -0.0077 -0.0247 1047 ASP B CG  
16789 O OD1 . ASP B 1049 ? 0.2761 0.2159 0.2657 0.0408  -0.0086 -0.0247 1047 ASP B OD1 
16790 O OD2 . ASP B 1049 ? 0.2610 0.2099 0.2538 0.0385  -0.0076 -0.0255 1047 ASP B OD2 
16791 N N   . PRO B 1050 ? 0.2698 0.2111 0.2566 0.0498  -0.0069 -0.0278 1048 PRO B N   
16792 C CA  . PRO B 1050 ? 0.2783 0.2122 0.2617 0.0524  -0.0074 -0.0286 1048 PRO B CA  
16793 C C   . PRO B 1050 ? 0.2797 0.2064 0.2613 0.0502  -0.0089 -0.0277 1048 PRO B C   
16794 O O   . PRO B 1050 ? 0.2999 0.2208 0.2794 0.0523  -0.0095 -0.0274 1048 PRO B O   
16795 C CB  . PRO B 1050 ? 0.3329 0.2648 0.3135 0.0533  -0.0071 -0.0312 1048 PRO B CB  
16796 C CG  . PRO B 1050 ? 0.3321 0.2680 0.3144 0.0497  -0.0070 -0.0314 1048 PRO B CG  
16797 C CD  . PRO B 1050 ? 0.2995 0.2430 0.2860 0.0486  -0.0064 -0.0295 1048 PRO B CD  
16798 N N   . VAL B 1051 ? 0.2898 0.2166 0.2724 0.0460  -0.0095 -0.0271 1049 VAL B N   
16799 C CA  . VAL B 1051 ? 0.2579 0.1783 0.2393 0.0436  -0.0108 -0.0260 1049 VAL B CA  
16800 C C   . VAL B 1051 ? 0.2590 0.1806 0.2420 0.0437  -0.0108 -0.0235 1049 VAL B C   
16801 O O   . VAL B 1051 ? 0.2884 0.2037 0.2694 0.0439  -0.0117 -0.0226 1049 VAL B O   
16802 C CB  . VAL B 1051 ? 0.3087 0.2295 0.2910 0.0392  -0.0114 -0.0261 1049 VAL B CB  
16803 C CG1 . VAL B 1051 ? 0.3258 0.2407 0.3073 0.0364  -0.0127 -0.0248 1049 VAL B CG1 
16804 C CG2 . VAL B 1051 ? 0.3448 0.2638 0.3249 0.0392  -0.0117 -0.0286 1049 VAL B CG2 
16805 N N   . LEU B 1052 ? 0.2396 0.1687 0.2258 0.0436  -0.0099 -0.0224 1050 LEU B N   
16806 C CA  . LEU B 1052 ? 0.2508 0.1815 0.2383 0.0444  -0.0098 -0.0202 1050 LEU B CA  
16807 C C   . LEU B 1052 ? 0.2913 0.2181 0.2766 0.0485  -0.0101 -0.0202 1050 LEU B C   
16808 O O   . LEU B 1052 ? 0.2806 0.2032 0.2647 0.0488  -0.0108 -0.0186 1050 LEU B O   
16809 C CB  . LEU B 1052 ? 0.2510 0.1907 0.2419 0.0443  -0.0088 -0.0195 1050 LEU B CB  
16810 C CG  . LEU B 1052 ? 0.2488 0.1915 0.2412 0.0449  -0.0088 -0.0173 1050 LEU B CG  
16811 C CD1 . LEU B 1052 ? 0.2513 0.1943 0.2432 0.0492  -0.0087 -0.0172 1050 LEU B CD1 
16812 C CD2 . LEU B 1052 ? 0.2547 0.1927 0.2461 0.0424  -0.0095 -0.0154 1050 LEU B CD2 
16813 N N   . LEU B 1053 ? 0.2682 0.1965 0.2530 0.0518  -0.0095 -0.0220 1051 LEU B N   
16814 C CA  . LEU B 1053 ? 0.2994 0.2244 0.2825 0.0561  -0.0096 -0.0221 1051 LEU B CA  
16815 C C   . LEU B 1053 ? 0.2974 0.2122 0.2764 0.0562  -0.0108 -0.0222 1051 LEU B C   
16816 O O   . LEU B 1053 ? 0.3154 0.2262 0.2932 0.0581  -0.0115 -0.0209 1051 LEU B O   
16817 C CB  . LEU B 1053 ? 0.3259 0.2541 0.3089 0.0595  -0.0086 -0.0241 1051 LEU B CB  
16818 C CG  . LEU B 1053 ? 0.3583 0.2964 0.3452 0.0604  -0.0074 -0.0237 1051 LEU B CG  
16819 C CD1 . LEU B 1053 ? 0.3292 0.2702 0.3159 0.0631  -0.0062 -0.0259 1051 LEU B CD1 
16820 C CD2 . LEU B 1053 ? 0.3573 0.2978 0.3458 0.0627  -0.0076 -0.0217 1051 LEU B CD2 
16821 N N   . ASP B 1054 ? 0.2934 0.2038 0.2704 0.0540  -0.0113 -0.0238 1052 ASP B N   
16822 C CA  . ASP B 1054 ? 0.3399 0.2402 0.3130 0.0536  -0.0126 -0.0240 1052 ASP B CA  
16823 C C   . ASP B 1054 ? 0.2869 0.1844 0.2603 0.0506  -0.0135 -0.0215 1052 ASP B C   
16824 O O   . ASP B 1054 ? 0.3280 0.2180 0.2986 0.0514  -0.0145 -0.0207 1052 ASP B O   
16825 C CB  . ASP B 1054 ? 0.3453 0.2421 0.3164 0.0513  -0.0130 -0.0262 1052 ASP B CB  
16826 C CG  . ASP B 1054 ? 0.4535 0.3507 0.4229 0.0545  -0.0123 -0.0288 1052 ASP B CG  
16827 O OD1 . ASP B 1054 ? 0.4229 0.3217 0.3922 0.0588  -0.0114 -0.0291 1052 ASP B OD1 
16828 O OD2 . ASP B 1054 ? 0.4669 0.3628 0.4348 0.0528  -0.0125 -0.0307 1052 ASP B OD2 
16829 N N   . PHE B 1055 ? 0.2968 0.2002 0.2735 0.0473  -0.0131 -0.0201 1053 PHE B N   
16830 C CA  . PHE B 1055 ? 0.2931 0.1948 0.2703 0.0445  -0.0137 -0.0176 1053 PHE B CA  
16831 C C   . PHE B 1055 ? 0.3162 0.2179 0.2932 0.0472  -0.0137 -0.0157 1053 PHE B C   
16832 O O   . PHE B 1055 ? 0.3177 0.2133 0.2927 0.0467  -0.0145 -0.0141 1053 PHE B O   
16833 C CB  . PHE B 1055 ? 0.3041 0.2127 0.2849 0.0408  -0.0130 -0.0168 1053 PHE B CB  
16834 C CG  . PHE B 1055 ? 0.2758 0.1830 0.2571 0.0375  -0.0133 -0.0143 1053 PHE B CG  
16835 C CD1 . PHE B 1055 ? 0.3199 0.2196 0.2990 0.0352  -0.0144 -0.0138 1053 PHE B CD1 
16836 C CD2 . PHE B 1055 ? 0.2726 0.1861 0.2566 0.0368  -0.0125 -0.0125 1053 PHE B CD2 
16837 C CE1 . PHE B 1055 ? 0.3131 0.2120 0.2929 0.0321  -0.0145 -0.0114 1053 PHE B CE1 
16838 C CE2 . PHE B 1055 ? 0.3002 0.2125 0.2844 0.0339  -0.0126 -0.0102 1053 PHE B CE2 
16839 C CZ  . PHE B 1055 ? 0.2975 0.2026 0.2797 0.0316  -0.0135 -0.0097 1053 PHE B CZ  
16840 N N   . ALA B 1056 ? 0.2888 0.1971 0.2678 0.0502  -0.0128 -0.0158 1054 ALA B N   
16841 C CA  . ALA B 1056 ? 0.3218 0.2306 0.3008 0.0530  -0.0130 -0.0139 1054 ALA B CA  
16842 C C   . ALA B 1056 ? 0.3031 0.2035 0.2784 0.0562  -0.0139 -0.0142 1054 ALA B C   
16843 O O   . ALA B 1056 ? 0.3339 0.2305 0.3079 0.0569  -0.0147 -0.0121 1054 ALA B O   
16844 C CB  . ALA B 1056 ? 0.3307 0.2483 0.3127 0.0555  -0.0121 -0.0142 1054 ALA B CB  
16845 N N   . LYS B 1057 ? 0.3304 0.2278 0.3040 0.0584  -0.0138 -0.0166 1055 LYS B N   
16846 C CA  . LYS B 1057 ? 0.3389 0.2277 0.3087 0.0617  -0.0146 -0.0171 1055 LYS B CA  
16847 C C   . LYS B 1057 ? 0.3810 0.2605 0.3475 0.0587  -0.0160 -0.0161 1055 LYS B C   
16848 O O   . LYS B 1057 ? 0.4092 0.2821 0.3731 0.0606  -0.0169 -0.0149 1055 LYS B O   
16849 C CB  . LYS B 1057 ? 0.4035 0.2907 0.3716 0.0643  -0.0141 -0.0202 1055 LYS B CB  
16850 C CG  . LYS B 1057 ? 0.4522 0.3469 0.4227 0.0685  -0.0129 -0.0210 1055 LYS B CG  
16851 C CD  . LYS B 1057 ? 0.3916 0.2840 0.3599 0.0712  -0.0123 -0.0240 1055 LYS B CD  
16852 C CE  . LYS B 1057 ? 0.4358 0.3279 0.4035 0.0674  -0.0121 -0.0258 1055 LYS B CE  
16853 N NZ  . LYS B 1057 ? 0.4793 0.3709 0.4450 0.0700  -0.0112 -0.0287 1055 LYS B NZ  
16854 N N   . TRP B 1058 ? 0.3670 0.2460 0.3340 0.0541  -0.0161 -0.0165 1056 TRP B N   
16855 C CA  . TRP B 1058 ? 0.3890 0.2600 0.3535 0.0507  -0.0173 -0.0153 1056 TRP B CA  
16856 C C   . TRP B 1058 ? 0.3817 0.2530 0.3468 0.0496  -0.0175 -0.0121 1056 TRP B C   
16857 O O   . TRP B 1058 ? 0.4126 0.2761 0.3747 0.0496  -0.0186 -0.0107 1056 TRP B O   
16858 C CB  . TRP B 1058 ? 0.3874 0.2594 0.3529 0.0460  -0.0174 -0.0162 1056 TRP B CB  
16859 C CG  . TRP B 1058 ? 0.3873 0.2525 0.3512 0.0419  -0.0185 -0.0149 1056 TRP B CG  
16860 C CD1 . TRP B 1058 ? 0.4711 0.3264 0.4309 0.0414  -0.0199 -0.0158 1056 TRP B CD1 
16861 C CD2 . TRP B 1058 ? 0.3696 0.2374 0.3358 0.0376  -0.0184 -0.0126 1056 TRP B CD2 
16862 N NE1 . TRP B 1058 ? 0.4728 0.3245 0.4325 0.0369  -0.0206 -0.0140 1056 TRP B NE1 
16863 C CE2 . TRP B 1058 ? 0.4461 0.3055 0.4097 0.0345  -0.0197 -0.0120 1056 TRP B CE2 
16864 C CE3 . TRP B 1058 ? 0.3929 0.2691 0.3629 0.0361  -0.0173 -0.0110 1056 TRP B CE3 
16865 C CZ2 . TRP B 1058 ? 0.4087 0.2685 0.3738 0.0300  -0.0197 -0.0097 1056 TRP B CZ2 
16866 C CZ3 . TRP B 1058 ? 0.4391 0.3153 0.4102 0.0318  -0.0173 -0.0088 1056 TRP B CZ3 
16867 C CH2 . TRP B 1058 ? 0.4290 0.2973 0.3979 0.0288  -0.0185 -0.0082 1056 TRP B CH2 
16868 N N   . LEU B 1059 ? 0.3267 0.2068 0.2956 0.0485  -0.0166 -0.0108 1057 LEU B N   
16869 C CA  . LEU B 1059 ? 0.3760 0.2570 0.3454 0.0475  -0.0167 -0.0078 1057 LEU B CA  
16870 C C   . LEU B 1059 ? 0.4378 0.3151 0.4049 0.0518  -0.0174 -0.0067 1057 LEU B C   
16871 O O   . LEU B 1059 ? 0.4441 0.3160 0.4091 0.0511  -0.0182 -0.0044 1057 LEU B O   
16872 C CB  . LEU B 1059 ? 0.3313 0.2226 0.3047 0.0464  -0.0155 -0.0071 1057 LEU B CB  
16873 C CG  . LEU B 1059 ? 0.3265 0.2214 0.3022 0.0417  -0.0149 -0.0074 1057 LEU B CG  
16874 C CD1 . LEU B 1059 ? 0.3333 0.2381 0.3127 0.0414  -0.0138 -0.0071 1057 LEU B CD1 
16875 C CD2 . LEU B 1059 ? 0.4031 0.2932 0.3776 0.0378  -0.0154 -0.0054 1057 LEU B CD2 
16876 N N   . ASP B 1060 ? 0.3966 0.2770 0.3644 0.0563  -0.0170 -0.0081 1058 ASP B N   
16877 C CA  . ASP B 1060 ? 0.4113 0.2883 0.3772 0.0607  -0.0178 -0.0070 1058 ASP B CA  
16878 C C   . ASP B 1060 ? 0.4570 0.3224 0.4183 0.0617  -0.0189 -0.0073 1058 ASP B C   
16879 O O   . ASP B 1060 ? 0.5091 0.3692 0.4681 0.0635  -0.0199 -0.0054 1058 ASP B O   
16880 C CB  . ASP B 1060 ? 0.4924 0.3756 0.4604 0.0654  -0.0171 -0.0084 1058 ASP B CB  
16881 C CG  . ASP B 1060 ? 0.5746 0.4671 0.5461 0.0659  -0.0166 -0.0068 1058 ASP B CG  
16882 O OD1 . ASP B 1060 ? 0.5731 0.4648 0.5441 0.0653  -0.0173 -0.0042 1058 ASP B OD1 
16883 O OD2 . ASP B 1060 ? 0.4766 0.3770 0.4512 0.0667  -0.0156 -0.0082 1058 ASP B OD2 
16884 N N   . GLY B 1061 ? 0.4670 0.3282 0.4268 0.0606  -0.0190 -0.0097 1059 GLY B N   
16885 C CA  . GLY B 1061 ? 0.4851 0.3347 0.4401 0.0610  -0.0202 -0.0102 1059 GLY B CA  
16886 C C   . GLY B 1061 ? 0.5589 0.4024 0.5120 0.0576  -0.0212 -0.0074 1059 GLY B C   
16887 O O   . GLY B 1061 ? 0.5387 0.3736 0.4881 0.0593  -0.0223 -0.0064 1059 GLY B O   
16888 N N   . LYS B 1062 ? 0.4881 0.3358 0.4436 0.0527  -0.0208 -0.0061 1060 LYS B N   
16889 C CA  . LYS B 1062 ? 0.5305 0.3733 0.4845 0.0490  -0.0215 -0.0034 1060 LYS B CA  
16890 C C   . LYS B 1062 ? 0.5584 0.4051 0.5134 0.0497  -0.0212 -0.0003 1060 LYS B C   
16891 O O   . LYS B 1062 ? 0.6071 0.4515 0.5614 0.0463  -0.0214 0.0022  1060 LYS B O   
16892 C CB  . LYS B 1062 ? 0.5787 0.4231 0.5344 0.0432  -0.0212 -0.0035 1060 LYS B CB  
16893 C CG  . LYS B 1062 ? 0.5823 0.4379 0.5427 0.0417  -0.0197 -0.0040 1060 LYS B CG  
16894 C CD  . LYS B 1062 ? 0.5172 0.3736 0.4791 0.0364  -0.0196 -0.0044 1060 LYS B CD  
16895 C CE  . LYS B 1062 ? 0.4811 0.3328 0.4419 0.0324  -0.0201 -0.0016 1060 LYS B CE  
16896 N NZ  . LYS B 1062 ? 0.5964 0.4473 0.5584 0.0274  -0.0202 -0.0021 1060 LYS B NZ  
16897 N N   . GLY B 1063 ? 0.5290 0.3816 0.4857 0.0538  -0.0208 -0.0005 1061 GLY B N   
16898 C CA  . GLY B 1063 ? 0.5155 0.3711 0.4726 0.0549  -0.0209 0.0023  1061 GLY B CA  
16899 C C   . GLY B 1063 ? 0.5972 0.4616 0.5577 0.0516  -0.0198 0.0036  1061 GLY B C   
16900 O O   . GLY B 1063 ? 0.5390 0.4050 0.4992 0.0518  -0.0200 0.0062  1061 GLY B O   
16901 N N   . ALA B 1064 ? 0.4735 0.3431 0.4368 0.0487  -0.0188 0.0020  1062 ALA B N   
16902 C CA  . ALA B 1064 ? 0.4780 0.3559 0.4445 0.0458  -0.0177 0.0030  1062 ALA B CA  
16903 C C   . ALA B 1064 ? 0.4649 0.3516 0.4341 0.0490  -0.0172 0.0023  1062 ALA B C   
16904 O O   . ALA B 1064 ? 0.4114 0.3046 0.3836 0.0488  -0.0163 0.0004  1062 ALA B O   
16905 C CB  . ALA B 1064 ? 0.4561 0.3361 0.4245 0.0416  -0.0170 0.0015  1062 ALA B CB  
16906 N N   . ARG B 1065 ? 0.4667 0.3533 0.4349 0.0519  -0.0178 0.0041  1063 ARG B N   
16907 C CA  . ARG B 1065 ? 0.4408 0.3346 0.4113 0.0556  -0.0177 0.0036  1063 ARG B CA  
16908 C C   . ARG B 1065 ? 0.4224 0.3258 0.3963 0.0534  -0.0166 0.0036  1063 ARG B C   
16909 O O   . ARG B 1065 ? 0.4103 0.3203 0.3870 0.0548  -0.0160 0.0018  1063 ARG B O   
16910 C CB  . ARG B 1065 ? 0.5087 0.3999 0.4771 0.0591  -0.0189 0.0057  1063 ARG B CB  
16911 N N   . ALA B 1066 ? 0.3734 0.2775 0.3469 0.0501  -0.0164 0.0057  1064 ALA B N   
16912 C CA  . ALA B 1066 ? 0.3920 0.3047 0.3685 0.0480  -0.0153 0.0056  1064 ALA B CA  
16913 C C   . ALA B 1066 ? 0.3819 0.2977 0.3608 0.0458  -0.0143 0.0032  1064 ALA B C   
16914 O O   . ALA B 1066 ? 0.3822 0.3055 0.3641 0.0459  -0.0135 0.0020  1064 ALA B O   
16915 C CB  . ALA B 1066 ? 0.4336 0.3457 0.4088 0.0447  -0.0151 0.0082  1064 ALA B CB  
16916 N N   . GLU B 1067 ? 0.3613 0.2715 0.3392 0.0437  -0.0142 0.0025  1065 GLU B N   
16917 C CA  . GLU B 1067 ? 0.3943 0.3072 0.3744 0.0415  -0.0134 0.0003  1065 GLU B CA  
16918 C C   . GLU B 1067 ? 0.3306 0.2457 0.3117 0.0446  -0.0134 -0.0022 1065 GLU B C   
16919 O O   . GLU B 1067 ? 0.3125 0.2336 0.2963 0.0439  -0.0126 -0.0038 1065 GLU B O   
16920 C CB  . GLU B 1067 ? 0.3544 0.2607 0.3330 0.0383  -0.0136 0.0004  1065 GLU B CB  
16921 C CG  . GLU B 1067 ? 0.3659 0.2719 0.3443 0.0345  -0.0132 0.0027  1065 GLU B CG  
16922 C CD  . GLU B 1067 ? 0.4424 0.3429 0.4176 0.0352  -0.0139 0.0053  1065 GLU B CD  
16923 O OE1 . GLU B 1067 ? 0.4200 0.3161 0.3931 0.0386  -0.0150 0.0053  1065 GLU B OE1 
16924 O OE2 . GLU B 1067 ? 0.4393 0.3399 0.4141 0.0323  -0.0134 0.0075  1065 GLU B OE2 
16925 N N   . ALA B 1068 ? 0.3455 0.2557 0.3246 0.0482  -0.0142 -0.0027 1066 ALA B N   
16926 C CA  . ALA B 1068 ? 0.3689 0.2814 0.3490 0.0515  -0.0140 -0.0050 1066 ALA B CA  
16927 C C   . ALA B 1068 ? 0.3483 0.2700 0.3314 0.0532  -0.0134 -0.0050 1066 ALA B C   
16928 O O   . ALA B 1068 ? 0.3051 0.2320 0.2904 0.0537  -0.0127 -0.0069 1066 ALA B O   
16929 C CB  . ALA B 1068 ? 0.3478 0.2534 0.3249 0.0554  -0.0150 -0.0052 1066 ALA B CB  
16930 N N   . GLU B 1069 ? 0.2982 0.2220 0.2814 0.0538  -0.0138 -0.0028 1067 GLU B N   
16931 C CA  . GLU B 1069 ? 0.3790 0.3115 0.3651 0.0550  -0.0135 -0.0027 1067 GLU B CA  
16932 C C   . GLU B 1069 ? 0.3819 0.3204 0.3704 0.0514  -0.0124 -0.0033 1067 GLU B C   
16933 O O   . GLU B 1069 ? 0.3240 0.2691 0.3151 0.0521  -0.0118 -0.0046 1067 GLU B O   
16934 C CB  . GLU B 1069 ? 0.3906 0.3234 0.3757 0.0560  -0.0144 -0.0001 1067 GLU B CB  
16935 C CG  . GLU B 1069 ? 0.3916 0.3332 0.3795 0.0568  -0.0143 0.0003  1067 GLU B CG  
16936 C CD  . GLU B 1069 ? 0.5017 0.4475 0.4917 0.0609  -0.0144 -0.0010 1067 GLU B CD  
16937 O OE1 . GLU B 1069 ? 0.5167 0.4583 0.5057 0.0636  -0.0145 -0.0022 1067 GLU B OE1 
16938 O OE2 . GLU B 1069 ? 0.5886 0.5419 0.5811 0.0615  -0.0144 -0.0008 1067 GLU B OE2 
16939 N N   . ALA B 1070 ? 0.3206 0.2569 0.3083 0.0476  -0.0121 -0.0024 1068 ALA B N   
16940 C CA  . ALA B 1070 ? 0.3313 0.2727 0.3213 0.0443  -0.0111 -0.0030 1068 ALA B CA  
16941 C C   . ALA B 1070 ? 0.2893 0.2317 0.2806 0.0442  -0.0106 -0.0056 1068 ALA B C   
16942 O O   . ALA B 1070 ? 0.3086 0.2571 0.3023 0.0434  -0.0098 -0.0066 1068 ALA B O   
16943 C CB  . ALA B 1070 ? 0.3792 0.3176 0.3682 0.0405  -0.0108 -0.0016 1068 ALA B CB  
16944 N N   . ALA B 1071 ? 0.2880 0.2242 0.2775 0.0450  -0.0110 -0.0066 1069 ALA B N   
16945 C CA  . ALA B 1071 ? 0.2848 0.2214 0.2749 0.0450  -0.0106 -0.0091 1069 ALA B CA  
16946 C C   . ALA B 1071 ? 0.2672 0.2093 0.2590 0.0481  -0.0101 -0.0104 1069 ALA B C   
16947 O O   . ALA B 1071 ? 0.2765 0.2236 0.2703 0.0473  -0.0094 -0.0118 1069 ALA B O   
16948 C CB  . ALA B 1071 ? 0.2635 0.1917 0.2508 0.0453  -0.0113 -0.0099 1069 ALA B CB  
16949 N N   . ARG B 1072 ? 0.2765 0.2181 0.2677 0.0519  -0.0106 -0.0099 1070 ARG B N   
16950 C CA  A ARG B 1072 ? 0.2913 0.2388 0.2845 0.0549  -0.0101 -0.0110 1070 ARG B CA  
16951 C CA  B ARG B 1072 ? 0.2915 0.2390 0.2847 0.0549  -0.0101 -0.0110 1070 ARG B CA  
16952 C C   . ARG B 1072 ? 0.2924 0.2483 0.2886 0.0535  -0.0096 -0.0105 1070 ARG B C   
16953 O O   . ARG B 1072 ? 0.2759 0.2373 0.2742 0.0538  -0.0088 -0.0119 1070 ARG B O   
16954 C CB  A ARG B 1072 ? 0.3020 0.2477 0.2942 0.0592  -0.0109 -0.0102 1070 ARG B CB  
16955 C CB  B ARG B 1072 ? 0.3028 0.2483 0.2950 0.0593  -0.0108 -0.0104 1070 ARG B CB  
16956 C CG  A ARG B 1072 ? 0.3372 0.2753 0.3266 0.0617  -0.0112 -0.0113 1070 ARG B CG  
16957 C CG  B ARG B 1072 ? 0.3325 0.2691 0.3213 0.0609  -0.0114 -0.0111 1070 ARG B CG  
16958 C CD  A ARG B 1072 ? 0.3417 0.2790 0.3306 0.0663  -0.0119 -0.0106 1070 ARG B CD  
16959 C CD  B ARG B 1072 ? 0.3381 0.2735 0.3263 0.0660  -0.0117 -0.0113 1070 ARG B CD  
16960 N NE  A ARG B 1072 ? 0.3628 0.2978 0.3506 0.0661  -0.0129 -0.0080 1070 ARG B NE  
16961 N NE  B ARG B 1072 ? 0.3440 0.2700 0.3285 0.0673  -0.0123 -0.0120 1070 ARG B NE  
16962 C CZ  A ARG B 1072 ? 0.3732 0.2998 0.3578 0.0661  -0.0139 -0.0069 1070 ARG B CZ  
16963 C CZ  B ARG B 1072 ? 0.3018 0.2247 0.2849 0.0680  -0.0118 -0.0144 1070 ARG B CZ  
16964 N NH1 A ARG B 1072 ? 0.3716 0.2909 0.3535 0.0665  -0.0140 -0.0083 1070 ARG B NH1 
16965 N NH1 B ARG B 1072 ? 0.3718 0.3004 0.3569 0.0677  -0.0107 -0.0162 1070 ARG B NH1 
16966 N NH2 A ARG B 1072 ? 0.3299 0.2552 0.3135 0.0657  -0.0148 -0.0044 1070 ARG B NH2 
16967 N NH2 B ARG B 1072 ? 0.3134 0.2270 0.2927 0.0688  -0.0126 -0.0149 1070 ARG B NH2 
16968 N N   . ASN B 1073 ? 0.2792 0.2361 0.2755 0.0518  -0.0099 -0.0085 1071 ASN B N   
16969 C CA  . ASN B 1073 ? 0.2840 0.2483 0.2827 0.0503  -0.0095 -0.0081 1071 ASN B CA  
16970 C C   . ASN B 1073 ? 0.2783 0.2450 0.2783 0.0471  -0.0086 -0.0093 1071 ASN B C   
16971 O O   . ASN B 1073 ? 0.2962 0.2692 0.2985 0.0468  -0.0080 -0.0101 1071 ASN B O   
16972 C CB  . ASN B 1073 ? 0.3070 0.2709 0.3048 0.0490  -0.0101 -0.0057 1071 ASN B CB  
16973 C CG  . ASN B 1073 ? 0.3923 0.3556 0.3893 0.0523  -0.0112 -0.0043 1071 ASN B CG  
16974 O OD1 . ASN B 1073 ? 0.4184 0.3840 0.4166 0.0556  -0.0113 -0.0051 1071 ASN B OD1 
16975 N ND2 . ASN B 1073 ? 0.4241 0.3846 0.4192 0.0515  -0.0119 -0.0022 1071 ASN B ND2 
16976 N N   . ALA B 1074 ? 0.2613 0.2232 0.2600 0.0447  -0.0085 -0.0095 1072 ALA B N   
16977 C CA  . ALA B 1074 ? 0.2573 0.2212 0.2573 0.0419  -0.0077 -0.0108 1072 ALA B CA  
16978 C C   . ALA B 1074 ? 0.2416 0.2072 0.2423 0.0434  -0.0073 -0.0129 1072 ALA B C   
16979 O O   . ALA B 1074 ? 0.2381 0.2086 0.2406 0.0422  -0.0066 -0.0138 1072 ALA B O   
16980 C CB  . ALA B 1074 ? 0.2587 0.2168 0.2572 0.0392  -0.0079 -0.0105 1072 ALA B CB  
16981 N N   . GLY B 1075 ? 0.2407 0.2023 0.2398 0.0461  -0.0076 -0.0138 1073 GLY B N   
16982 C CA  . GLY B 1075 ? 0.2542 0.2172 0.2535 0.0477  -0.0071 -0.0158 1073 GLY B CA  
16983 C C   . GLY B 1075 ? 0.2671 0.2378 0.2690 0.0491  -0.0064 -0.0161 1073 GLY B C   
16984 O O   . GLY B 1075 ? 0.2894 0.2637 0.2924 0.0486  -0.0056 -0.0174 1073 GLY B O   
16985 N N   . SER B 1076 ? 0.2758 0.2493 0.2786 0.0507  -0.0067 -0.0146 1074 SER B N   
16986 C CA  . SER B 1076 ? 0.2650 0.2461 0.2705 0.0520  -0.0063 -0.0146 1074 SER B CA  
16987 C C   . SER B 1076 ? 0.2773 0.2634 0.2846 0.0487  -0.0059 -0.0142 1074 SER B C   
16988 O O   . SER B 1076 ? 0.3106 0.3020 0.3197 0.0484  -0.0052 -0.0151 1074 SER B O   
16989 C CB  . SER B 1076 ? 0.3052 0.2876 0.3112 0.0548  -0.0070 -0.0132 1074 SER B CB  
16990 O OG  . SER B 1076 ? 0.3457 0.3244 0.3503 0.0584  -0.0072 -0.0138 1074 SER B OG  
16991 N N   . SER B 1077 ? 0.2426 0.2270 0.2492 0.0463  -0.0064 -0.0129 1075 SER B N   
16992 C CA  . SER B 1077 ? 0.2778 0.2668 0.2859 0.0435  -0.0060 -0.0125 1075 SER B CA  
16993 C C   . SER B 1077 ? 0.2689 0.2578 0.2773 0.0409  -0.0053 -0.0137 1075 SER B C   
16994 O O   . SER B 1077 ? 0.3233 0.3166 0.3332 0.0391  -0.0049 -0.0138 1075 SER B O   
16995 C CB  . SER B 1077 ? 0.3376 0.3254 0.3448 0.0422  -0.0066 -0.0106 1075 SER B CB  
16996 O OG  . SER B 1077 ? 0.3477 0.3303 0.3533 0.0400  -0.0065 -0.0103 1075 SER B OG  
16997 N N   . SER B 1078 ? 0.2186 0.2025 0.2256 0.0407  -0.0053 -0.0146 1076 SER B N   
16998 C CA  . SER B 1078 ? 0.2089 0.1928 0.2162 0.0385  -0.0048 -0.0159 1076 SER B CA  
16999 C C   . SER B 1078 ? 0.2237 0.2130 0.2325 0.0390  -0.0041 -0.0171 1076 SER B C   
17000 O O   . SER B 1078 ? 0.2268 0.2177 0.2358 0.0417  -0.0039 -0.0176 1076 SER B O   
17001 C CB  . SER B 1078 ? 0.2321 0.2101 0.2375 0.0388  -0.0051 -0.0169 1076 SER B CB  
17002 O OG  . SER B 1078 ? 0.2129 0.1913 0.2185 0.0371  -0.0047 -0.0183 1076 SER B OG  
17003 N N   . ALA B 1079 ? 0.1935 0.1854 0.2034 0.0366  -0.0037 -0.0174 1077 ALA B N   
17004 C CA  . ALA B 1079 ? 0.2030 0.1996 0.2141 0.0367  -0.0030 -0.0184 1077 ALA B CA  
17005 C C   . ALA B 1079 ? 0.1967 0.1911 0.2069 0.0361  -0.0027 -0.0199 1077 ALA B C   
17006 O O   . ALA B 1079 ? 0.1952 0.1930 0.2061 0.0356  -0.0022 -0.0207 1077 ALA B O   
17007 C CB  . ALA B 1079 ? 0.2303 0.2315 0.2430 0.0346  -0.0027 -0.0178 1077 ALA B CB  
17008 N N   . LEU B 1080 ? 0.1962 0.1850 0.2046 0.0360  -0.0032 -0.0203 1078 LEU B N   
17009 C CA  . LEU B 1080 ? 0.1907 0.1769 0.1978 0.0357  -0.0032 -0.0218 1078 LEU B CA  
17010 C C   . LEU B 1080 ? 0.1886 0.1772 0.1954 0.0380  -0.0025 -0.0231 1078 LEU B C   
17011 O O   . LEU B 1080 ? 0.2072 0.1959 0.2137 0.0408  -0.0024 -0.0231 1078 LEU B O   
17012 C CB  . LEU B 1080 ? 0.2007 0.1802 0.2057 0.0359  -0.0040 -0.0220 1078 LEU B CB  
17013 C CG  . LEU B 1080 ? 0.2079 0.1838 0.2109 0.0360  -0.0042 -0.0238 1078 LEU B CG  
17014 C CD1 . LEU B 1080 ? 0.2283 0.2049 0.2319 0.0329  -0.0045 -0.0241 1078 LEU B CD1 
17015 C CD2 . LEU B 1080 ? 0.2416 0.2106 0.2422 0.0368  -0.0051 -0.0240 1078 LEU B CD2 
17016 N N   . GLY B 1081 ? 0.1867 0.1773 0.1935 0.0369  -0.0021 -0.0241 1079 GLY B N   
17017 C CA  . GLY B 1081 ? 0.2109 0.2041 0.2174 0.0389  -0.0012 -0.0252 1079 GLY B CA  
17018 C C   . GLY B 1081 ? 0.2270 0.2270 0.2357 0.0388  -0.0004 -0.0247 1079 GLY B C   
17019 O O   . GLY B 1081 ? 0.2411 0.2441 0.2499 0.0401  0.0005  -0.0255 1079 GLY B O   
17020 N N   . LEU B 1082 ? 0.2078 0.2104 0.2184 0.0372  -0.0006 -0.0233 1080 LEU B N   
17021 C CA  A LEU B 1082 ? 0.2025 0.2112 0.2152 0.0365  -0.0001 -0.0228 1080 LEU B CA  
17022 C CA  B LEU B 1082 ? 0.2025 0.2112 0.2152 0.0365  -0.0001 -0.0228 1080 LEU B CA  
17023 C C   . LEU B 1082 ? 0.2028 0.2129 0.2151 0.0351  0.0005  -0.0237 1080 LEU B C   
17024 O O   . LEU B 1082 ? 0.2181 0.2249 0.2292 0.0334  0.0001  -0.0242 1080 LEU B O   
17025 C CB  A LEU B 1082 ? 0.2026 0.2124 0.2165 0.0345  -0.0006 -0.0214 1080 LEU B CB  
17026 C CB  B LEU B 1082 ? 0.2026 0.2124 0.2165 0.0344  -0.0006 -0.0214 1080 LEU B CB  
17027 C CG  A LEU B 1082 ? 0.1915 0.2071 0.2073 0.0333  -0.0002 -0.0209 1080 LEU B CG  
17028 C CG  B LEU B 1082 ? 0.1924 0.2076 0.2081 0.0331  -0.0003 -0.0208 1080 LEU B CG  
17029 C CD1 A LEU B 1082 ? 0.2318 0.2517 0.2489 0.0355  0.0001  -0.0207 1080 LEU B CD1 
17030 C CD1 B LEU B 1082 ? 0.2211 0.2370 0.2377 0.0323  -0.0009 -0.0195 1080 LEU B CD1 
17031 C CD2 A LEU B 1082 ? 0.2079 0.2237 0.2244 0.0314  -0.0008 -0.0197 1080 LEU B CD2 
17032 C CD2 B LEU B 1082 ? 0.1771 0.1928 0.1927 0.0306  -0.0001 -0.0213 1080 LEU B CD2 
17033 N N   . ASP B 1083 ? 0.2188 0.2336 0.2320 0.0357  0.0014  -0.0239 1081 ASP B N   
17034 C CA  . ASP B 1083 ? 0.2622 0.2782 0.2746 0.0346  0.0020  -0.0248 1081 ASP B CA  
17035 C C   . ASP B 1083 ? 0.2646 0.2869 0.2790 0.0341  0.0027  -0.0241 1081 ASP B C   
17036 O O   . ASP B 1083 ? 0.2919 0.3175 0.3071 0.0361  0.0036  -0.0243 1081 ASP B O   
17037 C CB  . ASP B 1083 ? 0.2775 0.2910 0.2877 0.0366  0.0025  -0.0262 1081 ASP B CB  
17038 C CG  . ASP B 1083 ? 0.4408 0.4552 0.4496 0.0356  0.0031  -0.0271 1081 ASP B CG  
17039 O OD1 . ASP B 1083 ? 0.4570 0.4726 0.4663 0.0331  0.0029  -0.0266 1081 ASP B OD1 
17040 O OD2 . ASP B 1083 ? 0.5036 0.5171 0.5106 0.0374  0.0039  -0.0282 1081 ASP B OD2 
17041 N N   . LEU B 1084 ? 0.2279 0.2519 0.2433 0.0316  0.0024  -0.0234 1082 LEU B N   
17042 C CA  . LEU B 1084 ? 0.2273 0.2568 0.2446 0.0306  0.0028  -0.0226 1082 LEU B CA  
17043 C C   . LEU B 1084 ? 0.2333 0.2639 0.2501 0.0285  0.0032  -0.0229 1082 LEU B C   
17044 O O   . LEU B 1084 ? 0.2224 0.2495 0.2377 0.0272  0.0028  -0.0233 1082 LEU B O   
17045 C CB  . LEU B 1084 ? 0.2709 0.3009 0.2895 0.0293  0.0020  -0.0215 1082 LEU B CB  
17046 C CG  . LEU B 1084 ? 0.3212 0.3507 0.3405 0.0310  0.0014  -0.0208 1082 LEU B CG  
17047 C CD1 . LEU B 1084 ? 0.3043 0.3337 0.3242 0.0293  0.0006  -0.0198 1082 LEU B CD1 
17048 C CD2 . LEU B 1084 ? 0.3491 0.3833 0.3701 0.0331  0.0019  -0.0206 1082 LEU B CD2 
17049 N N   . GLU B 1085 ? 0.2070 0.2425 0.2250 0.0281  0.0040  -0.0225 1083 GLU B N   
17050 C CA  . GLU B 1085 ? 0.1880 0.2251 0.2058 0.0257  0.0042  -0.0223 1083 GLU B CA  
17051 C C   . GLU B 1085 ? 0.2141 0.2534 0.2335 0.0238  0.0036  -0.0212 1083 GLU B C   
17052 O O   . GLU B 1085 ? 0.2358 0.2788 0.2571 0.0244  0.0036  -0.0206 1083 GLU B O   
17053 C CB  . GLU B 1085 ? 0.2158 0.2566 0.2336 0.0261  0.0055  -0.0226 1083 GLU B CB  
17054 C CG  . GLU B 1085 ? 0.2482 0.2898 0.2653 0.0234  0.0056  -0.0223 1083 GLU B CG  
17055 C CD  . GLU B 1085 ? 0.3301 0.3748 0.3466 0.0235  0.0070  -0.0224 1083 GLU B CD  
17056 O OE1 . GLU B 1085 ? 0.3645 0.4100 0.3806 0.0258  0.0080  -0.0231 1083 GLU B OE1 
17057 O OE2 . GLU B 1085 ? 0.3255 0.3715 0.3418 0.0212  0.0071  -0.0219 1083 GLU B OE2 
17058 N N   . LEU B 1086 ? 0.1994 0.2365 0.2180 0.0216  0.0030  -0.0210 1084 LEU B N   
17059 C CA  . LEU B 1086 ? 0.1956 0.2338 0.2151 0.0198  0.0024  -0.0202 1084 LEU B CA  
17060 C C   . LEU B 1086 ? 0.2515 0.2930 0.2714 0.0178  0.0028  -0.0198 1084 LEU B C   
17061 O O   . LEU B 1086 ? 0.2547 0.2957 0.2734 0.0172  0.0033  -0.0201 1084 LEU B O   
17062 C CB  . LEU B 1086 ? 0.2154 0.2492 0.2339 0.0186  0.0017  -0.0202 1084 LEU B CB  
17063 C CG  . LEU B 1086 ? 0.2232 0.2536 0.2413 0.0200  0.0013  -0.0205 1084 LEU B CG  
17064 C CD1 . LEU B 1086 ? 0.2330 0.2597 0.2504 0.0187  0.0007  -0.0204 1084 LEU B CD1 
17065 C CD2 . LEU B 1086 ? 0.2685 0.3006 0.2878 0.0213  0.0010  -0.0199 1084 LEU B CD2 
17066 N N   . PRO B 1087 ? 0.2219 0.2667 0.2433 0.0168  0.0025  -0.0190 1085 PRO B N   
17067 C CA  . PRO B 1087 ? 0.2296 0.2773 0.2512 0.0146  0.0027  -0.0185 1085 PRO B CA  
17068 C C   . PRO B 1087 ? 0.2236 0.2677 0.2434 0.0126  0.0024  -0.0186 1085 PRO B C   
17069 O O   . PRO B 1087 ? 0.2370 0.2775 0.2560 0.0122  0.0017  -0.0187 1085 PRO B O   
17070 C CB  . PRO B 1087 ? 0.2675 0.3182 0.2908 0.0137  0.0020  -0.0177 1085 PRO B CB  
17071 C CG  . PRO B 1087 ? 0.2611 0.3122 0.2854 0.0161  0.0017  -0.0177 1085 PRO B CG  
17072 C CD  . PRO B 1087 ? 0.2295 0.2757 0.2523 0.0176  0.0018  -0.0185 1085 PRO B CD  
17073 N N   . GLY B 1088 ? 0.2338 0.2788 0.2529 0.0113  0.0030  -0.0185 1086 GLY B N   
17074 C CA  . GLY B 1088 ? 0.2383 0.2799 0.2555 0.0095  0.0027  -0.0185 1086 GLY B CA  
17075 C C   . GLY B 1088 ? 0.2104 0.2542 0.2271 0.0079  0.0033  -0.0181 1086 GLY B C   
17076 O O   . GLY B 1088 ? 0.2197 0.2681 0.2378 0.0077  0.0039  -0.0176 1086 GLY B O   
17077 N N   . PRO B 1089 ? 0.2098 0.2504 0.2245 0.0068  0.0032  -0.0181 1087 PRO B N   
17078 C CA  . PRO B 1089 ? 0.2157 0.2578 0.2294 0.0050  0.0037  -0.0176 1087 PRO B CA  
17079 C C   . PRO B 1089 ? 0.2149 0.2595 0.2284 0.0063  0.0050  -0.0178 1087 PRO B C   
17080 O O   . PRO B 1089 ? 0.2208 0.2643 0.2340 0.0085  0.0053  -0.0186 1087 PRO B O   
17081 C CB  . PRO B 1089 ? 0.2340 0.2712 0.2454 0.0040  0.0031  -0.0176 1087 PRO B CB  
17082 C CG  . PRO B 1089 ? 0.2631 0.2971 0.2744 0.0060  0.0026  -0.0185 1087 PRO B CG  
17083 C CD  . PRO B 1089 ? 0.2270 0.2627 0.2403 0.0071  0.0025  -0.0186 1087 PRO B CD  
17084 N N   . VAL B 1090 ? 0.1875 0.2352 0.2009 0.0048  0.0058  -0.0171 1088 VAL B N   
17085 C CA  . VAL B 1090 ? 0.1985 0.2482 0.2111 0.0057  0.0071  -0.0173 1088 VAL B CA  
17086 C C   . VAL B 1090 ? 0.2010 0.2461 0.2106 0.0062  0.0070  -0.0178 1088 VAL B C   
17087 O O   . VAL B 1090 ? 0.2146 0.2555 0.2228 0.0051  0.0059  -0.0178 1088 VAL B O   
17088 C CB  . VAL B 1090 ? 0.2163 0.2704 0.2294 0.0037  0.0081  -0.0162 1088 VAL B CB  
17089 C CG1 . VAL B 1090 ? 0.2219 0.2811 0.2383 0.0032  0.0081  -0.0156 1088 VAL B CG1 
17090 C CG2 . VAL B 1090 ? 0.2148 0.2657 0.2256 0.0009  0.0075  -0.0154 1088 VAL B CG2 
17091 N N   . GLY B 1091 ? 0.2110 0.2568 0.2193 0.0078  0.0080  -0.0185 1089 GLY B N   
17092 C CA  . GLY B 1091 ? 0.2090 0.2507 0.2142 0.0082  0.0078  -0.0190 1089 GLY B CA  
17093 C C   . GLY B 1091 ? 0.2187 0.2561 0.2235 0.0096  0.0066  -0.0200 1089 GLY B C   
17094 O O   . GLY B 1091 ? 0.2140 0.2475 0.2165 0.0095  0.0059  -0.0203 1089 GLY B O   
17095 N N   . GLU B 1092 ? 0.2126 0.2505 0.2197 0.0108  0.0062  -0.0203 1090 GLU B N   
17096 C CA  . GLU B 1092 ? 0.2114 0.2456 0.2184 0.0122  0.0052  -0.0211 1090 GLU B CA  
17097 C C   . GLU B 1092 ? 0.2157 0.2519 0.2245 0.0143  0.0057  -0.0216 1090 GLU B C   
17098 O O   . GLU B 1092 ? 0.2363 0.2766 0.2473 0.0143  0.0063  -0.0211 1090 GLU B O   
17099 C CB  . GLU B 1092 ? 0.2439 0.2759 0.2519 0.0109  0.0040  -0.0206 1090 GLU B CB  
17100 C CG  . GLU B 1092 ? 0.3496 0.3770 0.3562 0.0107  0.0029  -0.0210 1090 GLU B CG  
17101 C CD  . GLU B 1092 ? 0.3395 0.3653 0.3471 0.0094  0.0020  -0.0204 1090 GLU B CD  
17102 O OE1 . GLU B 1092 ? 0.2900 0.3166 0.2994 0.0097  0.0018  -0.0203 1090 GLU B OE1 
17103 O OE2 . GLU B 1092 ? 0.3405 0.3640 0.3468 0.0082  0.0014  -0.0201 1090 GLU B OE2 
17104 N N   . ARG B 1093 ? 0.1957 0.2290 0.2037 0.0161  0.0054  -0.0226 1091 ARG B N   
17105 C CA  . ARG B 1093 ? 0.2050 0.2388 0.2145 0.0182  0.0054  -0.0230 1091 ARG B CA  
17106 C C   . ARG B 1093 ? 0.2111 0.2410 0.2209 0.0181  0.0041  -0.0232 1091 ARG B C   
17107 O O   . ARG B 1093 ? 0.2002 0.2263 0.2084 0.0179  0.0034  -0.0237 1091 ARG B O   
17108 C CB  . ARG B 1093 ? 0.2267 0.2602 0.2347 0.0205  0.0063  -0.0241 1091 ARG B CB  
17109 C CG  . ARG B 1093 ? 0.3681 0.4066 0.3768 0.0213  0.0079  -0.0239 1091 ARG B CG  
17110 C CD  . ARG B 1093 ? 0.4858 0.5241 0.4938 0.0243  0.0087  -0.0250 1091 ARG B CD  
17111 N NE  . ARG B 1093 ? 0.5238 0.5575 0.5284 0.0249  0.0085  -0.0262 1091 ARG B NE  
17112 C CZ  . ARG B 1093 ? 0.6566 0.6904 0.6586 0.0248  0.0094  -0.0266 1091 ARG B CZ  
17113 N NH1 . ARG B 1093 ? 0.6206 0.6590 0.6230 0.0242  0.0108  -0.0259 1091 ARG B NH1 
17114 N NH2 . ARG B 1093 ? 0.6188 0.6479 0.6174 0.0252  0.0088  -0.0277 1091 ARG B NH2 
17115 N N   . ASN B 1094 ? 0.1831 0.2141 0.1951 0.0182  0.0038  -0.0226 1092 ASN B N   
17116 C CA  . ASN B 1094 ? 0.1733 0.2011 0.1857 0.0179  0.0027  -0.0226 1092 ASN B CA  
17117 C C   . ASN B 1094 ? 0.1974 0.2248 0.2106 0.0200  0.0027  -0.0228 1092 ASN B C   
17118 O O   . ASN B 1094 ? 0.2137 0.2444 0.2285 0.0207  0.0031  -0.0224 1092 ASN B O   
17119 C CB  . ASN B 1094 ? 0.1900 0.2187 0.2036 0.0161  0.0023  -0.0217 1092 ASN B CB  
17120 C CG  . ASN B 1094 ? 0.1953 0.2229 0.2077 0.0142  0.0021  -0.0215 1092 ASN B CG  
17121 O OD1 . ASN B 1094 ? 0.2018 0.2261 0.2133 0.0139  0.0014  -0.0217 1092 ASN B OD1 
17122 N ND2 . ASN B 1094 ? 0.2036 0.2339 0.2160 0.0129  0.0026  -0.0209 1092 ASN B ND2 
17123 N N   . LEU B 1095 ? 0.1861 0.2097 0.1982 0.0209  0.0022  -0.0235 1093 LEU B N   
17124 C CA  . LEU B 1095 ? 0.1890 0.2114 0.2012 0.0230  0.0022  -0.0239 1093 LEU B CA  
17125 C C   . LEU B 1095 ? 0.1608 0.1802 0.1737 0.0227  0.0013  -0.0236 1093 LEU B C   
17126 O O   . LEU B 1095 ? 0.1879 0.2051 0.2006 0.0211  0.0007  -0.0235 1093 LEU B O   
17127 C CB  . LEU B 1095 ? 0.2134 0.2334 0.2235 0.0244  0.0024  -0.0251 1093 LEU B CB  
17128 C CG  . LEU B 1095 ? 0.2375 0.2602 0.2465 0.0246  0.0035  -0.0255 1093 LEU B CG  
17129 C CD1 . LEU B 1095 ? 0.2927 0.3123 0.2989 0.0260  0.0037  -0.0268 1093 LEU B CD1 
17130 C CD2 . LEU B 1095 ? 0.2445 0.2722 0.2553 0.0257  0.0046  -0.0250 1093 LEU B CD2 
17131 N N   . TYR B 1096 ? 0.1727 0.1920 0.1863 0.0241  0.0012  -0.0234 1094 TYR B N   
17132 C CA  . TYR B 1096 ? 0.1688 0.1855 0.1829 0.0238  0.0005  -0.0229 1094 TYR B CA  
17133 C C   . TYR B 1096 ? 0.1723 0.1866 0.1858 0.0260  0.0004  -0.0233 1094 TYR B C   
17134 O O   . TYR B 1096 ? 0.1842 0.2007 0.1981 0.0278  0.0009  -0.0232 1094 TYR B O   
17135 C CB  . TYR B 1096 ? 0.1777 0.1969 0.1933 0.0230  0.0005  -0.0218 1094 TYR B CB  
17136 C CG  . TYR B 1096 ? 0.1778 0.1948 0.1938 0.0230  -0.0001 -0.0211 1094 TYR B CG  
17137 C CD1 . TYR B 1096 ? 0.1848 0.1997 0.2008 0.0213  -0.0004 -0.0208 1094 TYR B CD1 
17138 C CD2 . TYR B 1096 ? 0.2237 0.2409 0.2401 0.0246  -0.0002 -0.0207 1094 TYR B CD2 
17139 C CE1 . TYR B 1096 ? 0.1828 0.1960 0.1991 0.0212  -0.0007 -0.0201 1094 TYR B CE1 
17140 C CE2 . TYR B 1096 ? 0.2103 0.2254 0.2267 0.0244  -0.0006 -0.0200 1094 TYR B CE2 
17141 C CZ  . TYR B 1096 ? 0.2043 0.2174 0.2206 0.0227  -0.0008 -0.0197 1094 TYR B CZ  
17142 O OH  . TYR B 1096 ? 0.2053 0.2166 0.2216 0.0224  -0.0011 -0.0189 1094 TYR B OH  
17143 N N   . THR B 1097 ? 0.1799 0.1899 0.1924 0.0258  -0.0002 -0.0236 1095 THR B N   
17144 C CA  . THR B 1097 ? 0.1925 0.1992 0.2038 0.0277  -0.0005 -0.0241 1095 THR B CA  
17145 C C   . THR B 1097 ? 0.1788 0.1820 0.1903 0.0270  -0.0012 -0.0235 1095 THR B C   
17146 O O   . THR B 1097 ? 0.2049 0.2073 0.2170 0.0250  -0.0016 -0.0231 1095 THR B O   
17147 C CB  . THR B 1097 ? 0.2419 0.2462 0.2511 0.0282  -0.0005 -0.0255 1095 THR B CB  
17148 O OG1 . THR B 1097 ? 0.2919 0.2940 0.3007 0.0261  -0.0012 -0.0256 1095 THR B OG1 
17149 C CG2 . THR B 1097 ? 0.2344 0.2422 0.2432 0.0289  0.0005  -0.0260 1095 THR B CG2 
17150 N N   . LEU B 1098 ? 0.1876 0.1887 0.1987 0.0287  -0.0014 -0.0233 1096 LEU B N   
17151 C CA  . LEU B 1098 ? 0.1723 0.1696 0.1833 0.0281  -0.0021 -0.0227 1096 LEU B CA  
17152 C C   . LEU B 1098 ? 0.1864 0.1787 0.1953 0.0289  -0.0027 -0.0236 1096 LEU B C   
17153 O O   . LEU B 1098 ? 0.2085 0.1997 0.2162 0.0312  -0.0025 -0.0242 1096 LEU B O   
17154 C CB  . LEU B 1098 ? 0.1732 0.1713 0.1848 0.0291  -0.0021 -0.0215 1096 LEU B CB  
17155 C CG  . LEU B 1098 ? 0.1779 0.1805 0.1912 0.0280  -0.0017 -0.0205 1096 LEU B CG  
17156 C CD1 . LEU B 1098 ? 0.1906 0.1935 0.2041 0.0291  -0.0019 -0.0194 1096 LEU B CD1 
17157 C CD2 . LEU B 1098 ? 0.1933 0.1957 0.2072 0.0255  -0.0018 -0.0202 1096 LEU B CD2 
17158 N N   . HIS B 1099 ? 0.2000 0.1892 0.2087 0.0270  -0.0034 -0.0236 1097 HIS B N   
17159 C CA  . HIS B 1099 ? 0.2108 0.1949 0.2176 0.0272  -0.0042 -0.0245 1097 HIS B CA  
17160 C C   . HIS B 1099 ? 0.2034 0.1842 0.2105 0.0261  -0.0048 -0.0234 1097 HIS B C   
17161 O O   . HIS B 1099 ? 0.1977 0.1804 0.2065 0.0251  -0.0045 -0.0221 1097 HIS B O   
17162 C CB  . HIS B 1099 ? 0.2213 0.2048 0.2276 0.0254  -0.0047 -0.0253 1097 HIS B CB  
17163 C CG  . HIS B 1099 ? 0.2432 0.2299 0.2490 0.0261  -0.0040 -0.0262 1097 HIS B CG  
17164 N ND1 . HIS B 1099 ? 0.2991 0.2840 0.3024 0.0273  -0.0040 -0.0277 1097 HIS B ND1 
17165 C CD2 . HIS B 1099 ? 0.2942 0.2856 0.3014 0.0256  -0.0033 -0.0258 1097 HIS B CD2 
17166 C CE1 . HIS B 1099 ? 0.3214 0.3101 0.3247 0.0275  -0.0033 -0.0281 1097 HIS B CE1 
17167 N NE2 . HIS B 1099 ? 0.3114 0.3039 0.3171 0.0264  -0.0029 -0.0269 1097 HIS B NE2 
17168 N N   . ALA B 1100 ? 0.2147 0.1903 0.2200 0.0262  -0.0056 -0.0240 1098 ALA B N   
17169 C CA  . ALA B 1100 ? 0.2337 0.2060 0.2394 0.0247  -0.0063 -0.0230 1098 ALA B CA  
17170 C C   . ALA B 1100 ? 0.2197 0.1937 0.2274 0.0218  -0.0065 -0.0224 1098 ALA B C   
17171 O O   . ALA B 1100 ? 0.2445 0.2204 0.2527 0.0210  -0.0066 -0.0231 1098 ALA B O   
17172 C CB  . ALA B 1100 ? 0.2509 0.2171 0.2541 0.0249  -0.0073 -0.0239 1098 ALA B CB  
17173 N N   . ARG B 1101 ? 0.2154 0.1891 0.2245 0.0205  -0.0064 -0.0209 1099 ARG B N   
17174 C CA  . ARG B 1101 ? 0.2104 0.1854 0.2217 0.0179  -0.0066 -0.0203 1099 ARG B CA  
17175 C C   . ARG B 1101 ? 0.2222 0.1938 0.2330 0.0164  -0.0078 -0.0210 1099 ARG B C   
17176 O O   . ARG B 1101 ? 0.2325 0.2058 0.2447 0.0148  -0.0082 -0.0212 1099 ARG B O   
17177 C CB  . ARG B 1101 ? 0.2539 0.2292 0.2666 0.0169  -0.0060 -0.0185 1099 ARG B CB  
17178 C CG  . ARG B 1101 ? 0.2523 0.2320 0.2660 0.0174  -0.0049 -0.0177 1099 ARG B CG  
17179 C CD  . ARG B 1101 ? 0.2631 0.2463 0.2790 0.0158  -0.0045 -0.0176 1099 ARG B CD  
17180 N NE  . ARG B 1101 ? 0.2830 0.2699 0.2995 0.0162  -0.0035 -0.0169 1099 ARG B NE  
17181 C CZ  . ARG B 1101 ? 0.2560 0.2452 0.2742 0.0149  -0.0028 -0.0162 1099 ARG B CZ  
17182 N NH1 . ARG B 1101 ? 0.2470 0.2360 0.2669 0.0131  -0.0029 -0.0159 1099 ARG B NH1 
17183 N NH2 . ARG B 1101 ? 0.2951 0.2870 0.3133 0.0153  -0.0020 -0.0158 1099 ARG B NH2 
17184 N N   . GLY B 1102 ? 0.2234 0.1899 0.2321 0.0168  -0.0086 -0.0213 1100 GLY B N   
17185 C CA  . GLY B 1102 ? 0.2484 0.2112 0.2566 0.0150  -0.0100 -0.0219 1100 GLY B CA  
17186 C C   . GLY B 1102 ? 0.2474 0.2056 0.2549 0.0142  -0.0105 -0.0209 1100 GLY B C   
17187 O O   . GLY B 1102 ? 0.2643 0.2192 0.2696 0.0160  -0.0104 -0.0209 1100 GLY B O   
17188 N N   . ARG B 1103 ? 0.2403 0.1979 0.2497 0.0114  -0.0111 -0.0200 1101 ARG B N   
17189 C CA  . ARG B 1103 ? 0.2575 0.2108 0.2664 0.0102  -0.0116 -0.0189 1101 ARG B CA  
17190 C C   . ARG B 1103 ? 0.2251 0.1815 0.2365 0.0093  -0.0103 -0.0169 1101 ARG B C   
17191 O O   . ARG B 1103 ? 0.2526 0.2134 0.2669 0.0079  -0.0098 -0.0162 1101 ARG B O   
17192 C CB  . ARG B 1103 ? 0.2724 0.2228 0.2817 0.0075  -0.0132 -0.0192 1101 ARG B CB  
17193 C CG  . ARG B 1103 ? 0.2958 0.2411 0.3043 0.0061  -0.0138 -0.0180 1101 ARG B CG  
17194 C CD  . ARG B 1103 ? 0.3518 0.2929 0.3597 0.0037  -0.0157 -0.0186 1101 ARG B CD  
17195 N NE  . ARG B 1103 ? 0.4226 0.3585 0.4264 0.0053  -0.0168 -0.0206 1101 ARG B NE  
17196 C CZ  . ARG B 1103 ? 0.4988 0.4343 0.5014 0.0053  -0.0179 -0.0224 1101 ARG B CZ  
17197 N NH1 . ARG B 1103 ? 0.5893 0.5294 0.5948 0.0035  -0.0183 -0.0224 1101 ARG B NH1 
17198 N NH2 . ARG B 1103 ? 0.4947 0.4252 0.4932 0.0070  -0.0187 -0.0242 1101 ARG B NH2 
17199 N N   . ILE B 1104 ? 0.2184 0.1724 0.2284 0.0103  -0.0099 -0.0158 1102 ILE B N   
17200 C CA  . ILE B 1104 ? 0.2267 0.1832 0.2383 0.0097  -0.0086 -0.0139 1102 ILE B CA  
17201 C C   . ILE B 1104 ? 0.2331 0.1860 0.2449 0.0073  -0.0091 -0.0124 1102 ILE B C   
17202 O O   . ILE B 1104 ? 0.2485 0.1957 0.2579 0.0074  -0.0101 -0.0126 1102 ILE B O   
17203 C CB  . ILE B 1104 ? 0.2237 0.1802 0.2334 0.0124  -0.0079 -0.0135 1102 ILE B CB  
17204 C CG1 . ILE B 1104 ? 0.2384 0.1982 0.2478 0.0148  -0.0076 -0.0150 1102 ILE B CG1 
17205 C CG2 . ILE B 1104 ? 0.2284 0.1875 0.2393 0.0118  -0.0066 -0.0116 1102 ILE B CG2 
17206 C CD1 . ILE B 1104 ? 0.2288 0.1944 0.2407 0.0140  -0.0068 -0.0152 1102 ILE B CD1 
17207 N N   . LEU B 1105 ? 0.2115 0.1677 0.2262 0.0052  -0.0082 -0.0110 1103 LEU B N   
17208 C CA  . LEU B 1105 ? 0.2232 0.1767 0.2385 0.0028  -0.0083 -0.0093 1103 LEU B CA  
17209 C C   . LEU B 1105 ? 0.2325 0.1841 0.2458 0.0039  -0.0074 -0.0077 1103 LEU B C   
17210 O O   . LEU B 1105 ? 0.2247 0.1800 0.2383 0.0051  -0.0061 -0.0072 1103 LEU B O   
17211 C CB  . LEU B 1105 ? 0.2347 0.1931 0.2540 0.0004  -0.0074 -0.0082 1103 LEU B CB  
17212 C CG  . LEU B 1105 ? 0.2252 0.1823 0.2457 -0.0023 -0.0070 -0.0061 1103 LEU B CG  
17213 C CD1 . LEU B 1105 ? 0.2370 0.1890 0.2569 -0.0043 -0.0088 -0.0063 1103 LEU B CD1 
17214 C CD2 . LEU B 1105 ? 0.2332 0.1963 0.2578 -0.0040 -0.0057 -0.0053 1103 LEU B CD2 
17215 N N   . LEU B 1106 ? 0.2259 0.1715 0.2367 0.0036  -0.0083 -0.0071 1104 LEU B N   
17216 C CA  . LEU B 1106 ? 0.2257 0.1688 0.2344 0.0046  -0.0077 -0.0055 1104 LEU B CA  
17217 C C   . LEU B 1106 ? 0.2385 0.1803 0.2482 0.0015  -0.0072 -0.0033 1104 LEU B C   
17218 O O   . LEU B 1106 ? 0.2582 0.1965 0.2682 -0.0008 -0.0083 -0.0032 1104 LEU B O   
17219 C CB  . LEU B 1106 ? 0.2476 0.1845 0.2525 0.0068  -0.0089 -0.0062 1104 LEU B CB  
17220 C CG  . LEU B 1106 ? 0.3411 0.2793 0.3444 0.0105  -0.0087 -0.0074 1104 LEU B CG  
17221 C CD1 . LEU B 1106 ? 0.3242 0.2683 0.3296 0.0112  -0.0082 -0.0090 1104 LEU B CD1 
17222 C CD2 . LEU B 1106 ? 0.2448 0.1767 0.2447 0.0126  -0.0100 -0.0085 1104 LEU B CD2 
17223 N N   . VAL B 1107 ? 0.2257 0.1702 0.2358 0.0014  -0.0057 -0.0016 1105 VAL B N   
17224 C CA  . VAL B 1107 ? 0.2177 0.1613 0.2286 -0.0014 -0.0049 0.0007  1105 VAL B CA  
17225 C C   . VAL B 1107 ? 0.2399 0.1801 0.2474 -0.0001 -0.0046 0.0024  1105 VAL B C   
17226 O O   . VAL B 1107 ? 0.2521 0.1956 0.2595 0.0005  -0.0031 0.0035  1105 VAL B O   
17227 C CB  . VAL B 1107 ? 0.2339 0.1840 0.2484 -0.0030 -0.0032 0.0014  1105 VAL B CB  
17228 C CG1 . VAL B 1107 ? 0.2517 0.2011 0.2674 -0.0062 -0.0024 0.0038  1105 VAL B CG1 
17229 C CG2 . VAL B 1107 ? 0.2355 0.1893 0.2532 -0.0035 -0.0038 -0.0004 1105 VAL B CG2 
17230 N N   . PRO B 1108 ? 0.2399 0.1734 0.2442 0.0006  -0.0059 0.0025  1106 PRO B N   
17231 C CA  . PRO B 1108 ? 0.2564 0.1864 0.2574 0.0021  -0.0057 0.0041  1106 PRO B CA  
17232 C C   . PRO B 1108 ? 0.2790 0.2069 0.2798 -0.0009 -0.0050 0.0068  1106 PRO B C   
17233 O O   . PRO B 1108 ? 0.3352 0.2631 0.3381 -0.0041 -0.0049 0.0073  1106 PRO B O   
17234 C CB  . PRO B 1108 ? 0.2750 0.1983 0.2729 0.0039  -0.0076 0.0030  1106 PRO B CB  
17235 C CG  . PRO B 1108 ? 0.2710 0.1923 0.2705 0.0014  -0.0086 0.0020  1106 PRO B CG  
17236 C CD  . PRO B 1108 ? 0.2613 0.1899 0.2648 0.0004  -0.0078 0.0010  1106 PRO B CD  
17237 N N   . ALA B 1109 ? 0.2776 0.2037 0.2755 0.0003  -0.0045 0.0086  1107 ALA B N   
17238 C CA  . ALA B 1109 ? 0.2892 0.2119 0.2858 -0.0021 -0.0039 0.0113  1107 ALA B CA  
17239 C C   . ALA B 1109 ? 0.3487 0.2633 0.3411 -0.0010 -0.0054 0.0122  1107 ALA B C   
17240 O O   . ALA B 1109 ? 0.3475 0.2570 0.3388 -0.0035 -0.0058 0.0137  1107 ALA B O   
17241 C CB  . ALA B 1109 ? 0.3007 0.2277 0.2970 -0.0021 -0.0020 0.0131  1107 ALA B CB  
17242 N N   . THR B 1110 ? 0.2934 0.2065 0.2833 0.0028  -0.0063 0.0112  1108 THR B N   
17243 C CA  . THR B 1110 ? 0.3116 0.2173 0.2974 0.0046  -0.0076 0.0120  1108 THR B CA  
17244 C C   . THR B 1110 ? 0.3102 0.2131 0.2952 0.0074  -0.0092 0.0095  1108 THR B C   
17245 O O   . THR B 1110 ? 0.2981 0.2057 0.2853 0.0087  -0.0091 0.0072  1108 THR B O   
17246 C CB  . THR B 1110 ? 0.3192 0.2256 0.3025 0.0069  -0.0071 0.0136  1108 THR B CB  
17247 O OG1 . THR B 1110 ? 0.3117 0.2237 0.2961 0.0100  -0.0070 0.0119  1108 THR B OG1 
17248 C CG2 . THR B 1110 ? 0.3459 0.2551 0.3295 0.0043  -0.0054 0.0161  1108 THR B CG2 
17249 N N   . GLU B 1111 ? 0.3201 0.2152 0.3016 0.0086  -0.0106 0.0099  1109 GLU B N   
17250 C CA  . GLU B 1111 ? 0.3187 0.2105 0.2989 0.0117  -0.0120 0.0075  1109 GLU B CA  
17251 C C   . GLU B 1111 ? 0.3167 0.2138 0.2974 0.0157  -0.0117 0.0063  1109 GLU B C   
17252 O O   . GLU B 1111 ? 0.3073 0.2073 0.2894 0.0172  -0.0119 0.0038  1109 GLU B O   
17253 C CB  . GLU B 1111 ? 0.3328 0.2151 0.3087 0.0127  -0.0135 0.0085  1109 GLU B CB  
17254 C CG  . GLU B 1111 ? 0.3722 0.2508 0.3462 0.0165  -0.0148 0.0062  1109 GLU B CG  
17255 C CD  . GLU B 1111 ? 0.4063 0.2747 0.3760 0.0173  -0.0162 0.0070  1109 GLU B CD  
17256 O OE1 . GLU B 1111 ? 0.4241 0.2868 0.3929 0.0147  -0.0171 0.0066  1109 GLU B OE1 
17257 O OE2 . GLU B 1111 ? 0.4625 0.3284 0.4297 0.0205  -0.0166 0.0081  1109 GLU B OE2 
17258 N N   . SER B 1112 ? 0.3140 0.2125 0.2934 0.0173  -0.0112 0.0081  1110 SER B N   
17259 C CA  . SER B 1112 ? 0.3226 0.2264 0.3026 0.0208  -0.0110 0.0071  1110 SER B CA  
17260 C C   . SER B 1112 ? 0.3174 0.2295 0.3012 0.0199  -0.0099 0.0057  1110 SER B C   
17261 O O   . SER B 1112 ? 0.3031 0.2188 0.2881 0.0222  -0.0100 0.0036  1110 SER B O   
17262 C CB  . SER B 1112 ? 0.3364 0.2404 0.3143 0.0222  -0.0109 0.0095  1110 SER B CB  
17263 O OG  . SER B 1112 ? 0.3579 0.2672 0.3366 0.0255  -0.0109 0.0086  1110 SER B OG  
17264 N N   . GLY B 1113 ? 0.2972 0.2123 0.2828 0.0164  -0.0087 0.0067  1111 GLY B N   
17265 C CA  . GLY B 1113 ? 0.2631 0.1854 0.2521 0.0155  -0.0076 0.0053  1111 GLY B CA  
17266 C C   . GLY B 1113 ? 0.2684 0.1909 0.2591 0.0155  -0.0082 0.0027  1111 GLY B C   
17267 O O   . GLY B 1113 ? 0.2678 0.1954 0.2603 0.0169  -0.0079 0.0010  1111 GLY B O   
17268 N N   . LEU B 1114 ? 0.2602 0.1771 0.2501 0.0139  -0.0091 0.0025  1112 LEU B N   
17269 C CA  . LEU B 1114 ? 0.2424 0.1588 0.2334 0.0140  -0.0099 0.0000  1112 LEU B CA  
17270 C C   . LEU B 1114 ? 0.2780 0.1939 0.2675 0.0180  -0.0106 -0.0018 1112 LEU B C   
17271 O O   . LEU B 1114 ? 0.2551 0.1747 0.2463 0.0189  -0.0105 -0.0039 1112 LEU B O   
17272 C CB  . LEU B 1114 ? 0.2924 0.2019 0.2822 0.0116  -0.0111 0.0002  1112 LEU B CB  
17273 C CG  . LEU B 1114 ? 0.3059 0.2132 0.2956 0.0117  -0.0122 -0.0024 1112 LEU B CG  
17274 C CD1 . LEU B 1114 ? 0.2742 0.1885 0.2676 0.0104  -0.0116 -0.0038 1112 LEU B CD1 
17275 C CD2 . LEU B 1114 ? 0.3205 0.2203 0.3085 0.0091  -0.0135 -0.0020 1112 LEU B CD2 
17276 N N   . TYR B 1115 ? 0.2814 0.1929 0.2680 0.0206  -0.0112 -0.0010 1113 TYR B N   
17277 C CA  . TYR B 1115 ? 0.2682 0.1797 0.2537 0.0247  -0.0117 -0.0027 1113 TYR B CA  
17278 C C   . TYR B 1115 ? 0.2763 0.1959 0.2641 0.0263  -0.0108 -0.0033 1113 TYR B C   
17279 O O   . TYR B 1115 ? 0.2744 0.1967 0.2631 0.0284  -0.0108 -0.0054 1113 TYR B O   
17280 C CB  . TYR B 1115 ? 0.2898 0.1956 0.2720 0.0274  -0.0126 -0.0014 1113 TYR B CB  
17281 C CG  . TYR B 1115 ? 0.3001 0.1967 0.2793 0.0265  -0.0137 -0.0011 1113 TYR B CG  
17282 C CD1 . TYR B 1115 ? 0.3040 0.1978 0.2835 0.0239  -0.0142 -0.0024 1113 TYR B CD1 
17283 C CD2 . TYR B 1115 ? 0.3441 0.2346 0.3201 0.0282  -0.0145 0.0006  1113 TYR B CD2 
17284 C CE1 . TYR B 1115 ? 0.3612 0.2462 0.3377 0.0229  -0.0154 -0.0022 1113 TYR B CE1 
17285 C CE2 . TYR B 1115 ? 0.3655 0.2471 0.3385 0.0273  -0.0157 0.0009  1113 TYR B CE2 
17286 C CZ  . TYR B 1115 ? 0.3816 0.2604 0.3548 0.0246  -0.0161 -0.0005 1113 TYR B CZ  
17287 O OH  . TYR B 1115 ? 0.4339 0.3035 0.4041 0.0235  -0.0174 -0.0003 1113 TYR B OH  
17288 N N   . HIS B 1116 ? 0.2576 0.1814 0.2465 0.0254  -0.0099 -0.0016 1114 HIS B N   
17289 C CA  . HIS B 1116 ? 0.2540 0.1853 0.2449 0.0265  -0.0091 -0.0021 1114 HIS B CA  
17290 C C   . HIS B 1116 ? 0.2697 0.2056 0.2635 0.0246  -0.0084 -0.0038 1114 HIS B C   
17291 O O   . HIS B 1116 ? 0.2762 0.2168 0.2714 0.0262  -0.0081 -0.0053 1114 HIS B O   
17292 C CB  . HIS B 1116 ? 0.2606 0.1946 0.2514 0.0256  -0.0084 0.0001  1114 HIS B CB  
17293 C CG  . HIS B 1116 ? 0.3101 0.2420 0.2985 0.0283  -0.0090 0.0015  1114 HIS B CG  
17294 N ND1 . HIS B 1116 ? 0.3377 0.2631 0.3233 0.0282  -0.0097 0.0033  1114 HIS B ND1 
17295 C CD2 . HIS B 1116 ? 0.3229 0.2585 0.3113 0.0311  -0.0093 0.0015  1114 HIS B CD2 
17296 C CE1 . HIS B 1116 ? 0.3610 0.2860 0.3449 0.0311  -0.0104 0.0043  1114 HIS B CE1 
17297 N NE2 . HIS B 1116 ? 0.3630 0.2943 0.3487 0.0328  -0.0101 0.0033  1114 HIS B NE2 
17298 N N   . GLN B 1117 ? 0.2426 0.1775 0.2375 0.0213  -0.0082 -0.0034 1115 GLN B N   
17299 C CA  . GLN B 1117 ? 0.2237 0.1627 0.2213 0.0196  -0.0077 -0.0050 1115 GLN B CA  
17300 C C   . GLN B 1117 ? 0.2441 0.1815 0.2412 0.0211  -0.0085 -0.0073 1115 GLN B C   
17301 O O   . GLN B 1117 ? 0.2335 0.1754 0.2323 0.0217  -0.0082 -0.0089 1115 GLN B O   
17302 C CB  . GLN B 1117 ? 0.2308 0.1686 0.2296 0.0158  -0.0075 -0.0041 1115 GLN B CB  
17303 C CG  . GLN B 1117 ? 0.2253 0.1659 0.2250 0.0141  -0.0062 -0.0020 1115 GLN B CG  
17304 C CD  . GLN B 1117 ? 0.2394 0.1791 0.2407 0.0105  -0.0059 -0.0010 1115 GLN B CD  
17305 O OE1 . GLN B 1117 ? 0.2629 0.1988 0.2641 0.0091  -0.0069 -0.0016 1115 GLN B OE1 
17306 N NE2 . GLN B 1117 ? 0.2485 0.1917 0.2510 0.0088  -0.0045 0.0005  1115 GLN B NE2 
17307 N N   . LEU B 1118 ? 0.2480 0.1786 0.2427 0.0217  -0.0096 -0.0076 1116 LEU B N   
17308 C CA  . LEU B 1118 ? 0.2437 0.1721 0.2373 0.0234  -0.0104 -0.0099 1116 LEU B CA  
17309 C C   . LEU B 1118 ? 0.2476 0.1796 0.2411 0.0271  -0.0100 -0.0109 1116 LEU B C   
17310 O O   . LEU B 1118 ? 0.2602 0.1948 0.2545 0.0279  -0.0099 -0.0128 1116 LEU B O   
17311 C CB  . LEU B 1118 ? 0.2721 0.1920 0.2625 0.0237  -0.0116 -0.0099 1116 LEU B CB  
17312 C CG  . LEU B 1118 ? 0.3439 0.2599 0.3344 0.0200  -0.0123 -0.0096 1116 LEU B CG  
17313 C CD1 . LEU B 1118 ? 0.3387 0.2459 0.3256 0.0204  -0.0135 -0.0091 1116 LEU B CD1 
17314 C CD2 . LEU B 1118 ? 0.3311 0.2486 0.3227 0.0190  -0.0127 -0.0118 1116 LEU B CD2 
17315 N N   . ALA B 1119 ? 0.2659 0.1980 0.2585 0.0292  -0.0099 -0.0096 1117 ALA B N   
17316 C CA  . ALA B 1119 ? 0.2542 0.1903 0.2472 0.0326  -0.0096 -0.0104 1117 ALA B CA  
17317 C C   . ALA B 1119 ? 0.2419 0.1856 0.2378 0.0319  -0.0087 -0.0112 1117 ALA B C   
17318 O O   . ALA B 1119 ? 0.2603 0.2067 0.2567 0.0335  -0.0084 -0.0129 1117 ALA B O   
17319 C CB  . ALA B 1119 ? 0.2730 0.2087 0.2650 0.0346  -0.0098 -0.0086 1117 ALA B CB  
17320 N N   . ALA B 1120 ? 0.2195 0.1665 0.2170 0.0293  -0.0080 -0.0099 1118 ALA B N   
17321 C CA  . ALA B 1120 ? 0.2102 0.1639 0.2101 0.0286  -0.0072 -0.0105 1118 ALA B CA  
17322 C C   . ALA B 1120 ? 0.2299 0.1844 0.2309 0.0275  -0.0072 -0.0124 1118 ALA B C   
17323 O O   . ALA B 1120 ? 0.2336 0.1922 0.2356 0.0285  -0.0068 -0.0137 1118 ALA B O   
17324 C CB  . ALA B 1120 ? 0.2339 0.1902 0.2350 0.0261  -0.0065 -0.0089 1118 ALA B CB  
17325 N N   . ALA B 1121 ? 0.2147 0.1651 0.2153 0.0253  -0.0077 -0.0125 1119 ALA B N   
17326 C CA  . ALA B 1121 ? 0.2152 0.1661 0.2166 0.0240  -0.0079 -0.0142 1119 ALA B CA  
17327 C C   . ALA B 1121 ? 0.2078 0.1568 0.2074 0.0265  -0.0084 -0.0161 1119 ALA B C   
17328 O O   . ALA B 1121 ? 0.2126 0.1648 0.2131 0.0267  -0.0081 -0.0176 1119 ALA B O   
17329 C CB  . ALA B 1121 ? 0.2341 0.1814 0.2357 0.0210  -0.0085 -0.0137 1119 ALA B CB  
17330 N N   . LEU B 1122 ? 0.2234 0.1669 0.2204 0.0284  -0.0090 -0.0162 1120 LEU B N   
17331 C CA  . LEU B 1122 ? 0.2174 0.1588 0.2125 0.0310  -0.0093 -0.0181 1120 LEU B CA  
17332 C C   . LEU B 1122 ? 0.2277 0.1746 0.2238 0.0337  -0.0084 -0.0187 1120 LEU B C   
17333 O O   . LEU B 1122 ? 0.2346 0.1830 0.2304 0.0349  -0.0082 -0.0205 1120 LEU B O   
17334 C CB  . LEU B 1122 ? 0.2376 0.1716 0.2296 0.0327  -0.0102 -0.0180 1120 LEU B CB  
17335 C CG  . LEU B 1122 ? 0.2892 0.2169 0.2799 0.0298  -0.0113 -0.0177 1120 LEU B CG  
17336 C CD1 . LEU B 1122 ? 0.2827 0.2030 0.2702 0.0316  -0.0121 -0.0172 1120 LEU B CD1 
17337 C CD2 . LEU B 1122 ? 0.2886 0.2150 0.2788 0.0283  -0.0118 -0.0196 1120 LEU B CD2 
17338 N N   . ALA B 1123 ? 0.2079 0.1580 0.2051 0.0347  -0.0080 -0.0172 1121 ALA B N   
17339 C CA  . ALA B 1123 ? 0.2206 0.1762 0.2190 0.0372  -0.0073 -0.0176 1121 ALA B CA  
17340 C C   . ALA B 1123 ? 0.2599 0.2212 0.2603 0.0359  -0.0066 -0.0185 1121 ALA B C   
17341 O O   . ALA B 1123 ? 0.2338 0.1992 0.2349 0.0378  -0.0060 -0.0194 1121 ALA B O   
17342 C CB  . ALA B 1123 ? 0.2175 0.1756 0.2168 0.0379  -0.0072 -0.0156 1121 ALA B CB  
17343 N N   . THR B 1124 ? 0.2064 0.1684 0.2079 0.0327  -0.0066 -0.0182 1122 THR B N   
17344 C CA  . THR B 1124 ? 0.1883 0.1552 0.1917 0.0313  -0.0060 -0.0189 1122 THR B CA  
17345 C C   . THR B 1124 ? 0.1807 0.1453 0.1832 0.0303  -0.0064 -0.0205 1122 THR B C   
17346 O O   . THR B 1124 ? 0.2139 0.1816 0.2178 0.0286  -0.0062 -0.0210 1122 THR B O   
17347 C CB  . THR B 1124 ? 0.2185 0.1883 0.2238 0.0288  -0.0056 -0.0175 1122 THR B CB  
17348 O OG1 . THR B 1124 ? 0.2104 0.1759 0.2152 0.0269  -0.0061 -0.0165 1122 THR B OG1 
17349 C CG2 . THR B 1124 ? 0.2030 0.1764 0.2090 0.0300  -0.0052 -0.0163 1122 THR B CG2 
17350 N N   . GLY B 1125 ? 0.2106 0.1697 0.2106 0.0314  -0.0071 -0.0214 1123 GLY B N   
17351 C CA  . GLY B 1125 ? 0.2136 0.1704 0.2122 0.0309  -0.0076 -0.0232 1123 GLY B CA  
17352 C C   . GLY B 1125 ? 0.2114 0.1650 0.2100 0.0278  -0.0085 -0.0231 1123 GLY B C   
17353 O O   . GLY B 1125 ? 0.2238 0.1758 0.2213 0.0270  -0.0091 -0.0246 1123 GLY B O   
17354 N N   . ASN B 1126 ? 0.2225 0.1755 0.2224 0.0259  -0.0087 -0.0214 1124 ASN B N   
17355 C CA  . ASN B 1126 ? 0.2057 0.1572 0.2066 0.0226  -0.0094 -0.0211 1124 ASN B CA  
17356 C C   . ASN B 1126 ? 0.2180 0.1624 0.2165 0.0219  -0.0106 -0.0213 1124 ASN B C   
17357 O O   . ASN B 1126 ? 0.2359 0.1761 0.2323 0.0238  -0.0109 -0.0212 1124 ASN B O   
17358 C CB  . ASN B 1126 ? 0.1948 0.1494 0.1983 0.0207  -0.0088 -0.0191 1124 ASN B CB  
17359 C CG  . ASN B 1126 ? 0.2048 0.1660 0.2104 0.0211  -0.0077 -0.0189 1124 ASN B CG  
17360 O OD1 . ASN B 1126 ? 0.2245 0.1886 0.2313 0.0202  -0.0076 -0.0197 1124 ASN B OD1 
17361 N ND2 . ASN B 1126 ? 0.2113 0.1746 0.2172 0.0225  -0.0069 -0.0179 1124 ASN B ND2 
17362 N N   . SER B 1127 ? 0.2379 0.1809 0.2370 0.0192  -0.0116 -0.0216 1125 SER B N   
17363 C CA  . SER B 1127 ? 0.2427 0.1795 0.2405 0.0174  -0.0128 -0.0212 1125 SER B CA  
17364 C C   . SER B 1127 ? 0.2429 0.1814 0.2434 0.0149  -0.0124 -0.0189 1125 SER B C   
17365 O O   . SER B 1127 ? 0.2296 0.1738 0.2328 0.0146  -0.0113 -0.0180 1125 SER B O   
17366 C CB  . SER B 1127 ? 0.2473 0.1819 0.2443 0.0155  -0.0142 -0.0227 1125 SER B CB  
17367 O OG  . SER B 1127 ? 0.3090 0.2489 0.3092 0.0134  -0.0141 -0.0224 1125 SER B OG  
17368 N N   . VAL B 1128 ? 0.2519 0.1853 0.2516 0.0131  -0.0133 -0.0181 1126 VAL B N   
17369 C CA  . VAL B 1128 ? 0.2291 0.1636 0.2310 0.0108  -0.0128 -0.0158 1126 VAL B CA  
17370 C C   . VAL B 1128 ? 0.2645 0.1957 0.2670 0.0073  -0.0141 -0.0154 1126 VAL B C   
17371 O O   . VAL B 1128 ? 0.2909 0.2166 0.2910 0.0070  -0.0155 -0.0166 1126 VAL B O   
17372 C CB  . VAL B 1128 ? 0.2537 0.1857 0.2540 0.0122  -0.0122 -0.0142 1126 VAL B CB  
17373 C CG1 . VAL B 1128 ? 0.2370 0.1731 0.2373 0.0155  -0.0111 -0.0144 1126 VAL B CG1 
17374 C CG2 . VAL B 1128 ? 0.2703 0.1941 0.2669 0.0130  -0.0135 -0.0147 1126 VAL B CG2 
17375 N N   . ALA B 1129 ? 0.2410 0.1758 0.2469 0.0047  -0.0134 -0.0137 1127 ALA B N   
17376 C CA  . ALA B 1129 ? 0.2597 0.1917 0.2667 0.0012  -0.0143 -0.0126 1127 ALA B CA  
17377 C C   . ALA B 1129 ? 0.2314 0.1632 0.2388 0.0005  -0.0132 -0.0101 1127 ALA B C   
17378 O O   . ALA B 1129 ? 0.2383 0.1756 0.2480 0.0007  -0.0116 -0.0090 1127 ALA B O   
17379 C CB  . ALA B 1129 ? 0.2865 0.2236 0.2974 -0.0014 -0.0145 -0.0126 1127 ALA B CB  
17380 N N   . ILE B 1130 ? 0.2413 0.1667 0.2464 -0.0003 -0.0139 -0.0092 1128 ILE B N   
17381 C CA  . ILE B 1130 ? 0.2326 0.1569 0.2373 -0.0008 -0.0129 -0.0068 1128 ILE B CA  
17382 C C   . ILE B 1130 ? 0.2565 0.1811 0.2639 -0.0050 -0.0130 -0.0051 1128 ILE B C   
17383 O O   . ILE B 1130 ? 0.2517 0.1730 0.2592 -0.0073 -0.0146 -0.0056 1128 ILE B O   
17384 C CB  . ILE B 1130 ? 0.2528 0.1695 0.2531 0.0010  -0.0137 -0.0067 1128 ILE B CB  
17385 C CG1 . ILE B 1130 ? 0.2975 0.2139 0.2954 0.0052  -0.0138 -0.0086 1128 ILE B CG1 
17386 C CG2 . ILE B 1130 ? 0.2727 0.1888 0.2725 0.0008  -0.0126 -0.0041 1128 ILE B CG2 
17387 C CD1 . ILE B 1130 ? 0.2899 0.1982 0.2834 0.0071  -0.0149 -0.0090 1128 ILE B CD1 
17388 N N   . ASP B 1131 ? 0.2505 0.1793 0.2601 -0.0059 -0.0113 -0.0031 1129 ASP B N   
17389 C CA  . ASP B 1131 ? 0.2468 0.1769 0.2593 -0.0098 -0.0109 -0.0012 1129 ASP B CA  
17390 C C   . ASP B 1131 ? 0.2634 0.1859 0.2735 -0.0117 -0.0121 -0.0001 1129 ASP B C   
17391 O O   . ASP B 1131 ? 0.2623 0.1807 0.2693 -0.0107 -0.0118 0.0012  1129 ASP B O   
17392 C CB  . ASP B 1131 ? 0.2460 0.1811 0.2602 -0.0098 -0.0086 0.0008  1129 ASP B CB  
17393 C CG  . ASP B 1131 ? 0.2674 0.2040 0.2845 -0.0136 -0.0078 0.0030  1129 ASP B CG  
17394 O OD1 . ASP B 1131 ? 0.2882 0.2253 0.3079 -0.0162 -0.0089 0.0026  1129 ASP B OD1 
17395 O OD2 . ASP B 1131 ? 0.2800 0.2174 0.2967 -0.0139 -0.0062 0.0050  1129 ASP B OD2 
17396 N N   . ALA B 1132 ? 0.2800 0.2004 0.2913 -0.0148 -0.0137 -0.0004 1130 ALA B N   
17397 C CA  . ALA B 1132 ? 0.2830 0.1957 0.2919 -0.0170 -0.0151 0.0006  1130 ALA B CA  
17398 C C   . ALA B 1132 ? 0.3050 0.2179 0.3148 -0.0194 -0.0136 0.0037  1130 ALA B C   
17399 O O   . ALA B 1132 ? 0.3117 0.2177 0.3184 -0.0201 -0.0142 0.0049  1130 ALA B O   
17400 C CB  . ALA B 1132 ? 0.2892 0.2000 0.2994 -0.0200 -0.0172 -0.0005 1130 ALA B CB  
17401 N N   . ALA B 1133 ? 0.2831 0.2036 0.2970 -0.0204 -0.0117 0.0049  1131 ALA B N   
17402 C CA  . ALA B 1133 ? 0.3320 0.2533 0.3469 -0.0226 -0.0101 0.0079  1131 ALA B CA  
17403 C C   . ALA B 1133 ? 0.3558 0.2739 0.3665 -0.0201 -0.0091 0.0091  1131 ALA B C   
17404 O O   . ALA B 1133 ? 0.3576 0.2746 0.3678 -0.0218 -0.0079 0.0117  1131 ALA B O   
17405 C CB  . ALA B 1133 ? 0.3130 0.2432 0.3330 -0.0240 -0.0080 0.0088  1131 ALA B CB  
17406 N N   . SER B 1134 ? 0.2869 0.2038 0.2948 -0.0160 -0.0094 0.0074  1132 SER B N   
17407 C CA  . SER B 1134 ? 0.2963 0.2097 0.3001 -0.0135 -0.0089 0.0084  1132 SER B CA  
17408 C C   . SER B 1134 ? 0.2711 0.1753 0.2710 -0.0145 -0.0103 0.0096  1132 SER B C   
17409 O O   . SER B 1134 ? 0.3228 0.2241 0.3199 -0.0136 -0.0097 0.0114  1132 SER B O   
17410 C CB  . SER B 1134 ? 0.2899 0.2039 0.2918 -0.0090 -0.0093 0.0062  1132 SER B CB  
17411 O OG  . SER B 1134 ? 0.3076 0.2164 0.3075 -0.0081 -0.0113 0.0041  1132 SER B OG  
17412 N N   . GLY B 1135 ? 0.3025 0.2020 0.3022 -0.0163 -0.0122 0.0085  1133 GLY B N   
17413 C CA  . GLY B 1135 ? 0.3475 0.2376 0.3432 -0.0173 -0.0137 0.0095  1133 GLY B CA  
17414 C C   . GLY B 1135 ? 0.3726 0.2566 0.3634 -0.0130 -0.0147 0.0083  1133 GLY B C   
17415 O O   . GLY B 1135 ? 0.3845 0.2606 0.3716 -0.0132 -0.0156 0.0095  1133 GLY B O   
17416 N N   . LEU B 1136 ? 0.3336 0.2211 0.3244 -0.0093 -0.0145 0.0061  1134 LEU B N   
17417 C CA  . LEU B 1136 ? 0.3235 0.2069 0.3103 -0.0048 -0.0151 0.0051  1134 LEU B CA  
17418 C C   . LEU B 1136 ? 0.3818 0.2598 0.3663 -0.0032 -0.0170 0.0024  1134 LEU B C   
17419 O O   . LEU B 1136 ? 0.3554 0.2319 0.3375 0.0009  -0.0172 0.0010  1134 LEU B O   
17420 C CB  . LEU B 1136 ? 0.2962 0.1870 0.2843 -0.0015 -0.0135 0.0046  1134 LEU B CB  
17421 C CG  . LEU B 1136 ? 0.3277 0.2232 0.3172 -0.0024 -0.0117 0.0072  1134 LEU B CG  
17422 C CD1 . LEU B 1136 ? 0.3318 0.2347 0.3228 0.0005  -0.0104 0.0063  1134 LEU B CD1 
17423 C CD2 . LEU B 1136 ? 0.3510 0.2402 0.3365 -0.0017 -0.0118 0.0095  1134 LEU B CD2 
17424 N N   . GLN B 1137 ? 0.3421 0.2173 0.3272 -0.0064 -0.0183 0.0016  1135 GLN B N   
17425 C CA  . GLN B 1137 ? 0.3376 0.2080 0.3203 -0.0050 -0.0201 -0.0012 1135 GLN B CA  
17426 C C   . GLN B 1137 ? 0.3951 0.2566 0.3725 -0.0020 -0.0211 -0.0016 1135 GLN B C   
17427 O O   . GLN B 1137 ? 0.3992 0.2588 0.3743 0.0015  -0.0217 -0.0040 1135 GLN B O   
17428 C CB  . GLN B 1137 ? 0.3993 0.2674 0.3833 -0.0095 -0.0216 -0.0017 1135 GLN B CB  
17429 C CG  . GLN B 1137 ? 0.3802 0.2571 0.3694 -0.0117 -0.0210 -0.0021 1135 GLN B CG  
17430 C CD  . GLN B 1137 ? 0.3271 0.2094 0.3203 -0.0151 -0.0195 0.0008  1135 GLN B CD  
17431 O OE1 . GLN B 1137 ? 0.3519 0.2324 0.3440 -0.0153 -0.0185 0.0031  1135 GLN B OE1 
17432 N NE2 . GLN B 1137 ? 0.3781 0.2670 0.3760 -0.0176 -0.0192 0.0006  1135 GLN B NE2 
17433 N N   . ALA B 1138 ? 0.3585 0.2144 0.3337 -0.0030 -0.0213 0.0009  1136 ALA B N   
17434 C CA  . ALA B 1138 ? 0.4103 0.2570 0.3802 -0.0001 -0.0223 0.0007  1136 ALA B CA  
17435 C C   . ALA B 1138 ? 0.4392 0.2887 0.4081 0.0053  -0.0214 0.0001  1136 ALA B C   
17436 O O   . ALA B 1138 ? 0.4585 0.3017 0.4235 0.0088  -0.0223 -0.0009 1136 ALA B O   
17437 C CB  . ALA B 1138 ? 0.4302 0.2707 0.3981 -0.0025 -0.0226 0.0038  1136 ALA B CB  
17438 N N   . SER B 1139 ? 0.4162 0.2750 0.3886 0.0060  -0.0197 0.0007  1137 SER B N   
17439 C CA  . SER B 1139 ? 0.3843 0.2466 0.3562 0.0108  -0.0188 0.0003  1137 SER B CA  
17440 C C   . SER B 1139 ? 0.4364 0.2995 0.4078 0.0142  -0.0193 -0.0029 1137 SER B C   
17441 O O   . SER B 1139 ? 0.4162 0.2799 0.3863 0.0186  -0.0190 -0.0035 1137 SER B O   
17442 C CB  . SER B 1139 ? 0.3581 0.2301 0.3339 0.0102  -0.0170 0.0016  1137 SER B CB  
17443 O OG  . SER B 1139 ? 0.3995 0.2708 0.3751 0.0080  -0.0163 0.0047  1137 SER B OG  
17444 N N   . LEU B 1140 ? 0.3924 0.2558 0.3648 0.0123  -0.0199 -0.0050 1138 LEU B N   
17445 C CA  . LEU B 1140 ? 0.4082 0.2720 0.3797 0.0152  -0.0203 -0.0081 1138 LEU B CA  
17446 C C   . LEU B 1140 ? 0.4745 0.3284 0.4416 0.0157  -0.0221 -0.0098 1138 LEU B C   
17447 O O   . LEU B 1140 ? 0.4695 0.3229 0.4358 0.0167  -0.0226 -0.0125 1138 LEU B O   
17448 C CB  . LEU B 1140 ? 0.3982 0.2698 0.3736 0.0135  -0.0197 -0.0095 1138 LEU B CB  
17449 C CG  . LEU B 1140 ? 0.4032 0.2846 0.3826 0.0136  -0.0179 -0.0084 1138 LEU B CG  
17450 C CD1 . LEU B 1140 ? 0.3774 0.2657 0.3602 0.0124  -0.0175 -0.0100 1138 LEU B CD1 
17451 C CD2 . LEU B 1140 ? 0.4722 0.3554 0.4505 0.0182  -0.0171 -0.0083 1138 LEU B CD2 
17452 N N   . LYS B 1141 ? 0.5152 0.3608 0.4793 0.0148  -0.0230 -0.0082 1139 LYS B N   
17453 C CA  . LYS B 1141 ? 0.5408 0.3761 0.5001 0.0155  -0.0248 -0.0098 1139 LYS B CA  
17454 C C   . LYS B 1141 ? 0.5408 0.3746 0.4974 0.0212  -0.0246 -0.0120 1139 LYS B C   
17455 O O   . LYS B 1141 ? 0.5270 0.3639 0.4840 0.0248  -0.0236 -0.0111 1139 LYS B O   
17456 C CB  . LYS B 1141 ? 0.5195 0.3461 0.4758 0.0140  -0.0257 -0.0074 1139 LYS B CB  
17457 N N   . ASN B 1142 ? 0.5105 0.3400 0.4646 0.0220  -0.0256 -0.0149 1140 ASN B N   
17458 C CA  . ASN B 1142 ? 0.5158 0.3430 0.4669 0.0273  -0.0255 -0.0173 1140 ASN B CA  
17459 C C   . ASN B 1142 ? 0.5145 0.3519 0.4689 0.0303  -0.0237 -0.0183 1140 ASN B C   
17460 O O   . ASN B 1142 ? 0.5043 0.3421 0.4574 0.0351  -0.0231 -0.0193 1140 ASN B O   
17461 C CB  . ASN B 1142 ? 0.5789 0.3983 0.5261 0.0309  -0.0259 -0.0164 1140 ASN B CB  
17462 C CG  . ASN B 1142 ? 0.7018 0.5106 0.6455 0.0278  -0.0276 -0.0152 1140 ASN B CG  
17463 O OD1 . ASN B 1142 ? 0.6975 0.5008 0.6391 0.0251  -0.0290 -0.0167 1140 ASN B OD1 
17464 N ND2 . ASN B 1142 ? 0.7372 0.5428 0.6800 0.0281  -0.0277 -0.0124 1140 ASN B ND2 
17465 N N   . LEU B 1143 ? 0.4902 0.3363 0.4491 0.0274  -0.0230 -0.0179 1141 LEU B N   
17466 C CA  . LEU B 1143 ? 0.4555 0.3110 0.4174 0.0297  -0.0214 -0.0189 1141 LEU B CA  
17467 C C   . LEU B 1143 ? 0.4735 0.3276 0.4330 0.0324  -0.0215 -0.0222 1141 LEU B C   
17468 O O   . LEU B 1143 ? 0.5327 0.3816 0.4899 0.0305  -0.0228 -0.0238 1141 LEU B O   
17469 C CB  . LEU B 1143 ? 0.4141 0.2777 0.3807 0.0257  -0.0208 -0.0180 1141 LEU B CB  
17470 C CG  . LEU B 1143 ? 0.4346 0.3088 0.4051 0.0271  -0.0191 -0.0181 1141 LEU B CG  
17471 C CD1 . LEU B 1143 ? 0.3922 0.2698 0.3640 0.0290  -0.0181 -0.0159 1141 LEU B CD1 
17472 C CD2 . LEU B 1143 ? 0.3929 0.2729 0.3671 0.0229  -0.0190 -0.0178 1141 LEU B CD2 
17473 N N   . PRO B 1144 ? 0.4749 0.3336 0.4350 0.0368  -0.0203 -0.0232 1142 PRO B N   
17474 C CA  . PRO B 1144 ? 0.5040 0.3623 0.4620 0.0393  -0.0201 -0.0263 1142 PRO B CA  
17475 C C   . PRO B 1144 ? 0.4521 0.3145 0.4118 0.0358  -0.0203 -0.0275 1142 PRO B C   
17476 O O   . PRO B 1144 ? 0.3962 0.2658 0.3602 0.0330  -0.0197 -0.0261 1142 PRO B O   
17477 C CB  . PRO B 1144 ? 0.5041 0.3695 0.4640 0.0437  -0.0184 -0.0263 1142 PRO B CB  
17478 C CG  . PRO B 1144 ? 0.4921 0.3582 0.4534 0.0445  -0.0182 -0.0235 1142 PRO B CG  
17479 C CD  . PRO B 1144 ? 0.4455 0.3106 0.4082 0.0394  -0.0189 -0.0215 1142 PRO B CD  
17480 N N   . GLN B 1145 ? 0.4552 0.3129 0.4115 0.0361  -0.0211 -0.0301 1143 GLN B N   
17481 C CA  . GLN B 1145 ? 0.4276 0.2884 0.3850 0.0329  -0.0215 -0.0314 1143 GLN B CA  
17482 C C   . GLN B 1145 ? 0.4066 0.2780 0.3679 0.0337  -0.0199 -0.0315 1143 GLN B C   
17483 O O   . GLN B 1145 ? 0.3996 0.2759 0.3637 0.0305  -0.0200 -0.0313 1143 GLN B O   
17484 C CB  . GLN B 1145 ? 0.4779 0.3316 0.4302 0.0337  -0.0227 -0.0344 1143 GLN B CB  
17485 N N   . THR B 1146 ? 0.4227 0.2978 0.3844 0.0381  -0.0183 -0.0318 1144 THR B N   
17486 C CA  . THR B 1146 ? 0.4184 0.3036 0.3840 0.0386  -0.0168 -0.0316 1144 THR B CA  
17487 C C   . THR B 1146 ? 0.4100 0.3010 0.3802 0.0355  -0.0165 -0.0291 1144 THR B C   
17488 O O   . THR B 1146 ? 0.4342 0.3317 0.4073 0.0334  -0.0160 -0.0290 1144 THR B O   
17489 C CB  . THR B 1146 ? 0.4324 0.3206 0.3979 0.0436  -0.0152 -0.0320 1144 THR B CB  
17490 O OG1 . THR B 1146 ? 0.5314 0.4158 0.4962 0.0454  -0.0154 -0.0304 1144 THR B OG1 
17491 C CG2 . THR B 1146 ? 0.5497 0.4346 0.5112 0.0467  -0.0149 -0.0349 1144 THR B CG2 
17492 N N   . VAL B 1147 ? 0.3716 0.2601 0.3422 0.0351  -0.0168 -0.0269 1145 VAL B N   
17493 C CA  . VAL B 1147 ? 0.3245 0.2181 0.2990 0.0321  -0.0164 -0.0245 1145 VAL B CA  
17494 C C   . VAL B 1147 ? 0.3529 0.2444 0.3281 0.0273  -0.0176 -0.0241 1145 VAL B C   
17495 O O   . VAL B 1147 ? 0.3629 0.2605 0.3418 0.0246  -0.0172 -0.0232 1145 VAL B O   
17496 C CB  . VAL B 1147 ? 0.3187 0.2108 0.2933 0.0333  -0.0162 -0.0222 1145 VAL B CB  
17497 C CG1 . VAL B 1147 ? 0.3526 0.2510 0.3313 0.0307  -0.0155 -0.0199 1145 VAL B CG1 
17498 C CG2 . VAL B 1147 ? 0.3293 0.2227 0.3031 0.0383  -0.0153 -0.0227 1145 VAL B CG2 
17499 N N   . GLY B 1148 ? 0.3559 0.2389 0.3277 0.0262  -0.0192 -0.0248 1146 GLY B N   
17500 C CA  . GLY B 1148 ? 0.3884 0.2694 0.3609 0.0215  -0.0205 -0.0244 1146 GLY B CA  
17501 C C   . GLY B 1148 ? 0.3659 0.2520 0.3405 0.0196  -0.0206 -0.0257 1146 GLY B C   
17502 O O   . GLY B 1148 ? 0.3705 0.2595 0.3482 0.0158  -0.0210 -0.0246 1146 GLY B O   
17503 N N   . LEU B 1149 ? 0.3653 0.2527 0.3382 0.0222  -0.0202 -0.0280 1147 LEU B N   
17504 C CA  . LEU B 1149 ? 0.4045 0.2966 0.3789 0.0206  -0.0204 -0.0292 1147 LEU B CA  
17505 C C   . LEU B 1149 ? 0.3874 0.2886 0.3669 0.0194  -0.0192 -0.0277 1147 LEU B C   
17506 O O   . LEU B 1149 ? 0.3990 0.3041 0.3805 0.0171  -0.0195 -0.0280 1147 LEU B O   
17507 C CB  . LEU B 1149 ? 0.4892 0.3811 0.4606 0.0240  -0.0199 -0.0318 1147 LEU B CB  
17508 N N   . ARG B 1150 ? 0.3404 0.2452 0.3219 0.0209  -0.0178 -0.0260 1148 ARG B N   
17509 C CA  . ARG B 1150 ? 0.3303 0.2432 0.3162 0.0198  -0.0165 -0.0245 1148 ARG B CA  
17510 C C   . ARG B 1150 ? 0.2983 0.2116 0.2869 0.0165  -0.0167 -0.0221 1148 ARG B C   
17511 O O   . ARG B 1150 ? 0.2990 0.2186 0.2911 0.0154  -0.0157 -0.0208 1148 ARG B O   
17512 C CB  . ARG B 1150 ? 0.3230 0.2399 0.3095 0.0232  -0.0149 -0.0239 1148 ARG B CB  
17513 C CG  . ARG B 1150 ? 0.3567 0.2762 0.3421 0.0263  -0.0142 -0.0259 1148 ARG B CG  
17514 C CD  . ARG B 1150 ? 0.3573 0.2854 0.3462 0.0264  -0.0128 -0.0253 1148 ARG B CD  
17515 N NE  . ARG B 1150 ? 0.3528 0.2837 0.3408 0.0297  -0.0119 -0.0267 1148 ARG B NE  
17516 C CZ  . ARG B 1150 ? 0.3377 0.2731 0.3271 0.0321  -0.0106 -0.0260 1148 ARG B CZ  
17517 N NH1 . ARG B 1150 ? 0.2744 0.2121 0.2659 0.0315  -0.0102 -0.0240 1148 ARG B NH1 
17518 N NH2 . ARG B 1150 ? 0.3008 0.2385 0.2893 0.0350  -0.0098 -0.0274 1148 ARG B NH2 
17519 N N   . VAL B 1151 ? 0.3152 0.2216 0.3018 0.0149  -0.0179 -0.0215 1149 VAL B N   
17520 C CA  . VAL B 1151 ? 0.2884 0.1946 0.2771 0.0120  -0.0179 -0.0191 1149 VAL B CA  
17521 C C   . VAL B 1151 ? 0.3328 0.2369 0.3224 0.0079  -0.0194 -0.0191 1149 VAL B C   
17522 O O   . VAL B 1151 ? 0.3360 0.2338 0.3225 0.0075  -0.0210 -0.0205 1149 VAL B O   
17523 C CB  . VAL B 1151 ? 0.3152 0.2153 0.3012 0.0133  -0.0180 -0.0179 1149 VAL B CB  
17524 C CG1 . VAL B 1151 ? 0.3621 0.2610 0.3497 0.0098  -0.0182 -0.0153 1149 VAL B CG1 
17525 C CG2 . VAL B 1151 ? 0.3553 0.2584 0.3411 0.0171  -0.0166 -0.0174 1149 VAL B CG2 
17526 N N   . SER B 1152 ? 0.3103 0.2195 0.3040 0.0050  -0.0189 -0.0175 1150 SER B N   
17527 C CA  . SER B 1152 ? 0.3212 0.2287 0.3163 0.0008  -0.0203 -0.0168 1150 SER B CA  
17528 C C   . SER B 1152 ? 0.3199 0.2293 0.3178 -0.0013 -0.0193 -0.0140 1150 SER B C   
17529 O O   . SER B 1152 ? 0.3006 0.2140 0.2997 0.0002  -0.0175 -0.0128 1150 SER B O   
17530 C CB  . SER B 1152 ? 0.3147 0.2272 0.3126 -0.0008 -0.0208 -0.0179 1150 SER B CB  
17531 O OG  . SER B 1152 ? 0.3807 0.3013 0.3824 -0.0005 -0.0191 -0.0170 1150 SER B OG  
17532 N N   . TRP B 1153 ? 0.3161 0.2225 0.3148 -0.0050 -0.0204 -0.0130 1151 TRP B N   
17533 C CA  . TRP B 1153 ? 0.2941 0.2025 0.2957 -0.0077 -0.0195 -0.0102 1151 TRP B CA  
17534 C C   . TRP B 1153 ? 0.3140 0.2281 0.3203 -0.0110 -0.0196 -0.0098 1151 TRP B C   
17535 O O   . TRP B 1153 ? 0.3486 0.2614 0.3552 -0.0128 -0.0214 -0.0111 1151 TRP B O   
17536 C CB  . TRP B 1153 ? 0.3272 0.2275 0.3260 -0.0095 -0.0206 -0.0091 1151 TRP B CB  
17537 C CG  . TRP B 1153 ? 0.3187 0.2139 0.3134 -0.0060 -0.0202 -0.0090 1151 TRP B CG  
17538 C CD1 . TRP B 1153 ? 0.3768 0.2662 0.3671 -0.0031 -0.0212 -0.0111 1151 TRP B CD1 
17539 C CD2 . TRP B 1153 ? 0.3102 0.2057 0.3045 -0.0050 -0.0187 -0.0068 1151 TRP B CD2 
17540 N NE1 . TRP B 1153 ? 0.3428 0.2292 0.3304 -0.0002 -0.0205 -0.0102 1151 TRP B NE1 
17541 C CE2 . TRP B 1153 ? 0.3148 0.2048 0.3047 -0.0014 -0.0190 -0.0076 1151 TRP B CE2 
17542 C CE3 . TRP B 1153 ? 0.3177 0.2178 0.3149 -0.0067 -0.0171 -0.0043 1151 TRP B CE3 
17543 C CZ2 . TRP B 1153 ? 0.3272 0.2160 0.3156 0.0005  -0.0180 -0.0058 1151 TRP B CZ2 
17544 C CZ3 . TRP B 1153 ? 0.3052 0.2039 0.3006 -0.0049 -0.0160 -0.0026 1151 TRP B CZ3 
17545 C CH2 . TRP B 1153 ? 0.3241 0.2172 0.3152 -0.0014 -0.0166 -0.0033 1151 TRP B CH2 
17546 N N   . SER B 1154 ? 0.2523 0.1729 0.2624 -0.0117 -0.0178 -0.0080 1152 SER B N   
17547 C CA  . SER B 1154 ? 0.2802 0.2071 0.2952 -0.0144 -0.0177 -0.0075 1152 SER B CA  
17548 C C   . SER B 1154 ? 0.2596 0.1875 0.2775 -0.0178 -0.0169 -0.0048 1152 SER B C   
17549 O O   . SER B 1154 ? 0.2739 0.2028 0.2917 -0.0172 -0.0151 -0.0030 1152 SER B O   
17550 C CB  . SER B 1154 ? 0.2970 0.2316 0.3145 -0.0123 -0.0161 -0.0080 1152 SER B CB  
17551 O OG  . SER B 1154 ? 0.2694 0.2099 0.2918 -0.0149 -0.0159 -0.0072 1152 SER B OG  
17552 N N   . LYS B 1155 ? 0.2535 0.1812 0.2738 -0.0215 -0.0184 -0.0045 1153 LYS B N   
17553 C CA  . LYS B 1155 ? 0.3230 0.2535 0.3473 -0.0250 -0.0176 -0.0019 1153 LYS B CA  
17554 C C   . LYS B 1155 ? 0.3008 0.2402 0.3307 -0.0261 -0.0167 -0.0016 1153 LYS B C   
17555 O O   . LYS B 1155 ? 0.3256 0.2683 0.3596 -0.0292 -0.0162 0.0003  1153 LYS B O   
17556 C CB  . LYS B 1155 ? 0.3523 0.2769 0.3759 -0.0288 -0.0198 -0.0015 1153 LYS B CB  
17557 N N   . ASP B 1156 ? 0.2438 0.1870 0.2741 -0.0235 -0.0166 -0.0034 1154 ASP B N   
17558 C CA  . ASP B 1156 ? 0.2231 0.1742 0.2585 -0.0242 -0.0161 -0.0034 1154 ASP B CA  
17559 C C   . ASP B 1156 ? 0.2252 0.1793 0.2594 -0.0204 -0.0151 -0.0050 1154 ASP B C   
17560 O O   . ASP B 1156 ? 0.2405 0.1938 0.2734 -0.0192 -0.0166 -0.0071 1154 ASP B O   
17561 C CB  . ASP B 1156 ? 0.2408 0.1916 0.2781 -0.0268 -0.0186 -0.0043 1154 ASP B CB  
17562 C CG  . ASP B 1156 ? 0.2390 0.1978 0.2821 -0.0279 -0.0183 -0.0038 1154 ASP B CG  
17563 O OD1 . ASP B 1156 ? 0.2288 0.1930 0.2735 -0.0257 -0.0163 -0.0037 1154 ASP B OD1 
17564 O OD2 . ASP B 1156 ? 0.2683 0.2280 0.3144 -0.0311 -0.0200 -0.0034 1154 ASP B OD2 
17565 N N   . TRP B 1157 ? 0.1994 0.1570 0.2341 -0.0186 -0.0127 -0.0040 1155 TRP B N   
17566 C CA  . TRP B 1157 ? 0.2094 0.1692 0.2425 -0.0151 -0.0118 -0.0054 1155 TRP B CA  
17567 C C   . TRP B 1157 ? 0.2333 0.1981 0.2693 -0.0148 -0.0124 -0.0067 1155 TRP B C   
17568 O O   . TRP B 1157 ? 0.2487 0.2132 0.2827 -0.0126 -0.0130 -0.0085 1155 TRP B O   
17569 C CB  . TRP B 1157 ? 0.2329 0.1958 0.2663 -0.0136 -0.0092 -0.0041 1155 TRP B CB  
17570 C CG  . TRP B 1157 ? 0.2153 0.1739 0.2459 -0.0136 -0.0085 -0.0027 1155 TRP B CG  
17571 C CD1 . TRP B 1157 ? 0.2248 0.1765 0.2522 -0.0143 -0.0099 -0.0026 1155 TRP B CD1 
17572 C CD2 . TRP B 1157 ? 0.2205 0.1810 0.2508 -0.0129 -0.0063 -0.0010 1155 TRP B CD2 
17573 N NE1 . TRP B 1157 ? 0.2453 0.1946 0.2707 -0.0140 -0.0087 -0.0009 1155 TRP B NE1 
17574 C CE2 . TRP B 1157 ? 0.2344 0.1891 0.2615 -0.0132 -0.0064 0.0001  1155 TRP B CE2 
17575 C CE3 . TRP B 1157 ? 0.2374 0.2038 0.2697 -0.0120 -0.0041 -0.0004 1155 TRP B CE3 
17576 C CZ2 . TRP B 1157 ? 0.2702 0.2251 0.2960 -0.0126 -0.0046 0.0019  1155 TRP B CZ2 
17577 C CZ3 . TRP B 1157 ? 0.2458 0.2122 0.2767 -0.0114 -0.0023 0.0012  1155 TRP B CZ3 
17578 C CH2 . TRP B 1157 ? 0.2542 0.2151 0.2819 -0.0118 -0.0026 0.0024  1155 TRP B CH2 
17579 N N   . ALA B 1158 ? 0.2204 0.1900 0.2612 -0.0170 -0.0121 -0.0056 1156 ALA B N   
17580 C CA  . ALA B 1158 ? 0.2232 0.1979 0.2669 -0.0166 -0.0125 -0.0065 1156 ALA B CA  
17581 C C   . ALA B 1158 ? 0.2599 0.2317 0.3024 -0.0173 -0.0153 -0.0083 1156 ALA B C   
17582 O O   . ALA B 1158 ? 0.3125 0.2866 0.3550 -0.0158 -0.0159 -0.0097 1156 ALA B O   
17583 C CB  . ALA B 1158 ? 0.2125 0.1932 0.2619 -0.0187 -0.0116 -0.0048 1156 ALA B CB  
17584 N N   . ALA B 1159 ? 0.2302 0.1971 0.2714 -0.0195 -0.0171 -0.0082 1157 ALA B N   
17585 C CA  . ALA B 1159 ? 0.2343 0.1980 0.2738 -0.0202 -0.0199 -0.0099 1157 ALA B CA  
17586 C C   . ALA B 1159 ? 0.2854 0.2440 0.3191 -0.0173 -0.0203 -0.0120 1157 ALA B C   
17587 O O   . ALA B 1159 ? 0.2874 0.2448 0.3194 -0.0168 -0.0220 -0.0138 1157 ALA B O   
17588 C CB  . ALA B 1159 ? 0.2693 0.2291 0.3093 -0.0238 -0.0218 -0.0092 1157 ALA B CB  
17589 N N   . ASP B 1160 ? 0.2825 0.2383 0.3133 -0.0154 -0.0188 -0.0117 1158 ASP B N   
17590 C CA  . ASP B 1160 ? 0.2836 0.2341 0.3090 -0.0128 -0.0192 -0.0134 1158 ASP B CA  
17591 C C   . ASP B 1160 ? 0.2937 0.2475 0.3182 -0.0094 -0.0178 -0.0143 1158 ASP B C   
17592 O O   . ASP B 1160 ? 0.3207 0.2711 0.3411 -0.0069 -0.0178 -0.0157 1158 ASP B O   
17593 C CB  . ASP B 1160 ? 0.2911 0.2360 0.3137 -0.0127 -0.0188 -0.0125 1158 ASP B CB  
17594 C CG  . ASP B 1160 ? 0.3081 0.2483 0.3307 -0.0161 -0.0207 -0.0119 1158 ASP B CG  
17595 O OD1 . ASP B 1160 ? 0.3678 0.3080 0.3914 -0.0180 -0.0226 -0.0127 1158 ASP B OD1 
17596 O OD2 . ASP B 1160 ? 0.3267 0.2631 0.3481 -0.0169 -0.0202 -0.0105 1158 ASP B OD2 
17597 N N   . GLY B 1161 ? 0.2669 0.2272 0.2949 -0.0091 -0.0164 -0.0136 1159 GLY B N   
17598 C CA  . GLY B 1161 ? 0.2804 0.2440 0.3078 -0.0063 -0.0152 -0.0145 1159 GLY B CA  
17599 C C   . GLY B 1161 ? 0.3340 0.2984 0.3608 -0.0059 -0.0167 -0.0163 1159 GLY B C   
17600 O O   . GLY B 1161 ? 0.3676 0.3292 0.3937 -0.0074 -0.0187 -0.0171 1159 GLY B O   
17601 N N   . PRO B 1162 ? 0.3244 0.2926 0.3513 -0.0039 -0.0157 -0.0169 1160 PRO B N   
17602 C CA  . PRO B 1162 ? 0.2993 0.2711 0.3271 -0.0022 -0.0134 -0.0161 1160 PRO B CA  
17603 C C   . PRO B 1162 ? 0.2766 0.2453 0.3008 0.0000  -0.0126 -0.0164 1160 PRO B C   
17604 O O   . PRO B 1162 ? 0.3017 0.2667 0.3225 0.0013  -0.0134 -0.0178 1160 PRO B O   
17605 C CB  . PRO B 1162 ? 0.3211 0.2970 0.3498 -0.0011 -0.0133 -0.0169 1160 PRO B CB  
17606 C CG  . PRO B 1162 ? 0.3697 0.3426 0.3957 -0.0010 -0.0152 -0.0187 1160 PRO B CG  
17607 C CD  . PRO B 1162 ? 0.3656 0.3348 0.3918 -0.0034 -0.0169 -0.0184 1160 PRO B CD  
17608 N N   . PHE B 1163 ? 0.2169 0.1871 0.2419 0.0005  -0.0109 -0.0150 1161 PHE B N   
17609 C CA  . PHE B 1163 ? 0.2256 0.1941 0.2477 0.0027  -0.0100 -0.0151 1161 PHE B CA  
17610 C C   . PHE B 1163 ? 0.2189 0.1917 0.2412 0.0047  -0.0087 -0.0155 1161 PHE B C   
17611 O O   . PHE B 1163 ? 0.2324 0.2092 0.2570 0.0042  -0.0085 -0.0156 1161 PHE B O   
17612 C CB  . PHE B 1163 ? 0.2206 0.1876 0.2429 0.0019  -0.0091 -0.0133 1161 PHE B CB  
17613 C CG  . PHE B 1163 ? 0.2326 0.1954 0.2549 -0.0003 -0.0103 -0.0127 1161 PHE B CG  
17614 C CD1 . PHE B 1163 ? 0.3186 0.2758 0.3377 0.0002  -0.0118 -0.0138 1161 PHE B CD1 
17615 C CD2 . PHE B 1163 ? 0.2571 0.2216 0.2826 -0.0029 -0.0100 -0.0111 1161 PHE B CD2 
17616 C CE1 . PHE B 1163 ? 0.3196 0.2723 0.3383 -0.0021 -0.0131 -0.0133 1161 PHE B CE1 
17617 C CE2 . PHE B 1163 ? 0.2803 0.2408 0.3058 -0.0053 -0.0112 -0.0105 1161 PHE B CE2 
17618 C CZ  . PHE B 1163 ? 0.2682 0.2227 0.2902 -0.0050 -0.0128 -0.0116 1161 PHE B CZ  
17619 N N   . ALA B 1164 ? 0.2261 0.1979 0.2459 0.0069  -0.0081 -0.0158 1162 ALA B N   
17620 C CA  . ALA B 1164 ? 0.2233 0.1989 0.2431 0.0086  -0.0070 -0.0161 1162 ALA B CA  
17621 C C   . ALA B 1164 ? 0.2594 0.2360 0.2790 0.0094  -0.0057 -0.0148 1162 ALA B C   
17622 O O   . ALA B 1164 ? 0.2647 0.2438 0.2837 0.0110  -0.0049 -0.0151 1162 ALA B O   
17623 C CB  . ALA B 1164 ? 0.2374 0.2120 0.2547 0.0106  -0.0075 -0.0177 1162 ALA B CB  
17624 N N   . GLY B 1165 ? 0.2106 0.1852 0.2304 0.0083  -0.0054 -0.0134 1163 GLY B N   
17625 C CA  . GLY B 1165 ? 0.2203 0.1955 0.2395 0.0089  -0.0043 -0.0121 1163 GLY B CA  
17626 C C   . GLY B 1165 ? 0.2085 0.1797 0.2271 0.0076  -0.0045 -0.0107 1163 GLY B C   
17627 O O   . GLY B 1165 ? 0.2142 0.1821 0.2327 0.0064  -0.0056 -0.0110 1163 GLY B O   
17628 N N   . ALA B 1166 ? 0.2172 0.1886 0.2352 0.0078  -0.0034 -0.0092 1164 ALA B N   
17629 C CA  . ALA B 1166 ? 0.1896 0.1572 0.2068 0.0066  -0.0035 -0.0077 1164 ALA B CA  
17630 C C   . ALA B 1166 ? 0.2182 0.1850 0.2331 0.0080  -0.0028 -0.0066 1164 ALA B C   
17631 O O   . ALA B 1166 ? 0.2461 0.2164 0.2610 0.0090  -0.0018 -0.0064 1164 ALA B O   
17632 C CB  . ALA B 1166 ? 0.2148 0.1844 0.2348 0.0039  -0.0027 -0.0064 1164 ALA B CB  
17633 N N   . LEU B 1167 ? 0.2090 0.1707 0.2217 0.0082  -0.0035 -0.0058 1165 LEU B N   
17634 C CA  . LEU B 1167 ? 0.2146 0.1748 0.2250 0.0093  -0.0031 -0.0043 1165 LEU B CA  
17635 C C   . LEU B 1167 ? 0.2422 0.1995 0.2524 0.0070  -0.0027 -0.0023 1165 LEU B C   
17636 O O   . LEU B 1167 ? 0.2395 0.1931 0.2498 0.0055  -0.0036 -0.0023 1165 LEU B O   
17637 C CB  . LEU B 1167 ? 0.2304 0.1867 0.2379 0.0119  -0.0042 -0.0050 1165 LEU B CB  
17638 C CG  . LEU B 1167 ? 0.2222 0.1811 0.2299 0.0141  -0.0046 -0.0070 1165 LEU B CG  
17639 C CD1 . LEU B 1167 ? 0.2606 0.2155 0.2656 0.0167  -0.0056 -0.0075 1165 LEU B CD1 
17640 C CD2 . LEU B 1167 ? 0.2445 0.2088 0.2529 0.0150  -0.0035 -0.0068 1165 LEU B CD2 
17641 N N   . VAL B 1168 ? 0.2365 0.1956 0.2464 0.0066  -0.0014 -0.0007 1166 VAL B N   
17642 C CA  . VAL B 1168 ? 0.2320 0.1894 0.2420 0.0042  -0.0007 0.0014  1166 VAL B CA  
17643 C C   . VAL B 1168 ? 0.2553 0.2102 0.2620 0.0053  -0.0004 0.0031  1166 VAL B C   
17644 O O   . VAL B 1168 ? 0.2407 0.1979 0.2462 0.0072  0.0000  0.0030  1166 VAL B O   
17645 C CB  . VAL B 1168 ? 0.2297 0.1924 0.2427 0.0024  0.0010  0.0019  1166 VAL B CB  
17646 C CG1 . VAL B 1168 ? 0.2486 0.2100 0.2619 -0.0002 0.0021  0.0042  1166 VAL B CG1 
17647 C CG2 . VAL B 1168 ? 0.2305 0.1959 0.2468 0.0016  0.0006  0.0002  1166 VAL B CG2 
17648 N N   . GLU B 1169 ? 0.2303 0.1803 0.2355 0.0040  -0.0007 0.0047  1167 GLU B N   
17649 C CA  . GLU B 1169 ? 0.2458 0.1930 0.2478 0.0046  -0.0005 0.0067  1167 GLU B CA  
17650 C C   . GLU B 1169 ? 0.2472 0.1941 0.2497 0.0015  0.0009  0.0089  1167 GLU B C   
17651 O O   . GLU B 1169 ? 0.2984 0.2439 0.3028 -0.0010 0.0007  0.0092  1167 GLU B O   
17652 C CB  . GLU B 1169 ? 0.2530 0.1935 0.2521 0.0059  -0.0022 0.0068  1167 GLU B CB  
17653 C CG  . GLU B 1169 ? 0.2704 0.2073 0.2659 0.0065  -0.0021 0.0090  1167 GLU B CG  
17654 C CD  . GLU B 1169 ? 0.2766 0.2061 0.2694 0.0073  -0.0038 0.0094  1167 GLU B CD  
17655 O OE1 . GLU B 1169 ? 0.2768 0.2037 0.2705 0.0069  -0.0049 0.0080  1167 GLU B OE1 
17656 O OE2 . GLU B 1169 ? 0.3254 0.2515 0.3150 0.0085  -0.0041 0.0111  1167 GLU B OE2 
17657 N N   . GLY B 1170 ? 0.2608 0.2091 0.2616 0.0016  0.0022  0.0105  1168 GLY B N   
17658 C CA  . GLY B 1170 ? 0.2771 0.2251 0.2780 -0.0011 0.0037  0.0128  1168 GLY B CA  
17659 C C   . GLY B 1170 ? 0.3277 0.2792 0.3272 -0.0007 0.0055  0.0139  1168 GLY B C   
17660 O O   . GLY B 1170 ? 0.2939 0.2482 0.2926 0.0016  0.0055  0.0128  1168 GLY B O   
17661 N N   . ASP B 1171 ? 0.3246 0.2757 0.3237 -0.0030 0.0070  0.0162  1169 ASP B N   
17662 C CA  . ASP B 1171 ? 0.3147 0.2692 0.3124 -0.0029 0.0090  0.0172  1169 ASP B CA  
17663 C C   . ASP B 1171 ? 0.2920 0.2528 0.2934 -0.0034 0.0106  0.0158  1169 ASP B C   
17664 O O   . ASP B 1171 ? 0.2897 0.2523 0.2948 -0.0040 0.0101  0.0143  1169 ASP B O   
17665 C CB  . ASP B 1171 ? 0.3157 0.2674 0.3110 -0.0049 0.0103  0.0202  1169 ASP B CB  
17666 C CG  . ASP B 1171 ? 0.3816 0.3340 0.3803 -0.0083 0.0114  0.0212  1169 ASP B CG  
17667 O OD1 . ASP B 1171 ? 0.3236 0.2790 0.3266 -0.0092 0.0113  0.0197  1169 ASP B OD1 
17668 O OD2 . ASP B 1171 ? 0.4473 0.3972 0.4443 -0.0103 0.0124  0.0237  1169 ASP B OD2 
17669 N N   . ALA B 1172 ? 0.3176 0.2818 0.3178 -0.0031 0.0124  0.0164  1170 ALA B N   
17670 C CA  . ALA B 1172 ? 0.3328 0.3027 0.3359 -0.0030 0.0139  0.0149  1170 ALA B CA  
17671 C C   . ALA B 1172 ? 0.3018 0.2741 0.3098 -0.0054 0.0147  0.0149  1170 ALA B C   
17672 O O   . ALA B 1172 ? 0.3002 0.2756 0.3116 -0.0050 0.0144  0.0131  1170 ALA B O   
17673 C CB  . ALA B 1172 ? 0.3404 0.3126 0.3409 -0.0026 0.0159  0.0157  1170 ALA B CB  
17674 N N   . GLU B 1173 ? 0.3254 0.2962 0.3337 -0.0078 0.0158  0.0171  1171 GLU B N   
17675 C CA  . GLU B 1173 ? 0.3029 0.2767 0.3161 -0.0102 0.0167  0.0173  1171 GLU B CA  
17676 C C   . GLU B 1173 ? 0.2830 0.2549 0.2989 -0.0108 0.0143  0.0161  1171 GLU B C   
17677 O O   . GLU B 1173 ? 0.2853 0.2606 0.3057 -0.0117 0.0144  0.0151  1171 GLU B O   
17678 C CB  . GLU B 1173 ? 0.4453 0.4191 0.4586 -0.0128 0.0187  0.0200  1171 GLU B CB  
17679 C CG  . GLU B 1173 ? 0.4913 0.4685 0.5028 -0.0123 0.0215  0.0208  1171 GLU B CG  
17680 C CD  . GLU B 1173 ? 0.5003 0.4836 0.5151 -0.0112 0.0228  0.0189  1171 GLU B CD  
17681 O OE1 . GLU B 1173 ? 0.4691 0.4554 0.4890 -0.0123 0.0228  0.0183  1171 GLU B OE1 
17682 O OE2 . GLU B 1173 ? 0.5304 0.5151 0.5425 -0.0092 0.0237  0.0182  1171 GLU B OE2 
17683 N N   . ARG B 1174 ? 0.2910 0.2572 0.3041 -0.0102 0.0122  0.0161  1172 ARG B N   
17684 C CA  . ARG B 1174 ? 0.2761 0.2401 0.2909 -0.0103 0.0099  0.0146  1172 ARG B CA  
17685 C C   . ARG B 1174 ? 0.2534 0.2207 0.2698 -0.0081 0.0092  0.0119  1172 ARG B C   
17686 O O   . ARG B 1174 ? 0.2644 0.2336 0.2844 -0.0088 0.0084  0.0106  1172 ARG B O   
17687 C CB  . ARG B 1174 ? 0.2929 0.2500 0.3038 -0.0094 0.0079  0.0150  1172 ARG B CB  
17688 C CG  . ARG B 1174 ? 0.2881 0.2420 0.2998 -0.0091 0.0055  0.0132  1172 ARG B CG  
17689 C CD  . ARG B 1174 ? 0.3439 0.2980 0.3593 -0.0124 0.0052  0.0136  1172 ARG B CD  
17690 N NE  . ARG B 1174 ? 0.3217 0.2723 0.3373 -0.0121 0.0028  0.0118  1172 ARG B NE  
17691 C CZ  . ARG B 1174 ? 0.3022 0.2538 0.3213 -0.0142 0.0019  0.0111  1172 ARG B CZ  
17692 N NH1 . ARG B 1174 ? 0.3148 0.2709 0.3379 -0.0168 0.0033  0.0121  1172 ARG B NH1 
17693 N NH2 . ARG B 1174 ? 0.2999 0.2479 0.3184 -0.0137 -0.0003 0.0094  1172 ARG B NH2 
17694 N N   . ILE B 1175 ? 0.2548 0.2230 0.2686 -0.0055 0.0093  0.0111  1173 ILE B N   
17695 C CA  . ILE B 1175 ? 0.2386 0.2101 0.2537 -0.0035 0.0088  0.0087  1173 ILE B CA  
17696 C C   . ILE B 1175 ? 0.2448 0.2217 0.2640 -0.0045 0.0102  0.0082  1173 ILE B C   
17697 O O   . ILE B 1175 ? 0.2495 0.2283 0.2715 -0.0043 0.0092  0.0065  1173 ILE B O   
17698 C CB  . ILE B 1175 ? 0.2401 0.2119 0.2517 -0.0009 0.0089  0.0083  1173 ILE B CB  
17699 C CG1 . ILE B 1175 ? 0.2725 0.2393 0.2807 0.0006  0.0071  0.0084  1173 ILE B CG1 
17700 C CG2 . ILE B 1175 ? 0.2584 0.2344 0.2715 0.0006  0.0089  0.0061  1173 ILE B CG2 
17701 C CD1 . ILE B 1175 ? 0.2753 0.2422 0.2799 0.0028  0.0071  0.0087  1173 ILE B CD1 
17702 N N   . ARG B 1176 ? 0.2660 0.2456 0.2857 -0.0056 0.0125  0.0096  1174 ARG B N   
17703 C CA  . ARG B 1176 ? 0.2512 0.2361 0.2750 -0.0063 0.0139  0.0091  1174 ARG B CA  
17704 C C   . ARG B 1176 ? 0.2440 0.2295 0.2721 -0.0085 0.0131  0.0091  1174 ARG B C   
17705 O O   . ARG B 1176 ? 0.2410 0.2298 0.2725 -0.0083 0.0127  0.0077  1174 ARG B O   
17706 C CB  . ARG B 1176 ? 0.2646 0.2520 0.2879 -0.0070 0.0167  0.0108  1174 ARG B CB  
17707 C CG  . ARG B 1176 ? 0.3174 0.3105 0.3445 -0.0071 0.0185  0.0102  1174 ARG B CG  
17708 C CD  . ARG B 1176 ? 0.3477 0.3433 0.3753 -0.0084 0.0214  0.0121  1174 ARG B CD  
17709 N NE  . ARG B 1176 ? 0.4032 0.3966 0.4257 -0.0077 0.0225  0.0132  1174 ARG B NE  
17710 C CZ  . ARG B 1176 ? 0.4304 0.4251 0.4500 -0.0059 0.0237  0.0125  1174 ARG B CZ  
17711 N NH1 . ARG B 1176 ? 0.3965 0.3947 0.4179 -0.0044 0.0240  0.0107  1174 ARG B NH1 
17712 N NH2 . ARG B 1176 ? 0.4450 0.4374 0.4598 -0.0055 0.0245  0.0138  1174 ARG B NH2 
17713 N N   . ALA B 1177 ? 0.2546 0.2368 0.2826 -0.0106 0.0127  0.0108  1175 ALA B N   
17714 C CA  . ALA B 1177 ? 0.2663 0.2490 0.2984 -0.0130 0.0117  0.0109  1175 ALA B CA  
17715 C C   . ALA B 1177 ? 0.2432 0.2242 0.2757 -0.0121 0.0091  0.0087  1175 ALA B C   
17716 O O   . ALA B 1177 ? 0.2507 0.2345 0.2872 -0.0129 0.0085  0.0078  1175 ALA B O   
17717 C CB  . ALA B 1177 ? 0.2874 0.2659 0.3185 -0.0155 0.0115  0.0131  1175 ALA B CB  
17718 N N   . VAL B 1178 ? 0.2401 0.2166 0.2687 -0.0103 0.0076  0.0079  1176 VAL B N   
17719 C CA  . VAL B 1178 ? 0.2250 0.1998 0.2536 -0.0092 0.0053  0.0058  1176 VAL B CA  
17720 C C   . VAL B 1178 ? 0.2321 0.2115 0.2624 -0.0074 0.0056  0.0039  1176 VAL B C   
17721 O O   . VAL B 1178 ? 0.2318 0.2123 0.2644 -0.0076 0.0043  0.0025  1176 VAL B O   
17722 C CB  . VAL B 1178 ? 0.2453 0.2145 0.2692 -0.0074 0.0040  0.0054  1176 VAL B CB  
17723 C CG1 . VAL B 1178 ? 0.2587 0.2267 0.2824 -0.0058 0.0020  0.0030  1176 VAL B CG1 
17724 C CG2 . VAL B 1178 ? 0.2943 0.2582 0.3167 -0.0093 0.0034  0.0071  1176 VAL B CG2 
17725 N N   . ASN B 1179 ? 0.2230 0.2050 0.2520 -0.0058 0.0072  0.0039  1177 ASN B N   
17726 C CA  . ASN B 1179 ? 0.2400 0.2259 0.2702 -0.0041 0.0074  0.0022  1177 ASN B CA  
17727 C C   . ASN B 1179 ? 0.2376 0.2280 0.2726 -0.0055 0.0081  0.0022  1177 ASN B C   
17728 O O   . ASN B 1179 ? 0.2433 0.2356 0.2802 -0.0049 0.0071  0.0006  1177 ASN B O   
17729 C CB  . ASN B 1179 ? 0.2381 0.2255 0.2658 -0.0025 0.0090  0.0025  1177 ASN B CB  
17730 C CG  . ASN B 1179 ? 0.2815 0.2713 0.3090 -0.0004 0.0088  0.0006  1177 ASN B CG  
17731 O OD1 . ASN B 1179 ? 0.2906 0.2798 0.3185 0.0003  0.0071  -0.0010 1177 ASN B OD1 
17732 N ND2 . ASN B 1179 ? 0.2868 0.2791 0.3133 0.0005  0.0104  0.0007  1177 ASN B ND2 
17733 N N   . LYS B 1180 ? 0.2402 0.2323 0.2773 -0.0075 0.0096  0.0040  1178 LYS B N   
17734 C CA  . LYS B 1180 ? 0.2416 0.2381 0.2837 -0.0089 0.0102  0.0041  1178 LYS B CA  
17735 C C   . LYS B 1180 ? 0.2092 0.2045 0.2536 -0.0103 0.0078  0.0034  1178 LYS B C   
17736 O O   . LYS B 1180 ? 0.2552 0.2537 0.3028 -0.0102 0.0072  0.0024  1178 LYS B O   
17737 C CB  . LYS B 1180 ? 0.2670 0.2656 0.3109 -0.0108 0.0124  0.0064  1178 LYS B CB  
17738 C CG  . LYS B 1180 ? 0.3229 0.3246 0.3659 -0.0095 0.0150  0.0068  1178 LYS B CG  
17739 C CD  . LYS B 1180 ? 0.3712 0.3747 0.4156 -0.0115 0.0174  0.0091  1178 LYS B CD  
17740 C CE  . LYS B 1180 ? 0.5219 0.5286 0.5721 -0.0139 0.0172  0.0098  1178 LYS B CE  
17741 N NZ  . LYS B 1180 ? 0.6297 0.6424 0.6841 -0.0130 0.0185  0.0092  1178 LYS B NZ  
17742 N N   . ALA B 1181 ? 0.2320 0.2225 0.2747 -0.0116 0.0064  0.0040  1179 ALA B N   
17743 C CA  . ALA B 1181 ? 0.2247 0.2134 0.2690 -0.0130 0.0040  0.0032  1179 ALA B CA  
17744 C C   . ALA B 1181 ? 0.2209 0.2090 0.2639 -0.0109 0.0023  0.0008  1179 ALA B C   
17745 O O   . ALA B 1181 ? 0.2389 0.2285 0.2846 -0.0116 0.0009  -0.0001 1179 ALA B O   
17746 C CB  . ALA B 1181 ? 0.2312 0.2138 0.2729 -0.0145 0.0028  0.0041  1179 ALA B CB  
17747 N N   . ILE B 1182 ? 0.2203 0.2064 0.2594 -0.0084 0.0024  0.0000  1180 ILE B N   
17748 C CA  . ILE B 1182 ? 0.2481 0.2339 0.2860 -0.0064 0.0011  -0.0022 1180 ILE B CA  
17749 C C   . ILE B 1182 ? 0.2303 0.2214 0.2711 -0.0057 0.0017  -0.0030 1180 ILE B C   
17750 O O   . ILE B 1182 ? 0.2406 0.2323 0.2823 -0.0054 0.0003  -0.0044 1180 ILE B O   
17751 C CB  . ILE B 1182 ? 0.2496 0.2328 0.2831 -0.0040 0.0012  -0.0027 1180 ILE B CB  
17752 C CG1 . ILE B 1182 ? 0.2471 0.2243 0.2777 -0.0044 -0.0001 -0.0023 1180 ILE B CG1 
17753 C CG2 . ILE B 1182 ? 0.2742 0.2585 0.3069 -0.0019 0.0004  -0.0047 1180 ILE B CG2 
17754 C CD1 . ILE B 1182 ? 0.2432 0.2179 0.2697 -0.0022 0.0002  -0.0023 1180 ILE B CD1 
17755 N N   . ALA B 1183 ? 0.2458 0.2405 0.2878 -0.0054 0.0039  -0.0021 1181 ALA B N   
17756 C CA  . ALA B 1183 ? 0.2681 0.2675 0.3127 -0.0046 0.0046  -0.0028 1181 ALA B CA  
17757 C C   . ALA B 1183 ? 0.2649 0.2669 0.3141 -0.0063 0.0037  -0.0027 1181 ALA B C   
17758 O O   . ALA B 1183 ? 0.3099 0.3147 0.3609 -0.0055 0.0033  -0.0037 1181 ALA B O   
17759 C CB  . ALA B 1183 ? 0.2465 0.2488 0.2912 -0.0040 0.0072  -0.0018 1181 ALA B CB  
17760 N N   . ALA B 1184 ? 0.2441 0.2450 0.2950 -0.0087 0.0032  -0.0015 1182 ALA B N   
17761 C CA  . ALA B 1184 ? 0.2657 0.2691 0.3211 -0.0106 0.0021  -0.0013 1182 ALA B CA  
17762 C C   . ALA B 1184 ? 0.2563 0.2565 0.3108 -0.0112 -0.0008 -0.0026 1182 ALA B C   
17763 O O   . ALA B 1184 ? 0.2709 0.2727 0.3288 -0.0129 -0.0022 -0.0025 1182 ALA B O   
17764 C CB  . ALA B 1184 ? 0.2699 0.2744 0.3281 -0.0133 0.0030  0.0008  1182 ALA B CB  
17765 N N   . LEU B 1185 ? 0.2322 0.2278 0.2821 -0.0098 -0.0018 -0.0038 1183 LEU B N   
17766 C CA  . LEU B 1185 ? 0.2377 0.2302 0.2865 -0.0101 -0.0044 -0.0052 1183 LEU B CA  
17767 C C   . LEU B 1185 ? 0.2709 0.2666 0.3212 -0.0090 -0.0052 -0.0066 1183 LEU B C   
17768 O O   . LEU B 1185 ? 0.2740 0.2723 0.3241 -0.0071 -0.0039 -0.0070 1183 LEU B O   
17769 C CB  . LEU B 1185 ? 0.2341 0.2213 0.2777 -0.0085 -0.0050 -0.0062 1183 LEU B CB  
17770 C CG  . LEU B 1185 ? 0.2358 0.2191 0.2774 -0.0094 -0.0045 -0.0049 1183 LEU B CG  
17771 C CD1 . LEU B 1185 ? 0.2473 0.2260 0.2840 -0.0072 -0.0050 -0.0059 1183 LEU B CD1 
17772 C CD2 . LEU B 1185 ? 0.2336 0.2146 0.2767 -0.0124 -0.0060 -0.0041 1183 LEU B CD2 
17773 N N   . PRO B 1186 ? 0.2574 0.2526 0.3090 -0.0103 -0.0074 -0.0073 1184 PRO B N   
17774 C CA  . PRO B 1186 ? 0.2808 0.2786 0.3333 -0.0092 -0.0084 -0.0085 1184 PRO B CA  
17775 C C   . PRO B 1186 ? 0.2448 0.2396 0.2927 -0.0069 -0.0088 -0.0102 1184 PRO B C   
17776 O O   . PRO B 1186 ? 0.2750 0.2655 0.3192 -0.0064 -0.0090 -0.0106 1184 PRO B O   
17777 C CB  . PRO B 1186 ? 0.3507 0.3479 0.4052 -0.0115 -0.0109 -0.0087 1184 PRO B CB  
17778 C CG  . PRO B 1186 ? 0.3790 0.3710 0.4313 -0.0130 -0.0117 -0.0084 1184 PRO B CG  
17779 C CD  . PRO B 1186 ? 0.2990 0.2910 0.3509 -0.0128 -0.0093 -0.0069 1184 PRO B CD  
17780 N N   . GLY B 1187 ? 0.2679 0.2651 0.3161 -0.0055 -0.0090 -0.0111 1185 GLY B N   
17781 C CA  . GLY B 1187 ? 0.2650 0.2600 0.3093 -0.0036 -0.0095 -0.0127 1185 GLY B CA  
17782 C C   . GLY B 1187 ? 0.2450 0.2408 0.2874 -0.0015 -0.0075 -0.0127 1185 GLY B C   
17783 O O   . GLY B 1187 ? 0.2912 0.2905 0.3357 -0.0011 -0.0059 -0.0119 1185 GLY B O   
17784 N N   . PRO B 1188 ? 0.2198 0.2126 0.2583 -0.0001 -0.0076 -0.0137 1186 PRO B N   
17785 C CA  . PRO B 1188 ? 0.2500 0.2439 0.2868 0.0019  -0.0060 -0.0138 1186 PRO B CA  
17786 C C   . PRO B 1188 ? 0.2290 0.2234 0.2662 0.0017  -0.0043 -0.0124 1186 PRO B C   
17787 O O   . PRO B 1188 ? 0.2630 0.2555 0.3005 0.0004  -0.0043 -0.0115 1186 PRO B O   
17788 C CB  . PRO B 1188 ? 0.2527 0.2431 0.2855 0.0032  -0.0068 -0.0150 1186 PRO B CB  
17789 C CG  . PRO B 1188 ? 0.3216 0.3083 0.3538 0.0019  -0.0083 -0.0151 1186 PRO B CG  
17790 C CD  . PRO B 1188 ? 0.2498 0.2382 0.2853 -0.0001 -0.0093 -0.0147 1186 PRO B CD  
17791 N N   . LEU B 1189 ? 0.2161 0.2129 0.2531 0.0029  -0.0028 -0.0123 1187 LEU B N   
17792 C CA  . LEU B 1189 ? 0.2135 0.2104 0.2499 0.0031  -0.0011 -0.0111 1187 LEU B CA  
17793 C C   . LEU B 1189 ? 0.2397 0.2334 0.2726 0.0042  -0.0013 -0.0114 1187 LEU B C   
17794 O O   . LEU B 1189 ? 0.2520 0.2453 0.2827 0.0057  -0.0017 -0.0125 1187 LEU B O   
17795 C CB  . LEU B 1189 ? 0.2104 0.2105 0.2471 0.0042  0.0004  -0.0111 1187 LEU B CB  
17796 C CG  . LEU B 1189 ? 0.2389 0.2425 0.2791 0.0035  0.0013  -0.0105 1187 LEU B CG  
17797 C CD1 . LEU B 1189 ? 0.3031 0.3081 0.3453 0.0034  0.0000  -0.0114 1187 LEU B CD1 
17798 C CD2 . LEU B 1189 ? 0.2571 0.2626 0.2965 0.0047  0.0031  -0.0104 1187 LEU B CD2 
17799 N N   . LEU B 1190 ? 0.2290 0.2203 0.2612 0.0034  -0.0011 -0.0103 1188 LEU B N   
17800 C CA  . LEU B 1190 ? 0.2140 0.2017 0.2429 0.0045  -0.0015 -0.0105 1188 LEU B CA  
17801 C C   . LEU B 1190 ? 0.2415 0.2301 0.2686 0.0058  -0.0001 -0.0099 1188 LEU B C   
17802 O O   . LEU B 1190 ? 0.2267 0.2169 0.2546 0.0052  0.0012  -0.0087 1188 LEU B O   
17803 C CB  . LEU B 1190 ? 0.2183 0.2023 0.2468 0.0032  -0.0021 -0.0096 1188 LEU B CB  
17804 C CG  . LEU B 1190 ? 0.2252 0.2076 0.2551 0.0016  -0.0037 -0.0101 1188 LEU B CG  
17805 C CD1 . LEU B 1190 ? 0.2458 0.2235 0.2742 0.0006  -0.0044 -0.0093 1188 LEU B CD1 
17806 C CD2 . LEU B 1190 ? 0.2503 0.2321 0.2789 0.0028  -0.0051 -0.0120 1188 LEU B CD2 
17807 N N   . LEU B 1191 ? 0.2192 0.2069 0.2439 0.0076  -0.0006 -0.0107 1189 LEU B N   
17808 C CA  . LEU B 1191 ? 0.2074 0.1954 0.2300 0.0089  0.0003  -0.0101 1189 LEU B CA  
17809 C C   . LEU B 1191 ? 0.2314 0.2157 0.2524 0.0087  0.0001  -0.0089 1189 LEU B C   
17810 O O   . LEU B 1191 ? 0.2432 0.2243 0.2627 0.0093  -0.0010 -0.0094 1189 LEU B O   
17811 C CB  . LEU B 1191 ? 0.2168 0.2054 0.2378 0.0108  -0.0002 -0.0114 1189 LEU B CB  
17812 C CG  . LEU B 1191 ? 0.2154 0.2057 0.2348 0.0119  0.0005  -0.0110 1189 LEU B CG  
17813 C CD1 . LEU B 1191 ? 0.2265 0.2185 0.2453 0.0134  0.0000  -0.0123 1189 LEU B CD1 
17814 C CD2 . LEU B 1191 ? 0.2151 0.2029 0.2325 0.0126  0.0005  -0.0099 1189 LEU B CD2 
17815 N N   . VAL B 1192 ? 0.2092 0.1939 0.2303 0.0078  0.0013  -0.0074 1190 VAL B N   
17816 C CA  . VAL B 1192 ? 0.2327 0.2141 0.2525 0.0071  0.0014  -0.0059 1190 VAL B CA  
17817 C C   . VAL B 1192 ? 0.2278 0.2088 0.2448 0.0087  0.0017  -0.0053 1190 VAL B C   
17818 O O   . VAL B 1192 ? 0.2466 0.2304 0.2632 0.0092  0.0027  -0.0052 1190 VAL B O   
17819 C CB  . VAL B 1192 ? 0.2309 0.2134 0.2527 0.0050  0.0026  -0.0045 1190 VAL B CB  
17820 C CG1 . VAL B 1192 ? 0.2500 0.2288 0.2700 0.0042  0.0027  -0.0027 1190 VAL B CG1 
17821 C CG2 . VAL B 1192 ? 0.2212 0.2047 0.2462 0.0034  0.0021  -0.0050 1190 VAL B CG2 
17822 N N   . GLN B 1193 ? 0.2207 0.1977 0.2355 0.0095  0.0009  -0.0048 1191 GLN B N   
17823 C CA  . GLN B 1193 ? 0.1951 0.1712 0.2072 0.0109  0.0010  -0.0039 1191 GLN B CA  
17824 C C   . GLN B 1193 ? 0.2150 0.1872 0.2258 0.0098  0.0012  -0.0020 1191 GLN B C   
17825 O O   . GLN B 1193 ? 0.2474 0.2160 0.2582 0.0091  0.0003  -0.0019 1191 GLN B O   
17826 C CB  . GLN B 1193 ? 0.2345 0.2093 0.2450 0.0132  -0.0002 -0.0049 1191 GLN B CB  
17827 C CG  . GLN B 1193 ? 0.2295 0.2079 0.2412 0.0142  -0.0004 -0.0066 1191 GLN B CG  
17828 C CD  . GLN B 1193 ? 0.2642 0.2424 0.2744 0.0166  -0.0012 -0.0073 1191 GLN B CD  
17829 O OE1 . GLN B 1193 ? 0.2547 0.2338 0.2634 0.0177  -0.0011 -0.0065 1191 GLN B OE1 
17830 N NE2 . GLN B 1193 ? 0.2532 0.2304 0.2636 0.0175  -0.0021 -0.0086 1191 GLN B NE2 
17831 N N   . ALA B 1194 ? 0.2236 0.1964 0.2329 0.0095  0.0022  -0.0005 1192 ALA B N   
17832 C CA  . ALA B 1194 ? 0.2330 0.2024 0.2409 0.0083  0.0026  0.0015  1192 ALA B CA  
17833 C C   . ALA B 1194 ? 0.2568 0.2246 0.2613 0.0098  0.0024  0.0027  1192 ALA B C   
17834 O O   . ALA B 1194 ? 0.2905 0.2612 0.2941 0.0112  0.0026  0.0023  1192 ALA B O   
17835 C CB  . ALA B 1194 ? 0.2609 0.2326 0.2705 0.0060  0.0043  0.0026  1192 ALA B CB  
17836 N N   . ALA B 1195 ? 0.2493 0.2125 0.2518 0.0095  0.0019  0.0042  1193 ALA B N   
17837 C CA  . ALA B 1195 ? 0.2687 0.2298 0.2677 0.0109  0.0016  0.0056  1193 ALA B CA  
17838 C C   . ALA B 1195 ? 0.3053 0.2619 0.3028 0.0093  0.0018  0.0078  1193 ALA B C   
17839 O O   . ALA B 1195 ? 0.2702 0.2241 0.2689 0.0077  0.0015  0.0079  1193 ALA B O   
17840 C CB  . ALA B 1195 ? 0.2900 0.2495 0.2877 0.0138  -0.0001 0.0047  1193 ALA B CB  
17841 N N   . SER B 1196 ? 0.2894 0.2448 0.2838 0.0096  0.0022  0.0096  1194 SER B N   
17842 C CA  . SER B 1196 ? 0.2980 0.2485 0.2903 0.0083  0.0022  0.0119  1194 SER B CA  
17843 C C   . SER B 1196 ? 0.3008 0.2460 0.2909 0.0103  0.0002  0.0119  1194 SER B C   
17844 O O   . SER B 1196 ? 0.3084 0.2547 0.2984 0.0130  -0.0010 0.0105  1194 SER B O   
17845 C CB  . SER B 1196 ? 0.3276 0.2786 0.3169 0.0080  0.0033  0.0139  1194 SER B CB  
17846 O OG  . SER B 1196 ? 0.3233 0.2745 0.3102 0.0108  0.0022  0.0137  1194 SER B OG  
17847 N N   . SER B 1197 ? 0.3044 0.2442 0.2929 0.0091  -0.0002 0.0136  1195 SER B N   
17848 C CA  . SER B 1197 ? 0.3136 0.2476 0.2995 0.0111  -0.0020 0.0140  1195 SER B CA  
17849 C C   . SER B 1197 ? 0.3203 0.2548 0.3033 0.0139  -0.0026 0.0147  1195 SER B C   
17850 O O   . SER B 1197 ? 0.3545 0.2877 0.3369 0.0168  -0.0041 0.0137  1195 SER B O   
17851 C CB  . SER B 1197 ? 0.3386 0.2664 0.3227 0.0090  -0.0021 0.0161  1195 SER B CB  
17852 O OG  . SER B 1197 ? 0.3407 0.2683 0.3277 0.0063  -0.0018 0.0154  1195 SER B OG  
17853 N N   . GLY B 1198 ? 0.3439 0.2804 0.3253 0.0132  -0.0015 0.0163  1196 GLY B N   
17854 C CA  . GLY B 1198 ? 0.3940 0.3313 0.3727 0.0157  -0.0023 0.0170  1196 GLY B CA  
17855 C C   . GLY B 1198 ? 0.3775 0.3201 0.3581 0.0179  -0.0028 0.0147  1196 GLY B C   
17856 O O   . GLY B 1198 ? 0.3690 0.3115 0.3484 0.0207  -0.0042 0.0146  1196 GLY B O   
17857 N N   . GLU B 1199 ? 0.3536 0.3010 0.3374 0.0166  -0.0016 0.0131  1197 GLU B N   
17858 C CA  . GLU B 1199 ? 0.3613 0.3136 0.3470 0.0183  -0.0020 0.0109  1197 GLU B CA  
17859 C C   . GLU B 1199 ? 0.3794 0.3302 0.3662 0.0205  -0.0035 0.0094  1197 GLU B C   
17860 O O   . GLU B 1199 ? 0.3750 0.3282 0.3621 0.0230  -0.0045 0.0085  1197 GLU B O   
17861 C CB  . GLU B 1199 ? 0.3618 0.3186 0.3504 0.0164  -0.0005 0.0096  1197 GLU B CB  
17862 C CG  . GLU B 1199 ? 0.4681 0.4303 0.4584 0.0176  -0.0006 0.0076  1197 GLU B CG  
17863 C CD  . GLU B 1199 ? 0.5229 0.4889 0.5156 0.0156  0.0011  0.0067  1197 GLU B CD  
17864 O OE1 . GLU B 1199 ? 0.5311 0.4961 0.5244 0.0134  0.0023  0.0075  1197 GLU B OE1 
17865 O OE2 . GLU B 1199 ? 0.5857 0.5558 0.5798 0.0162  0.0011  0.0051  1197 GLU B OE2 
17866 N N   . ILE B 1200 ? 0.3084 0.2553 0.2961 0.0196  -0.0037 0.0090  1198 ILE B N   
17867 C CA  . ILE B 1200 ? 0.3293 0.2742 0.3176 0.0218  -0.0051 0.0075  1198 ILE B CA  
17868 C C   . ILE B 1200 ? 0.3877 0.3294 0.3733 0.0247  -0.0065 0.0085  1198 ILE B C   
17869 O O   . ILE B 1200 ? 0.3596 0.3024 0.3458 0.0275  -0.0074 0.0073  1198 ILE B O   
17870 C CB  . ILE B 1200 ? 0.2948 0.2353 0.2839 0.0200  -0.0052 0.0071  1198 ILE B CB  
17871 C CG1 . ILE B 1200 ? 0.3031 0.2476 0.2954 0.0176  -0.0040 0.0058  1198 ILE B CG1 
17872 C CG2 . ILE B 1200 ? 0.3338 0.2710 0.3225 0.0224  -0.0066 0.0057  1198 ILE B CG2 
17873 C CD1 . ILE B 1200 ? 0.2963 0.2371 0.2896 0.0153  -0.0041 0.0056  1198 ILE B CD1 
17874 N N   . ALA B 1201 ? 0.3760 0.3138 0.3586 0.0242  -0.0066 0.0109  1199 ALA B N   
17875 C CA  . ALA B 1201 ? 0.3997 0.3340 0.3796 0.0270  -0.0081 0.0121  1199 ALA B CA  
17876 C C   . ALA B 1201 ? 0.3672 0.3066 0.3469 0.0291  -0.0085 0.0122  1199 ALA B C   
17877 O O   . ALA B 1201 ? 0.4356 0.3747 0.4149 0.0323  -0.0099 0.0120  1199 ALA B O   
17878 C CB  . ALA B 1201 ? 0.4121 0.3407 0.3887 0.0256  -0.0081 0.0149  1199 ALA B CB  
17879 N N   . ARG B 1202 ? 0.4205 0.3646 0.4006 0.0274  -0.0074 0.0124  1200 ARG B N   
17880 C CA  . ARG B 1202 ? 0.4319 0.3804 0.4113 0.0289  -0.0079 0.0127  1200 ARG B CA  
17881 C C   . ARG B 1202 ? 0.4411 0.3954 0.4237 0.0302  -0.0081 0.0104  1200 ARG B C   
17882 O O   . ARG B 1202 ? 0.4655 0.4225 0.4480 0.0325  -0.0092 0.0103  1200 ARG B O   
17883 C CB  . ARG B 1202 ? 0.4245 0.3751 0.4024 0.0265  -0.0066 0.0139  1200 ARG B CB  
17884 C CG  . ARG B 1202 ? 0.5978 0.5436 0.5722 0.0253  -0.0064 0.0165  1200 ARG B CG  
17885 C CD  . ARG B 1202 ? 0.6479 0.5964 0.6206 0.0233  -0.0050 0.0175  1200 ARG B CD  
17886 N NE  . ARG B 1202 ? 0.6418 0.5948 0.6174 0.0215  -0.0034 0.0157  1200 ARG B NE  
17887 C CZ  . ARG B 1202 ? 0.5765 0.5291 0.5531 0.0188  -0.0016 0.0158  1200 ARG B CZ  
17888 N NH1 . ARG B 1202 ? 0.5632 0.5111 0.5382 0.0173  -0.0011 0.0177  1200 ARG B NH1 
17889 N NH2 . ARG B 1202 ? 0.5325 0.4894 0.5119 0.0176  -0.0004 0.0141  1200 ARG B NH2 
17890 N N   . ASN B 1203 ? 0.3750 0.3313 0.3604 0.0287  -0.0071 0.0085  1201 ASN B N   
17891 C CA  . ASN B 1203 ? 0.3669 0.3290 0.3550 0.0292  -0.0069 0.0065  1201 ASN B CA  
17892 C C   . ASN B 1203 ? 0.3889 0.3507 0.3793 0.0304  -0.0072 0.0046  1201 ASN B C   
17893 O O   . ASN B 1203 ? 0.3458 0.3057 0.3373 0.0287  -0.0065 0.0038  1201 ASN B O   
17894 C CB  . ASN B 1203 ? 0.3995 0.3647 0.3886 0.0263  -0.0053 0.0061  1201 ASN B CB  
17895 C CG  . ASN B 1203 ? 0.3893 0.3602 0.3810 0.0265  -0.0050 0.0041  1201 ASN B CG  
17896 O OD1 . ASN B 1203 ? 0.4513 0.4244 0.4440 0.0286  -0.0060 0.0032  1201 ASN B OD1 
17897 N ND2 . ASN B 1203 ? 0.4283 0.4015 0.4211 0.0242  -0.0037 0.0034  1201 ASN B ND2 
17898 N N   . PRO B 1204 ? 0.3933 0.3570 0.3845 0.0332  -0.0082 0.0038  1202 PRO B N   
17899 C CA  . PRO B 1204 ? 0.3920 0.3558 0.3853 0.0344  -0.0083 0.0018  1202 PRO B CA  
17900 C C   . PRO B 1204 ? 0.3551 0.3223 0.3509 0.0325  -0.0072 0.0000  1202 PRO B C   
17901 O O   . PRO B 1204 ? 0.3669 0.3329 0.3638 0.0327  -0.0071 -0.0015 1202 PRO B O   
17902 C CB  . PRO B 1204 ? 0.4277 0.3946 0.4217 0.0377  -0.0094 0.0014  1202 PRO B CB  
17903 C CG  . PRO B 1204 ? 0.5019 0.4683 0.4937 0.0385  -0.0102 0.0036  1202 PRO B CG  
17904 C CD  . PRO B 1204 ? 0.4429 0.4094 0.4335 0.0353  -0.0093 0.0046  1202 PRO B CD  
17905 N N   . ASP B 1205 ? 0.3574 0.3288 0.3538 0.0307  -0.0065 0.0000  1203 ASP B N   
17906 C CA  . ASP B 1205 ? 0.3692 0.3439 0.3679 0.0290  -0.0055 -0.0015 1203 ASP B CA  
17907 C C   . ASP B 1205 ? 0.3553 0.3286 0.3539 0.0260  -0.0044 -0.0010 1203 ASP B C   
17908 O O   . ASP B 1205 ? 0.3478 0.3243 0.3478 0.0244  -0.0035 -0.0018 1203 ASP B O   
17909 C CB  . ASP B 1205 ? 0.3953 0.3759 0.3951 0.0293  -0.0055 -0.0022 1203 ASP B CB  
17910 C CG  . ASP B 1205 ? 0.4630 0.4459 0.4637 0.0320  -0.0065 -0.0029 1203 ASP B CG  
17911 O OD1 . ASP B 1205 ? 0.4355 0.4161 0.4365 0.0337  -0.0069 -0.0035 1203 ASP B OD1 
17912 O OD2 . ASP B 1205 ? 0.4926 0.4799 0.4937 0.0325  -0.0068 -0.0028 1203 ASP B OD2 
17913 N N   . ALA B 1206 ? 0.3415 0.3099 0.3384 0.0253  -0.0044 0.0004  1204 ALA B N   
17914 C CA  . ALA B 1206 ? 0.3600 0.3272 0.3571 0.0225  -0.0032 0.0010  1204 ALA B CA  
17915 C C   . ALA B 1206 ? 0.2976 0.2663 0.2974 0.0211  -0.0027 -0.0007 1204 ALA B C   
17916 O O   . ALA B 1206 ? 0.3329 0.3040 0.3340 0.0192  -0.0015 -0.0008 1204 ALA B O   
17917 C CB  . ALA B 1206 ? 0.3595 0.3208 0.3547 0.0219  -0.0035 0.0026  1204 ALA B CB  
17918 N N   . TYR B 1207 ? 0.2663 0.2338 0.2670 0.0223  -0.0035 -0.0021 1205 TYR B N   
17919 C CA  . TYR B 1207 ? 0.2899 0.2592 0.2929 0.0215  -0.0032 -0.0039 1205 TYR B CA  
17920 C C   . TYR B 1207 ? 0.2723 0.2456 0.2763 0.0234  -0.0035 -0.0054 1205 TYR B C   
17921 O O   . TYR B 1207 ? 0.3513 0.3239 0.3544 0.0257  -0.0043 -0.0056 1205 TYR B O   
17922 C CB  . TYR B 1207 ? 0.2836 0.2484 0.2866 0.0212  -0.0038 -0.0045 1205 TYR B CB  
17923 C CG  . TYR B 1207 ? 0.2554 0.2164 0.2577 0.0190  -0.0036 -0.0029 1205 TYR B CG  
17924 C CD1 . TYR B 1207 ? 0.2457 0.2088 0.2496 0.0164  -0.0025 -0.0024 1205 TYR B CD1 
17925 C CD2 . TYR B 1207 ? 0.2955 0.2507 0.2957 0.0195  -0.0044 -0.0020 1205 TYR B CD2 
17926 C CE1 . TYR B 1207 ? 0.2285 0.1886 0.2322 0.0142  -0.0021 -0.0009 1205 TYR B CE1 
17927 C CE2 . TYR B 1207 ? 0.2762 0.2280 0.2759 0.0172  -0.0042 -0.0005 1205 TYR B CE2 
17928 C CZ  . TYR B 1207 ? 0.2474 0.2018 0.2489 0.0145  -0.0030 0.0001  1205 TYR B CZ  
17929 O OH  . TYR B 1207 ? 0.2599 0.2113 0.2611 0.0121  -0.0026 0.0017  1205 TYR B OH  
17930 N N   . CYS B 1208 ? 0.2220 0.1994 0.2277 0.0223  -0.0028 -0.0063 1206 CYS B N   
17931 C CA  . CYS B 1208 ? 0.2205 0.2020 0.2272 0.0236  -0.0030 -0.0076 1206 CYS B CA  
17932 C C   . CYS B 1208 ? 0.2146 0.1957 0.2224 0.0241  -0.0033 -0.0093 1206 CYS B C   
17933 O O   . CYS B 1208 ? 0.2267 0.2074 0.2356 0.0224  -0.0030 -0.0099 1206 CYS B O   
17934 C CB  . CYS B 1208 ? 0.2434 0.2290 0.2510 0.0222  -0.0021 -0.0077 1206 CYS B CB  
17935 S SG  . CYS B 1208 ? 0.2796 0.2702 0.2883 0.0233  -0.0023 -0.0090 1206 CYS B SG  
17936 N N   . LEU B 1209 ? 0.2169 0.1984 0.2244 0.0264  -0.0039 -0.0101 1207 LEU B N   
17937 C CA  . LEU B 1209 ? 0.2218 0.2029 0.2298 0.0270  -0.0040 -0.0117 1207 LEU B CA  
17938 C C   . LEU B 1209 ? 0.2134 0.1989 0.2232 0.0260  -0.0035 -0.0129 1207 LEU B C   
17939 O O   . LEU B 1209 ? 0.1974 0.1824 0.2075 0.0259  -0.0036 -0.0142 1207 LEU B O   
17940 C CB  . LEU B 1209 ? 0.1996 0.1801 0.2069 0.0300  -0.0046 -0.0122 1207 LEU B CB  
17941 C CG  . LEU B 1209 ? 0.2372 0.2131 0.2426 0.0314  -0.0053 -0.0111 1207 LEU B CG  
17942 C CD1 . LEU B 1209 ? 0.2796 0.2549 0.2844 0.0346  -0.0057 -0.0119 1207 LEU B CD1 
17943 C CD2 . LEU B 1209 ? 0.2501 0.2206 0.2545 0.0297  -0.0055 -0.0108 1207 LEU B CD2 
17944 N N   . ASN B 1210 ? 0.2100 0.1993 0.2205 0.0253  -0.0030 -0.0124 1208 ASN B N   
17945 C CA  . ASN B 1210 ? 0.2358 0.2287 0.2477 0.0243  -0.0026 -0.0134 1208 ASN B CA  
17946 C C   . ASN B 1210 ? 0.2123 0.2037 0.2249 0.0223  -0.0023 -0.0139 1208 ASN B C   
17947 O O   . ASN B 1210 ? 0.2456 0.2386 0.2591 0.0219  -0.0022 -0.0150 1208 ASN B O   
17948 C CB  . ASN B 1210 ? 0.2729 0.2692 0.2850 0.0235  -0.0022 -0.0127 1208 ASN B CB  
17949 C CG  . ASN B 1210 ? 0.2703 0.2689 0.2819 0.0252  -0.0026 -0.0122 1208 ASN B CG  
17950 O OD1 . ASN B 1210 ? 0.3558 0.3532 0.3670 0.0272  -0.0032 -0.0121 1208 ASN B OD1 
17951 N ND2 . ASN B 1210 ? 0.4025 0.4043 0.4143 0.0246  -0.0025 -0.0119 1208 ASN B ND2 
17952 N N   . TRP B 1211 ? 0.2091 0.1976 0.2215 0.0211  -0.0022 -0.0129 1209 TRP B N   
17953 C CA  . TRP B 1211 ? 0.2116 0.1995 0.2252 0.0191  -0.0020 -0.0132 1209 TRP B CA  
17954 C C   . TRP B 1211 ? 0.2206 0.2050 0.2340 0.0190  -0.0027 -0.0139 1209 TRP B C   
17955 O O   . TRP B 1211 ? 0.2523 0.2361 0.2668 0.0174  -0.0028 -0.0141 1209 TRP B O   
17956 C CB  . TRP B 1211 ? 0.2417 0.2291 0.2556 0.0175  -0.0013 -0.0118 1209 TRP B CB  
17957 C CG  . TRP B 1211 ? 0.2346 0.2244 0.2479 0.0178  -0.0007 -0.0110 1209 TRP B CG  
17958 C CD1 . TRP B 1211 ? 0.2522 0.2407 0.2640 0.0179  -0.0005 -0.0095 1209 TRP B CD1 
17959 C CD2 . TRP B 1211 ? 0.2053 0.1989 0.2189 0.0181  -0.0005 -0.0116 1209 TRP B CD2 
17960 N NE1 . TRP B 1211 ? 0.2748 0.2661 0.2860 0.0182  -0.0002 -0.0093 1209 TRP B NE1 
17961 C CE2 . TRP B 1211 ? 0.2247 0.2191 0.2370 0.0183  -0.0001 -0.0105 1209 TRP B CE2 
17962 C CE3 . TRP B 1211 ? 0.2276 0.2237 0.2422 0.0181  -0.0005 -0.0128 1209 TRP B CE3 
17963 C CZ2 . TRP B 1211 ? 0.2685 0.2661 0.2805 0.0184  0.0000  -0.0108 1209 TRP B CZ2 
17964 C CZ3 . TRP B 1211 ? 0.2333 0.2326 0.2477 0.0182  -0.0002 -0.0130 1209 TRP B CZ3 
17965 C CH2 . TRP B 1211 ? 0.2398 0.2398 0.2530 0.0183  0.0000  -0.0120 1209 TRP B CH2 
17966 N N   . LEU B 1212 ? 0.2031 0.1851 0.2150 0.0208  -0.0034 -0.0142 1210 LEU B N   
17967 C CA  . LEU B 1212 ? 0.1872 0.1651 0.1983 0.0209  -0.0041 -0.0150 1210 LEU B CA  
17968 C C   . LEU B 1212 ? 0.1899 0.1685 0.2005 0.0221  -0.0044 -0.0167 1210 LEU B C   
17969 O O   . LEU B 1212 ? 0.2022 0.1772 0.2116 0.0225  -0.0051 -0.0176 1210 LEU B O   
17970 C CB  . LEU B 1212 ? 0.2081 0.1817 0.2172 0.0222  -0.0046 -0.0142 1210 LEU B CB  
17971 C CG  . LEU B 1212 ? 0.1885 0.1601 0.1977 0.0204  -0.0044 -0.0125 1210 LEU B CG  
17972 C CD1 . LEU B 1212 ? 0.2293 0.1974 0.2364 0.0219  -0.0048 -0.0114 1210 LEU B CD1 
17973 C CD2 . LEU B 1212 ? 0.2291 0.1980 0.2390 0.0182  -0.0048 -0.0126 1210 LEU B CD2 
17974 N N   . VAL B 1213 ? 0.2049 0.1879 0.2164 0.0227  -0.0039 -0.0172 1211 VAL B N   
17975 C CA  . VAL B 1213 ? 0.2073 0.1917 0.2186 0.0234  -0.0040 -0.0187 1211 VAL B CA  
17976 C C   . VAL B 1213 ? 0.1941 0.1814 0.2069 0.0216  -0.0037 -0.0189 1211 VAL B C   
17977 O O   . VAL B 1213 ? 0.2164 0.2055 0.2305 0.0202  -0.0033 -0.0180 1211 VAL B O   
17978 C CB  . VAL B 1213 ? 0.2003 0.1876 0.2113 0.0257  -0.0036 -0.0190 1211 VAL B CB  
17979 C CG1 . VAL B 1213 ? 0.2264 0.2105 0.2358 0.0279  -0.0039 -0.0189 1211 VAL B CG1 
17980 C CG2 . VAL B 1213 ? 0.2176 0.2089 0.2297 0.0253  -0.0030 -0.0180 1211 VAL B CG2 
17981 N N   . GLU B 1214 ? 0.1948 0.1823 0.2073 0.0215  -0.0039 -0.0202 1212 GLU B N   
17982 C CA  . GLU B 1214 ? 0.2292 0.2193 0.2429 0.0200  -0.0038 -0.0205 1212 GLU B CA  
17983 C C   . GLU B 1214 ? 0.1912 0.1847 0.2046 0.0211  -0.0033 -0.0211 1212 GLU B C   
17984 O O   . GLU B 1214 ? 0.2045 0.1976 0.2166 0.0227  -0.0033 -0.0220 1212 GLU B O   
17985 C CB  . GLU B 1214 ? 0.2419 0.2295 0.2552 0.0190  -0.0047 -0.0214 1212 GLU B CB  
17986 C CG  . GLU B 1214 ? 0.2954 0.2856 0.3101 0.0175  -0.0047 -0.0215 1212 GLU B CG  
17987 C CD  . GLU B 1214 ? 0.3615 0.3497 0.3756 0.0166  -0.0057 -0.0224 1212 GLU B CD  
17988 O OE1 . GLU B 1214 ? 0.3461 0.3307 0.3594 0.0163  -0.0065 -0.0227 1212 GLU B OE1 
17989 O OE2 . GLU B 1214 ? 0.3875 0.3778 0.4020 0.0160  -0.0058 -0.0228 1212 GLU B OE2 
17990 N N   . GLU B 1215 ? 0.1917 0.1886 0.2064 0.0202  -0.0028 -0.0207 1213 GLU B N   
17991 C CA  . GLU B 1215 ? 0.1866 0.1868 0.2012 0.0207  -0.0023 -0.0211 1213 GLU B CA  
17992 C C   . GLU B 1215 ? 0.1706 0.1708 0.1849 0.0199  -0.0026 -0.0220 1213 GLU B C   
17993 O O   . GLU B 1215 ? 0.1910 0.1903 0.2060 0.0184  -0.0030 -0.0219 1213 GLU B O   
17994 C CB  . GLU B 1215 ? 0.2068 0.2101 0.2226 0.0198  -0.0018 -0.0203 1213 GLU B CB  
17995 C CG  . GLU B 1215 ? 0.2188 0.2224 0.2348 0.0204  -0.0016 -0.0193 1213 GLU B CG  
17996 C CD  . GLU B 1215 ? 0.1938 0.1993 0.2105 0.0192  -0.0012 -0.0186 1213 GLU B CD  
17997 O OE1 . GLU B 1215 ? 0.2016 0.2058 0.2188 0.0180  -0.0011 -0.0181 1213 GLU B OE1 
17998 O OE2 . GLU B 1215 ? 0.1978 0.2063 0.2145 0.0193  -0.0010 -0.0185 1213 GLU B OE2 
17999 N N   . VAL B 1216 ? 0.1923 0.1937 0.2055 0.0209  -0.0024 -0.0228 1214 VAL B N   
18000 C CA  . VAL B 1216 ? 0.1959 0.1977 0.2085 0.0201  -0.0025 -0.0236 1214 VAL B CA  
18001 C C   . VAL B 1216 ? 0.1809 0.1865 0.1935 0.0203  -0.0018 -0.0235 1214 VAL B C   
18002 O O   . VAL B 1216 ? 0.1881 0.1954 0.2004 0.0218  -0.0012 -0.0237 1214 VAL B O   
18003 C CB  . VAL B 1216 ? 0.1822 0.1810 0.1928 0.0209  -0.0031 -0.0247 1214 VAL B CB  
18004 C CG1 . VAL B 1216 ? 0.2243 0.2237 0.2337 0.0201  -0.0033 -0.0254 1214 VAL B CG1 
18005 C CG2 . VAL B 1216 ? 0.2180 0.2128 0.2285 0.0203  -0.0040 -0.0247 1214 VAL B CG2 
18006 N N   . SER B 1217 ? 0.1619 0.1688 0.1749 0.0189  -0.0018 -0.0233 1215 SER B N   
18007 C CA  . SER B 1217 ? 0.1718 0.1820 0.1847 0.0186  -0.0012 -0.0232 1215 SER B CA  
18008 C C   . SER B 1217 ? 0.1678 0.1774 0.1791 0.0184  -0.0014 -0.0240 1215 SER B C   
18009 O O   . SER B 1217 ? 0.1781 0.1854 0.1891 0.0175  -0.0022 -0.0242 1215 SER B O   
18010 C CB  . SER B 1217 ? 0.1963 0.2078 0.2105 0.0171  -0.0012 -0.0224 1215 SER B CB  
18011 O OG  . SER B 1217 ? 0.2215 0.2351 0.2352 0.0163  -0.0009 -0.0224 1215 SER B OG  
18012 N N   . ALA B 1218 ? 0.1778 0.1895 0.1881 0.0190  -0.0006 -0.0243 1216 ALA B N   
18013 C CA  . ALA B 1218 ? 0.1930 0.2044 0.2014 0.0188  -0.0007 -0.0249 1216 ALA B CA  
18014 C C   . ALA B 1218 ? 0.1942 0.2091 0.2027 0.0181  0.0002  -0.0244 1216 ALA B C   
18015 O O   . ALA B 1218 ? 0.2037 0.2215 0.2129 0.0188  0.0010  -0.0242 1216 ALA B O   
18016 C CB  . ALA B 1218 ? 0.2129 0.2227 0.2193 0.0204  -0.0004 -0.0260 1216 ALA B CB  
18017 N N   . SER B 1219 ? 0.1782 0.1929 0.1860 0.0166  -0.0002 -0.0242 1217 SER B N   
18018 C CA  . SER B 1219 ? 0.1731 0.1905 0.1806 0.0157  0.0005  -0.0236 1217 SER B CA  
18019 C C   . SER B 1219 ? 0.1666 0.1835 0.1716 0.0156  0.0007  -0.0241 1217 SER B C   
18020 O O   . SER B 1219 ? 0.1850 0.1992 0.1887 0.0150  -0.0003 -0.0243 1217 SER B O   
18021 C CB  . SER B 1219 ? 0.1855 0.2027 0.1941 0.0140  0.0000  -0.0228 1217 SER B CB  
18022 O OG  . SER B 1219 ? 0.2017 0.2212 0.2099 0.0128  0.0005  -0.0222 1217 SER B OG  
18023 N N   . ILE B 1220 ? 0.1900 0.2096 0.1943 0.0163  0.0018  -0.0243 1218 ILE B N   
18024 C CA  . ILE B 1220 ? 0.1885 0.2078 0.1900 0.0164  0.0023  -0.0248 1218 ILE B CA  
18025 C C   . ILE B 1220 ? 0.2173 0.2395 0.2186 0.0149  0.0030  -0.0238 1218 ILE B C   
18026 O O   . ILE B 1220 ? 0.2103 0.2361 0.2132 0.0149  0.0040  -0.0233 1218 ILE B O   
18027 C CB  . ILE B 1220 ? 0.2287 0.2490 0.2293 0.0186  0.0033  -0.0257 1218 ILE B CB  
18028 C CG1 . ILE B 1220 ? 0.2530 0.2701 0.2539 0.0200  0.0025  -0.0265 1218 ILE B CG1 
18029 C CG2 . ILE B 1220 ? 0.2272 0.2470 0.2244 0.0187  0.0039  -0.0263 1218 ILE B CG2 
18030 C CD1 . ILE B 1220 ? 0.3871 0.4052 0.3879 0.0223  0.0035  -0.0272 1218 ILE B CD1 
18031 N N   . ASN B 1221 ? 0.2068 0.2273 0.2060 0.0137  0.0025  -0.0236 1219 ASN B N   
18032 C CA  . ASN B 1221 ? 0.2044 0.2271 0.2028 0.0122  0.0032  -0.0227 1219 ASN B CA  
18033 C C   . ASN B 1221 ? 0.2406 0.2654 0.2371 0.0130  0.0047  -0.0231 1219 ASN B C   
18034 O O   . ASN B 1221 ? 0.2435 0.2661 0.2369 0.0135  0.0046  -0.0238 1219 ASN B O   
18035 C CB  . ASN B 1221 ? 0.2156 0.2352 0.2121 0.0107  0.0020  -0.0222 1219 ASN B CB  
18036 C CG  . ASN B 1221 ? 0.2379 0.2589 0.2330 0.0091  0.0026  -0.0212 1219 ASN B CG  
18037 O OD1 . ASN B 1221 ? 0.2126 0.2372 0.2085 0.0087  0.0039  -0.0208 1219 ASN B OD1 
18038 N ND2 . ASN B 1221 ? 0.2503 0.2686 0.2434 0.0080  0.0016  -0.0208 1219 ASN B ND2 
18039 N N   . THR B 1222 ? 0.2115 0.2407 0.2096 0.0132  0.0061  -0.0227 1220 THR B N   
18040 C CA  . THR B 1222 ? 0.2233 0.2552 0.2200 0.0143  0.0078  -0.0230 1220 THR B CA  
18041 C C   . THR B 1222 ? 0.2667 0.3006 0.2620 0.0124  0.0086  -0.0220 1220 THR B C   
18042 O O   . THR B 1222 ? 0.3323 0.3691 0.3265 0.0129  0.0103  -0.0221 1220 THR B O   
18043 C CB  . THR B 1222 ? 0.2498 0.2860 0.2495 0.0158  0.0089  -0.0231 1220 THR B CB  
18044 O OG1 . THR B 1222 ? 0.2681 0.3073 0.2707 0.0141  0.0088  -0.0219 1220 THR B OG1 
18045 C CG2 . THR B 1222 ? 0.2754 0.3091 0.2760 0.0177  0.0081  -0.0241 1220 THR B CG2 
18046 N N   . ALA B 1223 ? 0.2472 0.2793 0.2421 0.0102  0.0076  -0.0211 1221 ALA B N   
18047 C CA  . ALA B 1223 ? 0.3132 0.3458 0.3060 0.0082  0.0081  -0.0200 1221 ALA B CA  
18048 C C   . ALA B 1223 ? 0.4398 0.4681 0.4288 0.0080  0.0071  -0.0203 1221 ALA B C   
18049 O O   . ALA B 1223 ? 0.4554 0.4834 0.4421 0.0064  0.0073  -0.0193 1221 ALA B O   
18050 C CB  . ALA B 1223 ? 0.3388 0.3720 0.3334 0.0059  0.0074  -0.0187 1221 ALA B CB  
18051 N N   . ALA B 1224 ? 0.3910 0.4159 0.3791 0.0095  0.0060  -0.0215 1222 ALA B N   
18052 C CA  . ALA B 1224 ? 0.3642 0.3849 0.3491 0.0092  0.0046  -0.0216 1222 ALA B CA  
18053 C C   . ALA B 1224 ? 0.4791 0.4997 0.4598 0.0091  0.0055  -0.0217 1222 ALA B C   
18054 O O   . ALA B 1224 ? 0.4890 0.5066 0.4669 0.0081  0.0044  -0.0213 1222 ALA B O   
18055 C CB  . ALA B 1224 ? 0.3591 0.3766 0.3443 0.0106  0.0032  -0.0229 1222 ALA B CB  
18056 N N   . ALA B 1225 ? 0.4934 0.5172 0.4735 0.0101  0.0075  -0.0221 1223 ALA B N   
18057 C CA  . ALA B 1225 ? 0.5155 0.5394 0.4913 0.0101  0.0087  -0.0221 1223 ALA B CA  
18058 C C   . ALA B 1225 ? 0.6042 0.6300 0.5792 0.0078  0.0095  -0.0204 1223 ALA B C   
18059 O O   . ALA B 1225 ? 0.6014 0.6272 0.5725 0.0074  0.0104  -0.0201 1223 ALA B O   
18060 C CB  . ALA B 1225 ? 0.5010 0.5278 0.4764 0.0123  0.0108  -0.0233 1223 ALA B CB  
18061 N N   . GLY B 1226 ? 0.5176 0.5447 0.4957 0.0061  0.0091  -0.0192 1224 GLY B N   
18062 C CA  . GLY B 1226 ? 0.5913 0.6198 0.5687 0.0037  0.0096  -0.0174 1224 GLY B CA  
18063 C C   . GLY B 1226 ? 0.6234 0.6572 0.6042 0.0028  0.0112  -0.0166 1224 GLY B C   
18064 O O   . GLY B 1226 ? 0.5647 0.5999 0.5451 0.0005  0.0118  -0.0151 1224 GLY B O   
18065 N N   . GLY B 1227 ? 0.4843 0.5212 0.4685 0.0045  0.0119  -0.0175 1225 GLY B N   
18066 C CA  . GLY B 1227 ? 0.5349 0.5772 0.5226 0.0037  0.0132  -0.0167 1225 GLY B CA  
18067 C C   . GLY B 1227 ? 0.5554 0.5998 0.5466 0.0059  0.0134  -0.0178 1225 GLY B C   
18068 O O   . GLY B 1227 ? 0.4993 0.5408 0.4900 0.0080  0.0126  -0.0192 1225 GLY B O   
18069 N N   . ASN B 1228 ? 0.4623 0.5119 0.4571 0.0054  0.0143  -0.0171 1226 ASN B N   
18070 C CA  . ASN B 1228 ? 0.5599 0.6119 0.5584 0.0073  0.0143  -0.0178 1226 ASN B CA  
18071 C C   . ASN B 1228 ? 0.6054 0.6631 0.6051 0.0089  0.0166  -0.0180 1226 ASN B C   
18072 O O   . ASN B 1228 ? 0.6530 0.7154 0.6538 0.0074  0.0180  -0.0169 1226 ASN B O   
18073 C CB  . ASN B 1228 ? 0.5324 0.5859 0.5342 0.0055  0.0133  -0.0169 1226 ASN B CB  
18074 C CG  . ASN B 1228 ? 0.5559 0.6107 0.5611 0.0074  0.0128  -0.0176 1226 ASN B CG  
18075 O OD1 . ASN B 1228 ? 0.5991 0.6556 0.6050 0.0100  0.0137  -0.0185 1226 ASN B OD1 
18076 N ND2 . ASN B 1228 ? 0.4115 0.4652 0.4185 0.0061  0.0113  -0.0172 1226 ASN B ND2 
18077 N N   . ALA B 1229 ? 0.5625 0.6197 0.5620 0.0121  0.0170  -0.0195 1227 ALA B N   
18078 C CA  . ALA B 1229 ? 0.5992 0.6616 0.5999 0.0142  0.0192  -0.0199 1227 ALA B CA  
18079 C C   . ALA B 1229 ? 0.6591 0.7275 0.6649 0.0140  0.0196  -0.0190 1227 ALA B C   
18080 O O   . ALA B 1229 ? 0.5761 0.6504 0.5836 0.0138  0.0214  -0.0182 1227 ALA B O   
18081 C CB  . ALA B 1229 ? 0.5203 0.5797 0.5194 0.0176  0.0193  -0.0217 1227 ALA B CB  
18082 N N   . SER B 1230 ? 0.6736 0.7406 0.6818 0.0142  0.0179  -0.0191 1228 SER B N   
18083 C CA  . SER B 1230 ? 0.6880 0.7604 0.7009 0.0144  0.0179  -0.0184 1228 SER B CA  
18084 C C   . SER B 1230 ? 0.7446 0.8212 0.7595 0.0110  0.0181  -0.0167 1228 SER B C   
18085 O O   . SER B 1230 ? 0.7439 0.8268 0.7623 0.0110  0.0190  -0.0160 1228 SER B O   
18086 C CB  . SER B 1230 ? 0.6648 0.7341 0.6792 0.0151  0.0160  -0.0189 1228 SER B CB  
18087 N N   . LEU B 1231 ? 0.6634 0.7365 0.6759 0.0081  0.0172  -0.0160 1229 LEU B N   
18088 C CA  . LEU B 1231 ? 0.6526 0.7288 0.6664 0.0047  0.0173  -0.0144 1229 LEU B CA  
18089 C C   . LEU B 1231 ? 0.7166 0.7967 0.7294 0.0036  0.0194  -0.0136 1229 LEU B C   
18090 O O   . LEU B 1231 ? 0.7109 0.7943 0.7250 0.0007  0.0197  -0.0121 1229 LEU B O   
18091 C CB  . LEU B 1231 ? 0.6388 0.7095 0.6507 0.0021  0.0154  -0.0139 1229 LEU B CB  
18092 C CG  . LEU B 1231 ? 0.4723 0.5401 0.4856 0.0018  0.0133  -0.0142 1229 LEU B CG  
18093 C CD1 . LEU B 1231 ? 0.3836 0.4467 0.3947 -0.0010 0.0119  -0.0136 1229 LEU B CD1 
18094 C CD2 . LEU B 1231 ? 0.5339 0.6072 0.5515 0.0014  0.0131  -0.0136 1229 LEU B CD2 
18095 N N   . MET B 1232 ? 0.7131 0.7928 0.7234 0.0059  0.0210  -0.0145 1230 MET B N   
18096 C CA  . MET B 1232 ? 0.6881 0.7724 0.6977 0.0053  0.0234  -0.0137 1230 MET B CA  
18097 C C   . MET B 1232 ? 0.7064 0.7991 0.7208 0.0057  0.0249  -0.0130 1230 MET B C   
18098 O O   . MET B 1232 ? 0.5218 0.6195 0.5372 0.0036  0.0264  -0.0116 1230 MET B O   
18099 C CB  . MET B 1232 ? 0.6235 0.7052 0.6289 0.0079  0.0248  -0.0150 1230 MET B CB  
18100 N N   . ALA B 1233 ? 0.7948 0.8894 0.8124 0.0084  0.0245  -0.0138 1231 ALA B N   
18101 C CA  . ALA B 1233 ? 0.8374 0.9402 0.8603 0.0090  0.0255  -0.0131 1231 ALA B CA  
18102 C C   . ALA B 1233 ? 0.8230 0.9281 0.8493 0.0058  0.0238  -0.0117 1231 ALA B C   
18103 O O   . ALA B 1233 ? 0.8445 0.9569 0.8754 0.0057  0.0244  -0.0108 1231 ALA B O   
18104 C CB  . ALA B 1233 ? 0.7687 0.8722 0.7934 0.0133  0.0256  -0.0145 1231 ALA B CB  
18105 N N   . ILE B 1234 ? 0.7823 0.8817 0.8067 0.0034  0.0217  -0.0115 1232 ILE B N   
18106 C CA  . ILE B 1234 ? 0.7537 0.8542 0.7806 0.0004  0.0199  -0.0104 1232 ILE B CA  
18107 C C   . ILE B 1234 ? 0.6902 0.7922 0.7163 -0.0037 0.0205  -0.0088 1232 ILE B C   
18108 O O   . ILE B 1234 ? 0.6251 0.7213 0.6473 -0.0056 0.0198  -0.0086 1232 ILE B O   
18109 C CB  . ILE B 1234 ? 0.6495 0.7428 0.6747 0.0003  0.0174  -0.0112 1232 ILE B CB  
18110 C CG1 . ILE B 1234 ? 0.7012 0.7937 0.7276 0.0042  0.0170  -0.0125 1232 ILE B CG1 
18111 C CG2 . ILE B 1234 ? 0.5774 0.6714 0.6044 -0.0030 0.0157  -0.0101 1232 ILE B CG2 
18112 C CD1 . ILE B 1234 ? 0.5546 0.6452 0.5826 0.0038  0.0147  -0.0126 1232 ILE B CD1 
18113 N N   . GLY B 1235 ? 0.6326 0.7423 0.6624 -0.0050 0.0216  -0.0075 1233 GLY B N   
18114 C CA  . GLY B 1235 ? 0.4884 0.6003 0.5181 -0.0092 0.0220  -0.0058 1233 GLY B CA  
18115 C C   . GLY B 1235 ? 0.4426 0.5598 0.4770 -0.0116 0.0209  -0.0046 1233 GLY B C   
18116 O O   . GLY B 1235 ? 0.6892 0.8124 0.7280 -0.0097 0.0211  -0.0047 1233 GLY B O   
18117 O OXT . GLY B 1235 ? 0.2576 0.3733 0.2915 -0.0155 0.0196  -0.0035 1233 GLY B OXT 
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